Crystal structure

Abstract
The present invention relates to the soakable crystals of a phosphodiesterase 5 (PDE5) and their uses in identifying PDE5 ligands, including PDE5 ligands and inhibitor compounds. The present invention also relates to methods of identifying such PDE5 inhibitor compounds and their medical use. The present invention additionally relates to crystals of PDE5 into which ligands may be soaked and crystals of PDE5 comprising PDE5 ligands that have been soaked into the crystal.
Description
TECHNICAL FIELD

The present invention relates to crystal structures of a phosphodiesterase 5 (PDE5) and ligand complexes of PDE5 and to their uses in identifying PDE5 ligands, including PDE5 inhibitor compounds. The present invention also relates to methods of identifying such PDE5 inhibitor compounds and their medical use. The present invention additionally relates to crystals of PDE5 into which ligands may be soaked and to crystals of PDE5 comprising ligands that have been soaked into the crystal. Also contemplated by the present invention is the use of crystals of PDE5 into which ligands may be soaked in identifying ligands of PDE5, including PDE5 inhibitor compounds.


BACKGROUND OF THE INVENTION

A wide variety of biological processes, including cardiac muscle contraction, regulation of blood flow, neural transmission, glandular secretion, cell differentiation and gene expression are affected by steady state levels of the cyclic nucleotide biological second messengers cAMP and cGMP. Intracellular receptors for these molecules include cyclic nucleotide dependent protein kinases (PGK) (Lohmann et al. 1997), cyclic nucleotide-gated channels, and class I phosphodiesterases (PDEs) (Charbonneau 1990). PDEs are a large family of proteins, which were first reported by Sutherland and co-workers (Rall & Sutherland 1958, Butcher & Sutherland 1962). The family of cyclic nucleotide phosphodiesterases catalyse the hydrolysis of 3′, 5′-cyclic nucleotides to the corresponding 5′ monophosphates. Current literature shows that there are eleven related, but biochemically distinct, human phosphodiesterase gene groups and that many of these groups include more than one gene subtype giving a total of twenty genes. Some PDEs are highly specific for hydrolysis of cAMP (PDE4, PDE7, PDE8), some are highly cGMP specific (PDE5, PDE6, PDE9), and some have mixed specificity (PDE1, PDE2, PDE3, PDE10, PDE11).


All PDEs are multi-domain proteins; each PDE has a ˜270 amino acid domain located towards the C-terminus, which has a high degree of amino acid sequence conservation between families (Charbonneau 1986). This domain has been extensively studied and shown to be responsible for the common catalytic function (Francis, S. H. et al. 1994). Non-homologous segments in the remainder of the protein have regulatory function or confer specific binding properties. PDE2, PDE5, PDE6 and PDE10 are all reported to contain putative GAF domains within their regulatory amino terminal portion (Aravind & Ponting 1997 and Soderling & Beavo 2000). These GAF domains have been shown to bind cGMP but their function is not yet fully understood. Full length mammalian PDEs characterised to date are dimeric in solution, but the relevance of the dimeric structure is unknown. The structure of the regulatory segment of PDE2A bound to cGMP has recently been solved and reveals a parallel dimer of four GAF domains, with cGMP binding to only one of the two GAF domains on each monomer (Martinez, et al. 2001).


PDE5, a cGMP specific PDE, has been recognised in recent years as an important therapeutic target. It is composed of the conserved C-terminal, zinc containing, catalytic domain, which catalyses the cleavage of cGMP, and an N-terminal regulatory portion, which contains two GAF domain repeats. Each GAF domain contains a cGMP-binding site, one of high affinity and the other of lower affinity. PDE5 activity is regulated through binding of cGMP to the high and low affinity cGMP binding sites followed by phosphorylation, which occurs only when both sites are occupied (Thomas et al. 1990). PDE5 is found in varying concentrations in a number of tissues including platelets, vascular and visceral smooth muscle, and skeletal muscle. The protein is a key regulator of cGMP levels in the smooth muscle of the erectile corpus cavemosal tissue. The physiological mechanism of erection involves release of nitric oxide (NO) in the corpus cavemosum during sexual stimulation. NO then activates the enzyme guanylate cyclase, which results in increased levels of cGMP, producing smooth muscle relaxation in the corpus cavemosum and allowing in flow of blood. Inhibition of PDE5 inhibits the breakdown of cGMP allowing the levels of cGMP, and hence smooth muscle relaxation, to be maintained (Corbin & Francis 1999). Sildenafil (UK-092,480), the active ingredient of Viagra® and a potent inhibitor of PDE5, has attracted widespread attention for the effective treatment of male erectile dysfunction.


Structural information has recently been shown for the catalytic domain of PDE4b a cAMP-specific PDE (Xu et al. 2000). This structure provides information about the overall fold of the catalytic domains of the PDE family, but, to date, no structural information is known about the way in which potential inhibitors bind to the enzyme.


The X-ray structure of a recombinant PDE5 comprising the catalytic domain in complex with Sildenafil has been determined (see earlier related patent application Number PCT/IB02/04426: Example 9, “crystallisation of wild type PDE5 catalytic domain with Sildenafil”, page 44, line 29 to page 45, line 17; Example 13, “Data collection, structure determination and refinement of wild type PDE5 with Sildenafil”, page 48, line 1 to page 49, line 9; Table 4, page 91 to 248; incorporated herein by reference). An engineered form of this PDE5, PDE5*, which shows improved qualities for the production of crystals of ligand complexes, has also been produced and the structure of such a complex has been determined (see Application Number PCT/IB02/04426: Example 11, “crystallisation of PDE5* with Sildenafil”, page 46, lines 8 to 25; Example 15, “data collection, structure determination and refinement of PDE5* with Sildenafil”, page 50, line 9 to page 51, line 6; and Table 6, “atomic co-ordinates for baculovirus-expressed PDE5* complex with Sildenafil”, pages 328 to 408; incorporated herein by reference). These complexes not only provide important structural information about this novel family of proteins but also assist the design of more potent and specific inhibitors of PDEs to treat the many diseases where PDEs play a role.


It is desirable to be able to obtain crystals of biological macromolecules in a complex with their ligands in order to obtain details of specific ligand interactions at a level of molecular resolution and, preferably, at atomic resolution. This invariably forms the critical step in providing information from which further, and possibly improved, ligands of the macromolecule may be designed and subsequently tested in further rounds of crystallisation. It is therefore most desirable that this process of obtaining complexes of the macromolecule be rapid and reproducible and minimise the need to constantly find new crystallisation conditions for each potential complex or use involved and time intensive structure solution methods for the solution of each potential complex structure. To this end the most desirable crystal form of a macromolecule of interest is one which is amenable to having potential ligands soaked into the preformed crystal of the apo macromolecule. This has distinct advantages over conventionally produced co-crystals. In particular no new crystallisation conditions need to be found for each potential complex. The lattice symmetry and cell dimensions for each new ligand complex will be substantially the same as for the apo macromolecule such that the data collection parameters for the apo and all complex crystals will essentially be identical. The structure solution can then occur using rapid difference fourier methods, thus avoiding more involved time and labour intensive phasing methods. Consequently, soakable crystals of macromolecules allow for particularly rapid screening and structural determination of new macromolecule-ligand complexes.


The engineered form of PDE5, PDE5*, allows the production of soakable crystals of ligand complexes, and the structure of such a soaked PDE5*-ligand complex has been determined.


SUMMARY OF THE INVENTION

It has been found that PDE5 can be crystallised. It has also been found that manipulating the wild-type PDE5 amino acid sequence can facilitate the crystallisation of PDE5. Specifically, it has been found that manipulations of certain portions of the PDE5 amino acid sequence can facilitate the crystallisation of PDE5. More specifically it has been shown that particular manipulations of the PDE5 amino acid sequence can provide soakable crystal forms of PDE5 into which potential PDE5 ligands may be introduced by the process of crystal soaking. Manipulating the wild-type PDE5 amino acid sequence results in a sequence modified PDE5 protein.


It has been shown that manipulations of the catalytic domain of PDE5, specifically the 657-682 region of PDE5 (the “loop region”), can facilitate the crystallisation of PDE5 and particularly provide soakable crystals of PDE5. More specifically, manipulations of the loop region amino acid sequence (HRGVNNSYIQRSEHPLAQLYCHSIME=SEQ ID NO: 1) of PDE5 can facilitate the crystallisation of PDE5 and provide soakable crystals of PDE5. This manipulation can be achieved by deletion, addition or substitution of one or more amino acid residues of the PDE5 loop region or it can be achieved by complete replacement of the PDE5 loop region with a loop region (or other amino acid sequence) from another protein, preferably another PDE, more preferably PDE4, most preferably PDE4b (Genbank Accession Number=L20966).


Crystals of PDE5 have been found to be useful for screening for PDE5 ligands, especially PDE5 inhibitors by (i) co-crystallising PDE5 with the PDE5 ligand (e.g. PDE5 inhibitor), as shown in Application Number PCT/IB02/04426 (Example 9, “crystallisation of wild type PDE5 catalytic domain with Sildenafil”, page 44, line 29 to page 45, line 17; Example 11, “crystallisation of PDE5* with Sildenafil”, page 46, lines 8 to 25; Example 13, “Data collection, structure determination and refinement of wild type PDE5 with Sildenafil”, page 48, line 1 to page 49, line 9; Example 15, “data collection, structure determination and refinement of PDE5* with Sildenafil”, page 50, line 9 to page 51, line 6; Table 4 “atomic co-ordinates for wild type PDE5 complexed with Sildenafil”, pages 91 to 240; and Table 6, “atomic co-ordinates for baculovirus-expressed PDE5* complex with Sildenafil”, pages 328 to 408; incorporated herein by reference), or (ii) by soaking the PDE5 ligand (e.g. PDE5 inhibitor) into the crystal of PDE5, as shown in the present invention.


PDE5 ligands, especially PDE5 inhibitors, as identified by the methods of the present invention are useful in curative, palliative or prophylactic treatments.


Thus, the present invention provides the following (numbered) aspects:


Aspects




  • 1. A crystal of phosphodiesterase 5 (PDE5), wherein the crystal is soakable.

  • 2. The crystal of PDE5 according to aspect 1, wherein said PDE5 is from a mammal.

  • 3. The crystal of PDE5 according to aspect 1 or aspect 2, wherein said PDE5 is from a human.

  • 4. The crystal of PDE5 according to any one of aspects 1 to 3, wherein said PDE5 is an isoform selected from the group consisting of PDE5A1, PDE5A2, PDE5A3 and PDE5A4.

  • 5. The crystal of PDE5 according to any one of aspects 1 to 4, wherein said PDE5 comprises SEQ ID NO: 1 (PDE5 loop region) or a homologue, fragment, variant, analogue or derivative thereof.



SEQ ID NO: 1 is the so-called “loop region” of PDE5. This loop region or a homologue, fragment, variant, analogue or derivative thereof includes additions, deletions or substitutions of amino acid residues comprised within the loop region.


Preferably, a variant in relation to the amino acid sequence of the crystal of the PDE5 of the present invention includes the deletion or substitution of the histidine (His/H) residue as shown emboldened and underlined in SEQ ID NO: 1 (HRGVNNSYIQRSEHPLAQLYCHSIME). Replacement of said histidine (H) residue is preferably by way of incorporating one or more amino acid residues (other than histidine), preferably wherein said amino acid residues are neutral or non-polar.


More preferably, a variant in relation to the amino acid sequence of the crystal of the PDE5 of the present invention includes the complete replacement of the loop region with a loop region (or other amino acid sequence) from another protein, preferably a PDE, more preferably PDE4, most preferably PDE4b (see hereinafter).

  • 6. The crystal of PDE5 according to any one of aspects 1 to 5, wherein said PDE5 comprises SEQ ID NO: 4 (PDE4 loop) or a homologue, fragment, variant, analogue or derivative thereof.
  • 7. The crystal of PDE5 according to any one of aspects 1 to 6, wherein said PDE5 comprises SEQ ID NO: 5 (PDE5*=loop swapped PDE5 catalytic domain) or a homologue, fragment, variant, analogue or derivative thereof
  • 8. The crystal of PDE5 according to any one of aspects 1 to 7, wherein said PDE5 comprises SEQ ID NO: 6 (full PDE5 sequence comprising PDE5*) or a homologue, fragment, variant, analogue or derivative thereof.
  • 9. The crystal of PDE5 according to any of the preceding aspects which is grown using polyethylene glycol as a precipitant. Polyethylene glycol of molecular weights 2000 to 8000 are commonly used. Preferably the molecular weight of the polyethylene glycol is 4000. The polyethylene glycol may be at a concentration of between 10% and 30%, but is most preferably 20%. Additionally, the PDE5 protein used to grow the crystals is desired to be of a concentration between 1 and 20 mg/ml, preferably between 5 and 15 mg/ml and most preferably is at 10 mg/ml concentration.
  • 10. The crystal of PDE5 according to any of the preceding aspects which is grown in a buffer in the pH range of 6.5 to 8.0. Preferably the pH is in the range of 7.0 to 7.8; most preferably the pH is 7.4. The buffer should be one capable of providing buffer capacity over the required pH range, preferably HEPES.
  • 11. The crystal of PDE5 according to any of the preceding aspects which is grown in the presence of an alcohol. Preferably the alcohol is isopropanol.
  • 12. The crystal of PDE5 according to any of the preceding aspects which is grown in a solution containing HEPES buffer, polyethylene glycol 4000 and iso-propanol. Preferably the solution contains 0.1M sodium HEPES pH 7.4, 20% polyethylene glycol 4000 and 10% iso-propanol. The crystal is grown from solution incubated at or below room temperature (20-25° C.). Preferably the crystal is grown from a solution incubated at a temperature within the range of 2-6° C. More preferably, the crystal is grown from a solution incubated at about 4° C.


Soakable crystals may be grown using a variety of methods such as dialysis, sitting drop vapour diffusion or batch methods, microcrystallisation methods, micro or macro seeding methods or gel crystallisation methods but are preferably grown using hanging drop vapour diffusion.

  • 13. The crystal of PDE5 as defined in any of the preceding aspects, which has one or more of the following characteristics:
    • (a) a space group C2;
    • (b) unit cell dimensions a˜56 ű1%, b˜77 ű1%, c˜81 ű1%, α=γ=90°, β=103°≅1%;
    • (c) 1 molecule per asymmetric unit;
    • (d) comprises a PDE5 of a molecular weight of approximately 40 kDa±2 kDa;
    • (e) a calculated solvent content of approximately 44±5%; and
    • (f) a monoclinic crystal system.
  • 14. The crystal of PDE5 according to any of the preceding aspects, wherein PDE5 has an active site within the third sub-domain of the protein which is bounded by Helices 15 (H15 813-824) and 14 (H14 772-797), the C-terminus of Helix 13 (H13 749-765), and the C-terminus of Helix 11 (H11 706-721) along with the loop region between Helices 11 and 12a (H12a 725-731) as shown in FIG. 2.
  • 15. The crystal of PDE5 according to aspect 14, wherein the active site is capable of accommodating a pyrazolo-pyrimidinone. An example of a preferred pyrazolo-pyrimidinone is UK-088,800.


UK-088,800 is illustrated in FIG. 4 and is a structural representation of the compound with the chemical name 5-(2-ethoxyphenyl)-1-methyl-3-propyl-1,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one.

  • 16. The crystal of PDE5 according to any of the preceding aspects, wherein PDE5 has an active site within the third sub-domain of the protein and comprises Leu 765, Ala 767 and Ile 768 and one or more of Phe 820, Val 782, Phe 786, Tyr 612, Leu 804, Ala 779, Ala 783, Ile 813, Met 816 and Gln 817.
  • 17. The crystal of PDE5 according to aspect 16, wherein the active site is capable of accommodating a pyrazolo-pyrimidinone. An example of a preferred pyrazolo-pyrimidinone is UK-088,800.
  • 18. The crystal of PDE5 according to any of the preceding aspects, wherein said PDE5 has a three-dimensional structure characterised by the atomic co-ordinates set out in Table 4 (PDE5* apo C2 form) or a derivative set as expressed in any reference frame.
  • 19. A heavy atom derivative of the crystal of PDE5 according to any of the preceding aspects.
  • 20. The crystal of PDE5 according to any of the preceding aspects, wherein a PDE5 ligand has been soaked in. The process of soaking may involve transferring the crystal to be soaked from the solution in which it is grown into a stabilising solution containing the ligand or to which the ligand is to be added once the crystal is present in it. It is desirable that the stabilising solution has the physical properties such that the crystal, when transferred, retains its structural integrity and does not crack or dissolve or alter significantly in its crystal parameters, symmetry or cell dimensions. Preferably, the stabilising solution comprises some or all of the chemical constituents from which the crystal was grown. More preferably, the stabilising solution is of similar or identical composition to the solutions used for crystal growth as set out in aspects 9 to 12 above, although the concentration of precipitant used may be slightly increased. Most preferably the stabilising solution has the same pH as the crystal growth solution. The ligand may be added to the solution containing, or to contain, the crystal for soaking as a solid or in a liquid form (i.e. the ligand already being in solution). Preferably the ligand is in solution and the solvent maybe aqueous, organic or non-organic. Most preferably the ligand is in DMSO. The ligand is commonly added to the soaking solution to yield a final ligand concentration above the expected binding constant for the ligand by PDE5; preferably this is greater than or equal to 10 times the binding constant. The final concentration of ligand present in the crystal soaking solution is preferably between 0.1 and 20 mg/ml, more preferably between 0.5 and 10 mg/ml, and most preferably between 1 and 5 mg/ml.
  • 21. The crystal of PDE5 according to aspect 20, wherein said PDE5 ligand is a PDE5 inhibitor.
  • 22. The crystal of PDE5 according to aspect 21, wherein said PDE5 inhibitor is a pyrazolo-pyrimidinone, preferably UK-088,800.
  • 23. The crystal of PDE5 according to aspect 22, wherein said PDE5 has a three-dimensional structure characterised by the atomic co-ordinates set out in Table 5 (PDE5*-UK-088,800 complex) or a derivative set as expressed in any reference frame.
  • 24. Use of the atomic co-ordinates determined from the crystal of PDE5 according to any one of the preceding aspects for deriving a three-dimensional structure of a PDE5 or a mutant, derivative, variant, analogue, homologue, sub-domain or fragment thereof.
  • 25. Use according to aspect 24, wherein the PDE5 sub-domain is the catalytic domain.
  • 26. Use of the three-dimensional structure of PDE5 as derivable according to aspect 24 or aspect 25 to computationally or otherwise evaluate the binding interactions of a chemical compound with an active site on PDE5.
  • 27. Use of the three-dimensional structure of PDE5 as derivable according to aspect 26 to design a compound capable of associating with PDE5. Preferably said compound is a pyrazolo-pyrimidinone, more preferably UK-088,800.
  • 28. Use according to aspect 26 or aspect 27, wherein the compound is a PDE5 ligand.
  • 29. Use according to aspect 28, wherein said compound is a PDE5 inhibitor.
  • 30. Use according to aspect 29, wherein said PDE5 inhibitor is a pyrazolo-pyrimidinone, preferably UK-088,800.
  • 31. A method of selecting a compound capable of associating with PDE5 from a group of potential PDE5 ligand compounds comprising the following steps:
    • i. soaking the crystal of PDE5 according to any one of aspects 1 to 19 in a solution containing a potential PDE5 ligand compound;
    • ii. determining the three-dimensional structure from the soaked crystal; and
    • iii. assessing whether the compound is bound to PDE5.
  • 32. A compound selected by the use according to aspect 31.
  • 33. A compound designed by the use according to any one of aspects 27 to 30 or identified by the method of aspect 31.
  • 34. The compound according to aspect 33, which is a PDE5 inhibitor.
  • 35. A method of selecting a PDE5 ligand from a group of potential PDE5 ligands, comprising the following steps:
    • (a) computationally creating a three-dimensional representation of the structure of PDE5 as derivable according to aspect 24 or aspect 25, and a three-dimensional representation of the structure of the potential PDE5 ligand;
    • (b) co-displaying the three-dimensional representation of the potential PDE5 ligand with the three-dimensional representation of the PDE5 structure; and
    • (c) assessing whether the three-dimensional representation of the potential PDE5 ligand fits the three-dimensional representation of an active site of the PDE5 structure.


Preferably, ligands are built using molecular graphics tools, more preferably the designed ligand is energy minimised prior to co-display and analysis.

  • 36. The method according to aspect 35, further comprising the following steps:
    • (d) incorporating the potential PDE5 ligand in a biological PDE5 activity assay; and
    • (e) determining whether the potential PDE5 ligand modulates PDE5 activity in said assay.
  • 37. The method according to aspect 35 or aspect 36 wherein said potential PDE5 ligand is a potential PDE5 inhibitor compound and said potential PDE5 inhibitor compound inhibits PDE5 activity.
  • 38. A PDE5 ligand selected by the method of any one of aspects 35 to 37. Preferably the ligand is a PDE5 inhibitor.
  • 39. Use of a PDE5 ligand according to aspect 38 as a pharmaceutical. Preferably the ligand is a PDE5 inhibitor.
  • 40. A pharmaceutical composition comprising one or more PDE5 ligands according to aspect 38 and one or more pharmaceutically acceptable excipients.
  • 41. Use of a PDE5 ligand according to aspect 38 in the manufacture of a medicament for the prophylaxis or treatment of a condition, disease, disorder or dysfunction where the inhibition of PDE5 is prophylactically or therapeutically beneficial.
  • 42. Use according to aspect 41, wherein said disorder is a mammalian sexual disorder.


The curative, palliative or prophylactic treatments contemplated by the present invention include the curative, palliative or prophylactic treatment of mammalian sexual disorders, in particular the treatment of mammalian sexual dysfunctions such as male erectile dysfunction (MED), impotence, female sexual dysfunction (FSD), clitoral dysfunction, female hypoactive sexual desire disorder, female sexual arousal disorder (FSAD), female sexual pain disorder or female sexual orgasmic dysfunction (FSOD) as well as sexual dysfunction due to spinal cord injury or selective serotonin re-uptake inhibitor (SSRI) induced sexual dysfunction but, clearly, will also be useful for treating other medical conditions for which PDE5 inhibitor is indicated. Such conditions include premature labour, dysmenorrhoea, benign prostatic hyperplasia (BPH), bladder outlet obstruction, incontinence, stable, unstable and variant (Prinzmetal) angina, hypertension, pulmonary hypertension, chronic obstructive pulmonary disease, coronary artery disease, congestive heart failure, atherosclerosis, conditions of reduced blood vessel patency, e.g. post-percutaneous transluminal coronary angioplasty (post-PTCA), peripheral vascular disease, stroke, nitrate induced tolerance, bronchitis, allergic asthma, chronic asthma, allergic rhinitis, diseases and conditions of the eye such as glaucoma, optic neuropathy, macular degeneration, elevated intra-occular pressure, retinal or arterial occlusion and diseases characterised by disorders of gut motility, e.g. irritable bowel syndrome (IBS).


Further medical conditions for which a PDE5 inhibitor is indicated, and for which treatment with compounds of the present invention may be useful include pre-eclampsia, Kawasaki's syndrome, nitrate tolerance, multiple sclerosis, diabetic nephropathy, neuropathy including autonomic and peripheral neuropathy and in particular diabetic neuropathy and symptoms thereof e.g. gastroparesis, peripheral diabetic neuropathy, Alzheimer's disease, acute respiratory failure, psoriasis, skin necrosis, cancer, metastasis, baldness, nutcracker oesophagus, anal fissure, haemorrhoids, the insulin resistance syndrome, diabetes, hypoxic vasoconstriction as well as the stabilisation of blood pressure during haemodialysis.


Particularly preferred conditions include MED and FSD (preferably FSAD).


Further (numbered) aspects of the present invention include:

  • 43. Use of the atomic co-ordinates determined from the crystal of PDE5 according to any one of aspects 1 to 23, to solve the crystal structure of a mutant, derivative, fragment, variant, analogue, homologue or complex of PDE5.
  • 44. Use of the atomic co-ordinates determined from the crystal of PDE5 according to any one of aspects 1 to 23, to produce a model of the three-dimensional structure of PDE5-related proteins.
  • 45. Use of the three-dimensional structure of PDE5 as derivable according to aspect 24 or aspect 25 to design site-directed mutants that mimic other PDE5 isoforms or variants thereof.
  • 46. A method of soaking a chemical compound into a crystal according to any one of aspects 1 to 19 comprising the following steps:
    • a) incubating the crystal in an aqueous stabilising solution comprising buffer and polyethylene glycol;
    • b) combining the chemical compound with the stabilising solution preferably wherein the chemical compound is in solid or liquid form, more preferably in liquid form, most preferably solublised in DMSO; and
    • c) optionally adding a cryo-protectant to the stabilising solution.
  • 47. A method according to aspect 46, wherein the stabilising solution comprises polyethylene glycol which is of the molecular weight 4000. The polyethylene glycol may be at a concentration of between 10% and 30%, but is most preferably 20%. Additionally the pH is preferably in the range of 7.0 to 7.8; most preferably the pH is 7.4. The buffer should be one capable of providing buffer capacity over the required pH range; preferably HEPES. Preferably the stabilising solution contains an alcohol; most preferably this is isopropanol. Preferably the stabilising solution contains 0.1M sodium HEPES pH 7.4, 20% polyethylene glycol 4000 and 10% iso-propanol. Examples of suitable cryoprotectants include 2-methyl-2,4-pentanediol (MPD) and organic polymers e.g. lower molecular weight PEG. Carbohydrates such as sorbitol or xylitol, and alcohols may also be used. Preferably the cryoprotectant is glycerol.


A PDE5 ligand (also known as a PDE5 inhibitor compound) according to aspect 38 (hereinafter referred to as “the compound”) can be administered alone but, in human therapy, will generally be administered in admixture with a suitable pharmaceutical excipient diluent or carrier selected with regard to the intended route of administration and standard pharmaceutical practice. Thus, the pharmaceutical compositions, pharmaceuticals and medicaments contemplated by the present invention may be formulated in various ways well-known to one of skill in the art and administered by similarly well-known methods.


For example, the compound of the invention can be administered orally, buccally or sublingually in the form of tablets, capsules (including soft gel capsules), ovules, elixirs, solutions or suspensions, which may contain flavouring or colouring agents, for immediate-, delayed-, modified-, or controlled-release such as sustained-, dual-, or pulsatile delivery applications. The compound may also be administered via intracavernosal injection. The compound may also be administered via fast dispersing or fast dissolving dosages forms or in the form of a high-energy dispersion or as coated particles. Suitable pharmaceutical formulations of the compound may be in coated or un-coated form as desired.


Such tablets may contain excipients such as microcrystalline cellulose, lactose, sodium citrate, calcium carbonate, dibasic calcium phosphate, glycine and starch (preferably corn, potato or tapioca starch), disintegrants such as sodium starch glycollate, croscarmellose sodium and certain complex silicates, and granulation binders such as polyvinylpyrrolidone, hydroxypropylmethyl cellulose (HPMC), hydroxypropylcellulose (HPC), sucrose, gelatin and acacia. Additionally, lubricating agents such as magnesium stearate, stearic acid, glyceryl behenate and talc may be included.


Solid compositions of a similar type may also be employed as fillers in gelatin capsules. Preferred excipients in this regard include lactose, starch, a cellulose, milk sugar or high molecular weight polyethylene glycols. For aqueous suspensions and/or elixirs, the compound may be combined with various sweetening or flavouring agents, colouring matter or dyes, with emulsifying and/or suspending agents and with diluents such as water, ethanol, propylene glycol and glycerin, and combinations thereof.


Modified release and pulsatile release dosage forms may contain excipients such as those detailed for immediate release dosage forms together with additional excipients that act as release rate modifiers, these being coated on and/or included in the body of the device. Release rate modifiers include, but are not exclusively limited to, hydroxypropylmethyl cellulose, methyl cellulose, sodium carboxymethylcellulose, ethyl cellulose, cellulose acetate, polyethylene oxide, Xanthan gum, Carbomer, ammonio methacrylate copolymer, hydrogenated castor oil, carnauba wax, paraffin wax, cellulose acetate phthalate, hydroxypropylmethyl cellulose phthalate, methacrylic acid copolymer and mixtures thereof. Modified release and pulsatile release dosage forms may contain one or a combination of release rate modifying excipients. Release rate-modifying excipients maybe present both within the dosage form i.e. within the matrix, and/or on the dosage form i.e. upon the surface or coating.


Fast dispersing or dissolving dosage formulations (FDDFs) may contain the following ingredients: aspartame, acesulfame potassium, citric acid, croscarmellose sodium, crospovidone, diascorbic acid, ethyl acrylate, ethyl cellulose, gelatin, hydroxypropylmethyl cellulose, magnesium stearate, mannitol, methyl methacrylate, mint flavouring, polyethylene glycol, fumed silica, silicon dioxide, sodium starch glycolate, sodium stearyl flimarate, sorbitol, xylitol. The terms dispersing or dissolving as used herein to describe FDDFs are dependent upon the solubility of the drug substance used i.e. where the drug substance is insoluble a fast dispersing dosage form can be prepared and where the drug substance is soluble a fast dissolving dosage form can be prepared.


The compound can also be administered parenterally, for example, intracavernosally, intravenously, intra-arterially, intraperitoneally, intrathecally, intraventricularly, intraurethrally intrastemally, intracranially, intramuscularly or subcutaneously, or they may be administered by infusion or needleless injection techniques. For such parenteral administration they are best used in the form of a sterile aqueous solution which may contain other substances, for example, enough salts or glucose to make the solution isotonic with blood. The aqueous solutions should be suitably buffered (preferably to a pH of from 3 to 9), if necessary. The preparation of suitable parenteral formulations under sterile conditions is readily accomplished by standard pharmaceutical techniques well-known to those skilled in the art.


For oral and parenteral administration to human patients, the daily dosage level of the compound will usually be from 10 to 500 mg (in single or divided doses).


Thus, for example, tablets or capsules of the compound may contain from 5 mg to 250 mg of active compound for administration singly or two or more at a time, as appropriate. The physician in any event will determine the actual dosage which will be most suitable for any individual patient and it will vary with the age, weight and response of the particular patient. The above dosages are exemplary of the average case. There can, of course, be individual instances where higher or lower dosage ranges are merited and such are within the scope of this invention. The skilled person will also appreciate that, in the treatment of certain conditions (including MED and FSD), the compound may be taken as a single dose on an “as required” basis (i.e. as needed or desired).


The compound can also be administered intranasally or by inhalation and are conveniently delivered in the form of a dry powder inhaler or an aerosol spray presentation from a pressurised container, pump, spray or nebuliser with the use of a suitable propellant, e.g. dichlorodifluoromethane, trichlorofluoromethane, dichlorotetrafluoroethane, a hydrofluoroalkane such as 1,1,1,2-tetrafluoroethane (HFA 134A™ or 1,1,1,2,3,3,3-heptafluoropropane (HFA 227EA™), carbon dioxide or other suitable gas. In the case of a pressurised aerosol, the dosage unit may be determined by providing a valve to deliver a metered amount. The pressurised container, pump, spray or nebuliser may contain a solution or suspension of the active compound, e.g. using a mixture of ethanol and the propellant as the solvent, which may additionally contain a lubricant, e.g. sorbitan trioleate. Capsules and cartridges (made, for example, from gelatin) for use in an inhaler or insufflator may be formulated to contain a powder mix of a compound of the invention and a suitable powder base such as lactose or starch.


Aerosol or dry powder formulations are preferably arranged so that each metered dose or “puff” contains from 1 to 50 mg of a compound of the invention for delivery to the patient. The overall daily dose with an aerosol will be in the range of from 1 to 50 mg which may be administered in a single dose or, more usually, in divided doses throughout the day.


The compound may also be formulated for delivery via an atomiser. Formulations for atomiser devices may contain the following ingredients as solubilisers, emulsifiers or suspending agents: water, ethanol, glycerol, propylene glycol, low molecular weight polyethylene glycols, sodium chloride, fluorocarbons, polyethylene glycol ethers, sorbitan trioleate, oleic acid.


Alternatively, the compound can be administered in the form of a suppository or pessary, or they may be applied topically in the form of a gel, hydrogel, lotion, solution, cream, ointment or dusting powder. The compound may also be dermally administered. The compound may also be transdermally administered, for example, by the use of a skin patch. The compound may also be administered by the ocular, pulmonary or rectal routes.


For ophthalmic use, the compound can be formulated as micronised suspensions in isotonic, pH adjusted, sterile saline, or, preferably, as solutions in isotonic, pH adjusted, sterile saline, optionally in combination with a preservative such as a benzylalkonium chloride. Alternatively, the compound may be formulated in an ointment such as petrolatum.


For application topically to the skin, the compound of the invention can be formulated as a suitable ointment containing the active compound suspended or dissolved in, for example, a mixture with one or more of the following: mineral oil, liquid petrolatum, white petrolatum, propylene glycol, polyoxyethylene polyoxypropylene compound, emulsifying wax and water. Alternatively, it can be formulated as a suitable lotion or cream, suspended or dissolved in, for example, a mixture of one or more of the following: mineral oil, sorbitan monostearate, a polyethylene glycol, liquid paraffin, polysorbate 60, cetyl esters wax, cetearyl alcohol, 2-octyldodecanol, benzyl alcohol and water.


The compound may also be used in combination with a cyclodextrin. Cyclodextrins are known to form inclusion and non-inclusion complexes with drug molecules. Formation of a drug-cyclodextrin complex may modify the solubility, dissolution rate, bioavailability and/or stability property of a drug molecule. Drug-cyclodextrin complexes are generally useful for most dosage forms and administration routes. As an alternative to direct complexation with the drug the cyclodextrin may be used as an auxiliary additive, e.g. as a carrier, diluent or solubiliser. Alpha-, beta- and gamma-cyclodextrins are most commonly used and suitable examples are described in WO-A-91/11172, WO-A-94/02518 and WO-A-98/55148.


Generally, in humans, oral administration the compound is the preferred route, being the most convenient and, for example in MED, avoiding the well-known disadvantages associated with intracavernosal (i.c.) administration. A preferred oral dosing regimen in MED for a typical man is from 25 to 250 mg of compound when required. In circumstances where the recipient suffers from a swallowing disorder or from impairment of drug absorption after oral administration, the drug may be administered parenterally, sublingually or buccally.


For veterinary use, the compound, or a veterinarily acceptable salt thereof, or a veterinarily acceptable solvate or pro-drug thereof, is administered as a suitably acceptable formulation in accordance with normal veterinary practice and the veterinary surgeon will determine the dosing regimen and route of administration which will be most appropriate for a particular animal.


The present invention provides the following numbered preferred aspects:


Preferred Aspects of the Invention




  • 1. A crystal of sequence-modified PDE5 protein comprising SEQ ID NO: 4 into which a compound of the formula represented in FIG. 4 is capable of being soaked such that the compound is bound to the active site of the protein.



The term “sequence modified PDE5 protein” as used herein includes the wild-type PDE5 protein amino acid sequence which has been manipulated to facilitate the crystallisation of the protein, and in particular provide soakable crystal forms of the protein into which a PDE5 ligand or potential ligand may be introduced by soaking the crystal in a solution comprising the ligand so that the ligand can enter the crystal and bind to the active site of the protein in the process of crystal soaking. The term includes a PDE5 protein that has been subjected to manipulations of the amino acid sequence of the catalytic domain of PDE5, specifically the 657-682 region of PDE5 (the “loop region”) or SEQ ID No:1, and that facilitate the crystallisation of the protein and particularly provide soakable crystal forms of the protein. The relevant manipulations include manipulation by deletion, addition or substitution of one or more amino acid residues of the PDE5 loop region. Such manipulations for example include the deletion or substitution of the histidine (His/H) residue as shown emboldened and underlined in SEQ ID NO: 1 (HRGVNNSYIQRSEHPLAQLYCHSIME) to incorporate one or more amino acid residues (other than histidine), particularly amino acid residues that are neutral or non-polar. The relevant manipulations also include manipulation by complete replacement of the PDE5 loop region with a loop region (or other amino acid sequence) from another protein or protein sequence, for example another PDE such as PDE4, preferably PDE4b. The sequence modified PDE5 protein may comprise a manipulated sequence of the full PDE5 sequence or alternatively a manipulated sequence of a sub-domain or fragment of the PDE5 sequence, and is preferably a manipulated sequence of the PDE5 catalytic domain.

  • 2. A crystal according to preferred aspect 1 comprising SEQ ID NO:5.
  • 3. A crystal according to either preferred aspect 1 or preferred aspect 2 which is grown using polyethylene glycol as a precipitant Polyethylene glycol of molecular weights 2000 to 8000 are commonly used. Preferably the molecular weight of the polyethylene glycol is 4000. The polyethylene glycol may be at a concentration of between 10% and 30%, but is most preferably 20%. Additionally, the protein used to grow the crystals is desired to be of a concentration between 1 and 20 mg/ml, preferably between 5 and 15 mg/ml and most preferably is at 10 mg/ml concentration.
  • 4. A crystal according to any of the preceding preferred aspects which is grown in a buffer in the pH range of 6.5 to 8.0. Preferably the pH is in the range of 7.0 to 7.8; most preferably the pH is 7.4. The buffer should be one capable of providing buffer capacity over the required pH range, preferably HEPES.
  • 5. A crystal according to any of the preceding preferred aspects which is grown in the presence of an alcohol. Preferably the alcohol is isopropanol.
  • 6. A crystal according to any of the preceding preferred aspects which is grown in a solution containing HEPES buffer, polyethylene glycol 4000 and iso-propanol. Preferably the solution contains 0.1M sodium HEPES pH 7.4, 20% polyethylene glycol 4000 and 10% iso-propanol. The crystal is grown from a solution incubated at or below room temperature (20-25° C.). Preferably the crystal is grown from a solution incubated at a temperature within the range of 2-6° C. More preferably, the crystal is grown from a solution incubated at about 4° C.
  • 7. A crystal according to any of the preceding preferred aspects, which has one or more of the following characteristics:
    • (a) a space group C2;
    • (b) unit cell dimensions a˜56 ű1%, b˜77 ű1%, c˜81 ű1%, α=γ=90°, β=103°±1%;
    • (c) 1 molecule per asymmetric unit;
    • (d) comprises a protein of a molecular weight of approximately 40 kDa±2 kDa;
    • (e) a calculated solvent content of approximately 44±5%; and
    • (f) a monoclinic crystal system.
  • 8. A crystal according to any of the preceding preferred aspects, wherein the protein has an active site within the third sub-domain of the protein which is bounded by Helices 15 (H15 813-824) and 14 (H14 772-797), the C-terminus of Helix 13 (H13 749-765), and the C-terminus of Helix 11 (H11 706-721) along with the loop region between Helices 11 and 12a (H12a 725-731) as shown in FIG. 2.
  • 9. A crystal according to any of the preceding preferred aspects, wherein the protein has an active site within the third sub-domain of the protein and comprises Leu 765, Ala 767 and Ile 768 and one or more of Phe 820, Val 782, Phe 786, Tyr 612, Leu 804, Ala 779, Ala 783, Ile 813, Met 816 and Gln 817.
  • 10. A crystal according to in any of the preceding preferred aspects, wherein the protein has a three-dimensional structure characterised by the atomic co-ordinates set out in Table 4 or a derivative set as expressed in any reference frame.
  • 11. A crystal according to any of the preceding preferred aspects, wherein a PDE5 ligand has been soaked in. The process of soaking may involve transferring the crystal to be soaked from the solution in which it is grown into a stabilising solution containing the ligand or to which the ligand is to be added once the crystal is present in it so that the ligand can enter the crystal and preferably bind to the active site of the protein. It is desirable that the stabilising solution has the physical properties such that the crystal, when transferred, retains its structural integrity and does not crack or dissolve or alter significantly in its crystal parameters, symmetry or cell dimensions. Preferably, the stabilising solution comprises some or all of the chemical constituents from which the crystal was grown. More preferably, the stabilising solution is of similar or identical composition to the solutions used for crystal growth as set out in aspects 3 to 6 above, although the concentration of precipitant used may be slightly increased by between 1 to 10%. Most preferably the stabilising solution has the same pH as the crystal growth solution. The ligand may be added to the solution containing, or to contain, the crystal for soaking as a solid or in a liquid form (i.e. the ligand already being in solution). Preferably the ligand is in solution and the solvent maybe aqueous, organic or non-organic. Most preferably the ligand is in DMSO. The ligand is commonly added to the soaking solution to yield a final ligand concentration above the expected binding constant for the ligand by PDE5; preferably this is greater than or equal to 10 times the binding constant. The final concentration of ligand present in the crystal soaking solution is preferably between 0.1 and 20 mg/ml, more preferably between 0.5 and 10 mg/ml, and most preferably between 1 and 5 mg/ml. Optionally a cryoprotectant such as 2-methyl-2,4-pentanediol (MPD), alcohols and organic polymers e.g. lower molecular weight PEG or carbohydrates such as sorbitol or xylitol, may also added to the soaking solution if the crystal is to be frozen prior to data collection.
  • 12. A crystal according to preferred aspect 11, wherein the protein has a three-dimensional structure characterised by the atomic co-ordinates set out in Table 5 or a derivative set as expressed in any reference frame.
  • 13. A heavy atom derivative of a crystal according to any of the preceding preferred aspects.
  • 14. Use of the atomic co-ordinates determined from a crystal according to any one of preferred aspects 1 to 13 for deriving a three-dimensional structure of a PDE5 or a mutant, derivative, variant, analogue, homologue, sub-domain or fragment thereof. The co-ordinate set or a part thereof can be used according to known methods to provide a full or partial phasing model for molecular replacement procedures to determine the X-ray crystal structure of a structurally similar or related protein or protein sub-domains or fragments, additionally the coordinate set can provide a structural model from which NMR assignments for NMR structure solution of structurally similar or related proteins or protein sub-domains or fragments can be determined.
  • 15. Use according to preferred aspect 14, wherein the sub-domain is the catalytic domain.
  • 16. A method of identifying a compound which is a ligand of PDE5 comprising the following steps:
    • a) providing a crystal according any one of preferred aspects 1 to 13,
    • b) contacting the crystal with the compound under conditions conducive to soaking the compound into the crystal,
    • c) determining, by X-ray diffraction and structure solution, whether or not the compound is bound to the active site of the protein in the resultant soaked crystal,
    • d) optionally assaying the ligand to determine whether it is an inhibitor of PDE5.
  • 17. The crystal may be soaked under the conditions as set out in preferred aspect 11 and the X-ray crystal structure may be determined by X-ray diffraction of the crystal and application of any suitable known method such as direct methods, heavy atom phasing methods, single or multiple anomalous dispersion, molecular replacement or difference Fourier methods. The presence or absence of the ligand at the active site of the protein can be determined from the electron density maps, for example from difference Fourier maps or omit maps, calculated from the X-ray diffraction data.
  • 18. A method according to preferred aspect 17 wherein the compound is based on the structural template as shown in FIG. 4.
  • 19. A method of designing a compound capable of associating with PDE5, comprising the following steps:
    • (a) computationally creating a three-dimensional representation of the structure of the protein present in the crystal according to any of preferred aspects 1 to 13, or a fragment or subdomain thereof,
    • (b) computationally creating a three-dimensional representation of the structure of a compound,
    • (c) co-displaying the three-dimensional representation of the compound structure with the three-dimensional representation of the protein structure,
    • (d) assessing whether the three-dimensional representation of the compound structure fits the three-dimensional representation of an active site of the protein structure,
    • (e) optionally making assaying the ligand to determine whether it is an inhibitor of PDE5.
  • 20. A method of selecting a PDE5 ligand from a group of potential PDE5 ligands, comprising the following steps:
    • (a) computationally creating a three-dimensional representation of the structure of the protein present in the crystal according to any of preferred aspects 1 to 13, or a fragment or subdomain thereof,
    • (b) computationally creating a three-dimensional representation of the structure of the ligand,
    • (c) co-displaying the three-dimensional representation of the ligand structure with the three-dimensional representation of the protein structure,
    • (d) assessing whether the three-dimensional representation of the ligand structure fits the three-dimensional representation of an active site of the protein structure,
    • (e) optionally making and assaying the ligand to determine whether it is an inhibitor of PDE5.
  • 21. According to preferred embodiments of the preferred aspects 19 and 20 the three-dimensional representation of the structure of the protein may be directly derived from the atomic coordinates determined for the crystal and may be suitably displayed to identify the active site of the protein as defined in preferred aspect 8 and 9. The active site of the protein may be computationally and graphically rendered to display the atomic radii of the atoms comprising the active site such that a similarly graphically rendered compound molecule may be docked into the active site to look for the goodness of fit between the protein active site and the compound, preferably by examination for steric clashes and/or favourable packing and/or bonding interactions between the groups and atoms comprising the active site of the protein and those of the compound. Alternatively the resulting docked compound-protein model may be analysed computationally to assess the fit or may be adjusted computationally, for example by molecular dynamics and energy minimisation of the model, to improve the fit of the compound in the active site prior to fit analysis.
  • 22. Use of the three-dimensional structure as derivable according to preferred aspect 17 to design site-directed mutants of PDE5.


In a preferred embodiment of the preferred aspect of the invention a site directed mutant is preferably designed by computationally creating a three-dimensional representation of the structure of the protein present in the crystal according to any of preferred aspects 1 to 14, or a protein fragment or protein subdomain as may be directly derived from the atomic coordinates determined for the crystal. The model may be overlayed with, or least squares fitted against, a model of a similar or related protein or protein sequence fragment in order to allow substitution of amino acids or whole peptide regions between the model on a knowledge based basis to alter the physical characteristics of the protein, for example to substitute a known unstable loop or region with a known stable loop or region between structures (the stability of a region of protein sequence can be judged by the B factors for the protein region in the coordinate set). One or more side chain replacements, additions or deletions may be made in the model of the protein or whole fragments of polypeptide may be replaced, added or deleted to potentially affect the physical property of the protein, for example, ability to crystallise by alteration of unstable regions, solubility by substitution of hydrophobic groups with hydrophilic groups. Optionally the site directed mutant of the protein may be made and tested for the improvement in the physical parameter for example by assessing ability to crystallise the mutated protein or the solubility of the mutated protein in comparison to the native protein. Alternatively site directed mutation of the active site residues may be designed in order to assess side chains involved in key bond donor or acceptor functions with a PDE5 ligand or potential ligand compound, or to design active site mutations to better accommodate a compound. This may be achieved by co-displaying the protein and compound models as detailed in preferred aspects 18 and/or 19 and making replacements of protein side chains at the active site of the protein model in order to assess, either by graphics visualisation of the fit and bonding interactions between the compound and the protein model or by computational analysis of the model complex for steric fit or clashing and/or bonding interactions, whether a compound is better accommodated in the active site by such changes; this process may optionally involve model energy minimisation and/or molecular dynamics steps as described in the persevered embodiments in preferred aspects 18 and/or 19. Optionally the site directed mutant of the protein may be made and assayed in a PDE5 ligand binding assay.

  • 23. A method of soaking a compound into a crystal according to any one of preferred aspects 1 to 13 comprising the following steps:
    • (a) incubating the crystal in an aqueous stabilising solution comprising buffer and polyethylene glycol;
    • (b) combining the compound with the stabilising solution; and
    • (c) optionally adding a cryo-protectant to the stabilising solution.


Preferably the stabilising solution is of similar or identical composition to the solutions used for crystal growth as set out in aspects 3 to 6 above, although the concentration of precipitant used may be slightly increased by between 1 to 10%. Most preferably the stabilising solution has the same pH as the crystal growth solution. More preferably the stabilising solution comprises 0.1M sodium hepes pH 7.4, 20% PEG 4000, 10% isopropanol. Preferably the compound is in solution and the solvent maybe aqueous, organic or non-organic. Most preferably the compound is in DMSO. The ligand is commonly added to the soaking solution to yield a final ligand concentration above the expected binding constant for the ligand by PDE5; preferably this is greater than or equal to 10 times the binding constant. The final concentration of ligand present in the crystal soaking solution is preferably between 0.1 and 20 mg/ml, more preferably between 0.5 and 10 mg/ml, and most preferably between 1 and 5 mg/ml. Preferably the cryoprotectant is selected from one or more of 2-methyl-2,4-pentanediol (MPD), alcohols, organic polymers e.g. lower molecular weight PEG, carbohydrates such as sorbitol or xylitol, most preferably the cryoprotectant is glycerol.


DETAILED DESCRIPTION OF THE INVENTION

The term “apo” as used herein is taken to mean macromolecule and in particular any protein (or named protein) that is detached from a/its ligand(s) and/or prosthetic group(s).


The term “buffer” as used herein is taken to include any solution containing a weak acid and a conjugate base of this acid (or, less commonly, a weak base and its conjugate acid). Thus, a “buffer” as used herein resists change in its pH level when an acid or a base is added to it, because the acid neutralises an added base (or, less commonly, the base neutralises an added acid).


An “activity assay” as referred to herein with reference to PDE5 is taken to mean an in vitro assay of PDE inhibitory activities against cyclic guanosine 3′,5′-monophosphate (cGMP) and cyclic adenosine 3′,5′-monophosphate (cAMP) phosphodiesterases which can be determined by measurement of their IC50 values (the concentration of compound required for 50% inhibition of enzyme activity). Preferably the required PDE enzymes can be isolated from a variety of sources, including human corpus cavernosum, human and rabbit platelets, human cardiac ventricle, human skeletal muscle and bovine retina, essentially by a modification of the method of Thompson W J and Appleman M M; Biochemistry 10(2),311-316, 1971, as described by Ballard S A et al.; J. Urology 159(6), 2164-2171, 1998. In particular, cGMP-specific PDE5 and cGMP-inhibited cAMP PDE3 can be obtained from human corpus cavernosum tissue, human platelets or rabbit platelets.


Assays can be performed either using a modification of the “batch” method of Thompson, W J et al.; Biochemistry 18(23), 5228-5237, 1979, essentially as described by Ballard S A et al.; J. Urology 159(6), 2164-2171, 1998, or using a scintillation proximity assay for the direct detection of [3H]-labelled AMP/GMP using a modification of the protocol described by Amersham plc under product code TRKQ7090/7100. In summary, for the scintillation proximity assay, the effect of PDE inhibitors are investigated by assaying a fixed amount of enzyme in the presence of varying inhibitor concentrations and low substrate (cGMP or cAMP in a 3:1 ratio unlabelled to [3H]-labeled at a concentration of ˜1/3 Km or less), such that IC50≅Ki. The final assay volume is made up to 100 μl with assay buffer [20 mM Tris-HCl pH 7.4, 5 mM MgCl2, 1 mg/ml bovine serum albumin]. Reactions are initiated with enzyme, incubated for 30-60 min at 30° C. to give <30% substrate turnover and terminated with 50 μl yttrium silicate SPA beads (containing 3 mM of the respective unlabelled cyclic nucleotide for PDE5). Plates are re-sealed and shaken for 20 min, after which the beads are allowed to settle for 30 min in the dark and then counted on a TopCount plate reader (Packard, Meriden, Conn.). Radioactivity units are converted to % activity of an uninhibited control (100%), plotted against inhibitor concentration, and inhibitor IC50 values obtained using the ‘Fit Curve’ Microsoft Excel extension.


The term “precipitant” as used herein is taken to include any substance that, when added to solution comprising a biological molecule, causes the biological molecule to precipitate or crystallise from the solution.


The term “complex” as used herein is taken to mean a biological macromolecule, preferably a protein, with ligand(s) bound and may be formed before, during or after protein crystallisation.


The term “soaking” or “capable of being soaked” as used herein is taken to mean a process of placing a crystal in an aqueous solution containing a chemical compound, (usually) small molecule (e.g. inhibitor), or adding a chemical compound to an aqueous solution containing a crystal such that the compound may be able to enter the crystal lattice by diffusion and may interact (e.g. contact and bond with) with the molecules comprising the lattice preferably, where the molecules comprising the lattice are protein molecules, to form a protein-ligand complex, most preferably where the molecules comprising the lattice are protein molecules and the ligand or compound become bound to the active site of the protein molecule. The compound may be added to the aqueous solution in solid form, or it may be dissolved in a suitable solvent, preferably di-methyl-sulphoxide (DMSO).


The term “soakable crystal” as used herein is taken to mean a crystal into which a small molecule or ligand may be soaked without significant disruption of the lattice such that the ligand can enter and pass through the crystal lattice and have access to, and may associate with, the molecules comprising the lattice. Preferably a soakable crystal is a crystal which is ameanable to the soaking process in which a small molecule or ligand either in solution or in solid form is added to the solution containing the crystal. The small molecule may then enter the crystal lattice by diffusion and associate with the molecules comprising the crystal lattice. It is preferable that the soakable crystal binds the ligand without disruption of the lattice or cracking of the crystal and that the lattice symmetry and crystal parameters are not significantly altered by the soaking and ligand binding process. It is preferable that the soakable crystal diffracts X-rays to atomic resolution, preferably to beyond 3.5 Å, more preferably beyond 2.5 Å, most preferably 1.5 Å, after undergoing the soaking process.


The term “stabilising solution” as used herein is taken to mean a solution into which a crystal may be transferred for the purposes of further manipulation, for example for soaking, and in which the crystal retains its structural integrity and does not crack or dissolve or alter significantly in its crystal parameters, symmetry or cell dimensions. Preferably the stabilising solution comprises some or all of the chemical constituents from which the crystal was grown and is of the approximately the same, and more preferably identical, pH.


The term “cryoprotectant” as used herein is taken to mean a chemical compound which, when added to a solution, allows the solution to be rapidly frozen without the formation of ice crystals. Such a cryoprotectant is preferably an alcohol such as ethanol or a carbohydrate such as xylitol or sorbitol, but may also be 2-methyl-2,4-pentanediol (MPD) or other organic polymers e.g. lower molecular weight PEG. Most preferably the cryoprotectant is glycerol.


The term “co-crystallisation” as used herein is taken to mean crystallisation of a pre-formed comple of a macromolecule with its ligand i.e. a protein/small molecule complex.


The terms “mutant”, “variant”, “homologue”, “analogue”, “derivative” or “fragment”, are in relation to the amino acid sequence of the PDE5 protein or polypeptide sequence which is used to produce the crystal of the present invention. The terms include any substitution of, variation of, modification of, replacement of, deletion of, or addition of one (or more) amino acids from (or to) the sequence providing the resultant PDE5 is capable of being crystallised.


Typically, for the “mutant”, “variant”, “homologue”, “analogue”, “derivative” or “fragment” in relation to the amino acid sequence of the protein or polypeptide of the PDE5 of the crystal of the present invention, the types of amino acid substitutions that could be made should maintain the hydrophobicity/hydrophilicity of the amino acid sequence. Amino acid substitutions may be made, for example from 1, 2 or 3 to 10, 20 or 30 substitutions, provided that the modified PDE5 retains the ability to be crystallised in accordance with present invention. Amino acid substitutions may include the use of non-naturally occurring analogues.


In relation to amino acid sequences, the term “variant” as used herein refers to additions, deletions or substitutions of amino acid residues comprised within the wild-type amino acid sequence or fragment thereof. Preferably, a variant in relation to the amino acid sequence of the crystal of the PDE5 of the present invention could include the deletion or substitution of the histidine (His/H) residue as shown emboldened and underlined in SEQ ID NO: 1 (HRGVNNSYIQRSEHPLAQLYCHSIME), which sequence is comprised in the protein or polypeptide of PDE5 of the crystal of the present invention. Replacement of said histidine (H) residue is preferably by way of incorporating one or more amino acid residues (other than histidine), preferably wherein said amino acid residues are neutral or non-polar.


The terms “mutant”, “variant”, “homologue”, “analogue”, “derivative” or “fragment” in relation to the nucleotide sequence coding for the PDE5 of the crystal of the present invention include any substitution of, variation of, modification of, replacement of, deletion of, or addition of, one (or more) nucleotide from (or to) the sequence providing the resultant nucleotide sequence codes for, or is capable of coding for, a PDE5 which is capable of being crystallised.


In relation to nucleotide sequences, the term “variant” as used herein refers to additions, deletions or substitutions of nucleotides of the wild-type nucleotide sequence or fragment thereof.


The term “fragment” as used herein refers to any portion of the PDE5 amino acid sequence as defined in the present invention provided the resultant PDE5 comprising said PDE5 portion is capable of being crystallised. Thus, the term “fragment” also includes PDE5, which comprises any portion of SEQ ID NOS: 1, 2, 3, 4, 5, or 6.


An example of a specific fragment of SEQ ID NO: 6 (full-length “loop-swapped” PDE5 sequence) according to the present invention could be SEQ ID NO: 5 (“loop-swapped” PDE5 catalytic domain). Moreover, an example of a specific fragment of SEQ ID NO: 5 (“loop-swapped” PDE5 catalytic domain) according to the present invention could be SEQ ID NO: 4 (PDE4 “loop region”; HPGVSNQFLINTNSELALMYNDESVLE).


The term “analogue” as used herein means a sequence similar to the amino acid sequence of the PDE5 polypeptide of the crystal of the present invention or of any one of SEQ ID NOS: 1, 2, 3, 4, 5 or 6, but wherein non-detrimental (i.e. not detrimental to the PDE5's capability of being crystallised) amino acid substitutions or deletions have been made.


The term “derivative” as used herein in relation to the amino acid sequence of the PDE5 of the crystal of the present invention, or of any one of SEQ ID NOS: 1, 2, 3, 4, 5 or 6, includes chemical modification of PDE5. Illustrative of such modifications would be replacement of hydrogen by an alkyl, acyl, or amino group.


The term “heavy atom derivative” as used herein in relation to crystals refers to a crystal comprising macromolecules in the crystal lattice which are modified by the inclusion of a heavy atoms (i.e. of significantly greater atomic mass than the atoms common to organic macromolecules, e.g. carbon, nitrogen, oxygen, phosphorous, etc.) into their structure. This is commonly achieved using ionic compounds such as salts of mercury, platinum, gold or silver which may covalently bond to certain groups on the macromolecule either during co-crystalisation with the ionic compound or by soaking the compound into the crystal. Other processes may also be used such as derivitisation with seleno-methionine or with noble gases such as Xenon. The purpose of such heavy atom derivatives of crystals is to provide phasing information for structure solution.


As used herein a “deletion” is defined as a change in either nucleotide or amino acid sequence in which one or more nucleotides or amino acid residues, respectively, are absent.


As used herein an “insertion” or “addition” is a change in a nucleotide or amino acid sequence, which has resulted in the addition of one or more nucleotides or amino acid residues, respectively, as compared to the sequences of the naturally occurring PDE5.


As used herein “substitution” results from the replacement of one or more nucleotides or amino acids by different nucleotides or amino acids, respectively.


Conservative substitutions may be made, for example according to the Table below. Amino acids in the same block in the second column and preferably in the same line in the third column may be substituted for each other:

ALIPHATICNon-polarG A PI L VPolar - unchargedC S T MN QPolar - chargedD EK RAROMATICH F W Y


The term “homologue” covers homology specifically with respect to protein structure, primary secondary, tertiary and quaternary, and covers any structural PDE5 homologue that is capable of being crystallised.


With respect to homology of the amino acid sequences detailed herein, preferably there is at least 70%, more preferably at least 75%, more preferably at least 80%, yet more preferably at least 85%, even more preferably at least 90% homology to SEQ ID NOS: 1, 2, 3, 4, 5 or 6. More preferably there is at least 95%, and most preferably at least 98%, homology to SEQ ID NOS: 1, 2, 3, 4, 5 or 6.


With respect to homology of the nucleotide sequences coding for the amino acid sequences detailed herein, preferably there is at least 70%, more preferably at least 75%, more preferably at least 80%, yet more preferably at least 85%, even more preferably at least 90% homology to the nucleotide sequences which code for SEQ ID NOS: 1, 2, 3, 4, 5 or 6. More preferably there is at least 95%, and most preferably at least 98%, homology to the nucleotide sequences which code for SEQ ID NOS: 1, 2, 3, 4, 5 or 6.


The term “homologue” with respect to the nucleotide sequence of the PDE5 as defined in the present invention and the amino acid sequence of the PDE5 as defined in the present invention may be synonymous with allelic variations of the sequences.


In particular, the term “homology” as used herein may be equated with the term “identity”. Here, sequence homology with respect to, for example, the amino acid sequence of PDE5 of the crystal of the present invention can be determined by a strict comparison of any one or more of the sequences with another sequence to see if that other sequence has at least 70% identity to the sequence(s). Relative sequence homology (i.e. sequence identity) can also be determined by commercially available computer programs that can calculate percentage (%) homology between two or more sequences. A typical example of such a computer program is CLUSTAL.


Percentage homology may be calculated over contiguous sequences, i.e. one sequence is aligned with the other sequence and each amino acid in one sequence directly compared with the corresponding amino acid in the other sequence, one residue at a time. This is called an “ungapped” alignment. Typically, such ungapped alignments are performed only over a relatively short number of residues (for example less than 50 contiguous amino acids).


Although this is a very simple and consistent method, it fails to take into consideration that, for example, in an otherwise identical pair of sequences, one insertion or deletion will cause the following amino acid residues to be put out of alignment, thus potentially resulting in a large reduction in % homology when a global alignment is performed. Consequently, most sequence comparison methods are designed to produce optimal alignments that take into consideration possible insertions and deletions without penalising unduly the overall homology score. This is achieved by inserting “gaps” in the sequence alignment to try to maximise local homology.


However, these more complex methods assign “gap penalties” to each gap that occurs in the alignment so that, for the same number of identical amino acids, a sequence alignment with as few gaps as possible—reflecting higher relatedness between the two compared sequences—will achieve a higher score than one with many gaps. “Affine gap costs” are typically used that charge a relatively high cost for the existence of a gap and a smaller penalty for each subsequent residue in the gap. This is the most commonly used gap scoring system. High gap penalties will of course produce optimised alignments with fewer gaps. Most alignment programs allow the gap penalties to be modified. However, it is preferred to use the default values when using such software for sequence comparisons. For example when using the GCG Wisconsin Bestfit package (see below) the default gap penalty for amino acid sequences is −12 for a gap and −4 for each extension.


Calculation of maximum percentage homology therefore firstly requires the production of an optimal alignment, taking into consideration gap penalties. A suitable computer program for carrying out such an alignment is the GCG Wisconsin Bestfit package (University of Wisconsin, U.S.A.; Devereux et al., 1984, Nucleic Acids Research 12:387). Examples of other software than can perform sequence comparisons include, but are not limited to, the BLAST package (see Ausubel et al., 1999 ibid—Chapter 18), FASTA (Atschul et al., 1990, J. Mol. Biol., 403-410) and the GENEWORKS suite of comparison tools. Both BLAST and FASTA are available for off-line and on-line searching (see Ausubel et al., 1999 ibid, pages 7-58 to 7-60). However, for some applications it is preferred to use the GCG Bestfit program.


Although the final percentage homology can be measured in terms of identity, in some cases, the alignment process itself is typically not based on an all-or-nothing pair comparison. Instead, a scaled similarity score matrix is generally used that assigns scores to each pairwise comparison based on chemical similarity or evolutionary distance. An example of such a matrix commonly used is the BLOSUM62 matrix—the default matrix for the BLAST suite of programs. GCG Wisconsin programs generally use either the public default values or a custom symbol comparison table if supplied (see user manual for further details). It is preferred to use the public default values for the GCG package, or in the case of other software, the default matrix, such as BLOSUM62.


Once the software has produced an optimal alignment, it is possible to calculate percentage homology, preferably percentage sequence identity. The software typically does this as part of the sequence comparison and generates a numerical result.


As indicated, for some applications, sequence homology (or identity) may be determined using any suitable homology algorithm, using for example default parameters. For a discussion of basic issues in similarity searching of sequence databases, see Altschul et al (1994) Nature Genetics 6:119-129. For some applications, the BLAST algorithm is employed, with parameters set to default values. The BLAST algorithm is described in detail at http://www.ncbi.nih.gov/BLAST/blast_help.html. Advantageously, “substantial homology” when assessed by BLAST equates to sequences which match with an EXPECT value of at least about 7, preferably at least about 9 and most preferably 10 or more. The default threshold for EXPECT in BLAST searching is usually 10.


Other computer program methods to determine identify and similarity between the two sequences include but are not limited to the GCG program package (Devereux et al 1984 Nucleic Acids Research 12: 387) and FASTA (Atschul et al 1990 J Molec Biol 403-410).


The amino acid sequence of the PDE5 of the present invention present invention may be produced by expression of a nucleotide sequence coding for the same in a suitable expression system.


In addition, or in the alternative, the protein itself could be produced using chemical methods to synthesize a PDE5 amino acid sequence, in whole or in part. For example, peptides can be synthesized by solid phase techniques, cleaved from the resin, and purified by preparative high performance liquid chromatography (e.g. Creighton (1983) Proteins Structures and Molecular Principles, W H Freeman and Co., New York, N.Y., USA). The composition of the synthetic peptides may be confirmed by amino acid analysis or sequencing (e.g. the Edman degradation procedure).


Direct peptide synthesis can be performed using various solid-phase techniques (Roberge J Y et al, Science, Vol 269, 1995, pp. 202-204) and automated synthesis may be achieved, for example, using the ABI 431 A Peptide Synthesizer (Perkin Elmer, Boston, Mass., USA) in accordance with the instructions provided by the manufacturer. Additionally, the amino acid sequence of PDE5, or any part thereof, may be altered during direct synthesis and/or combined using chemical methods with a sequence from other subunits, or any part thereof, to produce a variant polypeptide.


Protein Engineering of PDE5*


Analysis of the catalytic domain of wild-type PDE5 protein by mass spectrometry and SDS-PAGE (data not shown) shows that the protein is cleaved within the region of residues 664-682. High concentrations of protease inhibitors provide some stabilisation of the protein, but cleavage still prevents reproducible crystallisation.


An engineered form of the catalytic domain of PDE5, called ‘PDE5*’, has been produced where the 657-682 region of PDE5 has been replaced by the same region in PDE4 producing a chimeric construct, (see FIG. 1 for sequence alignment of this region). The C-terminus of this construct is also truncated (C-term 858) compared to the wild-type structure (C-term 875). Hereafter this engineered construct will be referred to as ‘PDE5*’.


This engineered protein has been shown to be stable to degradation by mass spectrometry and SDS-PAGE (data not shown). The protein shows improved biophysical properties allowing an alternative purification protocol to be developed.


The new protocol utilises binding to a Blue sepharose column and specific elution with cGMP. The wild-type protein had been shown not to bind to this column probably due to the disorder of the structure around the protease cleavage site. This PDE5* protein was used to produce crystals with inhibitors which diffract to higher resolution and have no disordered regions. The protein has also been used reproducibly to produce crystals with further inhibitors which routinely diffract to 1.8 Å resolution or higher, making it an improved protein for use in structure based drug design.


The Structure of PDE4 and Wild Type PDE5 Catalytic Domains


(This is also detailed in Application Number PCT/IB02/04426, page 28, line 19 to page 29, line 17 and is incorporated herein by reference.)


The structure of the catalytic domain of PDE4b was published (Xu et al. 2000). A topological comparison of the PDE5 catalytic domain with the structures in the Protein Data Bank (PDB) does not reveal significant additional homology with other known protein structures except for the PDE4 structure. Comparisons between the two structures have been made (FIG. 1 of the present application shows a sequence and secondary structural alignment of the two proteins). The structure and domain arrangement is virtually identical to that of PDE4, save that the second sub-domain highlighted in PDE4 is only partially present in the PDE5 structure, as detailed below.


The structure is composed of a single domain of 15 α helices arranged in a compact fold (FIG. 2 of the present application). Within the overall domain, three sub-domains can also be defined. Helices 1 (H1 539-545) and 2 (H2 551-554) lie on the exterior of the protein and comprise the N-terminal region of the construct. These two helices do not overlay with the equivalent ones (H0, H1 and H2) in the PDE4 structure. This region is not well conserved across the PDE protein family. Helices 3 (H3 568-582), 4 (H4 584-588), 5 (H5 592-604), 6 (H6 615-631) and 7 (H7 640-652) form the first sub-domain of the protein and are contained within the core of the protein. There is no observable electron density for helices 8 and 9 based on the PDE4 nomenclature. Helix 10 (H10 684-694) is again on the exterior and forms the dimer interface within the structure. Helices 10 and 11 (H11 706-721) are the visible portion of the second sub-domain. Helices 12 (H12a 725-731, H12b 733-741), 13 (H13 749-765), 14 (H14 772-797), 15 (H15 813-824), 16 (H16 826-836) and 17 (H17 841-861) form the third sub-domain of the protein. It should be noted that in PDE5 helix H12 is not a contiguous helix as in PDE4 but is composed of two short helices with a kink in the middle and helix H15 is a contiguous helix in PDE5 but not in PDE4.


Structure of PDE5* Catalytic Domain Complexed with UK-088,800


The structure of the catalytic domain of PDE5* protein complexed with UK-088,800 was determined by molecular replacement using one molecule of the protein structure from the PDE5* complex with Sildenafil (as described in Application Number PCT/IB02/04426: Example 11, “crystallisation of PDE5* with Sildenafil”, page 46, lines 8 to 25; Example 15, “data collection, structure determination and refinement PDE5* with Sildenafil”, page 50, line 9 to page 51, line 6 and Table 6, “atomic co-ordinates for baculovirus-expressed PDE5* complex with Sildenafil”, pages 328 to 408; incorporated herein by reference) as a basis for the search model, the co-ordinates for which are included in Table 3 of the present application. The PDE5* catalytic domain crystallises in the space group C2 as a monomer with one molecule present in the asymmetric unit. The C2 form of the PDE5* catalytic domain crystallises in the space group C2 with approximate cell dimensions a=55.97 Å, b=76.55 Å, c=80.50 Å and β=103.09. They contain one molecule per asymmetric unit and have a solvent content of 44% (Matthews, 1969). The structure of the PDE5* comprises 17 α helices and the overall fold is very similar to the wild-type structure with a number of important differences. The major difference in the structure is the presence of helices H8 and H9 composed of the swapped portion from PDE4, residues 657-682. These fold in an identical way to that observed in the PDE4 structure and complete the second sub-domain of the protein. The entire C-terminal region of this construct can also be built into the electron density leaving just three disordered residues at the N-terminus of this structure. This is likely to contribute to its enhanced properties for crystallisation.


PDE5*: Active Site and Protein-inhibitor Interactions


UK-088,800 occupies the same region of the active site as observed for the previously described UK-092,480, Sildenafil, as detailed below (Application Number PCT/IB02/04426: FIG. 4, “A view of compound Sildenafil bound to loop swapped PDE5 (PDE5*), page 425; incorporated herein by reference) and demonstrates the same mainly hydrophobic interactions with the protein (FIG. 3 “Comparison of the fo-fc electron density map contoured at 2.5σ of apo PDE5* (left) and PDE5* soaked with UK-088,800 (right), at the active site region” of the present application). The same two direct hydrogen bonds observed in the complex of PDE5* with Sildenafil are also observed between Gln 817 of the protein and inhibitor (Oε1-N4 2.9 Å and Nε2-O1 3.1 Å).


Carbon atom C7 of the inhibitor points into a small hydrophobic pocket formed by Leu 765, Ala 767 and Ile 768. These residues, together with Phe 820, form a planar face to the binding site against which the purine ring of the inhibitor stacks. The opposite side of the purine packs against Val 782. The C10 propyl substituent form good van der Waals contacts with Phe 786. Phe 786 packs against Leu 804 which in turn forms additional hydrophobic interactions with the phenyl moiety of the inhibitor. The O-alkyl moiety occupies a small pocket bounded by Ala 779, Phe 786, Ala 783, Val 782, Leu 804, Ile 813, Met 816 and Gln 817. There is no direct interaction between the inhibitor and the zinc ion found in the active site. The structure confirms the competitive nature of the mode of inhibition of UK-088,800 by binding in the active site, therefore blocking access for the cGMP substrate (which has also been modelled—data not included).


The main difference comparing Sildenafil and UK-088,800 is that the latter inhibitor lacks the sulphonylpiperazine present in Sildenafil which points out of the active site.


Wild-type PDE5-Sildenafil Complex: Active Site and Protein-inhibitor Interactions


(This is detailed in Application Number PCT/IB02/04426, page 30, line 8 to page 31, line 1, and is incorporated herein by reference.)


The active site lies mainly within the third sub-domain of the protein and is bounded by helices H15, H14, the C-terminus of H13, and the C-terminus of H11, along with the loop region between H11 and H12a. The majority of the interactions between the inhibitor and the protein are hydrophobic in nature, with only two direct hydrogen bonds observed (Application Number PCT/IB02/04426: FIG. 3, page 424, incorporated herein by reference). The first is between N17 of the purine ring of the inhibitor and Oε1 of Gln 817 (2.8 Å) and the second is from the adjacent oxygen atom O16 of the inhibitor to Nε2 of the same residue Gln 817 (3.1 Å).


Carbon atom C12 of the inhibitor points into a small hydrophobic pocket formed by Leu 765, Ala 767 and Ile 768. These residues, together with Phe 820, form a planar face to the binding site against which the purine ring of the inhibitor stacks. The opposite side of the purine packs against Val 782. The C5 propyl substituent forms good van der Waals contacts with Val 782 and Phe 786 and Tyr 612. Phe 786 and Leu 804 form additional hydrophobic interactions with the phenyl moiety of the inhibitor. The O-alkyl moiety occupies a small pocket bounded by Ala 779, Phe 786, Ala 783, Val 782, Leu 804, Ile 813, Met 816 and Gln 817. The sulphonamide group points out towards the solvent whilst the piperazine ring is bounded by the extended residues 662-665, although whether the conformation of this part of the structure is unaffected by the chain break is questionable. There is no direct interaction between the inhibitor and the zinc ion found in the active site. The structure confirms the competitive nature of the mode of inhibition of Sildenafil by binding in the active site therefore blocking access for the cGMP substrate (which has also been modelled—data not included).


Wild Type PDE5-Sildenafil Complex: Metal Ions in the Active Site


Only one zinc atom is present in the active site of this structure. The co-ordination of the ion within the active site is also consistent with that expected for zinc. The metal is co-ordinated by His 653 (Nε2-Zn 2.0 Å), His 617 (Nε2-Zn 2.1 Å), Asp 764 (OD2-Zn 2.2 Å) and also Asp 654 (OD2-Zn 2.2 Å). These residues are completely conserved across the PDE gene family. There is no evidence of a second metal ion in the active site.


The present invention will now be described, by way of example only, with reference to the accompanying Sequence Listing and Figures, in which:

  • SEQ ID NO: 1 shows the amino acid sequence of the loop region from PDE5.
  • SEQ ID NO: 2 shows the amino acid sequence of the wild-type PDE5 catalytic domain.
  • SEQ ID NO: 3 shows the amino acid sequence of the full-length wild-type PDE5 sequence.
  • SEQ ID NO: 4 shows the amino acid sequence of the loop region of PDE4.
  • SEQ ID NO: 5 shows the amino acid sequence of the loop-swapped PDE5 catalytic domain=PDE5*.
  • SEQ ID NO: 6 shows the amino acid sequence of full-length PDE5 sequence comprising PDE5*.
  • SEQ ID NOS: 7-14 are oligonucleotide primers.



FIG. 1 shows an alignment of PDE5 (upper sequence) and PDE4b (lower sequence) catalytic domains. Positions and numbering of helices from the structures are marked for each. Residues in bold show a sequence alignment for the engineered region. The sequence from PDE4 has been used to replace the corresponding region in PDE5. This results in a residue insertion in this region. Underlining highlight C-terminal region absent in PDE5*.



FIG. 2 shows a ribbon representation of the overall fold of proteins showing secondary structure elements. The inhibitor is shown in an all atom stick representation and the metal ions as spheres. (A)=PDE4b, (B)=wild-type PDE5+Sildenafil, (C)=“loop-swapped” PDE5 (PDE5*)+Sildenafil. Helices are numbered using PDE4 structure as reference. Helices H0-H7 form sub-domain 1, helices H8-H11 form sub-domain 2, and helices H12-H16 form sub-domain 3.



FIG. 3: Comparison of the fo-fc electron density map contoured at 2.5σ of apo PDE5* (“loop-swapped” PDE5) (left) and PDE5* soaked with UK-088,800 (right), at the active site region.



FIG. 4: A two dimensional representation of the structure of UK-088,800, 5-(2-ethoxyphenyl)-1-methyl-3-propyl-1,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one (only the Hydrogen on N4 is illustrated).


Experimental Section







EXAMPLE 1
Construction and Expression of PDE5 Wild-type Catalytic Domain (E534-N875)

Oligonucleotide primers were designed from the sequence of human PDE5 (Accession number=AB001635). DNA fragments were generated by PCR amplification from a full-length PDE5 clone. The following oligonucleotides were used:

PDE5 5′ Untagged Oligo:CGTGAATTCATGGAGGAAGAAACAAGAGAGCTAC(SEQ ID NO: 7)PDE5 3′ Long Oligo:CGTTCTAGACTATCAGTTCCGCTTGGCCTGGCCGCT(SEQ ID NO: 8)TTCCCC


The PCR reaction was carried out for 30 cycles in a total volume of 50 μl in a solution containing 1.5 mM MgCl2, 200 μM dNTPs, 50 pmol of each primer and 2.5 units of Expand DNA polymerase (Roche, East Sussex, UK). Each cycle was 94° C., 1 min, 50° C., 1 min and 72° C., 2 mins.


The final amplified DNA fragments for both constructs were separated on a 1% agarose gel and purified using a QIAquick gel extraction kit (Qiagen, West Sussex, UK). The fragment was then digested using EcoRI and XbaI, and ligated into pFastbacl EcoRI/XbaI-digested vector (Life Technologies, Paisley, UK). The ligation was carried out at 12° C. for 16 hours. The ligation mix was then electroporated into E. coli (TOP 10) (Invitrogen, Gronigen, The Netherlands).


Clones containing the desired insert were selected by using 2YT plates containing 100 μg/ml ampicillin and checked using endonuclease digestion for presence of correct size insert. DNA sequence analysis was carried out by Lark (Saffron Waldon, UK).


Recombinant bacmid DNA was produced by transforming E.coli DH10BAC™ with pFastbacl::PDE5 catalytic domain (534-875) plasmid DNA. This was carried out according to the method shown in the Bac to Bac™ baculovirus expression manual (Life Technologies, Paisley, UK). PCR analysis was used to verify successful transposition to the bacmid using pUC/M13 amplification primers (Invitrogen, Gronigen, The Netherlands).


Generation of primary baculovirus stocks was carried out by transfection using Sf-9 insect cells. Bacmid DNA containing the correct insert was mixed with CELLFECTIN™ transfection reagent (Life Technologies, Paisley, UK) and added to a monolayer of Sf-9 insect cells using SF-900II serum free medium (Invitrogen, Gronigen, The Netherlands). Following 72 hours incubation at 27° C. the supernatant was harvested as the initial baculovirus stock. This stock was amplified by adding the initial virus stock into a suspension of Sf-9 insect cells at 1×106 cells/ml in 1 litre Erlenmeyer flasks (Corning Life Sciences, New York, USA), at an agitation of 125 rpm at 27° C. After 6 days post infection the supernatant was harvested by centrifugation and stored at 4° C. as the working virus stock. The titre of this working stock was determined by conventional plaque assay analysis as in the Bac to Bac baculovirus expression manual (Invitrogen, Gronigen, The Netherlands).


Protein expression was optimised in Erlenmeyer flask cultures using Sf-9 and T.ni High5 insect cell cultures looking at different multiplicity's of infection (MOI) and harvest times, the optimal conditions found were then scaled up into fermenters.


The fermenters used were autoclavable Applikon 3 litre stirred vessels controlled using Applikon 1030 biocontrollers. Inoculum of T.ni High5 cells was initially prepared from shake flask cultures. The fermenter was inoculated with 5×105 cells/ml, with an initial working volume of 1.8 litres made up in Excel 405 serum free medium (JRH Biosciences, Kansas, USA). Temperature was controlled at 27° C., dissolved oxygen concentration controlled at 60% and pH was measured but not controlled. Oxygen concentration was controlled throughout. Agitation was set at 150 rpm with a double impeller system of marine impeller within the culture and Rushton impeller at the liquid/headspace interface. Aeration was continuous to the headspace at 0.5 l/min.


When the viable cell density reached 2×106 cells/ml the culture was infected using an MOI of 1 from the titred baculovirus working stock. Harvest time for the culture was 48 hours post infection. This was achieved by centrifugation at 2000 g for 15 mins; the insect cell pellet was then stored at −80° C. prior to purification.


EXAMPLE 2
Construction and Expression of His6-tagged PDE5 Wild-type Catalytic Domain (E534-N875)

Oligonucleotide primers were designed from the sequence of human PDE5 (=PDE5A1 isoform; Accession number=AB001635). DNA fragments were generated by PCR amplification from a full-length PDE5 clone. The following oligonucleotides were used:

PDE5 5′ His6 OligoCGTGAATTCATGCATCATCATCATCATCATCTTCTG(SEQ ID NO: 9)GTTCCGCGTGGATCTGCGCCCGAGGAAGAAACAAGAGAGCTACPDE5 3′ Long OligoCGTTCTAGACTATCAGTTCCGCTTGGCCTGGCCGCT(SEQ ID NO: 8)TTCCCC


The PCR reaction was carried out for 30 cycles in a total volume of 50 μl in a solution containing 1.5 mM MgCl2, 200 μM dNTPs, 50 pmol of each primer and 2.5 units of Expand DNA polymerase (Roche, East Sussex, UK). Each cycle was 94° C., 1 min, 50° C., 1 min and 72° C., 2 mins.


The final amplified DNA fragments for both constructs were separated on a 1% agarose gel and purified using a QIAquick gel extraction kit (Qiagen, West Sussex, UK). The fragment was then digested using EcoRI and XbaI, and ligated into pFastbacl EcoRI/XbaI-digested vector (Life Technologies, Paisley, UK). The ligation was carried out at 12° C. for 16 hours. The ligation mix was then electroporated into E. coli (TOP 10) (Invitrogen, Gronigen, The Netherlands).


Clones containing the desired insert were selected by using 2YT plates containing 100 μg/ml ampicillin and checked using endonuclease digestion for presence of correct size insert. DNA sequence analysis was carried out by Lark (Saffron Waldon, UK).


Methods to generate the recombinant baculovirus were as those for wild-type PDE5 catalytic domain (see EXAMPLE 1).


Expression optimisation again showed T.ni High5 insect cells to give the best expression. Therefore baculovirus expression in fermenters was carried out using the same procedures as for the previous construct.


EXAMPLE 3
Construction and Expression of PDE5* (E534-E858) in Baculovirus

The PDE5* construct was produced by using overlap extension PCR where the following oligonucleotides were used:

A:CGTGAATTCATGGAGGAAGAAACAAGAGAGCTAC(SEQ ID NO: 7)B:CAAAGAAAGTTCTGAATTTGTGTTGATGAGAAAC(SEQ ID NO: 10)TGATTGGAGACTCCAGGATGATCCAAATCGTGGCTTAGC:ATCAACACAAATTCAGAACTTGCTTTGATGTATA(SEQ ID NO: 11)ATGATGAATCTGTGTTGGAACACCATCATTTTGACCAGD:CGTTCTAGACTATCATTCTGCAAGGGCCTGCCAT(SEQ ID NO: 12)TTCTG


Initial DNA fragments were generated using oligonucleotides A+B and C+D with the same template DNA as for the wild-type PDE5 catalytic domain construct. The PCR reaction was carried out for 30 cycles in a total volume of 50 μl in a solution containing 1.5 mM MgCl2, 200 μM dNTPs, 50 pmol of each primer and 2 units of Expand DNA polymerase (Roche, East Sussex, UK). Each cycle was 94° C., 1 min, 50° C., 2 min, and 72° C., 3 min. In the second round of PCR, DNA products from PCR A+B and C+D were used as template DNA with the oligonucleotides A+D used to amplify the full-length construct. The PCR conditions were the same as the initial PCR reaction. This generates a construct with the PDE4 swapped region and a C-terminal truncation (C-term 858) as compared to PDE5 catalytic domain (C-term 875).


Methods to generate the recombinant baculovirus were as those for wild-type PDE5 catalytic domain (see EXAMPLE 1).


Expression optimisation again showed T.ni High5 insect cells to give the best expression. Therefore baculovirus expression in fermenters was carried out using the same procedures as for the previous construct.


EXAMPLE 4
Construction and Expression of PDE5* (E534-E858) in E. coli

The PDE5* construct in E. coli was produced by using PCR where the following oligonucleotides were used and the template DNA being pFastbacl::PDE5* plasmid DNA (sequence verified), produced in EXAMPLE 3.

E:CGTCATATGGAGGAAGAAACAAGAGAGCTAC(SEQ ID NO: 13)F:CGTCTCGAGCTATCATTCTGCAAGGGCCTGCCAT(SEQ ID NO: 14)TTCTG


The PCR reaction was carried out for 30 cycles in a total volume of 50 μl in a solution containing 1.5 mM MgCl2, 200 μM dNTPs, 50 pmol of each primer and 2.5 units of Expand DNA polymerase (Roche, East Sussex, UK). Each cycle was 94° C., 1 min, 50° C., 1 min and 72° C., 2 mins.


The final amplified DNA fragment was separated on a 1% agarose gel and purified using a QIAquick gel extraction kit (Qiagen, West Sussex, UK). The fragments were then digested using Ndel and Xhol, and ligated into pET21C (Novagen, Nottingham, UK) Ndel/Xhol-digested vector. The ligation was carried out at 12° C. for 16 hours. The ligation mix was then electroporated into E. coli (TOP 10) (Invitrogen, Gronigen, The Netherlands).


Clones containing the desired insert were selected by using 2YT plates containing 100 μg/ml ampicillin. Plasmid DNA was also checked using endonuclease digestion for presence of correct size insert. DNA sequence analysis was carried out by Lark (Saffron Waldon, UK).


The correctly sequenced plasmid DNA was then electroporated into E. coli BL21 (DE3) (Novagen, Nottingham, UK) for expression. Expression was carried out in 7 litre Applikon fermenters using 5 litre 2YT broth containing 100 μg/ml carbenicillin as the medium. Agitation was set at 1000 rpm using a double rushton impeller assembly and aeration to the sparger at 2 litres/min. The fermenter was inoculated with an overnight shake flask culture grown at 37° C. and 200 rpm, the inoculation density was 1% vol/vol. The fermentation was pH controlled at 7.2 using 20% vol/vol NH4OH solution and temperature initially set to 37° C. When the OD600 nm reached 1.5 the temperature set-point was reduced to 25° C. and then the culture was induced with EPTG at a final concentration of 1 mM. The fermentation was then harvested 4 hours post-induction by batch centrifugation (8,000 rpm for 10 minutes). The final pellet was then frozen (−80° C.) to await subsequent purification.


EXAMPLE 5
Purification of PDE5* Catalytic Domain

Pellet from the E. coli fermentation was resuspended into 10 mls lysis buffer per gram wet cell weight and mechanically broken using a continuous cell disrupter (Constant Systems, Warwickshire, UK) at a pressure of 20 kpsi. The lysis buffer consisted of 50 mM Tris HCl (pH 7.5), 100 mM NaCl, 1 mM DTT containing EDTA-free protease inhibitor cocktail tablets (Roche, East Sussex, UK) and 10 μM E-64. The lysate was chilled and centrifuged at 14000 g for 45 min to remove cell debris. All purifications were subsequently carried out using an Äkta Explorer purification system (Amersham Pharmacia, Buckinghamshire, UK). The supernatant was applied to a 50 ml Q-sepharose fast-flow column (Amersham Pharmacia, Buckinghamshire, UK) at 5 ml/min with the flow-through collected. The flow-through sample was then applied at 50 ml/min to a 2 litre G-25 superfine desalting column (Amersham Pharmacia, Buckinghamshire, UK) pre-equilibrated in Blue sepharose buffer A (50 mM Bis-Tris (pH 6.4), 50 mM NaCl, 2 mM EDTA, 2 mM EGTA and 1 mM DTT). The protein fraction was eluted in Blue sepharose buffer A.


The next column step was carried out in series, loading the sample initially onto a 20 ml SP-sepharose high performance column (Amersham Pharmacia, Buckinghamshire, UK) then flow-through from this directly onto a 10 ml Blue sepharose fast-flow column (Amersham Pharmacia, Buckinghamshire, UK) at a flow-rate of 2 ml/min. Once loading was complete, the SP-sepharose column was taken out of line and the Blue sepharose column washed with 5 column volumes of Blue sepharose buffer A. The column was washed with Blue sepharose buffer A containing 1 M NaCl until the absorbance 280 nm reached baseline and then washed with 5 column volumes of Blue sepharose buffer A. PDE5* protein was step-eluted using Blue sepharose buffer containing 20 mM cGMP (Na-salt) (Sigma, Dorset, UK). Fractions were assayed on Tris-glycine SDS gels (Invitrogen, Gronigen, The Netherlands) and pooled accordingly. These fractions were concentrated to 2.5 mg/ml using centrifugal concentrators (Vivascience, Gloucestershire, UK) and loaded at 1.5 ml/min onto a Superdex-200 prep grade 26/60 column pre-equilibrated with 50 mM Bis-Tris (pH 6.8), 500 mM NaCl, 1 mM DTT and 2 μM E-64. The eluted fractions were analysed on Tris-glycine SDS PAGE gels.


EXAMPLE 6
Crystallisation of PDE5*

The PDE5* fractions from the final gel filtration column were pooled (total volume of 25 mls) and the protein concentration was assayed (0.2 mg/ml). The protein solution was supplemented with 10 μM E-64 and 1 mg/ml leupeptin (Sigma, Dorset, UK). The solution was concentrated to 10 mg/ml using a Centriprep 10 kDa Molecular weight cut-off centrifugal concentrator (Amicon Bioseparations, Maine, USA) at 3,000 rpm, 4° C. Prior to crystallisation, the protein solution was centrifuged for 5 min at 14,000 rpm in an Eppendorf centrifuge.


Hanging drop vapour diffusion crystallisation trials were set up at 4° C. Drops comprised of 2 μl reservoir buffer mixed with 2 μl protein solution were suspended on cover slips over 500 μl reservoir solutions containing 0.1M sodium HEPES pH 7.4, 20% Polyethylene glycol 4000 and 10% iso-Propanol. Plate-shaped crystals, up to 700 μm in largest dimension, grew after 1-3 days. Crystals were transferred to a 20 μl drop of 0.1M sodium HEPES pH 7.4 and 20% Polyethylene glycol 4000 in square microbridges. Crystals were then transferred to a solution of 0.1M sodium HEPES pH 7.4, 20% Polyethylene glycol 4000 with 15% glycerol and then frozen during X-ray data collection.


The crystals belong to space group C2 with cell dimensions a=55.97 Å, b=76.55 Å, c=80.50 Å and β=103.09. They contain one molecule per asymmetric unit and have a solvent content of 44% (Matthews, 1969).


EXAMPLE 7
Soaking Inhibitor into PDE5*

Plate-shaped crystals of apo PDE5* obtained according to methods detailed in EXAMPLE 6 were transferred to a 20 μl drop of 0.1M sodium HEPES and 20% Polyethylene glycol 4000 in square microbridges. To this, 1.0 μl of a 20 mg/ml concentration of inhibitor dissolved in DMSO was added. Crystals were then transferred to a solution of 0.1M sodium HEPES pH 7.4, 20% Polyethylene glycol 4000 with 15% glycerol and then frozen during X-ray data collection.


EXAMPLE 8
Data Collection, Structure Determination and Refinement of the Soakable C2 Crystal Form of PDE5*

The structure of the E. coli-engineered PDE5* was solved by molecular replacement (MR) using the coordinates of one subunit of PDE5* in the P21 crystal form (the crystals belong to the monoclinic space group P21, with unit cell dimensions a=54.93 Å, b=77.77 Å, c=82.05 Å, α=γ=90° 62 =100.955°) the coordinate set is detailed in Table 3. Molecular replacement was performed using AMORE (CCP4, J.Navaza 1994). The resulting map was of good quality and the structure was refitted using QUANTA® (Accelrys products).


A representative X-ray diffraction data set was collected with a Rigaku Saturn92 CCD detector on an in-house FR-D rotating anode (Rigaku), with Osmic mirrors (MSC). Data were processed using the CrystalClear/D*Trek processing package (Rigaku-MSC). Data collection statistics are summarised in Table 1 (Apo).


The crystals belong to space group C2 with cell dimensions a=55.97 Å, b=76.55 Å, c=80.50 Å and β=103.09. They contain one molecule per asymmetric unit and have a solvent content of 44% (Matthews, 1968).


Refinement was carried out in the resolution range 30-1.6 Å using CNX (Brünger et al., 1998) with the “mlf” maximum likelihood target function. Partial structure factors from a flat bulk-solvent model and anisotropic B-factor correction were supplied throughout the refinement. The R-factor for the refined model is 0.231 (free R-factor, 5% of data, 0.267) for all data in the resolution range 30-1.6 Å. The refinement statistics are summarised in Table 2 (Apo).


The co-ordinate set for the refined model of apo PDE5* is recorded in Table 4. The model contains 323 amino acid residues, 537-858 (residue Glu 681A has been numbered to maintain PDE5 numbering scheme), a zinc ion and a magnesium ion, as well as 222 water molecules.


EXAMPLE 9
Data Collection, Structure Determination and Refinement of the Soakable C2 Crystal Form of PDE5* Soaked with UK-088,800

The structure of the UK-088,800 soaked into the C2 crystal form of PDE5* was solved by difference Fourier methods.


X-ray diffraction data were collected with an RaxisIV image plate detector on an in-house FR-D rotating anode (Rigaku), with Osmic mirrors (MSC). All data were processed using the HKL package (Otwinowski & Minor, 1997). Data collection statistics are summarised in Table 1 (UK-088,800).


Refinement was carried out in the resolution range 30-1.5 Å using CNX (Brünger et al., 1998) with the “mlf” maximum likelihood target function. Partial structure factors from a flat bulk-solvent model and anisotropic B-factor correction were supplied throughout the refinement. The R-factor for the refined model is 0.219 (free R-factor, 5% of data, 0.228) for all data in the resolution range 30-1.5 Å. The refinement statistics are summarised in Table 2 (UK-088,800).


The co-ordinate set for the refined model of PDE5*-UK-088,800 is recorded in Table 5. The model contains 323 amino acid residues, 537-858 (residue Glu 681A has been numbered to maintain PDE5 numbering scheme), the ligand UK-088,800, a zinc ion and a magnesium ion, as well as 183 water molecules.


EXAMPLE 10
Comparison of the Apo PDE5* and PDE5* Soaked with UK-088,800

The (fo-fc)αcalc electron density map of PDE5* soaked with UK-088,800 calculated with experimental structure factor amplitudes and model phases derived prior to incorporation of the ligand into the model, shows a clearly featured peak that can unequivocally be interpreted as UK-088,880 (FIG. 3). In contrast, the equivalent (fo-fc)αcalc electron density map of apo PDE5* shows no significant residual features that could be interpreted as a small molecule ligand. The experiment allowed the experimental determination of the binding mode of UK-088,800 to PDE5* and demonstrates that the C2 crystal form of PDE5* as described herein is amenable to ligand soaking. The structure of PDE5* in the C2 crystal form does not show significant differences to that observed with the P21, crystal form.

TABLE 1Data collection statistics for the soakable C2crystal form of PDE5*ApoUK-088,800Resolution [Å]1.61.5Unique reflections4118952038Completeness [%]94.599.5Redundancy2.93.5Rsyma0.0740.049Rsyma=hkliIi(hkl)-I(hkl)_/hkliIi(hkl)









TABLE 2










Refinement statistics of soakable C2 crystal form of PDE5*










Apo
UK-088,800













Resolution range, Å
30.0-1.6
30.0-1.5


Amino acid residues, no.
323
323


Water molecules, no.
222
183


rmsd bond length, Å
0.005
0.005


rmsd bond angles, °
1.130
1.158



aR-factor

0.231
0.219


Free R-factor (5% of data)
0.267
0.228





















a


R
=



hkl









F
obs



-

k




F
calc







/



hkl





F
obs























TABLE 3










Atomic coordinates for baculovirus - expressed PDE5* complex with Sildenafil


Atom Number, Atom Type, Residue Type, Residue Number Cartesian Coordinates


X, Y, Z, Atom Occupancy (O) and Temperature Factor (B)













X
Y
Z
O
B





















ATOM
1
CB
THR
A
537
−3.008
28.295
13.745
1.00
40.04


ATOM
2
OG1
THR
A
537
−4.423
28.364
13.527
1.00
40.20


ATOM
3
CG2
THR
A
537
−2.273
28.516
12.435
1.00
40.01


ATOM
4
C
THR
A
537
−2.764
26.998
15.853
1.00
42.52


ATOM
5
O
THR
A
537
−3.657
26.395
16.451
1.00
44.33


ATOM
6
N
THR
A
537
−3.513
25.856
13.760
1.00
44.29


ATOM
7
CA
THR
A
537
−2.652
26.924
14.338
1.00
43.47


ATOM
8
N
ARG
A
538
−1.857
27.751
16.466
1.00
33.65


ATOM
9
CA
ARG
A
538
−1.818
27.897
17.916
1.00
31.51


ATOM
10
CB
ARG
A
538
−3.201
28.267
18.463
1.00
51.67


ATOM
11
CG
ARG
A
538
−3.420
27.913
19.928
1.00
52.25


ATOM
12
CD
ARG
A
538
−2.377
28.532
20.845
1.00
52.37


ATOM
13
NE
ARG
A
538
−1.851
27.547
21.788
1.00
52.59


ATOM
14
CZ
ARG
A
538
−1.048
27.833
22.809
1.00
52.58


ATOM
15
NH1
ARG
A
538
−0.676
29.087
23.032
1.00
52.27


ATOM
16
NH2
ARG
A
538
−0.608
26.864
23.600
1.00
52.33


ATOM
17
C
ARG
A
538
−1.336
26.584
18.521
1.00
30.67


ATOM
18
O
ARG
A
538
−0.175
26.465
18.906
1.00
30.03


ATOM
19
N
GLU
A
539
−2.221
25.594
18.593
1.00
27.90


ATOM
20
CA
GLU
A
539
−1.827
24.310
19.151
1.00
27.13


ATOM
21
CB
GLU
A
539
−3.000
23.322
19.146
1.00
33.40


ATOM
22
CG
GLU
A
539
−2.627
21.946
19.679
1.00
34.46


ATOM
23
CD
GLU
A
539
−3.814
21.007
19.761
1.00
34.35


ATOM
24
OE1
GLU
A
539
−4.656
21.037
18.843
1.00
34.50


ATOM
25
OE2
GLU
A
539
−3.899
20.233
20.738
1.00
34.57


ATOM
26
C
GLU
A
539
−0.666
23.734
18.346
1.00
27.02


ATOM
27
O
GLU
A
539
0.280
23.189
18.909
1.00
27.32


ATOM
28
N
LEU
A
540
−0.739
23.866
17.027
1.00
26.77


ATOM
29
CA
LEU
A
540
0.320
23.354
16.166
1.00
26.36


ATOM
30
CB
LEU
A
540
−0.070
23.496
14.695
1.00
24.87


ATOM
31
CG
LEU
A
540
1.027
23.155
13.682
1.00
24.86


ATOM
32
CD1
LEU
A
540
1.426
21.689
13.833
1.00
25.12


ATOM
33
CD2
LEU
A
540
0.531
23.447
12.264
1.00
25.63


ATOM
34
C
LEU
A
540
1.631
24.091
16.415
1.00
26.72


ATOM
35
O
LEU
A
540
2.681
23.479
16.603
1.00
26.47


ATOM
36
N
GLN
A
541
1.573
25.416
16.407
1.00
25.80


ATOM
37
CA
GLN
A
541
2.777
26.196
16.626
1.00
26.31


ATOM
38
CB
GLN
A
541
2.455
27.682
16.484
1.00
28.46


ATOM
39
CG
GLN
A
541
2.334
28.108
15.029
1.00
28.55


ATOM
40
CD
GLN
A
541
1.709
29.475
14.868
1.00
28.37


ATOM
41
OE1
GLN
A
541
1.843
30.334
15.736
1.00
28.46


ATOM
42
NE2
GLN
A
541
1.033
29.687
13.747
1.00
29.26


ATOM
43
C
GLN
A
541
3.415
25.894
17.978
1.00
25.96


ATOM
44
O
GLN
A
541
4.636
25.785
18.082
1.00
26.05


ATOM
45
N
SER
A
542
2.589
25.733
19.008
1.00
27.15


ATOM
46
CA
SER
A
542
3.103
25.440
20.341
1.00
27.52


ATOM
47
CB
SER
A
542
1.980
25.510
21.379
1.00
38.20


ATOM
48
OG
SER
A
542
1.535
26.841
21.558
1.00
38.87


ATOM
49
C
SER
A
542
3.752
24.067
20.390
1.00
27.50


ATOM
50
O
SER
A
542
4.795
23.888
21.015
1.00
27.75


ATOM
51
N
LEU
A
543
3.131
23.095
19.732
1.00
23.90


ATOM
52
CA
LEU
A
543
3.676
21.743
19.723
1.00
23.62


ATOM
53
CB
LEU
A
543
2.702
20.785
19.022
1.00
31.43


ATOM
54
CG
LEU
A
543
2.929
19.274
19.167
1.00
32.27


ATOM
55
CD1
LEU
A
543
1.959
18.529
18.263
1.00
31.54


ATOM
56
CD2
LEU
A
543
4.340
18.904
18.800
1.00
32.06


ATOM
57
C
LEU
A
543
5.025
21.725
19.009
1.00
23.65


ATOM
58
O
LEU
A
543
5.998
21.144
19.498
1.00
23.61


ATOM
59
N
ALA
A
544
5.079
22.365
17.848
1.00
24.41


ATOM
60
CA
ALA
A
544
6.295
22.402
17.052
1.00
24.73


ATOM
61
CB
ALA
A
544
6.014
23.090
15.728
1.00
23.31


ATOM
62
C
ALA
A
544
7.477
23.076
17.748
1.00
25.97


ATOM
63
O
ALA
A
544
8.619
22.642
17.600
1.00
25.19


ATOM
64
N
ALA
A
545
7.202
24.125
18.512
1.00
29.21


ATOM
65
CA
ALA
A
545
8.259
24.861
19.196
1.00
30.03


ATOM
66
CB
ALA
A
545
7.837
26.315
19.351
1.00
32.13


ATOM
67
C
ALA
A
545
8.660
24.288
20.553
1.00
30.21


ATOM
68
O
ALA
A
545
9.698
24.657
21.105
1.00
30.14


ATOM
69
N
ALA
A
546
7.849
23.382
21.088
1.00
28.91


ATOM
70
CA
ALA
A
546
8.126
22.790
22.391
1.00
28.92


ATOM
71
CB
ALA
A
546
6.878
22.068
22.913
1.00
27.14


ATOM
72
C
ALA
A
546
9.308
21.831
22.400
1.00
29.12


ATOM
73
O
ALA
A
546
9.648
21.222
21.381
1.00
29.57


ATOM
74
N
VAL
A
547
9.936
21.702
23.564
1.00
27.29


ATOM
75
CA
VAL
A
547
11.060
20.791
23.714
1.00
26.19


ATOM
76
CB
VAL
A
547
11.917
21.148
24.947
1.00
37.00


ATOM
77
CG1
VAL
A
547
12.925
20.042
25.223
1.00
37.18


ATOM
78
CG2
VAL
A
547
12.635
22.464
24.711
1.00
37.04


ATOM
79
C
VAL
A
547
10.482
19.395
23.903
1.00
26.09


ATOM
80
O
VAL
A
547
9.473
19.226
24.588
1.00
27.35


ATOM
81
N
VAL
A
548
11.110
18.400
23.286
1.00
28.09


ATOM
82
CA
VAL
A
548
10.638
17.029
23.409
1.00
28.48


ATOM
83
CB
VAL
A
548
10.792
16.254
22.079
1.00
23.53


ATOM
84
CG1
VAL
A
548
10.198
14.845
22.215
1.00
24.59


ATOM
85
CG2
VAL
A
548
10.123
17.016
20.953
1.00
23.63


ATOM
86
C
VAL
A
548
11.468
16.336
24.475
1.00
28.05


ATOM
87
O
VAL
A
548
12.637
16.033
24.252
1.00
29.14


ATOM
88
N
PRO
A
549
10.879
16.080
25.655
1.00
28.24


ATOM
89
CD
PRO
A
549
9.550
16.472
26.151
1.00
28.37


ATOM
90
CA
PRO
A
549
11.647
15.414
26.709
1.00
28.05


ATOM
91
CB
PRO
A
549
10.648
15.321
27.858
1.00
28.48


ATOM
92
CG
PRO
A
549
9.781
16.524
27.640
1.00
28.59


ATOM
93
C
PRO
A
549
12.133
14.045
26.254
1.00
28.74


ATOM
94
O
PRO
A
549
11.639
13.495
25.262
1.00
27.64


ATOM
95
N
SER
A
550
13.103
13.505
26.977
1.00
30.38


ATOM
96
CA
SER
A
550
13.658
12.202
26.649
1.00
30.47


ATOM
97
CB
SER
A
550
14.923
11.963
27.464
1.00
32.70


ATOM
98
OG
SER
A
550
14.611
11.959
28.843
1.00
32.28


ATOM
99
C
SER
A
550
12.654
11.101
26.955
1.00
29.91


ATOM
100
O
SER
A
550
11.683
11.310
27.684
1.00
30.19


ATOM
101
N
ALA
A
551
12.898
9.922
26.396
1.00
27.46


ATOM
102
CA
ALA
A
551
12.022
8.784
26.626
1.00
27.31


ATOM
103
CB
ALA
A
551
12.451
7.610
25.756
1.00
33.59


ATOM
104
C
ALA
A
551
12.064
8.389
28.097
1.00
27.99


ATOM
105
O
ALA
A
551
11.031
8.093
28.700
1.00
27.97


ATOM
106
N
GLN
A
552
13.264
8.382
28.670
1.00
30.15


ATOM
107
CA
GLN
A
552
13.433
8.019
30.074
1.00
31.28


ATOM
108
CB
GLN
A
552
14.917
8.099
30.457
1.00
50.35


ATOM
109
CG
GLN
A
552
15.547
9.470
30.254
1.00
51.01


ATOM
110
CD
GLN
A
552
17.068
9.439
30.310
1.00
51.35


ATOM
111
OE1
GLN
A
552
17.725
8.932
29.398
1.00
51.08


ATOM
112
NE2
GLN
A
552
17.635
9.979
31.385
1.00
51.12


ATOM
113
C
GLN
A
552
12.595
8.934
30.969
1.00
31.11


ATOM
114
O
GLN
A
552
11.888
8.470
31.868
1.00
30.93


ATOM
115
N
THR
A
553
12.660
10.232
30.704
1.00
32.81


ATOM
116
CA
THR
A
553
11.904
11.202
31.484
1.00
32.49


ATOM
117
CB
THR
A
553
12.250
12.637
31.060
1.00
35.77


ATOM
118
OG1
THR
A
553
13.615
12.915
31.399
1.00
35.76


ATOM
119
CG2
THR
A
553
11.339
13.639
31.761
1.00
35.80


ATOM
120
C
THR
A
553
10.399
10.999
31.333
1.00
32.89


ATOM
121
O
THR
A
553
9.658
11.065
32.313
1.00
33.04


ATOM
122
N
LEU
A
554
9.954
10.750
30.105
1.00
29.86


ATOM
123
CA
LEU
A
554
8.534
10.545
29.827
1.00
28.95


ATOM
124
CB
LEU
A
554
8.278
10.693
28.325
1.00
27.17


ATOM
125
CG
LEU
A
554
8.586
12.088
27.769
1.00
27.34


ATOM
126
CD1
LEU
A
554
8.439
12.101
26.255
1.00
27.36


ATOM
127
CD2
LEU
A
554
7.650
13.105
28.410
1.00
27.14


ATOM
128
C
LEU
A
554
8.011
9.197
30.326
1.00
28.80


ATOM
129
O
LEU
A
554
6.803
9.014
30.486
1.00
28.57


ATOM
130
N
LYS
A
555
8.925
8.260
30.561
1.00
24.74


ATOM
131
CA
LYS
A
555
8.588
6.935
31.071
1.00
25.34


ATOM
132
CB
LYS
A
555
7.764
7.072
32.356
1.00
44.27


ATOM
133
CG
LYS
A
555
8.420
7.960
33.402
1.00
45.10


ATOM
134
CD
LYS
A
555
7.451
8.363
34.501
1.00
45.29


ATOM
135
CE
LYS
A
555
8.106
9.352
35.455
1.00
45.10


ATOM
136
NZ
LYS
A
555
7.173
9.818
36.518
1.00
45.31


ATOM
137
C
LYS
A
555
7.818
6.084
30.060
1.00
24.58


ATOM
138
O
LYS
A
555
7.148
5.116
30.433
1.00
25.45


ATOM
139
N
ILE
A
556
7.932
6.430
28.783
1.00
26.12


ATOM
140
CA
ILE
A
556
7.222
5.699
27.740
1.00
26.45


ATOM
141
CB
ILE
A
556
7.160
6.515
26.432
1.00
24.50


ATOM
142
CG2
ILE
A
556
6.294
7.753
26.640
1.00
24.65


ATOM
143
CG1
ILE
A
556
8.571
6.907
25.987
1.00
24.30


ATOM
144
CD1
ILE
A
556
8.631
7.477
24.582
1.00
24.18


ATOM
145
C
ILE
A
556
7.806
4.321
27.446
1.00
26.74


ATOM
146
O
ILE
A
556
7.203
3.525
26.722
1.00
26.46


ATOM
147
N
THR
A
557
8.974
4.027
28.004
1.00
26.58


ATOM
148
CA
THR
A
557
9.571
2.718
27.782
1.00
26.91


ATOM
149
CB
THR
A
557
11.098
2.750
27.964
1.00
33.52


ATOM
150
OG1
THR
A
557
11.653
3.811
27.179
1.00
33.53


ATOM
151
CG2
THR
A
557
11.709
1.430
27.506
1.00
33.78


ATOM
152
C
THR
A
557
8.983
1.711
28.766
1.00
26.91


ATOM
153
O
THR
A
557
9.108
0.501
28.578
1.00
27.08


ATOM
154
N
ASP
A
558
8.327
2.213
29.810
1.00
22.97


ATOM
155
CA
ASP
A
558
7.739
1.347
30.824
1.00
24.55


ATOM
156
CB
ASP
A
558
7.564
2.101
32.145
1.00
42.16


ATOM
157
CG
ASP
A
558
8.816
2.834
32.573
1.00
43.08


ATOM
158
OD1
ASP
A
558
9.918
2.258
32.459
1.00
43.16


ATOM
159
OD2
ASP
A
558
8.692
3.987
33.036
1.00
43.34


ATOM
160
C
ASP
A
558
6.386
0.797
30.408
1.00
23.87


ATOM
161
O
ASP
A
558
5.522
1.537
29.940
1.00
24.35


ATOM
162
N
PHE
A
559
6.200
−0.505
30.593
1.00
26.69


ATOM
163
CA
PHE
A
559
4.936
−1.140
30.257
1.00
26.24


ATOM
164
CB
PHE
A
559
5.052
−2.662
30.372
1.00
34.04


ATOM
165
CG
PHE
A
559
5.885
−3.290
29.292
1.00
34.73


ATOM
166
CD1
PHE
A
559
5.537
−3.135
27.952
1.00
34.65


ATOM
167
CD2
PHE
A
559
7.018
−4.036
29.610
1.00
34.64


ATOM
168
CE1
PHE
A
559
6.304
−3.713
26.943
1.00
34.43


ATOM
169
CE2
PHE
A
559
7.793
−4.618
28.610
1.00
34.92


ATOM
170
CZ
PHE
A
559
7.435
−4.456
27.272
1.00
34.80


ATOM
171
C
PHE
A
559
3.841
−0.639
31.196
1.00
26.88


ATOM
172
O
PHE
A
559
2.664
−0.631
30.837
1.00
25.97


ATOM
173
N
SER
A
560
4.245
−0.213
32.389
1.00
25.49


ATOM
174
CA
SER
A
560
3.321
0.285
33.407
1.00
26.93


ATOM
175
CB
SER
A
560
3.945
0.120
34.797
1.00
39.67


ATOM
176
OG
SER
A
560
5.170
0.830
34.899
1.00
40.02


ATOM
177
C
SER
A
560
2.920
1.745
33.197
1.00
26.06


ATOM
178
O
SER
A
560
2.205
2.327
34.018
1.00
26.04


ATOM
179
N
PHE
A
561
3.382
2.326
32.098
1.00
26.05


ATOM
180
CA
PHE
A
561
3.081
3.711
31.751
1.00
25.67


ATOM
181
CB
PHE
A
561
3.551
3.982
30.321
1.00
26.66


ATOM
182
CG
PHE
A
561
3.158
5.330
29.795
1.00
25.48


ATOM
183
CD1
PHE
A
561
3.990
6.430
29.972
1.00
26.67


ATOM
184
CD2
PHE
A
561
1.948
5.502
29.127
1.00
26.67


ATOM
185
CE1
PHE
A
561
3.624
7.686
29.489
1.00
26.12


ATOM
186
CE2
PHE
A
561
1.571
6.748
28.642
1.00
25.76


ATOM
187
CZ
PHE
A
561
2.412
7.844
28.823
1.00
26.46


ATOM
188
C
PHE
A
561
1.597
4.082
31.865
1.00
26.23


ATOM
189
O
PHE
A
561
0.715
3.293
31.533
1.00
25.55


ATOM
190
N
SER
A
562
1.335
5.304
32.320
1.00
24.91


ATOM
191
CA
SER
A
562
−0.029
5.803
32.463
1.00
26.24


ATOM
192
CB
SER
A
562
−0.406
5.906
33.940
1.00
42.72


ATOM
193
OG
SER
A
562
−1.720
6.414
34.084
1.00
43.29


ATOM
194
C
SER
A
562
−0.134
7.179
31.817
1.00
24.23


ATOM
195
O
SER
A
562
0.730
8.024
32.013
1.00
25.59


ATOM
196
N
ASP
A
563
−1.199
7.401
31.055
1.00
23.00


ATOM
197
CA
ASP
A
563
−1.410
8.675
30.373
1.00
22.76


ATOM
198
CB
ASP
A
563
−2.135
8.446
29.043
1.00
25.24


ATOM
199
CG
ASP
A
563
−3.635
8.228
29.230
1.00
23.77


ATOM
200
OD1
ASP
A
563
−4.037
7.150
29.718
1.00
23.35


ATOM
201
OD2
ASP
A
563
−4.421
9.143
28.906
1.00
24.81


ATOM
202
C
ASP
A
563
−2.263
9.659
31.176
1.00
22.96


ATOM
203
O
ASP
A
563
−2.297
10.848
30.865
1.00
21.79


ATOM
204
N
PHE
A
564
−2.958
9.150
32.187
1.00
24.29


ATOM
205
CA
PHE
A
564
−3.878
9.962
32.987
1.00
25.23


ATOM
206
CB
PHE
A
564
−4.394
9.157
34.180
1.00
41.24


ATOM
207
CG
PHE
A
564
−5.576
9.787
34.857
1.00
41.58


ATOM
208
CD1
PHE
A
564
−6.793
9.895
34.191
1.00
41.99


ATOM
209
CD2
PHE
A
564
−5.469
10.300
36.146
1.00
42.28


ATOM
210
CE1
PHE
A
564
−7.888
10.506
34.797
1.00
41.91


ATOM
211
CE2
PHE
A
564
−6.558
10.915
36.763
1.00
41.92


ATOM
212
CZ
PHE
A
564
−7.769
11.018
36.086
1.00
41.83


ATOM
213
C
PHE
A
564
−3.410
11.321
33.490
1.00
25.10


ATOM
214
O
PHE
A
564
−4.185
12.278
33.488
1.00
25.27


ATOM
215
N
GLU
A
565
−2.158
11.406
33.921
1.00
29.45


ATOM
216
CA
GLU
A
565
−1.618
12.651
34.459
1.00
30.36


ATOM
217
CB
GLU
A
565
−0.456
12.341
35.408
1.00
40.02


ATOM
218
CG
GLU
A
565
−0.821
11.524
36.645
1.00
40.24


ATOM
219
CD
GLU
A
565
−1.312
10.120
36.320
1.00
40.61


ATOM
220
OE1
GLU
A
565
−0.655
9.424
35.514
1.00
40.05


ATOM
221
OE2
GLU
A
565
−2.352
9.711
36.883
1.00
40.18


ATOM
222
C
GLU
A
565
−1.144
13.652
33.409
1.00
30.08


ATOM
223
O
GLU
A
565
−0.860
14.810
33.732
1.00
30.87


ATOM
224
N
LEU
A
566
−1.070
13.217
32.155
1.00
25.91


ATOM
225
CA
LEU
A
566
−0.587
14.073
31.078
1.00
25.51


ATOM
226
CB
LEU
A
566
0.157
13.219
30.051
1.00
30.68


ATOM
227
CG
LEU
A
566
1.256
12.294
30.578
1.00
31.45


ATOM
228
CD1
LEU
A
566
1.775
11.429
29.437
1.00
30.44


ATOM
229
CD2
LEU
A
566
2.377
13.112
31.186
1.00
31.07


ATOM
230
C
LEU
A
566
−1.642
14.889
30.349
1.00
25.31


ATOM
231
O
LEU
A
566
−2.793
14.475
30.220
1.00
24.57


ATOM
232
N
SER
A
567
−1.228
16.054
29.859
1.00
27.06


ATOM
233
CA
SER
A
567
−2.110
16.928
29.096
1.00
26.87


ATOM
234
CB
SER
A
567
−1.619
18.373
29.159
1.00
26.86


ATOM
235
OG
SER
A
567
−0.406
18.519
28.439
1.00
26.48


ATOM
236
C
SER
A
567
−2.038
16.447
27.650
1.00
26.54


ATOM
237
O
SER
A
567
−1.187
15.617
27.314
1.00
25.78


ATOM
238
N
ASP
A
568
−2.921
16.963
26.800
1.00
25.65


ATOM
239
CA
ASP
A
568
−2.935
16.588
25.388
1.00
25.44


ATOM
240
CB
ASP
A
568
−4.077
17.292
24.657
1.00
35.03


ATOM
241
CG
ASP
A
568
−5.437
16.732
25.028
1.00
35.82


ATOM
242
OD1
ASP
A
568
−6.450
17.284
24.555
1.00
36.02


ATOM
243
OD2
ASP
A
568
−5.489
15.744
25.788
1.00
35.24


ATOM
244
C
ASP
A
568
−1.604
16.946
24.739
1.00
26.02


ATOM
245
O
ASP
A
568
−1.040
16.154
23.981
1.00
24.45


ATOM
246
N
LEU
A
569
−1.104
18.140
25.040
1.00
26.56


ATOM
247
CA
LEU
A
569
0.177
18.584
24.501
1.00
27.05


ATOM
248
CB
LEU
A
569
0.544
19.958
25.066
1.00
35.85


ATOM
249
CG
LEU
A
569
1.958
20.460
24.751
1.00
36.55


ATOM
250
CD1
LEU
A
569
2.110
20.683
23.255
1.00
36.24


ATOM
251
CD2
LEU
A
569
2.211
21.755
25.509
1.00
36.44


ATOM
252
C
LEU
A
569
1.267
17.582
24.864
1.00
25.81


ATOM
253
O
LEU
A
569
2.080
17.214
24.021
1.00
27.30


ATOM
254
N
GLU
A
570
1.283
17.151
26.126
1.00
24.45


ATOM
255
CA
GLU
A
570
2.266
16.183
26.596
1.00
23.61


ATOM
256
CB
GLU
A
570
2.143
15.984
28.104
1.00
28.33


ATOM
257
CG
GLU
A
570
2.600
17.182
28.912
1.00
28.49


ATOM
258
CD
GLU
A
570
2.473
16.953
30.402
1.00
28.93


ATOM
259
OE1
GLU
A
570
1.346
16.679
30.864
1.00
27.96


ATOM
260
OE2
GLU
A
570
3.500
17.049
31.111
1.00
29.89


ATOM
261
C
GLU
A
570
2.149
14.832
25.892
1.00
23.15


ATOM
262
O
GLU
A
570
3.166
14.194
25.622
1.00
23.63


ATOM
263
N
THR
A
571
0.931
14.382
25.592
1.00
21.78


ATOM
264
CA
THR
A
571
0.803
13.099
24.897
1.00
21.61


ATOM
265
CB
THR
A
571
−0.670
12.597
24.814
1.00
20.96


ATOM
266
OG1
THR
A
571
−1.477
13.550
24.117
1.00
22.41


ATOM
267
CG2
THR
A
571
−1.242
12.365
26.212
1.00
20.91


ATOM
268
C
THR
A
571
1.362
13.236
23.483
1.00
22.39


ATOM
269
O
THR
A
571
1.924
12.283
22.929
1.00
21.33


ATOM
270
N
ALA
A
572
1.218
14.425
22.906
1.00
21.89


ATOM
271
CA
ALA
A
572
1.726
14.683
21.564
1.00
22.51


ATOM
272
CB
ALA
A
572
1.235
16.037
21.061
1.00
23.95


ATOM
273
C
ALA
A
572
3.247
14.647
21.603
1.00
23.15


ATOM
274
O
ALA
A
572
3.885
14.120
20.690
1.00
23.62


ATOM
275
N
LEU
A
573
3.830
15.211
22.660
1.00
24.60


ATOM
276
CA
LEU
A
573
5.281
15.215
22.805
1.00
25.21


ATOM
277
CB
LEU
A
573
5.694
16.061
24.013
1.00
27.78


ATOM
278
CG
LEU
A
573
5.470
17.565
23.808
1.00
27.76


ATOM
279
CD1
LEU
A
573
5.732
18.313
25.101
1.00
27.67


ATOM
280
CD2
LEU
A
573
6.391
18.074
22.699
1.00
27.52


ATOM
281
C
LEU
A
573
5.777
13.784
22.953
1.00
25.21


ATOM
282
O
LEU
A
573
6.797
13.413
22.374
1.00
25.36


ATOM
283
N
CYS
A
574
5.052
12.979
23.725
1.00
21.84


ATOM
284
CA
CYS
A
574
5.432
11.581
23.897
1.00
21.46


ATOM
285
CB
CYS
A
574
4.446
10.852
24.807
1.00
23.13


ATOM
286
SG
CYS
A
574
4.663
11.173
26.560
1.00
22.80


ATOM
287
C
CYS
A
574
5.426
10.890
22.540
1.00
21.90


ATOM
288
O
CYS
A
574
6.277
10.047
22.260
1.00
21.49


ATOM
289
N
THR
A
575
4.449
11.240
21.705
1.00
23.44


ATOM
290
CA
THR
A
575
4.334
10.631
20.384
1.00
21.88


ATOM
291
CB
THR
A
575
3.006
11.042
19.699
1.00
21.68


ATOM
292
OG1
THR
A
575
1.916
10.641
20.536
1.00
22.63


ATOM
293
CG2
THR
A
575
2.857
10.370
18.340
1.00
22.72


ATOM
294
C
THR
A
575
5.534
11.000
19.518
1.00
22.93


ATOM
295
O
THR
A
575
6.111
10.140
18.865
1.00
20.91


ATOM
296
N
ILE
A
576
5.929
12.268
19.529
1.00
22.16


ATOM
297
CA
ILE
A
576
7.091
12.673
18.748
1.00
23.75


ATOM
298
CB
ILE
A
576
7.403
14.171
18.924
1.00
26.26


ATOM
299
CG2
ILE
A
576
8.756
14.495
18.311
1.00
26.23


ATOM
300
CG1
ILE
A
576
6.318
15.016
18.260
1.00
26.29


ATOM
301
CD1
ILE
A
576
6.476
16.494
18.490
1.00
26.83


ATOM
302
C
ILE
A
576
8.311
11.872
19.209
1.00
22.92


ATOM
303
O
ILE
A
576
9.111
11.416
18.394
1.00
23.77


ATOM
304
N
ARG
A
577
8.447
11.703
20.521
1.00
24.95


ATOM
305
CA
ARG
A
577
9.575
10.965
21.077
1.00
24.47


ATOM
306
CB
ARG
A
577
9.560
11.050
22.609
1.00
26.95


ATOM
307
CG
ARG
A
577
10.652
10.234
23.294
1.00
27.15


ATOM
308
CD
ARG
A
577
12.031
10.561
22.731
1.00
27.06


ATOM
309
NE
ARG
A
577
12.398
11.956
22.957
1.00
26.65


ATOM
310
CZ
ARG
A
577
13.447
12.556
22.401
1.00
27.38


ATOM
311
NH1
ARG
A
577
14.247
11.888
21.578
1.00
27.39


ATOM
312
NH2
ARG
A
577
13.696
13.829
22.666
1.00
26.81


ATOM
313
C
ARG
A
577
9.565
9.509
20.625
1.00
24.18


ATOM
314
O
ARG
A
577
10.619
8.913
20.416
1.00
24.97


ATOM
315
N
MET
A
578
8.372
8.938
20.471
1.00
21.76


ATOM
316
CA
MET
A
578
8.247
7.552
20.032
1.00
21.44


ATOM
317
CB
MET
A
578
6.782
7.122
20.042
1.00
25.13


ATOM
318
CG
MET
A
578
6.222
6.855
21.425
1.00
23.93


ATOM
319
SD
MET
A
578
4.483
6.363
21.351
1.00
23.95


ATOM
320
CE
MET
A
578
3.892
6.945
22.915
1.00
24.88


ATOM
321
C
MET
A
578
8.820
7.370
18.630
1.00
22.27


ATOM
322
O
MET
A
578
9.562
6.422
18.373
1.00
22.21


ATOM
323
N
PHE
A
579
8.462
8.270
17.722
1.00
22.29


ATOM
324
CA
PHE
A
579
8.960
8.194
16.355
1.00
22.58


ATOM
325
CB
PHE
A
579
8.317
9.267
15.474
1.00
22.36


ATOM
326
CG
PHE
A
579
6.970
8.885
14.925
1.00
22.77


ATOM
327
CD1
PHE
A
579
5.812
9.077
15.672
1.00
22.73


ATOM
328
CD2
PHE
A
579
6.864
8.341
13.649
1.00
21.91


ATOM
329
CE1
PHE
A
579
4.560
8.733
15.151
1.00
22.92


ATOM
330
CE2
PHE
A
579
5.625
7.993
13.119
1.00
22.30


ATOM
331
CZ
PHE
A
579
4.469
8.190
13.871
1.00
22.31


ATOM
332
C
PHE
A
579
10.466
8.390
16.328
1.00
24.14


ATOM
333
O
PHE
A
579
11.183
7.701
15.600
1.00
22.99


ATOM
334
N
THR
A
580
10.935
9.336
17.133
1.00
24.07


ATOM
335
CA
THR
A
580
12.350
9.667
17.198
1.00
24.45


ATOM
336
CB
THR
A
580
12.567
10.901
18.085
1.00
24.15


ATOM
337
OG1
THR
A
580
11.712
11.961
17.636
1.00
24.88


ATOM
338
OG2
THR
A
580
14.008
11.370
18.009
1.00
24.18


ATOM
339
C
THR
A
580
13.239
8.535
17.691
1.00
24.89


ATOM
340
O
THR
A
580
14.218
8.188
17.030
1.00
24.15


ATOM
341
N
ASP
A
581
12.903
7.955
18.840
1.00
26.03


ATOM
342
CA
ASP
A
581
13.703
6.870
19.402
1.00
26.27


ATOM
343
CB
ASP
A
581
13.395
6.710
20.894
1.00
26.96


ATOM
344
CG
ASP
A
581
14.029
7.808
21.733
1.00
26.96


ATOM
345
OD1
ASP
A
581
14.376
8.868
21.167
1.00
26.78


ATOM
346
OD2
ASP
A
581
14.176
7.620
22.958
1.00
27.14


ATOM
347
C
ASP
A
581
13.578
5.534
18.676
1.00
26.95


ATOM
348
O
ASP
A
581
14.306
4.589
18.978
1.00
27.55


ATOM
349
N
LEU
A
582
12.654
5.447
17.727
1.00
25.40


ATOM
350
CA
LEU
A
582
12.516
4.231
16.934
1.00
25.74


ATOM
351
CB
LEU
A
582
11.040
3.918
16.642
1.00
23.64


ATOM
352
CG
LEU
A
582
10.286
3.274
17.817
1.00
22.73


ATOM
353
CD1
LEU
A
582
8.801
3.146
17.484
1.00
21.47


ATOM
354
CD2
LEU
A
582
10.873
1.900
18.125
1.00
22.27


ATOM
355
C
LEU
A
582
13.284
4.483
15.635
1.00
26.83


ATOM
356
O
LEU
A
582
13.259
3.669
14.710
1.00
26.36


ATOM
357
N
ASN
A
583
13.967
5.625
15.588
1.00
30.93


ATOM
358
CA
ASN
A
583
14.767
6.026
14.433
1.00
32.87


ATOM
359
CB
ASN
A
583
15.944
5.065
14.247
1.00
52.34


ATOM
360
CG
ASN
A
583
17.069
5.331
15.225
1.00
53.08


ATOM
361
OD1
ASN
A
583
18.026
4.561
15.312
1.00
53.41


ATOM
362
ND2
ASN
A
583
16.967
6.432
15.962
1.00
53.31


ATOM
363
C
ASN
A
583
13.973
6.114
13.143
1.00
31.76


ATOM
364
O
ASN
A
583
14.443
5.706
12.085
1.00
32.63


ATOM
365
N
LEU
A
584
12.769
6.665
13.235
1.00
27.18


ATOM
366
CA
LEU
A
584
11.904
6.813
12.073
1.00
27.03


ATOM
367
CB
LEU
A
584
10.455
6.521
12.468
1.00
25.42


ATOM
368
CG
LEU
A
584
9.877
5.107
12.377
1.00
27.73


ATOM
369
CD1
LEU
A
584
10.936
4.047
12.537
1.00
26.75


ATOM
370
CD2
LEU
A
584
8.771
4.975
13.422
1.00
25.52


ATOM
371
C
LEU
A
584
11.971
8.208
11.468
1.00
26.54


ATOM
372
O
LEU
A
584
11.760
8.380
10.270
1.00
27.46


ATOM
373
N
VAL
A
585
12.265
9.204
12.296
1.00
28.54


ATOM
374
CA
VAL
A
585
12.300
10.589
11.831
1.00
29.02


ATOM
375
CB
VAL
A
585
12.403
11.550
13.025
1.00
27.38


ATOM
376
CG1
VAL
A
585
12.404
12.993
12.545
1.00
27.75


ATOM
377
CG2
VAL
A
585
11.236
11.310
13.971
1.00
27.59


ATOM
378
C
VAL
A
585
13.375
10.951
10.804
1.00
30.26


ATOM
379
O
VAL
A
585
13.059
11.379
9.693
1.00
29.85


ATOM
380
N
GLN
A
586
14.639
10.799
11.167
1.00
36.79


ATOM
381
CA
GLN
A
586
15.697
11.132
10.228
1.00
38.86


ATOM
382
CB
GLN
A
586
17.024
11.300
10.969
1.00
56.08


ATOM
383
CG
GLN
A
586
16.935
12.315
12.102
1.00
56.46


ATOM
384
CD
GLN
A
586
18.288
12.833
12.551
1.00
56.85


ATOM
385
OE1
GLN
A
586
18.393
13.538
13.556
1.00
56.83


ATOM
386
NE2
GLN
A
586
19.332
12.494
11.801
1.00
56.71


ATOM
387
C
GLN
A
586
15.796
10.046
9.163
1.00
38.13


ATOM
388
O
GLN
A
586
16.005
10.336
7.985
1.00
38.63


ATOM
389
N
ASN
A
587
15.615
8.799
9.586
1.00
34.73


ATOM
390
CA
ASN
A
587
15.665
7.652
8.685
1.00
34.34


ATOM
391
CB
ASN
A
587
15.120
6.420
9.399
1.00
37.16


ATOM
392
CG
ASN
A
587
15.340
5.140
8.620
1.00
36.75


ATOM
393
OD1
ASN
A
587
15.392
5.141
7.389
1.00
36.63


ATOM
394
ND2
ASN
A
587
15.450
4.031
9.341
1.00
37.09


ATOM
395
C
ASN
A
587
14.834
7.911
7.430
1.00
34.66


ATOM
396
O
ASN
A
587
15.294
7.691
6.307
1.00
34.46


ATOM
397
N
PHE
A
588
13.600
8.372
7.628
1.00
30.54


ATOM
398
CA
PHE
A
588
12.711
8.654
6.511
1.00
30.38


ATOM
399
CB
PHE
A
588
11.366
7.964
6.734
1.00
24.15


ATOM
400
CG
PHE
A
588
11.487
6.479
6.910
1.00
23.77


ATOM
401
CD1
PHE
A
588
11.369
5.896
8.169
1.00
24.08


ATOM
402
CD2
PHE
A
588
11.762
5.663
5.820
1.00
23.24


ATOM
403
CE1
PHE
A
588
11.526
4.515
8.336
1.00
24.41


ATOM
404
CE2
PHE
A
588
11.921
4.285
5.969
1.00
23.43


ATOM
405
CZ
PHE
A
588
11.804
3.707
7.228
1.00
23.76


ATOM
406
C
PHE
A
588
12.535
10.151
6.304
1.00
30.36


ATOM
407
O
PHE
A
588
11.595
10.599
5.649
1.00
30.79


ATOM
408
N
GLN
A
589
13.462
10.912
6.873
1.00
35.42


ATOM
409
CA
GLN
A
589
13.489
12.366
6.750
1.00
36.58


ATOM
410
CB
GLN
A
589
14.167
12.739
5.433
1.00
49.72


ATOM
411
CG
GLN
A
589
15.501
12.043
5.243
1.00
49.96


ATOM
412
CD
GLN
A
589
15.680
11.505
3.839
1.00
50.27


ATOM
413
OE1
GLN
A
589
14.788
10.852
3.296
1.00
50.16


ATOM
414
NE2
GLN
A
589
16.839
11.762
3.249
1.00
50.04


ATOM
415
C
GLN
A
589
12.133
13.055
6.846
1.00
36.29


ATOM
416
O
GLN
A
589
11.648
13.655
5.882
1.00
36.29


ATOM
417
N
MET
A
590
11.524
12.969
8.021
1.00
36.14


ATOM
418
CA
MET
A
590
10.240
13.608
8.258
1.00
35.67


ATOM
419
CB
MET
A
590
9.459
12.847
9.331
1.00
32.44


ATOM
420
CG
MET
A
590
9.055
11.431
8.966
1.00
31.88


ATOM
421
SD
MET
A
590
8.254
10.607
10.373
1.00
31.19


ATOM
422
CE
MET
A
590
6.882
11.641
10.615
1.00
32.88


ATOM
423
C
MET
A
590
10.515
15.022
8.759
1.00
35.35


ATOM
424
O
MET
A
590
11.351
15.209
9.641
1.00
35.80


ATOM
425
N
LYS
A
591
9.839
16.014
8.191
1.00
35.07


ATOM
426
CA
LYS
A
591
10.016
17.389
8.648
1.00
34.67


ATOM
427
CB
LYS
A
591
9.427
18.381
7.641
1.00
46.77


ATOM
428
CG
LYS
A
591
10.350
18.721
6.480
1.00
47.35


ATOM
429
CD
LYS
A
591
10.650
17.509
5.612
1.00
47.48


ATOM
430
CE
LYS
A
591
11.738
17.813
4.587
1.00
47.57


ATOM
431
NZ
LYS
A
591
11.398
18.958
3.694
1.00
47.52


ATOM
432
C
LYS
A
591
9.274
17.492
9.976
1.00
33.93


ATOM
433
O
LYS
A
591
8.132
17.049
10.081
1.00
34.06


ATOM
434
N
HIS
A
592
9.926
18.068
10.983
1.00
27.75


ATOM
435
CA
HIS
A
592
9.332
18.205
12.310
1.00
26.86


ATOM
436
CB
HIS
A
592
10.227
19.071
13.208
1.00
27.82


ATOM
437
CG
HIS
A
592
9.770
19.139
14.632
1.00
26.72


ATOM
438
CD2
HIS
A
592
9.317
20.178
15.374
1.00
27.57


ATOM
439
ND1
HIS
A
592
9.755
18.040
15.464
1.00
27.40


ATOM
440
CE1
HIS
A
592
9.314
18.399
16.657
1.00
27.96


ATOM
441
NE2
HIS
A
592
9.041
19.692
16.628
1.00
27.67


ATOM
442
C
HIS
A
592
7.927
18.796
12.277
1.00
28.09


ATOM
443
O
HIS
A
592
7.021
18.288
12.933
1.00
26.68


ATOM
444
N
GLU
A
593
7.749
19.865
11.508
1.00
32.89


ATOM
445
CA
GLU
A
593
6.456
20.534
11.405
1.00
34.01


ATOM
446
CB
GLU
A
593
6.572
21.771
10.510
1.00
53.17


ATOM
447
CG
GLU
A
593
7.483
22.870
11.051
1.00
53.98


ATOM
448
CD
GLU
A
593
8.914
22.403
11.272
1.00
54.08


ATOM
449
OE1
GLU
A
593
9.519
21.853
10.326
1.00
53.79


ATOM
450
OE2
GLU
A
593
9.434
22.591
12.394
1.00
53.97


ATOM
451
C
GLU
A
593
5.370
19.613
10.856
1.00
33.01


ATOM
452
O
GLU
A
593
4.230
19.634
11.319
1.00
32.84


ATOM
453
N
VAL
A
594
5.730
18.808
9.864
1.00
27.04


ATOM
454
CA
VAL
A
594
4.783
17.886
9.249
1.00
25.85


ATOM
455
CB
VAL
A
594
5.382
17.279
7.962
1.00
24.72


ATOM
456
CG1
VAL
A
594
4.446
16.233
7.381
1.00
24.57


ATOM
457
CG2
VAL
A
594
5.631
18.383
6.945
1.00
24.02


ATOM
458
C
VAL
A
594
4.386
16.771
10.215
1.00
26.36


ATOM
459
O
VAL
A
594
3.214
16.386
10.283
1.00
25.05


ATOM
460
N
LEU
A
595
5.356
16.246
10.956
1.00
24.15


ATOM
461
CA
LEU
A
595
5.062
15.187
11.918
1.00
25.41


ATOM
462
CB
LEU
A
595
6.352
14.633
12.536
1.00
24.61


ATOM
463
CG
LEU
A
595
6.204
13.640
13.696
1.00
25.86


ATOM
464
CD1
LEU
A
595
5.345
12.453
13.272
1.00
24.75


ATOM
465
CD2
LEU
A
595
7.577
13.163
14.141
1.00
25.05


ATOM
466
C
LEU
A
595
4.148
15.745
13.009
1.00
25.02


ATOM
467
O
LEU
A
595
3.197
15.088
13.435
1.00
24.20


ATOM
468
N
CYS
A
596
4.426
16.970
13.451
1.00
24.36


ATOM
469
CA
CYS
A
596
3.603
17.588
14.479
1.00
24.03


ATOM
470
CB
CYS
A
596
4.195
18.931
14.907
1.00
27.15


ATOM
471
SG
CYS
A
596
5.699
18.771
15.892
1.00
26.30


ATOM
472
C
CYS
A
596
2.177
17.789
13.987
1.00
24.31


ATOM
473
O
CYS
A
596
1.222
17.537
14.721
1.00
24.29


ATOM
474
N
ARG
A
597
2.032
18.233
12.742
1.00
22.43


ATOM
475
CA
ARG
A
597
0.703
18.460
12.194
1.00
22.27


ATOM
476
CB
ARG
A
597
0.777
19.177
10.841
1.00
37.36


ATOM
477
CG
ARG
A
597
−0.597
19.576
10.315
1.00
38.44


ATOM
478
CD
ARG
A
597
−0.541
20.392
9.032
1.00
38.82


ATOM
479
NE
ARG
A
597
0.033
21.719
9.233
1.00
38.78


ATOM
480
CZ
ARG
A
597
1.286
22.043
8.936
1.00
38.71


ATOM
481
NH1
ARG
A
597
2.101
21.133
8.421
1.00
38.58


ATOM
482
NH2
ARG
A
597
1.721
23.278
9.149
1.00
38.90


ATOM
483
C
ARG
A
597
−0.042
17.140
12.042
1.00
21.87


ATOM
484
O
ARG
A
597
−1.231
17.049
12.347
1.00
22.25


ATOM
485
N
TRP
A
598
0.661
16.114
11.578
1.00
22.62


ATOM
486
CA
TRP
A
598
0.039
14.802
11.396
1.00
20.68


ATOM
487
CB
TRP
A
598
1.048
13.826
10.788
1.00
21.19


ATOM
488
CG
TRP
A
598
0.506
12.443
10.641
1.00
20.61


ATOM
489
CD2
TRP
A
598
0.680
11.358
11.554
1.00
21.45


ATOM
490
CE2
TRP
A
598
−0.059
10.262
11.048
1.00
20.54


ATOM
491
CE3
TRP
A
598
1.386
11.201
12.755
1.00
20.69


ATOM
492
CD1
TRP
A
598
−0.304
11.982
9.644
1.00
21.12


ATOM
493
NE1
TRP
A
598
−0.648
10.671
9.882
1.00
21.75


ATOM
494
CZ2
TRP
A
598
−0.111
9.028
11.701
1.00
20.03


ATOM
495
CZ3
TRP
A
598
1.334
9.974
13.406
1.00
21.23


ATOM
496
CH2
TRP
A
598
0.588
8.901
12.875
1.00
21.56


ATOM
497
C
TRP
A
598
−0.461
14.256
12.734
1.00
20.83


ATOM
498
O
TRP
A
598
−1.575
13.743
12.833
1.00
20.85


ATOM
499
N
ILE
A
599
0.371
14.362
13.762
1.00
18.38


ATOM
500
CA
ILE
A
599
−0.001
13.881
15.081
1.00
17.01


ATOM
501
CB
ILE
A
599
1.138
14.106
16.103
1.00
18.07


ATOM
502
CG2
ILE
A
599
0.625
13.881
17.516
1.00
18.87


ATOM
503
CG1
ILE
A
599
2.304
13.158
15.794
1.00
18.94


ATOM
504
CD1
ILE
A
599
3.523
13.367
16.669
1.00
18.33


ATOM
505
C
ILE
A
599
−1.263
14.596
15.554
1.00
18.40


ATOM
506
O
ILE
A
599
−2.184
13.969
16.081
1.00
16.74


ATOM
507
N
LEU
A
600
−1.311
15.912
15.371
1.00
21.06


ATOM
508
CA
LEU
A
600
−2.486
16.657
15.802
1.00
21.13


ATOM
509
CB
LEU
A
600
−2.202
18.162
15.761
1.00
21.76


ATOM
510
CG
LEU
A
600
−1.149
18.582
16.788
1.00
21.76


ATOM
511
CD1
LEU
A
600
−0.811
20.053
16.597
1.00
21.85


ATOM
512
CD2
LEU
A
600
−1.672
18.324
18.201
1.00
22.51


ATOM
513
C
LEU
A
600
−3.728
16.325
14.979
1.00
20.73


ATOM
514
O
LEU
A
600
−4.841
16.351
15.501
1.00
21.49


ATOM
515
N
SER
A
601
−3.540
16.032
13.694
1.00
21.08


ATOM
516
CA
SER
A
601
−4.665
15.674
12.833
1.00
20.75


ATOM
517
CB
SER
A
601
−4.225
15.579
11.372
1.00
22.55


ATOM
518
OG
SER
A
601
−4.008
16.869
10.822
1.00
23.14


ATOM
519
C
SER
A
601
−5.228
14.333
13.287
1.00
20.19


ATOM
520
O
SER
A
601
−6.438
14.125
13.275
1.00
20.13


ATOM
521
N
VAL
A
602
−4.340
13.424
13.679
1.00
21.43


ATOM
522
CA
VAL
A
602
−4.773
12.116
14.168
1.00
21.85


ATOM
523
CB
VAL
A
602
−3.564
11.204
14.471
1.00
17.69


ATOM
524
CG1
VAL
A
602
−4.018
9.928
15.198
1.00
18.88


ATOM
525
CG2
VAL
A
602
−2.867
10.845
13.174
1.00
19.25


ATOM
526
C
VAL
A
602
−5.581
12.312
15.445
1.00
21.58


ATOM
527
O
VAL
A
602
−6.705
11.823
15.566
1.00
20.63


ATOM
528
N
LYS
A
603
−5.011
13.052
16.394
1.00
20.30


ATOM
529
CA
LYS
A
603
−5.697
13.303
17.655
1.00
19.93


ATOM
530
CB
LYS
A
603
−4.833
14.186
18.567
1.00
29.59


ATOM
531
CG
LYS
A
603
−5.553
14.663
19.829
1.00
29.47


ATOM
532
CD
LYS
A
603
−4.587
15.206
20.882
1.00
30.01


ATOM
533
CE
LYS
A
603
−3.846
16.449
20.416
1.00
30.55


ATOM
534
NZ
LYS
A
603
−2.899
16.934
21.464
1.00
31.23


ATOM
535
C
LYS
A
603
−7.052
13.968
17.430
1.00
19.43


ATOM
536
O
LYS
A
603
−8.034
13.636
18.095
1.00
20.76


ATOM
537
N
LYS
A
604
−7.100
14.894
16.481
1.00
19.98


ATOM
538
CA
LYS
A
604
−8.325
15.629
16.174
1.00
21.57


ATOM
539
CB
LYS
A
604
−8.024
16.775
15.207
1.00
38.76


ATOM
540
CG
LYS
A
604
−9.262
17.531
14.741
1.00
39.38


ATOM
541
CD
LYS
A
604
−8.910
18.610
13.732
1.00
39.39


ATOM
542
CE
LYS
A
604
−10.158
19.340
13.255
1.00
39.74


ATOM
543
NZ
LYS
A
604
−9.843
20.385
12.242
1.00
39.72


ATOM
544
C
LYS
A
604
−9.413
14.754
15.579
1.00
20.90


ATOM
545
O
LYS
A
604
−10.609
15.039
15.742
1.00
21.11


ATOM
546
N
ASN
A
605
−9.009
13.688
14.892
1.00
21.37


ATOM
547
CA
ASN
A
605
−9.987
12.812
14.273
1.00
21.04


ATOM
548
CB
ASN
A
605
−9.486
12.315
12.920
1.00
27.07


ATOM
549
CG
ASN
A
605
−9.635
13.366
11.836
1.00
27.98


ATOM
550
OD1
ASN
A
605
−8.775
14.234
11.666
1.00
27.85


ATOM
551
ND2
ASN
A
605
−10.745
13.308
11.112
1.00
27.52


ATOM
552
C
ASN
A
605
−10.506
11.662
15.116
1.00
21.57


ATOM
553
O
ASN
A
605
−11.072
10.702
14.590
1.00
23.07


ATOM
554
N
TYR
A
606
−10.292
11.754
16.422
1.00
20.07


ATOM
555
CA
TYR
A
606
−10.853
10.792
17.349
1.00
20.46


ATOM
556
CB
TYR
A
606
−9.858
10.374
18.437
1.00
18.79


ATOM
557
CG
TYR
A
606
−8.993
9.216
17.992
1.00
18.19


ATOM
558
CD1
TYR
A
606
−7.745
9.430
17.409
1.00
19.08


ATOM
559
CE1
TYR
A
606
−6.989
8.362
16.913
1.00
18.94


ATOM
560
CD2
TYR
A
606
−9.467
7.909
18.074
1.00
18.23


ATOM
561
CE2
TYR
A
606
−8.722
6.840
17.578
1.00
17.63


ATOM
562
CZ
TYR
A
606
−7.485
7.077
16.999
1.00
18.23


ATOM
563
OH
TYR
A
606
−6.747
6.029
16.489
1.00
15.86


ATOM
564
C
TYR
A
606
−12.015
11.580
17.947
1.00
21.76


ATOM
565
O
TYR
A
606
−11.975
12.819
18.007
1.00
20.70


ATOM
566
N
ARG
A
607
−13.060
10.882
18.365
1.00
19.57


ATOM
567
CA
ARG
A
607
−14.223
11.562
18.931
1.00
20.12


ATOM
568
CB
ARG
A
607
−15.497
10.791
18.575
1.00
23.54


ATOM
569
CG
ARG
A
607
−15.679
10.605
17.074
1.00
23.38


ATOM
570
CD
ARG
A
607
−17.034
10.010
16.715
1.00
23.37


ATOM
571
NE
ARG
A
607
−17.142
9.734
15.282
1.00
24.11


ATOM
572
CZ
ARG
A
607
−18.274
9.408
14.665
1.00
24.11


ATOM
573
NH1
ARG
A
607
−19.405
9.321
15.355
1.00
24.42


ATOM
574
NH2
ARG
A
607
−18.274
9.163
13.362
1.00
25.10


ATOM
575
C
ARG
A
607
−14.037
11.647
20.438
1.00
20.33


ATOM
576
O
ARG
A
607
−14.168
10.648
21.150
1.00
20.09


ATOM
577
N
LYS
A
608
−13.736
12.847
20.926
1.00
25.24


ATOM
578
CA
LYS
A
608
−13.484
13.033
22.349
1.00
25.95


ATOM
579
CB
LYS
A
608
−13.108
14.491
22.636
1.00
41.13


ATOM
580
CG
LYS
A
608
−14.175
15.511
22.294
1.00
41.73


ATOM
581
CD
LYS
A
608
−13.670
16.916
22.603
1.00
41.87


ATOM
582
CE
LYS
A
608
−14.750
17.972
22.413
1.00
41.79


ATOM
583
NZ
LYS
A
608
−14.231
19.340
22.703
1.00
41.73


ATOM
584
C
LYS
A
608
−14.625
12.599
23.254
1.00
26.44


ATOM
585
O
LYS
A
608
−14.397
12.225
24.405
1.00
25.96


ATOM
586
N
ASN
A
609
−15.847
12.626
22.732
1.00
27.23


ATOM
587
CA
ASN
A
609
−17.005
12.248
23.522
1.00
27.32


ATOM
588
CB
ASN
A
609
−18.212
13.066
23.071
1.00
36.30


ATOM
589
CG
ASN
A
609
−17.995
14.554
23.282
1.00
36.84


ATOM
590
OD1
ASN
A
609
−17.809
15.008
24.411
1.00
37.02


ATOM
591
ND2
ASN
A
609
−17.998
15.316
22.199
1.00
37.30


ATOM
592
C
ASN
A
609
−17.317
10.758
23.541
1.00
26.80


ATOM
593
O
ASN
A
609
−18.330
10.332
24.098
1.00
27.72


ATOM
594
N
VAL
A
610
−16.451
9.964
22.920
1.00
21.65


ATOM
595
CA
VAL
A
610
−16.616
8.512
22.946
1.00
20.92


ATOM
596
CB
VAL
A
610
−16.097
7.862
21.645
1.00
20.35


ATOM
597
CG1
VAL
A
610
−15.897
6.370
21.846
1.00
20.76


ATOM
598
CG2
VAL
A
610
−17.120
8.086
20.522
1.00
18.26


ATOM
599
C
VAL
A
610
−15.780
8.109
24.171
1.00
19.89


ATOM
600
O
VAL
A
610
−14.590
8.414
24.254
1.00
20.96


ATOM
601
N
ALA
A
611
−16.423
7.450
25.130
1.00
19.80


ATOM
602
CA
ALA
A
611
−15.791
7.078
26.397
1.00
19.90


ATOM
603
CB
ALA
A
611
−16.780
6.287
27.251
1.00
20.34


ATOM
604
C
ALA
A
611
−14.448
6.363
26.383
1.00
19.34


ATOM
605
O
ALA
A
611
−13.549
6.731
27.138
1.00
20.80


ATOM
606
N
TYR
A
612
−14.307
5.343
25.542
1.00
18.10


ATOM
607
CA
TYR
A
612
−13.060
4.599
25.512
1.00
15.69


ATOM
608
CB
TYR
A
612
−13.321
3.134
25.873
1.00
20.49


ATOM
609
CG
TYR
A
612
−12.107
2.251
25.709
1.00
20.53


ATOM
610
CD1
TYR
A
612
−12.047
1.304
24.685
1.00
21.50


ATOM
611
CE1
TYR
A
612
−10.932
0.484
24.536
1.00
20.27


ATOM
612
CD2
TYR
A
612
−11.020
2.359
26.577
1.00
20.70


ATOM
613
CE2
TYR
A
612
−9.906
1.546
26.434
1.00
19.44


ATOM
614
CZ
TYR
A
612
−9.870
0.611
25.414
1.00
20.76


ATOM
615
OH
TYR
A
612
−8.769
−0.205
25.284
1.00
20.43


ATOM
616
C
TYR
A
612
−12.264
4.682
24.218
1.00
14.59


ATOM
617
O
TYR
A
612
−11.064
4.921
24.268
1.00
15.21


ATOM
618
N
HIS
A
613
−12.915
4.500
23.069
1.00
16.35


ATOM
619
CA
HIS
A
613
−12.197
4.553
21.793
1.00
15.66


ATOM
620
CB
HIS
A
613
−12.942
3.763
20.705
1.00
19.05


ATOM
621
CG
HIS
A
613
−12.971
2.286
20.941
1.00
21.28


ATOM
622
CD2
HIS
A
613
−12.010
1.341
20.797
1.00
20.01


ATOM
623
ND1
HIS
A
613
−14.087
1.628
21.408
1.00
19.61


ATOM
624
CE1
HIS
A
613
−13.816
0.342
21.541
1.00
20.40


ATOM
625
NE2
HIS
A
613
−12.562
0.140
21.176
1.00
20.73


ATOM
626
C
HIS
A
613
−11.998
5.989
21.330
1.00
15.17


ATOM
627
O
HIS
A
613
−12.633
6.451
20.376
1.00
17.00


ATOM
628
N
ASN
A
614
−11.101
6.682
22.020
1.00
18.64


ATOM
629
CA
ASN
A
614
−10.784
8.068
21.725
1.00
17.28


ATOM
630
CB
ASN
A
614
−11.344
8.977
22.827
1.00
21.97


ATOM
631
CG
ASN
A
614
−10.939
8.530
24.219
1.00
21.21


ATOM
632
OD1
ASN
A
614
−9.752
8.417
24.526
1.00
22.66


ATOM
633
ND2
ASN
A
614
−11.928
8.277
25.074
1.00
21.32


ATOM
634
C
ASN
A
614
−9.265
8.207
21.628
1.00
18.30


ATOM
635
O
ASN
A
614
−8.543
7.210
21.671
1.00
17.11


ATOM
636
N
TRP
A
615
−8.773
9.434
21.504
1.00
20.23


ATOM
637
CA
TRP
A
615
−7.335
9.650
21.388
1.00
20.84


ATOM
638
CB
TRP
A
615
−7.020
11.152
21.346
1.00
18.84


ATOM
639
CG
TRP
A
615
−5.567
11.469
21.610
1.00
20.81


ATOM
640
CD2
TRP
A
615
−4.446
11.146
20.775
1.00
20.87


ATOM
641
CE2
TRP
A
615
−3.287
11.632
21.427
1.00
20.24


ATOM
642
CE3
TRP
A
615
−4.307
10.493
19.542
1.00
20.69


ATOM
643
CD1
TRP
A
615
−5.055
12.115
22.700
1.00
19.88


ATOM
644
NE1
TRP
A
615
−3.689
12.217
22.599
1.00
19.37


ATOM
645
CZ2
TRP
A
615
−2.007
11.488
20.886
1.00
21.34


ATOM
646
CZ3
TRP
A
615
−3.031
10.346
19.004
1.00
21.28


ATOM
647
CH2
TRP
A
615
−1.897
10.845
19.679
1.00
21.14


ATOM
648
C
TRP
A
615
−6.457
8.993
22.453
1.00
19.80


ATOM
649
O
TRP
A
615
−5.383
8.479
22.133
1.00
19.45


ATOM
650
N
ARG
A
616
−6.888
9.010
23.713
1.00
19.15


ATOM
651
CA
ARG
A
616
−6.063
8.424
24.764
1.00
18.73


ATOM
652
CB
ARG
A
616
−6.658
8.707
26.146
1.00
20.84


ATOM
653
CG
ARG
A
616
−6.628
10.197
26.516
1.00
20.98


ATOM
654
CD
ARG
A
616
−5.208
10.754
26.511
1.00
21.78


ATOM
655
NE
ARG
A
616
−5.185
12.195
26.772
1.00
22.05


ATOM
656
CZ
ARG
A
616
−4.519
12.760
27.773
1.00
22.62


ATOM
657
NH1
ARG
A
616
−3.820
12.012
28.610
1.00
22.11


ATOM
658
NH2
ARG
A
616
−4.558
14.074
27.936
1.00
22.34


ATOM
659
C
ARG
A
616
−5.869
6.922
24.559
1.00
18.23


ATOM
660
O
ARG
A
616
−4.799
6.388
24.857
1.00
18.43


ATOM
661
N
HIS
A
617
−6.889
6.246
24.041
1.00
17.23


ATOM
662
CA
HIS
A
617
−6.754
4.812
23.796
1.00
17.41


ATOM
663
CB
HIS
A
617
−8.095
4.194
23.403
1.00
16.86


ATOM
664
CG
HIS
A
617
−7.964
2.830
22.798
1.00
13.76


ATOM
665
CD2
HIS
A
617
−8.291
2.369
21.569
1.00
17.85


ATOM
666
ND1
HIS
A
617
−7.384
1.772
23.465
1.00
17.12


ATOM
667
CE1
HIS
A
617
−7.357
0.716
22.670
1.00
15.55


ATOM
668
NE2
HIS
A
617
−7.899
1.052
21.515
1.00
16.82


ATOM
669
C
HIS
A
617
−5.737
4.566
22.682
1.00
17.79


ATOM
670
O
HIS
A
617
−4.911
3.643
22.770
1.00
17.66


ATOM
671
N
ALA
A
618
−5.807
5.384
21.635
1.00
16.69


ATOM
672
CA
ALA
A
618
−4.897
5.268
20.499
1.00
17.60


ATOM
673
CB
ALA
A
618
−5.268
6.270
19.416
1.00
19.06


ATOM
674
C
ALA
A
618
−3.478
5.517
20.973
1.00
18.60


ATOM
675
O
ALA
A
618
−2.553
4.777
20.642
1.00
16.65


ATOM
676
N
PHE
A
619
−3.327
6.573
21.764
1.00
16.36


ATOM
677
CA
PHE
A
619
−2.040
6.942
22.316
1.00
18.60


ATOM
678
CB
PHE
A
619
−2.205
8.224
23.142
1.00
21.01


ATOM
679
CG
PHE
A
619
−0.989
8.594
23.938
1.00
22.31


ATOM
680
CD1
PHE
A
619
0.166
9.041
23.305
1.00
21.99


ATOM
681
CD2
PHE
A
619
−0.995
8.475
25.326
1.00
22.04


ATOM
682
CE1
PHE
A
619
1.304
9.366
24.045
1.00
21.42


ATOM
683
CE2
PHE
A
619
0.139
8.798
26.076
1.00
21.94


ATOM
684
CZ
PHE
A
619
1.292
9.246
25.426
1.00
21.32


ATOM
685
C
PHE
A
619
−1.459
5.816
23.176
1.00
17.86


ATOM
686
O
PHE
A
619
−0.285
5.470
23.040
1.00
17.74


ATOM
687
N
ASN
A
620
−2.281
5.239
24.049
1.00
17.68


ATOM
688
CA
ASN
A
620
−1.814
4.160
24.920
1.00
18.84


ATOM
689
CB
ASN
A
620
−2.868
3.793
25.972
1.00
22.20


ATOM
690
CG
ASN
A
620
−3.028
4.867
27.037
1.00
22.41


ATOM
691
OD1
ASN
A
620
−2.078
5.578
27.354
1.00
22.93


ATOM
692
ND2
ASN
A
620
−4.220
4.969
27.611
1.00
21.57


ATOM
693
C
ASN
A
620
−1.450
2.921
24.113
1.00
18.91


ATOM
694
O
ASN
A
620
−0.514
2.201
24.461
1.00
18.42


ATOM
695
N
THR
A
621
−2.184
2.682
23.031
1.00
16.41


ATOM
696
CA
THR
A
621
−1.901
1.519
22.191
1.00
16.82


ATOM
697
CB
THR
A
621
−2.965
1.360
21.093
1.00
17.95


ATOM
698
OG1
THR
A
621
−4.246
1.190
21.704
1.00
17.42


ATOM
699
CG2
THR
A
621
−2.664
0.130
20.233
1.00
17.02


ATOM
700
C
THR
A
621
−0.526
1.693
21.556
1.00
18.34


ATOM
701
O
THR
A
621
0.276
0.749
21.505
1.00
18.19


ATOM
702
N
ALA
A
622
−0.249
2.901
21.085
1.00
15.98


ATOM
703
CA
ALA
A
622
1.041
3.211
20.479
1.00
18.35


ATOM
704
CB
ALA
A
622
1.005
4.592
19.864
1.00
16.90


ATOM
705
C
ALA
A
622
2.151
3.138
21.529
1.00
17.61


ATOM
706
O
ALA
A
622
3.242
2.656
21.248
1.00
16.57


ATOM
707
N
GLN
A
623
1.876
3.622
22.740
1.00
17.78


ATOM
708
CA
GLN
A
623
2.878
3.578
23.803
1.00
19.17


ATOM
709
CB
GLN
A
623
2.351
4.260
25.071
1.00
19.99


ATOM
710
CG
GLN
A
623
3.361
4.335
26.219
1.00
19.42


ATOM
711
CD
GLN
A
623
3.358
3.103
27.110
1.00
20.35


ATOM
712
OE1
GLN
A
623
2.302
2.595
27.488
1.00
19.39


ATOM
713
NE2
GLN
A
623
4.547
2.634
27.475
1.00
19.48


ATOM
714
C
GLN
A
623
3.251
2.137
24.114
1.00
19.45


ATOM
715
O
GLN
A
623
4.420
1.824
24.358
1.00
19.89


ATOM
716
N
CYS
A
624
2.258
1.256
24.118
1.00
17.26


ATOM
717
CA
CYS
A
624
2.533
−0.146
24.385
1.00
19.37


ATOM
718
CB
CYS
A
624
1.234
−0.938
24.530
1.00
19.88


ATOM
719
SG
CYS
A
624
1.499
−2.658
25.026
1.00
19.62


ATOM
720
C
CYS
A
624
3.369
−0.708
23.237
1.00
18.34


ATOM
721
O
CYS
A
624
4.255
−1.528
23.460
1.00
18.71


ATOM
722
N
MET
A
625
3.094
−0.258
22.015
1.00
19.30


ATOM
723
CA
MET
A
625
3.844
−0.720
20.843
1.00
18.88


ATOM
724
CB
MET
A
625
3.259
−0.102
19.567
1.00
21.69


ATOM
725
CG
MET
A
625
3.952
−0.521
18.267
1.00
19.33


ATOM
726
SD
MET
A
625
3.854
−2.291
17.926
1.00
18.96


ATOM
727
CE
MET
A
625
2.148
−2.414
17.292
1.00
20.28


ATOM
728
C
MET
A
625
5.307
−0.296
21.019
1.00
20.73


ATOM
729
O
MET
A
625
6.226
−1.097
20.832
1.00
19.61


ATOM
730
N
PHE
A
626
5.515
0.968
21.381
1.00
21.46


ATOM
731
CA
PHE
A
626
6.862
1.487
21.604
1.00
22.24


ATOM
732
CB
PHE
A
626
6.810
2.973
22.003
1.00
18.30


ATOM
733
CG
PHE
A
626
8.162
3.566
22.325
1.00
18.77


ATOM
734
CD1
PHE
A
626
8.662
3.539
23.628
1.00
19.77


ATOM
735
CD2
PHE
A
626
8.943
4.126
21.321
1.00
19.03


ATOM
736
CE1
PHE
A
626
9.920
4.060
23.921
1.00
19.58


ATOM
737
CE2
PHE
A
626
10.207
4.650
21.607
1.00
19.50


ATOM
738
CZ
PHE
A
626
10.693
4.616
22.907
1.00
17.99


ATOM
739
C
PHE
A
626
7.578
0.684
22.685
1.00
22.81


ATOM
740
O
PHE
A
626
8.747
0.321
22.528
1.00
22.67


ATOM
741
N
ALA
A
627
6.878
0.405
23.781
1.00
23.57


ATOM
742
CA
ALA
A
627
7.460
−0.351
24.883
1.00
24.17


ATOM
743
CB
ALA
A
627
6.511
−0.357
26.082
1.00
26.38


ATOM
744
C
ALA
A
627
7.794
−1.787
24.477
1.00
24.26


ATOM
745
O
ALA
A
627
8.854
−2.305
24.834
1.00
25.36


ATOM
746
N
ALA
A
628
6.898
−2.428
23.728
1.00
21.99


ATOM
747
CA
ALA
A
628
7.127
−3.806
23.296
1.00
22.22


ATOM
748
CB
ALA
A
628
5.884
−4.364
22.609
1.00
18.57


ATOM
749
C
ALA
A
628
8.315
−3.879
22.350
1.00
23.09


ATOM
750
O
ALA
A
628
9.085
−4.838
22.382
1.00
22.87


ATOM
751
N
LEU
A
629
8.462
−2.864
21.506
1.00
21.79


ATOM
752
CA
LEU
A
629
9.565
−2.835
20.555
1.00
24.56


ATOM
753
CB
LEU
A
629
9.338
−1.737
19.521
1.00
24.39


ATOM
754
CG
LEU
A
629
8.155
−1.980
18.582
1.00
25.70


ATOM
755
CD1
LEU
A
629
7.906
−0.753
17.734
1.00
25.30


ATOM
756
CD2
LEU
A
629
8.446
−3.200
17.711
1.00
26.08


ATOM
757
C
LEU
A
629
10.897
−2.608
21.256
1.00
25.12


ATOM
758
O
LEU
A
629
11.898
−3.243
20.920
1.00
25.35


ATOM
759
N
LYS
A
630
10.907
−1.705
22.234
1.00
32.90


ATOM
760
CA
LYS
A
630
12.126
−1.394
22.981
1.00
33.87


ATOM
761
CB
LYS
A
630
12.033
0.012
23.573
1.00
31.73


ATOM
762
CG
LYS
A
630
12.137
1.116
22.544
1.00
31.51


ATOM
763
CD
LYS
A
630
13.494
1.089
21.868
1.00
32.17


ATOM
764
CE
LYS
A
630
13.682
2.292
20.966
1.00
31.52


ATOM
765
NZ
LYS
A
630
14.984
2.243
20.254
1.00
31.88


ATOM
766
C
LYS
A
630
12.416
−2.394
24.096
1.00
34.55


ATOM
767
O
LYS
A
630
13.176
−3.347
23.906
1.00
35.07


ATOM
768
N
ALA
A
631
11.814
−2.168
25.260
1.00
30.54


ATOM
769
CA
ALA
A
631
12.005
−3.047
26.406
1.00
30.93


ATOM
770
CB
ALA
A
631
11.175
−2.548
27.590
1.00
31.25


ATOM
771
C
ALA
A
631
11.630
−4.492
26.070
1.00
30.76


ATOM
772
O
ALA
A
631
12.270
−5.432
26.538
1.00
30.38


ATOM
773
N
GLY
A
632
10.588
−4.660
25.257
1.00
30.21


ATOM
774
CA
GLY
A
632
10.147
−5.991
24.871
1.00
30.31


ATOM
775
C
GLY
A
632
11.073
−6.644
23.860
1.00
30.73


ATOM
776
O
GLY
A
632
10.975
−7.843
23.592
1.00
30.32


ATOM
777
N
LYS
A
633
11.967
−5.848
23.287
1.00
31.93


ATOM
778
CA
LYS
A
633
12.937
−6.346
22.315
1.00
32.77


ATOM
779
CB
LYS
A
633
13.858
−7.374
22.979
1.00
44.15


ATOM
780
CG
LYS
A
633
14.875
−6.775
23.929
1.00
44.47


ATOM
781
CD
LYS
A
633
15.841
−7.835
24.426
1.00
44.54


ATOM
782
CE
LYS
A
633
17.052
−7.197
25.079
1.00
44.74


ATOM
783
NZ
LYS
A
633
17.770
−6.316
24.114
1.00
44.90


ATOM
784
C
LYS
A
633
12.352
−6.948
21.041
1.00
32.00


ATOM
785
O
LYS
A
633
12.862
−7.944
20.522
1.00
32.88


ATOM
786
N
ILE
A
634
11.292
−6.338
20.527
1.00
26.60


ATOM
787
CA
ILE
A
634
10.670
−6.818
19.305
1.00
25.39


ATOM
788
CB
ILE
A
634
9.124
−6.695
19.400
1.00
26.41


ATOM
789
CG2
ILE
A
634
8.473
−7.074
18.076
1.00
27.54


ATOM
790
CG1
ILE
A
634
8.607
−7.612
20.510
1.00
27.29


ATOM
791
CD1
ILE
A
634
7.113
−7.543
20.725
1.00
27.31


ATOM
792
C
ILE
A
634
11.200
−6.013
18.117
1.00
25.00


ATOM
793
O
ILE
A
634
11.127
−6.446
16.968
1.00
25.10


ATOM
794
N
GLN
A
635
11.770
−4.850
18.409
1.00
23.96


ATOM
795
CA
GLN
A
635
12.305
−3.975
17.377
1.00
23.37


ATOM
796
CB
GLN
A
635
12.904
−2.716
18.010
1.00
27.98


ATOM
797
CG
GLN
A
635
13.476
−1.740
17.002
1.00
28.57


ATOM
798
CD
GLN
A
635
14.111
−0.516
17.645
1.00
28.17


ATOM
799
OE1
GLN
A
635
14.635
0.354
16.953
1.00
29.49


ATOM
800
NE2
GLN
A
635
14.059
−0.444
18.967
1.00
27.30


ATOM
801
C
GLN
A
635
13.368
−4.672
16.535
1.00
24.49


ATOM
802
O
GLN
A
635
13.445
−4.468
15.324
1.00
24.24


ATOM
803
N
ASN
A
636
14.180
−5.493
17.195
1.00
30.08


ATOM
804
CA
ASN
A
636
15.266
−6.222
16.547
1.00
31.17


ATOM
805
CB
ASN
A
636
16.172
−6.829
17.618
1.00
31.58


ATOM
806
CG
ASN
A
636
16.612
−5.811
18.651
1.00
32.71


ATOM
807
OD1
ASN
A
636
17.739
−5.309
18.607
1.00
32.53


ATOM
808
ND2
ASN
A
636
15.716
−5.490
19.585
1.00
31.94


ATOM
809
C
ASN
A
636
14.782
−7.330
15.617
1.00
31.51


ATOM
810
O
ASN
A
636
15.553
−7.853
14.809
1.00
31.97


ATOM
811
N
LYS
A
637
13.510
−7.690
15.732
1.00
28.95


ATOM
812
CA
LYS
A
637
12.944
−8.750
14.904
1.00
28.44


ATOM
813
CB
LYS
A
637
11.983
−9.596
15.740
1.00
31.06


ATOM
814
CG
LYS
A
637
12.590
−10.196
16.993
1.00
30.31


ATOM
815
CD
LYS
A
637
11.502
−10.770
17.889
1.00
30.88


ATOM
816
CE
LYS
A
637
12.072
−11.316
19.186
1.00
31.13


ATOM
817
NZ
LYS
A
637
12.956
−12.494
18.960
1.00
31.42


ATOM
818
C
LYS
A
637
12.200
−8.219
13.683
1.00
28.47


ATOM
819
O
LYS
A
637
11.696
−9.003
12.875
1.00
29.67


ATOM
820
N
LEU
A
638
12.137
−6.898
13.539
1.00
27.41


ATOM
821
CA
LEU
A
638
11.401
−6.297
12.427
1.00
27.76


ATOM
822
CB
LEU
A
638
10.187
−5.546
12.977
1.00
24.26


ATOM
823
CG
LEU
A
638
9.349
−6.293
14.016
1.00
24.56


ATOM
824
CD1
LEU
A
638
8.265
−5.366
14.549
1.00
25.02


ATOM
825
CD2
LEU
A
638
8.740
−7.549
13.396
1.00
24.12


ATOM
826
C
LEU
A
638
12.203
−5.348
11.543
1.00
26.64


ATOM
827
O
LEU
A
638
13.301
−4.925
11.896
1.00
28.43


ATOM
828
N
THR
A
639
11.630
−5.011
10.389
1.00
23.44


ATOM
829
CA
THR
A
639
12.253
−4.093
9.441
1.00
22.41


ATOM
830
CB
THR
A
639
11.772
−4.343
8.004
1.00
28.95


ATOM
831
OG1
THR
A
639
10.378
−4.021
7.908
1.00
28.33


ATOM
832
CG2
THR
A
639
11.982
−5.794
7.611
1.00
28.40


ATOM
833
C
THR
A
639
11.870
−2.662
9.798
1.00
22.44


ATOM
834
O
THR
A
639
10.921
−2.445
10.551
1.00
23.44


ATOM
835
N
ASP
A
640
12.601
−1.695
9.250
1.00
24.48


ATOM
836
CA
ASP
A
640
12.321
−0.288
9.508
1.00
24.67


ATOM
837
CB
ASP
A
640
13.313
0.604
8.747
1.00
30.57


ATOM
838
CG
ASP
A
640
14.693
0.642
9.393
1.00
30.89


ATOM
839
OD1
ASP
A
640
15.634
1.146
8.743
1.00
30.85


ATOM
840
OD2
ASP
A
640
14.838
0.184
10.548
1.00
30.86


ATOM
841
C
ASP
A
640
10.895
0.038
9.074
1.00
24.64


ATOM
842
O
ASP
A
640
10.177
0.761
9.765
1.00
24.23


ATOM
843
N
LEU
A
641
10.491
−0.513
7.931
1.00
24.25


ATOM
844
CA
LEU
A
641
9.153
−0.291
7.392
1.00
23.81


ATOM
845
CB
LEU
A
641
9.066
−0.863
5.975
1.00
25.82


ATOM
846
CG
LEU
A
641
9.326
0.063
4.781
1.00
27.50


ATOM
847
CD1
LEU
A
641
10.267
1.188
5.137
1.00
25.96


ATOM
848
CD2
LEU
A
641
9.858
−0.767
3.629
1.00
26.21


ATOM
849
C
LEU
A
641
8.074
−0.914
8.269
1.00
23.08


ATOM
850
O
LEU
A
641
7.013
−0.332
8.464
1.00
24.13


ATOM
851
N
GLU
A
642
8.336
−2.110
8.778
1.00
23.58


ATOM
852
CA
GLU
A
642
7.371
−2.771
9.639
1.00
24.03


ATOM
853
CB
GLU
A
642
7.847
−4.188
9.966
1.00
29.79


ATOM
854
CG
GLU
A
642
7.607
−5.150
8.816
1.00
30.52


ATOM
855
CD
GLU
A
642
8.276
−6.492
9.004
1.00
30.88


ATOM
856
OE1
GLU
A
642
7.928
−7.424
8.246
1.00
30.84


ATOM
857
OE2
GLU
A
642
9.147
−6.615
9.893
1.00
30.40


ATOM
858
C
GLU
A
642
7.166
−1.947
10.911
1.00
24.17


ATOM
859
O
GLU
A
642
6.043
−1.816
11.404
1.00
24.58


ATOM
860
N
ILE
A
643
8.260
−1.382
11.419
1.00
21.47


ATOM
861
CA
ILE
A
643
8.230
−0.555
12.625
1.00
21.07


ATOM
862
CB
ILE
A
643
9.659
−0.184
13.062
1.00
24.97


ATOM
863
CG2
ILE
A
643
9.614
0.833
14.195
1.00
23.30


ATOM
864
CG1
ILE
A
643
10.409
−1.444
13.502
1.00
23.69


ATOM
865
CD1
ILE
A
643
11.900
−1.229
13.673
1.00
24.32


ATOM
866
C
ILE
A
643
7.440
0.727
12.350
1.00
20.73


ATOM
867
O
ILE
A
643
6.536
1.088
13.109
1.00
20.07


ATOM
868
N
LEU
A
644
7.792
1.405
11.259
1.00
21.45


ATOM
869
CA
LEU
A
644
7.122
2.632
10.843
1.00
22.42


ATOM
870
CB
LEU
A
644
7.707
3.112
9.510
1.00
22.90


ATOM
871
CG
LEU
A
644
7.028
4.294
8.816
1.00
23.31


ATOM
872
CD1
LEU
A
644
7.162
5.546
9.670
1.00
23.35


ATOM
873
CD2
LEU
A
644
7.671
4.506
7.449
1.00
22.87


ATOM
874
C
LEU
A
644
5.623
2.400
10.686
1.00
22.48


ATOM
875
O
LEU
A
644
4.809
3.178
11.183
1.00
21.76


ATOM
876
N
ALA
A
645
5.262
1.327
9.993
1.00
19.64


ATOM
877
CA
ALA
A
645
3.858
1.003
9.770
1.00
19.40


ATOM
878
CB
ALA
A
645
3.747
−0.144
8.759
1.00
19.42


ATOM
879
C
ALA
A
645
3.110
0.643
11.062
1.00
18.96


ATOM
880
O
ALA
A
645
1.946
1.016
11.238
1.00
16.29


ATOM
881
N
LEU
A
646
3.767
−0.073
11.970
1.00
15.67


ATOM
882
CA
LEU
A
646
3.113
−0.458
13.218
1.00
17.59


ATOM
883
CB
LEU
A
646
3.972
−1.464
13.982
1.00
21.09


ATOM
884
CG
LEU
A
646
4.011
−2.880
13.401
1.00
20.20


ATOM
885
CD1
LEU
A
646
5.105
−3.678
14.102
1.00
20.69


ATOM
886
CD2
LEU
A
646
2.654
−3.552
13.561
1.00
21.23


ATOM
887
C
LEU
A
646
2.826
0.750
14.112
1.00
16.19


ATOM
888
O
LEU
A
646
1.770
0.824
14.748
1.00
17.93


ATOM
889
N
LEU
A
647
3.767
1.687
14.168
1.00
20.47


ATOM
890
CA
LEU
A
647
3.578
2.875
15.000
1.00
18.59


ATOM
891
CB
LEU
A
647
4.874
3.682
15.097
1.00
19.99


ATOM
892
CG
LEU
A
647
4.819
4.890
16.042
1.00
19.72


ATOM
893
CD1
LEU
A
647
4.422
4.432
17.445
1.00
21.01


ATOM
894
CD2
LEU
A
647
6.168
5.563
16.078
1.00
21.38


ATOM
895
C
LEU
A
647
2.447
3.735
14.436
1.00
19.57


ATOM
896
O
LEU
A
647
1.583
4.199
15.183
1.00
19.14


ATOM
897
N
ILE
A
648
2.447
3.935
13.120
1.00
17.04


ATOM
898
CA
ILE
A
648
1.393
4.714
12.475
1.00
16.34


ATOM
899
CB
ILE
A
648
1.671
4.884
10.962
1.00
16.27


ATOM
900
CG2
ILE
A
648
0.428
5.441
10.251
1.00
17.73


ATOM
901
CG1
ILE
A
648
2.895
5.787
10.770
1.00
18.41


ATOM
902
CD1
ILE
A
648
3.350
5.921
9.339
1.00
17.00


ATOM
903
C
ILE
A
648
0.060
3.999
12.674
1.00
17.17


ATOM
904
O
ILE
A
648
−0.946
4.620
13.027
1.00
16.88


ATOM
905
N
ALA
A
649
0.056
2.684
12.477
1.00
17.97


ATOM
906
CA
ALA
A
649
−1.171
1.912
12.634
1.00
18.14


ATOM
907
CB
ALA
A
649
−0.927
0.460
12.228
1.00
19.75


ATOM
908
C
ALA
A
649
−1.724
1.977
14.060
1.00
17.69


ATOM
909
O
ALA
A
649
−2.928
2.180
14.266
1.00
17.10


ATOM
910
N
ALA
A
650
−0.850
1.802
15.047
1.00
16.14


ATOM
911
CA
ALA
A
650
−1.276
1.846
16.438
1.00
15.98


ATOM
912
CB
ALA
A
650
−0.070
1.703
17.365
1.00
18.40


ATOM
913
C
ALA
A
650
−1.987
3.175
16.708
1.00
16.55


ATOM
914
O
ALA
A
650
−3.049
3.214
17.327
1.00
17.85


ATOM
915
N
LEU
A
651
−1.401
4.259
16.226
1.00
17.09


ATOM
916
CA
LEU
A
651
−1.974
5.589
16.438
1.00
17.07


ATOM
917
CB
LEU
A
651
−0.956
6.659
16.056
1.00
20.77


ATOM
918
CG
LEU
A
651
0.304
6.766
16.906
1.00
20.44


ATOM
919
CD1
LEU
A
651
1.326
7.596
16.156
1.00
20.57


ATOM
920
CD2
LEU
A
651
−0.036
7.402
18.255
1.00
20.14


ATOM
921
C
LEU
A
651
−3.246
5.846
15.648
1.00
17.89


ATOM
922
O
LEU
A
651
−4.133
6.569
16.102
1.00
17.40


ATOM
923
N
SER
A
652
−3.335
5.248
14.465
1.00
14.66


ATOM
924
CA
SER
A
652
−4.484
5.470
13.591
1.00
16.84


ATOM
925
CB
SER
A
652
−4.013
5.620
12.141
1.00
19.10


ATOM
926
OG
SER
A
652
−2.948
6.535
12.014
1.00
18.78


ATOM
927
C
SER
A
652
−5.549
4.386
13.596
1.00
17.02


ATOM
928
O
SER
A
652
−6.593
4.574
12.987
1.00
16.48


ATOM
929
N
HIS
A
653
−5.302
3.280
14.292
1.00
19.51


ATOM
930
CA
HIS
A
653
−6.219
2.143
14.241
1.00
18.51


ATOM
931
CB
HIS
A
653
−5.607
0.939
14.972
1.00
15.82


ATOM
932
CG
HIS
A
653
−5.944
0.882
16.427
1.00
16.43


ATOM
933
CD2
HIS
A
653
−6.947
0.252
17.079
1.00
15.65


ATOM
934
ND1
HIS
A
653
−5.237
1.574
17.385
1.00
14.87


ATOM
935
CE1
HIS
A
653
−5.794
1.376
18.567
1.00
15.10


ATOM
936
NE2
HIS
A
653
−6.838
0.580
18.406
1.00
15.73


ATOM
937
C
HIS
A
653
−7.681
2.284
14.652
1.00
19.28


ATOM
938
O
HIS
A
653
−8.486
1.441
14.289
1.00
17.55


ATOM
939
N
ASP
A
654
−8.039
3.329
15.395
1.00
14.03


ATOM
940
CA
ASP
A
654
−9.434
3.505
15.811
1.00
13.68


ATOM
941
CB
ASP
A
654
−9.576
3.404
17.342
1.00
17.23


ATOM
942
CG
ASP
A
654
−9.893
1.995
17.816
1.00
16.81


ATOM
943
OD1
ASP
A
654
−10.559
1.251
17.063
1.00
16.45


ATOM
944
OD2
ASP
A
654
−9.510
1.647
18.953
1.00
16.54


ATOM
945
C
ASP
A
654
−9.986
4.858
15.351
1.00
14.35


ATOM
946
O
ASP
A
654
−11.004
5.325
15.870
1.00
15.00


ATOM
947
N
LEU
A
655
−9.342
5.461
14.353
1.00
14.26


ATOM
948
CA
LEU
A
655
−9.745
6.777
13.838
1.00
15.05


ATOM
949
CB
LEU
A
655
−8.976
7.071
12.542
1.00
21.81


ATOM
950
CG
LEU
A
655
−8.028
8.263
12.357
1.00
25.53


ATOM
951
CD1
LEU
A
655
−7.712
8.958
13.671
1.00
22.91


ATOM
952
CD2
LEU
A
655
−6.766
7.763
11.665
1.00
22.84


ATOM
953
C
LEU
A
655
−11.257
6.941
13.591
1.00
16.32


ATOM
954
O
LEU
A
655
−11.889
6.120
12.923
1.00
15.44


ATOM
955
N
ASP
A
656
−11.826
8.013
14.147
1.00
16.42


ATOM
956
CA
ASP
A
656
−13.251
8.326
13.988
1.00
17.71


ATOM
957
CB
ASP
A
656
−13.556
8.647
12.508
1.00
20.19


ATOM
958
CG
ASP
A
656
−14.905
9.353
12.312
1.00
20.24


ATOM
959
OD1
ASP
A
656
−15.243
10.252
13.110
1.00
19.07


ATOM
960
OD2
ASP
A
656
−15.623
9.021
11.344
1.00
19.47


ATOM
961
C
ASP
A
656
−14.197
7.232
14.496
1.00
16.50


ATOM
962
O
ASP
A
656
−15.295
7.060
13.971
1.00
16.42


ATOM
963
N
HIS
A
657
−13.777
6.502
15.523
1.00
16.01


ATOM
964
CA
HIS
A
657
−14.627
5.454
16.073
1.00
15.64


ATOM
965
CB
HIS
A
657
−13.902
4.710
17.196
1.00
18.44


ATOM
966
CG
HIS
A
657
−14.585
3.446
17.606
1.00
19.68


ATOM
967
CD2
HIS
A
657
−15.832
3.224
18.080
1.00
15.96


ATOM
968
ND1
HIS
A
657
−13.979
2.209
17.524
1.00
19.05


ATOM
969
CE1
HIS
A
657
−14.825
1.281
17.930
1.00
16.34


ATOM
970
NE2
HIS
A
657
−15.958
1.871
18.271
1.00
21.05


ATOM
971
C
HIS
A
657
−15.893
6.126
16.611
1.00
17.49


ATOM
972
O
HIS
A
657
−15.826
7.093
17.377
1.00
16.58


ATOM
973
N
PRO
A
658
−17.068
5.625
16.216
1.00
19.29


ATOM
974
CD
PRO
A
658
−17.281
4.579
15.199
1.00
17.12


ATOM
975
CA
PRO
A
658
−18.346
6.189
16.659
1.00
19.86


ATOM
976
CB
PRO
A
658
−19.313
5.701
15.595
1.00
16.51


ATOM
977
CG
PRO
A
658
−18.772
4.311
15.313
1.00
15.25


ATOM
978
C
PRO
A
658
−18.789
5.780
18.058
1.00
19.74


ATOM
979
O
PRO
A
658
−19.745
6.335
18.589
1.00
20.03


ATOM
980
N
GLY
A
659
−18.125
4.788
18.639
1.00
16.93


ATOM
981
CA
GLY
A
659
−18.500
4.360
19.972
1.00
18.25


ATOM
982
C
GLY
A
659
−19.458
3.189
20.003
1.00
18.14


ATOM
983
O
GLY
A
659
−19.993
2.857
21.060
1.00
17.96


ATOM
984
N
VAL
A
660
−19.695
2.581
18.844
1.00
19.22


ATOM
985
CA
VAL
A
660
−20.573
1.418
18.749
1.00
20.26


ATOM
986
CB
VAL
A
660
−21.909
1.771
18.060
1.00
19.84


ATOM
987
CG1
VAL
A
660
−22.697
2.730
18.941
1.00
20.64


ATOM
988
CG2
VAL
A
660
−21.655
2.391
16.698
1.00
20.17


ATOM
989
C
VAL
A
660
−19.844
0.334
17.958
1.00
20.35


ATOM
990
O
VAL
A
660
−18.953
0.630
17.160
1.00
20.64


ATOM
991
N
SER
A
661
−20.226
−0.915
18.190
1.00
18.66


ATOM
992
CA
SER
A
661
−19.605
−2.069
17.541
1.00
19.40


ATOM
993
CB
SER
A
661
−20.001
−3.341
18.278
1.00
23.46


ATOM
994
OG
SER
A
661
−21.369
−3.622
18.044
1.00
22.76


ATOM
995
C
SER
A
661
−19.955
−2.260
16.069
1.00
19.19


ATOM
996
O
SER
A
661
−20.857
−1.614
15.539
1.00
19.47


ATOM
997
N
ASN
A
662
−19.237
−3.175
15.421
1.00
20.96


ATOM
998
CA
ASN
A
662
−19.493
−3.489
14.018
1.00
21.17


ATOM
999
CB
ASN
A
662
−18.474
−4.500
13.487
1.00
20.86


ATOM
1000
CG
ASN
A
662
−17.189
−3.844
13.053
1.00
20.37


ATOM
1001
OD1
ASN
A
662
−17.200
−2.702
12.606
1.00
21.25


ATOM
1002
ND2
ASN
A
662
−16.078
−4.566
13.158
1.00
19.75


ATOM
1003
C
ASN
A
662
−20.894
−4.065
13.895
1.00
21.10


ATOM
1004
O
ASN
A
662
−21.651
−3.713
12.985
1.00
21.05


ATOM
1005
N
GLN
A
663
−21.242
−4.941
14.831
1.00
25.13


ATOM
1006
CA
GLN
A
663
−22.556
−5.555
14.836
1.00
26.08


ATOM
1007
CB
GLN
A
663
−22.696
−6.503
16.031
1.00
35.28


ATOM
1008
CG
GLN
A
663
−21.884
−7.790
15.904
1.00
36.63


ATOM
1009
CD
GLN
A
663
−20.381
−7.582
16.043
1.00
36.48


ATOM
1010
OE1
GLN
A
663
−19.588
−8.447
15.665
1.00
36.95


ATOM
1011
NE2
GLN
A
663
−19.983
−6.441
16.600
1.00
36.26


ATOM
1012
C
GLN
A
663
−23.638
−4.480
14.881
1.00
25.84


ATOM
1013
O
GLN
A
663
−24.625
−4.554
14.153
1.00
25.82


ATOM
1014
N
PHE
A
664
−23.451
−3.474
15.730
1.00
24.41


ATOM
1015
CA
PHE
A
664
−24.423
−2.394
15.832
1.00
25.34


ATOM
1016
CB
PHE
A
664
−23.991
−1.391
16.906
1.00
26.39


ATOM
1017
CG
PHE
A
664
−24.932
−0.226
17.069
1.00
27.42


ATOM
1018
CD1
PHE
A
664
−24.841
0.881
16.230
1.00
26.41


ATOM
1019
CD2
PHE
A
664
−25.915
−0.240
18.057
1.00
27.03


ATOM
1020
CE1
PHE
A
664
−25.713
1.963
16.367
1.00
27.10


ATOM
1021
CE2
PHE
A
664
−26.795
0.840
18.202
1.00
27.63


ATOM
1022
CZ
PHE
A
664
−26.687
1.943
17.350
1.00
26.59


ATOM
1023
C
PHE
A
664
−24.577
−1.697
14.476
1.00
25.16


ATOM
1024
O
PHE
A
664
−25.691
−1.485
14.006
1.00
24.58


ATOM
1025
N
LEU
A
665
−23.454
−1.361
13.847
1.00
21.05


ATOM
1026
CA
LEU
A
665
−23.479
−0.698
12.542
1.00
22.93


ATOM
1027
CB
LEU
A
665
−22.058
−0.348
12.104
1.00
22.29


ATOM
1028
CG
LEU
A
665
−21.328
0.745
12.893
1.00
22.66


ATOM
1029
CD1
LEU
A
665
−19.914
0.890
12.347
1.00
22.68


ATOM
1030
CD2
LEU
A
665
−22.069
2.064
12.776
1.00
22.45


ATOM
1031
C
LEU
A
665
−24.147
−1.563
11.471
1.00
22.68


ATOM
1032
O
LEU
A
665
−24.748
−1.053
10.520
1.00
23.83


ATOM
1033
N
ILE
A
666
−24.031
−2.874
11.618
1.00
24.12


ATOM
1034
CA
ILE
A
666
−24.635
−3.794
10.664
1.00
24.57


ATOM
1035
CB
ILE
A
666
−24.023
−5.204
10.785
1.00
26.67


ATOM
1036
CG2
ILE
A
666
−24.819
−6.195
9.951
1.00
26.86


ATOM
1037
CG1
ILE
A
666
−22.559
−5.176
10.340
1.00
25.51


ATOM
1038
CD1
ILE
A
666
−21.811
−6.483
10.553
1.00
26.41


ATOM
1039
C
ILE
A
666
−26.136
−3.880
10.926
1.00
26.29


ATOM
1040
O
ILE
A
666
−26.937
−3.859
9.993
1.00
26.10


ATOM
1041
N
ASN
A
667
−26.511
−3.968
12.197
1.00
31.89


ATOM
1042
CA
ASN
A
667
−27.920
−4.070
12.563
1.00
34.09


ATOM
1043
CB
ASN
A
667
−28.063
−4.437
14.044
1.00
34.18


ATOM
1044
CG
ASN
A
667
−27.511
−5.809
14.355
1.00
33.95


ATOM
1045
OD1
ASN
A
667
−27.608
−6.722
13.538
1.00
34.50


ATOM
1046
ND2
ASN
A
667
−26.939
−5.969
15.544
1.00
34.36


ATOM
1047
C
ASN
A
667
−28.733
−2.816
12.270
1.00
34.67


ATOM
1048
O
ASN
A
667
−29.944
−2.891
12.058
1.00
34.88


ATOM
1049
N
THR
A
668
−28.073
−1.665
12.264
1.00
41.41


ATOM
1050
CA
THR
A
668
−28.755
−0.408
11.993
1.00
41.66


ATOM
1051
CB
THR
A
668
−28.180
0.728
12.851
1.00
34.82


ATOM
1052
OG1
THR
A
668
−26.774
0.855
12.598
1.00
34.37


ATOM
1053
CG2
THR
A
668
−28.404
0.438
14.325
1.00
34.77


ATOM
1054
C
THR
A
668
−28.630
−0.028
10.521
1.00
41.72


ATOM
1055
O
THR
A
668
−29.012
1.070
10.121
1.00
42.66


ATOM
1056
N
ASN
A
669
−28.096
−0.945
9.720
1.00
36.50


ATOM
1057
CA
ASN
A
669
−27.916
−0.715
8.289
1.00
35.43


ATOM
1058
CB
ASN
A
669
−29.271
−0.756
7.581
1.00
39.66


ATOM
1059
CG
ASN
A
669
−29.861
−2.147
7.553
1.00
39.15


ATOM
1060
OD1
ASN
A
669
−29.314
−3.048
6.919
1.00
39.61


ATOM
1061
ND2
ASN
A
669
−30.974
−2.334
8.247
1.00
39.97


ATOM
1062
C
ASN
A
669
−27.217
0.603
8.002
1.00
33.95


ATOM
1063
O
ASN
A
669
−27.676
1.406
7.187
1.00
35.22


ATOM
1064
N
SER
A
670
−26.098
0.816
8.684
1.00
24.12


ATOM
1065
CA
SER
A
670
−25.304
2.020
8.524
1.00
24.45


ATOM
1066
CB
SER
A
670
−24.162
2.032
9.543
1.00
36.85


ATOM
1067
OG
SER
A
670
−23.245
3.081
9.279
1.00
38.12


ATOM
1068
C
SER
A
670
−24.727
2.056
7.120
1.00
22.19


ATOM
1069
O
SER
A
670
−24.529
1.013
6.498
1.00
22.80


ATOM
1070
N
GLU
A
671
−24.461
3.261
6.626
1.00
25.15


ATOM
1071
CA
GLU
A
671
−23.888
3.426
5.299
1.00
25.09


ATOM
1072
CB
GLU
A
671
−23.736
4.911
4.975
1.00
30.03


ATOM
1073
CG
GLU
A
671
−23.322
5.198
3.547
1.00
30.00


ATOM
1074
CD
GLU
A
671
−23.174
6.683
3.277
1.00
30.78


ATOM
1075
OE1
GLU
A
671
−22.113
7.253
3.613
1.00
30.04


ATOM
1076
OE2
GLU
A
671
−24.132
7.283
2.742
1.00
30.29


ATOM
1077
C
GLU
A
671
−22.521
2.757
5.281
1.00
23.99


ATOM
1078
O
GLU
A
671
−22.087
2.222
4.267
1.00
24.80


ATOM
1079
N
LEU
A
672
−21.857
2.786
6.429
1.00
23.33


ATOM
1080
CA
LEU
A
672
−20.533
2.196
6.581
1.00
21.52


ATOM
1081
CB
LEU
A
672
−20.010
2.512
7.984
1.00
30.40


ATOM
1082
CG
LEU
A
672
−18.683
3.260
8.158
1.00
31.15


ATOM
1083
CD1
LEU
A
672
−18.555
4.398
7.164
1.00
30.73


ATOM
1084
CD2
LEU
A
672
−18.603
3.772
9.586
1.00
31.17


ATOM
1085
C
LEU
A
672
−20.561
0.685
6.349
1.00
22.19


ATOM
1086
O
LEU
A
672
−19.688
0.138
5.673
1.00
20.56


ATOM
1087
N
ALA
A
673
−21.565
0.014
6.910
1.00
20.08


ATOM
1088
CA
ALA
A
673
−21.685
−1.434
6.766
1.00
20.23


ATOM
1089
CB
ALA
A
673
−22.827
−1.958
7.639
1.00
23.81


ATOM
1090
C
ALA
A
673
−21.934
−1.794
5.310
1.00
20.27


ATOM
1091
O
ALA
A
673
−21.446
−2.808
4.821
1.00
20.29


ATOM
1092
N
LEU
A
674
−22.714
−0.970
4.620
1.00
18.83


ATOM
1093
CA
LEU
A
674
−22.998
−1.229
3.213
1.00
20.25


ATOM
1094
CB
LEU
A
674
−24.063
−0.265
2.694
1.00
26.85


ATOM
1095
CG
LEU
A
674
−24.330
−0.385
1.189
1.00
27.73


ATOM
1096
CD1
LEU
A
674
−24.803
−1.793
0.849
1.00
27.05


ATOM
1097
CD2
LEU
A
674
−25.364
0.646
0.779
1.00
27.39


ATOM
1098
C
LEU
A
674
−21.740
−1.082
2.363
1.00
18.25


ATOM
1099
O
LEU
A
674
−21.454
−1.915
1.500
1.00
21.42


ATOM
1100
N
MET
A
675
−20.980
−0.027
2.624
1.00
22.09


ATOM
1101
CA
MET
A
675
−19.758
0.244
1.874
1.00
23.03


ATOM
1102
CB
MET
A
675
−19.140
1.562
2.330
1.00
41.71


ATOM
1103
CG
MET
A
675
−20.013
2.771
2.096
1.00
42.43


ATOM
1104
SD
MET
A
675
−19.158
4.258
2.607
1.00
43.58


ATOM
1105
CE
MET
A
675
−18.192
4.598
1.138
1.00
42.87


ATOM
1106
C
MET
A
675
−18.711
−0.848
2.018
1.00
23.59


ATOM
1107
O
MET
A
675
−17.961
−1.130
1.079
1.00
22.39


ATOM
1108
N
TYR
A
676
−18.662
−1.463
3.193
1.00
22.64


ATOM
1109
CA
TYR
A
676
−17.670
−2.495
3.451
1.00
22.20


ATOM
1110
CB
TYR
A
676
−16.894
−2.113
4.717
1.00
21.16


ATOM
1111
CG
TYR
A
676
−16.197
−0.767
4.574
1.00
21.36


ATOM
1112
CD1
TYR
A
676
−16.385
0.249
5.513
1.00
21.19


ATOM
1113
CE1
TYR
A
676
−15.774
1.501
5.352
1.00
20.94


ATOM
1114
CD2
TYR
A
676
−15.378
−0.503
3.475
1.00
20.92


ATOM
1115
CE2
TYR
A
676
−14.760
0.739
3.307
1.00
20.99


ATOM
1116
CZ
TYR
A
676
−14.964
1.734
4.242
1.00
21.41


ATOM
1117
OH
TYR
A
676
−14.374
2.969
4.059
1.00
22.70


ATOM
1118
C
TYR
A
676
−18.206
−3.926
3.531
1.00
23.64


ATOM
1119
O
TYR
A
676
−17.519
−4.824
4.019
1.00
22.37


ATOM
1120
N
ASN
A
677
−19.421
−4.129
3.025
1.00
21.83


ATOM
1121
CA
ASN
A
677
−20.071
−5.444
2.995
1.00
23.13


ATOM
1122
CB
ASN
A
677
−19.487
−6.296
1.861
1.00
56.74


ATOM
1123
CG
ASN
A
677
−18.007
−6.571
2.033
1.00
57.80


ATOM
1124
OD1
ASN
A
677
−17.594
−7.241
2.979
1.00
58.17


ATOM
1125
ND2
ASN
A
677
−17.197
−6.052
1.116
1.00
58.15


ATOM
1126
C
ASN
A
677
−20.019
−6.223
4.311
1.00
22.92


ATOM
1127
O
ASN
A
677
−19.726
−7.425
4.332
1.00
22.51


ATOM
1128
N
ASP
A
678
−20.317
−5.521
5.398
1.00
22.36


ATOM
1129
CA
ASP
A
678
−20.353
−6.096
6.742
1.00
23.31


ATOM
1130
CB
ASP
A
678
−21.461
−7.146
6.843
1.00
24.85


ATOM
1131
CG
ASP
A
678
−22.824
−6.604
6.466
1.00
25.27


ATOM
1132
OD1
ASP
A
678
−23.031
−5.376
6.536
1.00
23.89


ATOM
1133
OD2
ASP
A
678
−23.699
−7.420
6.111
1.00
26.42


ATOM
1134
C
ASP
A
678
−19.070
−6.725
7.261
1.00
21.81


ATOM
1135
O
ASP
A
678
−19.084
−7.336
8.332
1.00
23.49


ATOM
1136
N
GLU
A
679
−17.972
−6.578
6.533
1.00
19.14


ATOM
1137
CA
GLU
A
679
−16.703
−7.166
6.962
1.00
20.71


ATOM
1138
CB
GLU
A
679
−15.988
−7.819
5.778
1.00
46.03


ATOM
1139
CG
GLU
A
679
−16.640
−9.084
5.259
1.00
47.01


ATOM
1140
CD
GLU
A
679
−15.840
−9.724
4.139
1.00
47.28


ATOM
1141
OE1
GLU
A
679
−15.723
−9.106
3.059
1.00
47.36


ATOM
1142
OE2
GLU
A
679
−15.320
−10.841
4.337
1.00
47.19


ATOM
1143
C
GLU
A
679
−15.770
−6.137
7.582
1.00
19.51


ATOM
1144
O
GLU
A
679
−15.378
−5.185
6.912
1.00
20.45


ATOM
1145
N
SER
A
680
−15.407
−6.345
8.848
1.00
17.83


ATOM
1146
CA
SER
A
680
−14.505
−5.442
9.574
1.00
17.23


ATOM
1147
CB
SER
A
680
−13.043
−5.747
9.224
1.00
21.15


ATOM
1148
OG
SER
A
680
−12.707
−7.098
9.511
1.00
20.61


ATOM
1149
C
SER
A
680
−14.827
−3.997
9.202
1.00
16.25


ATOM
1150
O
SER
A
680
−13.941
−3.218
8.844
1.00
15.64


ATOM
1151
N
VAL
A
681
−16.108
−3.664
9.309
1.00
18.34


ATOM
1152
CA
VAL
A
681
−16.629
−2.353
8.947
1.00
16.30


ATOM
1153
CB
VAL
A
681
−18.115
−2.245
9.327
1.00
19.28


ATOM
1154
CG1
VAL
A
681
−18.674
−0.895
8.881
1.00
20.72


ATOM
1155
CG2
VAL
A
681
−18.894
−3.397
8.665
1.00
19.24


ATOM
1156
C
VAL
A
681
−15.864
−1.173
9.529
1.00
16.04


ATOM
1157
O
VAL
A
681
−15.356
−0.347
8.790
1.00
17.05


ATOM
1158
N
LEU
A
681A
−15.782
−1.110
10.852
1.00
15.07


ATOM
1159
CA
LEU
A
681A
−15.079
−0.028
11.529
1.00
16.07


ATOM
1160
CB
LEU
A
681A
−15.166
−0.217
13.043
1.00
22.39


ATOM
1161
CG
LEU
A
681A
−16.520
0.073
13.680
1.00
24.40


ATOM
1162
CD1
LEU
A
681A
−16.571
−0.536
15.076
1.00
24.68


ATOM
1163
CD2
LEU
A
681A
−16.732
1.573
13.710
1.00
25.32


ATOM
1164
C
LEU
A
681A
−13.613
0.027
11.125
1.00
15.73


ATOM
1165
O
LEU
A
681A
−13.070
1.089
10.848
1.00
14.66


ATOM
1166
N
GLU
A
682
−12.975
−1.134
11.078
1.00
14.20


ATOM
1167
CA
GLU
A
682
−11.566
−1.181
10.731
1.00
16.26


ATOM
1168
CB
GLU
A
682
−11.042
−2.601
10.954
1.00
17.70


ATOM
1169
CG
GLU
A
682
−11.075
−3.043
12.424
1.00
17.27


ATOM
1170
CD
GLU
A
682
−12.466
−3.381
12.956
1.00
17.63


ATOM
1171
OE1
GLU
A
682
−13.350
−3.778
12.164
1.00
16.51


ATOM
1172
OE2
GLU
A
682
−12.672
−3.273
14.192
1.00
18.25


ATOM
1173
C
GLU
A
682
−11.272
−0.675
9.313
1.00
13.40


ATOM
1174
O
GLU
A
682
−10.257
−0.010
9.088
1.00
16.15


ATOM
1175
N
HIS
A
683
−12.140
−0.983
8.353
1.00
14.40


ATOM
1176
CA
HIS
A
683
−11.943
−0.474
7.001
1.00
15.72


ATOM
1177
CB
HIS
A
683
−12.955
−1.084
6.030
1.00
20.22


ATOM
1178
CG
HIS
A
683
−12.527
−2.406
5.483
1.00
21.36


ATOM
1179
CD2
HIS
A
683
−12.905
−3.667
5.800
1.00
22.11


ATOM
1180
ND1
HIS
A
683
−11.538
−2.529
4.531
1.00
19.70


ATOM
1181
CE1
HIS
A
683
−11.325
−3.810
4.286
1.00
20.00


ATOM
1182
NE2
HIS
A
683
−12.139
−4.520
5.044
1.00
21.26


ATOM
1183
C
HIS
A
683
−12.102
1.046
7.044
1.00
15.07


ATOM
1184
O
HIS
A
683
−11.395
1.772
6.343
1.00
16.13


ATOM
1185
N
HIS
A
684
−13.033
1.519
7.874
1.00
16.25


ATOM
1186
CA
HIS
A
684
−13.258
2.952
8.026
1.00
17.73


ATOM
1187
CB
HIS
A
684
−14.505
3.216
8.878
1.00
19.40


ATOM
1188
CG
HIS
A
684
−14.776
4.670
9.116
1.00
20.37


ATOM
1189
CD2
HIS
A
684
−14.870
5.387
10.261
1.00
19.50


ATOM
1190
ND1
HIS
A
684
−14.982
5.563
8.087
1.00
20.04


ATOM
1191
CE1
HIS
A
684
−15.194
6.766
8.588
1.00
19.05


ATOM
1192
NE2
HIS
A
684
−15.131
6.688
9.903
1.00
18.64


ATOM
1193
C
HIS
A
684
−12.038
3.601
8.677
1.00
17.41


ATOM
1194
O
HIS
A
684
−11.602
4.677
8.248
1.00
17.52


ATOM
1195
N
HIS
A
685
−11.491
2.952
9.704
1.00
16.56


ATOM
1196
CA
HIS
A
685
−10.316
3.481
10.387
1.00
17.88


ATOM
1197
CB
HIS
A
685
−9.886
2.568
11.553
1.00
17.97


ATOM
1198
CG
HIS
A
685
−10.943
2.365
12.599
1.00
17.64


ATOM
1199
CD2
HIS
A
685
−11.311
1.258
13.291
1.00
17.69


ATOM
1200
ND1
HIS
A
685
−11.728
3.392
13.079
1.00
16.45


ATOM
1201
CE1
HIS
A
685
−12.533
2.927
14.020
1.00
18.14


ATOM
1202
NE2
HIS
A
685
−12.299
1.634
14.168
1.00
17.23


ATOM
1203
C
HIS
A
685
−9.178
3.619
9.380
1.00
17.11


ATOM
1204
O
HIS
A
685
−8.482
4.639
9.348
1.00
17.09


ATOM
1205
N
PHE
A
686
−8.984
2.596
8.551
1.00
17.41


ATOM
1206
CA
PHE
A
686
−7.928
2.656
7.551
1.00
17.43


ATOM
1207
CB
PHE
A
686
−7.766
1.325
6.810
1.00
22.00


ATOM
1208
CG
PHE
A
686
−6.738
1.384
5.715
1.00
21.91


ATOM
1209
CD1
PHE
A
686
−5.396
1.591
6.014
1.00
22.44


ATOM
1210
CD2
PHE
A
686
−7.123
1.328
4.379
1.00
22.63


ATOM
1211
CE1
PHE
A
686
−4.449
1.754
4.998
1.00
21.95


ATOM
1212
CE2
PHE
A
686
−6.186
1.487
3.356
1.00
22.74


ATOM
1213
CZ
PHE
A
686
−4.847
1.704
3.668
1.00
23.18


ATOM
1214
C
PHE
A
686
−8.183
3.760
6.531
1.00
18.51


ATOM
1215
O
PHE
A
686
−7.250
4.436
6.104
1.00
18.35


ATOM
1216
N
ASP
A
687
−9.439
3.934
6.130
1.00
17.80


ATOM
1217
CA
ASP
A
687
−9.768
4.974
5.166
1.00
18.73


ATOM
1218
CB
ASP
A
687
−11.262
4.969
4.836
1.00
27.45


ATOM
1219
CG
ASP
A
687
−11.661
6.129
3.932
1.00
29.42


ATOM
1220
OD1
ASP
A
687
−11.162
6.190
2.789
1.00
29.29


ATOM
1221
OD2
ASP
A
687
−12.465
6.984
4.366
1.00
29.84


ATOM
1222
C
ASP
A
687
−9.389
6.329
5.751
1.00
17.84


ATOM
1223
O
ASP
A
687
−8.793
7.164
5.070
1.00
18.06


ATOM
1224
N
GLN
A
688
−9.726
6.534
7.020
1.00
20.35


ATOM
1225
CA
GLN
A
688
−9.412
7.786
7.703
1.00
19.96


ATOM
1226
CB
GLN
A
688
−10.060
7.804
9.085
1.00
24.85


ATOM
1227
CG
GLN
A
688
−11.577
7.795
9.021
1.00
25.62


ATOM
1228
CD
GLN
A
688
−12.120
9.081
8.440
1.00
26.01


ATOM
1229
OE1
GLN
A
688
−12.052
10.129
9.076
1.00
27.97


ATOM
1230
NE2
GLN
A
688
−12.647
9.012
7.221
1.00
27.26


ATOM
1231
C
GLN
A
688
−7.911
7.969
7.831
1.00
20.01


ATOM
1232
O
GLN
A
688
−7.406
9.077
7.689
1.00
19.66


ATOM
1233
N
CYS
A
689
−7.202
6.871
8.091
1.00
18.42


ATOM
1234
CA
CYS
A
689
−5.746
6.902
8.229
1.00
18.66


ATOM
1235
CB
CYS
A
689
−5.224
5.498
8.556
1.00
19.50


ATOM
1236
SG
CYS
A
689
−3.425
5.370
8.637
1.00
16.97


ATOM
1237
C
CYS
A
689
−5.098
7.413
6.942
1.00
18.50


ATOM
1238
O
CYS
A
689
−4.234
8.295
6.977
1.00
19.39


ATOM
1239
N
LEU
A
690
−5.524
6.854
5.812
1.00
19.82


ATOM
1240
CA
LEU
A
690
−5.006
7.235
4.497
1.00
20.55


ATOM
1241
CB
LEU
A
690
−5.556
6.288
3.429
1.00
25.80


ATOM
1242
CG
LEU
A
690
−4.985
6.446
2.017
1.00
26.79


ATOM
1243
CD1
LEU
A
690
−3.507
6.105
2.029
1.00
27.37


ATOM
1244
CD2
LEU
A
690
−5.728
5.535
1.059
1.00
27.51


ATOM
1245
C
LEU
A
690
−5.389
8.678
4.148
1.00
19.76


ATOM
1246
O
LEU
A
690
−4.621
9.401
3.521
1.00
21.37


ATOM
1247
N
MET
A
691
−6.587
9.088
4.549
1.00
21.76


ATOM
1248
CA
MET
A
691
−7.044
10.451
4.285
1.00
21.56


ATOM
1249
CB
MET
A
691
−8.450
10.654
4.851
1.00
39.93


ATOM
1250
CG
MET
A
691
−9.006
12.052
4.633
1.00
40.74


ATOM
1251
SD
MET
A
691
−10.617
12.278
5.400
1.00
42.16


ATOM
1252
CE
MET
A
691
−10.138
12.715
7.088
1.00
40.97


ATOM
1253
C
MET
A
691
−6.079
11.451
4.928
1.00
22.42


ATOM
1254
O
MET
A
691
−5.673
12.435
4.300
1.00
21.69


ATOM
1255
N
ILE
A
692
−5.712
11.200
6.179
1.00
20.61


ATOM
1256
CA
ILE
A
692
−4.799
12.094
6.878
1.00
21.43


ATOM
1257
CB
ILE
A
692
−4.704
11.744
8.385
1.00
23.64


ATOM
1258
CG2
ILE
A
692
−3.670
12.633
9.066
1.00
23.04


ATOM
1259
CG1
ILE
A
692
−6.072
11.921
9.056
1.00
23.49


ATOM
1260
CD1
ILE
A
692
−6.591
13.352
9.054
1.00
25.57


ATOM
1261
C
ILE
A
692
−3.403
12.045
6.252
1.00
22.50


ATOM
1262
O
ILE
A
692
−2.759
13.081
6.084
1.00
22.01


ATOM
1263
N
LEU
A
693
−2.940
10.846
5.901
1.00
24.42


ATOM
1264
CA
LEU
A
693
−1.615
10.689
5.298
1.00
25.47


ATOM
1265
CB
LEU
A
693
−1.288
9.203
5.087
1.00
21.69


ATOM
1266
CG
LEU
A
693
−0.950
8.368
6.333
1.00
21.16


ATOM
1267
CD1
LEU
A
693
−0.945
6.888
5.985
1.00
22.43


ATOM
1268
CD2
LEU
A
693
0.411
8.794
6.887
1.00
21.71


ATOM
1269
C
LEU
A
693
−1.499
11.437
3.972
1.00
25.25


ATOM
1270
O
LEU
A
693
−0.414
11.883
3.601
1.00
26.01


ATOM
1271
N
ASN
A
694
−2.614
11.579
3.261
1.00
23.58


ATOM
1272
CA
ASN
A
694
−2.610
12.284
1.981
1.00
22.99


ATOM
1273
CB
ASN
A
694
−3.613
11.656
1.005
1.00
26.66


ATOM
1274
CG
ASN
A
694
−3.178
10.294
0.514
1.00
26.69


ATOM
1275
OD1
ASN
A
694
−2.009
10.078
0.209
1.00
27.10


ATOM
1276
ND2
ASN
A
694
−4.127
9.369
0.413
1.00
27.29


ATOM
1277
C
ASN
A
694
−2.949
13.763
2.132
1.00
23.59


ATOM
1278
O
ASN
A
694
−2.913
14.508
1.155
1.00
24.38


ATOM
1279
N
SER
A
695
−3.285
14.181
3.348
1.00
24.35


ATOM
1280
CA
SER
A
695
−3.644
15.572
3.596
1.00
24.87


ATOM
1281
CB
SER
A
695
−4.279
15.727
4.980
1.00
30.85


ATOM
1282
OG
SER
A
695
−5.570
15.146
5.009
1.00
31.53


ATOM
1283
C
SER
A
695
−2.431
16.475
3.496
1.00
25.45


ATOM
1284
O
SER
A
695
−1.399
16.213
4.108
1.00
25.07


ATOM
1285
N
PRO
A
696
−2.544
17.558
2.717
1.00
28.09


ATOM
1286
CD
PRO
A
696
−3.728
18.069
2.009
1.00
32.92


ATOM
1287
CA
PRO
A
696
−1.410
18.471
2.579
1.00
28.93


ATOM
1288
CB
PRO
A
696
−1.978
19.603
1.718
1.00
32.61


ATOM
1289
CG
PRO
A
696
−3.460
19.552
1.991
1.00
33.55


ATOM
1290
C
PRO
A
696
−0.900
18.944
3.940
1.00
28.17


ATOM
1291
O
PRO
A
696
−1.686
19.310
4.818
1.00
27.52


ATOM
1292
N
GLY
A
697
0.419
18.913
4.104
1.00
27.38


ATOM
1293
CA
GLY
A
697
1.035
19.336
5.347
1.00
27.26


ATOM
1294
C
GLY
A
697
1.106
18.239
6.391
1.00
27.36


ATOM
1295
O
GLY
A
697
1.688
18.430
7.460
1.00
27.28


ATOM
1296
N
ASN
A
698
0.523
17.084
6.080
1.00
24.05


ATOM
1297
CA
ASN
A
698
0.506
15.951
7.006
1.00
24.41


ATOM
1298
CB
ASN
A
698
−0.937
15.592
7.379
1.00
26.46


ATOM
1299
CG
ASN
A
698
−1.624
16.668
8.190
1.00
26.12


ATOM
1300
OD1
ASN
A
698
−2.038
17.702
7.664
1.00
27.64


ATOM
1301
ND2
ASN
A
698
−1.749
16.428
9.486
1.00
26.42


ATOM
1302
C
ASN
A
698
1.165
14.698
6.436
1.00
24.62


ATOM
1303
O
ASN
A
698
1.157
13.643
7.076
1.00
22.80


ATOM
1304
N
GLN
A
699
1.734
14.812
5.240
1.00
24.05


ATOM
1305
CA
GLN
A
699
2.348
13.669
4.572
1.00
24.71


ATOM
1306
CB
GLN
A
699
2.486
13.982
3.083
1.00
37.81


ATOM
1307
CG
GLN
A
699
1.165
14.399
2.451
1.00
38.52


ATOM
1308
CD
GLN
A
699
1.324
14.910
1.036
1.00
38.73


ATOM
1309
OE1
GLN
A
699
1.768
14.184
0.148
1.00
39.77


ATOM
1310
NE2
GLN
A
699
0.964
16.170
0.819
1.00
38.87


ATOM
1311
C
GLN
A
699
3.687
13.229
5.151
1.00
23.74


ATOM
1312
O
GLN
A
699
4.739
13.494
4.573
1.00
24.82


ATOM
1313
N
ILE
A
700
3.639
12.530
6.284
1.00
23.85


ATOM
1314
CA
ILE
A
700
4.853
12.058
6.938
1.00
23.88


ATOM
1315
CB
ILE
A
700
4.572
11.572
8.374
1.00
25.21


ATOM
1316
CG2
ILE
A
700
4.101
12.736
9.225
1.00
24.98


ATOM
1317
CG1
ILE
A
700
3.528
10.454
8.363
1.00
25.64


ATOM
1318
CD1
ILE
A
700
3.370
9.764
9.699
1.00
25.16


ATOM
1319
C
ILE
A
700
5.550
10.935
6.182
1.00
24.95


ATOM
1320
O
ILE
A
700
6.662
10.540
6.546
1.00
24.94


ATOM
1321
N
LEU
A
701
4.904
10.426
5.135
1.00
25.36


ATOM
1322
CA
LEU
A
701
5.476
9.350
4.327
1.00
25.43


ATOM
1323
CB
LEU
A
701
4.460
8.218
4.146
1.00
25.64


ATOM
1324
CG
LEU
A
701
3.976
7.487
5.401
1.00
25.01


ATOM
1325
CD1
LEU
A
701
2.975
6.403
5.008
1.00
25.21


ATOM
1326
CD2
LEU
A
701
5.161
6.879
6.124
1.00
25.48


ATOM
1327
C
LEU
A
701
5.904
9.859
2.951
1.00
27.13


ATOM
1328
O
LEU
A
701
6.280
9.075
2.082
1.00
26.39


ATOM
1329
N
SER
A
702
5.851
11.172
2.764
1.00
36.40


ATOM
1330
CA
SER
A
702
6.218
11.787
1.488
1.00
38.48


ATOM
1331
CB
SER
A
702
6.077
13.303
1.581
1.00
34.20


ATOM
1332
OG
SER
A
702
7.065
13.837
2.446
1.00
34.77


ATOM
1333
C
SER
A
702
7.639
11.459
1.036
1.00
38.77


ATOM
1334
O
SER
A
702
7.915
11.380
−0.162
1.00
39.14


ATOM
1335
N
GLY
A
703
8.537
11.278
1.997
1.00
37.92


ATOM
1336
CA
GLY
A
703
9.920
10.984
1.673
1.00
37.06


ATOM
1337
C
GLY
A
703
10.242
9.556
1.271
1.00
36.77


ATOM
1338
O
GLY
A
703
11.329
9.293
0.760
1.00
37.21


ATOM
1339
N
LEU
A
704
9.316
8.628
1.493
1.00
28.47


ATOM
1340
CA
LEU
A
704
9.566
7.231
1.138
1.00
27.53


ATOM
1341
CB
LEU
A
704
8.446
6.321
1.655
1.00
29.58


ATOM
1342
CG
LEU
A
704
8.208
6.233
3.161
1.00
30.45


ATOM
1343
CD1
LEU
A
704
7.255
5.088
3.465
1.00
29.64


ATOM
1344
CD2
LEU
A
704
9.510
6.005
3.855
1.00
30.15


ATOM
1345
C
LEU
A
704
9.682
7.037
−0.364
1.00
26.70


ATOM
1346
O
LEU
A
704
9.092
7.783
−1.142
1.00
27.33


ATOM
1347
N
SER
A
705
10.450
6.028
−0.762
1.00
29.04


ATOM
1348
CA
SER
A
705
10.606
5.704
−2.171
1.00
28.79


ATOM
1349
CB
SER
A
705
11.734
4.690
−2.369
1.00
23.35


ATOM
1350
OG
SER
A
705
11.393
3.441
−1.802
1.00
24.99


ATOM
1351
C
SER
A
705
9.275
5.062
−2.540
1.00
29.09


ATOM
1352
O
SER
A
705
8.493
4.712
−1.654
1.00
29.81


ATOM
1353
N
ILE
A
706
9.019
4.894
−3.831
1.00
27.02


ATOM
1354
CA
ILE
A
706
7.764
4.295
−4.268
1.00
26.47


ATOM
1355
CB
ILE
A
706
7.700
4.211
−5.809
1.00
35.41


ATOM
1356
CG2
ILE
A
706
6.441
3.472
−6.241
1.00
36.09


ATOM
1357
CG1
ILE
A
706
7.728
5.622
−6.402
1.00
36.23


ATOM
1358
CD1
ILE
A
706
7.821
5.658
−7.917
1.00
36.02


ATOM
1359
C
ILE
A
706
7.561
2.902
−3.681
1.00
26.18


ATOM
1360
O
ILE
A
706
6.487
2.584
−3.175
1.00
26.02


ATOM
1361
N
GLU
A
707
8.594
2.071
−3.736
1.00
25.11


ATOM
1362
CA
GLU
A
707
8.484
0.720
−3.206
1.00
25.30


ATOM
1363
CB
GLU
A
707
9.725
−0.092
−3.577
1.00
46.28


ATOM
1364
CG
GLU
A
707
9.775
−0.446
−5.051
1.00
47.07


ATOM
1365
CD
GLU
A
707
8.667
−1.406
−5.452
1.00
47.32


ATOM
1366
OE1
GLU
A
707
8.296
−1.422
−6.645
1.00
47.31


ATOM
1367
OE2
GLU
A
707
8.177
−2.153
−4.576
1.00
47.02


ATOM
1368
C
GLU
A
707
8.284
0.730
−1.692
1.00
25.18


ATOM
1369
O
GLU
A
707
7.483
−0.042
−1.164
1.00
24.41


ATOM
1370
N
GLU
A
708
9.005
1.610
−1.002
1.00
23.37


ATOM
1371
CA
GLU
A
708
8.887
1.708
0.448
1.00
24.60


ATOM
1372
CB
GLU
A
708
9.904
2.704
1.011
1.00
30.84


ATOM
1373
CG
GLU
A
708
11.278
2.100
1.265
1.00
31.16


ATOM
1374
CD
GLU
A
708
12.236
3.077
1.921
1.00
31.10


ATOM
1375
OE1
GLU
A
708
13.164
2.615
2.617
1.00
31.36


ATOM
1376
OE2
GLU
A
708
12.073
4.301
1.732
1.00
31.87


ATOM
1377
C
GLU
A
708
7.481
2.138
0.839
1.00
24.78


ATOM
1378
O
GLU
A
708
6.886
1.579
1.768
1.00
23.94


ATOM
1379
N
TYR
A
709
6.961
3.133
0.128
1.00
23.21


ATOM
1380
CA
TYR
A
709
5.619
3.644
0.390
1.00
25.29


ATOM
1381
CB
TYR
A
709
5.295
4.802
−0.550
1.00
27.48


ATOM
1382
CG
TYR
A
709
3.912
5.365
−0.325
1.00
28.20


ATOM
1383
CD1
TYR
A
709
3.654
6.221
0.743
1.00
28.35


ATOM
1384
CE1
TYR
A
709
2.375
6.712
0.980
1.00
28.11


ATOM
1385
CD2
TYR
A
709
2.853
5.011
−1.157
1.00
29.10


ATOM
1386
CE2
TYR
A
709
1.567
5.496
−0.927
1.00
29.20


ATOM
1387
CZ
TYR
A
709
1.337
6.343
0.142
1.00
29.09


ATOM
1388
OH
TYR
A
709
0.065
6.813
0.379
1.00
28.65


ATOM
1389
C
TYR
A
709
4.568
2.549
0.224
1.00
25.53


ATOM
1390
O
TYR
A
709
3.740
2.336
1.111
1.00
24.94


ATOM
1391
N
LYS
A
710
4.602
1.859
−0.915
1.00
25.86


ATOM
1392
CA
LYS
A
710
3.658
0.778
−1.191
1.00
26.20


ATOM
1393
CB
LYS
A
710
3.955
0.144
−2.551
1.00
48.58


ATOM
1394
CG
LYS
A
710
3.417
−1.276
−2.683
1.00
49.43


ATOM
1395
CD
LYS
A
710
3.795
−1.914
−4.008
1.00
49.56


ATOM
1396
CE
LYS
A
710
3.501
−3.408
−3.993
1.00
49.72


ATOM
1397
NZ
LYS
A
710
2.086
−3.707
−3.633
1.00
49.51


ATOM
1398
C
LYS
A
710
3.689
−0.309
−0.123
1.00
25.97


ATOM
1399
O
LYS
A
710
2.640
−0.743
0.356
1.00
25.66


ATOM
1400
N
THR
A
711
4.891
−0.756
0.236
1.00
24.32


ATOM
1401
CA
THR
A
711
5.049
−1.800
1.240
1.00
23.82


ATOM
1402
CB
THR
A
711
6.528
−2.205
1.399
1.00
33.44


ATOM
1403
OG1
THR
A
711
7.030
−2.673
0.141
1.00
33.80


ATOM
1404
CG2
THR
A
711
6.669
−3.307
2.441
1.00
33.11


ATOM
1405
C
THR
A
711
4.523
−1.346
2.596
1.00
23.74


ATOM
1406
O
THR
A
711
3.861
−2.106
3.295
1.00
24.01


ATOM
1407
N
THR
A
712
4.813
−0.100
2.951
1.00
22.39


ATOM
1408
CA
THR
A
712
4.379
0.449
4.227
1.00
21.87


ATOM
1409
CB
THR
A
712
5.003
1.831
4.468
1.00
23.06


ATOM
1410
OG1
THR
A
712
6.432
1.713
4.416
1.00
24.85


ATOM
1411
CG2
THR
A
712
4.604
2.371
5.832
1.00
23.79


ATOM
1412
C
THR
A
712
2.859
0.548
4.330
1.00
21.27


ATOM
1413
O
THR
A
712
2.287
0.150
5.340
1.00
22.87


ATOM
1414
N
LEU
A
713
2.207
1.060
3.291
1.00
23.23


ATOM
1415
CA
LEU
A
713
0.751
1.189
3.314
1.00
22.85


ATOM
1416
CB
LEU
A
713
0.249
1.892
2.049
1.00
31.38


ATOM
1417
CG
LEU
A
713
−0.070
3.382
2.200
1.00
32.26


ATOM
1418
CD1
LEU
A
713
−1.303
3.560
3.082
1.00
32.03


ATOM
1419
CD2
LEU
A
713
1.117
4.106
2.804
1.00
32.84


ATOM
1420
C
LEU
A
713
0.051
−0.154
3.473
1.00
22.64


ATOM
1421
O
LEU
A
713
−0.966
−0.251
4.159
1.00
22.10


ATOM
1422
N
LYS
A
714
0.605
−1.187
2.844
1.00
20.65


ATOM
1423
CA
LYS
A
714
0.054
−2.534
2.919
1.00
20.74


ATOM
1424
CB
LYS
A
714
0.822
−3.457
1.970
1.00
43.81


ATOM
1425
CG
LYS
A
714
0.599
−4.943
2.199
1.00
44.63


ATOM
1426
CD
LYS
A
714
1.492
−5.772
1.278
1.00
44.93


ATOM
1427
CE
LYS
A
714
1.524
−7.235
1.692
1.00
44.98


ATOM
1428
NZ
LYS
A
714
0.178
−7.868
1.647
1.00
44.80


ATOM
1429
C
LYS
A
714
0.165
−3.051
4.348
1.00
19.68


ATOM
1430
O
LYS
A
714
−0.755
−3.693
4.865
1.00
20.74


ATOM
1431
N
ILE
A
715
1.300
−2.777
4.984
1.00
20.42


ATOM
1432
CA
ILE
A
715
1.504
−3.216
6.348
1.00
20.28


ATOM
1433
CB
ILE
A
715
2.950
−2.960
6.818
1.00
24.09


ATOM
1434
CG2
ILE
A
715
3.105
−3.399
8.264
1.00
24.82


ATOM
1435
CG1
ILE
A
715
3.930
−3.718
5.917
1.00
25.35


ATOM
1436
CD1
ILE
A
715
5.381
−3.440
6.231
1.00
24.56


ATOM
1437
C
ILE
A
715
0.539
−2.476
7.257
1.00
19.19


ATOM
1438
O
ILE
A
715
−0.035
−3.073
8.161
1.00
19.49


ATOM
1439
N
ILE
A
716
0.367
−1.180
7.005
1.00
19.27


ATOM
1440
CA
ILE
A
716
−0.546
−0.361
7.800
1.00
18.10


ATOM
1441
CB
ILE
A
716
−0.519
1.112
7.345
1.00
20.08


ATOM
1442
CG2
ILE
A
716
−1.672
1.877
7.984
1.00
20.73


ATOM
1443
CG1
ILE
A
716
0.828
1.743
7.717
1.00
19.90


ATOM
1444
CD1
ILE
A
716
1.027
3.151
7.204
1.00
20.14


ATOM
1445
C
ILE
A
716
−1.977
−0.890
7.705
1.00
16.92


ATOM
1446
O
ILE
A
716
−2.647
−1.066
8.727
1.00
17.86


ATOM
1447
N
LYS
A
717
−2.449
−1.143
6.488
1.00
18.04


ATOM
1448
CA
LYS
A
717
−3.808
−1.656
6.315
1.00
19.57


ATOM
1449
CB
LYS
A
717
−4.150
−1.839
4.834
1.00
22.85


ATOM
1450
CG
LYS
A
717
−5.590
−2.297
4.619
1.00
22.42


ATOM
1451
CD
LYS
A
717
−5.930
−2.486
3.144
1.00
23.58


ATOM
1452
CE
LYS
A
717
−7.357
−2.986
2.980
1.00
22.98


ATOM
1453
NZ
LYS
A
717
−7.730
−3.216
1.552
1.00
24.81


ATOM
1454
C
LYS
A
717
−3.977
−2.985
7.042
1.00
19.43


ATOM
1455
O
LYS
A
717
−4.957
−3.197
7.753
1.00
18.92


ATOM
1456
N
GLN
A
718
−3.024
−3.894
6.870
1.00
19.29


ATOM
1457
CA
GLN
A
718
−3.136
−5.173
7.552
1.00
17.73


ATOM
1458
CB
GLN
A
718
−2.009
−6.099
7.096
1.00
35.14


ATOM
1459
CG
GLN
A
718
−2.134
−6.456
5.621
1.00
35.99


ATOM
1460
CD
GLN
A
718
−0.956
−7.249
5.095
1.00
36.88


ATOM
1461
OE1
GLN
A
718
−0.973
−7.718
3.956
1.00
37.13


ATOM
1462
NE2
GLN
A
718
0.076
−7.396
5.915
1.00
36.21


ATOM
1463
C
GLN
A
718
−3.144
−5.031
9.073
1.00
16.21


ATOM
1464
O
GLN
A
718
−3.899
−5.725
9.764
1.00
16.17


ATOM
1465
N
ALA
A
719
−2.326
−4.117
9.585
1.00
17.17


ATOM
1466
CA
ALA
A
719
−2.236
−3.886
11.020
1.00
16.40


ATOM
1467
CB
ALA
A
719
−1.062
−2.939
11.335
1.00
18.08


ATOM
1468
C
ALA
A
719
−3.542
−3.325
11.577
1.00
15.71


ATOM
1469
O
ALA
A
719
−3.996
−3.754
12.637
1.00
15.47


ATOM
1470
N
ILE
A
720
−4.150
−2.380
10.864
1.00
15.28


ATOM
1471
CA
ILE
A
720
−5.402
−1.802
11.330
1.00
17.34


ATOM
1472
CB
ILE
A
720
−5.758
−0.520
10.525
1.00
16.58


ATOM
1473
CG2
ILE
A
720
−7.185
−0.054
10.855
1.00
17.16


ATOM
1474
CG1
ILE
A
720
−4.736
0.570
10.852
1.00
17.26


ATOM
1475
CD1
ILE
A
720
−5.042
1.931
10.241
1.00
17.39


ATOM
1476
C
ILE
A
720
−6.516
−2.847
11.257
1.00
14.75


ATOM
1477
O
ILE
A
720
−7.288
−3.002
12.199
1.00
16.06


ATOM
1478
N
LEU
A
721
−6.583
−3.605
10.165
1.00
16.72


ATOM
1479
CA
LEU
A
721
−7.617
−4.629
10.070
1.00
17.03


ATOM
1480
CB
LEU
A
721
−7.616
−5.282
8.684
1.00
21.51


ATOM
1481
CG
LEU
A
721
−8.136
−4.398
7.544
1.00
22.77


ATOM
1482
CD1
LEU
A
721
−8.089
−5.164
6.236
1.00
22.53


ATOM
1483
CD2
LEU
A
721
−9.556
−3.947
7.834
1.00
22.98


ATOM
1484
C
LEU
A
721
−7.442
−5.694
11.148
1.00
15.19


ATOM
1485
O
LEU
A
721
−8.416
−6.269
11.624
1.00
16.45


ATOM
1486
N
ALA
A
722
−6.199
−5.940
11.546
1.00
17.48


ATOM
1487
CA
ALA
A
722
−5.924
−6.935
12.571
1.00
17.80


ATOM
1488
CB
ALA
A
722
−4.431
−7.113
12.735
1.00
18.14


ATOM
1489
C
ALA
A
722
−6.547
−6.557
13.905
1.00
18.00


ATOM
1490
O
ALA
A
722
−6.764
−7.420
14.750
1.00
18.41


ATOM
1491
N
THR
A
723
−6.854
−5.274
14.094
1.00
15.61


ATOM
1492
CA
THR
A
723
−7.434
−4.856
15.359
1.00
15.90


ATOM
1493
CB
THR
A
723
−7.199
−3.360
15.650
1.00
16.83


ATOM
1494
OG1
THR
A
723
−7.801
−2.550
14.635
1.00
17.34


ATOM
1495
CG2
THR
A
723
−5.701
−3.084
15.726
1.00
18.33


ATOM
1496
C
THR
A
723
−8.909
−5.192
15.499
1.00
16.50


ATOM
1497
O
THR
A
723
−9.542
−4.838
16.492
1.00
17.29


ATOM
1498
N
ASP
A
724
−9.452
−5.875
14.498
1.00
17.56


ATOM
1499
CA
ASP
A
724
−10.826
−6.342
14.549
1.00
18.40


ATOM
1500
CB
ASP
A
724
−11.304
−6.762
13.157
1.00
16.11


ATOM
1501
CG
ASP
A
724
−12.737
−7.273
13.160
1.00
14.99


ATOM
1502
OD1
ASP
A
724
−13.297
−7.492
14.254
1.00
16.02


ATOM
1503
OD2
ASP
A
724
−13.310
−7.458
12.069
1.00
18.73


ATOM
1504
C
ASP
A
724
−10.707
−7.582
15.431
1.00
18.02


ATOM
1505
O
ASP
A
724
−10.114
−8.571
15.006
1.00
18.53


ATOM
1506
N
LEU
A
725
−11.242
−7.536
16.649
1.00
20.52


ATOM
1507
CA
LEU
A
725
−11.140
−8.685
17.545
1.00
21.37


ATOM
1508
CB
LEU
A
725
−11.851
−8.407
18.873
1.00
31.10


ATOM
1509
CG
LEU
A
725
−10.960
−7.911
20.016
1.00
32.17


ATOM
1510
CD1
LEU
A
725
−11.782
−7.798
21.293
1.00
32.32


ATOM
1511
CD2
LEU
A
725
−9.809
−8.885
20.232
1.00
31.61


ATOM
1512
C
LEU
A
725
−11.673
−9.981
16.942
1.00
22.61


ATOM
1513
O
LEU
A
725
−11.229
−11.061
17.316
1.00
22.86


ATOM
1514
N
ALA
A
726
−12.613
−9.887
16.006
1.00
24.20


ATOM
1515
CA
ALA
A
726
−13.158
−11.095
15.376
1.00
26.25


ATOM
1516
CB
ALA
A
726
−14.375
−10.746
14.520
1.00
26.36


ATOM
1517
C
ALA
A
726
−12.093
−11.782
14.520
1.00
25.26


ATOM
1518
O
ALA
A
726
−12.043
−13.015
14.431
1.00
26.23


ATOM
1519
N
LEU
A
727
−11.253
−10.981
13.879
1.00
25.84


ATOM
1520
CA
LEU
A
727
−10.183
−11.497
13.037
1.00
27.01


ATOM
1521
CB
LEU
A
727
−9.582
−10.354
12.217
1.00
27.22


ATOM
1522
CG
LEU
A
727
−9.355
−10.566
10.718
1.00
29.26


ATOM
1523
CD1
LEU
A
727
−10.607
−11.167
10.073
1.00
27.54


ATOM
1524
CD2
LEU
A
727
−9.011
−9.229
10.069
1.00
28.24


ATOM
1525
C
LEU
A
727
−9.123
−12.118
13.946
1.00
26.83


ATOM
1526
O
LEU
A
727
−8.441
−13.077
13.575
1.00
27.75


ATOM
1527
N
TYR
A
728
−8.982
−11.566
15.144
1.00
23.72


ATOM
1528
CA
TYR
A
728
−8.013
−12.096
16.094
1.00
24.54


ATOM
1529
CB
TYR
A
728
−7.843
−11.144
17.280
1.00
26.68


ATOM
1530
CG
TYR
A
728
−7.128
−11.784
18.440
1.00
27.14


ATOM
1531
CD1
TYR
A
728
−7.828
−12.208
19.568
1.00
27.32


ATOM
1532
CE1
TYR
A
728
−7.183
−12.878
20.602
1.00
27.41


ATOM
1533
CD2
TYR
A
728
−5.762
−12.040
18.377
1.00
27.43


ATOM
1534
CE2
TYR
A
728
−5.111
−12.709
19.400
1.00
27.27


ATOM
1535
CZ
TYR
A
728
−5.825
−13.126
20.505
1.00
27.40


ATOM
1536
OH
TYR
A
728
−5.178
−13.810
21.507
1.00
28.59


ATOM
1537
C
TYR
A
728
−8.483
−13.462
16.593
1.00
24.46


ATOM
1538
O
TYR
A
728
−7.713
−14.425
16.643
1.00
24.91


ATOM
1539
N
ILE
A
729
−9.753
−13.536
16.968
1.00
25.84


ATOM
1540
CA
ILE
A
729
−10.335
−14.779
17.463
1.00
26.31


ATOM
1541
CB
ILE
A
729
−11.803
−14.555
17.876
1.00
28.61


ATOM
1542
CG2
ILE
A
729
−12.482
−15.887
18.155
1.00
28.30


ATOM
1543
CG1
ILE
A
729
−11.855
−13.646
19.106
1.00
27.91


ATOM
1544
CD1
ILE
A
729
−13.251
−13.165
19.462
1.00
28.85


ATOM
1545
C
ILE
A
729
−10.265
−15.874
16.401
1.00
28.18


ATOM
1546
O
ILE
A
729
−10.162
−17.061
16.727
1.00
28.43


ATOM
1547
N
LYS
A
730
−10.304
−15.469
15.135
1.00
32.05


ATOM
1548
CA
LYS
A
730
−10.265
−16.402
14.008
1.00
33.23


ATOM
1549
CB
LYS
A
730
−10.833
−15.714
12.758
1.00
40.71


ATOM
1550
CG
LYS
A
730
−10.709
−16.526
11.475
1.00
40.87


ATOM
1551
CD
LYS
A
730
−11.146
−15.727
10.251
1.00
40.83


ATOM
1552
CE
LYS
A
730
−11.013
−16.555
8.977
1.00
41.35


ATOM
1553
NZ
LYS
A
730
−11.478
−15.810
7.772
1.00
41.21


ATOM
1554
C
LYS
A
730
−8.865
−16.938
13.697
1.00
33.75


ATOM
1555
O
LYS
A
730
−8.688
−18.137
13.457
1.00
33.39


ATOM
1556
N
ARG
A
731
−7.876
−16.050
13.703
1.00
31.85


ATOM
1557
CA
ARG
A
731
−6.503
−16.428
13.380
1.00
31.83


ATOM
1558
CB
ARG
A
731
−5.825
−15.293
12.604
1.00
43.64


ATOM
1559
CG
ARG
A
731
−6.375
−15.070
11.205
1.00
44.14


ATOM
1560
CD
ARG
A
731
−5.975
−13.707
10.644
1.00
44.16


ATOM
1561
NE
ARG
A
731
−4.534
−13.536
10.456
1.00
44.52


ATOM
1562
CZ
ARG
A
731
−3.809
−14.173
9.541
1.00
44.27


ATOM
1563
NH1
ARG
A
731
−4.383
−15.039
8.716
1.00
44.55


ATOM
1564
NH2
ARG
A
731
−2.507
−13.933
9.440
1.00
44.01


ATOM
1565
C
ARG
A
731
−5.603
−16.813
14.549
1.00
31.39


ATOM
1566
O
ARG
A
731
−4.510
−17.339
14.333
1.00
31.88


ATOM
1567
N
ARG
A
732
−6.040
−16.566
15.780
1.00
27.33


ATOM
1568
CA
ARG
A
732
−5.189
−16.880
16.923
1.00
27.09


ATOM
1569
CB
ARG
A
732
−5.783
−16.315
18.218
1.00
27.95


ATOM
1570
CG
ARG
A
732
−7.063
−16.972
18.680
1.00
27.63


ATOM
1571
CD
ARG
A
732
−7.423
−16.469
20.056
1.00
27.47


ATOM
1572
NE
ARG
A
732
−8.557
−17.178
20.632
1.00
27.81


ATOM
1573
CZ
ARG
A
732
−8.915
−17.083
21.907
1.00
28.15


ATOM
1574
NH1
ARG
A
732
−8.225
−16.308
22.735
1.00
28.26


ATOM
1575
NH2
ARG
A
732
−9.955
−17.772
22.358
1.00
29.20


ATOM
1576
C
ARG
A
732
−4.928
−18.372
17.086
1.00
26.60


ATOM
1577
O
ARG
A
732
−3.853
−18.767
17.524
1.00
26.91


ATOM
1578
N
GLY
A
733
−5.909
−19.195
16.733
1.00
28.21


ATOM
1579
CA
GLY
A
733
−5.741
−20.633
16.860
1.00
28.94


ATOM
1580
C
GLY
A
733
−4.533
−21.138
16.097
1.00
28.70


ATOM
1581
O
GLY
A
733
−3.785
−21.991
16.582
1.00
29.01


ATOM
1582
N
GLU
A
734
−4.344
−20.609
14.895
1.00
26.13


ATOM
1583
CA
GLU
A
734
−3.224
−20.999
14.049
1.00
26.64


ATOM
1584
CB
GLU
A
734
−3.257
−20.213
12.741
1.00
32.54


ATOM
1585
CG
GLU
A
734
−2.289
−20.720
11.697
1.00
32.73


ATOM
1586
CD
GLU
A
734
−2.261
−19.855
10.458
1.00
32.93


ATOM
1587
OE1
GLU
A
734
−3.330
−19.331
10.068
1.00
32.62


ATOM
1588
OE2
GLU
A
734
−1.168
−19.713
9.867
1.00
33.12


ATOM
1589
C
GLU
A
734
−1.927
−20.705
14.783
1.00
26.89


ATOM
1590
O
GLU
A
734
−1.071
−21.571
14.935
1.00
26.89


ATOM
1591
N
PHE
A
735
−1.797
−19.463
15.233
1.00
26.37


ATOM
1592
CA
PHE
A
735
−0.630
−18.996
15.965
1.00
26.70


ATOM
1593
CB
PHE
A
735
−0.911
−17.569
16.455
1.00
35.10


ATOM
1594
CG
PHE
A
735
0.263
−16.884
17.099
1.00
35.60


ATOM
1595
CD1
PHE
A
735
1.487
−16.801
16.448
1.00
35.44


ATOM
1596
CD2
PHE
A
735
0.116
−16.256
18.333
1.00
35.57


ATOM
1597
CE1
PHE
A
735
2.549
−16.098
17.013
1.00
35.65


ATOM
1598
CE2
PHE
A
735
1.168
−15.550
18.909
1.00
35.48


ATOM
1599
CZ
PHE
A
735
2.388
−15.469
18.247
1.00
35.90


ATOM
1600
C
PHE
A
735
−0.309
−19.919
17.148
1.00
26.06


ATOM
1601
O
PHE
A
735
0.819
−20.387
17.297
1.00
26.34


ATOM
1602
N
PHE
A
736
−1.313
−20.186
17.978
1.00
27.83


ATOM
1603
CA
PHE
A
736
−1.144
−21.049
19.146
1.00
27.77


ATOM
1604
CB
PHE
A
736
−2.462
−21.134
19.925
1.00
26.06


ATOM
1605
CG
PHE
A
736
−2.927
−19.810
20.492
1.00
26.21


ATOM
1606
CD1
PHE
A
736
−4.239
−19.659
20.948
1.00
25.79


ATOM
1607
CD2
PHE
A
736
−2.059
−18.727
20.587
1.00
25.60


ATOM
1608
CE1
PHE
A
736
−4.676
−18.450
21.489
1.00
25.76


ATOM
1609
CE2
PHE
A
736
−2.490
−17.508
21.130
1.00
25.65


ATOM
1610
CZ
PHE
A
736
−3.801
−17.376
21.580
1.00
25.15


ATOM
1611
C
PHE
A
736
−0.692
−22.453
18.737
1.00
27.64


ATOM
1612
O
PHE
A
736
0.212
−23.020
19.352
1.00
28.68


ATOM
1613
N
GLU
A
737
−1.335
−23.001
17.709
1.00
26.38


ATOM
1614
CA
GLU
A
737
−1.015
−24.335
17.187
1.00
26.87


ATOM
1615
CB
GLU
A
737
−1.860
−24.633
15.943
1.00
54.89


ATOM
1616
CG
GLU
A
737
−3.324
−24.925
16.215
1.00
55.77


ATOM
1617
CD
GLU
A
737
−3.541
−26.319
16.765
1.00
56.24


ATOM
1618
OE1
GLU
A
737
−3.171
−27.293
16.074
1.00
56.16


ATOM
1619
OE2
GLU
A
737
−4.081
−26.440
17.885
1.00
55.95


ATOM
1620
C
GLU
A
737
0.458
−24.431
16.809
1.00
26.60


ATOM
1621
O
GLU
A
737
1.158
−25.385
17.181
1.00
24.87


ATOM
1622
N
LEU
A
738
0.919
−23.446
16.047
1.00
24.73


ATOM
1623
CA
LEU
A
738
2.304
−23.402
15.603
1.00
25.81


ATOM
1624
CB
LEU
A
738
2.558
−22.131
14.790
1.00
23.18


ATOM
1625
CG
LEU
A
738
2.098
−22.127
13.326
1.00
24.63


ATOM
1626
CD1
LEU
A
738
0.728
−22.761
13.172
1.00
25.88


ATOM
1627
CD2
LEU
A
738
2.093
−20.699
12.816
1.00
24.42


ATOM
1628
C
LEU
A
738
3.271
−23.459
16.771
1.00
25.22


ATOM
1629
O
LEU
A
738
4.259
−24.190
16.730
1.00
26.20


ATOM
1630
N
ILE
A
739
2.992
−22.676
17.809
1.00
22.89


ATOM
1631
CA
ILE
A
739
3.851
−22.643
18.983
1.00
23.09


ATOM
1632
CB
ILE
A
739
3.406
−21.531
19.961
1.00
29.33


ATOM
1633
CG2
ILE
A
739
4.227
−21.594
21.237
1.00
29.45


ATOM
1634
CG1
ILE
A
739
3.554
−20.161
19.293
1.00
29.28


ATOM
1635
CD1
ILE
A
739
4.978
−19.789
18.968
1.00
29.71


ATOM
1636
C
ILE
A
739
3.850
−23.981
19.717
1.00
23.52


ATOM
1637
O
ILE
A
739
4.904
−24.513
20.040
1.00
24.40


ATOM
1638
N
ARG
A
740
2.665
−24.523
19.971
1.00
25.73


ATOM
1639
CA
ARG
A
740
2.545
−25.790
20.683
1.00
27.35


ATOM
1640
CB
ARG
A
740
1.070
−26.135
20.897
1.00
48.66


ATOM
1641
CG
ARG
A
740
0.840
−27.418
21.679
1.00
49.28


ATOM
1642
CD
ARG
A
740
−0.625
−27.566
22.043
1.00
49.58


ATOM
1643
NE
ARG
A
740
−1.484
−27.521
20.863
1.00
49.67


ATOM
1644
CZ
ARG
A
740
−1.504
−28.454
19.916
1.00
49.81


ATOM
1645
NH1
ARG
A
740
−0.709
−29.514
20.008
1.00
50.00


ATOM
1646
NH2
ARG
A
740
−2.317
−28.330
18.876
1.00
49.79


ATOM
1647
C
ARG
A
740
3.241
−26.950
19.975
1.00
27.41


ATOM
1648
O
ARG
A
740
3.784
−27.845
20.628
1.00
27.24


ATOM
1649
N
LYS
A
741
3.230
−26.935
18.646
1.00
27.03


ATOM
1650
CA
LYS
A
741
3.863
−27.999
17.874
1.00
27.38


ATOM
1651
CB
LYS
A
741
3.055
−28.279
16.605
1.00
33.72


ATOM
1652
CG
LYS
A
741
1.670
−28.843
16.885
1.00
34.15


ATOM
1653
CD
LYS
A
741
0.952
−29.259
15.614
1.00
34.24


ATOM
1654
CE
LYS
A
741
−0.401
−29.874
15.943
1.00
34.27


ATOM
1655
NZ
LYS
A
741
−1.166
−30.255
14.726
1.00
34.95


ATOM
1656
C
LYS
A
741
5.315
−27.692
17.511
1.00
27.29


ATOM
1657
O
LYS
A
741
5.937
−28.430
16.745
1.00
28.07


ATOM
1658
N
ASN
A
742
5.854
−26.606
18.061
1.00
25.30


ATOM
1659
CA
ASN
A
742
7.239
−26.224
17.797
1.00
25.09


ATOM
1660
CB
ASN
A
742
8.189
−27.297
18.332
1.00
29.88


ATOM
1661
CG
ASN
A
742
8.202
−27.351
19.837
1.00
30.15


ATOM
1662
OD1
ASN
A
742
8.592
−26.389
20.491
1.00
30.86


ATOM
1663
ND2
ASN
A
742
7.768
−28.474
20.400
1.00
30.30


ATOM
1664
C
ASN
A
742
7.498
−26.005
16.318
1.00
24.75


ATOM
1665
O
ASN
A
742
8.526
−26.431
15.782
1.00
23.22


ATOM
1666
N
GLN
A
743
6.564
−25.319
15.665
1.00
27.53


ATOM
1667
CA
GLN
A
743
6.670
−25.035
14.240
1.00
28.70


ATOM
1668
CB
GLN
A
743
5.451
−25.592
13.495
1.00
37.55


ATOM
1669
CG
GLN
A
743
5.093
−27.027
13.845
1.00
37.58


ATOM
1670
CD
GLN
A
743
3.960
−27.566
12.992
1.00
38.11


ATOM
1671
OE1
GLN
A
743
2.923
−26.918
12.830
1.00
38.11


ATOM
1672
NE2
GLN
A
743
4.147
−28.763
12.447
1.00
37.75


ATOM
1673
C
GLN
A
743
6.755
−23.533
13.979
1.00
28.82


ATOM
1674
O
GLN
A
743
6.881
−23.105
12.832
1.00
28.92


ATOM
1675
N
PHE
A
744
6.681
−22.729
15.035
1.00
28.91


ATOM
1676
CA
PHE
A
744
6.743
−21.284
14.850
1.00
29.47


ATOM
1677
CB
PHE
A
744
6.432
−20.556
16.157
1.00
40.72


ATOM
1678
CG
PHE
A
744
6.298
−19.064
15.997
1.00
40.67


ATOM
1679
CD1
PHE
A
744
5.279
−18.525
15.214
1.00
41.29


ATOM
1680
CD2
PHE
A
744
7.191
−18.200
16.618
1.00
41.11


ATOM
1681
CE1
PHE
A
744
5.153
−17.145
15.053
1.00
41.25


ATOM
1682
CE2
PHE
A
744
7.074
−16.819
16.464
1.00
41.16


ATOM
1683
CZ
PHE
A
744
6.053
−16.292
15.680
1.00
41.33


ATOM
1684
C
PHE
A
744
8.097
−20.819
14.326
1.00
29.13


ATOM
1685
O
PHE
A
744
9.146
−21.260
14.792
1.00
30.17


ATOM
1686
N
ASN
A
745
8.055
−19.921
13.349
1.00
28.18


ATOM
1687
CA
ASN
A
745
9.260
−19.363
12.750
1.00
29.83


ATOM
1688
CB
ASN
A
745
9.795
−20.272
11.648
1.00
38.97


ATOM
1689
CG
ASN
A
745
10.919
−19.622
10.867
1.00
39.20


ATOM
1690
OD1
ASN
A
745
11.985
−19.348
11.411
1.00
39.54


ATOM
1691
ND2
ASN
A
745
10.679
−19.357
9.590
1.00
40.15


ATOM
1692
C
ASN
A
745
8.941
−18.005
12.149
1.00
29.56


ATOM
1693
O
ASN
A
745
8.208
−17.914
11.165
1.00
29.59


ATOM
1694
N
LEU
A
746
9.499
−16.956
12.741
1.00
38.07


ATOM
1695
CA
LEU
A
746
9.268
−15.597
12.270
1.00
39.23


ATOM
1696
CB
LEU
A
746
9.822
−14.591
13.280
1.00
38.00


ATOM
1697
CG
LEU
A
746
8.967
−14.381
14.528
1.00
37.62


ATOM
1698
CD1
LEU
A
746
9.676
−13.427
15.475
1.00
38.20


ATOM
1699
CD2
LEU
A
746
7.609
−13.821
14.125
1.00
37.68


ATOM
1700
C
LEU
A
746
9.852
−15.302
10.895
1.00
39.66


ATOM
1701
O
LEU
A
746
9.455
−14.335
10.245
1.00
39.51


ATOM
1702
N
GLU
A
747
10.792
−16.128
10.449
1.00
39.64


ATOM
1703
CA
GLU
A
747
11.404
−15.918
9.143
1.00
39.71


ATOM
1704
CB
GLU
A
747
12.605
−16.845
8.965
1.00
45.59


ATOM
1705
CG
GLU
A
747
13.921
−16.094
8.881
1.00
46.56


ATOM
1706
CD
GLU
A
747
15.125
−16.981
9.132
1.00
46.55


ATOM
1707
OE1
GLU
A
747
15.305
−17.974
8.395
1.00
46.54


ATOM
1708
OE2
GLU
A
747
15.890
−16.679
10.072
1.00
46.60


ATOM
1709
C
GLU
A
747
10.391
−16.136
8.029
1.00
38.87


ATOM
1710
O
GLU
A
747
10.422
−15.454
7.002
1.00
39.21


ATOM
1711
N
ASP
A
748
9.487
−17.086
8.234
1.00
32.77


ATOM
1712
CA
ASP
A
748
8.455
−17.363
7.248
1.00
32.31


ATOM
1713
CB
ASP
A
748
7.654
−18.600
7.652
1.00
47.03


ATOM
1714
CG
ASP
A
748
6.639
−19.002
6.603
1.00
47.67


ATOM
1715
OD1
ASP
A
748
5.613
−18.305
6.459
1.00
47.81


ATOM
1716
OD2
ASP
A
748
6.876
−20.018
5.912
1.00
48.36


ATOM
1717
C
ASP
A
748
7.544
−16.141
7.190
1.00
32.61


ATOM
1718
O
ASP
A
748
6.915
−15.777
8.185
1.00
30.88


ATOM
1719
N
PRO
A
749
7.466
−15.490
6.018
1.00
39.12


ATOM
1720
CD
PRO
A
749
8.049
−15.930
4.739
1.00
38.16


ATOM
1721
CA
PRO
A
749
6.634
−14.299
5.824
1.00
39.58


ATOM
1722
CB
PRO
A
749
6.773
−14.021
4.325
1.00
38.14


ATOM
1723
CG
PRO
A
749
7.069
−15.367
3.745
1.00
38.10


ATOM
1724
C
PRO
A
749
5.176
−14.417
6.274
1.00
39.62


ATOM
1725
O
PRO
A
749
4.601
−13.447
6.770
1.00
39.95


ATOM
1726
N
HIS
A
750
4.571
−15.588
6.108
1.00
32.50


ATOM
1727
CA
HIS
A
750
3.181
−15.742
6.524
1.00
31.88


ATOM
1728
CB
HIS
A
750
2.562
−17.016
5.946
1.00
30.66


ATOM
1729
CG
HIS
A
750
1.149
−17.240
6.384
1.00
30.76


ATOM
1730
CD2
HIS
A
750
−0.008
−16.667
5.981
1.00
30.83


ATOM
1731
ND1
HIS
A
750
0.815
−18.097
7.410
1.00
31.54


ATOM
1732
CE1
HIS
A
750
−0.488
−18.041
7.621
1.00
31.23


ATOM
1733
NE2
HIS
A
750
−1.011
−17.180
6.768
1.00
31.56


ATOM
1734
C
HIS
A
750
3.055
−15.761
8.042
1.00
31.66


ATOM
1735
O
HIS
A
750
2.146
−15.148
8.604
1.00
31.17


ATOM
1736
N
GLU
A
751
3.957
−16.470
8.711
1.00
31.26


ATOM
1737
CA
GLU
A
751
3.913
−16.519
10.165
1.00
31.20


ATOM
1738
CB
GLU
A
751
4.898
−17.563
10.703
1.00
33.16


ATOM
1739
CG
GLU
A
751
4.444
−19.000
10.455
1.00
33.17


ATOM
1740
CD
GLU
A
751
5.215
−20.017
11.274
1.00
33.56


ATOM
1741
OE1
GLU
A
751
5.432
−19.772
12.478
1.00
33.10


ATOM
1742
OE2
GLU
A
751
5.587
−21.071
10.720
1.00
33.79


ATOM
1743
C
GLU
A
751
4.247
−15.127
10.699
1.00
31.23


ATOM
1744
O
GLU
A
751
3.836
−14.753
11.800
1.00
31.00


ATOM
1745
N
LYS
A
752
4.979
−14.364
9.892
1.00
29.23


ATOM
1746
CA
LYS
A
752
5.372
−13.008
10.239
1.00
29.88


ATOM
1747
CB
LYS
A
752
6.292
−12.439
9.154
1.00
37.79


ATOM
1748
CG
LYS
A
752
6.867
−11.058
9.453
1.00
38.37


ATOM
1749
CD
LYS
A
752
7.766
−11.087
10.684
1.00
38.41


ATOM
1750
CE
LYS
A
752
8.526
−9.783
10.861
1.00
38.61


ATOM
1751
NZ
LYS
A
752
9.473
−9.521
9.748
1.00
38.19


ATOM
1752
C
LYS
A
752
4.143
−12.120
10.373
1.00
29.16


ATOM
1753
O
LYS
A
752
3.921
−11.510
11.425
1.00
29.42


ATOM
1754
N
GLU
A
753
3.341
−12.029
9.315
1.00
30.11


ATOM
1755
CA
GLU
A
753
2.156
−11.191
9.402
1.00
30.60


ATOM
1756
CB
GLU
A
753
1.467
−11.040
8.038
1.00
54.85


ATOM
1757
CG
GLU
A
753
1.100
−12.316
7.315
1.00
55.61


ATOM
1758
CD
GLU
A
753
0.501
−12.034
5.942
1.00
55.82


ATOM
1759
OE1
GLU
A
753
1.195
−11.420
5.102
1.00
55.58


ATOM
1760
OE2
GLU
A
753
−0.663
−12.420
5.705
1.00
55.80


ATOM
1761
C
GLU
A
753
1.201
−11.736
10.458
1.00
29.96


ATOM
1762
O
GLU
A
753
0.476
−10.973
11.094
1.00
30.36


ATOM
1763
N
LEU
A
754
1.215
−13.050
10.668
1.00
25.09


ATOM
1764
CA
LEU
A
754
0.364
−13.638
11.695
1.00
23.83


ATOM
1765
CB
LEU
A
754
0.510
−15.160
11.719
1.00
25.34


ATOM
1766
CG
LEU
A
754
−0.242
−15.857
12.852
1.00
26.46


ATOM
1767
CD1
LEU
A
754
−1.730
−15.558
12.759
1.00
25.32


ATOM
1768
CD2
LEU
A
754
0.010
−17.364
12.767
1.00
25.75


ATOM
1769
C
LEU
A
754
0.812
−13.064
13.039
1.00
23.90


ATOM
1770
O
LEU
A
754
−0.011
−12.728
13.896
1.00
24.10


ATOM
1771
N
PHE
A
755
2.126
−12.953
13.215
1.00
22.27


ATOM
1772
CA
PHE
A
755
2.673
−12.405
14.444
1.00
23.27


ATOM
1773
CB
PHE
A
755
4.188
−12.601
14.506
1.00
27.67


ATOM
1774
CG
PHE
A
755
4.811
−11.977
15.715
1.00
27.49


ATOM
1775
CD1
PHE
A
755
4.559
−12.492
16.981
1.00
27.28


ATOM
1776
CD2
PHE
A
755
5.589
−10.834
15.596
1.00
26.66


ATOM
1777
CE1
PHE
A
755
5.070
−11.872
18.117
1.00
28.85


ATOM
1778
CE2
PHE
A
755
6.108
−10.200
16.727
1.00
27.67


ATOM
1779
CZ
PHE
A
755
5.849
−10.718
17.987
1.00
27.51


ATOM
1780
C
PHE
A
755
2.352
−10.914
14.590
1.00
23.26


ATOM
1781
O
PHE
A
755
1.932
−10.469
15.665
1.00
22.65


ATOM
1782
N
LEU
A
756
2.553
−10.148
13.520
1.00
21.99


ATOM
1783
CA
LEU
A
756
2.274
−8.712
13.552
1.00
23.22


ATOM
1784
CB
LEU
A
756
2.593
−8.059
12.206
1.00
24.32


ATOM
1785
CG
LEU
A
756
4.060
−7.993
11.785
1.00
25.68


ATOM
1786
CD1
LEU
A
756
4.163
−7.476
10.364
1.00
24.86


ATOM
1787
CD2
LEU
A
756
4.821
−7.094
12.737
1.00
25.84


ATOM
1788
C
LEU
A
756
0.820
−8.435
13.906
1.00
22.88


ATOM
1789
O
LEU
A
756
0.520
−7.441
14.561
1.00
22.05


ATOM
1790
N
ALA
A
757
−0.078
−9.316
13.477
1.00
22.97


ATOM
1791
CA
ALA
A
757
−1.498
−9.152
13.770
1.00
22.24


ATOM
1792
CB
ALA
A
757
−2.326
−10.143
12.950
1.00
21.11


ATOM
1793
C
ALA
A
757
−1.733
−9.387
15.255
1.00
23.73


ATOM
1794
O
ALA
A
757
−2.491
−8.668
15.907
1.00
22.64


ATOM
1795
N
MET
A
758
−1.080
−10.407
15.794
1.00
17.51


ATOM
1796
CA
MET
A
758
−1.234
−10.717
17.198
1.00
18.28


ATOM
1797
CB
MET
A
758
−0.581
−12.072
17.503
1.00
27.85


ATOM
1798
CG
MET
A
758
−1.181
−13.255
16.720
1.00
27.03


ATOM
1799
SD
MET
A
758
−2.826
−13.794
17.241
1.00
29.72


ATOM
1800
CE
MET
A
758
−3.778
−13.473
15.747
1.00
28.03


ATOM
1801
C
MET
A
758
−0.608
−9.605
18.039
1.00
17.15


ATOM
1802
O
MET
A
758
−1.088
−9.319
19.137
1.00
18.07


ATOM
1803
N
LEU
A
759
0.447
−8.979
17.515
1.00
17.47


ATOM
1804
CA
LEU
A
759
1.139
−7.898
18.225
1.00
19.04


ATOM
1805
CB
LEU
A
759
2.418
−7.482
17.491
1.00
19.37


ATOM
1806
CG
LEU
A
759
3.214
−6.328
18.112
1.00
20.18


ATOM
1807
CD1
LEU
A
759
3.610
−6.669
19.550
1.00
21.45


ATOM
1808
CD2
LEU
A
759
4.439
−6.039
17.261
1.00
21.48


ATOM
1809
C
LEU
A
759
0.213
−6.699
18.342
1.00
19.95


ATOM
1810
O
LEU
A
759
0.119
−6.081
19.406
1.00
18.11


ATOM
1811
N
MET
A
760
−0.454
−6.367
17.240
1.00
17.24


ATOM
1812
CA
MET
A
760
−1.393
−5.240
17.251
1.00
17.90


ATOM
1813
CB
MET
A
760
−2.032
−5.063
15.874
1.00
18.91


ATOM
1814
CG
MET
A
760
−1.140
−4.422
14.835
1.00
19.09


ATOM
1815
SD
MET
A
760
−0.717
−2.696
15.216
1.00
18.56


ATOM
1816
CE
MET
A
760
−2.370
−1.939
15.227
1.00
17.91


ATOM
1817
C
MET
A
760
−2.468
−5.487
18.302
1.00
18.32


ATOM
1818
O
MET
A
760
−2.808
−4.590
19.072
1.00
15.93


ATOM
1819
N
THR
A
761
−3.002
−6.706
18.350
1.00
17.94


ATOM
1820
CA
THR
A
761
−4.024
−7.021
19.336
1.00
17.15


ATOM
1821
CB
THR
A
761
−4.540
−8.454
19.164
1.00
18.32


ATOM
1822
OG1
THR
A
761
−5.103
−8.594
17.856
1.00
18.56


ATOM
1823
CG2
THR
A
761
−5.594
−8.772
20.220
1.00
17.55


ATOM
1824
C
THR
A
761
−3.446
−6.880
20.746
1.00
17.99


ATOM
1825
O
THR
A
761
−4.089
−6.332
21.635
1.00
19.05


ATOM
1826
N
ALA
A
762
−2.228
−7.381
20.946
1.00
16.64


ATOM
1827
CA
ALA
A
762
−1.590
−7.298
22.255
1.00
16.82


ATOM
1828
CB
ALA
A
762
−0.194
−7.908
22.202
1.00
19.67


ATOM
1829
C
ALA
A
762
−1.514
−5.854
22.755
1.00
18.11


ATOM
1830
O
ALA
A
762
−1.766
−5.585
23.933
1.00
16.84


ATOM
1831
N
CYS
A
763
−1.169
−4.936
21.860
1.00
15.07


ATOM
1832
CA
CYS
A
763
−1.081
−3.523
22.216
1.00
16.86


ATOM
1833
CB
CYS
A
763
−0.303
−2.767
21.147
1.00
16.42


ATOM
1834
SG
CYS
A
763
1.450
−3.220
21.036
1.00
16.68


ATOM
1835
C
CYS
A
763
−2.469
−2.904
22.372
1.00
18.36


ATOM
1836
O
CYS
A
763
−2.705
−2.091
23.269
1.00
15.92


ATOM
1837
N
ASP
A
764
−3.385
−3.289
21.494
1.00
17.47


ATOM
1838
CA
ASP
A
764
−4.743
−2.766
21.528
1.00
18.98


ATOM
1839
CB
ASP
A
764
−5.539
−3.360
20.360
1.00
18.28


ATOM
1840
CG
ASP
A
764
−6.834
−2.624
20.089
1.00
19.27


ATOM
1841
OD1
ASP
A
764
−7.670
−3.161
19.333
1.00
22.03


ATOM
1842
OD2
ASP
A
764
−7.013
−1.507
20.614
1.00
18.63


ATOM
1843
C
ASP
A
764
−5.446
−3.078
22.857
1.00
18.67


ATOM
1844
O
ASP
A
764
−6.269
−2.290
23.331
1.00
19.51


ATOM
1845
N
LEU
A
765
−5.126
−4.217
23.470
1.00
16.07


ATOM
1846
CA
LEU
A
765
−5.771
−4.596
24.726
1.00
16.91


ATOM
1847
CB
LEU
A
765
−6.108
−6.098
24.712
1.00
22.31


ATOM
1848
CG
LEU
A
765
−6.925
−6.653
23.540
1.00
22.32


ATOM
1849
CD1
LEU
A
765
−7.143
−8.152
23.733
1.00
22.41


ATOM
1850
CD2
LEU
A
765
−8.260
−5.940
23.451
1.00
22.60


ATOM
1851
C
LEU
A
765
−4.911
−4.288
25.953
1.00
17.63


ATOM
1852
O
LEU
A
765
−5.250
−4.699
27.062
1.00
18.64


ATOM
1853
N
SER
A
766
−3.830
−3.541
25.750
1.00
17.02


ATOM
1854
CA
SER
A
766
−2.869
−3.230
26.812
1.00
18.24


ATOM
1855
CB
SER
A
766
−1.846
−2.205
26.312
1.00
20.09


ATOM
1856
OG
SER
A
766
−2.378
−0.892
26.319
1.00
21.90


ATOM
1857
C
SER
A
766
−3.400
−2.775
28.171
1.00
17.35


ATOM
1858
O
SER
A
766
−2.738
−2.975
29.197
1.00
16.73


ATOM
1859
N
ALA
A
767
−4.571
−2.152
28.196
1.00
18.41


ATOM
1860
CA
ALA
A
767
−5.113
−1.682
29.466
1.00
19.58


ATOM
1861
CB
ALA
A
767
−6.465
−0.994
29.242
1.00
14.05


ATOM
1862
C
ALA
A
767
−5.272
−2.823
30.461
1.00
20.35


ATOM
1863
O
ALA
A
767
−5.111
−2.636
31.666
1.00
20.93


ATOM
1864
N
ILE
A
768
−5.580
−4.008
29.949
1.00
18.87


ATOM
1865
CA
ILE
A
768
−5.789
−5.176
30.786
1.00
20.62


ATOM
1866
CB
ILE
A
768
−6.405
−6.330
29.943
1.00
19.42


ATOM
1867
CG2
ILE
A
768
−5.323
−7.008
29.112
1.00
20.41


ATOM
1868
CG1
ILE
A
768
−7.087
−7.351
30.856
1.00
20.44


ATOM
1869
CD1
ILE
A
768
−8.333
−6.831
31.548
1.00
20.90


ATOM
1870
C
ILE
A
768
−4.499
−5.657
31.466
1.00
20.39


ATOM
1871
O
ILE
A
768
−4.543
−6.544
32.307
1.00
21.21


ATOM
1872
N
THR
A
769
−3.364
−5.061
31.108
1.00
19.18


ATOM
1873
CA
THR
A
769
−2.075
−5.437
31.693
1.00
19.16


ATOM
1874
CB
THR
A
769
−0.996
−5.672
30.620
1.00
20.58


ATOM
1875
OG1
THR
A
769
−0.519
−4.408
30.131
1.00
19.24


ATOM
1876
CG2
THR
A
769
−1.561
−6.478
29.453
1.00
20.09


ATOM
1877
C
THR
A
769
−1.496
−4.379
32.637
1.00
21.13


ATOM
1878
O
THR
A
769
−0.488
−4.618
33.300
1.00
21.47


ATOM
1879
N
LYS
A
770
−2.127
−3.214
32.691
1.00
19.99


ATOM
1880
CA
LYS
A
770
−1.634
−2.120
33.527
1.00
20.68


ATOM
1881
CB
LYS
A
770
−2.313
−0.812
33.108
1.00
20.27


ATOM
1882
CG
LYS
A
770
−2.103
−0.409
31.660
1.00
19.98


ATOM
1883
CD
LYS
A
770
−0.711
0.136
31.431
1.00
20.21


ATOM
1884
CE
LYS
A
770
−0.502
0.464
29.960
1.00
20.34


ATOM
1885
NZ
LYS
A
770
0.829
1.065
29.701
1.00
21.28


ATOM
1886
C
LYS
A
770
−1.861
−2.330
35.026
1.00
19.97


ATOM
1887
O
LYS
A
770
−2.628
−3.204
35.437
1.00
20.86


ATOM
1888
N
PRO
A
771
−1.186
−1.521
35.866
1.00
23.24


ATOM
1889
CD
PRO
A
771
−0.150
−0.537
35.512
1.00
25.67


ATOM
1890
CA
PRO
A
771
−1.329
−1.615
37.321
1.00
24.06


ATOM
1891
CB
PRO
A
771
−0.461
−0.463
37.823
1.00
25.01


ATOM
1892
CG
PRO
A
771
0.636
−0.421
36.809
1.00
24.38


ATOM
1893
C
PRO
A
771
−2.804
−1.429
37.672
1.00
23.94


ATOM
1894
O
PRO
A
771
−3.529
−0.723
36.970
1.00
23.81


ATOM
1895
N
TRP
A
772
−3.236
−2.057
38.759
1.00
22.70


ATOM
1896
CA
TRP
A
772
−4.626
−2.009
39.201
1.00
23.47


ATOM
1897
CB
TRP
A
772
−4.721
−2.480
40.652
1.00
31.03


ATOM
1898
CG
TRP
A
772
−6.120
−2.631
41.148
1.00
31.98


ATOM
1899
CD2
TRP
A
772
−7.205
−3.295
40.484
1.00
31.41


ATOM
1900
CE2
TRP
A
772
−8.322
−3.228
41.345
1.00
32.26


ATOM
1901
CE3
TRP
A
772
−7.342
−3.940
39.246
1.00
31.94


ATOM
1902
CD1
TRP
A
772
−6.611
−2.199
42.346
1.00
31.60


ATOM
1903
NE1
TRP
A
772
−7.930
−2.553
42.471
1.00
31.93


ATOM
1904
CZ2
TRP
A
772
−9.565
−3.785
41.009
1.00
32.15


ATOM
1905
CZ3
TRP
A
772
−8.579
−4.493
38.912
1.00
31.45


ATOM
1906
CH2
TRP
A
772
−9.672
−4.411
39.792
1.00
31.98


ATOM
1907
C
TRP
A
772
−5.368
−0.678
39.057
1.00
23.85


ATOM
1908
O
TRP
A
772
−6.409
−0.609
38.399
1.00
22.22


ATOM
1909
N
PRO
A
773
−4.857
0.398
39.678
1.00
25.77


ATOM
1910
CD
PRO
A
773
−3.583
0.541
40.403
1.00
32.22


ATOM
1911
CA
PRO
A
773
−5.546
1.689
39.567
1.00
26.04


ATOM
1912
CB
PRO
A
773
−4.609
2.650
40.304
1.00
32.61


ATOM
1913
CG
PRO
A
773
−3.259
1.991
40.171
1.00
33.14


ATOM
1914
C
PRO
A
773
−5.831
2.122
38.134
1.00
25.71


ATOM
1915
O
PRO
A
773
−6.900
2.653
37.834
1.00
26.03


ATOM
1916
N
ILE
A
774
−4.869
1.885
37.253
1.00
21.46


ATOM
1917
CA
ILE
A
774
−5.008
2.236
35.850
1.00
20.45


ATOM
1918
CB
ILE
A
774
−3.648
2.105
35.135
1.00
25.41


ATOM
1919
CG2
ILE
A
774
−3.790
2.436
33.654
1.00
25.27


ATOM
1920
CG1
ILE
A
774
−2.633
3.037
35.802
1.00
26.17


ATOM
1921
CD1
ILE
A
774
−1.205
2.807
35.355
1.00
25.47


ATOM
1922
C
ILE
A
774
−6.038
1.329
35.173
1.00
19.51


ATOM
1923
O
ILE
A
774
−6.928
1.804
34.471
1.00
18.75


ATOM
1924
N
GLN
A
775
−5.925
0.021
35.388
1.00
22.02


ATOM
1925
CA
GLN
A
775
−6.868
−0.916
34.783
1.00
21.75


ATOM
1926
CB
GLN
A
775
−6.491
−2.361
35.135
1.00
20.94


ATOM
1927
CG
GLN
A
775
−7.668
−3.340
35.192
1.00
21.03


ATOM
1928
CD
GLN
A
775
−8.395
−3.531
33.864
1.00
21.36


ATOM
1929
OE1
GLN
A
775
−9.457
−4.141
33.826
1.00
21.09


ATOM
1930
NE2
GLN
A
775
−7.826
−3.018
32.779
1.00
21.40


ATOM
1931
C
GLN
A
775
−8.300
−0.626
35.219
1.00
21.97


ATOM
1932
O
GLN
A
775
−9.216
−0.637
34.402
1.00
21.91


ATOM
1933
N
GLN
A
776
−8.486
−0.372
36.510
1.00
21.52


ATOM
1934
CA
GLN
A
776
−9.807
−0.066
37.051
1.00
23.77


ATOM
1935
CB
GLN
A
776
−9.709
0.263
38.537
1.00
38.83


ATOM
1936
CG
GLN
A
776
−9.798
−0.919
39.456
1.00
39.61


ATOM
1937
CD
GLN
A
776
−9.747
−0.503
40.910
1.00
39.43


ATOM
1938
OE1
GLN
A
776
−8.717
−0.035
41.397
1.00
39.77


ATOM
1939
NE2
GLN
A
776
−10.865
−0.662
41.610
1.00
39.38


ATOM
1940
C
GLN
A
776
−10.420
1.133
36.350
1.00
23.07


ATOM
1941
O
GLN
A
776
−11.582
1.106
35.942
1.00
24.26


ATOM
1942
N
ARG
A
777
−9.628
2.190
36.231
1.00
23.71


ATOM
1943
CA
ARG
A
777
−10.081
3.413
35.598
1.00
23.28


ATOM
1944
CB
ARG
A
777
−8.993
4.489
35.692
1.00
27.59


ATOM
1945
CG
ARG
A
777
−9.423
5.850
35.159
1.00
27.74


ATOM
1946
CD
ARG
A
777
−8.305
6.873
35.280
1.00
27.86


ATOM
1947
NE
ARG
A
777
−7.155
6.535
34.445
1.00
27.75


ATOM
1948
CZ
ARG
A
777
−7.161
6.545
33.114
1.00
27.57


ATOM
1949
NH1
ARG
A
777
−8.257
6.881
32.448
1.00
28.23


ATOM
1950
NH2
ARG
A
777
−6.066
6.216
32.446
1.00
28.20


ATOM
1951
C
ARG
A
777
−10.465
3.191
34.139
1.00
23.20


ATOM
1952
O
ARG
A
777
−11.537
3.605
33.704
1.00
22.51


ATOM
1953
N
ILE
A
778
−9.592
2.535
33.380
1.00
17.78


ATOM
1954
CA
ILE
A
778
−9.884
2.297
31.972
1.00
17.96


ATOM
1955
CB
ILE
A
778
−8.633
1.806
31.225
1.00
19.43


ATOM
1956
CG2
ILE
A
778
−8.967
1.520
29.764
1.00
18.09


ATOM
1957
CG1
ILE
A
778
−7.560
2.894
31.305
1.00
19.35


ATOM
1958
CD1
ILE
A
778
−6.214
2.505
30.738
1.00
19.60


ATOM
1959
C
ILE
A
778
−11.038
1.323
31.796
1.00
18.56


ATOM
1960
O
ILE
A
778
−11.872
1.502
30.903
1.00
18.79


ATOM
1961
N
ALA
A
779
−11.106
0.309
32.654
1.00
20.16


ATOM
1962
CA
ALA
A
779
−12.199
−0.656
32.590
1.00
21.21


ATOM
1963
CB
ALA
A
779
−12.066
−1.680
33.708
1.00
24.43


ATOM
1964
C
ALA
A
779
−13.531
0.091
32.712
1.00
21.19


ATOM
1965
O
ALA
A
779
−14.519
−0.280
32.085
1.00
20.38


ATOM
1966
N
GLU
A
780
−13.558
1.147
33.518
1.00
20.96


ATOM
1967
CA
GLU
A
780
−14.786
1.926
33.682
1.00
22.15


ATOM
1968
CB
GLU
A
780
−14.652
2.894
34.863
1.00
51.37


ATOM
1969
CG
GLU
A
780
−14.497
2.196
36.206
1.00
52.40


ATOM
1970
CD
GLU
A
780
−14.449
3.163
37.373
1.00
53.03


ATOM
1971
OE1
GLU
A
780
−13.590
4.072
37.359
1.00
53.05


ATOM
1972
OE2
GLU
A
780
−15.266
3.013
38.306
1.00
52.97


ATOM
1973
C
GLU
A
780
−15.147
2.696
32.407
1.00
21.53


ATOM
1974
O
GLU
A
780
−16.326
2.918
32.127
1.00
20.90


ATOM
1975
N
LEU
A
781
−14.134
3.105
31.642
1.00
18.46


ATOM
1976
CA
LEU
A
781
−14.365
3.818
30.390
1.00
19.53


ATOM
1977
CB
LEU
A
781
−13.050
4.399
29.847
1.00
20.51


ATOM
1978
CG
LEU
A
781
−12.392
5.516
30.672
1.00
21.84


ATOM
1979
CD1
LEU
A
781
−11.131
6.026
29.976
1.00
21.36


ATOM
1980
CD2
LEU
A
781
−13.389
6.660
30.828
1.00
20.48


ATOM
1981
C
LEU
A
781
−14.949
2.824
29.389
1.00
19.65


ATOM
1982
O
LEU
A
781
−15.898
3.133
28.654
1.00
19.62


ATOM
1983
N
VAL
A
782
−14.368
1.628
29.362
1.00
21.76


ATOM
1984
CA
VAL
A
782
−14.837
0.569
28.474
1.00
22.54


ATOM
1985
CB
VAL
A
782
−14.026
−0.740
28.693
1.00
22.92


ATOM
1986
CG1
VAL
A
782
−14.659
−1.889
27.931
1.00
21.63


ATOM
1987
CG2
VAL
A
782
−12.588
−0.554
28.231
1.00
22.05


ATOM
1988
C
VAL
A
782
−16.311
0.290
28.766
1.00
21.93


ATOM
1989
O
VAL
A
782
−17.142
0.238
27.857
1.00
23.01


ATOM
1990
N
ALA
A
783
−16.632
0.123
30.045
1.00
19.50


ATOM
1991
CA
ALA
A
783
−18.000
−0.166
30.445
1.00
21.17


ATOM
1992
CB
ALA
A
783
−18.061
−0.447
31.942
1.00
21.14


ATOM
1993
C
ALA
A
783
−18.940
0.979
30.078
1.00
20.67


ATOM
1994
O
ALA
A
783
−20.051
0.755
29.598
1.00
21.82


ATOM
1995
N
THR
A
784
−18.490
2.209
30.291
1.00
23.13


ATOM
1996
CA
THR
A
784
−19.312
3.362
29.962
1.00
23.26


ATOM
1997
CB
THR
A
784
−18.577
4.668
30.312
1.00
24.94


ATOM
1998
OG1
THR
A
784
−18.379
4.726
31.731
1.00
25.01


ATOM
1999
CG2
THR
A
784
−19.379
5.877
29.864
1.00
24.89


ATOM
2000
C
THR
A
784
−19.702
3.364
28.481
1.00
24.33


ATOM
2001
O
THR
A
784
−20.881
3.543
28.130
1.00
22.64


ATOM
2002
N
GLU
A
785
−18.720
3.153
27.612
1.00
19.82


ATOM
2003
CA
GLU
A
785
−18.991
3.136
26.182
1.00
21.00


ATOM
2004
CB
GLU
A
785
−17.678
2.998
25.387
1.00
21.06


ATOM
2005
CG
GLU
A
785
−17.871
2.918
23.873
1.00
20.31


ATOM
2006
CD
GLU
A
785
−16.575
3.080
23.081
1.00
21.05


ATOM
2007
OE1
GLU
A
785
−16.506
2.557
21.947
1.00
20.57


ATOM
2008
OE2
GLU
A
785
−15.637
3.740
23.572
1.00
18.86


ATOM
2009
C
GLU
A
785
−19.965
2.006
25.846
1.00
20.29


ATOM
2010
O
GLU
A
785
−20.905
2.211
25.083
1.00
20.32


ATOM
2011
N
PHE
A
786
−19.753
0.824
26.422
1.00
21.26


ATOM
2012
CA
PHE
A
786
−20.643
−0.307
26.161
1.00
21.97


ATOM
2013
CB
PHE
A
786
−20.185
−1.567
26.901
1.00
26.06


ATOM
2014
CG
PHE
A
786
−18.955
−2.216
26.324
1.00
27.41


ATOM
2015
CD1
PHE
A
786
−18.629
−2.067
24.978
1.00
27.06


ATOM
2016
CD2
PHE
A
786
−18.146
−3.021
27.122
1.00
26.60


ATOM
2017
CE1
PHE
A
786
−17.519
−2.711
24.437
1.00
27.27


ATOM
2018
CE2
PHE
A
786
−17.032
−3.672
26.586
1.00
27.24


ATOM
2019
CZ
PHE
A
786
−16.722
−3.515
25.244
1.00
27.18


ATOM
2020
C
PHE
A
786
−22.068
0.011
26.599
1.00
23.40


ATOM
2021
O
PHE
A
786
−23.023
−0.269
25.878
1.00
21.69


ATOM
2022
N
PHE
A
787
−22.206
0.594
27.787
1.00
23.44


ATOM
2023
CA
PHE
A
787
−23.530
0.926
28.297
1.00
22.70


ATOM
2024
CB
PHE
A
787
−23.445
1.413
29.751
1.00
22.93


ATOM
2025
CG
PHE
A
787
−22.945
0.370
30.719
1.00
21.91


ATOM
2026
CD1
PHE
A
787
−23.122
−0.991
30.464
1.00
22.94


ATOM
2027
CD2
PHE
A
787
−22.335
0.749
31.910
1.00
23.07


ATOM
2028
CE1
PHE
A
787
−22.697
−1.954
31.383
1.00
23.17


ATOM
2029
CE2
PHE
A
787
−21.907
−0.201
32.833
1.00
22.50


ATOM
2030
CZ
PHE
A
787
−22.087
−1.555
32.572
1.00
23.33


ATOM
2031
C
PHE
A
787
−24.215
1.968
27.417
1.00
23.79


ATOM
2032
O
PHE
A
787
−25.431
1.906
27.205
1.00
21.92


ATOM
2033
N
ASP
A
788
−23.442
2.912
26.884
1.00
23.70


ATOM
2034
CA
ASP
A
788
−24.021
3.923
26.010
1.00
25.33


ATOM
2035
CB
ASP
A
788
−22.978
4.959
25.591
1.00
54.55


ATOM
2036
CG
ASP
A
788
−23.605
6.296
25.233
1.00
55.82


ATOM
2037
OD1
ASP
A
788
−24.157
6.955
26.141
1.00
56.10


ATOM
2038
OD2
ASP
A
788
−23.558
6.686
24.046
1.00
55.97


ATOM
2039
C
ASP
A
788
−24.571
3.216
24.774
1.00
24.36


ATOM
2040
O
ASP
A
788
−25.646
3.551
24.283
1.00
25.06


ATOM
2041
N
GLN
A
789
−23.837
2.235
24.257
1.00
20.19


ATOM
2042
CA
GLN
A
789
−24.350
1.522
23.101
1.00
19.43


ATOM
2043
CB
GLN
A
789
−23.340
0.508
22.566
1.00
19.05


ATOM
2044
CG
GLN
A
789
−23.987
−0.433
21.563
1.00
19.55


ATOM
2045
CD
GLN
A
789
−23.011
−1.268
20.781
1.00
19.48


ATOM
2046
OE1
GLN
A
789
−23.388
−2.299
20.222
1.00
20.82


ATOM
2047
NE2
GLN
A
789
−21.755
−0.833
20.718
1.00
18.14


ATOM
2048
C
GLN
A
789
−25.629
0.802
23.503
1.00
20.46


ATOM
2049
O
GLN
A
789
−26.586
0.735
22.729
1.00
20.11


ATOM
2050
N
GLY
A
790
−25.639
0.266
24.721
1.00
22.31


ATOM
2051
CA
GLY
A
790
−26.810
−0.436
25.216
1.00
24.09


ATOM
2052
C
GLY
A
790
−28.031
0.463
25.175
1.00
25.10


ATOM
2053
O
GLY
A
790
−29.115
0.025
24.783
1.00
24.31


ATOM
2054
N
ASP
A
791
−27.857
1.722
25.573
1.00
25.00


ATOM
2055
CA
ASP
A
791
−28.963
2.683
25.568
1.00
25.93


ATOM
2056
CB
ASP
A
791
−28.525
4.026
26.160
1.00
29.26


ATOM
2057
CG
ASP
A
791
−28.107
3.918
27.611
1.00
29.25


ATOM
2058
OD1
ASP
A
791
−28.575
2.987
28.297
1.00
29.11


ATOM
2059
OD2
ASP
A
791
−27.323
4.778
28.068
1.00
30.04


ATOM
2060
C
ASP
A
791
−29.464
2.909
24.143
1.00
25.33


ATOM
2061
O
ASP
A
791
−30.669
3.029
23.907
1.00
26.34


ATOM
2062
N
ARG
A
792
−28.527
2.984
23.205
1.00
25.90


ATOM
2063
CA
ARG
A
792
−28.842
3.185
21.794
1.00
25.99


ATOM
2064
CB
ARG
A
792
−27.546
3.326
20.990
1.00
34.02


ATOM
2065
CG
ARG
A
792
−26.801
4.633
21.228
1.00
34.62


ATOM
2066
CD
ARG
A
792
−27.310
5.716
20.300
1.00
35.57


ATOM
2067
NE
ARG
A
792
−26.820
5.533
18.935
1.00
35.28


ATOM
2068
CZ
ARG
A
792
−25.591
5.845
18.537
1.00
34.46


ATOM
2069
NH1
ARG
A
792
−24.726
6.358
19.403
1.00
34.52


ATOM
2070
NH2
ARG
A
792
−25.225
5.647
17.278
1.00
34.52


ATOM
2071
C
ARG
A
792
−29.645
2.005
21.261
1.00
26.14


ATOM
2072
O
ARG
A
792
−30.634
2.179
20.553
1.00
26.08


ATOM
2073
N
GLU
A
793
−29.219
0.797
21.608
1.00
25.23


ATOM
2074
CA
GLU
A
793
−29.910
−0.396
21.141
1.00
25.15


ATOM
2075
CB
GLU
A
793
−29.156
−1.650
21.584
1.00
28.67


ATOM
2076
CG
GLU
A
793
−27.715
−1.688
21.120
1.00
29.21


ATOM
2077
CD
GLU
A
793
−27.005
−2.958
21.543
1.00
29.03


ATOM
2078
OE1
GLU
A
793
−27.219
−3.406
22.689
1.00
28.67


ATOM
2079
OE2
GLU
A
793
−26.222
−3.501
20.737
1.00
28.60


ATOM
2080
C
GLU
A
793
−31.343
−0.444
21.660
1.00
26.11


ATOM
2081
O
GLU
A
793
−32.254
−0.858
20.945
1.00
25.51


ATOM
2082
N
ARG
A
794
−31.546
−0.022
22.904
1.00
30.47


ATOM
2083
CA
ARG
A
794
−32.887
−0.041
23.477
1.00
30.88


ATOM
2084
CB
ARG
A
794
−32.861
0.402
24.945
1.00
42.43


ATOM
2085
CG
ARO
A
794
−31.776
−0.241
25.786
1.00
42.99


ATOM
2086
CD
ARG
A
794
−31.978
0.056
27.266
1.00
43.11


ATOM
2087
NE
ARG
A
794
−32.839
−0.939
27.893
1.00
43.32


ATOM
2088
CZ
ARG
A
794
−32.425
−1.820
28.798
1.00
42.83


ATOM
2089
NH1
ARG
A
794
−31.158
−1.826
29.194
1.00
43.06


ATOM
2090
NH2
ARG
A
794
−33.274
−2.708
29.295
1.00
43.25


ATOM
2091
C
ARG
A
794
−33.818
0.886
22.701
1.00
31.12


ATOM
2092
O
ARG
A
794
−34.972
0.547
22.451
1.00
30.32


ATOM
2093
N
LYS
A
795
−33.307
2.050
22.314
1.00
28.47


ATOM
2094
CA
LYS
A
795
−34.111
3.036
21.597
1.00
30.19


ATOM
2095
CB
LYS
A
795
−33.538
4.438
21.833
1.00
43.10


ATOM
2096
CG
LYS
A
795
−33.084
4.688
23.262
1.00
43.51


ATOM
2097
CD
LYS
A
795
−32.642
6.129
23.482
1.00
44.03


ATOM
2098
CE
LYS
A
795
−33.794
6.991
23.976
1.00
43.69


ATOM
2099
NZ
LYS
A
795
−34.961
6.964
23.051
1.00
43.61


ATOM
2100
C
LYS
A
795
−34.238
2.799
20.093
1.00
29.44


ATOM
2101
O
LYS
A
795
−35.341
2.832
19.545
1.00
29.39


ATOM
2102
N
GLU
A
796
−33.110
2.558
19.433
1.00
32.97


ATOM
2103
CA
GLU
A
796
−33.080
2.358
17.987
1.00
33.23


ATOM
2104
CB
GLU
A
796
−31.723
2.803
17.443
1.00
31.41


ATOM
2105
CG
GLU
A
796
−31.265
4.158
17.957
1.00
31.18


ATOM
2106
CD
GLU
A
796
−29.913
4.573
17.401
1.00
31.42


ATOM
2107
OE1
GLU
A
796
−29.334
5.558
17.904
1.00
31.78


ATOM
2108
OE2
GLU
A
796
−29.432
3.917
16.455
1.00
32.26


ATOM
2109
C
GLU
A
796
−33.376
0.939
17.496
1.00
33.01


ATOM
2110
O
GLU
A
796
−33.778
0.750
16.347
1.00
33.78


ATOM
2111
N
LEU
A
797
−33.170
−0.058
18.347
1.00
29.85


ATOM
2112
CA
LEU
A
797
−33.424
−1.438
17.952
1.00
29.25


ATOM
2113
CB
LEU
A
797
−32.134
−2.261
18.059
1.00
32.07


ATOM
2114
CG
LEU
A
797
−30.951
−1.828
17.185
1.00
32.45


ATOM
2115
CD1
LEU
A
797
−29.759
−2.731
17.475
1.00
32.42


ATOM
2116
CD2
LEU
A
797
−31.325
−1.904
15.709
1.00
32.29


ATOM
2117
C
LEU
A
797
−34.513
−2.073
18.807
1.00
29.52


ATOM
2118
O
LEU
A
797
−34.954
−3.192
18.534
1.00
29.88


ATOM
2119
N
ASN
A
798
−34.940
−1.348
19.839
1.00
31.24


ATOM
2120
CA
ASN
A
798
−35.972
−1.815
20.757
1.00
31.79


ATOM
2121
CB
ASN
A
798
−37.332
−1.805
20.062
1.00
46.67


ATOM
2122
CG
ASN
A
798
−37.975
−0.439
20.083
1.00
47.32


ATOM
2123
OD1
ASN
A
798
−38.405
0.038
21.136
1.00
47.67


ATOM
2124
ND2
ASN
A
798
−38.037
0.208
18.924
1.00
47.41


ATOM
2125
C
ASN
A
798
−35.694
−3.189
21.338
1.00
31.17


ATOM
2126
O
ASN
A
798
−36.593
−4.016
21.468
1.00
30.69


ATOM
2127
N
ILE
A
799
−34.438
−3.427
21.694
1.00
29.19


ATOM
2128
CA
ILE
A
799
−34.046
−4.701
22.274
1.00
29.70


ATOM
2129
CB
ILE
A
799
−33.026
−5.444
21.379
1.00
28.41


ATOM
2130
CG2
ILE
A
799
−33.660
−5.795
20.036
1.00
29.14


ATOM
2131
CG1
ILE
A
799
−31.781
−4.571
21.191
1.00
28.71


ATOM
2132
CD1
ILE
A
799
−30.632
−5.251
20.494
1.00
28.52


ATOM
2133
C
ILE
A
799
−33.389
−4.463
23.627
1.00
29.70


ATOM
2134
O
ILE
A
799
−32.889
−3.370
23.904
1.00
29.11


ATOM
2135
N
GLU
A
800
−33.410
−5.481
24.477
1.00
31.12


ATOM
2136
CA
GLU
A
800
−32.764
−5.369
25.775
1.00
32.32


ATOM
2137
CB
GLU
A
800
−33.322
−6.394
26.768
1.00
47.83


ATOM
2138
CG
GLU
A
800
−32.572
−6.418
28.099
1.00
48.49


ATOM
2139
CD
GLU
A
800
−32.999
−7.559
29.007
1.00
48.67


ATOM
2140
OE1
GLU
A
800
−32.393
−7.713
30.091
1.00
48.86


ATOM
2141
OE2
GLU
A
800
−33.938
−8.299
28.640
1.00
48.41


ATOM
2142
C
GLU
A
800
−31.309
−5.692
25.474
1.00
31.85


ATOM
2143
O
GLU
A
800
−31.009
−6.731
24.888
1.00
31.72


ATOM
2144
N
PRO
A
801
−30.386
−4.801
25.855
1.00
32.29


ATOM
2145
CD
PRO
A
801
−30.534
−3.557
26.629
1.00
32.84


ATOM
2146
CA
PRO
A
801
−28.976
−5.083
25.578
1.00
32.39


ATOM
2147
CB
PRO
A
801
−28.281
−3.798
26.019
1.00
33.48


ATOM
2148
CG
PRO
A
801
−29.143
−3.351
27.168
1.00
33.84


ATOM
2149
C
PRO
A
801
−28.462
−6.308
26.323
1.00
31.89


ATOM
2150
O
PRO
A
801
−29.056
−6.752
27.312
1.00
31.79


ATOM
2151
N
THR
A
802
−27.362
−6.863
25.826
1.00
28.76


ATOM
2152
CA
THR
A
802
−26.739
−8.016
26.456
1.00
28.15


ATOM
2153
CB
THR
A
802
−25.626
−8.603
25.569
1.00
44.26


ATOM
2154
OG1
THR
A
802
−25.026
−9.721
26.233
1.00
45.50


ATOM
2155
CG2
THR
A
802
−24.561
−7.555
25.282
1.00
44.69


ATOM
2156
C
THR
A
802
−26.139
−7.521
27.767
1.00
28.29


ATOM
2157
O
THR
A
802
−25.956
−6.317
27.960
1.00
27.03


ATOM
2158
N
ASP
A
803
−25.843
−8.448
28.669
1.00
28.44


ATOM
2159
CA
ASP
A
803
−25.275
−8.094
29.963
1.00
28.64


ATOM
2160
CB
ASP
A
803
−24.779
−9.358
30.667
1.00
34.48


ATOM
2161
CG
ASP
A
803
−25.893
−10.098
31.379
1.00
34.81


ATOM
2162
OD1
ASP
A
803
−27.045
−10.054
30.893
1.00
34.90


ATOM
2163
OD2
ASP
A
803
−25.611
−10.730
32.420
1.00
35.01


ATOM
2164
C
ASP
A
803
−24.153
−7.063
29.906
1.00
28.44


ATOM
2165
O
ASP
A
803
−24.176
−6.074
30.635
1.00
28.48


ATOM
2166
N
LEU
A
804
−23.177
−7.275
29.031
1.00
25.97


ATOM
2167
CA
LEU
A
804
−22.058
−6.348
28.952
1.00
26.25


ATOM
2168
CB
LEU
A
804
−20.951
−6.937
28.075
1.00
47.64


ATOM
2169
CG
LEU
A
804
−21.304
−7.412
26.671
1.00
48.05


ATOM
2170
CD1
LEU
A
804
−21.264
−6.244
25.708
1.00
48.53


ATOM
2171
CD2
LEU
A
804
−20.301
−8.466
26.242
1.00
48.25


ATOM
2172
C
LEU
A
804
−22.415
−4.938
28.501
1.00
26.00


ATOM
2173
O
LEU
A
804
−21.654
−4.007
28.728
1.00
25.68


ATOM
2174
N
MET
A
805
−23.576
−4.763
27.881
1.00
25.47


ATOM
2175
CA
MET
A
805
−23.971
−3.427
27.445
1.00
25.62


ATOM
2176
CB
MET
A
805
−24.246
−3.422
25.940
1.00
32.20


ATOM
2177
CG
MET
A
805
−22.992
−3.634
25.113
1.00
31.73


ATOM
2178
SD
MET
A
805
−23.263
−3.668
23.345
1.00
32.78


ATOM
2179
CE
MET
A
805
−21.557
−3.485
22.751
1.00
31.70


ATOM
2180
C
MET
A
805
−25.186
−2.920
28.209
1.00
24.74


ATOM
2181
O
MET
A
805
−25.808
−1.932
27.813
1.00
25.55


ATOM
2182
N
ASN
A
806
−25.502
−3.596
29.311
1.00
23.96


ATOM
2183
CA
ASN
A
806
−26.645
−3.239
30.151
1.00
25.57


ATOM
2184
CB
ASN
A
806
−27.467
−4.495
30.463
1.00
28.17


ATOM
2185
CG
ASN
A
806
−28.738
−4.190
31.241
1.00
28.82


ATOM
2186
OD1
ASN
A
806
−28.985
−3.049
31.628
1.00
28.36


ATOM
2187
ND2
ASN
A
806
−29.550
−5.216
31.474
1.00
28.76


ATOM
2188
C
ASN
A
806
−26.159
−2.592
31.448
1.00
25.52


ATOM
2189
O
ASN
A
806
−25.648
−3.273
32.338
1.00
25.16


ATOM
2190
N
ARG
A
807
−26.321
−1.276
31.544
1.00
25.21


ATOM
2191
CA
ARG
A
807
−25.892
−0.512
32.717
1.00
25.42


ATOM
2192
CB
ARG
A
807
−26.254
0.963
32.532
1.00
30.28


ATOM
2193
CG
ARG
A
807
−25.516
1.919
33.450
1.00
31.10


ATOM
2194
CD
ARG
A
807
−26.051
3.331
33.290
1.00
31.22


ATOM
2195
NE
ARG
A
807
−26.092
3.752
31.892
1.00
31.51


ATOM
2196
CZ
ARG
A
807
−25.040
4.157
31.192
1.00
31.00


ATOM
2197
NH1
ARG
A
807
−23.839
4.205
31.753
1.00
32.13


ATOM
2198
NH2
ARG
A
807
−25.191
4.516
29.923
1.00
30.26


ATOM
2199
C
ARG
A
807
−26.528
−1.030
34.002
1.00
27.00


ATOM
2200
O
ARG
A
807
−25.916
−0.988
35.073
1.00
26.42


ATOM
2201
N
GLU
A
808
−27.762
−1.508
33.895
1.00
29.47


ATOM
2202
CA
GLU
A
808
−28.477
−2.031
35.053
1.00
30.52


ATOM
2203
CB
GLU
A
808
−29.914
−2.372
34.659
1.00
44.58


ATOM
2204
CG
GLU
A
808
−30.775
−1.147
34.408
1.00
45.18


ATOM
2205
CD
GLU
A
808
−32.132
−1.492
33.837
1.00
45.51


ATOM
2206
OE1
GLU
A
808
−32.761
−2.451
34.332
1.00
45.53


ATOM
2207
OE2
GLU
A
808
−32.573
−0.796
32.898
1.00
45.65


ATOM
2208
C
GLU
A
808
−27.780
−3.261
35.629
1.00
30.44


ATOM
2209
O
GLU
A
808
−27.875
−3.542
36.828
1.00
30.33


ATOM
2210
N
LYS
A
809
−27.077
−3.985
34.765
1.00
31.29


ATOM
2211
CA
LYS
A
809
−26.355
−5.190
35.162
1.00
31.25


ATOM
2212
CB
LYS
A
809
−26.522
−6.279
34.092
1.00
41.16


ATOM
2213
CG
LYS
A
809
−27.951
−6.773
33.888
1.00
41.47


ATOM
2214
CD
LYS
A
809
−28.391
−7.716
34.995
1.00
41.55


ATOM
2215
CE
LYS
A
809
−27.714
−9.075
34.885
1.00
41.48


ATOM
2216
NZ
LYS
A
809
−28.230
−9.865
33.733
1.00
41.41


ATOM
2217
C
LYS
A
809
−24.870
−4.879
35.338
1.00
30.98


ATOM
2218
O
LYS
A
809
−24.023
−5.744
35.129
1.00
30.77


ATOM
2219
N
LYS
A
810
−24.551
−3.646
35.721
1.00
26.58


ATOM
2220
CA
LYS
A
810
−23.155
−3.259
35.901
1.00
26.99


ATOM
2221
CB
LYS
A
810
−23.050
−1.768
36.235
1.00
43.46


ATOM
2222
CG
LYS
A
810
−23.626
−1.387
37.587
1.00
44.21


ATOM
2223
CD
LYS
A
810
−23.413
0.090
37.878
1.00
44.21


ATOM
2224
CE
LYS
A
810
−23.942
0.459
39.256
1.00
44.19


ATOM
2225
NZ
LYS
A
810
−23.718
1.897
39.566
1.00
44.47


ATOM
2226
C
LYS
A
810
−22.462
−4.077
36.997
1.00
26.09


ATOM
2227
O
LYS
A
810
−21.234
−4.128
37.060
1.00
26.59


ATOM
2228
N
ASN
A
811
−23.250
−4.720
37.852
1.00
29.32


ATOM
2229
CA
ASN
A
811
−22.693
−5.526
38.934
1.00
29.87


ATOM
2230
CB
ASN
A
811
−23.812
−6.017
39.858
1.00
45.97


ATOM
2231
CG
ASN
A
811
−24.632
−7.135
39.240
1.00
46.38


ATOM
2232
OD1
ASN
A
811
−24.137
−8.247
39.042
1.00
46.84


ATOM
2233
ND2
ASN
A
811
−25.887
−6.847
38.927
1.00
46.45


ATOM
2234
C
ASN
A
811
−21.931
−6.730
38.385
1.00
29.68


ATOM
2235
O
ASN
A
811
−21.228
−7.425
39.121
1.00
29.10


ATOM
2236
N
LYS
A
812
−22.075
−6.970
37.086
1.00
24.91


ATOM
2237
CA
LYS
A
812
−21.418
−8.100
36.438
1.00
25.57


ATOM
2238
CB
LYS
A
812
−22.292
−8.623
35.295
1.00
45.40


ATOM
2239
CG
LYS
A
812
−22.850
−10.016
35.509
1.00
46.25


ATOM
2240
CD
LYS
A
812
−23.811
−10.060
36.678
1.00
46.19


ATOM
2241
CE
LYS
A
812
−24.429
−11.439
36.816
1.00
46.23


ATOM
2242
NZ
LYS
A
812
−23.387
−12.487
37.001
1.00
46.38


ATOM
2243
C
LYS
A
812
−20.025
−7.789
35.886
1.00
24.76


ATOM
2244
O
LYS
A
812
−19.340
−8.688
35.401
1.00
24.68


ATOM
2245
N
ILE
A
813
−19.598
−6.534
35.963
1.00
26.65


ATOM
2246
CA
ILE
A
813
−18.294
−6.162
35.424
1.00
26.72


ATOM
2247
CB
ILE
A
813
−18.008
−4.656
35.630
1.00
25.86


ATOM
2248
CG2
ILE
A
813
−16.564
−4.337
35.260
1.00
25.72


ATOM
2249
CG1
ILE
A
813
−18.955
−3.830
34.751
1.00
25.85


ATOM
2250
CD1
ILE
A
813
−18.880
−2.335
34.984
1.00
26.75


ATOM
2251
C
ILE
A
813
−17.123
−6.986
35.957
1.00
26.25


ATOM
2252
O
ILE
A
813
−16.271
−7.426
35.185
1.00
25.98


ATOM
2253
N
PRO
A
814
−17.055
−7.205
37.280
1.00
22.10


ATOM
2254
CD
PRO
A
814
−17.742
−6.559
38.415
1.00
23.22


ATOM
2255
CA
PRO
A
814
−15.916
−8.003
37.741
1.00
23.12


ATOM
2256
CB
PRO
A
814
−16.116
−8.048
39.253
1.00
22.48


ATOM
2257
CG
PRO
A
814
−16.722
−6.697
39.537
1.00
22.19


ATOM
2258
C
PRO
A
814
−15.842
−9.392
37.115
1.00
23.05


ATOM
2259
O
PRO
A
814
−14.792
−9.796
36.619
1.00
23.01


ATOM
2260
N
SER
A
815
−16.952
−10.123
37.129
1.00
24.56


ATOM
2261
CA
SER
A
815
−16.955
−11.465
36.555
1.00
24.61


ATOM
2262
CB
SER
A
815
−18.286
−12.174
36.844
1.00
32.62


ATOM
2263
OG
SER
A
815
−19.393
−11.454
36.330
1.00
33.36


ATOM
2264
C
SER
A
815
−16.687
−11.440
35.049
1.00
24.80


ATOM
2265
O
SER
A
815
−16.055
−12.349
34.513
1.00
25.10


ATOM
2266
N
MET
A
816
−17.153
−10.398
34.368
1.00
25.71


ATOM
2267
CA
MET
A
816
−16.938
−10.286
32.925
1.00
24.80


ATOM
2268
CB
MET
A
816
−17.820
−9.188
32.332
1.00
40.93


ATOM
2269
CG
MET
A
816
−19.302
−9.432
32.489
1.00
41.93


ATOM
2270
SD
MET
A
816
−20.264
−8.316
31.459
1.00
42.83


ATOM
2271
CE
MET
A
816
−19.866
−6.716
32.201
1.00
41.73


ATOM
2272
C
MET
A
816
−15.479
−10.000
32.585
1.00
24.22


ATOM
2273
O
MET
A
816
−14.969
−10.476
31.574
1.00
24.07


ATOM
2274
N
GLN
A
817
−14.806
−9.216
33.420
1.00
24.08


ATOM
2275
CA
GLN
A
817
−13.403
−8.909
33.182
1.00
22.68


ATOM
2276
CB
GLN
A
817
−12.904
−7.844
34.161
1.00
21.90


ATOM
2277
CG
GLN
A
817
−13.287
−6.415
33.786
1.00
21.57


ATOM
2278
CD
GLN
A
817
−12.797
−6.020
32.407
1.00
22.28


ATOM
2279
OE1
GLN
A
817
−13.389
−6.392
31.396
1.00
21.33


ATOM
2280
NE2
GLN
A
817
−11.704
−5.272
32.359
1.00
21.19


ATOM
2281
C
GLN
A
817
−12.587
−10.185
33.344
1.00
24.08


ATOM
2282
O
GLN
A
817
−11.655
−10.435
32.588
1.00
22.00


ATOM
2283
N
VAL
A
818
−12.947
−10.990
34.340
1.00
22.79


ATOM
2284
CA
VAL
A
818
−12.262
−12.256
34.582
1.00
23.81


ATOM
2285
CB
VAL
A
818
−12.839
−12.958
35.828
1.00
26.49


ATOM
2286
CG1
VAL
A
818
−12.225
−14.338
35.983
1.00
26.65


ATOM
2287
CG2
VAL
A
818
−12.567
−12.115
37.064
1.00
26.49


ATOM
2288
C
VAL
A
818
−12.453
−13.161
33.364
1.00
24.69


ATOM
2289
O
VAL
A
818
−11.502
−13.776
32.871
1.00
23.39


ATOM
2290
N
GLY
A
819
−13.687
−13.234
32.878
1.00
25.13


ATOM
2291
CA
GLY
A
819
−13.971
−14.061
31.716
1.00
24.79


ATOM
2292
C
GLY
A
819
−13.221
−13.571
30.490
1.00
24.86


ATOM
2293
O
GLY
A
819
−12.729
−14.354
29.677
1.00
25.43


ATOM
2294
N
PHE
A
820
−13.140
−12.255
30.355
1.00
24.15


ATOM
2295
CA
PHE
A
820
−12.440
−11.635
29.241
1.00
22.60


ATOM
2296
CB
PHE
A
820
−12.606
−10.113
29.336
1.00
22.65


ATOM
2297
CG
PHE
A
820
−11.736
−9.335
28.389
1.00
22.10


ATOM
2298
CD1
PHE
A
820
−11.863
−9.490
27.011
1.00
22.63


ATOM
2299
CD2
PHE
A
820
−10.803
−8.424
28.879
1.00
22.66


ATOM
2300
CE1
PHE
A
820
−11.069
−8.743
26.133
1.00
22.28


ATOM
2301
CE2
PHE
A
820
−10.008
−7.677
28.011
1.00
22.73


ATOM
2302
CZ
PHE
A
820
−10.143
−7.839
26.637
1.00
22.74


ATOM
2303
C
PHE
A
820
−10.964
−12.024
29.293
1.00
23.46


ATOM
2304
O
PHE
A
820
−10.357
−12.369
28.283
1.00
21.24


ATOM
2305
N
ILE
A
821
−10.390
−11.984
30.488
1.00
21.23


ATOM
2306
CA
ILE
A
821
−8.990
−12.323
30.646
1.00
21.89


ATOM
2307
CB
ILE
A
821
−8.525
−12.044
32.088
1.00
22.37


ATOM
2308
CG2
ILE
A
821
−7.130
−12.596
32.315
1.00
22.42


ATOM
2309
CG1
ILE
A
821
−8.526
−10.534
32.332
1.00
21.45


ATOM
2310
CD1
ILE
A
821
−8.377
−10.160
33.777
1.00
23.29


ATOM
2311
C
ILE
A
821
−8.744
−13.784
30.292
1.00
22.08


ATOM
2312
O
ILE
A
821
−7.864
−14.081
29.488
1.00
24.60


ATOM
2313
N
ASP
A
822
−9.528
−14.687
30.873
1.00
31.25


ATOM
2314
CA
ASP
A
822
−9.364
−16.113
30.600
1.00
32.20


ATOM
2315
CB
ASP
A
822
−10.379
−16.950
31.390
1.00
31.68


ATOM
2316
CG
ASP
A
822
−10.096
−16.978
32.876
1.00
30.88


ATOM
2317
OD1
ASP
A
822
−8.923
−16.812
33.265
1.00
31.47


ATOM
2318
OD2
ASP
A
822
−11.054
−17.186
33.652
1.00
31.29


ATOM
2319
C
ASP
A
822
−9.520
−16.474
29.127
1.00
33.01


ATOM
2320
O
ASP
A
822
−8.680
−17.165
28.552
1.00
33.17


ATOM
2321
N
ALA
A
823
−10.600
−15.996
28.523
1.00
31.01


ATOM
2322
CA
ALA
A
823
−10.912
−16.309
27.131
1.00
30.74


ATOM
2323
CB
ALA
A
823
−12.402
−16.092
26.894
1.00
28.33


ATOM
2324
C
ALA
A
823
−10.123
−15.608
26.030
1.00
30.37


ATOM
2325
O
ALA
A
823
−9.919
−16.179
24.959
1.00
30.71


ATOM
2326
N
ILE
A
824
−9.671
−14.385
26.281
1.00
26.40


ATOM
2327
CA
ILE
A
824
−8.968
−13.624
25.250
1.00
25.53


ATOM
2328
CB
ILE
A
824
−9.761
−12.325
24.898
1.00
28.97


ATOM
2329
CG2
ILE
A
824
−8.978
−11.487
23.899
1.00
29.02


ATOM
2330
CG1
ILE
A
824
−11.154
−12.665
24.357
1.00
29.19


ATOM
2331
CD1
ILE
A
824
−11.151
−13.353
23.013
1.00
29.99


ATOM
2332
C
ILE
A
824
−7.537
−13.185
25.546
1.00
27.07


ATOM
2333
O
ILE
A
824
−6.639
−13.358
24.722
1.00
26.42


ATOM
2334
N
CYS
A
825
−7.324
−12.617
26.726
1.00
24.64


ATOM
2335
CA
CYS
A
825
−6.020
−12.070
27.075
1.00
24.29


ATOM
2336
CB
CYS
A
825
−6.207
−11.003
28.145
1.00
22.55


ATOM
2337
SG
CYS
A
825
−7.489
−9.813
27.703
1.00
21.61


ATOM
2338
C
CYS
A
825
−4.878
−12.979
27.493
1.00
23.81


ATOM
2339
O
CYS
A
825
−3.776
−12.856
26.971
1.00
23.60


ATOM
2340
N
LEU
A
826
−5.131
−13.866
28.448
1.00
25.10


ATOM
2341
CA
LEU
A
826
−4.098
−14.761
28.955
1.00
26.70


ATOM
2342
CB
LEU
A
826
−4.727
−15.770
29.921
1.00
38.73


ATOM
2343
CG
LEU
A
826
−4.228
−15.764
31.370
1.00
39.48


ATOM
2344
CD1
LEU
A
826
−4.024
−14.343
31.867
1.00
38.99


ATOM
2345
CD2
LEU
A
826
−5.230
−16.498
32.243
1.00
39.26


ATOM
2346
C
LEU
A
826
−3.301
−15.492
27.873
1.00
25.78


ATOM
2347
O
LEU
A
826
−2.072
−15.427
27.854
1.00
26.14


ATOM
2348
N
GLN
A
827
−3.993
−16.179
26.972
1.00
26.44


ATOM
2349
CA
GLN
A
827
−3.308
−16.919
25.920
1.00
26.16


ATOM
2350
CB
GLN
A
827
−4.313
−17.689
25.065
1.00
31.94


ATOM
2351
CG
GLN
A
827
−5.146
−18.687
25.839
1.00
32.38


ATOM
2352
CD
GLN
A
827
−6.176
−19.374
24.967
1.00
33.15


ATOM
2353
OE1
GLN
A
827
−5.844
−20.233
24.146
1.00
33.30


ATOM
2354
NE2
GLN
A
827
−7.437
−18.989
25.130
1.00
33.01


ATOM
2355
C
GLN
A
827
−2.483
−16.005
25.034
1.00
26.24


ATOM
2356
O
GLN
A
827
−1.394
−16.372
24.593
1.00
26.27


ATOM
2357
N
LEU
A
828
−2.995
−14.811
24.761
1.00
23.62


ATOM
2358
CA
LEU
A
828
−2.256
−13.887
23.912
1.00
23.54


ATOM
2359
CB
LEU
A
828
−3.121
−12.678
23.547
1.00
27.47


ATOM
2360
CG
LEU
A
828
−2.393
−11.621
22.705
1.00
27.18


ATOM
2361
CD1
LEU
A
828
−1.769
−12.267
21.474
1.00
28.21


ATOM
2362
CD2
LEU
A
828
−3.361
−10.534
22.293
1.00
27.24


ATOM
2363
C
LEU
A
828
−0.948
−13.398
24.525
1.00
24.07


ATOM
2364
O
LEU
A
828
0.089
−13.389
23.863
1.00
23.90


ATOM
2365
N
TYR
A
829
−0.984
−12.979
25.785
1.00
22.58


ATOM
2366
CA
TYR
A
829
0.232
−12.492
26.410
1.00
23.51


ATOM
2367
CB
TYR
A
829
−0.108
−11.655
27.652
1.00
22.13


ATOM
2368
CG
TYR
A
829
−0.797
−10.352
27.273
1.00
22.65


ATOM
2369
CD1
TYR
A
829
−0.133
−9.395
26.504
1.00
21.70


ATOM
2370
CE1
TYR
A
829
−0.778
−8.224
26.084
1.00
22.06


ATOM
2371
CD2
TYR
A
829
−2.126
−10.110
27.622
1.00
22.96


ATOM
2372
CE2
TYR
A
829
−2.782
−8.939
27.202
1.00
21.69


ATOM
2373
CZ
TYR
A
829
−2.096
−8.009
26.437
1.00
22.78


ATOM
2374
OH
TYR
A
829
−2.717
−6.850
26.023
1.00
20.96


ATOM
2375
C
TYR
A
829
1.171
−13.653
26.725
1.00
22.44


ATOM
2376
O
TYR
A
829
2.378
−13.469
26.803
1.00
23.40


ATOM
2377
N
GLU
A
830
0.615
−14.851
26.877
1.00
26.33


ATOM
2378
CA
GLU
A
830
1.451
−16.025
27.127
1.00
27.63


ATOM
2379
CB
GLU
A
830
0.602
−17.227
27.539
1.00
34.99


ATOM
2380
CG
GLU
A
830
0.034
−17.110
28.941
1.00
35.86


ATOM
2381
CD
GLU
A
830
−0.865
−18.266
29.318
1.00
36.17


ATOM
2382
OE1
GLU
A
830
−1.246
−18.349
30.507
1.00
35.89


ATOM
2383
OE2
GLU
A
830
−1.195
−19.084
28.430
1.00
36.49


ATOM
2384
C
GLU
A
830
2.186
−16.326
25.826
1.00
26.91


ATOM
2385
O
GLU
A
830
3.383
−16.614
25.827
1.00
27.95


ATOM
2386
N
ALA
A
831
1.465
−16.235
24.711
1.00
26.22


ATOM
2387
CA
ALA
A
831
2.056
−16.489
23.398
1.00
26.36


ATOM
2388
CB
ALA
A
831
0.965
−16.533
22.328
1.00
20.71


ATOM
2389
C
ALA
A
831
3.091
−15.425
23.044
1.00
25.92


ATOM
2390
O
ALA
A
831
4.108
−15.725
22.429
1.00
26.14


ATOM
2391
N
LEU
A
832
2.833
−14.180
23.432
1.00
25.86


ATOM
2392
CA
LEU
A
832
3.767
−13.096
23.138
1.00
24.48


ATOM
2393
CB
LEU
A
832
3.127
−11.738
23.447
1.00
23.29


ATOM
2394
CG
LEU
A
832
4.036
−10.513
23.333
1.00
22.75


ATOM
2395
CD1
LEU
A
832
4.597
−10.387
21.926
1.00
22.85


ATOM
2396
CD2
LEU
A
832
3.237
−9.268
23.701
1.00
23.24


ATOM
2397
C
LEU
A
832
5.056
−13.238
23.936
1.00
25.65


ATOM
2398
O
LEU
A
832
6.140
−12.902
23.454
1.00
25.17


ATOM
2399
N
THR
A
833
4.931
−13.720
25.166
1.00
26.35


ATOM
2400
CA
THR
A
833
6.092
−13.910
26.021
1.00
27.50


ATOM
2401
CB
THR
A
833
5.654
−14.289
27.446
1.00
28.58


ATOM
2402
OG1
THR
A
833
4.872
−13.218
27.994
1.00
28.28


ATOM
2403
CG2
THR
A
833
6.868
−14.531
28.339
1.00
28.51


ATOM
2404
C
THR
A
833
6.968
−15.007
25.418
1.00
28.22


ATOM
2405
O
THR
A
833
8.197
−14.977
25.540
1.00
28.01


ATOM
2406
N
HIS
A
834
6.333
−15.964
24.750
1.00
32.53


ATOM
2407
CA
HIS
A
834
7.080
−17.044
24.117
1.00
33.13


ATOM
2408
CB
HIS
A
834
6.131
−18.053
23.473
1.00
41.03


ATOM
2409
CG
HIS
A
834
6.833
−19.200
22.820
1.00
41.66


ATOM
2410
CD2
HIS
A
834
7.017
−19.505
21.514
1.00
41.45


ATOM
2411
ND1
HIS
A
834
7.497
−20.170
23.538
1.00
41.66


ATOM
2412
CE1
HIS
A
834
8.060
−21.024
22.702
1.00
41.76


ATOM
2413
NE2
HIS
A
834
7.785
−20.643
21.467
1.00
41.58


ATOM
2414
C
HIS
A
834
7.979
−16.433
23.050
1.00
33.02


ATOM
2415
O
HIS
A
834
9.179
−16.701
23.003
1.00
33.90


ATOM
2416
N
VAL
A
835
7.390
−15.603
22.195
1.00
34.00


ATOM
2417
CA
VAL
A
835
8.142
−14.943
21.136
1.00
33.47


ATOM
2418
CB
VAL
A
835
7.235
−14.027
20.282
1.00
34.13


ATOM
2419
CG1
VAL
A
835
8.082
−13.226
19.304
1.00
33.51


ATOM
2420
CG2
VAL
A
835
6.213
−14.863
19.533
1.00
33.76


ATOM
2421
C
VAL
A
835
9.278
−14.105
21.705
1.00
34.04


ATOM
2422
O
VAL
A
835
10.373
−14.076
21.147
1.00
33.58


ATOM
2423
N
SER
A
836
9.017
−13.416
22.813
1.00
31.52


ATOM
2424
CA
SER
A
836
10.041
−12.585
23.436
1.00
32.24


ATOM
2425
CB
SER
A
836
10.016
−11.176
22.838
1.00
33.50


ATOM
2426
OG
SER
A
836
11.125
−10.416
23.284
1.00
33.58


ATOM
2427
C
SER
A
836
9.861
−12.503
24.949
1.00
31.70


ATOM
2428
O
SER
A
836
8.937
−11.856
25.447
1.00
30.73


ATOM
2429
N
GLU
A
837
10.758
−13.168
25.668
1.00
32.13


ATOM
2430
CA
GLU
A
837
10.742
−13.209
27.126
1.00
32.75


ATOM
2431
CB
GLU
A
837
12.035
−13.862
27.624
1.00
50.88


ATOM
2432
CG
GLU
A
837
13.295
−13.194
27.082
1.00
51.44


ATOM
2433
CD
GLU
A
837
14.564
−13.981
27.368
1.00
51.73


ATOM
2434
OE1
GLU
A
837
14.863
−14.226
28.558
1.00
51.76


ATOM
2435
OE2
GLU
A
837
15.264
−14.349
26.399
1.00
51.58


ATOM
2436
C
GLU
A
837
10.579
−11.836
27.779
1.00
32.06


ATOM
2437
O
GLU
A
837
9.916
−11.702
28.808
1.00
32.57


ATOM
2438
N
ASP
A
838
11.185
−10.821
27.175
1.00
27.93


ATOM
2439
CA
ASP
A
838
11.135
−9.463
27.699
1.00
28.49


ATOM
2440
CB
ASP
A
838
12.085
−8.574
26.896
1.00
35.78


ATOM
2441
CG
ASP
A
838
13.511
−9.093
26.908
1.00
37.30


ATOM
2442
OD1
ASP
A
838
14.167
−9.014
27.969
1.00
36.40


ATOM
2443
OD2
ASP
A
838
13.971
−9.589
25.857
1.00
37.49


ATOM
2444
C
ASP
A
838
9.738
−8.838
27.723
1.00
27.26


ATOM
2445
O
ASP
A
838
9.570
−7.716
28.202
1.00
27.48


ATOM
2446
N
CYS
A
839
8.740
−9.550
27.207
1.00
26.97


ATOM
2447
CA
CYS
A
839
7.372
−9.035
27.207
1.00
26.65


ATOM
2448
CB
CYS
A
839
6.668
−9.360
25.882
1.00
26.64


ATOM
2449
SG
CYS
A
839
7.139
−8.301
24.485
1.00
26.65


ATOM
2450
C
CYS
A
839
6.586
−9.638
28.365
1.00
27.57


ATOM
2451
O
CYS
A
839
5.373
−9.461
28.471
1.00
26.86


ATOM
2452
N
PHE
A
840
7.282
−10.352
29.243
1.00
26.10


ATOM
2453
CA
PHE
A
840
6.626
−10.976
30.385
1.00
26.52


ATOM
2454
CB
PHE
A
840
7.653
−11.679
31.281
1.00
35.43


ATOM
2455
CG
PHE
A
840
7.045
−12.344
32.485
1.00
35.52


ATOM
2456
CD1
PHE
A
840
6.211
−13.450
32.340
1.00
35.69


ATOM
2457
CD2
PHE
A
840
7.273
−11.842
33.762
1.00
35.56


ATOM
2458
CE1
PHE
A
840
5.610
−14.046
33.450
1.00
35.99


ATOM
2459
CE2
PHE
A
840
6.678
−12.429
34.878
1.00
35.60


ATOM
2460
CZ
PHE
A
840
5.843
−13.533
34.722
1.00
35.62


ATOM
2461
C
PHE
A
840
5.810
−9.991
31.227
1.00
25.53


ATOM
2462
O
PHE
A
840
4.726
−10.332
31.698
1.00
26.75


ATOM
2463
N
PRO
A
841
6.311
−8.757
31.422
1.00
24.00


ATOM
2464
CD
PRO
A
841
7.585
−8.177
30.965
1.00
27.23


ATOM
2465
CA
PRO
A
841
5.567
−7.783
32.225
1.00
23.95


ATOM
2466
CB
PRO
A
841
6.345
−6.491
32.002
1.00
26.33


ATOM
2467
CG
PRO
A
841
7.751
−6.988
31.890
1.00
27.03


ATOM
2468
C
PRO
A
841
4.104
−7.662
31.821
1.00
24.02


ATOM
2469
O
PRO
A
841
3.238
−7.446
32.667
1.00
23.76


ATOM
2470
N
LEU
A
842
3.826
−7.809
30.531
1.00
23.41


ATOM
2471
CA
LEU
A
842
2.447
−7.711
30.069
1.00
22.32


ATOM
2472
CB
LEU
A
842
2.400
−7.647
28.540
1.00
22.25


ATOM
2473
CG
LEU
A
842
3.064
−6.397
27.957
1.00
22.19


ATOM
2474
CD1
LEU
A
842
3.184
−6.527
26.442
1.00
21.97


ATOM
2475
CD2
LEU
A
842
2.255
−5.154
28.349
1.00
23.44


ATOM
2476
C
LEU
A
842
1.633
−8.888
30.590
1.00
23.15


ATOM
2477
O
LEU
A
842
0.508
−8.714
31.048
1.00
22.28


ATOM
2478
N
LEU
A
843
2.210
−10.085
30.537
1.00
20.37


ATOM
2479
CA
LEU
A
843
1.528
−11.277
31.019
1.00
22.54


ATOM
2480
CB
LEU
A
843
2.369
−12.517
30.716
1.00
30.62


ATOM
2481
CG
LEU
A
843
1.666
−13.867
30.542
1.00
32.10


ATOM
2482
CD1
LEU
A
843
2.718
−14.960
30.647
1.00
31.42


ATOM
2483
CD2
LEU
A
843
0.586
−14.078
31.579
1.00
31.97


ATOM
2484
C
LEU
A
843
1.338
−11.162
32.531
1.00
20.83


ATOM
2485
O
LEU
A
843
0.252
−11.406
33.057
1.00
22.49


ATOM
2486
N
ASP
A
844
2.410
−10.791
33.222
1.00
25.10


ATOM
2487
CA
ASP
A
844
2.381
−10.650
34.673
1.00
25.84


ATOM
2488
CB
ASP
A
844
3.756
−10.204
35.177
1.00
33.41


ATOM
2489
CG
ASP
A
844
3.889
−10.316
36.680
1.00
33.77


ATOM
2490
OD1
ASP
A
844
3.499
−11.367
37.233
1.00
33.62


ATOM
2491
OD2
ASP
A
844
4.392
−9.360
37.305
1.00
34.08


ATOM
2492
C
ASP
A
844
1.306
−9.667
35.129
1.00
25.11


ATOM
2493
O
ASP
A
844
0.517
−9.976
36.020
1.00
25.50


ATOM
2494
N
GLY
A
845
1.272
−8.492
34.505
1.00
23.99


ATOM
2495
CA
GLY
A
845
0.282
−7.488
34.861
1.00
24.47


ATOM
2496
C
GLY
A
845
−1.141
−7.954
34.612
1.00
24.36


ATOM
2497
O
GLY
A
845
−2.057
−7.628
35.366
1.00
23.75


ATOM
2498
N
CYS
A
846
−1.325
−8.720
33.542
1.00
23.31


ATOM
2499
CA
CYS
A
846
−2.631
−9.252
33.188
1.00
22.27


ATOM
2500
CB
CYS
A
846
−2.556
−9.961
31.833
1.00
24.57


ATOM
2501
SG
CYS
A
846
−4.118
−10.668
31.278
1.00
23.77


ATOM
2502
C
CYS
A
846
−3.093
−10.236
34.255
1.00
23.19


ATOM
2503
O
CYS
A
846
−4.237
−10.197
34.699
1.00
23.71


ATOM
2504
N
ARG
A
847
−2.197
−11.126
34.669
1.00
25.45


ATOM
2505
CA
ARG
A
847
−2.554
−12.103
35.681
1.00
26.33


ATOM
2506
CB
ARG
A
847
−1.454
−13.170
35.788
1.00
44.92


ATOM
2507
CG
ARG
A
847
−1.334
−13.973
34.489
1.00
45.65


ATOM
2508
CD
ARG
A
847
−0.520
−15.257
34.590
1.00
45.89


ATOM
2509
NE
ARG
A
847
0.924
−15.037
34.557
1.00
45.99


ATOM
2510
CZ
ARG
A
847
1.805
−15.950
34.155
1.00
45.73


ATOM
2511
NH1
ARG
A
847
1.392
−17.142
33.743
1.00
45.92


ATOM
2512
NH2
ARG
A
847
3.102
−15.678
34.178
1.00
45.71


ATOM
2513
C
ARG
A
847
−2.839
−11.434
37.021
1.00
25.65


ATOM
2514
O
ARG
A
847
−3.673
−11.909
37.794
1.00
25.84


ATOM
2515
N
LYS
A
848
−2.172
−10.319
37.291
1.00
27.18


ATOM
2516
CA
LYS
A
848
−2.408
−9.606
38.540
1.00
27.41


ATOM
2517
CB
LYS
A
848
−1.344
−8.529
38.755
1.00
29.68


ATOM
2518
CG
LYS
A
848
0.011
−9.082
39.165
1.00
30.06


ATOM
2519
CD
LYS
A
848
1.023
−7.964
39.328
1.00
30.03


ATOM
2520
CE
LYS
A
848
2.406
−8.518
39.644
1.00
30.39


ATOM
2521
NZ
LYS
A
848
3.450
−7.453
39.583
1.00
30.98


ATOM
2522
C
LYS
A
848
−3.796
−8.974
38.514
1.00
27.81


ATOM
2523
O
LYS
A
848
−4.515
−8.996
39.511
1.00
28.26


ATOM
2524
N
ASN
A
849
−4.179
−8.412
37.372
1.00
28.20


ATOM
2525
CA
ASN
A
849
−5.498
−7.807
37.270
1.00
26.64


ATOM
2526
CB
ASN
A
849
−5.640
−7.028
35.961
1.00
26.08


ATOM
2527
CG
ASN
A
849
−4.970
−5.674
36.027
1.00
25.73


ATOM
2528
OD1
ASN
A
849
−4.993
−5.012
37.067
1.00
26.13


ATOM
2529
ND2
ASN
A
849
−4.382
−5.247
34.923
1.00
26.48


ATOM
2530
C
ASN
A
849
−6.572
−8.875
37.372
1.00
27.18


ATOM
2531
O
ASN
A
849
−7.679
−8.612
37.844
1.00
26.84


ATOM
2532
N
ARG
A
850
−6.244
−10.086
36.934
1.00
25.96


ATOM
2533
CA
ARG
A
850
−7.194
−11.177
37.017
1.00
26.10


ATOM
2534
CB
ARG
A
850
−6.640
−12.431
36.338
1.00
38.03


ATOM
2535
CG
ARG
A
850
−7.583
−13.607
36.453
1.00
38.77


ATOM
2536
CD
ARG
A
850
−6.976
−14.898
35.941
1.00
38.89


ATOM
2537
NE
ARG
A
850
−7.798
−16.037
36.336
1.00
39.62


ATOM
2538
CZ
ARG
A
850
−9.075
−16.181
36.003
1.00
39.00


ATOM
2539
NH1
ARG
A
850
−9.669
−15.255
35.264
1.00
40.11


ATOM
2540
NH2
ARG
A
850
−9.765
−17.235
36.417
1.00
38.97


ATOM
2541
C
ARG
A
850
−7.513
−11.488
38.480
1.00
25.71


ATOM
2542
O
ARG
A
850
−8.675
−11.647
38.849
1.00
26.96


ATOM
2543
N
GLN
A
851
−6.476
−11.564
39.311
1.00
29.93


ATOM
2544
CA
GLN
A
851
−6.659
−11.860
40.728
1.00
30.30


ATOM
2545
CB
GLN
A
851
−5.294
−11.993
41.413
1.00
53.42


ATOM
2546
CG
GLN
A
851
−4.938
−10.873
42.375
1.00
54.29


ATOM
2547
CD
GLN
A
851
−3.479
−10.910
42.794
1.00
54.54


ATOM
2548
OE1
GLN
A
851
−3.071
−10.204
43.717
1.00
54.48


ATOM
2549
NE2
GLN
A
851
−2.681
−11.724
42.106
1.00
54.48


ATOM
2550
C
GLN
A
851
−7.493
−10.765
41.381
1.00
29.94


ATOM
2551
O
GLN
A
851
−8.377
−11.042
42.189
1.00
30.04


ATOM
2552
N
LYS
A
852
−7.213
−9.518
41.017
1.00
27.54


ATOM
2553
CA
LYS
A
852
−7.950
−8.381
41.557
1.00
27.65


ATOM
2554
CB
LYS
A
852
−7.378
−7.075
40.998
1.00
40.34


ATOM
2555
CG
LYS
A
852
−6.005
−6.705
41.527
1.00
40.79


ATOM
2556
CD
LYS
A
852
−6.096
−6.263
42.977
1.00
40.88


ATOM
2557
CE
LYS
A
852
−4.760
−5.766
43.497
1.00
40.95


ATOM
2558
NZ
LYS
A
852
−4.883
−5.208
44.879
1.00
41.45


ATOM
2559
C
LYS
A
852
−9.433
−8.470
41.204
1.00
27.70


ATOM
2560
O
LYS
A
852
−10.301
−8.360
42.075
1.00
27.95


ATOM
2561
N
TRP
A
853
−9.722
−8.655
39.920
1.00
24.75


ATOM
2562
CA
TRP
A
853
−11.103
−8.747
39.467
1.00
25.36


ATOM
2563
CB
TRP
A
853
−11.150
−8.857
37.940
1.00
23.18


ATOM
2564
CG
TRP
A
853
−10.967
−7.544
37.240
1.00
23.11


ATOM
2565
CD2
TRP
A
853
−11.771
−6.368
37.399
1.00
22.95


ATOM
2566
CE2
TRP
A
853
−11.244
−5.382
36.534
1.00
22.63


ATOM
2567
CE3
TRP
A
853
−12.886
−6.052
38.189
1.00
23.00


ATOM
2568
CD1
TRP
A
853
−10.013
−7.233
36.312
1.00
23.06


ATOM
2569
NE1
TRP
A
853
−10.173
−5.937
35.884
1.00
22.64


ATOM
2570
CZ2
TRP
A
853
−11.794
−4.101
36.436
1.00
22.97


ATOM
2571
CZ3
TRP
A
853
−13.433
−4.778
38.092
1.00
22.86


ATOM
2572
CH2
TRP
A
853
−12.886
−3.818
37.220
1.00
22.99


ATOM
2573
C
TRP
A
853
−11.816
−9.931
40.101
1.00
24.85


ATOM
2574
O
TRP
A
853
−12.976
−9.824
40.505
1.00
24.94


ATOM
2575
N
GLN
A
854
−11.107
−11.051
40.202
1.00
28.90


ATOM
2576
CA
GLN
A
854
−11.662
−12.264
40.785
1.00
30.44


ATOM
2577
CB
GLN
A
854
−10.673
−13.419
40.625
1.00
37.29


ATOM
2578
CG
GLN
A
854
−11.183
−14.749
41.152
1.00
37.88


ATOM
2579
CD
GLN
A
854
−12.554
−15.102
40.608
1.00
38.02


ATOM
2580
OE1
GLN
A
854
−12.812
−14.978
39.411
1.00
38.44


ATOM
2581
NE2
GLN
A
854
−13.439
−15.557
41.487
1.00
38.37


ATOM
2582
C
GLN
A
854
−12.014
−12.081
42.257
1.00
30.52


ATOM
2583
O
GLN
A
854
−12.994
−12.650
42.736
1.00
31.44


ATOM
2584
N
ALA
A
855
−11.219
−11.288
42.969
1.00
32.15


ATOM
2585
CA
ALA
A
855
−11.465
−11.039
44.388
1.00
32.96


ATOM
2586
CB
ALA
A
855
−10.282
−10.300
45.003
1.00
27.28


ATOM
2587
C
ALA
A
855
−12.747
−10.231
44.572
1.00
33.38


ATOM
2588
O
ALA
A
855
−13.473
−10.411
45.551
1.00
33.79


ATOM
2589
N
LEU
A
856
−13.020
−9.338
43.627
1.00
34.25


ATOM
2590
CA
LEU
A
856
−14.223
−8.517
43.685
1.00
34.81


ATOM
2591
CB
LEU
A
856
−14.102
−7.325
42.732
1.00
29.75


ATOM
2592
CG
LEU
A
856
−12.988
−6.310
43.001
1.00
29.61


ATOM
2593
CD1
LEU
A
856
−12.998
−5.251
41.926
1.00
29.93


ATOM
2594
CD2
LEU
A
856
−13.180
−5.679
44.373
1.00
29.63


ATOM
2595
C
LEU
A
856
−15.455
−9.339
43.315
1.00
35.51


ATOM
2596
O
LEU
A
856
−16.560
−9.063
43.786
1.00
35.20


ATOM
2597
N
ALA
A
857
−15.258
−10.358
42.484
1.00
39.71


ATOM
2598
CA
ALA
A
857
−16.354
−11.208
42.030
1.00
40.78


ATOM
2599
CB
ALA
A
857
−16.044
−11.745
40.640
1.00
32.69


ATOM
2600
C
ALA
A
857
−16.710
−12.369
42.956
1.00
41.78


ATOM
2601
O
ALA
A
857
−17.849
−12.833
42.951
1.00
41.70


ATOM
2602
N
GLU
A
858
−15.748
−12.847
43.738
1.00
51.08


ATOM
2603
CA
GLU
A
858
−16.005
−13.967
44.639
1.00
52.63


ATOM
2604
CB
GLU
A
858
−14.710
−14.741
44.909
1.00
56.18


ATOM
2605
CG
GLU
A
858
−13.570
−13.890
45.433
1.00
56.32


ATOM
2606
CD
GLU
A
858
−12.341
−14.710
45.778
1.00
56.60


ATOM
2607
OE1
GLU
A
858
−11.844
−15.446
44.898
1.00
56.57


ATOM
2608
OE2
GLU
A
858
−11.871
−14.614
46.930
1.00
56.45


ATOM
2609
C
GLU
A
858
−16.635
−13.536
45.960
1.00
53.20


ATOM
2610
O
GLU
A
858
−15.986
−13.709
47.014
1.00
53.41


ATOM
2611
OXT
GLU
A
858
−17.776
−13.032
45.927
1.00
56.42


TER


ATOM
2613
CB
THR
B
537
25.255
66.687
12.776
1.00
47.44


ATOM
2614
OG1
THR
B
537
24.336
67.782
12.890
1.00
47.61


ATOM
2615
CG2
THR
B
537
25.471
66.356
11.307
1.00
47.41


ATOM
2616
C
THR
B
537
24.866
65.684
15.026
1.00
50.26


ATOM
2617
O
THR
B
537
24.138
65.096
15.828
1.00
50.63


ATOM
2618
N
THR
B
537
23.266
65.220
13.181
1.00
50.23


ATOM
2619
CA
THR
B
537
24.695
65.462
13.530
1.00
50.15


ATOM
2620
N
ARG
B
538
25.822
66.534
15.395
1.00
48.27


ATOM
2621
CA
ARG
B
538
26.099
66.827
16.801
1.00
48.37


ATOM
2622
CB
ARG
B
538
24.804
67.211
17.532
1.00
55.34


ATOM
2623
CG
ARG
B
538
24.941
67.437
19.040
1.00
55.68


ATOM
2624
CD
ARG
B
538
25.783
68.664
19.378
1.00
55.76


ATOM
2625
NE
ARG
B
538
25.806
68.927
20.818
1.00
55.63


ATOM
2626
CZ
ARG
B
538
26.529
69.882
21.401
1.00
55.83


ATOM
2627
NH1
ARG
B
538
27.302
70.677
20.672
1.00
55.58


ATOM
2628
NH2
ARG
B
538
26.481
70.040
22.718
1.00
55.68


ATOM
2629
C
ARG
B
538
26.707
65.579
17.427
1.00
48.47


ATOM
2630
O
ARG
B
538
27.882
65.561
17.796
1.00
47.96


ATOM
2631
N
GLU
B
539
25.895
64.534
17.532
1.00
51.41


ATOM
2632
CA
GLU
B
539
26.331
63.265
18.096
1.00
50.79


ATOM
2633
CB
GLU
B
539
25.162
62.280
18.093
1.00
45.27


ATOM
2634
CG
GLU
B
539
25.499
60.877
18.559
1.00
45.43


ATOM
2635
CD
GLU
B
539
24.274
59.985
18.595
1.00
45.09


ATOM
2636
OE1
GLU
B
539
23.553
59.931
17.576
1.00
45.02


ATOM
2637
OE2
GLU
B
539
24.032
59.340
19.636
1.00
45.34


ATOM
2638
C
GLU
B
539
27.490
62.719
17.268
1.00
49.89


ATOM
2639
O
GLU
B
539
28.360
62.015
17.783
1.00
51.14


ATOM
2640
N
LEU
B
540
27.493
63.056
15.981
1.00
35.39


ATOM
2641
CA
LEU
B
540
28.537
62.617
15.066
1.00
34.61


ATOM
2642
CB
LEU
B
540
28.047
62.729
13.621
1.00
33.85


ATOM
2643
CG
LEU
B
540
29.094
62.491
12.529
1.00
33.88


ATOM
2644
CD1
LEU
B
540
29.755
61.135
12.722
1.00
33.93


ATOM
2645
CD2
LEU
B
540
28.436
62.579
11.166
1.00
34.03


ATOM
2646
C
LEU
B
540
29.798
63.451
15.245
1.00
33.92


ATOM
2647
O
LEU
B
540
30.910
62.923
15.296
1.00
33.74


ATOM
2648
N
GLN
B
541
29.620
64.763
15.328
1.00
38.91


ATOM
2649
CA
GLN
B
541
30.747
65.664
15.511
1.00
38.96


ATOM
2650
CB
GLN
B
541
30.265
67.110
15.475
1.00
49.53


ATOM
2651
CG
GLN
B
541
29.654
67.501
14.147
1.00
49.81


ATOM
2652
CD
GLN
B
541
29.118
68.910
14.156
1.00
49.94


ATOM
2653
OE1
GLN
B
541
28.185
69.225
14.896
1.00
50.34


ATOM
2654
NE2
GLN
B
541
29.707
69.774
13.336
1.00
50.07


ATOM
2655
C
GLN
B
541
31.389
65.356
16.850
1.00
38.55


ATOM
2656
O
GLN
B
541
32.613
65.343
16.980
1.00
39.00


ATOM
2657
N
SER
B
542
30.551
65.099
17.847
1.00
32.80


ATOM
2658
CA
SER
B
542
31.034
64.772
19.177
1.00
32.42


ATOM
2659
CB
SER
B
542
29.861
64.645
20.153
1.00
41.30


ATOM
2660
OG
SER
B
542
29.144
65.863
20.263
1.00
42.04


ATOM
2661
C
SER
B
542
31.789
63.456
19.113
1.00
30.70


ATOM
2662
O
SER
B
542
32.848
63.305
19.714
1.00
31.49


ATOM
2663
N
LEU
B
543
31.233
62.505
18.370
1.00
31.05


ATOM
2664
CA
LEU
B
543
31.841
61.188
18.228
1.00
30.13


ATOM
2665
CB
LEU
B
543
30.895
60.257
17.460
1.00
31.49


ATOM
2666
CG
LEU
B
543
30.924
58.757
17.783
1.00
32.02


ATOM
2667
CD1
LEU
B
543
30.315
57.991
16.615
1.00
31.51


ATOM
2668
CD2
LEU
B
543
32.336
58.278
18.036
1.00
31.28


ATOM
2669
C
LEU
B
543
33.175
61.259
17.492
1.00
29.52


ATOM
2670
O
LEU
B
543
34.183
60.737
17.963
1.00
29.71


ATOM
2671
N
ALA
B
544
33.175
61.911
16.335
1.00
27.41


ATOM
2672
CA
ALA
B
544
34.374
62.027
15.522
1.00
26.77


ATOM
2673
CB
ALA
B
544
34.040
62.722
14.213
1.00
32.00


ATOM
2674
C
ALA
B
544
35.529
62.748
16.214
1.00
27.56


ATOM
2675
O
ALA
B
544
36.685
62.357
16.075
1.00
27.33


ATOM
2676
N
ALA
B
545
35.214
63.801
16.960
1.00
29.78


ATOM
2677
CA
ALA
B
545
36.241
64.580
17.642
1.00
29.66


ATOM
2678
CB
ALA
B
545
35.723
65.990
17.905
1.00
33.66


ATOM
2679
C
ALA
B
545
36.731
63.962
18.948
1.00
30.65


ATOM
2680
O
ALA
B
545
37.829
64.272
19.417
1.00
29.67


ATOM
2681
N
ALA
B
546
35.921
63.090
19.537
1.00
29.20


ATOM
2682
CA
ALA
B
546
36.284
62.464
20.801
1.00
30.23


ATOM
2683
CB
ALA
B
546
35.090
61.705
21.364
1.00
34.60


ATOM
2684
C
ALA
B
546
37.493
61.538
20.713
1.00
29.49


ATOM
2685
O
ALA
B
546
37.779
60.959
19.664
1.00
29.95


ATOM
2686
N
VAL
B
547
38.219
61.423
21.820
1.00
29.24


ATOM
2687
CA
VAL
B
547
39.377
60.543
21.872
1.00
29.27


ATOM
2688
CB
VAL
B
547
40.359
60.950
22.990
1.00
28.05


ATOM
2689
CG1
VAL
B
547
41.419
59.877
23.158
1.00
27.67


ATOM
2690
CG2
VAL
B
547
41.010
62.282
22.650
1.00
28.10


ATOM
2691
C
VAL
B
547
38.845
59.151
22.179
1.00
29.34


ATOM
2692
O
VAL
B
547
38.009
58.988
23.066
1.00
30.26


ATOM
2693
N
VAL
B
548
39.324
58.152
21.443
1.00
28.29


ATOM
2694
CA
VAL
B
548
38.879
56.778
21.653
1.00
27.44


ATOM
2695
CB
VAL
B
548
38.971
55.953
20.349
1.00
28.22


ATOM
2696
CG1
VAL
B
548
38.545
54.510
20.613
1.00
27.84


ATOM
2697
CG2
VAL
B
548
38.100
56.585
19.271
1.00
28.24


ATOM
2698
C
VAL
B
548
39.721
56.099
22.724
1.00
26.75


ATOM
2699
O
VAL
B
548
40.903
55.822
22.518
1.00
26.81


ATOM
2700
N
PRO
B
549
39.121
55.826
23.890
1.00
24.59


ATOM
2701
CD
PRO
B
549
37.783
56.267
24.317
1.00
25.72


ATOM
2702
CA
PRO
B
549
39.830
55.172
24.995
1.00
25.08


ATOM
2703
CB
PRO
B
549
38.764
55.089
26.081
1.00
25.73


ATOM
2704
CG
PRO
B
549
37.932
56.312
25.818
1.00
26.01


ATOM
2705
C
PRO
B
549
40.362
53.795
24.600
1.00
26.03


ATOM
2706
O
PRO
B
549
39.894
53.197
23.628
1.00
24.91


ATOM
2707
N
SER
B
550
41.334
53.298
25.361
1.00
27.34


ATOM
2708
CA
SER
B
550
41.935
51.997
25.088
1.00
27.02


ATOM
2709
CB
SER
B
550
43.224
51.821
25.896
1.00
31.88


ATOM
2710
OG
SER
B
550
42.943
51.600
27.267
1.00
31.82


ATOM
2711
C
SER
B
550
40.975
50.873
25.440
1.00
26.64


ATOM
2712
O
SER
B
550
40.052
51.062
26.229
1.00
26.84


ATOM
2713
N
ALA
B
551
41.193
49.701
24.853
1.00
26.78


ATOM
2714
CA
ALA
B
551
40.336
48.558
25.135
1.00
27.11


ATOM
2715
CB
ALA
B
551
40.790
47.342
24.317
1.00
24.60


ATOM
2716
C
ALA
B
551
40.385
48.244
26.630
1.00
27.04


ATOM
2717
O
ALA
B
551
39.373
47.895
27.237
1.00
26.84


ATOM
2718
N
GLN
B
552
41.573
48.370
27.213
1.00
28.38


ATOM
2719
CA
GLN
B
552
41.775
48.112
28.636
1.00
29.31


ATOM
2720
CB
GLN
B
552
43.233
48.374
29.014
1.00
41.60


ATOM
2721
CG
GLN
B
552
44.219
47.373
28.448
1.00
42.50


ATOM
2722
CD
GLN
B
552
45.646
47.898
28.453
1.00
42.52


ATOM
2723
OE1
GLN
B
552
46.015
48.738
27.626
1.00
42.19


ATOM
2724
NE2
GLN
B
552
46.453
47.413
29.392
1.00
42.63


ATOM
2725
C
GLN
B
552
40.878
49.011
29.475
1.00
28.87


ATOM
2726
O
GLN
B
552
40.149
48.544
30.355
1.00
28.59


ATOM
2727
N
THR
B
553
40.944
50.307
29.196
1.00
30.11


ATOM
2728
CA
THR
B
553
40.145
51.283
29.915
1.00
29.74


ATOM
2729
CB
THR
B
553
40.415
52.713
29.399
1.00
32.61


ATOM
2730
OG1
THR
B
553
41.795
53.047
29.598
1.00
32.65


ATOM
2731
CG2
THR
B
553
39.541
53.718
30.142
1.00
32.91


ATOM
2732
C
THR
B
553
38.655
50.990
29.765
1.00
29.20


ATOM
2733
O
THR
B
553
37.919
50.996
30.747
1.00
29.52


ATOM
2734
N
LEU
B
554
38.225
50.723
28.534
1.00
27.01


ATOM
2735
CA
LEU
B
554
36.820
50.455
28.244
1.00
26.50


ATOM
2736
CB
LEU
B
554
36.562
50.590
26.741
1.00
28.84


ATOM
2737
CG
LEU
B
554
36.851
51.973
26.146
1.00
29.16


ATOM
2738
CD1
LEU
B
554
36.766
51.908
24.630
1.00
29.33


ATOM
2739
CD2
LEU
B
554
35.862
52.992
26.699
1.00
29.62


ATOM
2740
C
LEU
B
554
36.324
49.098
28.733
1.00
26.37


ATOM
2741
O
LEU
B
554
35.117
48.879
28.832
1.00
26.37


ATOM
2742
N
LYS
B
555
37.255
48.192
29.026
1.00
25.28


ATOM
2743
CA
LYS
B
555
36.931
46.857
29.524
1.00
24.39


ATOM
2744
CB
LYS
B
555
36.089
46.958
30.802
1.00
35.97


ATOM
2745
CG
LYS
B
555
36.740
47.722
31.945
1.00
36.48


ATOM
2746
CD
LYS
B
555
35.806
47.781
33.150
1.00
36.95


ATOM
2747
CE
LYS
B
555
36.409
48.579
34.297
1.00
36.81


ATOM
2748
NZ
LYS
B
555
35.499
48.633
35.478
1.00
37.17


ATOM
2749
C
LYS
B
555
36.188
45.975
28.520
1.00
24.71


ATOM
2750
O
LYS
B
555
35.592
44.966
28.905
1.00
24.80


ATOM
2751
N
ILE
B
556
36.229
46.336
27.242
1.00
24.43


ATOM
2752
CA
ILE
B
556
35.520
45.556
26.231
1.00
24.37


ATOM
2753
CB
ILE
B
556
35.436
46.312
24.895
1.00
23.67


ATOM
2754
CG2
ILE
B
556
34.651
47.601
25.078
1.00
24.41


ATOM
2755
CG1
ILE
B
556
36.838
46.637
24.384
1.00
24.28


ATOM
2756
CD1
ILE
B
556
36.847
47.138
22.956
1.00
23.53


ATOM
2757
C
ILE
B
556
36.095
44.167
25.966
1.00
23.99


ATOM
2758
O
ILE
B
556
35.499
43.380
25.235
1.00
23.82


ATOM
2759
N
THR
B
557
37.246
43.860
26.551
1.00
24.82


ATOM
2760
CA
THR
B
557
37.843
42.545
26.345
1.00
25.70


ATOM
2761
CB
THR
B
557
39.381
42.593
26.486
1.00
34.81


ATOM
2762
OG1
THR
B
557
39.901
43.678
25.706
1.00
34.99


ATOM
2763
CG2
THR
B
557
40.001
41.289
25.991
1.00
34.84


ATOM
2764
C
THR
B
557
37.289
41.526
27.344
1.00
25.75


ATOM
2765
O
THR
B
557
37.425
40.318
27.154
1.00
25.95


ATOM
2766
N
ASP
B
558
36.646
42.013
28.400
1.00
21.17


ATOM
2767
CA
ASP
B
558
36.099
41.126
29.423
1.00
20.89


ATOM
2768
CB
ASP
B
558
35.952
41.873
30.750
1.00
39.26


ATOM
2769
CG
ASP
B
558
37.214
42.607
31.147
1.00
40.04


ATOM
2770
OD1
ASP
B
558
38.293
41.981
31.148
1.00
40.44


ATOM
2771
OD2
ASP
B
558
37.124
43.809
31.464
1.00
40.62


ATOM
2772
C
ASP
B
558
34.742
40.543
29.045
1.00
21.50


ATOM
2773
O
ASP
B
558
33.846
41.259
28.594
1.00
21.10


ATOM
2774
N
PHE
B
559
34.586
39.242
29.246
1.00
27.65


ATOM
2775
CA
PHE
B
559
33.322
38.583
28.942
1.00
28.56


ATOM
2776
CB
PHE
B
559
33.474
37.067
29.076
1.00
27.72


ATOM
2777
CG
PHE
B
559
34.269
36.438
27.968
1.00
27.53


ATOM
2778
CD1
PHE
B
559
33.773
36.407
26.670
1.00
27.89


ATOM
2779
CD2
PHE
B
559
35.509
35.863
28.224
1.00
27.40


ATOM
2780
CE1
PHE
B
559
34.499
35.809
25.642
1.00
27.88


ATOM
2781
CE2
PHE
B
559
36.243
35.263
27.202
1.00
27.42


ATOM
2782
CZ
PHE
B
559
35.738
35.236
25.911
1.00
27.16


ATOM
2783
C
PHE
B
559
32.214
39.072
29.872
1.00
28.90


ATOM
2784
O
PHE
B
559
31.030
38.983
29.545
1.00
28.49


ATOM
2785
N
SER
B
560
32.604
39.597
31.029
1.00
29.75


ATOM
2786
CA
SER
B
560
31.638
40.087
32.008
1.00
30.25


ATOM
2787
CB
SER
B
560
32.204
39.924
33.421
1.00
41.19


ATOM
2788
OG
SER
B
560
33.408
40.654
33.576
1.00
41.28


ATOM
2789
C
SER
B
560
31.248
41.543
31.778
1.00
30.07


ATOM
2790
O
SER
B
560
30.571
42.149
32.609
1.00
29.90


ATOM
2791
N
PHE
B
561
31.674
42.098
30.648
1.00
25.27


ATOM
2792
CA
PHE
B
561
31.377
43.484
30.297
1.00
24.91


ATOM
2793
CB
PHE
B
561
31.775
43.744
28.842
1.00
26.48


ATOM
2794
CG
PHE
B
561
31.458
45.135
28.357
1.00
26.42


ATOM
2795
CD1
PHE
B
561
32.349
46.181
28.564
1.00
26.47


ATOM
2796
CD2
PHE
B
561
30.267
45.392
27.679
1.00
26.27


ATOM
2797
CE1
PHE
B
561
32.061
47.468
28.100
1.00
27.33


ATOM
2798
CE2
PHE
B
561
29.970
46.676
27.210
1.00
26.55


ATOM
2799
CZ
PHE
B
561
30.870
47.715
27.421
1.00
26.39


ATOM
2800
C
PHE
B
561
29.904
43.837
30.476
1.00
24.69


ATOM
2801
O
PHE
B
561
29.020
43.040
30.170
1.00
25.07


ATOM
2802
N
SER
B
562
29.652
45.047
30.966
1.00
26.30


ATOM
2803
CA
SER
B
562
28.291
45.538
31.163
1.00
27.46


ATOM
2804
CB
SER
B
562
27.992
45.694
32.655
1.00
44.74


ATOM
2805
OG
SER
B
562
26.657
46.118
32.861
1.00
45.35


ATOM
2806
C
SER
B
562
28.188
46.895
30.476
1.00
25.80


ATOM
2807
O
SER
B
562
29.092
47.721
30.593
1.00
25.80


ATOM
2808
N
ASP
B
563
27.094
47.120
29.756
1.00
22.70


ATOM
2809
CA
ASP
B
563
26.896
48.380
29.050
1.00
23.18


ATOM
2810
CB
ASP
B
563
26.203
48.138
27.709
1.00
23.75


ATOM
2811
CG
ASP
B
563
24.700
47.931
27.861
1.00
23.45


ATOM
2812
OD1
ASP
B
563
24.282
46.853
28.330
1.00
23.97


ATOM
2813
OD2
ASP
B
563
23.936
48.858
27.522
1.00
24.26


ATOM
2814
C
ASP
B
563
26.014
49.330
29.847
1.00
22.69


ATOM
2815
O
ASP
B
563
25.889
50.504
29.503
1.00
23.59


ATOM
2816
N
PHE
B
564
25.398
48.813
30.902
1.00
25.43


ATOM
2817
CA
PHE
B
564
24.471
49.599
31.708
1.00
26.75


ATOM
2818
CB
PHE
B
564
24.056
48.800
32.942
1.00
37.63


ATOM
2819
CG
PHE
B
564
22.817
49.324
33.606
1.00
38.09


ATOM
2820
CD1
PHE
B
564
21.604
49.337
32.921
1.00
38.40


ATOM
2821
CD2
PHE
B
564
22.858
49.809
34.907
1.00
38.36


ATOM
2822
CE1
PHE
B
564
20.446
49.826
33.525
1.00
38.54


ATOM
2823
CE2
PHE
B
564
21.706
50.301
35.522
1.00
38.90


ATOM
2824
CZ
PHE
B
564
20.498
50.309
34.829
1.00
38.44


ATOM
2825
C
PHE
B
564
24.907
50.999
32.137
1.00
27.15


ATOM
2826
O
PHE
B
564
24.118
51.945
32.064
1.00
26.92


ATOM
2827
N
GLU
B
565
26.156
51.139
32.566
1.00
29.91


ATOM
2828
CA
GLU
B
565
26.654
52.431
33.034
1.00
30.93


ATOM
2829
CB
GLU
B
565
27.762
52.219
34.069
1.00
40.08


ATOM
2830
CG
GLU
B
565
27.372
51.367
35.270
1.00
40.03


ATOM
2831
CD
GLU
B
565
27.050
49.935
34.890
1.00
40.48


ATOM
2832
OE1
GLU
B
565
27.787
49.363
34.058
1.00
40.51


ATOM
2833
OE2
GLU
B
565
26.066
49.378
35.428
1.00
40.01


ATOM
2834
C
GLU
B
565
27.173
53.361
31.944
1.00
30.09


ATOM
2835
O
GLU
B
565
27.567
54.497
32.227
1.00
30.95


ATOM
2836
N
LEU
B
566
27.167
52.894
30.700
1.00
27.08


ATOM
2837
CA
LEU
B
566
27.671
53.692
29.594
1.00
26.42


ATOM
2838
CB
LEU
B
566
28.395
52.784
28.591
1.00
35.46


ATOM
2839
CG
LEU
B
566
29.522
51.884
29.106
1.00
36.46


ATOM
2840
CD1
LEU
B
566
30.022
50.996
27.969
1.00
35.95


ATOM
2841
CD2
LEU
B
566
30.659
52.730
29.659
1.00
36.32


ATOM
2842
C
LEU
B
566
26.600
54.483
28.860
1.00
25.95


ATOM
2843
O
LEU
B
566
25.454
54.048
28.756
1.00
24.61


ATOM
2844
N
SER
B
567
26.986
55.655
28.358
1.00
25.45


ATOM
2845
CA
SER
B
567
26.080
56.501
27.590
1.00
25.56


ATOM
2846
CB
SER
B
567
26.519
57.963
27.665
1.00
33.98


ATOM
2847
OG
SER
B
567
27.722
58.173
26.947
1.00
34.14


ATOM
2848
C
SER
B
567
26.155
56.027
26.140
1.00
25.50


ATOM
2849
O
SER
B
567
27.047
55.247
25.791
1.00
23.97


ATOM
2850
N
ASP
B
568
25.234
56.490
25.300
1.00
26.74


ATOM
2851
CA
ASP
B
568
25.240
56.101
23.892
1.00
26.93


ATOM
2852
CB
ASP
B
568
24.110
56.790
23.127
1.00
31.14


ATOM
2853
CG
ASP
B
568
22.760
56.161
23.390
1.00
31.71


ATOM
2854
OD1
ASP
B
568
21.783
56.584
22.743
1.00
32.07


ATOM
2855
OD2
ASP
B
568
22.678
55.246
24.240
1.00
31.51


ATOM
2856
C
ASP
B
568
26.569
56.455
23.241
1.00
26.60


ATOM
2857
O
ASP
B
568
27.130
55.656
22.494
1.00
26.36


ATOM
2858
N
LEU
B
569
27.071
57.656
23.526
1.00
26.00


ATOM
2859
CA
LEU
B
569
28.341
58.091
22.964
1.00
25.02


ATOM
2860
CB
LEU
B
569
28.683
59.507
23.446
1.00
35.36


ATOM
2861
CG
LEU
B
569
30.009
60.124
22.980
1.00
35.65


ATOM
2862
CD1
LEU
B
569
30.050
60.203
21.464
1.00
36.29


ATOM
2863
CD2
LEU
B
569
30.153
61.516
23.583
1.00
35.93


ATOM
2864
C
LEU
B
569
29.432
57.113
23.388
1.00
24.35


ATOM
2865
O
LEU
B
569
30.267
56.716
22.574
1.00
25.31


ATOM
2866
N
GLU
B
570
29.412
56.715
24.659
1.00
23.22


ATOM
2867
CA
GLU
B
570
30.406
55.784
25.173
1.00
23.38


ATOM
2868
CB
GLU
B
570
30.216
55.560
26.676
1.00
33.69


ATOM
2869
CG
GLU
B
570
30.567
56.787
27.522
1.00
34.19


ATOM
2870
CD
GLU
B
570
30.543
56.509
29.017
1.00
34.09


ATOM
2871
OE1
GLU
B
570
29.467
56.160
29.548
1.00
33.38


ATOM
2872
OE2
GLU
B
570
31.605
56.642
29.665
1.00
35.27


ATOM
2873
C
GLU
B
570
30.351
54.458
24.423
1.00
23.12


ATOM
2874
O
GLU
B
570
31.397
53.899
24.085
1.00
23.04


ATOM
2875
N
THR
B
571
29.148
53.954
24.155
1.00
23.20


ATOM
2876
CA
THR
B
571
29.038
52.692
23.423
1.00
23.72


ATOM
2877
CB
THR
B
571
27.582
52.146
23.367
1.00
22.43


ATOM
2878
OG1
THR
B
571
26.753
53.014
22.589
1.00
23.16


ATOM
2879
CG2
THR
B
571
27.010
52.013
24.772
1.00
23.40


ATOM
2880
C
THR
B
571
29.564
52.865
22.000
1.00
22.59


ATOM
2881
O
THR
B
571
30.147
51.937
21.441
1.00
23.35


ATOM
2882
N
ALA
B
572
29.367
54.047
21.418
1.00
23.15


ATOM
2883
CA
ALA
B
572
29.852
54.323
20.065
1.00
23.02


ATOM
2884
CB
ALA
B
572
29.330
55.671
19.575
1.00
25.21


ATOM
2885
C
ALA
B
572
31.381
54.315
20.061
1.00
24.49


ATOM
2886
O
ALA
B
572
32.007
53.797
19.133
1.00
23.72


ATOM
2887
N
LEU
B
573
31.984
54.906
21.092
1.00
24.96


ATOM
2888
CA
LEU
B
573
33.438
54.924
21.203
1.00
25.56


ATOM
2889
CB
LEU
B
573
33.870
55.787
22.395
1.00
25.61


ATOM
2890
CG
LEU
B
573
33.684
57.294
22.204
1.00
25.96


ATOM
2891
CD1
LEU
B
573
33.998
58.025
23.505
1.00
25.46


ATOM
2892
CD2
LEU
B
573
34.581
57.784
21.076
1.00
24.77


ATOM
2893
C
LEU
B
573
33.961
53.490
21.363
1.00
23.87


ATOM
2894
O
LEU
B
573
34.960
53.116
20.744
1.00
25.16


ATOM
2895
N
CYS
B
574
33.291
52.697
22.195
1.00
21.17


ATOM
2896
CA
CYS
B
574
33.672
51.297
22.406
1.00
20.66


ATOM
2897
CB
CYS
B
574
32.687
50.593
23.342
1.00
22.74


ATOM
2898
SG
CYS
B
574
32.882
50.908
25.120
1.00
21.69


ATOM
2899
C
CYS
B
574
33.665
50.555
21.072
1.00
21.23


ATOM
2900
O
CYS
B
574
34.536
49.727
20.801
1.00
19.77


ATOM
2901
N
THR
B
575
32.668
50.849
20.248
1.00
21.05


ATOM
2902
CA
THR
B
575
32.543
50.203
18.948
1.00
20.83


ATOM
2903
CB
THR
B
575
31.211
50.590
18.273
1.00
21.54


ATOM
2904
OG1
THR
B
575
30.128
50.166
19.109
1.00
22.40


ATOM
2905
CG2
THR
B
575
31.067
49.917
16.912
1.00
22.61


ATOM
2906
C
THR
B
575
33.722
50.565
18.052
1.00
21.63


ATOM
2907
O
THR
B
575
34.268
49.708
17.357
1.00
20.92


ATOM
2908
N
ILE
B
576
34.122
51.833
18.068
1.00
21.26


ATOM
2909
CA
ILE
B
576
35.256
52.261
17.254
1.00
21.61


ATOM
2910
CB
ILE
B
576
35.510
53.786
17.365
1.00
24.97


ATOM
2911
CG2
ILE
B
576
36.817
54.147
16.660
1.00
25.32


ATOM
2912
CG1
ILE
B
576
34.333
54.558
16.757
1.00
25.33


ATOM
2913
CD1
ILE
B
576
34.503
56.083
16.761
1.00
25.78


ATOM
2914
C
ILE
B
576
36.506
51.521
17.717
1.00
22.18


ATOM
2915
O
ILE
B
576
37.344
51.139
16.900
1.00
21.36


ATOM
2916
N
ARG
B
577
36.619
51.318
19.028
1.00
21.36


ATOM
2917
CA
ARG
B
577
37.761
50.620
19.598
1.00
22.50


ATOM
2918
CB
ARG
B
577
37.749
50.702
21.131
1.00
20.87


ATOM
2919
CG
ARG
B
577
38.879
49.924
21.796
1.00
21.90


ATOM
2920
CD
ARG
B
577
40.239
50.280
21.195
1.00
21.96


ATOM
2921
NE
ARG
B
577
40.657
51.648
21.501
1.00
21.18


ATOM
2922
CZ
ARG
B
577
41.693
52.255
20.927
1.00
22.44


ATOM
2923
NH1
ARG
B
577
42.421
51.622
20.011
1.00
22.46


ATOM
2924
NH2
ARG
B
577
42.005
53.504
21.265
1.00
22.38


ATOM
2925
C
ARG
B
577
37.779
49.164
19.149
1.00
21.04


ATOM
2926
O
ARG
B
577
38.846
48.599
18.938
1.00
23.18


ATOM
2927
N
MET
B
578
36.600
48.560
19.000
1.00
21.91


ATOM
2928
CA
MET
B
578
36.507
47.172
18.548
1.00
21.13


ATOM
2929
CB
MET
B
578
35.054
46.705
18.554
1.00
20.87


ATOM
2930
CG
MET
B
578
34.503
46.404
19.925
1.00
21.65


ATOM
2931
SD
MET
B
578
32.749
46.041
19.841
1.00
22.25


ATOM
2932
CE
MET
B
578
32.205
46.673
21.420
1.00
22.99


ATOM
2933
C
MET
B
578
37.079
47.018
17.135
1.00
21.37


ATOM
2934
O
MET
B
578
37.872
46.114
16.876
1.00
21.93


ATOM
2935
N
PHE
B
579
36.660
47.886
16.222
1.00
21.44


ATOM
2936
CA
PHE
B
579
37.160
47.840
14.850
1.00
20.75


ATOM
2937
CB
PHE
B
579
36.496
48.908
13.979
1.00
23.89


ATOM
2938
CG
PHE
B
579
35.160
48.512
13.440
1.00
22.77


ATOM
2939
CD1
PHE
B
579
34.009
48.672
14.203
1.00
22.94


ATOM
2940
CD2
PHE
B
579
35.051
47.979
12.161
1.00
22.86


ATOM
2941
CE1
PHE
B
579
32.765
48.302
13.695
1.00
23.49


ATOM
2942
CE2
PHE
B
579
33.813
47.607
11.645
1.00
23.55


ATOM
2943
CZ
PHE
B
579
32.668
47.769
12.415
1.00
23.73


ATOM
2944
C
PHE
B
579
38.660
48.101
14.832
1.00
21.82


ATOM
2945
O
PHE
B
579
39.411
47.442
14.113
1.00
20.97


ATOM
2946
N
THR
B
580
39.085
49.074
15.628
1.00
23.77


ATOM
2947
CA
THR
B
580
40.488
49.450
15.684
1.00
23.88


ATOM
2948
CB
THR
B
580
40.684
50.693
16.572
1.00
24.40


ATOM
2949
OG1
THR
B
580
39.895
51.770
16.051
1.00
25.13


ATOM
2950
CG2
THR
B
580
42.153
51.109
16.596
1.00
24.68


ATOM
2951
C
THR
B
580
41.402
48.338
16.174
1.00
24.19


ATOM
2952
O
THR
B
580
42.389
48.011
15.512
1.00
24.60


ATOM
2953
N
ASP
B
581
41.072
47.743
17.314
1.00
26.39


ATOM
2954
CA
ASP
B
581
41.903
46.687
17.872
1.00
27.24


ATOM
2955
CB
ASP
B
581
41.635
46.554
19.369
1.00
26.21


ATOM
2956
CG
ASP
B
581
42.295
47.666
20.171
1.00
26.06


ATOM
2957
OD1
ASP
B
581
42.688
48.690
19.565
1.00
25.91


ATOM
2958
OD2
ASP
B
581
42.418
47.520
21.402
1.00
26.26


ATOM
2959
C
ASP
B
581
41.821
45.333
17.182
1.00
27.49


ATOM
2960
O
ASP
B
581
42.535
44.403
17.552
1.00
27.57


ATOM
2961
N
LEU
B
582
40.947
45.217
16.189
1.00
23.58


ATOM
2962
CA
LEU
B
582
40.859
43.984
15.415
1.00
24.50


ATOM
2963
CB
LEU
B
582
39.395
43.600
15.139
1.00
22.05


ATOM
2964
CG
LEU
B
582
38.660
42.981
16.337
1.00
21.75


ATOM
2965
CD1
LEU
B
582
37.178
42.787
16.035
1.00
22.80


ATOM
2966
CD2
LEU
B
582
39.309
41.648
16.680
1.00
21.90


ATOM
2967
C
LEU
B
582
41.605
44.305
14.117
1.00
24.79


ATOM
2968
O
LEU
B
582
41.591
43.531
13.153
1.00
25.28


ATOM
2969
N
ASN
B
583
42.255
45.469
14.117
1.00
27.83


ATOM
2970
CA
ASN
B
583
43.037
45.956
12.984
1.00
30.24


ATOM
2971
CB
ASN
B
583
44.235
45.037
12.740
1.00
52.59


ATOM
2972
CG
ASN
B
583
45.196
45.017
13.906
1.00
53.50


ATOM
2973
OD1
ASN
B
583
44.827
44.655
15.023
1.00
53.73


ATOM
2974
ND2
ASN
B
583
46.440
45.410
13.655
1.00
53.71


ATOM
2975
C
ASN
B
583
42.223
46.074
11.704
1.00
29.60


ATOM
2976
O
ASN
B
583
42.733
45.818
10.614
1.00
30.55


ATOM
2977
N
LEU
B
584
40.964
46.478
11.840
1.00
27.68


ATOM
2978
CA
LEU
B
584
40.069
46.620
10.696
1.00
27.10


ATOM
2979
CB
LEU
B
584
38.632
46.323
11.131
1.00
25.59


ATOM
2980
CG
LEU
B
584
38.111
44.884
11.080
1.00
26.48


ATOM
2981
CD1
LEU
B
584
39.198
43.891
11.360
1.00
26.71


ATOM
2982
CD2
LEU
B
584
36.954
44.746
12.065
1.00
24.71


ATOM
2983
C
LEU
B
584
40.115
47.992
10.047
1.00
27.65


ATOM
2984
O
LEU
B
584
39.908
48.120
8.843
1.00
26.67


ATOM
2985
N
VAL
B
585
40.380
49.021
10.845
1.00
28.02


ATOM
2986
CA
VAL
B
585
40.415
50.380
10.326
1.00
28.97


ATOM
2987
CB
VAL
B
585
40.586
51.400
11.467
1.00
33.37


ATOM
2988
CG1
VAL
B
585
40.639
52.812
10.902
1.00
33.53


ATOM
2989
CG2
VAL
B
585
39.436
51.267
12.448
1.00
33.91


ATOM
2990
C
VAL
B
585
41.502
50.620
9.283
1.00
29.73


ATOM
2991
O
VAL
B
585
41.210
51.056
8.172
1.00
29.62


ATOM
2992
N
GLN
B
586
42.749
50.330
9.638
1.00
34.73


ATOM
2993
CA
GLN
B
586
43.860
50.536
8.718
1.00
36.38


ATOM
2994
CB
GLN
B
586
45.171
50.626
9.501
1.00
56.06


ATOM
2995
CG
GLN
B
586
45.261
51.887
10.349
1.00
56.60


ATOM
2996
CD
GLN
B
586
46.523
51.955
11.184
1.00
57.01


ATOM
2997
OE1
GLN
B
586
46.729
51.142
12.085
1.00
56.81


ATOM
2998
NE2
GLN
B
586
47.378
52.930
10.887
1.00
56.83


ATOM
2999
C
GLN
B
586
43.936
49.439
7.666
1.00
35.19


ATOM
3000
O
GLN
B
586
44.176
49.716
6.492
1.00
36.38


ATOM
3001
N
ASN
B
587
43.716
48.199
8.088
1.00
28.60


ATOM
3002
CA
ASN
B
587
43.749
47.058
7.180
1.00
27.39


ATOM
3003
CB
ASN
B
587
43.208
45.816
7.893
1.00
34.50


ATOM
3004
CG
ASN
B
587
43.520
44.530
7.155
1.00
34.35


ATOM
3005
OD1
ASN
B
587
43.721
44.528
5.943
1.00
34.55


ATOM
3006
ND2
ASN
B
587
43.549
43.423
7.888
1.00
34.96


ATOM
3007
C
ASN
B
587
42.895
47.331
5.941
1.00
27.36


ATOM
3008
O
ASN
B
587
43.336
47.133
4.811
1.00
26.90


ATOM
3009
N
PHE
B
588
41.666
47.796
6.154
1.00
26.94


ATOM
3010
CA
PHE
B
588
40.765
48.048
5.040
1.00
26.43


ATOM
3011
CB
PHE
B
588
39.423
47.350
5.317
1.00
20.94


ATOM
3012
CG
PHE
B
588
39.558
45.856
5.503
1.00
20.97


ATOM
3013
CD1
PHE
B
588
39.472
45.277
6.765
1.00
20.43


ATOM
3014
CD2
PHE
B
588
39.845
45.038
4.417
1.00
20.60


ATOM
3015
CE1
PHE
B
588
39.678
43.899
6.940
1.00
20.54


ATOM
3016
CE2
PHE
B
588
40.052
43.662
4.576
1.00
19.56


ATOM
3017
CZ
PHE
B
588
39.969
43.091
5.842
1.00
21.12


ATOM
3018
C
PHE
B
588
40.573
49.521
4.670
1.00
27.33


ATOM
3019
O
PHE
B
588
39.625
49.878
3.973
1.00
27.04


ATOM
3020
N
GLN
B
589
41.502
50.365
5.111
1.00
28.79


ATOM
3021
CA
GLN
B
589
41.465
51.800
4.818
1.00
29.49


ATOM
3022
CB
GLN
B
589
41.843
52.064
3.350
1.00
45.46


ATOM
3023
CG
GLN
B
589
43.334
51.986
3.014
1.00
45.82


ATOM
3024
CD
GLN
B
589
43.797
50.588
2.639
1.00
46.29


ATOM
3025
OE1
GLN
B
589
42.993
49.736
2.257
1.00
46.04


ATOM
3026
NE2
GLN
B
589
45.104
50.353
2.724
1.00
45.90


ATOM
3027
C
GLN
B
589
40.127
52.481
5.106
1.00
29.77


ATOM
3028
O
GLN
B
589
39.509
53.063
4.212
1.00
29.22


ATOM
3029
N
MET
B
590
39.686
52.421
6.357
1.00
30.86


ATOM
3030
CA
MET
B
590
38.432
53.050
6.743
1.00
30.28


ATOM
3031
CB
MET
B
590
37.759
52.259
7.865
1.00
26.11


ATOM
3032
CG
MET
B
590
37.254
50.888
7.485
1.00
26.11


ATOM
3033
SD
MET
B
590
36.366
50.192
8.891
1.00
24.81


ATOM
3034
CE
MET
B
590
35.005
51.232
8.953
1.00
27.02


ATOM
3035
C
MET
B
590
38.680
54.467
7.241
1.00
30.44


ATOM
3036
O
MET
B
590
39.453
54.666
8.175
1.00
30.43


ATOM
3037
N
LYS
B
591
38.039
55.449
6.616
1.00
28.66


ATOM
3038
CA
LYS
B
591
38.181
56.833
7.059
1.00
29.65


ATOM
3039
CB
LYS
B
591
37.556
57.798
6.045
1.00
48.54


ATOM
3040
CG
LYS
B
591
38.530
58.376
5.022
1.00
49.40


ATOM
3041
CD
LYS
B
591
39.125
57.314
4.114
1.00
49.46


ATOM
3042
CE
LYS
B
591
40.123
57.925
3.141
1.00
49.63


ATOM
3043
NZ
LYS
B
591
39.519
59.026
2.336
1.00
49.46


ATOM
3044
C
LYS
B
591
37.453
56.951
8.399
1.00
28.39


ATOM
3045
O
LYS
B
591
36.361
56.409
8.566
1.00
28.80


ATOM
3046
N
HIS
B
592
38.060
57.646
9.354
1.00
26.99


ATOM
3047
CA
HIS
B
592
37.447
57.803
10.669
1.00
26.60


ATOM
3048
CB
HIS
B
592
38.305
58.713
11.554
1.00
26.53


ATOM
3049
CG
HIS
B
592
37.869
58.742
12.985
1.00
26.27


ATOM
3050
CD2
HIS
B
592
37.395
59.750
13.755
1.00
26.34


ATOM
3051
ND1
HIS
B
592
37.888
57.622
13.788
1.00
26.28


ATOM
3052
CE1
HIS
B
592
37.446
57.939
14.992
1.00
26.55


ATOM
3053
NE2
HIS
B
592
37.140
59.224
14.998
1.00
26.20


ATOM
3054
C
HIS
B
592
36.027
58.366
10.594
1.00
26.93


ATOM
3055
O
HIS
B
592
35.114
57.856
11.244
1.00
26.72


ATOM
3056
N
GLU
B
593
35.844
59.423
9.810
1.00
25.99


ATOM
3057
CA
GLU
B
593
34.532
60.049
9.675
1.00
26.68


ATOM
3058
CB
GLU
B
593
34.615
61.240
8.717
1.00
47.65


ATOM
3059
CG
GLU
B
593
35.479
62.386
9.232
1.00
48.65


ATOM
3060
CD
GLU
B
593
36.880
61.942
9.628
1.00
48.66


ATOM
3061
OE1
GLU
B
593
37.595
61.373
8.773
1.00
48.66


ATOM
3062
OE2
GLU
B
593
37.266
62.160
10.798
1.00
48.65


ATOM
3063
C
GLU
B
593
33.479
59.056
9.188
1.00
25.92


ATOM
3064
O
GLU
B
593
32.368
59.011
9.717
1.00
25.44


ATOM
3065
N
VAL
B
594
33.837
58.257
8.188
1.00
23.11


ATOM
3066
CA
VAL
B
594
32.914
57.265
7.640
1.00
23.96


ATOM
3067
CB
VAL
B
594
33.511
56.574
6.390
1.00
21.56


ATOM
3068
CG1
VAL
B
594
32.576
55.471
5.891
1.00
21.95


ATOM
3069
CG2
VAL
B
594
33.747
57.604
5.297
1.00
21.81


ATOM
3070
C
VAL
B
594
32.556
56.196
8.667
1.00
23.30


ATOM
3071
O
VAL
B
594
31.385
55.849
8.824
1.00
23.33


ATOM
3072
N
LEU
B
595
33.558
55.663
9.360
1.00
24.80


ATOM
3073
CA
LEU
B
595
33.300
54.639
10.364
1.00
24.45


ATOM
3074
CB
LEU
B
595
34.616
54.127
10.959
1.00
24.30


ATOM
3075
CG
LEU
B
595
34.502
53.137
12.123
1.00
25.09


ATOM
3076
CD1
LEU
B
595
33.643
51.938
11.723
1.00
23.72


ATOM
3077
CD2
LEU
B
595
35.892
52.686
12.545
1.00
23.89


ATOM
3078
C
LEU
B
595
32.391
55.190
11.464
1.00
24.32


ATOM
3079
O
LEU
B
595
31.482
54.501
11.935
1.00
24.28


ATOM
3080
N
CYS
B
596
32.625
56.437
11.866
1.00
23.70


ATOM
3081
CA
CYS
B
596
31.794
57.057
12.895
1.00
22.77


ATOM
3082
CB
CYS
B
596
32.354
58.426
13.302
1.00
27.45


ATOM
3083
SG
CYS
B
596
33.875
58.384
14.277
1.00
27.23


ATOM
3084
C
CYS
B
596
30.363
57.233
12.386
1.00
22.78


ATOM
3085
O
CYS
B
596
29.404
56.963
13.108
1.00
22.99


ATOM
3086
N
ARG
B
597
30.221
57.681
11.140
1.00
22.21


ATOM
3087
CA
ARG
B
597
28.899
57.893
10.562
1.00
21.97


ATOM
3088
CB
ARG
B
597
29.018
58.543
9.178
1.00
33.99


ATOM
3089
CG
ARG
B
597
27.678
58.924
8.570
1.00
35.29


ATOM
3090
CD
ARG
B
597
27.807
59.645
7.228
1.00
35.28


ATOM
3091
NE
ARG
B
597
28.241
61.035
7.362
1.00
35.24


ATOM
3092
CZ
ARG
B
597
29.494
61.455
7.216
1.00
35.37


ATOM
3093
NH1
ARG
B
597
30.463
60.596
6.926
1.00
35.79


ATOM
3094
NH2
ARG
B
597
29.778
62.745
7.354
1.00
35.68


ATOM
3095
C
ARG
B
597
28.149
56.563
10.459
1.00
21.87


ATOM
3096
O
ARG
B
597
26.954
56.496
10.729
1.00
21.94


ATOM
3097
N
TRP
B
598
28.862
55.511
10.069
1.00
23.25


ATOM
3098
CA
TRP
B
598
28.264
54.185
9.944
1.00
23.59


ATOM
3099
CB
TRP
B
598
29.287
53.194
9.374
1.00
21.37


ATOM
3100
CG
TRP
B
598
28.744
51.811
9.234
1.00
19.95


ATOM
3101
CD2
TRP
B
598
28.905
50.725
10.157
1.00
20.76


ATOM
3102
CE2
TRP
B
598
28.159
49.636
9.653
1.00
21.16


ATOM
3103
CE3
TRP
B
598
29.602
50.568
11.363
1.00
20.58


ATOM
3104
CD1
TRP
B
598
27.937
51.349
8.237
1.00
20.72


ATOM
3105
NE1
TRP
B
598
27.581
50.044
8.481
1.00
20.01


ATOM
3106
CZ2
TRP
B
598
28.091
48.404
10.313
1.00
19.36


ATOM
3107
CZ3
TRP
B
598
29.534
49.346
12.019
1.00
21.53


ATOM
3108
CH2
TRP
B
598
28.780
48.277
11.491
1.00
21.51


ATOM
3109
C
TRP
B
598
27.774
53.687
11.301
1.00
23.33


ATOM
3110
O
TRP
B
598
26.660
53.170
11.429
1.00
22.55


ATOM
3111
N
ILE
B
599
28.614
53.836
12.318
1.00
19.88


ATOM
3112
CA
ILE
B
599
28.250
53.401
13.652
1.00
19.76


ATOM
3113
CB
ILE
B
599
29.400
53.659
14.656
1.00
18.66


ATOM
3114
CG2
ILE
B
599
28.917
53.410
16.078
1.00
20.09


ATOM
3115
CG1
ILE
B
599
30.586
52.742
14.328
1.00
19.91


ATOM
3116
CD1
ILE
B
599
31.835
53.042
15.140
1.00
18.69


ATOM
3117
C
ILE
B
599
26.989
54.124
14.105
1.00
20.60


ATOM
3118
O
ILE
B
599
26.072
53.501
14.636
1.00
20.28


ATOM
3119
N
LEU
B
600
26.933
55.435
13.883
1.00
24.36


ATOM
3120
CA
LEU
B
600
25.761
56.200
14.292
1.00
24.27


ATOM
3121
CB
LEU
B
600
26.023
57.700
14.135
1.00
30.88


ATOM
3122
CG
LEU
B
600
27.104
58.235
15.080
1.00
31.45


ATOM
3123
CD1
LEU
B
600
27.378
59.680
14.764
1.00
31.56


ATOM
3124
CD2
LEU
B
600
26.663
58.079
16.529
1.00
31.65


ATOM
3125
C
LEU
B
600
24.518
55.788
13.512
1.00
25.39


ATOM
3126
O
LEU
B
600
23.432
55.697
14.086
1.00
24.82


ATOM
3127
N
SER
B
601
24.681
55.522
12.216
1.00
24.46


ATOM
3128
CA
SER
B
601
23.563
55.098
11.373
1.00
23.76


ATOM
3129
CB
SER
B
601
24.018
54.931
9.920
1.00
24.34


ATOM
3130
OG
SER
B
601
24.232
56.181
9.287
1.00
24.61


ATOM
3131
C
SER
B
601
23.004
53.771
11.884
1.00
23.31


ATOM
3132
O
SER
B
601
21.793
53.574
11.947
1.00
24.08


ATOM
3133
N
VAL
B
602
23.895
52.855
12.248
1.00
20.00


ATOM
3134
CA
VAL
B
602
23.465
51.560
12.765
1.00
19.52


ATOM
3135
CB
VAL
B
602
24.681
50.622
12.998
1.00
20.56


ATOM
3136
CG1
VAL
B
602
24.271
49.399
13.806
1.00
20.50


ATOM
3137
CG2
VAL
B
602
25.258
50.193
11.659
1.00
20.79


ATOM
3138
C
VAL
B
602
22.685
51.742
14.073
1.00
18.74


ATOM
3139
O
VAL
B
602
21.598
51.188
14.243
1.00
19.51


ATOM
3140
N
LYS
B
603
23.230
52.533
14.989
1.00
21.59


ATOM
3141
CA
LYS
B
603
22.568
52.767
16.268
1.00
22.24


ATOM
3142
CB
LYS
B
603
23.433
53.674
17.156
1.00
32.07


ATOM
3143
CG
LYS
B
603
22.812
53.968
18.523
1.00
32.67


ATOM
3144
CD
LYS
B
603
23.775
54.700
19.457
1.00
32.26


ATOM
3145
CE
LYS
B
603
24.152
56.067
18.910
1.00
33.03


ATOM
3146
NZ
LYS
B
603
24.991
56.838
19.866
1.00
33.90


ATOM
3147
C
LYS
B
603
21.193
53.404
16.072
1.00
21.31


ATOM
3148
O
LYS
B
603
20.229
53.057
16.758
1.00
21.06


ATOM
3149
N
LYS
B
604
21.103
54.318
15.116
1.00
21.77


ATOM
3150
CA
LYS
B
604
19.846
55.003
14.860
1.00
22.10


ATOM
3151
CB
LYS
B
604
20.071
56.179
13.904
1.00
35.05


ATOM
3152
CG
LYS
B
604
18.815
56.987
13.614
1.00
35.34


ATOM
3153
CD
LYS
B
604
19.111
58.153
12.691
1.00
35.68


ATOM
3154
CE
LYS
B
604
17.841
58.897
12.313
1.00
35.70


ATOM
3155
NZ
LYS
B
604
18.118
60.009
11.357
1.00
35.94


ATOM
3156
C
LYS
B
604
18.781
54.088
14.290
1.00
23.45


ATOM
3157
O
LYS
B
604
17.588
54.266
14.567
1.00
23.47


ATOM
3158
N
ASN
B
605
19.200
53.104
13.497
1.00
24.27


ATOM
3159
CA
ASN
B
605
18.238
52.198
12.887
1.00
24.84


ATOM
3160
CB
ASN
B
605
18.790
51.629
11.580
1.00
33.82


ATOM
3161
CG
ASN
B
605
18.757
52.650
10.461
1.00
34.72


ATOM
3162
OD1
ASN
B
605
19.593
53.552
10.401
1.00
35.05


ATOM
3163
ND2
ASN
B
605
17.771
52.529
9.579
1.00
34.67


ATOM
3164
C
ASN
B
605
17.713
51.091
13.784
1.00
25.28


ATOM
3165
O
ASN
B
605
17.138
50.109
13.309
1.00
26.57


ATOM
3166
N
TYR
B
606
17.935
51.237
15.083
1.00
22.80


ATOM
3167
CA
TYR
B
606
17.381
50.301
16.047
1.00
21.47


ATOM
3168
CB
TYR
B
606
18.406
49.906
17.116
1.00
19.39


ATOM
3169
CG
TYR
B
606
19.259
48.734
16.684
1.00
18.74


ATOM
3170
CD1
TYR
B
606
20.482
48.930
16.047
1.00
19.52


ATOM
3171
CE1
TYR
B
606
21.221
47.852
15.566
1.00
19.69


ATOM
3172
CD2
TYR
B
606
18.795
47.427
16.836
1.00
18.61


ATOM
3173
CE2
TYR
B
606
19.530
46.337
16.355
1.00
19.30


ATOM
3174
CZ
TYR
B
606
20.739
46.563
15.719
1.00
19.25


ATOM
3175
OH
TYR
B
606
21.459
45.499
15.209
1.00
18.12


ATOM
3176
C
TYR
B
606
16.234
51.093
16.662
1.00
22.67


ATOM
3177
O
TYR
B
606
16.323
52.319
16.782
1.00
24.05


ATOM
3178
N
ARG
B
607
15.146
50.419
17.009
1.00
23.34


ATOM
3179
CA
ARG
B
607
13.997
51.106
17.602
1.00
23.02


ATOM
3180
CB
ARG
B
607
12.718
50.315
17.322
1.00
22.58


ATOM
3181
CG
ARG
B
607
12.516
50.043
15.838
1.00
22.23


ATOM
3182
CD
ARG
B
607
11.149
49.467
15.533
1.00
23.26


ATOM
3183
NE
ARG
B
607
11.044
49.076
14.131
1.00
21.78


ATOM
3184
CZ
ARG
B
607
9.916
48.698
13.537
1.00
23.35


ATOM
3185
NH1
ARG
B
607
8.780
48.661
14.220
1.00
22.77


ATOM
3186
NH2
ARG
B
607
9.931
48.344
12.258
1.00
23.68


ATOM
3187
C
ARG
B
607
14.247
51.243
19.100
1.00
23.25


ATOM
3188
O
ARG
B
607
14.123
50.282
19.855
1.00
22.89


ATOM
3189
N
LYS
B
608
14.602
52.450
19.526
1.00
26.06


ATOM
3190
CA
LYS
B
608
14.921
52.697
20.928
1.00
27.43


ATOM
3191
CB
LYS
B
608
15.228
54.183
21.147
1.00
43.34


ATOM
3192
CG
LYS
B
608
14.041
55.104
20.946
1.00
43.63


ATOM
3193
CD
LYS
B
608
14.394
56.538
21.307
1.00
43.77


ATOM
3194
CE
LYS
B
608
13.192
57.458
21.141
1.00
44.09


ATOM
3195
NZ
LYS
B
608
13.518
58.878
21.457
1.00
43.98


ATOM
3196
C
LYS
B
608
13.878
52.248
21.940
1.00
26.36


ATOM
3197
O
LYS
B
608
14.221
51.870
23.062
1.00
27.18


ATOM
3198
N
ASN
B
609
12.606
52.277
21.559
1.00
24.76


ATOM
3199
CA
ASN
B
609
11.560
51.890
22.490
1.00
25.81


ATOM
3200
CB
ASN
B
609
10.305
52.718
22.222
1.00
34.37


ATOM
3201
CG
ASN
B
609
10.558
54.201
22.378
1.00
35.05


ATOM
3202
OD1
ASN
B
609
10.969
54.657
23.444
1.00
35.79


ATOM
3203
ND2
ASN
B
609
10.326
54.961
21.315
1.00
35.63


ATOM
3204
C
ASN
B
609
11.226
50.406
22.548
1.00
24.40


ATOM
3205
O
ASN
B
609
10.336
49.993
23.294
1.00
24.72


ATOM
3206
N
VAL
B
610
11.925
49.596
21.759
1.00
22.64


ATOM
3207
CA
VAL
B
610
11.699
48.160
21.814
1.00
21.87


ATOM
3208
CB
VAL
B
610
12.205
47.456
20.536
1.00
21.44


ATOM
3209
CG1
VAL
B
610
12.237
45.953
20.746
1.00
21.17


ATOM
3210
CG2
VAL
B
610
11.276
47.783
19.377
1.00
21.07


ATOM
3211
C
VAL
B
610
12.513
47.729
23.037
1.00
22.60


ATOM
3212
O
VAL
B
610
13.704
48.016
23.127
1.00
22.78


ATOM
3213
N
ALA
B
611
11.865
47.051
23.976
1.00
21.43


ATOM
3214
CA
ALA
B
611
12.500
46.651
25.232
1.00
21.58


ATOM
3215
CB
ALA
B
611
11.521
45.828
26.061
1.00
24.34


ATOM
3216
C
ALA
B
611
13.851
45.941
25.176
1.00
21.37


ATOM
3217
O
ALA
B
611
14.795
46.361
25.851
1.00
21.07


ATOM
3218
N
TYR
B
612
13.951
44.878
24.382
1.00
20.78


ATOM
3219
CA
TYR
B
612
15.202
44.119
24.301
1.00
19.11


ATOM
3220
CB
TYR
B
612
14.926
42.648
24.623
1.00
19.45


ATOM
3221
CG
TYR
B
612
16.144
41.756
24.493
1.00
19.72


ATOM
3222
CD1
TYR
B
612
16.194
40.756
23.523
1.00
19.82


ATOM
3223
CE1
TYR
B
612
17.304
39.933
23.401
1.00
19.95


ATOM
3224
CD2
TYR
B
612
17.238
41.914
25.337
1.00
19.48


ATOM
3225
CE2
TYR
B
612
18.359
41.094
25.222
1.00
20.02


ATOM
3226
CZ
TYR
B
612
18.382
40.109
24.259
1.00
20.21


ATOM
3227
OH
TYR
B
612
19.471
39.271
24.168
1.00
20.28


ATOM
3228
C
TYR
B
612
15.994
44.218
22.994
1.00
20.06


ATOM
3229
O
TYR
B
612
17.203
44.465
23.027
1.00
19.27


ATOM
3230
N
HIS
B
613
15.338
44.021
21.851
1.00
20.51


ATOM
3231
CA
HIS
B
613
16.046
44.096
20.569
1.00
19.40


ATOM
3232
CB
HIS
B
613
15.310
43.290
19.493
1.00
21.37


ATOM
3233
CG
HIS
B
613
15.351
41.811
19.712
1.00
21.97


ATOM
3234
CD2
HIS
B
613
16.338
40.907
19.503
1.00
21.44


ATOM
3235
ND1
HIS
B
613
14.283
41.101
20.216
1.00
21.50


ATOM
3236
CE1
HIS
B
613
14.608
39.824
20.307
1.00
22.37


ATOM
3237
NE2
HIS
B
613
15.851
39.679
19.881
1.00
22.50


ATOM
3238
C
HIS
B
613
16.229
45.530
20.093
1.00
19.18


ATOM
3239
O
HIS
B
613
15.583
45.971
19.149
1.00
19.28


ATOM
3240
N
ASN
B
614
17.137
46.241
20.749
1.00
19.04


ATOM
3241
CA
ASN
B
614
17.429
47.631
20.425
1.00
19.60


ATOM
3242
CB
ASN
B
614
16.895
48.526
21.541
1.00
24.32


ATOM
3243
CG
ASN
B
614
17.245
47.996
22.914
1.00
24.73


ATOM
3244
OD1
ASN
B
614
18.405
47.678
23.188
1.00
26.31


ATOM
3245
ND2
ASN
B
614
16.247
47.890
23.787
1.00
24.39


ATOM
3246
C
ASN
B
614
18.948
47.761
20.311
1.00
19.61


ATOM
3247
O
ASN
B
614
19.658
46.757
20.336
1.00
19.88


ATOM
3248
N
TRP
B
615
19.451
48.986
20.188
1.00
20.60


ATOM
3249
CA
TRP
B
615
20.893
49.189
20.052
1.00
20.16


ATOM
3250
CB
TRP
B
615
21.219
50.686
20.022
1.00
22.74


ATOM
3251
CG
TRP
B
615
22.672
50.982
20.262
1.00
23.84


ATOM
3252
CD2
TRP
B
615
23.773
50.638
19.412
1.00
23.87


ATOM
3253
CE2
TRP
B
615
24.949
51.101
20.046
1.00
24.13


ATOM
3254
CE3
TRP
B
615
23.882
49.985
18.179
1.00
24.34


ATOM
3255
CD1
TRP
B
615
23.209
51.620
21.346
1.00
23.95


ATOM
3256
NE1
TRP
B
615
24.574
51.694
21.224
1.00
24.06


ATOM
3257
CZ2
TRP
B
615
26.222
50.932
19.485
1.00
24.74


ATOM
3258
CZ3
TRP
B
615
25.152
49.816
17.618
1.00
24.67


ATOM
3259
CH2
TRP
B
615
26.304
50.290
18.276
1.00
23.93


ATOM
3260
C
TRP
B
615
21.776
48.514
21.098
1.00
19.91


ATOM
3261
O
TRP
B
615
22.834
47.960
20.766
1.00
18.94


ATOM
3262
N
ARG
B
616
21.373
48.572
22.361
1.00
18.07


ATOM
3263
CA
ARG
B
616
22.193
47.978
23.403
1.00
19.36


ATOM
3264
CB
ARG
B
616
21.610
48.286
24.785
1.00
22.36


ATOM
3265
CG
ARG
B
616
21.612
49.788
25.119
1.00
22.18


ATOM
3266
CD
ARG
B
616
23.029
50.377
25.052
1.00
22.30


ATOM
3267
NE
ARG
B
616
23.086
51.816
25.313
1.00
23.22


ATOM
3268
CZ
ARG
B
616
23.686
52.364
26.368
1.00
23.02


ATOM
3269
NH1
ARG
B
616
24.280
51.600
27.272
1.00
22.92


ATOM
3270
NH2
ARG
B
616
23.714
53.685
26.504
1.00
23.10


ATOM
3271
C
ARG
B
616
22.392
46.479
23.208
1.00
18.33


ATOM
3272
O
ARG
B
616
23.483
45.970
23.476
1.00
18.59


ATOM
3273
N
HIS
B
617
21.363
45.772
22.736
1.00
20.45


ATOM
3274
CA
HIS
B
617
21.495
44.333
22.512
1.00
17.68


ATOM
3275
CB
HIS
B
617
20.156
43.690
22.143
1.00
17.10


ATOM
3276
CG
HIS
B
617
20.300
42.309
21.571
1.00
16.72


ATOM
3277
CD2
HIS
B
617
20.008
41.819
20.343
1.00
19.45


ATOM
3278
ND1
HIS
B
617
20.842
41.261
22.283
1.00
17.70


ATOM
3279
CE1
HIS
B
617
20.880
40.183
21.517
1.00
16.30


ATOM
3280
NE2
HIS
B
617
20.380
40.497
20.336
1.00
14.56


ATOM
3281
C
HIS
B
617
22.507
44.058
21.402
1.00
18.17


ATOM
3282
O
HIS
B
617
23.343
43.151
21.528
1.00
17.84


ATOM
3283
N
ALA
B
618
22.420
44.836
20.326
1.00
18.42


ATOM
3284
CA
ALA
B
618
23.329
44.707
19.189
1.00
17.70


ATOM
3285
CB
ALA
B
618
22.918
45.659
18.067
1.00
21.95


ATOM
3286
C
ALA
B
618
24.749
45.026
19.652
1.00
17.93


ATOM
3287
O
ALA
B
618
25.701
44.320
19.324
1.00
18.41


ATOM
3288
N
PHE
B
619
24.882
46.100
20.421
1.00
17.19


ATOM
3289
CA
PHE
B
619
26.184
46.502
20.936
1.00
17.81


ATOM
3290
CB
PHE
B
619
26.040
47.811
21.726
1.00
18.98


ATOM
3291
CG
PHE
B
619
27.290
48.224
22.454
1.00
18.41


ATOM
3292
CD1
PHE
B
619
28.423
48.626
21.755
1.00
18.73


ATOM
3293
CD2
PHE
B
619
27.340
48.172
23.842
1.00
19.11


ATOM
3294
CE1
PHE
B
619
29.588
48.966
22.427
1.00
19.47


ATOM
3295
CE2
PHE
B
619
28.498
48.509
24.527
1.00
19.39


ATOM
3296
CZ
PHE
B
619
29.627
48.907
23.816
1.00
19.32


ATOM
3297
C
PHE
B
619
26.791
45.407
21.818
1.00
18.52


ATOM
3298
O
PHE
B
619
27.979
45.091
21.695
1.00
18.60


ATOM
3299
N
ASN
B
620
25.983
44.819
22.699
1.00
18.74


ATOM
3300
CA
ASN
B
620
26.484
43.774
23.585
1.00
19.38


ATOM
3301
CB
ASN
B
620
25.457
43.424
24.670
1.00
22.15


ATOM
3302
CG
ASN
B
620
25.289
44.538
25.691
1.00
22.79


ATOM
3303
OD1
ASN
B
620
26.218
45.288
25.941
1.00
23.65


ATOM
3304
ND2
ASN
B
620
24.110
44.632
26.292
1.00
22.68


ATOM
3305
C
ASN
B
620
26.857
42.524
22.806
1.00
18.58


ATOM
3306
O
ASN
B
620
27.787
41.809
23.178
1.00
19.87


ATOM
3307
N
THR
B
621
26.134
42.262
21.723
1.00
19.05


ATOM
3308
CA
THR
B
621
26.438
41.099
20.903
1.00
18.12


ATOM
3309
CB
THR
B
621
25.352
40.874
19.823
1.00
17.52


ATOM
3310
OG1
THR
B
621
24.095
40.640
20.462
1.00
18.11


ATOM
3311
CG2
THR
B
621
25.694
39.657
18.953
1.00
18.01


ATOM
3312
C
THR
B
621
27.796
41.323
20.233
1.00
18.57


ATOM
3313
O
THR
B
621
28.601
40.398
20.134
1.00
19.61


ATOM
3314
N
ALA
B
622
28.046
42.550
19.785
1.00
19.36


ATOM
3315
CA
ALA
B
622
29.310
42.896
19.140
1.00
18.22


ATOM
3316
CB
ALA
B
622
29.221
44.288
18.511
1.00
22.38


ATOM
3317
C
ALA
B
622
30.452
42.843
20.152
1.00
20.92


ATOM
3318
O
ALA
B
622
31.555
42.407
19.829
1.00
18.90


ATOM
3319
N
GLN
B
623
30.192
43.285
21.381
1.00
17.97


ATOM
3320
CA
GLN
B
623
31.219
43.257
22.420
1.00
19.34


ATOM
3321
CB
GLN
B
623
30.709
43.970
23.677
1.00
20.66


ATOM
3322
CG
GLN
B
623
31.720
44.081
24.823
1.00
21.04


ATOM
3323
CD
GLN
B
623
31.756
42.848
25.704
1.00
21.30


ATOM
3324
OE1
GLN
B
623
30.712
42.346
26.134
1.00
22.15


ATOM
3325
NE2
GLN
B
623
32.956
42.362
25.995
1.00
21.86


ATOM
3326
C
GLN
B
623
31.600
41.811
22.739
1.00
18.06


ATOM
3327
O
GLN
B
623
32.776
41.499
22.963
1.00
19.37


ATOM
3328
N
CYS
B
624
30.609
40.924
22.755
1.00
18.07


ATOM
3329
CA
CYS
B
624
30.880
39.519
23.027
1.00
17.94


ATOM
3330
CB
CYS
B
624
29.585
38.724
23.171
1.00
21.24


ATOM
3331
SG
CYS
B
624
29.857
37.007
23.684
1.00
20.09


ATOM
3332
C
CYS
B
624
31.695
38.961
21.866
1.00
19.06


ATOM
3333
O
CYS
B
624
32.615
38.158
22.067
1.00
18.98


ATOM
3334
N
MET
B
625
31.371
39.400
20.653
1.00
18.53


ATOM
3335
CA
MET
B
625
32.102
38.937
19.470
1.00
18.30


ATOM
3336
CB
MET
B
625
31.491
39.521
18.195
1.00
19.41


ATOM
3337
CG
MET
B
625
32.164
39.070
16.897
1.00
19.09


ATOM
3338
SD
MET
B
625
32.084
37.274
16.604
1.00
16.39


ATOM
3339
CE
MET
B
625
30.324
37.033
16.399
1.00
18.22


ATOM
3340
C
MET
B
625
33.555
39.393
19.606
1.00
18.55


ATOM
3341
O
MET
B
625
34.483
38.640
19.332
1.00
19.67


ATOM
3342
N
PHE
B
626
33.749
40.636
20.036
1.00
19.00


ATOM
3343
CA
PHE
B
626
35.101
41.156
20.225
1.00
18.99


ATOM
3344
CB
PHE
B
626
35.063
42.625
20.649
1.00
19.58


ATOM
3345
CG
PHE
B
626
36.421
43.211
20.909
1.00
19.51


ATOM
3346
CD1
PHE
B
626
36.965
43.200
22.190
1.00
21.50


ATOM
3347
CD2
PHE
B
626
37.162
43.759
19.868
1.00
20.23


ATOM
3348
CE1
PHE
B
626
38.234
43.731
22.433
1.00
19.73


ATOM
3349
CE2
PHE
B
626
38.433
44.292
20.095
1.00
20.70


ATOM
3350
CZ
PHE
B
626
38.971
44.277
21.384
1.00
20.75


ATOM
3351
C
PHE
B
626
35.851
40.352
21.279
1.00
20.36


ATOM
3352
O
PHE
B
626
36.993
39.951
21.066
1.00
19.87


ATOM
3353
N
ALA
B
627
35.211
40.117
22.420
1.00
20.43


ATOM
3354
CA
ALA
B
627
35.853
39.367
23.490
1.00
21.24


ATOM
3355
CB
ALA
B
627
34.950
39.322
24.713
1.00
23.11


ATOM
3356
C
ALA
B
627
36.192
37.949
23.033
1.00
20.95


ATOM
3357
O
ALA
B
627
37.274
37.433
23.329
1.00
21.81


ATOM
3358
N
ALA
B
628
35.267
37.327
22.305
1.00
19.64


ATOM
3359
CA
ALA
B
628
35.474
35.970
21.808
1.00
18.50


ATOM
3360
CB
ALA
B
628
34.194
35.453
21.156
1.00
21.27


ATOM
3361
C
ALA
B
628
36.619
35.901
20.808
1.00
18.67


ATOM
3362
O
ALA
B
628
37.415
34.958
20.827
1.00
21.28


ATOM
3363
N
LEU
B
629
36.695
36.890
19.921
1.00
19.77


ATOM
3364
CA
LEU
B
629
37.748
36.926
18.911
1.00
20.08


ATOM
3365
CB
LEU
B
629
37.449
38.026
17.885
1.00
20.64


ATOM
3366
CG
LEU
B
629
36.265
37.740
16.957
1.00
20.56


ATOM
3367
CD1
LEU
B
629
35.933
38.980
16.138
1.00
20.95


ATOM
3368
CD2
LEU
B
629
36.612
36.556
16.048
1.00
21.88


ATOM
3369
C
LEU
B
629
39.097
37.175
19.565
1.00
20.23


ATOM
3370
O
LEU
B
629
40.083
36.505
19.254
1.00
20.58


ATOM
3371
N
LYS
B
630
39.131
38.142
20.478
1.00
22.49


ATOM
3372
CA
LYS
B
630
40.354
38.517
21.184
1.00
24.06


ATOM
3373
CB
LYS
B
630
40.218
39.936
21.730
1.00
29.47


ATOM
3374
CG
LYS
B
630
40.467
41.003
20.712
1.00
30.15


ATOM
3375
CD
LYS
B
630
41.918
40.980
20.304
1.00
30.05


ATOM
3376
CE
LYS
B
630
42.193
42.037
19.271
1.00
29.88


ATOM
3377
NZ
LYS
B
630
43.597
41.963
18.828
1.00
29.81


ATOM
3378
C
LYS
B
630
40.727
37.597
22.331
1.00
24.07


ATOM
3379
O
LYS
B
630
41.585
36.724
22.197
1.00
23.83


ATOM
3380
N
ALA
B
631
40.091
37.815
23.475
1.00
24.13


ATOM
3381
CA
ALA
B
631
40.368
37.020
24.659
1.00
24.70


ATOM
3382
CB
ALA
B
631
39.527
37.516
25.828
1.00
25.17


ATOM
3383
C
ALA
B
631
40.121
35.534
24.437
1.00
25.41


ATOM
3384
O
ALA
B
631
40.882
34.700
24.922
1.00
25.73


ATOM
3385
N
GLY
B
632
39.060
35.203
23.705
1.00
24.21


ATOM
3386
CA
GLY
B
632
38.743
33.804
23.468
1.00
23.42


ATOM
3387
C
GLY
B
632
39.586
33.166
22.380
1.00
22.70


ATOM
3388
O
GLY
B
632
39.440
31.978
22.090
1.00
24.46


ATOM
3389
N
LYS
B
633
40.456
33.968
21.775
1.00
23.53


ATOM
3390
CA
LYS
B
633
41.357
33.531
20.717
1.00
24.70


ATOM
3391
CB
LYS
B
633
42.419
32.592
21.292
1.00
32.80


ATOM
3392
CG
LYS
B
633
43.316
33.272
22.310
1.00
33.19


ATOM
3393
CD
LYS
B
633
44.524
32.424
22.662
1.00
33.59


ATOM
3394
CE
LYS
B
633
45.416
33.167
23.643
1.00
33.78


ATOM
3395
NZ
LYS
B
633
45.749
34.527
23.130
1.00
34.10


ATOM
3396
C
LYS
B
633
40.709
32.888
19.499
1.00
24.23


ATOM
3397
O
LYS
B
633
41.243
31.935
18.928
1.00
24.88


ATOM
3398
N
ILE
B
634
39.565
33.411
19.079
1.00
22.51


ATOM
3399
CA
ILE
B
634
38.911
32.861
17.907
1.00
20.76


ATOM
3400
CB
ILE
B
634
37.376
32.982
18.036
1.00
22.93


ATOM
3401
CG2
ILE
B
634
36.694
32.531
16.750
1.00
23.15


ATOM
3402
CG1
ILE
B
634
36.907
32.122
19.218
1.00
22.60


ATOM
3403
CD1
ILE
B
634
35.410
32.116
19.444
1.00
24.49


ATOM
3404
C
ILE
B
634
39.424
33.612
16.680
1.00
21.02


ATOM
3405
O
ILE
B
634
39.394
33.109
15.559
1.00
21.18


ATOM
3406
N
GLN
B
635
39.920
34.821
16.911
1.00
20.73


ATOM
3407
CA
GLN
B
635
40.453
35.656
15.848
1.00
21.87


ATOM
3408
CB
GLN
B
635
41.023
36.933
16.464
1.00
28.05


ATOM
3409
CG
GLN
B
635
41.703
37.868
15.503
1.00
29.39


ATOM
3410
CD
GLN
B
635
42.362
39.034
16.217
1.00
27.87


ATOM
3411
OE1
GLN
B
635
43.020
39.856
15.596
1.00
29.76


ATOM
3412
NE2
GLN
B
635
42.178
39.110
17.532
1.00
27.16


ATOM
3413
C
GLN
B
635
41.543
34.904
15.089
1.00
22.14


ATOM
3414
O
GLN
B
635
41.600
34.934
13.858
1.00
21.83


ATOM
3415
N
ASN
B
636
42.387
34.224
15.854
1.00
23.53


ATOM
3416
CA
ASN
B
636
43.504
33.447
15.335
1.00
24.32


ATOM
3417
CB
ASN
B
636
44.216
32.735
16.486
1.00
22.54


ATOM
3418
CG
ASN
B
636
44.607
33.675
17.606
1.00
22.42


ATOM
3419
OD1
ASN
B
636
45.788
33.821
17.921
1.00
23.23


ATOM
3420
ND2
ASN
B
636
43.620
34.307
18.221
1.00
21.19


ATOM
3421
C
ASN
B
636
43.089
32.390
14.325
1.00
24.28


ATOM
3422
O
ASN
B
636
43.868
32.022
13.443
1.00
24.97


ATOM
3423
N
LYS
B
637
41.864
31.899
14.463
1.00
22.71


ATOM
3424
CA
LYS
B
637
41.355
30.842
13.597
1.00
22.76


ATOM
3425
CB
LYS
B
637
40.417
29.948
14.409
1.00
25.00


ATOM
3426
CG
LYS
B
637
41.028
29.410
15.688
1.00
25.88


ATOM
3427
CD
LYS
B
637
39.983
28.674
16.515
1.00
24.87


ATOM
3428
CE
LYS
B
637
40.570
28.186
17.820
1.00
26.38


ATOM
3429
NZ
LYS
B
637
41.716
27.261
17.598
1.00
26.67


ATOM
3430
C
LYS
B
637
40.630
31.305
12.341
1.00
22.83


ATOM
3431
O
LYS
B
637
40.289
30.488
11.483
1.00
22.28


ATOM
3432
N
LEU
B
638
40.407
32.610
12.218
1.00
21.88


ATOM
3433
CA
LEU
B
638
39.669
33.131
11.081
1.00
22.21


ATOM
3434
CB
LEU
B
638
38.421
33.855
11.601
1.00
18.60


ATOM
3435
CG
LEU
B
638
37.598
33.093
12.650
1.00
20.22


ATOM
3436
CD1
LEU
B
638
36.507
34.001
13.212
1.00
18.99


ATOM
3437
CD2
LEU
B
638
36.985
31.847
12.035
1.00
19.54


ATOM
3438
C
LEU
B
638
40.447
34.061
10.160
1.00
21.99


ATOM
3439
O
LEU
B
638
41.531
34.549
10.502
1.00
21.62


ATOM
3440
N
THR
B
639
39.878
34.299
8.982
1.00
19.43


ATOM
3441
CA
THR
B
639
40.474
35.188
7.998
1.00
20.58


ATOM
3442
CB
THR
B
639
39.900
34.937
6.593
1.00
24.74


ATOM
3443
OG1
THR
B
639
38.501
35.257
6.581
1.00
23.76


ATOM
3444
CG2
THR
B
639
40.075
33.472
6.195
1.00
24.89


ATOM
3445
C
THR
B
639
40.110
36.609
8.413
1.00
20.43


ATOM
3446
O
THR
B
639
39.185
36.802
9.203
1.00
20.14


ATOM
3447
N
ASP
B
640
40.828
37.594
7.884
1.00
22.11


ATOM
3448
CA
ASP
B
640
40.550
38.989
8.195
1.00
21.37


ATOM
3449
CB
ASP
B
640
41.576
39.908
7.528
1.00
24.51


ATOM
3450
CG
ASP
B
640
42.964
39.763
8.119
1.00
24.64


ATOM
3451
OD1
ASP
B
640
43.900
40.381
7.575
1.00
23.86


ATOM
3452
OD2
ASP
B
640
43.118
39.040
9.124
1.00
24.36


ATOM
3453
C
ASP
B
640
39.150
39.360
7.718
1.00
22.46


ATOM
3454
O
ASP
B
640
38.440
40.094
8.398
1.00
21.08


ATOM
3455
N
LEU
B
641
38.761
38.850
6.549
1.00
22.62


ATOM
3456
CA
LEU
B
641
37.436
39.127
5.988
1.00
22.81


ATOM
3457
CB
LEU
B
641
37.312
38.504
4.594
1.00
24.97


ATOM
3458
CG
LEU
B
641
37.449
39.409
3.365
1.00
27.28


ATOM
3459
CD1
LEU
B
641
38.476
40.500
3.601
1.00
25.76


ATOM
3460
CD2
LEU
B
641
37.793
38.557
2.152
1.00
25.23


ATOM
3461
C
LEU
B
641
36.338
38.574
6.888
1.00
22.25


ATOM
3462
O
LEU
B
641
35.295
39.204
7.086
1.00
21.31


ATOM
3463
N
GLU
B
642
36.561
37.379
7.417
1.00
20.49


ATOM
3464
CA
GLU
B
642
35.588
36.765
8.301
1.00
20.51


ATOM
3465
CB
GLU
B
642
36.005
35.327
8.615
1.00
24.37


ATOM
3466
CG
GLU
B
642
35.704
34.391
7.460
1.00
24.67


ATOM
3467
CD
GLU
B
642
36.405
33.053
7.574
1.00
24.64


ATOM
3468
OE1
GLU
B
642
36.092
32.159
6.760
1.00
27.01


ATOM
3469
OE2
GLU
B
642
37.267
32.893
8.461
1.00
24.86


ATOM
3470
C
GLU
B
642
35.427
37.579
9.581
1.00
20.92


ATOM
3471
O
GLU
B
642
34.309
37.764
10.069
1.00
20.75


ATOM
3472
N
ILE
B
643
36.542
38.076
10.108
1.00
21.11


ATOM
3473
CA
ILE
B
643
36.529
38.880
11.325
1.00
19.45


ATOM
3474
CB
ILE
B
643
37.973
39.195
11.771
1.00
22.34


ATOM
3475
CG2
ILE
B
643
37.970
40.210
12.912
1.00
21.69


ATOM
3476
CG1
ILE
B
643
38.652
37.895
12.217
1.00
20.78


ATOM
3477
CD1
ILE
B
643
40.165
37.993
12.357
1.00
22.35


ATOM
3478
C
ILE
B
643
35.762
40.177
11.055
1.00
19.94


ATOM
3479
O
ILE
B
643
34.921
40.598
11.858
1.00
19.49


ATOM
3480
N
LEU
B
644
36.044
40.790
9.911
1.00
19.97


ATOM
3481
CA
LEU
B
644
35.385
42.027
9.502
1.00
19.99


ATOM
3482
CB
LEU
B
644
35.926
42.466
8.135
1.00
21.41


ATOM
3483
CG
LEU
B
644
35.277
43.650
7.415
1.00
21.06


ATOM
3484
CD1
LEU
B
644
35.449
44.915
8.234
1.00
22.38


ATOM
3485
CD2
LEU
B
644
35.921
43.809
6.042
1.00
21.65


ATOM
3486
C
LEU
B
644
33.877
41.817
9.409
1.00
21.45


ATOM
3487
O
LEU
B
644
33.093
42.583
9.970
1.00
18.41


ATOM
3488
N
ALA
B
645
33.485
40.770
8.691
1.00
19.49


ATOM
3489
CA
ALA
B
645
32.076
40.444
8.499
1.00
20.21


ATOM
3490
CB
ALA
B
645
31.940
39.266
7.539
1.00
18.61


ATOM
3491
C
ALA
B
645
31.371
40.125
9.806
1.00
20.78


ATOM
3492
O
ALA
B
645
30.229
40.535
10.009
1.00
19.80


ATOM
3493
N
LEU
B
646
32.047
39.395
10.688
1.00
17.92


ATOM
3494
CA
LEU
B
646
31.455
39.028
11.968
1.00
18.51


ATOM
3495
CB
LEU
B
646
32.381
38.084
12.735
1.00
21.14


ATOM
3496
CG
LEU
B
646
32.393
36.631
12.250
1.00
19.75


ATOM
3497
CD1
LEU
B
646
33.560
35.903
12.894
1.00
20.35


ATOM
3498
CD2
LEU
B
646
31.077
35.951
12.587
1.00
20.12


ATOM
3499
C
LEU
B
646
31.138
40.241
12.837
1.00
17.72


ATOM
3500
O
LEU
B
646
30.075
40.304
13.460
1.00
18.91


ATOM
3501
N
LEU
B
647
32.054
41.202
12.893
1.00
18.38


ATOM
3502
CA
LEU
B
647
31.815
42.387
13.710
1.00
18.99


ATOM
3503
CB
LEU
B
647
33.074
43.255
13.800
1.00
16.80


ATOM
3504
CG
LEU
B
647
32.940
44.461
14.734
1.00
18.47


ATOM
3505
CD1
LEU
B
647
32.637
43.978
16.146
1.00
18.48


ATOM
3506
CD2
LEU
B
647
34.221
45.278
14.707
1.00
18.50


ATOM
3507
C
LEU
B
647
30.666
43.201
13.128
1.00
18.90


ATOM
3508
O
LEU
B
647
29.776
43.646
13.861
1.00
18.98


ATOM
3509
N
ILE
B
648
30.689
43.399
11.813
1.00
18.80


ATOM
3510
CA
ILE
B
648
29.633
44.146
11.134
1.00
17.53


ATOM
3511
CB
ILE
B
648
29.948
44.298
9.620
1.00
17.43


ATOM
3512
CG2
ILE
B
648
28.747
44.886
8.884
1.00
16.56


ATOM
3513
CG1
ILE
B
648
31.189
45.181
9.439
1.00
16.47


ATOM
3514
CD1
ILE
B
648
31.622
45.377
7.987
1.00
16.64


ATOM
3515
C
ILE
B
648
28.303
43.405
11.322
1.00
19.67


ATOM
3516
O
ILE
B
648
27.268
44.020
11.608
1.00
19.92


ATOM
3517
N
ALA
B
649
28.327
42.084
11.170
1.00
17.14


ATOM
3518
CA
ALA
B
649
27.105
41.297
11.335
1.00
19.06


ATOM
3519
CB
ALA
B
649
27.353
39.830
10.964
1.00
15.65


ATOM
3520
C
ALA
B
649
26.562
41.381
12.753
1.00
17.80


ATOM
3521
O
ALA
B
649
25.360
41.559
12.957
1.00
16.89


ATOM
3522
N
ALA
B
650
27.442
41.245
13.738
1.00
17.06


ATOM
3523
CA
ALA
B
650
27.016
41.316
15.128
1.00
16.09


ATOM
3524
CB
ALA
B
650
28.219
41.166
16.056
1.00
20.12


ATOM
3525
C
ALA
B
650
26.299
42.641
15.406
1.00
17.22


ATOM
3526
O
ALA
B
650
25.239
42.660
16.031
1.00
18.13


ATOM
3527
N
LEU
B
651
26.875
43.739
14.935
1.00
18.31


ATOM
3528
CA
LEU
B
651
26.295
45.065
15.145
1.00
18.19


ATOM
3529
CB
LEU
B
651
27.302
46.143
14.744
1.00
17.38


ATOM
3530
CG
LEU
B
651
28.532
46.318
15.633
1.00
17.82


ATOM
3531
CD1
LEU
B
651
29.580
47.146
14.917
1.00
17.72


ATOM
3532
CD2
LEU
B
651
28.108
46.993
16.939
1.00
16.75


ATOM
3533
C
LEU
B
651
25.010
45.305
14.363
1.00
19.12


ATOM
3534
O
LEU
B
651
24.145
46.073
14.792
1.00
19.03


ATOM
3535
N
SER
B
652
24.879
44.644
13.218
1.00
16.50


ATOM
3536
CA
SER
B
652
23.717
44.861
12.361
1.00
15.50


ATOM
3537
CB
SER
B
652
24.165
45.025
10.902
1.00
19.61


ATOM
3538
OG
SER
B
652
25.258
45.908
10.760
1.00
18.90


ATOM
3539
C
SER
B
652
22.667
43.764
12.374
1.00
17.20


ATOM
3540
O
SER
B
652
21.616
43.932
11.770
1.00
16.98


ATOM
3541
N
HIS
B
653
22.922
42.664
13.073
1.00
19.06


ATOM
3542
CA
HIS
B
653
22.001
41.533
12.998
1.00
19.69


ATOM
3543
CB
HIS
B
653
22.594
40.312
13.697
1.00
17.94


ATOM
3544
CG
HIS
B
653
22.332
40.270
15.165
1.00
17.54


ATOM
3545
CD2
HIS
B
653
21.396
39.612
15.888
1.00
16.38


ATOM
3546
ND1
HIS
B
653
23.064
41.010
16.066
1.00
17.02


ATOM
3547
CE1
HIS
B
653
22.592
40.809
17.282
1.00
14.84


ATOM
3548
NE2
HIS
B
653
21.582
39.965
17.202
1.00
19.75


ATOM
3549
C
HIS
B
653
20.548
41.689
13.430
1.00
20.16


ATOM
3550
O
HIS
B
653
19.734
40.833
13.106
1.00
18.45


ATOM
3551
N
ASP
B
654
20.206
42.762
14.143
1.00
15.51


ATOM
3552
CA
ASP
B
654
18.808
42.945
14.562
1.00
15.82


ATOM
3553
CB
ASP
B
654
18.680
42.848
16.082
1.00
17.70


ATOM
3554
CG
ASP
B
654
18.401
41.444
16.565
1.00
16.46


ATOM
3555
OD1
ASP
B
654
17.724
40.681
15.845
1.00
17.13


ATOM
3556
OD2
ASP
B
654
18.826
41.109
17.689
1.00
16.53


ATOM
3557
C
ASP
B
654
18.246
44.300
14.120
1.00
15.98


ATOM
3558
O
ASP
B
654
17.249
44.775
14.679
1.00
16.02


ATOM
3559
N
LEU
B
655
18.875
44.903
13.113
1.00
14.12


ATOM
3560
CA
LEU
B
655
18.474
46.212
12.585
1.00
16.45


ATOM
3561
CB
LEU
B
655
19.191
46.465
11.253
1.00
22.99


ATOM
3562
CG
LEU
B
655
20.250
47.557
11.043
1.00
25.93


ATOM
3563
CD1
LEU
B
655
20.660
48.211
12.341
1.00
24.18


ATOM
3564
CD2
LEU
B
655
21.435
46.946
10.315
1.00
23.72


ATOM
3565
C
LEU
B
655
16.968
46.355
12.374
1.00
15.99


ATOM
3566
O
LEU
B
655
16.332
45.488
11.777
1.00
16.81


ATOM
3567
N
ASP
B
656
16.403
47.452
12.877
1.00
18.46


ATOM
3568
CA
ASP
B
656
14.975
47.741
12.723
1.00
18.67


ATOM
3569
CB
ASP
B
656
14.676
48.025
11.243
1.00
19.71


ATOM
3570
CG
ASP
B
656
13.318
48.677
11.028
1.00
21.79


ATOM
3571
OD1
ASP
B
656
12.968
49.591
11.803
1.00
19.47


ATOM
3572
OD2
ASP
B
656
12.612
48.282
10.075
1.00
21.77


ATOM
3573
C
ASP
B
656
14.046
46.647
13.244
1.00
19.00


ATOM
3574
O
ASP
B
656
12.965
46.434
12.697
1.00
18.21


ATOM
3575
N
HIS
B
657
14.460
45.952
14.298
1.00
17.23


ATOM
3576
CA
HIS
B
657
13.631
44.899
14.864
1.00
16.33


ATOM
3577
CB
HIS
B
657
14.377
44.174
15.983
1.00
19.47


ATOM
3578
CG
HIS
B
657
13.705
42.915
16.419
1.00
18.64


ATOM
3579
CD2
HIS
B
657
12.475
42.701
16.941
1.00
17.65


ATOM
3580
ND1
HIS
B
657
14.300
41.673
16.318
1.00
19.33


ATOM
3581
CE1
HIS
B
657
13.467
40.752
16.763
1.00
16.32


ATOM
3582
NE2
HIS
B
657
12.352
41.349
17.147
1.00
20.76


ATOM
3583
C
HIS
B
657
12.352
45.546
15.409
1.00
17.90


ATOM
3584
O
HIS
B
657
12.419
46.529
16.151
1.00
17.75


ATOM
3585
N
PRO
B
658
11.176
45.011
15.034
1.00
19.30


ATOM
3586
CD
PRO
B
658
11.026
43.936
14.032
1.00
15.12


ATOM
3587
CA
PRO
B
658
9.863
45.519
15.463
1.00
20.23


ATOM
3588
CB
PRO
B
658
8.922
44.970
14.398
1.00
15.90


ATOM
3589
CG
PRO
B
658
9.539
43.612
14.093
1.00
14.22


ATOM
3590
C
PRO
B
658
9.422
45.146
16.877
1.00
19.73


ATOM
3591
O
PRO
B
658
8.411
45.650
17.371
1.00
20.21


ATOM
3592
N
GLY
B
659
10.160
44.258
17.530
1.00
20.02


ATOM
3593
CA
GLY
B
659
9.800
43.886
18.884
1.00
20.59


ATOM
3594
C
GLY
B
659
8.794
42.760
18.918
1.00
20.21


ATOM
3595
O
GLY
B
659
8.194
42.491
19.954
1.00
21.72


ATOM
3596
N
VAL
B
660
8.589
42.117
17.772
1.00
20.05


ATOM
3597
CA
VAL
B
660
7.685
40.980
17.675
1.00
19.03


ATOM
3598
CB
VAL
B
660
6.353
41.336
16.963
1.00
22.30


ATOM
3599
CG1
VAL
B
660
5.551
42.293
17.825
1.00
23.15


ATOM
3600
CG2
VAL
B
660
6.623
41.946
15.599
1.00
22.17


ATOM
3601
C
VAL
B
660
8.432
39.915
16.882
1.00
20.57


ATOM
3602
O
VAL
B
660
9.340
40.233
16.115
1.00
20.96


ATOM
3603
N
SER
B
661
8.043
38.660
17.068
1.00
18.27


ATOM
3604
CA
SER
B
661
8.707
37.525
16.413
1.00
19.30


ATOM
3605
CB
SER
B
661
8.450
36.256
17.217
1.00
23.22


ATOM
3606
OG
SER
B
661
7.108
35.823
17.058
1.00
22.03


ATOM
3607
C
SER
B
661
8.337
37.237
14.961
1.00
19.20


ATOM
3608
O
SER
B
661
7.410
37.814
14.402
1.00
16.38


ATOM
3609
N
ASN
B
662
9.080
36.311
14.360
1.00
18.48


ATOM
3610
CA
ASN
B
662
8.810
35.905
12.989
1.00
17.98


ATOM
3611
CB
ASN
B
662
9.832
34.868
12.521
1.00
19.15


ATOM
3612
CG
ASN
B
662
11.117
35.491
12.060
1.00
20.55


ATOM
3613
OD1
ASN
B
662
11.113
36.584
11.504
1.00
18.07


ATOM
3614
ND2
ASN
B
662
12.229
34.788
12.263
1.00
19.60


ATOM
3615
C
ASN
B
662
7.428
35.275
12.943
1.00
18.27


ATOM
3616
O
ASN
B
662
6.651
35.512
12.020
1.00
19.29


ATOM
3617
N
GLN
B
663
7.129
34.463
13.952
1.00
19.10


ATOM
3618
CA
GLN
B
663
5.845
33.793
14.020
1.00
19.98


ATOM
3619
CB
GLN
B
663
5.763
32.909
15.267
1.00
47.82


ATOM
3620
CG
GLN
B
663
6.544
31.609
15.160
1.00
48.95


ATOM
3621
CD
GLN
B
663
8.056
31.793
15.228
1.00
49.43


ATOM
3622
OE1
GLN
B
663
8.814
30.853
14.978
1.00
49.36


ATOM
3623
NE2
GLN
B
663
8.499
32.997
15.576
1.00
48.96


ATOM
3624
C
GLN
B
663
4.708
34.798
14.029
1.00
19.45


ATOM
3625
O
GLN
B
663
3.701
34.609
13.352
1.00
19.22


ATOM
3626
N
PHE
B
664
4.883
35.869
14.795
1.00
17.76


ATOM
3627
CA
PHE
B
664
3.866
36.909
14.888
1.00
18.71


ATOM
3628
CB
PHE
B
664
4.266
37.946
15.938
1.00
20.58


ATOM
3629
CG
PHE
B
664
3.280
39.077
16.084
1.00
20.67


ATOM
3630
CD1
PHE
B
664
3.340
40.185
15.243
1.00
20.97


ATOM
3631
CD2
PHE
B
664
2.291
39.031
17.064
1.00
20.35


ATOM
3632
CE1
PHE
B
664
2.428
41.232
15.377
1.00
20.58


ATOM
3633
CE2
PHE
B
664
1.377
40.074
17.203
1.00
21.94


ATOM
3634
CZ
PHE
B
664
1.448
41.174
16.357
1.00
21.03


ATOM
3635
C
PHE
B
664
3.691
37.571
13.525
1.00
17.64


ATOM
3636
O
PHE
B
664
2.574
37.781
13.071
1.00
17.39


ATOM
3637
N
LEU
B
665
4.801
37.883
12.865
1.00
18.84


ATOM
3638
CA
LEU
B
665
4.734
38.504
11.552
1.00
20.08


ATOM
3639
CB
LEU
B
665
6.146
38.866
11.078
1.00
18.16


ATOM
3640
CG
LEU
B
665
6.834
39.975
11.886
1.00
19.07


ATOM
3641
CD1
LEU
B
665
8.288
40.092
11.490
1.00
19.47


ATOM
3642
CD2
LEU
B
665
6.119
41.289
11.654
1.00
18.80


ATOM
3643
C
LEU
B
665
4.039
37.582
10.540
1.00
20.00


ATOM
3644
O
LEU
B
665
3.350
38.044
9.627
1.00
21.88


ATOM
3645
N
ILE
B
666
4.222
36.276
10.700
1.00
18.71


ATOM
3646
CA
ILE
B
666
3.593
35.317
9.806
1.00
19.12


ATOM
3647
CB
ILE
B
666
4.239
33.920
9.951
1.00
22.08


ATOM
3648
CG2
ILE
B
666
3.423
32.879
9.199
1.00
21.74


ATOM
3649
CG1
ILE
B
666
5.674
33.967
9.421
1.00
21.76


ATOM
3650
CD1
ILE
B
666
6.456
32.684
9.619
1.00
21.29


ATOM
3651
C
ILE
B
666
2.104
35.218
10.119
1.00
18.58


ATOM
3652
O
ILE
B
666
1.274
35.193
9.211
1.00
20.21


ATOM
3653
N
ASN
B
667
1.773
35.183
11.408
1.00
21.92


ATOM
3654
CA
ASN
B
667
0.378
35.072
11.837
1.00
22.79


ATOM
3655
CB
ASN
B
667
0.295
34.756
13.334
1.00
23.85


ATOM
3656
CG
ASN
B
667
0.779
33.354
13.669
1.00
23.91


ATOM
3657
OD1
ASN
B
667
0.712
32.444
12.843
1.00
24.94


ATOM
3658
ND2
ASN
B
667
1.250
33.173
14.895
1.00
23.83


ATOM
3659
C
ASN
B
667
−0.472
36.305
11.544
1.00
23.14


ATOM
3660
O
ASN
B
667
−1.702
36.213
11.470
1.00
22.85


ATOM
3661
N
THR
B
668
0.169
37.459
11.392
1.00
24.81


ATOM
3662
CA
THR
B
668
−0.566
38.677
11.086
1.00
25.96


ATOM
3663
CB
THR
B
668
−0.019
39.894
11.882
1.00
21.17


ATOM
3664
OG1
THR
B
668
1.404
39.984
11.714
1.00
23.05


ATOM
3665
CG2
THR
B
668
−0.338
39.753
13.362
1.00
22.09


ATOM
3666
C
THR
B
668
−0.511
38.973
9.585
1.00
26.69


ATOM
3667
O
THR
B
668
−0.961
40.022
9.139
1.00
27.70


ATOM
3668
N
ASN
B
669
0.026
38.030
8.815
1.00
26.73


ATOM
3669
CA
ASN
B
669
0.138
38.169
7.362
1.00
27.16


ATOM
3670
CB
ASN
B
669
−1.255
38.135
6.726
1.00
36.60


ATOM
3671
CG
ASN
B
669
−1.940
36.796
6.906
1.00
36.71


ATOM
3672
OD1
ASN
B
669
−1.482
35.775
6.387
1.00
36.69


ATOM
3673
ND2
ASN
B
669
−3.039
36.789
7.650
1.00
37.50


ATOM
3674
C
ASN
B
669
0.867
39.453
6.978
1.00
27.24


ATOM
3675
O
ASN
B
669
0.440
40.195
6.088
1.00
26.93


ATOM
3676
N
SER
B
670
1.981
39.696
7.659
1.00
23.11


ATOM
3677
CA
SER
B
670
2.802
40.876
7.435
1.00
22.67


ATOM
3678
CB
SER
B
670
3.949
40.898
8.448
1.00
34.05


ATOM
3679
OG
SER
B
670
4.874
41.925
8.154
1.00
35.41


ATOM
3680
C
SER
B
670
3.382
40.916
6.028
1.00
22.16


ATOM
3681
O
SER
B
670
3.580
39.880
5.388
1.00
22.16


ATOM
3682
N
GLU
B
671
3.662
42.125
5.548
1.00
21.76


ATOM
3683
CA
GLU
B
671
4.236
42.279
4.225
1.00
21.00


ATOM
3684
CB
GLU
B
671
4.388
43.757
3.872
1.00
26.81


ATOM
3685
CG
GLU
B
671
4.799
43.990
2.433
1.00
26.53


ATOM
3686
CD
GLU
B
671
4.963
45.461
2.099
1.00
27.67


ATOM
3687
OE1
GLU
B
671
6.052
46.018
2.361
1.00
28.24


ATOM
3688
OE2
GLU
B
671
3.995
46.062
1.584
1.00
26.44


ATOM
3689
C
GLU
B
671
5.607
41.617
4.228
1.00
20.25


ATOM
3690
O
GLU
B
671
5.996
40.962
3.271
1.00
20.37


ATOM
3691
N
LEU
B
672
6.332
41.799
5.323
1.00
20.82


ATOM
3692
CA
LEU
B
672
7.664
41.222
5.476
1.00
21.28


ATOM
3693
CB
LEU
B
672
8.189
41.544
6.872
1.00
29.67


ATOM
3694
CG
LEU
B
672
9.522
42.279
7.026
1.00
30.73


ATOM
3695
CD1
LEU
B
672
9.670
43.391
6.003
1.00
30.03


ATOM
3696
CD2
LEU
B
672
9.588
42.833
8.438
1.00
30.18


ATOM
3697
C
LEU
B
672
7.610
39.711
5.277
1.00
21.18


ATOM
3698
O
LEU
B
672
8.470
39.121
4.620
1.00
20.85


ATOM
3699
N
ALA
B
673
6.585
39.084
5.844
1.00
21.74


ATOM
3700
CA
ALA
B
673
6.435
37.635
5.726
1.00
21.93


ATOM
3701
CB
ALA
B
673
5.285
37.150
6.607
1.00
19.72


ATOM
3702
C
ALA
B
673
6.202
37.211
4.282
1.00
22.57


ATOM
3703
O
ALA
B
673
6.723
36.189
3.839
1.00
21.41


ATOM
3704
N
LEU
B
674
5.410
37.987
3.548
1.00
20.77


ATOM
3705
CA
LEU
B
674
5.151
37.664
2.153
1.00
21.89


ATOM
3706
CB
LEU
B
674
4.078
38.586
1.572
1.00
30.80


ATOM
3707
CG
LEU
B
674
3.816
38.413
0.069
1.00
31.55


ATOM
3708
CD1
LEU
B
674
3.312
37.005
−0.217
1.00
31.01


ATOM
3709
CD2
LEU
B
674
2.799
39.449
−0.391
1.00
30.99


ATOM
3710
C
LEU
B
674
6.431
37.811
1.336
1.00
22.16


ATOM
3711
O
LEU
B
674
6.775
36.929
0.552
1.00
21.85


ATOM
3712
N
MET
B
675
7.132
38.922
1.536
1.00
23.84


ATOM
3713
CA
MET
B
675
8.366
39.192
0.809
1.00
25.40


ATOM
3714
CB
MET
B
675
8.979
40.513
1.278
1.00
42.14


ATOM
3715
CG
MET
B
675
8.153
41.746
0.946
1.00
42.93


ATOM
3716
SD
MET
B
675
8.869
43.254
1.635
1.00
43.64


ATOM
3717
CE
MET
B
675
10.093
43.646
0.397
1.00
43.26


ATOM
3718
C
MET
B
675
9.397
38.080
0.973
1.00
24.69


ATOM
3719
O
MET
B
675
10.072
37.706
0.010
1.00
25.28


ATOM
3720
N
TYR
B
676
9.514
37.546
2.186
1.00
22.91


ATOM
3721
CA
TYR
B
676
10.503
36.506
2.449
1.00
23.58


ATOM
3722
CB
TYR
B
676
11.316
36.899
3.687
1.00
22.54


ATOM
3723
CG
TYR
B
676
11.987
38.248
3.527
1.00
23.06


ATOM
3724
CD1
TYR
B
676
11.763
39.276
4.437
1.00
23.12


ATOM
3725
CE1
TYR
B
676
12.338
40.539
4.259
1.00
22.13


ATOM
3726
CD2
TYR
B
676
12.814
38.508
2.432
1.00
24.18


ATOM
3727
CE2
TYR
B
676
13.400
39.762
2.247
1.00
22.56


ATOM
3728
CZ
TYR
B
676
13.155
40.772
3.161
1.00
23.95


ATOM
3729
OH
TYR
B
676
13.719
42.015
2.974
1.00
23.51


ATOM
3730
C
TYR
B
676
9.973
35.074
2.578
1.00
22.94


ATOM
3731
O
TYR
B
676
10.640
34.204
3.144
1.00
23.18


ATOM
3732
N
ASN
B
677
8.781
34.840
2.034
1.00
23.86


ATOM
3733
CA
ASN
B
677
8.137
33.524
2.034
1.00
25.01


ATOM
3734
CB
ASN
B
677
8.760
32.633
0.948
1.00
56.05


ATOM
3735
CG
ASN
B
677
10.243
32.381
1.169
1.00
57.14


ATOM
3736
OD1
ASN
B
677
10.642
31.796
2.177
1.00
57.41


ATOM
3737
ND2
ASN
B
677
11.069
32.819
0.222
1.00
57.47


ATOM
3738
C
ASN
B
677
8.139
32.783
3.373
1.00
24.18


ATOM
3739
O
ASN
B
677
8.385
31.575
3.430
1.00
22.27


ATOM
3740
N
ASP
B
678
7.850
33.519
4.442
1.00
20.57


ATOM
3741
CA
ASP
B
678
7.783
32.970
5.794
1.00
20.56


ATOM
3742
CB
ASP
B
678
6.692
31.895
5.876
1.00
24.90


ATOM
3743
CG
ASP
B
678
5.310
32.442
5.609
1.00
26.44


ATOM
3744
OD1
ASP
B
678
5.139
33.676
5.661
1.00
24.56


ATOM
3745
OD2
ASP
B
678
4.386
31.632
5.359
1.00
26.91


ATOM
3746
C
ASP
B
678
9.074
32.390
6.358
1.00
19.72


ATOM
3747
O
ASP
B
678
9.067
31.843
7.464
1.00
21.82


ATOM
3748
N
GLU
B
679
10.175
32.513
5.625
1.00
18.31


ATOM
3749
CA
GLU
B
679
11.452
31.964
6.086
1.00
18.54


ATOM
3750
CB
GLU
B
679
12.148
31.211
4.955
1.00
42.65


ATOM
3751
CG
GLU
B
679
11.459
29.942
4.518
1.00
43.73


ATOM
3752
CD
GLU
B
679
12.276
29.188
3.492
1.00
44.02


ATOM
3753
OE1
GLU
B
679
12.480
29.723
2.381
1.00
44.05


ATOM
3754
OE2
GLU
B
679
12.723
28.066
3.803
1.00
44.29


ATOM
3755
C
GLU
B
679
12.407
33.021
6.611
1.00
18.73


ATOM
3756
O
GLU
B
679
12.768
33.939
5.875
1.00
19.73


ATOM
3757
N
SER
B
680
12.832
32.866
7.867
1.00
18.88


ATOM
3758
CA
SER
B
680
13.758
33.798
8.506
1.00
16.49


ATOM
3759
CB
SER
B
680
15.197
33.508
8.065
1.00
21.45


ATOM
3760
OG
SER
B
680
15.556
32.162
8.358
1.00
20.83


ATOM
3761
C
SER
B
680
13.383
35.226
8.127
1.00
16.21


ATOM
3762
O
SER
B
680
14.232
36.019
7.722
1.00
14.77


ATOM
3763
N
VAL
B
681
12.099
35.536
8.272
1.00
17.92


ATOM
3764
CA
VAL
B
681
11.558
36.838
7.904
1.00
16.01


ATOM
3765
CB
VAL
B
681
10.084
36.928
8.328
1.00
18.23


ATOM
3766
CG1
VAL
B
681
9.501
38.295
7.956
1.00
18.53


ATOM
3767
CG2
VAL
B
681
9.295
35.822
7.634
1.00
19.77


ATOM
3768
C
VAL
B
681
12.328
38.038
8.440
1.00
15.81


ATOM
3769
O
VAL
B
681
12.799
38.872
7.667
1.00
17.42


ATOM
3770
N
LEU
B
681A
12.449
38.120
9.761
1.00
15.91


ATOM
3771
CA
LEU
B
681A
13.164
39.216
10.410
1.00
17.15


ATOM
3772
CB
LEU
B
681A
13.094
39.055
11.925
1.00
20.96


ATOM
3773
CG
LEU
B
681A
11.729
39.310
12.559
1.00
24.02


ATOM
3774
CD1
LEU
B
681A
11.671
38.670
13.947
1.00
23.49


ATOM
3775
CD2
LEU
B
681A
11.500
40.805
12.619
1.00
23.37


ATOM
3776
C
LEU
B
681A
14.626
39.293
9.997
1.00
17.72


ATOM
3777
O
LEU
B
681A
15.151
40.367
9.733
1.00
16.37


ATOM
3778
N
GLU
B
682
15.281
38.141
9.936
1.00
16.35


ATOM
3779
CA
GLU
B
682
16.690
38.112
9.582
1.00
16.54


ATOM
3780
CB
GLU
B
682
17.226
36.693
9.797
1.00
17.48


ATOM
3781
CG
GLU
B
682
17.172
36.219
11.264
1.00
19.45


ATOM
3782
CD
GLU
B
682
15.765
35.939
11.783
1.00
17.96


ATOM
3783
OE1
GLU
B
682
14.873
35.587
10.975
1.00
16.02


ATOM
3784
OE2
GLU
B
682
15.553
36.043
13.015
1.00
18.67


ATOM
3785
C
GLU
B
682
16.957
38.616
8.162
1.00
16.65


ATOM
3786
O
GLU
B
682
17.956
39.307
7.908
1.00
17.06


ATOM
3787
N
HIS
B
683
16.068
38.286
7.233
1.00
16.83


ATOM
3788
CA
HIS
B
683
16.225
38.780
5.880
1.00
17.12


ATOM
3789
CB
HIS
B
683
15.193
38.144
4.953
1.00
21.77


ATOM
3790
CG
HIS
B
683
15.579
36.779
4.481
1.00
20.98


ATOM
3791
CD2
HIS
B
683
15.140
35.552
4.845
1.00
21.60


ATOM
3792
ND1
HIS
B
683
16.550
36.571
3.524
1.00
21.61


ATOM
3793
CE1
HIS
B
683
16.690
35.274
3.317
1.00
20.39


ATOM
3794
NE2
HIS
B
683
15.847
34.634
4.107
1.00
21.29


ATOM
3795
C
HIS
B
683
16.050
40.291
5.923
1.00
16.91


ATOM
3796
O
HIS
B
683
16.745
41.017
5.220
1.00
18.17


ATOM
3797
N
HIS
B
684
15.136
40.756
6.772
1.00
16.37


ATOM
3798
CA
HIS
B
684
14.900
42.194
6.906
1.00
18.67


ATOM
3799
CB
HIS
B
684
13.674
42.472
7.789
1.00
18.26


ATOM
3800
CG
HIS
B
684
13.376
43.934
7.962
1.00
19.15


ATOM
3801
CD2
HIS
B
684
13.327
44.714
9.068
1.00
20.53


ATOM
3802
ND1
HIS
B
684
13.124
44.769
6.896
1.00
20.23


ATOM
3803
CE1
HIS
B
684
12.939
46.002
7.336
1.00
19.60


ATOM
3804
NE2
HIS
B
684
13.056
45.996
8.650
1.00
19.94


ATOM
3805
C
HIS
B
684
16.131
42.858
7.516
1.00
18.24


ATOM
3806
O
HIS
B
684
16.556
43.927
7.066
1.00
19.27


ATOM
3807
N
HIS
B
685
16.706
42.228
8.537
1.00
18.19


ATOM
3808
CA
HIS
B
685
17.890
42.797
9.180
1.00
17.28


ATOM
3809
CB
HIS
B
685
18.349
41.957
10.376
1.00
17.43


ATOM
3810
CG
HIS
B
685
17.301
41.751
11.425
1.00
18.40


ATOM
3811
CD2
HIS
B
685
16.971
40.654
12.148
1.00
18.57


ATOM
3812
ND1
HIS
B
685
16.479
42.765
11.871
1.00
17.46


ATOM
3813
CE1
HIS
B
685
15.689
42.299
12.823
1.00
17.20


ATOM
3814
NE2
HIS
B
685
15.967
41.022
13.011
1.00
17.24


ATOM
3815
C
HIS
B
685
19.028
42.908
8.175
1.00
18.93


ATOM
3816
O
HIS
B
685
19.725
43.919
8.140
1.00
16.49


ATOM
3817
N
PHE
B
686
19.227
41.870
7.363
1.00
18.43


ATOM
3818
CA
PHE
B
686
20.289
41.922
6.363
1.00
19.77


ATOM
3819
CB
PHE
B
686
20.430
40.587
5.625
1.00
22.01


ATOM
3820
CG
PHE
B
686
21.424
40.635
4.501
1.00
22.74


ATOM
3821
CD1
PHE
B
686
22.771
40.879
4.757
1.00
22.40


ATOM
3822
CD2
PHE
B
686
21.008
40.509
3.185
1.00
22.19


ATOM
3823
CE1
PHE
B
686
23.689
41.003
3.714
1.00
22.33


ATOM
3824
CE2
PHE
B
686
21.915
40.631
2.139
1.00
23.22


ATOM
3825
CZ
PHE
B
686
23.259
40.882
2.406
1.00
22.45


ATOM
3826
C
PHE
B
686
20.017
43.025
5.345
1.00
19.33


ATOM
3827
O
PHE
B
686
20.924
43.747
4.938
1.00
19.34


ATOM
3828
N
ASP
B
687
18.762
43.149
4.927
1.00
20.18


ATOM
3829
CA
ASP
B
687
18.390
44.175
3.974
1.00
21.34


ATOM
3830
CB
ASP
B
687
16.886
44.130
3.728
1.00
29.63


ATOM
3831
CG
ASP
B
687
16.421
45.207
2.777
1.00
30.70


ATOM
3832
OD1
ASP
B
687
16.880
45.210
1.616
1.00
31.13


ATOM
3833
OD2
ASP
B
687
15.602
46.053
3.194
1.00
32.12


ATOM
3834
C
ASP
B
687
18.789
45.539
4.526
1.00
20.19


ATOM
3835
O
ASP
B
687
19.402
46.344
3.826
1.00
20.58


ATOM
3836
N
GLN
B
688
18.447
45.779
5.790
1.00
19.31


ATOM
3837
CA
GLN
B
688
18.773
47.044
6.447
1.00
20.14


ATOM
3838
CB
GLN
B
688
18.145
47.090
7.842
1.00
25.17


ATOM
3839
CG
GLN
B
688
16.621
47.113
7.823
1.00
26.26


ATOM
3840
CD
GLN
B
688
16.074
48.399
7.241
1.00
26.81


ATOM
3841
OE1
GLN
B
688
16.218
49.471
7.835
1.00
28.04


ATOM
3842
NE2
GLN
B
688
15.456
48.306
6.071
1.00
26.91


ATOM
3843
C
GLN
B
688
20.282
47.246
6.549
1.00
20.35


ATOM
3844
O
GLN
B
688
20.777
48.366
6.389
1.00
19.51


ATOM
3845
N
CYS
B
689
21.003
46.159
6.811
1.00
19.79


ATOM
3846
CA
CYS
B
689
22.457
46.199
6.924
1.00
20.08


ATOM
3847
CB
CYS
B
689
22.984
44.803
7.271
1.00
19.48


ATOM
3848
SG
CYS
B
689
24.795
44.663
7.336
1.00
17.52


ATOM
3849
C
CYS
B
689
23.085
46.679
5.617
1.00
19.76


ATOM
3850
O
CYS
B
689
23.949
47.563
5.605
1.00
19.63


ATOM
3851
N
LEU
B
690
22.655
46.072
4.517
1.00
19.56


ATOM
3852
CA
LEU
B
690
23.147
46.417
3.192
1.00
20.27


ATOM
3853
CB
LEU
B
690
22.516
45.489
2.154
1.00
27.59


ATOM
3854
CG
LEU
B
690
23.083
45.572
0.739
1.00
27.68


ATOM
3855
CD1
LEU
B
690
24.542
45.123
0.746
1.00
28.21


ATOM
3856
CD2
LEU
B
690
22.257
44.692
−0.183
1.00
28.78


ATOM
3857
C
LEU
B
690
22.795
47.867
2.872
1.00
20.36


ATOM
3858
O
LEU
B
690
23.607
48.606
2.332
1.00
21.09


ATOM
3859
N
MET
B
691
21.571
48.264
3.206
1.00
21.14


ATOM
3860
CA
MET
B
691
21.120
49.630
2.961
1.00
22.00


ATOM
3861
CB
MET
B
691
19.730
49.839
3.568
1.00
37.31


ATOM
3862
CG
MET
B
691
19.151
51.226
3.340
1.00
37.86


ATOM
3863
SD
MET
B
691
17.539
51.412
4.127
1.00
38.97


ATOM
3864
CE
MET
B
691
18.030
51.835
5.809
1.00
38.00


ATOM
3865
C
MET
B
691
22.109
50.629
3.572
1.00
22.35


ATOM
3866
O
MET
B
691
22.552
51.559
2.902
1.00
22.19


ATOM
3867
N
ILE
B
692
22.455
50.420
4.839
1.00
21.40


ATOM
3868
CA
ILE
B
692
23.385
51.308
5.534
1.00
21.97


ATOM
3869
CB
ILE
B
692
23.522
50.930
7.029
1.00
25.90


ATOM
3870
CG2
ILE
B
692
24.515
51.866
7.710
1.00
24.75


ATOM
3871
CG1
ILE
B
692
22.159
51.011
7.727
1.00
26.02


ATOM
3872
CD1
ILE
B
692
21.569
52.395
7.770
1.00
26.52


ATOM
3873
C
ILE
B
692
24.775
51.286
4.899
1.00
22.83


ATOM
3874
O
ILE
B
692
25.391
52.332
4.704
1.00
21.06


ATOM
3875
N
LEU
B
693
25.261
50.092
4.566
1.00
21.77


ATOM
3876
CA
LEU
B
693
26.581
49.951
3.951
1.00
23.08


ATOM
3877
CB
LEU
B
693
26.940
48.468
3.787
1.00
21.71


ATOM
3878
CG
LEU
B
693
27.301
47.701
5.060
1.00
21.98


ATOM
3879
CD1
LEU
B
693
27.277
46.218
4.784
1.00
22.22


ATOM
3880
CD2
LEU
B
693
28.677
48.144
5.553
1.00
22.27


ATOM
3881
C
LEU
B
693
26.664
50.635
2.595
1.00
23.02


ATOM
3882
O
LEU
B
693
27.752
51.009
2.153
1.00
24.07


ATOM
3883
N
ASN
B
694
25.519
50.794
1.934
1.00
24.41


ATOM
3884
CA
ASN
B
694
25.478
51.437
0.626
1.00
24.18


ATOM
3885
CB
ASN
B
694
24.448
50.760
−0.285
1.00
28.06


ATOM
3886
CG
ASN
B
694
24.886
49.387
−0.756
1.00
28.56


ATOM
3887
OD1
ASN
B
694
26.040
49.184
−1.122
1.00
29.03


ATOM
3888
ND2
ASN
B
694
23.953
48.439
−0.769
1.00
28.87


ATOM
3889
C
ASN
B
694
25.149
52.922
0.715
1.00
25.26


ATOM
3890
O
ASN
B
694
25.185
53.625
−0.295
1.00
25.49


ATOM
3891
N
SER
B
695
24.830
53.392
1.917
1.00
24.51


ATOM
3892
CA
SER
B
695
24.483
54.796
2.124
1.00
26.67


ATOM
3893
CB
SER
B
695
23.842
54.991
3.497
1.00
38.96


ATOM
3894
OG
SER
B
695
22.544
54.433
3.532
1.00
40.66


ATOM
3895
C
SER
B
695
25.679
55.724
1.999
1.00
26.23


ATOM
3896
O
SER
B
695
26.750
55.447
2.534
1.00
25.50


ATOM
3897
N
PRO
B
696
25.503
56.854
1.298
1.00
30.83


ATOM
3898
CD
PRO
B
696
24.242
57.397
0.766
1.00
35.10


ATOM
3899
CA
PRO
B
696
26.600
57.810
1.125
1.00
31.36


ATOM
3900
CB
PRO
B
696
25.936
58.959
0.362
1.00
35.40


ATOM
3901
CG
PRO
B
696
24.499
58.882
0.813
1.00
35.60


ATOM
3902
C
PRO
B
696
27.205
58.251
2.461
1.00
31.40


ATOM
3903
O
PRO
B
696
26.480
58.569
3.406
1.00
31.21


ATOM
3904
N
GLY
B
697
28.535
58.250
2.528
1.00
27.19


ATOM
3905
CA
GLY
B
697
29.227
58.653
3.741
1.00
26.21


ATOM
3906
C
GLY
B
697
29.268
57.587
4.821
1.00
25.99


ATOM
3907
O
GLY
B
697
29.813
57.811
5.901
1.00
25.64


ATOM
3908
N
ASN
B
698
28.698
56.422
4.532
1.00
25.20


ATOM
3909
CA
ASN
B
698
28.661
55.328
5.498
1.00
24.25


ATOM
3910
CB
ASN
B
698
27.215
54.970
5.867
1.00
26.49


ATOM
3911
CG
ASN
B
698
26.516
56.050
6.651
1.00
26.36


ATOM
3912
OD1
ASN
B
698
26.081
57.067
6.101
1.00
28.19


ATOM
3913
ND2
ASN
B
698
26.399
55.834
7.948
1.00
26.66


ATOM
3914
C
ASN
B
698
29.302
54.053
4.967
1.00
25.12


ATOM
3915
O
ASN
B
698
29.271
53.025
5.639
1.00
23.91


ATOM
3916
N
GLN
B
699
29.876
54.114
3.771
1.00
24.45


ATOM
3917
CA
GLN
B
699
30.456
52.923
3.146
1.00
24.83


ATOM
3918
CB
GLN
B
699
30.510
53.143
1.633
1.00
34.19


ATOM
3919
CG
GLN
B
699
29.191
53.687
1.093
1.00
34.82


ATOM
3920
CD
GLN
B
699
29.205
53.911
−0.399
1.00
35.20


ATOM
3921
OE1
GLN
B
699
29.346
52.971
−1.178
1.00
35.77


ATOM
3922
NE2
GLN
B
699
29.056
55.163
−0.808
1.00
35.33


ATOM
3923
C
GLN
B
699
31.819
52.493
3.683
1.00
23.99


ATOM
3924
O
GLN
B
699
32.860
52.768
3.083
1.00
25.36


ATOM
3925
N
ILE
B
700
31.791
51.794
4.814
1.00
20.88


ATOM
3926
CA
ILE
B
700
32.996
51.309
5.475
1.00
21.48


ATOM
3927
CB
ILE
B
700
32.696
50.857
6.919
1.00
24.53


ATOM
3928
CG2
ILE
B
700
32.254
52.056
7.759
1.00
24.80


ATOM
3929
CG1
ILE
B
700
31.623
49.765
6.917
1.00
24.49


ATOM
3930
CD1
ILE
B
700
31.415
49.110
8.268
1.00
24.76


ATOM
3931
C
ILE
B
700
33.674
50.154
4.740
1.00
20.59


ATOM
3932
O
ILE
B
700
34.754
49.717
5.141
1.00
22.27


ATOM
3933
N
LEU
B
701
33.051
49.665
3.669
1.00
23.58


ATOM
3934
CA
LEU
B
701
33.627
48.571
2.892
1.00
23.94


ATOM
3935
CB
LEU
B
701
32.609
47.433
2.711
1.00
22.71


ATOM
3936
CG
LEU
B
701
32.080
46.709
3.955
1.00
22.35


ATOM
3937
CD1
LEU
B
701
31.078
45.635
3.527
1.00
22.17


ATOM
3938
CD2
LEU
B
701
33.235
46.087
4.732
1.00
22.94


ATOM
3939
C
LEU
B
701
34.058
49.086
1.523
1.00
25.02


ATOM
3940
O
LEU
B
701
34.425
48.308
0.643
1.00
25.13


ATOM
3941
N
SER
B
702
34.020
50.404
1.354
1.00
28.81


ATOM
3942
CA
SER
B
702
34.383
51.035
0.087
1.00
30.23


ATOM
3943
CB
SER
B
702
34.177
52.549
0.174
1.00
36.19


ATOM
3944
OG
SER
B
702
35.139
53.137
1.032
1.00
36.39


ATOM
3945
C
SER
B
702
35.825
50.761
−0.323
1.00
30.61


ATOM
3946
O
SER
B
702
36.154
50.788
−1.511
1.00
30.09


ATOM
3947
N
GLY
B
703
36.680
50.504
0.661
1.00
30.88


ATOM
3948
CA
GLY
B
703
38.083
50.258
0.379
1.00
30.78


ATOM
3949
C
GLY
B
703
38.446
48.843
−0.029
1.00
31.56


ATOM
3950
O
GLY
B
703
39.570
48.595
−0.461
1.00
31.02


ATOM
3951
N
LEU
B
704
37.506
47.914
0.109
1.00
27.62


ATOM
3952
CA
LEU
B
704
37.748
46.522
−0.252
1.00
28.14


ATOM
3953
CB
LEU
B
704
36.638
45.628
0.312
1.00
24.97


ATOM
3954
CG
LEU
B
704
36.734
45.205
1.775
1.00
25.06


ATOM
3955
CD1
LEU
B
704
35.542
44.349
2.161
1.00
25.71


ATOM
3956
CD2
LEU
B
704
38.002
44.413
1.965
1.00
26.03


ATOM
3957
C
LEU
B
704
37.834
46.306
−1.760
1.00
27.32


ATOM
3958
O
LEU
B
704
37.211
47.026
−2.537
1.00
27.75


ATOM
3959
N
SER
B
705
38.610
45.305
−2.164
1.00
25.03


ATOM
3960
CA
SER
B
705
38.740
44.982
−3.576
1.00
25.33


ATOM
3961
CB
SER
B
705
39.909
44.019
−3.807
1.00
22.63


ATOM
3962
OG
SER
B
705
39.647
42.746
−3.249
1.00
22.15


ATOM
3963
C
SER
B
705
37.428
44.308
−3.952
1.00
25.55


ATOM
3964
O
SER
B
705
36.645
43.950
−3.073
1.00
25.89


ATOM
3965
N
ILE
B
706
37.190
44.134
−5.248
1.00
28.89


ATOM
3966
CA
ILE
B
706
35.960
43.503
−5.712
1.00
30.40


ATOM
3967
CB
ILE
B
706
35.967
43.351
−7.249
1.00
38.06


ATOM
3968
CG2
ILE
B
706
34.756
42.548
−7.701
1.00
38.45


ATOM
3969
CG1
ILE
B
706
35.984
44.737
−7.900
1.00
38.67


ATOM
3970
CD1
ILE
B
706
36.141
44.717
−9.410
1.00
38.81


ATOM
3971
C
ILE
B
706
35.735
42.134
−5.070
1.00
29.62


ATOM
3972
O
ILE
B
706
34.697
41.897
−4.452
1.00
29.75


ATOM
3973
N
GLU
B
707
36.704
41.234
−5.210
1.00
26.84


ATOM
3974
CA
GLU
B
707
36.579
39.900
−4.631
1.00
26.37


ATOM
3975
CB
GLU
B
707
37.811
39.056
−4.958
1.00
46.28


ATOM
3976
CG
GLU
B
707
37.665
38.188
−6.198
1.00
47.22


ATOM
3977
CD
GLU
B
707
36.441
37.287
−6.135
1.00
47.50


ATOM
3978
OE1
GLU
B
707
35.368
37.699
−6.626
1.00
47.38


ATOM
3979
OE2
GLU
B
707
36.548
36.171
−5.581
1.00
47.48


ATOM
3980
C
GLU
B
707
36.372
39.927
−3.121
1.00
25.62


ATOM
3981
O
GLU
B
707
35.505
39.227
−2.591
1.00
24.84


ATOM
3982
N
GLU
B
708
37.175
40.723
−2.419
1.00
24.00


ATOM
3983
CA
GLU
B
708
37.031
40.803
−0.974
1.00
22.95


ATOM
3984
CB
GLU
B
708
38.126
41.683
−0.365
1.00
34.88


ATOM
3985
CG
GLU
B
708
39.451
40.952
−0.225
1.00
34.89


ATOM
3986
CD
GLU
B
708
40.418
41.646
0.714
1.00
35.05


ATOM
3987
OE1
GLU
B
708
41.368
40.981
1.167
1.00
35.66


ATOM
3988
OE2
GLU
B
708
40.235
42.846
0.994
1.00
35.78


ATOM
3989
C
GLU
B
708
35.654
41.327
−0.579
1.00
23.54


ATOM
3990
O
GLU
B
708
35.049
40.824
0.368
1.00
23.08


ATOM
3991
N
TYR
B
709
35.169
42.332
−1.302
1.00
22.88


ATOM
3992
CA
TYR
B
709
33.855
42.908
−1.022
1.00
23.56


ATOM
3993
CB
TYR
B
709
33.583
44.072
−1.975
1.00
28.79


ATOM
3994
CG
TYR
B
709
32.228
44.708
−1.784
1.00
29.56


ATOM
3995
CD1
TYR
B
709
31.950
45.476
−0.656
1.00
29.43


ATOM
3996
CE1
TYR
B
709
30.691
46.039
−0.461
1.00
29.53


ATOM
3997
CD2
TYR
B
709
31.214
44.516
−2.718
1.00
30.32


ATOM
3998
CE2
TYR
B
709
29.950
45.072
−2.533
1.00
29.63


ATOM
3999
CZ
TYR
B
709
29.696
45.830
−1.404
1.00
30.45


ATOM
4000
OH
TYR
B
709
28.447
46.375
−1.221
1.00
30.77


ATOM
4001
C
TYR
B
709
32.764
41.841
−1.174
1.00
24.17


ATOM
4002
O
TYR
B
709
31.909
41.677
−0.297
1.00
23.90


ATOM
4003
N
LYS
B
710
32.800
41.117
−2.289
1.00
25.48


ATOM
4004
CA
LYS
B
710
31.821
40.062
−2.543
1.00
27.03


ATOM
4005
CB
LYS
B
710
32.064
39.418
−3.910
1.00
49.22


ATOM
4006
CG
LYS
B
710
31.519
37.999
−3.992
1.00
50.09


ATOM
4007
CD
LYS
B
710
31.985
37.258
−5.227
1.00
50.44


ATOM
4008
CE
LYS
B
710
31.769
35.762
−5.057
1.00
50.21


ATOM
4009
NZ
LYS
B
710
30.379
35.439
−4.621
1.00
50.37


ATOM
4010
C
LYS
B
710
31.872
38.972
−1.480
1.00
25.65


ATOM
4011
O
LYS
B
710
30.840
38.500
−0.998
1.00
26.50


ATOM
4012
N
THR
B
711
33.081
38.556
−1.128
1.00
23.83


ATOM
4013
CA
THR
B
711
33.249
37.511
−0.135
1.00
22.67


ATOM
4014
CB
THR
B
711
34.727
37.120
−0.008
1.00
25.01


ATOM
4015
OG1
THR
B
711
35.193
36.642
−1.275
1.00
25.50


ATOM
4016
CG2
THR
B
711
34.904
36.029
1.038
1.00
24.57


ATOM
4017
C
THR
B
711
32.723
37.944
1.232
1.00
22.92


ATOM
4018
O
THR
B
711
32.095
37.157
1.940
1.00
23.60


ATOM
4019
N
THR
B
712
32.975
39.202
1.586
1.00
20.46


ATOM
4020
CA
THR
B
712
32.551
39.742
2.871
1.00
20.53


ATOM
4021
CB
THR
B
712
33.201
41.117
3.125
1.00
22.65


ATOM
4022
OG1
THR
B
712
34.624
40.993
3.023
1.00
23.36


ATOM
4023
CG2
THR
B
712
32.849
41.628
4.515
1.00
22.01


ATOM
4024
C
THR
B
712
31.030
39.887
2.964
1.00
20.03


ATOM
4025
O
THR
B
712
30.433
39.564
3.992
1.00
19.56


ATOM
4026
N
LEU
B
713
30.405
40.375
1.899
1.00
20.53


ATOM
4027
CA
LEU
B
713
28.957
40.551
1.907
1.00
21.14


ATOM
4028
CB
LEU
B
713
28.484
41.186
0.599
1.00
32.94


ATOM
4029
CG
LEU
B
713
27.729
42.511
0.729
1.00
34.20


ATOM
4030
CD1
LEU
B
713
26.628
42.370
1.774
1.00
34.24


ATOM
4031
CD2
LEU
B
713
28.684
43.616
1.134
1.00
34.00


ATOM
4032
C
LEU
B
713
28.263
39.212
2.116
1.00
21.40


ATOM
4033
O
LEU
B
713
27.265
39.117
2.834
1.00
19.21


ATOM
4034
N
LYS
B
714
28.795
38.171
1.488
1.00
20.01


ATOM
4035
CA
LYS
B
714
28.220
36.837
1.620
1.00
20.38


ATOM
4036
CB
LYS
B
714
28.920
35.876
0.657
1.00
40.77


ATOM
4037
CG
LYS
B
714
28.564
34.419
0.847
1.00
41.45


ATOM
4038
CD
LYS
B
714
29.316
33.548
−0.149
1.00
42.11


ATOM
4039
CE
LYS
B
714
29.138
32.073
0.165
1.00
42.05


ATOM
4040
NZ
LYS
B
714
27.703
31.694
0.221
1.00
42.14


ATOM
4041
C
LYS
B
714
28.343
36.322
3.052
1.00
19.95


ATOM
4042
O
LYS
B
714
27.417
35.721
3.597
1.00
20.70


ATOM
4043
N
ILE
B
715
29.499
36.544
3.662
1.00
19.98


ATOM
4044
CA
ILE
B
715
29.705
36.101
5.029
1.00
18.62


ATOM
4045
CB
ILE
B
715
31.145
36.386
5.500
1.00
22.51


ATOM
4046
CG2
ILE
B
715
31.317
35.943
6.939
1.00
21.50


ATOM
4047
CG1
ILE
B
715
32.141
35.638
4.612
1.00
22.82


ATOM
4048
CD1
ILE
B
715
33.571
36.088
4.812
1.00
22.76


ATOM
4049
C
ILE
B
715
28.732
36.838
5.955
1.00
18.65


ATOM
4050
O
ILE
B
715
28.190
36.245
6.882
1.00
17.75


ATOM
4051
N
ILE
B
716
28.528
38.127
5.693
1.00
18.42


ATOM
4052
CA
ILE
B
716
27.624
38.951
6.500
1.00
17.16


ATOM
4053
CB
ILE
B
716
27.676
40.424
6.040
1.00
19.95


ATOM
4054
CG2
ILE
B
716
26.549
41.225
6.683
1.00
19.27


ATOM
4055
CG1
ILE
B
716
29.037
41.024
6.404
1.00
18.80


ATOM
4056
CD1
ILE
B
716
29.258
42.434
5.887
1.00
18.71


ATOM
4057
C
ILE
B
716
26.192
38.426
6.411
1.00
19.67


ATOM
4058
O
ILE
B
716
25.544
38.183
7.436
1.00
16.84


ATOM
4059
N
LYS
B
717
25.706
38.224
5.192
1.00
17.44


ATOM
4060
CA
LYS
B
717
24.344
37.721
5.040
1.00
19.23


ATOM
4061
CB
LYS
B
717
23.980
37.489
3.573
1.00
19.08


ATOM
4062
CG
LYS
B
717
22.575
36.915
3.425
1.00
19.36


ATOM
4063
CD
LYS
B
717
22.145
36.779
1.975
1.00
20.95


ATOM
4064
CE
LYS
B
717
20.713
36.253
1.906
1.00
20.68


ATOM
4065
NZ
LYS
B
717
20.177
36.245
0.520
1.00
22.57


ATOM
4066
C
LYS
B
717
24.167
36.408
5.797
1.00
18.60


ATOM
4067
O
LYS
B
717
23.204
36.240
6.539
1.00
19.65


ATOM
4068
N
GLN
B
718
25.091
35.469
5.602
1.00
18.67


ATOM
4069
CA
GLN
B
718
24.992
34.181
6.280
1.00
18.42


ATOM
4070
CB
GLN
B
718
26.110
33.256
5.794
1.00
35.34


ATOM
4071
CG
GLN
B
718
25.885
32.724
4.386
1.00
36.06


ATOM
4072
CD
GLN
B
718
27.121
32.072
3.798
1.00
36.81


ATOM
4073
OE1
GLN
B
718
27.036
31.295
2.843
1.00
37.02


ATOM
4074
NE2
GLN
B
718
28.282
32.397
4.356
1.00
36.65


ATOM
4075
C
GLN
B
718
25.039
34.298
7.802
1.00
16.64


ATOM
4076
O
GLN
B
718
24.337
33.577
8.517
1.00
17.20


ATOM
4077
N
ALA
B
719
25.855
35.221
8.299
1.00
17.42


ATOM
4078
CA
ALA
B
719
25.989
35.400
9.737
1.00
16.91


ATOM
4079
CB
ALA
B
719
27.181
36.314
10.037
1.00
18.95


ATOM
4080
C
ALA
B
719
24.705
35.979
10.338
1.00
16.46


ATOM
4081
O
ALA
B
719
24.280
35.566
11.415
1.00
16.41


ATOM
4082
N
ILE
B
720
24.087
36.923
9.632
1.00
16.16


ATOM
4083
CA
ILE
B
720
22.848
37.517
10.128
1.00
18.05


ATOM
4084
CB
ILE
B
720
22.463
38.775
9.317
1.00
16.77


ATOM
4085
CG2
ILE
B
720
21.021
39.200
9.634
1.00
17.00


ATOM
4086
CG1
ILE
B
720
23.458
39.903
9.626
1.00
17.24


ATOM
4087
CD1
ILE
B
720
23.165
41.216
8.938
1.00
18.75


ATOM
4088
C
ILE
B
720
21.725
36.484
10.083
1.00
16.85


ATOM
4089
O
ILE
B
720
20.966
36.339
11.044
1.00
17.13


ATOM
4090
N
LEU
B
721
21.628
35.741
8.983
1.00
17.26


ATOM
4091
CA
LEU
B
721
20.588
34.726
8.886
1.00
17.99


ATOM
4092
CB
LEU
B
721
20.611
34.056
7.507
1.00
21.38


ATOM
4093
CG
LEU
B
721
19.998
34.910
6.390
1.00
22.95


ATOM
4094
CD1
LEU
B
721
20.102
34.181
5.071
1.00
22.96


ATOM
4095
CD2
LEU
B
721
18.544
35.204
6.707
1.00
22.88


ATOM
4096
C
LEU
B
721
20.764
33.686
9.984
1.00
17.50


ATOM
4097
O
LEU
B
721
19.791
33.142
10.493
1.00
18.24


ATOM
4098
N
ALA
B
722
22.013
33.425
10.359
1.00
18.93


ATOM
4099
CA
ALA
B
722
22.305
32.448
11.398
1.00
19.70


ATOM
4100
CB
ALA
B
722
23.818
32.282
11.556
1.00
22.76


ATOM
4101
C
ALA
B
722
21.689
32.803
12.748
1.00
19.06


ATOM
4102
O
ALA
B
722
21.491
31.926
13.581
1.00
19.32


ATOM
4103
N
THR
B
723
21.389
34.081
12.972
1.00
19.12


ATOM
4104
CA
THR
B
723
20.820
34.484
14.255
1.00
18.93


ATOM
4105
CB
THR
B
723
20.997
36.000
14.503
1.00
16.46


ATOM
4106
OG1
THR
B
723
20.359
36.746
13.463
1.00
18.08


ATOM
4107
CG2
THR
B
723
22.485
36.355
14.536
1.00
17.70


ATOM
4108
C
THR
B
723
19.352
34.093
14.440
1.00
20.30


ATOM
4109
O
THR
B
723
18.744
34.373
15.474
1.00
18.88


ATOM
4110
N
ASP
B
724
18.785
33.464
13.421
1.00
20.75


ATOM
4111
CA
ASP
B
724
17.417
32.977
13.495
1.00
21.45


ATOM
4112
CB
ASP
B
724
16.901
32.670
12.084
1.00
20.47


ATOM
4113
CG
ASP
B
724
15.541
31.991
12.091
1.00
19.47


ATOM
4114
OD1
ASP
B
724
14.982
31.769
13.183
1.00
20.37


ATOM
4115
OD2
ASP
B
724
15.029
31.683
10.995
1.00
20.97


ATOM
4116
C
ASP
B
724
17.571
31.684
14.296
1.00
22.80


ATOM
4117
O
ASP
B
724
18.171
30.729
13.803
1.00
21.11


ATOM
4118
N
LEU
B
725
17.057
31.648
15.524
1.00
21.88


ATOM
4119
CA
LEU
B
725
17.211
30.454
16.354
1.00
23.26


ATOM
4120
CB
LEU
B
725
16.575
30.659
17.734
1.00
21.15


ATOM
4121
CG
LEU
B
725
17.439
31.482
18.698
1.00
22.29


ATOM
4122
CD1
LEU
B
725
16.712
31.674
20.019
1.00
22.69


ATOM
4123
CD2
LEU
B
725
18.768
30.765
18.927
1.00
22.08


ATOM
4124
C
LEU
B
725
16.685
29.178
15.720
1.00
24.43


ATOM
4125
O
LEU
B
725
17.084
28.074
16.110
1.00
24.43


ATOM
4126
N
ALA
B
726
15.802
29.322
14.735
1.00
24.46


ATOM
4127
CA
ALA
B
726
15.256
28.158
14.042
1.00
24.85


ATOM
4128
CB
ALA
B
726
14.096
28.576
13.144
1.00
26.10


ATOM
4129
C
ALA
B
726
16.361
27.502
13.219
1.00
25.58


ATOM
4130
O
ALA
B
726
16.436
26.277
13.127
1.00
24.81


ATOM
4131
N
LEU
B
727
17.217
28.323
12.617
1.00
25.66


ATOM
4132
CA
LEU
B
727
18.332
27.826
11.825
1.00
26.45


ATOM
4133
CB
LEU
B
727
18.952
28.969
11.016
1.00
32.52


ATOM
4134
CG
LEU
B
727
18.730
28.953
9.499
1.00
34.10


ATOM
4135
CD1
LEU
B
727
17.320
28.490
9.163
1.00
32.76


ATOM
4136
CD2
LEU
B
727
18.999
30.343
8.938
1.00
32.91


ATOM
4137
C
LEU
B
727
19.370
27.216
12.767
1.00
26.66


ATOM
4138
O
LEU
B
727
19.994
26.208
12.448
1.00
27.25


ATOM
4139
N
TYR
B
728
19.549
27.828
13.933
1.00
23.88


ATOM
4140
CA
TYR
B
728
20.497
27.311
14.912
1.00
24.96


ATOM
4141
CB
TYR
B
728
20.576
28.246
16.127
1.00
22.32


ATOM
4142
CG
TYR
B
728
21.197
27.606
17.348
1.00
22.57


ATOM
4143
CD1
TYR
B
728
20.402
27.173
18.410
1.00
23.27


ATOM
4144
CE1
TYR
B
728
20.958
26.520
19.512
1.00
22.36


ATOM
4145
CD2
TYR
B
728
22.569
27.372
17.416
1.00
23.33


ATOM
4146
CE2
TYR
B
728
23.133
26.713
18.512
1.00
22.71


ATOM
4147
CZ
TYR
B
728
22.322
26.292
19.553
1.00
23.34


ATOM
4148
OH
TYR
B
728
22.876
25.642
20.638
1.00
25.15


ATOM
4149
C
TYR
B
728
20.085
25.908
15.365
1.00
25.55


ATOM
4150
O
TYR
B
728
20.894
24.982
15.368
1.00
25.79


ATOM
4151
N
ILE
B
729
18.821
25.759
15.747
1.00
27.10


ATOM
4152
CA
ILE
B
729
18.313
24.476
16.218
1.00
27.90


ATOM
4153
CB
ILE
B
729
16.849
24.608
16.692
1.00
33.37


ATOM
4154
CG2
ILE
B
729
16.245
23.231
16.936
1.00
34.11


ATOM
4155
CG1
ILE
B
729
16.800
25.447
17.969
1.00
33.59


ATOM
4156
CD1
ILE
B
729
15.400
25.662
18.512
1.00
34.44


ATOM
4157
C
ILE
B
729
18.396
23.395
15.151
1.00
28.43


ATOM
4158
O
ILE
B
729
18.561
22.212
15.463
1.00
28.49


ATOM
4159
N
LYS
B
730
18.286
23.803
13.893
1.00
30.10


ATOM
4160
CA
LYS
B
730
18.335
22.865
12.777
1.00
30.87


ATOM
4161
CB
LYS
B
730
17.637
23.474
11.554
1.00
41.47


ATOM
4162
CG
LYS
B
730
17.736
22.627
10.292
1.00
41.83


ATOM
4163
CD
LYS
B
730
17.082
23.312
9.099
1.00
41.85


ATOM
4164
CE
LYS
B
730
17.161
22.437
7.856
1.00
42.29


ATOM
4165
NZ
LYS
B
730
16.471
23.056
6.689
1.00
41.92


ATOM
4166
C
LYS
B
730
19.753
22.450
12.390
1.00
30.30


ATOM
4167
O
LYS
B
730
19.968
21.341
11.899
1.00
30.78


ATOM
4168
N
ARG
B
731
20.722
23.330
12.611
1.00
26.44


ATOM
4169
CA
ARG
B
731
22.101
23.029
12.234
1.00
26.05


ATOM
4170
CB
ARG
B
731
22.691
24.207
11.455
1.00
44.87


ATOM
4171
CG
ARG
B
731
22.027
24.477
10.123
1.00
45.35


ATOM
4172
CD
ARG
B
731
22.579
25.739
9.481
1.00
45.70


ATOM
4173
NE
ARG
B
731
24.018
25.666
9.236
1.00
45.72


ATOM
4174
CZ
ARG
B
731
24.600
24.771
8.445
1.00
45.64


ATOM
4175
NH1
ARG
B
731
23.870
23.859
7.816
1.00
45.97


ATOM
4176
NH2
ARG
B
731
25.915
24.793
8.272
1.00
45.83


ATOM
4177
C
ARG
B
731
23.076
22.657
13.349
1.00
25.87


ATOM
4178
O
ARG
B
731
24.144
22.121
13.069
1.00
25.60


ATOM
4179
N
ARG
B
732
22.724
22.931
14.600
1.00
24.75


ATOM
4180
CA
ARG
B
732
23.636
22.646
15.704
1.00
24.59


ATOM
4181
CB
ARG
B
732
23.051
23.154
17.021
1.00
28.71


ATOM
4182
CG
ARG
B
732
21.825
22.412
17.490
1.00
28.36


ATOM
4183
CD
ARG
B
732
21.266
23.052
18.742
1.00
28.99


ATOM
4184
NE
ARG
B
732
20.160
22.282
19.295
1.00
28.09


ATOM
4185
CZ
ARG
B
732
19.555
22.567
20.444
1.00
29.06


ATOM
4186
NH1
ARG
B
732
19.951
23.607
21.164
1.00
29.87


ATOM
4187
NH2
ARG
B
732
18.560
21.807
20.878
1.00
29.81


ATOM
4188
C
ARG
B
732
24.027
21.177
15.845
1.00
24.59


ATOM
4189
O
ARG
B
732
25.143
20.871
16.272
1.00
24.56


ATOM
4190
N
GLY
B
733
23.114
20.278
15.495
1.00
28.28


ATOM
4191
CA
GLY
B
733
23.409
18.857
15.592
1.00
29.55


ATOM
4192
C
GLY
B
733
24.686
18.506
14.852
1.00
29.73


ATOM
4193
O
GLY
B
733
25.582
17.856
15.402
1.00
29.54


ATOM
4194
N
GLU
B
734
24.775
18.940
13.599
1.00
29.63


ATOM
4195
CA
GLU
B
734
25.954
18.676
12.779
1.00
29.74


ATOM
4196
CB
GLU
B
734
25.772
19.317
11.396
1.00
37.09


ATOM
4197
CG
GLU
B
734
27.011
19.313
10.513
1.00
37.69


ATOM
4198
CD
GLU
B
734
26.712
19.749
9.090
1.00
37.69


ATOM
4199
OE1
GLU
B
734
25.895
20.673
8.905
1.00
37.77


ATOM
4200
OE2
GLU
B
734
27.302
19.174
8.153
1.00
37.96


ATOM
4201
C
GLU
B
734
27.234
19.187
13.448
1.00
29.89


ATOM
4202
O
GLU
B
734
28.241
18.481
13.508
1.00
29.99


ATOM
4203
N
PHE
B
735
27.193
20.416
13.953
1.00
26.19


ATOM
4204
CA
PHE
B
735
28.348
21.015
14.617
1.00
28.01


ATOM
4205
CB
PHE
B
735
28.001
22.449
15.051
1.00
32.46


ATOM
4206
CG
PHE
B
735
29.121
23.170
15.748
1.00
32.58


ATOM
4207
CD1
PHE
B
735
30.350
23.353
15.121
1.00
32.98


ATOM
4208
CD2
PHE
B
735
28.930
23.710
17.018
1.00
32.86


ATOM
4209
CE1
PHE
B
735
31.374
24.067
15.746
1.00
33.43


ATOM
4210
CE2
PHE
B
735
29.941
24.424
17.653
1.00
33.17


ATOM
4211
CZ
PHE
B
735
31.168
24.606
17.017
1.00
33.32


ATOM
4212
C
PHE
B
735
28.759
20.185
15.832
1.00
28.38


ATOM
4213
O
PHE
B
735
29.943
19.877
16.023
1.00
28.13


ATOM
4214
N
PHE
B
736
27.772
19.823
16.646
1.00
35.56


ATOM
4215
CA
PHE
B
736
28.008
19.033
17.848
1.00
36.50


ATOM
4216
CB
PHE
B
736
26.695
18.843
18.615
1.00
29.57


ATOM
4217
CG
PHE
B
736
26.153
20.118
19.217
1.00
28.48


ATOM
4218
CD1
PHE
B
736
24.849
20.174
19.707
1.00
29.25


ATOM
4219
CD2
PHE
B
736
26.947
21.261
19.298
1.00
28.68


ATOM
4220
CE1
PHE
B
736
24.343
21.351
20.270
1.00
28.48


ATOM
4221
CE2
PHE
B
736
26.451
22.440
19.857
1.00
28.64


ATOM
4222
CZ
PHE
B
736
25.142
22.481
20.344
1.00
28.27


ATOM
4223
C
PHE
B
736
28.636
17.678
17.538
1.00
36.98


ATOM
4224
O
PHE
B
736
29.472
17.192
18.299
1.00
37.51


ATOM
4225
N
GLU
B
737
28.236
17.074
16.422
1.00
35.33


ATOM
4226
CA
GLU
B
737
28.779
15.778
16.019
1.00
34.66


ATOM
4227
CB
GLU
B
737
28.042
15.245
14.788
1.00
48.23


ATOM
4228
CG
GLU
B
737
26.624
14.782
15.052
1.00
48.59


ATOM
4229
CD
GLU
B
737
26.562
13.677
16.084
1.00
48.98


ATOM
4230
OE1
GLU
B
737
27.347
12.710
15.969
1.00
48.80


ATOM
4231
OE2
GLU
B
737
25.724
13.771
17.004
1.00
49.04


ATOM
4232
C
GLU
B
737
30.264
15.895
15.698
1.00
35.25


ATOM
4233
O
GLU
B
737
31.095
15.184
16.276
1.00
34.50


ATOM
4234
N
LEU
B
738
30.582
16.792
14.766
1.00
34.53


ATOM
4235
CA
LEU
B
738
31.958
17.036
14.339
1.00
34.99


ATOM
4236
CB
LEU
B
738
32.010
18.266
13.422
1.00
33.43


ATOM
4237
CG
LEU
B
738
31.532
18.137
11.969
1.00
33.44


ATOM
4238
CD1
LEU
B
738
30.237
17.345
11.885
1.00
33.77


ATOM
4239
CD2
LEU
B
738
31.345
19.531
11.388
1.00
33.47


ATOM
4240
C
LEU
B
738
32.889
17.243
15.530
1.00
35.52


ATOM
4241
O
LEU
B
738
34.020
16.760
15.535
1.00
35.19


ATOM
4242
N
ILE
B
739
32.403
17.960
16.538
1.00
35.96


ATOM
4243
CA
ILE
B
739
33.177
18.243
17.740
1.00
36.59


ATOM
4244
CB
ILE
B
739
32.489
19.347
18.578
1.00
41.13


ATOM
4245
CG2
ILE
B
739
33.192
19.509
19.913
1.00
41.32


ATOM
4246
CG1
ILE
B
739
32.478
20.665
17.798
1.00
41.45


ATOM
4247
CD1
ILE
B
739
33.852
21.224
17.510
1.00
41.21


ATOM
4248
C
ILE
B
739
33.353
16.998
18.610
1.00
37.53


ATOM
4249
O
ILE
B
739
34.455
16.711
19.088
1.00
36.85


ATOM
4250
N
ARG
B
740
32.262
16.264
18.808
1.00
40.80


ATOM
4251
CA
ARG
B
740
32.276
15.058
19.627
1.00
41.57


ATOM
4252
CB
ARG
B
740
30.860
14.490
19.744
1.00
49.23


ATOM
4253
CG
ARG
B
740
30.708
13.372
20.763
1.00
49.50


ATOM
4254
CD
ARG
B
740
29.268
12.894
20.816
1.00
49.76


ATOM
4255
NE
ARG
B
740
28.870
12.228
19.577
1.00
49.63


ATOM
4256
CZ
ARG
B
740
29.192
10.977
19.264
1.00
49.97


ATOM
4257
NH1
ARG
B
740
29.917
10.246
20.103
1.00
49.93


ATOM
4258
NH2
ARG
B
740
28.795
10.456
18.111
1.00
49.81


ATOM
4259
C
ARG
B
740
33.202
13.999
19.045
1.00
41.31


ATOM
4260
O
ARG
B
740
34.041
13.437
19.750
1.00
41.75


ATOM
4261
N
LYS
B
741
33.048
13.734
17.753
1.00
36.01


ATOM
4262
CA
LYS
B
741
33.858
12.734
17.074
1.00
36.04


ATOM
4263
CB
LYS
B
741
33.142
12.261
15.806
1.00
51.86


ATOM
4264
CG
LYS
B
741
31.823
11.547
16.084
1.00
52.33


ATOM
4265
CD
LYS
B
741
31.198
10.984
14.819
1.00
52.60


ATOM
4266
CE
LYS
B
741
29.956
10.164
15.147
1.00
52.72


ATOM
4267
NZ
LYS
B
741
29.371
9.514
13.941
1.00
52.84


ATOM
4268
C
LYS
B
741
35.257
13.229
16.739
1.00
36.83


ATOM
4269
O
LYS
B
741
36.017
12.544
16.056
1.00
35.76


ATOM
4270
N
ASN
B
742
35.598
14.424
17.217
1.00
47.96


ATOM
4271
CA
ASN
B
742
36.925
14.991
16.979
1.00
48.89


ATOM
4272
CB
ASN
B
742
37.984
14.073
17.601
1.00
45.18


ATOM
4273
CG
ASN
B
742
37.660
13.696
19.038
1.00
45.25


ATOM
4274
OD1
ASN
B
742
37.873
14.481
19.958
1.00
45.19


ATOM
4275
ND2
ASN
B
742
37.127
12.492
19.231
1.00
45.61


ATOM
4276
C
ASN
B
742
37.210
15.160
15.482
1.00
48.30


ATOM
4277
O
ASN
B
742
38.318
14.886
15.023
1.00
49.56


ATOM
4278
N
GLN
B
743
36.214
15.627
14.733
1.00
35.63


ATOM
4279
CA
GLN
B
743
36.345
15.806
13.288
1.00
33.02


ATOM
4280
CB
GLN
B
743
35.226
15.034
12.583
1.00
55.29


ATOM
4281
CG
GLN
B
743
34.914
13.679
13.206
1.00
55.90


ATOM
4282
CD
GLN
B
743
33.531
13.159
12.830
1.00
56.30


ATOM
4283
OE1
GLN
B
743
32.531
13.872
12.943
1.00
56.03


ATOM
4284
NE2
GLN
B
743
33.470
11.903
12.396
1.00
56.30


ATOM
4285
C
GLN
B
743
36.296
17.272
12.833
1.00
32.63


ATOM
4286
O
GLN
B
743
36.519
17.568
11.659
1.00
30.98


ATOM
4287
N
PHE
B
744
36.008
18.186
13.754
1.00
30.07


ATOM
4288
CA
PHE
B
744
35.913
19.600
13.396
1.00
29.86


ATOM
4289
CB
PHE
B
744
35.664
20.451
14.646
1.00
36.04


ATOM
4290
CG
PHE
B
744
35.433
21.906
14.349
1.00
36.02


ATOM
4291
CD1
PHE
B
744
34.426
22.294
13.472
1.00
36.51


ATOM
4292
CD2
PHE
B
744
36.224
22.886
14.939
1.00
36.37


ATOM
4293
CE1
PHE
B
744
34.210
23.641
13.186
1.00
36.33


ATOM
4294
CE2
PHE
B
744
36.017
24.237
14.660
1.00
36.35


ATOM
4295
CZ
PHE
B
744
35.007
24.613
13.781
1.00
36.44


ATOM
4296
C
PHE
B
744
37.158
20.101
12.671
1.00
30.17


ATOM
4297
O
PHE
B
744
38.274
19.948
13.163
1.00
29.71


ATOM
4298
N
ASN
B
745
36.953
20.703
11.500
1.00
33.40


ATOM
4299
CA
ASN
B
745
38.047
21.229
10.685
1.00
34.97


ATOM
4300
CB
ASN
B
745
38.463
20.192
9.634
1.00
36.63


ATOM
4301
CG
ASN
B
745
39.397
20.765
8.586
1.00
36.73


ATOM
4302
OD1
ASN
B
745
40.281
21.562
8.896
1.00
37.02


ATOM
4303
ND2
ASN
B
745
39.216
20.345
7.337
1.00
37.05


ATOM
4304
C
ASN
B
745
37.674
22.537
9.992
1.00
34.71


ATOM
4305
O
ASN
B
745
36.930
22.540
9.011
1.00
34.81


ATOM
4306
N
LEU
B
746
38.209
23.645
10.495
1.00
32.32


ATOM
4307
CA
LEU
B
746
37.914
24.961
9.934
1.00
31.51


ATOM
4308
CB
LEU
B
746
38.459
26.059
10.853
1.00
35.95


ATOM
4309
CG
LEU
B
746
37.591
26.325
12.083
1.00
36.41


ATOM
4310
CD1
LEU
B
746
38.239
27.390
12.951
1.00
36.26


ATOM
4311
CD2
LEU
B
746
36.200
26.773
11.635
1.00
36.10


ATOM
4312
C
LEU
B
746
38.419
25.181
8.511
1.00
31.36


ATOM
4313
O
LEU
B
746
38.085
26.183
7.877
1.00
31.04


ATOM
4314
N
GLU
B
747
39.224
24.252
8.010
1.00
30.95


ATOM
4315
CA
GLU
B
747
39.738
24.357
6.650
1.00
31.86


ATOM
4316
CB
GLU
B
747
40.918
23.402
6.453
1.00
51.07


ATOM
4317
CG
GLU
B
747
42.129
23.738
7.311
1.00
51.73


ATOM
4318
CD
GLU
B
747
43.251
22.728
7.163
1.00
52.11


ATOM
4319
OE1
GLU
B
747
43.666
22.467
6.014
1.00
52.03


ATOM
4320
OE2
GLU
B
747
43.718
22.201
8.196
1.00
52.21


ATOM
4321
C
GLU
B
747
38.617
24.014
5.670
1.00
31.25


ATOM
4322
O
GLU
B
747
38.646
24.421
4.507
1.00
30.95


ATOM
4323
N
ASP
B
748
37.634
23.260
6.156
1.00
31.79


ATOM
4324
CA
ASP
B
748
36.480
22.864
5.357
1.00
31.93


ATOM
4325
CB
ASP
B
748
35.754
21.697
6.031
1.00
39.97


ATOM
4326
CG
ASP
B
748
34.571
21.193
5.223
1.00
40.51


ATOM
4327
OD1
ASP
B
748
33.678
21.995
4.889
1.00
40.27


ATOM
4328
OD2
ASP
B
748
34.533
19.981
4.928
1.00
40.36


ATOM
4329
C
ASP
B
748
35.546
24.071
5.265
1.00
32.12


ATOM
4330
O
ASP
B
748
35.026
24.538
6.280
1.00
31.68


ATOM
4331
N
PRO
B
749
35.317
24.586
4.046
1.00
30.33


ATOM
4332
CD
PRO
B
749
35.694
23.972
2.761
1.00
44.68


ATOM
4333
CA
PRO
B
749
34.445
25.746
3.827
1.00
30.40


ATOM
4334
CB
PRO
B
749
34.380
25.845
2.304
1.00
44.80


ATOM
4335
CG
PRO
B
749
34.577
24.423
1.863
1.00
45.23


ATOM
4336
C
PRO
B
749
33.065
25.626
4.470
1.00
30.78


ATOM
4337
O
PRO
B
749
32.553
26.591
5.045
1.00
29.64


ATOM
4338
N
HIS
B
750
32.464
24.443
4.379
1.00
31.42


ATOM
4339
CA
HIS
B
750
31.148
24.231
4.963
1.00
31.75


ATOM
4340
CB
HIS
B
750
30.569
22.890
4.513
1.00
36.05


ATOM
4341
CG
HIS
B
750
29.289
22.529
5.200
1.00
36.27


ATOM
4342
CD2
HIS
B
750
28.002
22.836
4.908
1.00
35.87


ATOM
4343
ND1
HIS
B
750
29.250
21.786
6.360
1.00
36.16


ATOM
4344
CE1
HIS
B
750
27.996
21.648
6.752
1.00
36.46


ATOM
4345
NE2
HIS
B
750
27.219
22.276
5.888
1.00
36.37


ATOM
4346
C
HIS
B
750
31.212
24.288
6.480
1.00
31.05


ATOM
4347
O
HIS
B
750
30.373
24.922
7.118
1.00
31.52


ATOM
4348
N
GLU
B
751
32.208
23.629
7.062
1.00
26.46


ATOM
4349
CA
GLU
B
751
32.356
23.642
8.512
1.00
26.08


ATOM
4350
CB
GLU
B
751
33.415
22.625
8.946
1.00
32.16


ATOM
4351
CG
GLU
B
751
33.004
21.185
8.700
1.00
32.81


ATOM
4352
CD
GLU
B
751
34.040
20.193
9.190
1.00
32.54


ATOM
4353
OE1
GLU
B
751
34.381
20.234
10.392
1.00
32.25


ATOM
4354
OE2
GLU
B
751
34.507
19.373
8.372
1.00
33.04


ATOM
4355
C
GLU
B
751
32.741
25.038
8.997
1.00
25.23


ATOM
4356
O
GLU
B
751
32.426
25.424
10.127
1.00
26.00


ATOM
4357
N
LYS
B
752
33.413
25.791
8.134
1.00
25.46


ATOM
4358
CA
LYS
B
752
33.835
27.144
8.477
1.00
25.14


ATOM
4359
CB
LYS
B
752
34.760
27.710
7.400
1.00
34.00


ATOM
4360
CG
LYS
B
752
35.473
28.988
7.807
1.00
34.35


ATOM
4361
CD
LYS
B
752
36.445
28.715
8.950
1.00
34.98


ATOM
4362
CE
LYS
B
752
37.386
29.878
9.166
1.00
34.20


ATOM
4363
NZ
LYS
B
752
38.098
30.208
7.910
1.00
34.22


ATOM
4364
C
LYS
B
752
32.600
28.024
8.593
1.00
25.44


ATOM
4365
O
LYS
B
752
32.435
28.747
9.574
1.00
25.14


ATOM
4366
N
GLU
B
753
31.724
27.956
7.597
1.00
26.17


ATOM
4367
CA
GLU
B
753
30.519
28.775
7.639
1.00
27.32


ATOM
4368
CB
GLU
B
753
29.773
28.743
6.300
1.00
47.16


ATOM
4369
CG
GLU
B
753
29.010
27.468
6.008
1.00
48.02


ATOM
4370
CD
GLU
B
753
28.190
27.578
4.738
1.00
48.29


ATOM
4371
OE1
GLU
B
753
28.791
27.692
3.647
1.00
48.21


ATOM
4372
OE2
GLU
B
753
26.944
27.561
4.832
1.00
48.25


ATOM
4373
C
GLU
B
753
29.620
28.287
8.764
1.00
26.46


ATOM
4374
O
GLU
B
753
28.913
29.080
9.383
1.00
26.43


ATOM
4375
N
LEU
B
754
29.658
26.983
9.035
1.00
24.18


ATOM
4376
CA
LEU
B
754
28.860
26.406
10.110
1.00
22.29


ATOM
4377
CB
LEU
B
754
28.981
24.877
10.116
1.00
25.44


ATOM
4378
CG
LEU
B
754
28.264
24.173
11.273
1.00
25.42


ATOM
4379
CD1
LEU
B
754
26.772
24.485
11.234
1.00
26.03


ATOM
4380
CD2
LEU
B
754
28.494
22.674
11.174
1.00
26.23


ATOM
4381
C
LEU
B
754
29.338
26.957
11.451
1.00
22.78


ATOM
4382
O
LEU
B
754
28.524
27.323
12.308
1.00
23.06


ATOM
4383
N
PHE
B
755
30.657
27.015
11.636
1.00
20.22


ATOM
4384
CA
PHE
B
755
31.216
27.528
12.872
1.00
20.52


ATOM
4385
CB
PHE
B
755
32.745
27.445
12.870
1.00
21.28


ATOM
4386
CG
PHE
B
755
33.380
28.142
14.042
1.00
20.97


ATOM
4387
CD1
PHE
B
755
33.212
27.654
15.332
1.00
21.53


ATOM
4388
CD2
PHE
B
755
34.111
29.309
13.858
1.00
22.19


ATOM
4389
CE1
PHE
B
755
33.763
28.323
16.426
1.00
21.26


ATOM
4390
CE2
PHE
B
755
34.667
29.989
14.949
1.00
21.93


ATOM
4391
CZ
PHE
B
755
34.492
29.496
16.230
1.00
21.53


ATOM
4392
C
PHE
B
755
30.811
28.982
13.064
1.00
19.98


ATOM
4393
O
PHE
B
755
30.378
29.372
14.147
1.00
22.32


ATOM
4394
N
LEU
B
756
30.968
29.778
12.010
1.00
19.82


ATOM
4395
CA
LEU
B
756
30.621
31.193
12.070
1.00
19.75


ATOM
4396
CB
LEU
B
756
30.868
31.858
10.716
1.00
18.84


ATOM
4397
CG
LEU
B
756
32.329
31.854
10.252
1.00
18.79


ATOM
4398
CD1
LEU
B
756
32.433
32.482
8.864
1.00
19.24


ATOM
4399
CD2
LEU
B
756
33.192
32.610
11.262
1.00
19.62


ATOM
4400
C
LEU
B
756
29.165
31.372
12.488
1.00
21.11


ATOM
4401
O
LEU
B
756
28.839
32.294
13.233
1.00
19.94


ATOM
4402
N
ALA
B
757
28.291
30.488
12.014
1.00
20.80


ATOM
4403
CA
ALA
B
757
26.873
30.568
12.373
1.00
21.25


ATOM
4404
CB
ALA
B
757
26.064
29.560
11.552
1.00
23.40


ATOM
4405
C
ALA
B
757
26.693
30.294
13.861
1.00
22.25


ATOM
4406
O
ALA
B
757
25.917
30.971
14.542
1.00
22.17


ATOM
4407
N
MET
B
758
27.412
29.291
14.364
1.00
19.96


ATOM
4408
CA
MET
B
758
27.348
28.926
15.771
1.00
20.73


ATOM
4409
CB
MET
B
758
28.154
27.647
16.023
1.00
27.97


ATOM
4410
CG
MET
B
758
27.601
26.422
15.324
1.00
27.07


ATOM
4411
SD
MET
B
758
25.940
25.980
15.881
1.00
27.12


ATOM
4412
CE
MET
B
758
24.971
26.627
14.530
1.00
27.43


ATOM
4413
C
MET
B
758
27.895
30.043
16.656
1.00
18.82


ATOM
4414
O
MET
B
758
27.352
30.315
17.725
1.00
21.47


ATOM
4415
N
LEU
B
759
28.976
30.674
16.208
1.00
19.71


ATOM
4416
CA
LEU
B
759
29.597
31.756
16.954
1.00
18.16


ATOM
4417
CB
LEU
B
759
30.892
32.189
16.270
1.00
20.33


ATOM
4418
CG
LEU
B
759
31.646
33.349
16.919
1.00
19.85


ATOM
4419
CD1
LEU
B
759
31.992
33.005
18.363
1.00
21.09


ATOM
4420
CD2
LEU
B
759
32.891
33.646
16.103
1.00
19.80


ATOM
4421
C
LEU
B
759
28.635
32.933
17.048
1.00
20.05


ATOM
4422
O
LEU
B
759
28.535
33.577
18.091
1.00
19.37


ATOM
4423
N
MET
B
760
27.921
33.202
15.960
1.00
18.13


ATOM
4424
CA
MET
B
760
26.955
34.302
15.959
1.00
19.70


ATOM
4425
CB
MET
B
760
26.325
34.455
14.575
1.00
17.26


ATOM
4426
CG
MET
B
760
27.211
35.177
13.547
1.00
16.88


ATOM
4427
SD
MET
B
760
27.567
36.936
13.895
1.00
17.69


ATOM
4428
CE
MET
B
760
25.887
37.644
13.962
1.00
17.02


ATOM
4429
C
MET
B
760
25.879
34.059
17.017
1.00
18.46


ATOM
4430
O
MET
B
760
25.510
34.970
17.765
1.00
18.74


ATOM
4431
N
THR
B
761
25.380
32.831
17.102
1.00
17.88


ATOM
4432
CA
THR
B
761
24.358
32.516
18.092
1.00
17.90


ATOM
4433
CB
THR
B
761
23.858
31.070
17.933
1.00
20.06


ATOM
4434
OG1
THR
B
761
23.316
30.905
16.619
1.00
20.01


ATOM
4435
OG2
THR
B
761
22.778
30.746
18.971
1.00
19.13


ATOM
4436
C
THR
B
761
24.922
32.694
19.495
1.00
18.35


ATOM
4437
O
THR
B
761
24.265
33.241
20.375
1.00
17.84


ATOM
4438
N
ALA
B
762
26.160
32.244
19.695
1.00
18.42


ATOM
4439
CA
ALA
B
762
26.808
32.347
20.996
1.00
17.98


ATOM
4440
CB
ALA
B
762
28.224
31.780
20.930
1.00
19.48


ATOM
4441
C
ALA
B
762
26.843
33.795
21.472
1.00
17.59


ATOM
4442
O
ALA
B
762
26.567
34.077
22.637
1.00
20.01


ATOM
4443
N
CYS
B
763
27.186
34.705
20.570
1.00
17.78


ATOM
4444
CA
CYS
B
763
27.247
36.115
20.914
1.00
18.49


ATOM
4445
CB
CYS
B
763
28.041
36.869
19.850
1.00
20.27


ATOM
4446
SG
CYS
B
763
29.790
36.353
19.790
1.00
21.15


ATOM
4447
C
CYS
B
763
25.841
36.704
21.071
1.00
19.17


ATOM
4448
O
CYS
B
763
25.596
37.521
21.957
1.00
19.53


ATOM
4449
N
ASP
B
764
24.921
36.265
20.219
1.00
20.39


ATOM
4450
CA
ASP
B
764
23.534
36.729
20.254
1.00
20.66


ATOM
4451
CB
ASP
B
764
22.739
36.046
19.130
1.00
19.31


ATOM
4452
CG
ASP
B
764
21.474
36.802
18.767
1.00
19.31


ATOM
4453
OD1
ASP
B
764
20.707
36.320
17.903
1.00
19.87


ATOM
4454
OD2
ASP
B
764
21.265
37.889
19.341
1.00
17.76


ATOM
4455
C
ASP
B
764
22.862
36.429
21.598
1.00
20.80


ATOM
4456
O
ASP
B
764
22.021
37.191
22.074
1.00
20.53


ATOM
4457
N
LEU
B
765
23.235
35.319
22.220
1.00
17.19


ATOM
4458
CA
LEU
B
765
22.626
34.934
23.489
1.00
17.73


ATOM
4459
CB
LEU
B
765
22.337
33.428
23.476
1.00
20.86


ATOM
4460
CG
LEU
B
765
21.556
32.898
22.270
1.00
21.66


ATOM
4461
CD1
LEU
B
765
21.264
31.422
22.444
1.00
21.03


ATOM
4462
CD2
LEU
B
765
20.257
33.679
22.125
1.00
20.47


ATOM
4463
C
LEU
B
765
23.497
35.276
24.697
1.00
18.18


ATOM
4464
O
LEU
B
765
23.205
34.833
25.813
1.00
19.59


ATOM
4465
N
SER
B
766
24.516
36.111
24.475
1.00
19.68


ATOM
4466
CA
SER
B
766
25.498
36.475
25.504
1.00
20.44


ATOM
4467
CB
SER
B
766
26.478
37.527
24.959
1.00
23.53


ATOM
4468
OG
SER
B
766
25.937
38.837
24.998
1.00
25.78


ATOM
4469
C
SER
B
766
24.997
36.932
26.872
1.00
20.03


ATOM
4470
O
SER
B
766
25.695
36.770
27.871
1.00
19.65


ATOM
4471
N
ALA
B
767
23.806
37.513
26.929
1.00
22.57


ATOM
4472
CA
ALA
B
767
23.284
37.974
28.210
1.00
23.91


ATOM
4473
CB
ALA
B
767
21.943
38.682
28.002
1.00
17.04


ATOM
4474
C
ALA
B
767
23.123
36.832
29.213
1.00
23.55


ATOM
4475
O
ALA
B
767
23.202
37.045
30.426
1.00
24.64


ATOM
4476
N
ILE
B
768
22.911
35.621
28.703
1.00
23.20


ATOM
4477
CA
ILE
B
768
22.718
34.448
29.546
1.00
22.31


ATOM
4478
CB
ILE
B
768
22.143
33.257
28.717
1.00
23.65


ATOM
4479
CG2
ILE
B
768
23.253
32.563
27.933
1.00
22.89


ATOM
4480
CG1
ILE
B
768
21.457
32.255
29.641
1.00
23.26


ATOM
4481
CD1
ILE
B
768
20.179
32.796
30.272
1.00
23.73


ATOM
4482
C
ILE
B
768
24.004
33.999
30.247
1.00
22.60


ATOM
4483
O
ILE
B
768
23.958
33.164
31.140
1.00
22.93


ATOM
4484
N
THR
B
769
25.138
34.571
29.849
1.00
21.92


ATOM
4485
CA
THR
B
769
26.438
34.224
30.435
1.00
21.95


ATOM
4486
CB
THR
B
769
27.525
34.077
29.356
1.00
23.33


ATOM
4487
OG1
THR
B
769
27.793
35.362
28.778
1.00
24.40


ATOM
4488
CG2
THR
B
769
27.087
33.111
28.267
1.00
24.02


ATOM
4489
C
THR
B
769
26.962
35.287
31.399
1.00
22.67


ATOM
4490
O
THR
B
769
27.973
35.086
32.073
1.00
22.65


ATOM
4491
N
LYS
B
770
26.284
36.425
31.452
1.00
23.25


ATOM
4492
CA
LYS
B
770
26.720
37.530
32.296
1.00
23.60


ATOM
4493
CB
LYS
B
770
25.996
38.802
31.849
1.00
21.12


ATOM
4494
CG
LYS
B
770
26.258
39.179
30.403
1.00
20.96


ATOM
4495
CD
LYS
B
770
27.656
39.759
30.206
1.00
20.82


ATOM
4496
CE
LYS
B
770
27.893
40.115
28.739
1.00
20.75


ATOM
4497
NZ
LYS
B
770
29.176
40.840
28.511
1.00
21.62


ATOM
4498
C
LYS
B
770
26.525
37.339
33.802
1.00
24.02


ATOM
4499
O
LYS
B
770
25.758
36.476
34.239
1.00
23.96


ATOM
4500
N
PRO
B
771
27.238
38.140
34.618
1.00
24.80


ATOM
4501
CD
PRO
B
771
28.330
39.060
34.249
1.00
25.87


ATOM
4502
CA
PRO
B
771
27.109
38.045
36.076
1.00
25.95


ATOM
4503
CB
PRO
B
771
27.976
39.198
36.569
1.00
25.81


ATOM
4504
CG
PRO
B
771
29.083
39.215
35.563
1.00
26.51


ATOM
4505
C
PRO
B
771
25.631
38.220
36.440
1.00
26.70


ATOM
4506
O
PRO
B
771
24.905
38.955
35.763
1.00
25.64


ATOM
4507
N
TRP
B
772
25.202
37.546
37.503
1.00
27.13


ATOM
4508
CA
TRP
B
772
23.811
37.553
37.959
1.00
27.52


ATOM
4509
CB
TRP
B
772
23.744
37.021
39.394
1.00
31.16


ATOM
4510
CG
TRP
B
772
22.355
36.817
39.921
1.00
31.91


ATOM
4511
CD2
TRP
B
772
21.272
36.141
39.267
1.00
31.55


ATOM
4512
CE2
TRP
B
772
20.171
36.166
40.150
1.00
31.84


ATOM
4513
CE3
TRP
B
772
21.126
35.516
38.021
1.00
31.35


ATOM
4514
CD1
TRP
B
772
21.878
37.212
41.138
1.00
31.40


ATOM
4515
NE1
TRP
B
772
20.569
36.827
41.283
1.00
32.07


ATOM
4516
CZ2
TRP
B
772
18.937
35.591
39.828
1.00
32.13


ATOM
4517
CZ3
TRP
B
772
19.897
34.944
37.701
1.00
31.80


ATOM
4518
CH2
TRP
B
772
18.819
34.987
38.602
1.00
31.93


ATOM
4519
C
TRP
B
772
23.009
38.853
37.865
1.00
27.06


ATOM
4520
O
TRP
B
772
21.913
38.864
37.305
1.00
27.10


ATOM
4521
N
PRO
B
773
23.533
39.964
38.409
1.00
27.24


ATOM
4522
CD
PRO
B
773
24.841
40.176
39.050
1.00
36.67


ATOM
4523
CA
PRO
B
773
22.778
41.220
38.336
1.00
26.63


ATOM
4524
CB
PRO
B
773
23.649
42.192
39.133
1.00
36.87


ATOM
4525
CG
PRO
B
773
25.027
41.669
38.902
1.00
37.42


ATOM
4526
C
PRO
B
773
22.520
41.692
36.914
1.00
25.67


ATOM
4527
O
PRO
B
773
21.476
42.272
36.626
1.00
26.52


ATOM
4528
N
ILE
B
774
23.480
41.443
36.029
1.00
21.82


ATOM
4529
CA
ILE
B
774
23.341
41.834
34.636
1.00
21.26


ATOM
4530
CB
ILE
B
774
24.707
41.788
33.915
1.00
30.27


ATOM
4531
CG2
ILE
B
774
24.523
42.062
32.429
1.00
30.62


ATOM
4532
CG1
ILE
B
774
25.649
42.821
34.543
1.00
31.27


ATOM
4533
CD1
ILE
B
774
27.075
42.765
34.037
1.00
31.12


ATOM
4534
C
ILE
B
774
22.342
40.909
33.947
1.00
20.74


ATOM
4535
O
ILE
B
774
21.452
41.375
33.239
1.00
21.33


ATOM
4536
N
GLN
B
775
22.482
39.604
34.166
1.00
22.90


ATOM
4537
CA
GLN
B
775
21.569
38.636
33.565
1.00
23.62


ATOM
4538
CB
GLN
B
775
21.965
37.205
33.956
1.00
24.73


ATOM
4539
CG
GLN
B
775
20.801
36.214
33.995
1.00
25.27


ATOM
4540
CD
GLN
B
775
20.070
36.062
32.661
1.00
25.01


ATOM
4541
OE1
GLN
B
775
18.983
35.495
32.610
1.00
23.97


ATOM
4542
NE2
GLN
B
775
20.669
36.556
31.583
1.00
25.73


ATOM
4543
C
GLN
B
775
20.127
38.905
33.987
1.00
24.69


ATOM
4544
O
GLN
B
775
19.213
38.883
33.161
1.00
23.74


ATOM
4545
N
GLN
B
776
19.930
39.158
35.277
1.00
24.42


ATOM
4546
CA
GLN
B
776
18.596
39.440
35.800
1.00
25.46


ATOM
4547
CB
GLN
B
776
18.647
39.710
37.303
1.00
39.22


ATOM
4548
CG
GLN
B
776
18.627
38.482
38.172
1.00
40.03


ATOM
4549
CD
GLN
B
776
18.641
38.828
39.648
1.00
40.44


ATOM
4550
OE1
GLN
B
776
19.635
39.339
40.167
1.00
40.18


ATOM
4551
NE2
GLN
B
776
17.536
38.554
40.332
1.00
40.01


ATOM
4552
C
GLN
B
776
17.989
40.658
35.121
1.00
24.70


ATOM
4553
O
GLN
B
776
16.832
40.641
34.712
1.00
25.09


ATOM
4554
N
ARG
B
777
18.773
41.725
35.028
1.00
23.31


ATOM
4555
CA
ARG
B
777
18.298
42.949
34.410
1.00
23.89


ATOM
4556
CB
ARG
B
777
19.369
44.038
34.481
1.00
27.39


ATOM
4557
CG
ARG
B
777
18.902
45.369
33.917
1.00
27.72


ATOM
4558
CD
ARG
B
777
19.965
46.434
34.058
1.00
28.34


ATOM
4559
NE
ARG
B
777
21.102
46.209
33.170
1.00
27.57


ATOM
4560
CZ
ARG
B
777
21.029
46.232
31.843
1.00
27.93


ATOM
4561
NH1
ARG
B
777
19.870
46.468
31.244
1.00
28.38


ATOM
4562
NH2
ARG
B
777
22.119
46.032
31.113
1.00
27.27


ATOM
4563
C
ARG
B
777
17.905
42.728
32.958
1.00
23.38


ATOM
4564
O
ARG
B
777
16.814
43.119
32.535
1.00
24.57


ATOM
4565
N
ILE
B
778
18.784
42.089
32.191
1.00
18.64


ATOM
4566
CA
ILE
B
778
18.487
41.853
30.783
1.00
19.91


ATOM
4567
CB
ILE
B
778
19.729
41.350
30.028
1.00
21.48


ATOM
4568
CG2
ILE
B
778
19.371
41.065
28.575
1.00
21.88


ATOM
4569
CG1
ILE
B
778
20.809
42.432
30.077
1.00
22.67


ATOM
4570
CD1
ILE
B
778
22.127
42.024
29.472
1.00
22.44


ATOM
4571
C
ILE
B
778
17.333
40.880
30.605
1.00
19.30


ATOM
4572
O
ILE
B
778
16.494
41.063
29.718
1.00
18.16


ATOM
4573
N
ALA
B
779
17.272
39.865
31.459
1.00
20.27


ATOM
4574
CA
ALA
B
779
16.193
38.890
31.393
1.00
21.96


ATOM
4575
CB
ALA
B
779
16.333
37.880
32.513
1.00
23.30


ATOM
4576
C
ALA
B
779
14.851
39.610
31.495
1.00
21.94


ATOM
4577
O
ALA
B
779
13.896
39.271
30.790
1.00
21.55


ATOM
4578
N
GLU
B
780
14.780
40.615
32.361
1.00
23.66


ATOM
4579
CA
GLU
B
780
13.539
41.368
32.520
1.00
24.79


ATOM
4580
CB
GLU
B
780
13.643
42.309
33.723
1.00
46.99


ATOM
4581
CG
GLU
B
780
13.971
41.572
35.016
1.00
47.98


ATOM
4582
CD
GLU
B
780
13.473
42.287
36.255
1.00
48.28


ATOM
4583
OE1
GLU
B
780
13.748
43.499
36.398
1.00
48.22


ATOM
4584
OE2
GLU
B
780
12.814
41.630
37.089
1.00
48.29


ATOM
4585
C
GLU
B
780
13.171
42.144
31.251
1.00
23.73


ATOM
4586
O
GLU
B
780
11.989
42.308
30.931
1.00
23.36


ATOM
4587
N
LEU
B
781
14.180
42.615
30.525
1.00
21.19


ATOM
4588
CA
LEU
B
781
13.949
43.336
29.282
1.00
19.63


ATOM
4589
CB
LEU
B
781
15.257
43.926
28.761
1.00
24.73


ATOM
4590
CG
LEU
B
781
15.902
44.956
29.687
1.00
25.34


ATOM
4591
CD1
LEU
B
781
17.189
45.469
29.065
1.00
25.01


ATOM
4592
CD2
LEU
B
781
14.926
46.101
29.913
1.00
24.85


ATOM
4593
C
LEU
B
781
13.393
42.353
28.261
1.00
21.36


ATOM
4594
O
LEU
B
781
12.510
42.686
27.466
1.00
20.39


ATOM
4595
N
VAL
B
782
13.918
41.134
28.286
1.00
21.98


ATOM
4596
CA
VAL
B
782
13.455
40.112
27.360
1.00
22.60


ATOM
4597
CB
VAL
B
782
14.275
38.812
27.499
1.00
22.53


ATOM
4598
CG1
VAL
B
782
13.660
37.713
26.643
1.00
22.91


ATOM
4599
CG2
VAL
B
782
15.712
39.056
27.054
1.00
23.90


ATOM
4600
C
VAL
B
782
11.988
39.808
27.648
1.00
22.59


ATOM
4601
O
VAL
B
782
11.159
39.746
26.737
1.00
22.68


ATOM
4602
N
ALA
B
783
11.671
39.628
28.925
1.00
20.36


ATOM
4603
CA
ALA
B
783
10.301
39.327
29.323
1.00
20.69


ATOM
4604
CB
ALA
B
783
10.232
39.082
30.821
1.00
21.72


ATOM
4605
C
ALA
B
783
9.376
40.474
28.932
1.00
20.76


ATOM
4606
O
ALA
B
783
8.283
40.249
28.426
1.00
22.62


ATOM
4607
N
THR
B
784
9.823
41.704
29.155
1.00
22.97


ATOM
4608
CA
THR
B
784
9.013
42.862
28.807
1.00
23.28


ATOM
4609
CB
THR
B
784
9.752
44.182
29.139
1.00
23.34


ATOM
4610
OG1
THR
B
784
9.934
44.280
30.562
1.00
23.54


ATOM
4611
CG2
THR
B
784
8.956
45.387
28.645
1.00
23.16


ATOM
4612
C
THR
B
784
8.643
42.846
27.322
1.00
23.86


ATOM
4613
O
THR
B
784
7.485
43.086
26.963
1.00
24.06


ATOM
4614
N
GLU
B
785
9.612
42.547
26.459
1.00
20.32


ATOM
4615
CA
GLU
B
785
9.333
42.519
25.029
1.00
19.62


ATOM
4616
CB
GLU
B
785
10.633
42.371
24.221
1.00
19.82


ATOM
4617
CG
GLU
B
785
10.424
42.346
22.703
1.00
19.80


ATOM
4618
CD
GLU
B
785
11.708
42.572
21.908
1.00
22.07


ATOM
4619
OE1
GLU
B
785
11.800
42.066
20.765
1.00
20.56


ATOM
4620
OE2
GLU
B
785
12.620
43.264
22.408
1.00
19.00


ATOM
4621
C
GLU
B
785
8.360
41.386
24.709
1.00
20.53


ATOM
4622
O
GLU
B
785
7.395
41.588
23.964
1.00
20.48


ATOM
4623
N
PHE
B
786
8.603
40.205
25.276
1.00
19.27


ATOM
4624
CA
PHE
B
786
7.725
39.053
25.054
1.00
20.35


ATOM
4625
CB
PHE
B
786
8.185
37.824
25.853
1.00
27.64


ATOM
4626
CG
PHE
B
786
9.394
37.122
25.285
1.00
28.61


ATOM
4627
CD1
PHE
B
786
9.799
37.330
23.971
1.00
28.46


ATOM
4628
CD2
PHE
B
786
10.111
36.225
26.072
1.00
28.06


ATOM
4629
CE1
PHE
B
786
10.903
36.652
23.451
1.00
28.92


ATOM
4630
CE2
PHE
B
786
11.212
35.543
25.561
1.00
28.43


ATOM
4631
CZ
PHE
B
786
11.608
35.758
24.250
1.00
28.30


ATOM
4632
C
PHE
B
786
6.289
39.380
25.475
1.00
20.75


ATOM
4633
O
PHE
B
786
5.340
39.061
24.760
1.00
18.68


ATOM
4634
N
PHE
B
787
6.144
40.003
26.646
1.00
22.35


ATOM
4635
CA
PHE
B
787
4.825
40.361
27.160
1.00
21.89


ATOM
4636
CB
PHE
B
787
4.917
40.801
28.632
1.00
21.52


ATOM
4637
CG
PHE
B
787
5.419
39.729
29.567
1.00
22.41


ATOM
4638
CD1
PHE
B
787
5.256
38.376
29.265
1.00
22.32


ATOM
4639
CD2
PHE
B
787
6.035
40.070
30.771
1.00
21.61


ATOM
4640
CE1
PHE
B
787
5.698
37.384
30.148
1.00
22.73


ATOM
4641
CE2
PHE
B
787
6.478
39.085
31.653
1.00
22.56


ATOM
4642
CZ
PHE
B
787
6.309
37.742
31.341
1.00
21.88


ATOM
4643
C
PHE
B
787
4.154
41.453
26.317
1.00
21.60


ATOM
4644
O
PHE
B
787
2.924
41.484
26.195
1.00
21.58


ATOM
4645
N
ASP
B
788
4.950
42.338
25.721
1.00
20.66


ATOM
4646
CA
ASP
B
788
4.387
43.384
24.872
1.00
21.38


ATOM
4647
CB
ASP
B
788
5.459
44.404
24.467
1.00
29.62


ATOM
4648
CG
ASP
B
788
4.892
45.559
23.646
1.00
31.03


ATOM
4649
OD1
ASP
B
788
4.010
46.284
24.159
1.00
31.00


ATOM
4650
OD2
ASP
B
788
5.327
45.750
22.486
1.00
30.30


ATOM
4651
C
ASP
B
788
3.802
42.712
23.630
1.00
21.98


ATOM
4652
O
ASP
B
788
2.754
43.116
23.138
1.00
20.90


ATOM
4653
N
GLN
B
789
4.480
41.686
23.117
1.00
18.78


ATOM
4654
CA
GLN
B
789
3.950
40.980
21.958
1.00
19.35


ATOM
4655
CB
GLN
B
789
4.947
39.965
21.397
1.00
18.41


ATOM
4656
CG
GLN
B
789
4.283
39.057
20.363
1.00
19.65


ATOM
4657
CD
GLN
B
789
5.228
38.067
19.715
1.00
19.91


ATOM
4658
OE1
GLN
B
789
4.805
37.004
19.253
1.00
20.58


ATOM
4659
NE2
GLN
B
789
6.503
38.413
19.663
1.00
17.85


ATOM
4660
C
GLN
B
789
2.690
40.240
22.382
1.00
19.10


ATOM
4661
O
GLN
B
789
1.728
40.154
21.622
1.00
19.13


ATOM
4662
N
GLY
B
790
2.713
39.701
23.598
1.00
20.13


ATOM
4663
CA
GLY
B
790
1.565
38.983
24.118
1.00
21.62


ATOM
4664
C
GLY
B
790
0.338
39.870
24.089
1.00
21.39


ATOM
4665
O
GLY
B
790
−0.748
39.426
23.711
1.00
20.51


ATOM
4666
N
ASP
B
791
0.506
41.127
24.491
1.00
21.64


ATOM
4667
CA
ASP
B
791
−0.612
42.066
24.488
1.00
23.10


ATOM
4668
CB
ASP
B
791
−0.205
43.401
25.128
1.00
27.91


ATOM
4669
CG
ASP
B
791
0.161
43.263
26.599
1.00
28.04


ATOM
4670
OD1
ASP
B
791
−0.368
42.352
27.271
1.00
28.51


ATOM
4671
OD2
ASP
B
791
0.967
44.083
27.092
1.00
29.30


ATOM
4672
C
ASP
B
791
−1.118
42.307
23.061
1.00
22.57


ATOM
4673
O
ASP
B
791
−2.328
42.422
22.837
1.00
22.71


ATOM
4674
N
ARG
B
792
−0.196
42.388
22.103
1.00
22.55


ATOM
4675
CA
ARG
B
792
−0.557
42.600
20.701
1.00
21.86


ATOM
4676
CB
ARG
B
792
0.697
42.794
19.831
1.00
25.58


ATOM
4677
CG
ARG
B
792
1.559
44.015
20.155
1.00
26.82


ATOM
4678
CD
ARG
B
792
1.268
45.192
19.225
1.00
27.03


ATOM
4679
NE
ARG
B
792
1.602
44.929
17.819
1.00
26.18


ATOM
4680
CZ
ARG
B
792
2.768
45.220
17.247
1.00
26.00


ATOM
4681
NH1
ARG
B
792
3.746
45.785
17.950
1.00
26.11


ATOM
4682
NH2
ARG
B
792
2.943
44.982
15.954
1.00
27.12


ATOM
4683
C
ARG
B
792
−1.338
41.393
20.179
1.00
21.59


ATOM
4684
O
ARG
B
792
−2.251
41.541
19.366
1.00
22.04


ATOM
4685
N
GLU
B
793
−0.981
40.199
20.640
1.00
21.27


ATOM
4686
CA
GLU
B
793
−1.678
38.999
20.189
1.00
23.41


ATOM
4687
CB
GLU
B
793
−0.915
37.741
20.613
1.00
32.13


ATOM
4688
CG
GLU
B
793
0.523
37.716
20.126
1.00
32.18


ATOM
4689
CD
GLU
B
793
1.199
36.378
20.354
1.00
32.76


ATOM
4690
OE1
GLU
B
793
0.883
35.713
21.363
1.00
33.25


ATOM
4691
OE2
GLU
B
793
2.058
35.998
19.531
1.00
32.81


ATOM
4692
C
GLU
B
793
−3.106
38.946
20.726
1.00
23.75


ATOM
4693
O
GLU
B
793
−4.044
38.610
19.995
1.00
22.66


ATOM
4694
N
ARG
B
794
−3.277
39.283
21.999
1.00
24.04


ATOM
4695
CA
ARG
B
794
−4.603
39.256
22.599
1.00
24.34


ATOM
4696
CB
ARG
B
794
−4.564
39.780
24.038
1.00
32.14


ATOM
4697
CG
ARG
B
794
−3.332
39.401
24.824
1.00
33.26


ATOM
4698
CD
ARG
B
794
−3.543
39.603
26.316
1.00
33.20


ATOM
4699
NE
ARG
B
794
−4.342
38.518
26.866
1.00
33.66


ATOM
4700
CZ
ARG
B
794
−3.964
37.749
27.881
1.00
33.17


ATOM
4701
NH1
ARG
B
794
−2.794
37.948
28.472
1.00
33.10


ATOM
4702
NH2
ARG
B
794
−4.748
36.759
28.285
1.00
33.54


ATOM
4703
C
ARG
B
794
−5.566
40.119
21.797
1.00
25.06


ATOM
4704
O
ARG
B
794
−6.713
39.740
21.563
1.00
24.85


ATOM
4705
N
LYS
B
795
−5.090
41.279
21.369
1.00
26.49


ATOM
4706
CA
LYS
B
795
−5.928
42.205
20.627
1.00
27.67


ATOM
4707
CB
LYS
B
795
−5.412
43.633
20.821
1.00
43.32


ATOM
4708
CG
LYS
B
795
−5.021
43.940
22.260
1.00
43.98


ATOM
4709
CD
LYS
B
795
−4.846
45.433
22.504
1.00
44.35


ATOM
4710
CE
LYS
B
795
−6.121
46.059
23.052
1.00
44.46


ATOM
4711
NZ
LYS
B
795
−7.293
45.855
22.159
1.00
44.56


ATOM
4712
C
LYS
B
795
−6.032
41.883
19.140
1.00
27.05


ATOM
4713
O
LYS
B
795
−7.125
41.624
18.636
1.00
28.54


ATOM
4714
N
GLU
B
796
−4.894
41.885
18.451
1.00
25.18


ATOM
4715
CA
GLU
B
796
−4.842
41.634
17.007
1.00
24.55


ATOM
4716
CB
GLU
B
796
−3.464
42.009
16.464
1.00
28.07


ATOM
4717
CG
GLU
B
796
−2.991
43.391
16.889
1.00
29.00


ATOM
4718
CD
GLU
B
796
−1.615
43.741
16.348
1.00
28.65


ATOM
4719
OE1
GLU
B
796
−0.962
44.626
16.931
1.00
29.39


ATOM
4720
OE2
GLU
B
796
−1.187
43.144
15.340
1.00
29.53


ATOM
4721
C
GLU
B
796
−5.173
40.214
16.549
1.00
24.25


ATOM
4722
O
GLU
B
796
−5.637
40.011
15.423
1.00
25.17


ATOM
4723
N
LEU
B
797
−4.922
39.228
17.399
1.00
22.33


ATOM
4724
CA
LEU
B
797
−5.201
37.847
17.021
1.00
21.19


ATOM
4725
CB
LEU
B
797
−3.923
36.999
17.111
1.00
24.95


ATOM
4726
CG
LEU
B
797
−2.757
37.369
16.184
1.00
24.74


ATOM
4727
CD1
LEU
B
797
−1.555
36.486
16.498
1.00
24.36


ATOM
4728
CD2
LEU
B
797
−3.173
37.209
14.720
1.00
25.36


ATOM
4729
C
LEU
B
797
−6.295
37.239
17.889
1.00
22.61


ATOM
4730
O
LEU
B
797
−6.717
36.108
17.657
1.00
21.44


ATOM
4731
N
ASN
B
798
−6.756
38.002
18.877
1.00
22.45


ATOM
4732
CA
ASN
B
798
−7.807
37.556
19.791
1.00
23.65


ATOM
4733
CB
ASN
B
798
−9.165
37.569
19.089
1.00
32.89


ATOM
4734
CG
ASN
B
798
−10.163
38.479
19.777
1.00
34.23


ATOM
4735
OD1
ASN
B
798
−10.392
38.372
20.982
1.00
32.44


ATOM
4736
ND2
ASN
B
798
−10.767
39.381
19.010
1.00
35.38


ATOM
4737
C
ASN
B
798
−7.532
36.164
20.352
1.00
23.21


ATOM
4738
O
ASN
B
798
−8.414
35.305
20.384
1.00
23.77


ATOM
4739
N
ILE
B
799
−6.299
35.945
20.794
1.00
22.30


ATOM
4740
CA
ILE
B
799
−5.914
34.655
21.359
1.00
24.01


ATOM
4741
CB
ILE
B
799
−4.993
33.868
20.403
1.00
37.22


ATOM
4742
CG2
ILE
B
799
−5.661
33.695
19.047
1.00
37.98


ATOM
4743
CG1
ILE
B
799
−3.664
34.613
20.244
1.00
37.41


ATOM
4744
CD1
ILE
B
799
−2.556
33.780
19.633
1.00
37.91


ATOM
4745
C
ILE
B
799
−5.146
34.867
22.658
1.00
23.86


ATOM
4746
O
ILE
B
799
−4.542
35.922
22.867
1.00
22.69


ATOM
4747
N
GLU
B
800
−5.178
33.870
23.533
1.00
27.63


ATOM
4748
CA
GLU
B
800
−4.442
33.961
24.787
1.00
28.49


ATOM
4749
CB
GLU
B
800
−4.912
32.882
25.766
1.00
54.96


ATOM
4750
CG
GLU
B
800
−4.159
32.874
27.091
1.00
55.87


ATOM
4751
CD
GLU
B
800
−4.612
31.758
28.018
1.00
56.25


ATOM
4752
OE1
GLU
B
800
−4.037
31.633
29.121
1.00
56.19


ATOM
4753
OE2
GLU
B
800
−5.541
31.008
27.645
1.00
56.33


ATOM
4754
C
GLU
B
800
−2.995
33.711
24.385
1.00
28.05


ATOM
4755
O
GLU
B
800
−2.712
32.791
23.616
1.00
28.04


ATOM
4756
N
PRO
B
801
−2.060
34.539
24.866
1.00
26.29


ATOM
4757
CD
PRO
B
801
−2.159
35.766
25.673
1.00
32.02


ATOM
4758
CA
PRO
B
801
−0.675
34.280
24.465
1.00
25.59


ATOM
4759
CB
PRO
B
801
0.047
35.561
24.875
1.00
32.25


ATOM
4760
CG
PRO
B
801
−0.719
35.993
26.085
1.00
32.69


ATOM
4761
C
PRO
B
801
−0.115
33.044
25.155
1.00
25.64


ATOM
4762
O
PRO
B
801
−0.688
32.552
26.127
1.00
26.27


ATOM
4763
N
THR
B
802
0.990
32.529
24.634
1.00
27.06


ATOM
4764
CA
THR
B
802
1.622
31.366
25.242
1.00
27.00


ATOM
4765
CB
THR
B
802
2.731
30.798
24.340
1.00
41.37


ATOM
4766
OG1
THR
B
802
3.289
29.626
24.947
1.00
42.49


ATOM
4767
CG2
THR
B
802
3.824
31.831
24.124
1.00
41.44


ATOM
4768
C
THR
B
802
2.220
31.839
26.562
1.00
26.88


ATOM
4769
O
THR
B
802
2.390
33.041
26.776
1.00
25.80


ATOM
4770
N
ASP
B
803
2.526
30.902
27.449
1.00
25.95


ATOM
4771
CA
ASP
B
803
3.096
31.248
28.744
1.00
25.37


ATOM
4772
CB
ASP
B
803
3.534
29.974
29.469
1.00
34.61


ATOM
4773
CG
ASP
B
803
2.374
29.260
30.141
1.00
34.77


ATOM
4774
OD1
ASP
B
803
1.263
29.252
29.568
1.00
34.79


ATOM
4775
OD2
ASP
B
803
2.581
28.699
31.238
1.00
35.35


ATOM
4776
C
ASP
B
803
4.260
32.240
28.673
1.00
24.64


ATOM
4777
O
ASP
B
803
4.283
33.226
29.409
1.00
25.72


ATOM
4778
N
LEU
B
804
5.217
31.999
27.785
1.00
27.10


ATOM
4779
CA
LEU
B
804
6.359
32.899
27.686
1.00
26.94


ATOM
4780
CB
LEU
B
804
7.423
32.300
26.757
1.00
52.26


ATOM
4781
CG
LEU
B
804
7.015
31.757
25.390
1.00
53.10


ATOM
4782
CD1
LEU
B
804
7.196
32.830
24.331
1.00
53.31


ATOM
4783
CD2
LEU
B
804
7.882
30.551
25.052
1.00
53.28


ATOM
4784
C
LEU
B
804
6.012
34.329
27.268
1.00
26.18


ATOM
4785
O
LEU
B
804
6.806
35.240
27.474
1.00
26.67


ATOM
4786
N
MET
B
805
4.823
34.537
26.705
1.00
24.63


ATOM
4787
CA
MET
B
805
4.423
35.880
26.285
1.00
24.58


ATOM
4788
CB
MET
B
805
4.151
35.902
24.780
1.00
30.72


ATOM
4789
CG
MET
B
805
5.333
35.419
23.963
1.00
31.20


ATOM
4790
SD
MET
B
805
5.137
35.642
22.209
1.00
31.94


ATOM
4791
CE
MET
B
805
6.846
35.924
21.734
1.00
31.24


ATOM
4792
C
MET
B
805
3.191
36.373
27.044
1.00
23.91


ATOM
4793
O
MET
B
805
2.552
37.352
26.647
1.00
23.70


ATOM
4794
N
ASN
B
806
2.884
35.699
28.147
1.00
22.71


ATOM
4795
CA
ASN
B
806
1.728
36.042
28.970
1.00
23.25


ATOM
4796
CB
ASN
B
806
0.917
34.772
29.255
1.00
28.25


ATOM
4797
CG
ASN
B
806
−0.352
35.045
30.054
1.00
27.90


ATOM
4798
OD1
ASN
B
806
−0.642
36.181
30.420
1.00
28.09


ATOM
4799
ND2
ASN
B
806
−1.114
33.991
30.325
1.00
28.50


ATOM
4800
C
ASN
B
806
2.177
36.683
30.281
1.00
23.54


ATOM
4801
O
ASN
B
806
2.651
35.992
31.178
1.00
24.88


ATOM
4802
N
ARG
B
807
2.023
38.003
30.386
1.00
22.01


ATOM
4803
CA
ARG
B
807
2.417
38.748
31.585
1.00
22.16


ATOM
4804
CB
ARG
B
807
2.040
40.223
31.426
1.00
30.21


ATOM
4805
CG
ARG
B
807
2.729
41.167
32.399
1.00
30.83


ATOM
4806
CD
ARG
B
807
2.164
42.572
32.270
1.00
30.96


ATOM
4807
NE
ARG
B
807
2.118
43.013
30.879
1.00
31.52


ATOM
4808
CZ
ARG
B
807
3.161
43.482
30.205
1.00
31.30


ATOM
4809
NH1
ARG
B
807
4.347
43.583
30.795
1.00
31.76


ATOM
4810
NH2
ARG
B
807
3.019
43.843
28.935
1.00
30.41


ATOM
4811
C
ARG
B
807
1.753
38.186
32.844
1.00
23.50


ATOM
4812
O
ARG
B
807
2.324
38.241
33.933
1.00
22.48


ATOM
4813
N
GLU
B
808
0.549
37.645
32.694
1.00
27.30


ATOM
4814
CA
GLU
B
808
−0.164
37.075
33.833
1.00
27.61


ATOM
4815
CB
GLU
B
808
−1.585
36.680
33.421
1.00
44.18


ATOM
4816
CG
GLU
B
808
−2.572
37.835
33.427
1.00
44.75


ATOM
4817
CD
GLU
B
808
−3.887
37.494
32.750
1.00
45.10


ATOM
4818
OE1
GLU
B
808
−4.418
36.388
32.990
1.00
44.66


ATOM
4819
OE2
GLU
B
808
−4.390
38.342
31.982
1.00
44.84


ATOM
4820
C
GLU
B
808
0.559
35.865
34.416
1.00
28.07


ATOM
4821
O
GLU
B
808
0.426
35.572
35.604
1.00
27.52


ATOM
4822
N
LYS
B
809
1.328
35.171
33.582
1.00
30.73


ATOM
4823
CA
LYS
B
809
2.063
33.984
34.015
1.00
31.34


ATOM
4824
CB
LYS
B
809
1.888
32.856
32.988
1.00
44.52


ATOM
4825
CG
LYS
B
809
0.443
32.434
32.739
1.00
44.86


ATOM
4826
CD
LYS
B
809
−0.095
31.554
33.853
1.00
45.24


ATOM
4827
CE
LYS
B
809
0.499
30.152
33.794
1.00
45.08


ATOM
4828
NZ
LYS
B
809
0.023
29.386
32.607
1.00
45.32


ATOM
4829
C
LYS
B
809
3.549
34.280
34.187
1.00
31.41


ATOM
4830
O
LYS
B
809
4.389
33.396
34.014
1.00
31.64


ATOM
4831
N
LYS
B
810
3.874
35.522
34.534
1.00
29.88


ATOM
4832
CA
LYS
B
810
5.266
35.924
34.714
1.00
29.67


ATOM
4833
CB
LYS
B
810
5.350
37.417
35.033
1.00
35.65


ATOM
4834
CG
LYS
B
810
4.772
37.787
36.384
1.00
35.72


ATOM
4835
CD
LYS
B
810
4.977
39.256
36.681
1.00
36.06


ATOM
4836
CE
LYS
B
810
4.445
39.617
38.058
1.00
36.21


ATOM
4837
NZ
LYS
B
810
4.806
41.010
38.416
1.00
36.50


ATOM
4838
C
LYS
B
810
5.981
35.135
35.815
1.00
29.55


ATOM
4839
O
LYS
B
810
7.204
35.220
35.954
1.00
29.80


ATOM
4840
N
ASN
B
811
5.221
34.371
36.595
1.00
28.77


ATOM
4841
CA
ASN
B
811
5.809
33.576
37.672
1.00
28.26


ATOM
4842
CB
ASN
B
811
4.716
33.113
38.643
1.00
33.98


ATOM
4843
CG
ASN
B
811
3.760
32.122
38.012
1.00
33.96


ATOM
4844
OD1
ASN
B
811
4.059
30.935
37.904
1.00
34.26


ATOM
4845
ND2
ASN
B
811
2.607
32.611
37.578
1.00
34.21


ATOM
4846
C
ASN
B
811
6.558
32.364
37.122
1.00
28.78


ATOM
4847
O
ASN
B
811
7.277
31.681
37.852
1.00
28.05


ATOM
4848
N
LYS
B
812
6.391
32.112
35.826
1.00
27.42


ATOM
4849
CA
LYS
B
812
7.034
30.983
35.161
1.00
27.06


ATOM
4850
CB
LYS
B
812
6.175
30.518
33.980
1.00
41.02


ATOM
4851
CG
LYS
B
812
5.384
29.246
34.224
1.00
41.61


ATOM
4852
CD
LYS
B
812
4.485
29.360
35.436
1.00
41.66


ATOM
4853
CE
LYS
B
812
3.735
28.062
35.681
1.00
41.87


ATOM
4854
NZ
LYS
B
812
4.665
26.921
35.913
1.00
41.60


ATOM
4855
C
LYS
B
812
8.436
31.306
34.655
1.00
25.94


ATOM
4856
O
LYS
B
812
9.169
30.409
34.248
1.00
27.20


ATOM
4857
N
ILE
B
813
8.814
32.579
34.693
1.00
24.47


ATOM
4858
CA
ILE
B
813
10.126
32.993
34.203
1.00
24.87


ATOM
4859
CB
ILE
B
813
10.353
34.509
34.452
1.00
27.03


ATOM
4860
CG2
ILE
B
813
11.812
34.887
34.190
1.00
26.32


ATOM
4861
CG1
ILE
B
813
9.420
35.312
33.537
1.00
27.43


ATOM
4862
CD1
ILE
B
813
9.422
36.809
33.792
1.00
27.47


ATOM
4863
C
ILE
B
813
11.321
32.198
34.725
1.00
24.94


ATOM
4864
O
ILE
B
813
12.153
31.747
33.940
1.00
24.37


ATOM
4865
N
PRO
B
814
11.433
32.015
36.051
1.00
23.33


ATOM
4866
CD
PRO
B
814
10.649
32.549
37.180
1.00
25.56


ATOM
4867
CA
PRO
B
814
12.588
31.251
36.536
1.00
24.96


ATOM
4868
CB
PRO
B
814
12.336
31.171
38.041
1.00
25.58


ATOM
4869
CG
PRO
B
814
11.650
32.478
38.317
1.00
25.37


ATOM
4870
C
PRO
B
814
12.708
29.870
35.892
1.00
24.30


ATOM
4871
O
PRO
B
814
13.752
29.519
35.346
1.00
26.00


ATOM
4872
N
SER
B
815
11.629
29.101
35.942
1.00
27.38


ATOM
4873
CA
SER
B
815
11.631
27.759
35.372
1.00
28.28


ATOM
4874
CB
SER
B
815
10.320
27.048
35.705
1.00
30.12


ATOM
4875
OG
SER
B
815
9.214
27.762
35.193
1.00
30.40


ATOM
4876
C
SER
B
815
11.852
27.767
33.860
1.00
28.08


ATOM
4877
O
SER
B
815
12.426
26.831
33.307
1.00
28.51


ATOM
4878
N
MET
B
816
11.405
28.822
33.190
1.00
26.53


ATOM
4879
CA
MET
B
816
11.581
28.899
31.743
1.00
25.98


ATOM
4880
CB
MET
B
816
10.633
29.940
31.147
1.00
38.18


ATOM
4881
CG
MET
B
816
9.173
29.635
31.422
1.00
38.60


ATOM
4882
SD
MET
B
816
8.038
30.687
30.502
1.00
40.03


ATOM
4883
CE
MET
B
816
8.543
32.319
31.070
1.00
38.78


ATOM
4884
C
MET
B
816
13.021
29.224
31.384
1.00
25.44


ATOM
4885
O
MET
B
816
13.540
28.736
30.383
1.00
25.22


ATOM
4886
N
GLN
B
817
13.666
30.047
32.207
1.00
24.56


ATOM
4887
CA
GLN
B
817
15.057
30.413
31.984
1.00
24.03


ATOM
4888
CB
GLN
B
817
15.503
31.465
33.000
1.00
23.33


ATOM
4889
CG
GLN
B
817
15.074
32.885
32.672
1.00
23.25


ATOM
4890
CD
GLN
B
817
15.603
33.349
31.331
1.00
24.23


ATOM
4891
OE1
GLN
B
817
15.073
32.980
30.285
1.00
23.44


ATOM
4892
NE2
GLN
B
817
16.666
34.146
31.354
1.00
23.50


ATOM
4893
C
GLN
B
817
15.923
29.166
32.122
1.00
24.21


ATOM
4894
O
GLN
B
817
16.862
28.961
31.350
1.00
25.39


ATOM
4895
N
VAL
B
818
15.609
28.342
33.116
1.00
22.52


ATOM
4896
CA
VAL
B
818
16.350
27.103
33.331
1.00
24.31


ATOM
4897
CB
VAL
B
818
15.820
26.335
34.562
1.00
26.47


ATOM
4898
CG1
VAL
B
818
16.541
24.993
34.688
1.00
26.36


ATOM
4899
CG2
VAL
B
818
16.037
27.164
35.815
1.00
26.36


ATOM
4900
C
VAL
B
818
16.182
26.236
32.085
1.00
23.82


ATOM
4901
O
VAL
B
818
17.148
25.659
31.588
1.00
23.44


ATOM
4902
N
GLY
B
819
14.953
26.172
31.577
1.00
26.53


ATOM
4903
CA
GLY
B
819
14.669
25.386
30.385
1.00
25.97


ATOM
4904
C
GLY
B
819
15.410
25.903
29.164
1.00
25.98


ATOM
4905
O
GLY
B
819
15.928
25.128
28.365
1.00
25.51


ATOM
4906
N
PHE
B
820
15.455
27.223
29.021
1.00
22.89


ATOM
4907
CA
PHE
B
820
16.149
27.869
27.906
1.00
22.59


ATOM
4908
CB
PHE
B
820
15.941
29.389
27.997
1.00
24.78


ATOM
4909
CG
PHE
B
820
16.821
30.195
27.078
1.00
26.25


ATOM
4910
CD1
PHE
B
820
16.716
30.071
25.696
1.00
25.90


ATOM
4911
CD2
PHE
B
820
17.742
31.104
27.601
1.00
24.43


ATOM
4912
CE1
PHE
B
820
17.513
30.841
24.845
1.00
25.64


ATOM
4913
CE2
PHE
B
820
18.545
31.877
26.762
1.00
25.89


ATOM
4914
CZ
PHE
B
820
18.432
31.747
25.381
1.00
25.35


ATOM
4915
C
PHE
B
820
17.641
27.535
27.953
1.00
22.74


ATOM
4916
O
PHE
B
820
18.256
27.231
26.932
1.00
21.86


ATOM
4917
N
ILE
B
821
18.222
27.595
29.143
1.00
24.60


ATOM
4918
CA
ILE
B
821
19.640
27.303
29.295
1.00
26.01


ATOM
4919
CB
ILE
B
821
20.099
27.593
30.739
1.00
23.25


ATOM
4920
CG2
ILE
B
821
21.480
27.001
30.984
1.00
23.21


ATOM
4921
CG1
ILE
B
821
20.096
29.105
30.980
1.00
22.99


ATOM
4922
CD1
ILE
B
821
20.409
29.506
32.410
1.00
23.26


ATOM
4923
C
ILE
B
821
19.944
25.848
28.929
1.00
26.27


ATOM
4924
O
ILE
B
821
20.893
25.565
28.187
1.00
26.66


ATOM
4925
N
ASP
B
822
19.129
24.931
29.436
1.00
29.94


ATOM
4926
CA
ASP
B
822
19.332
23.511
29.168
1.00
30.98


ATOM
4927
CB
ASP
B
822
18.391
22.657
30.023
1.00
31.31


ATOM
4928
CG
ASP
B
822
18.798
22.617
31.478
1.00
31.53


ATOM
4929
OD1
ASP
B
822
19.984
22.882
31.771
1.00
31.53


ATOM
4930
OD2
ASP
B
822
17.939
22.301
32.330
1.00
31.44


ATOM
4931
C
ASP
B
822
19.147
23.103
27.715
1.00
30.90


ATOM
4932
O
ASP
B
822
19.963
22.368
27.162
1.00
31.36


ATOM
4933
N
ALA
B
823
18.070
23.577
27.102
1.00
28.23


ATOM
4934
CA
ALA
B
823
17.757
23.217
25.724
1.00
27.21


ATOM
4935
CB
ALA
B
823
16.268
23.438
25.470
1.00
28.57


ATOM
4936
C
ALA
B
823
18.563
23.923
24.642
1.00
27.07


ATOM
4937
O
ALA
B
823
18.861
23.330
23.607
1.00
27.74


ATOM
4938
N
ILE
B
824
18.926
25.178
24.878
1.00
23.52


ATOM
4939
CA
ILE
B
824
19.639
25.950
23.869
1.00
23.73


ATOM
4940
CB
ILE
B
824
18.802
27.205
23.482
1.00
34.66


ATOM
4941
CG2
ILE
B
824
19.646
28.198
22.686
1.00
35.04


ATOM
4942
CG1
ILE
B
824
17.571
26.780
22.682
1.00
35.26


ATOM
4943
CD1
ILE
B
824
17.912
26.136
21.354
1.00
35.75


ATOM
4944
C
ILE
B
824
21.052
26.416
24.195
1.00
23.62


ATOM
4945
O
ILE
B
824
21.963
26.256
23.387
1.00
24.76


ATOM
4946
N
CYS
B
825
21.242
26.982
25.381
1.00
25.35


ATOM
4947
CA
CYS
B
825
22.537
27.545
25.750
1.00
25.12


ATOM
4948
CB
CYS
B
825
22.322
28.602
26.827
1.00
22.81


ATOM
4949
SG
CYS
B
825
21.059
29.783
26.356
1.00
22.83


ATOM
4950
C
CYS
B
825
23.700
26.653
26.169
1.00
25.45


ATOM
4951
O
CYS
B
825
24.796
26.778
25.627
1.00
26.37


ATOM
4952
N
LEU
B
826
23.477
25.783
27.145
1.00
25.06


ATOM
4953
CA
LEU
B
826
24.541
24.921
27.651
1.00
26.86


ATOM
4954
CB
LEU
B
826
23.954
23.898
28.626
1.00
41.13


ATOM
4955
CG
LEU
B
826
24.523
23.958
30.048
1.00
41.95


ATOM
4956
CD1
LEU
B
826
24.537
25.392
30.550
1.00
41.82


ATOM
4957
CD2
LEU
B
826
23.695
23.076
30.967
1.00
41.66


ATOM
4958
C
LEU
B
826
25.397
24.208
26.606
1.00
25.29


ATOM
4959
O
LEU
B
826
26.623
24.327
26.619
1.00
27.23


ATOM
4960
N
GLN
B
827
24.764
23.467
25.703
1.00
27.86


ATOM
4961
CA
GLN
B
827
25.512
22.737
24.679
1.00
27.22


ATOM
4962
CB
GLN
B
827
24.560
21.935
23.796
1.00
43.35


ATOM
4963
CG
GLN
B
827
23.663
20.981
24.546
1.00
43.82


ATOM
4964
CD
GLN
B
827
22.683
20.289
23.626
1.00
44.18


ATOM
4965
OE1
GLN
B
827
23.077
19.509
22.759
1.00
44.12


ATOM
4966
NE2
GLN
B
827
21.396
20.582
23.800
1.00
44.14


ATOM
4967
C
GLN
B
827
26.346
23.652
23.791
1.00
27.96


ATOM
4968
O
GLN
B
827
27.469
23.310
23.417
1.00
27.98


ATOM
4969
N
LEU
B
828
25.789
24.807
23.439
1.00
23.58


ATOM
4970
CA
LEU
B
828
26.491
25.753
22.585
1.00
23.82


ATOM
4971
CB
LEU
B
828
25.574
26.922
22.212
1.00
24.08


ATOM
4972
CG
LEU
B
828
26.222
28.012
21.353
1.00
24.69


ATOM
4973
CD1
LEU
B
828
26.835
27.406
20.087
1.00
24.52


ATOM
4974
CD2
LEU
B
828
25.180
29.058
21.001
1.00
24.55


ATOM
4975
C
LEU
B
828
27.768
26.289
23.218
1.00
23.20


ATOM
4976
O
LEU
B
828
28.824
26.307
22.586
1.00
23.94


ATOM
4977
N
TYR
B
829
27.681
26.736
24.464
1.00
24.32


ATOM
4978
CA
TYR
B
829
28.866
27.266
25.122
1.00
24.21


ATOM
4979
CB
TYR
B
829
28.461
28.040
26.378
1.00
23.28


ATOM
4980
CG
TYR
B
829
27.724
29.315
26.015
1.00
21.35


ATOM
4981
CD1
TYR
B
829
28.358
30.318
25.280
1.00
22.17


ATOM
4982
CE1
TYR
B
829
27.673
31.462
24.866
1.00
21.77


ATOM
4983
CD2
TYR
B
829
26.383
29.488
26.337
1.00
23.05


ATOM
4984
CE2
TYR
B
829
25.686
30.630
25.928
1.00
21.86


ATOM
4985
CZ
TYR
B
829
26.338
31.609
25.192
1.00
22.76


ATOM
4986
OH
TYR
B
829
25.662
32.733
24.759
1.00
20.79


ATOM
4987
C
TYR
B
829
29.871
26.163
25.428
1.00
25.08


ATOM
4988
O
TYR
B
829
31.076
26.408
25.465
1.00
24.92


ATOM
4989
N
GLU
B
830
29.380
24.944
25.628
1.00
25.46


ATOM
4990
CA
GLU
B
830
30.278
23.826
25.892
1.00
27.34


ATOM
4991
CB
GLU
B
830
29.482
22.572
26.268
1.00
35.78


ATOM
4992
CG
GLU
B
830
28.822
22.637
27.635
1.00
36.70


ATOM
4993
CD
GLU
B
830
27.981
21.409
27.938
1.00
36.51


ATOM
4994
OE1
GLU
B
830
27.433
21.318
29.056
1.00
36.91


ATOM
4995
OE2
GLU
B
830
27.863
20.533
27.053
1.00
37.38


ATOM
4996
C
GLU
B
830
31.087
23.563
24.624
1.00
26.06


ATOM
4997
O
GLU
B
830
32.305
23.377
24.679
1.00
26.54


ATOM
4998
N
ALA
B
831
30.398
23.566
23.486
1.00
25.64


ATOM
4999
CA
ALA
B
831
31.026
23.332
22.189
1.00
23.78


ATOM
5000
CB
ALA
B
831
29.952
23.253
21.093
1.00
30.54


ATOM
5001
C
ALA
B
831
32.031
24.427
21.853
1.00
24.89


ATOM
5002
O
ALA
B
831
33.110
24.151
21.328
1.00
24.70


ATOM
5003
N
LEU
B
832
31.679
25.671
22.158
1.00
22.52


ATOM
5004
CA
LEU
B
832
32.578
26.778
21.872
1.00
23.49


ATOM
5005
CB
LEU
B
832
31.905
28.116
22.198
1.00
21.26


ATOM
5006
CG
LEU
B
832
32.754
29.333
21.824
1.00
22.68


ATOM
5007
CD1
LEU
B
832
33.199
29.213
20.369
1.00
21.78


ATOM
5008
CD2
LEU
B
832
31.963
30.613
22.042
1.00
22.23


ATOM
5009
C
LEU
B
832
33.854
26.627
22.694
1.00
22.63


ATOM
5010
O
LEU
B
832
34.955
26.916
22.220
1.00
23.62


ATOM
5011
N
THR
B
833
33.697
26.165
23.928
1.00
26.15


ATOM
5012
CA
THR
B
833
34.828
25.973
24.822
1.00
27.69


ATOM
5013
CB
THR
B
833
34.350
25.621
26.247
1.00
25.51


ATOM
5014
OG1
THR
B
833
33.549
26.695
26.759
1.00
27.15


ATOM
5015
CG2
THR
B
833
35.539
25.401
27.181
1.00
26.42


ATOM
5016
C
THR
B
833
35.733
24.862
24.293
1.00
27.86


ATOM
5017
O
THR
B
833
36.949
24.876
24.506
1.00
27.78


ATOM
5018
N
HIS
B
834
35.132
23.904
23.600
1.00
29.42


ATOM
5019
CA
HIS
B
834
35.885
22.795
23.026
1.00
30.11


ATOM
5020
CB
HIS
B
834
34.920
21.755
22.449
1.00
46.85


ATOM
5021
CG
HIS
B
834
35.571
20.457
22.084
1.00
47.63


ATOM
5022
CD2
HIS
B
834
36.207
20.064
20.955
1.00
47.79


ATOM
5023
ND1
HIS
B
834
35.621
19.382
22.945
1.00
47.75


ATOM
5024
CE1
HIS
B
834
36.257
18.381
22.361
1.00
47.72


ATOM
5025
NE2
HIS
B
834
36.623
18.769
21.153
1.00
47.50


ATOM
5026
C
HIS
B
834
36.773
23.351
21.912
1.00
30.08


ATOM
5027
O
HIS
B
834
37.939
22.972
21.773
1.00
30.93


ATOM
5028
N
VAL
B
835
36.209
24.259
21.119
1.00
25.19


ATOM
5029
CA
VAL
B
835
36.935
24.866
20.015
1.00
25.37


ATOM
5030
CB
VAL
B
835
35.986
25.730
19.144
1.00
27.06


ATOM
5031
CG1
VAL
B
835
36.764
26.460
18.071
1.00
27.88


ATOM
5032
CG2
VAL
B
835
34.932
24.842
18.505
1.00
27.32


ATOM
5033
C
VAL
B
835
38.107
25.704
20.515
1.00
25.36


ATOM
5034
O
VAL
B
835
39.204
25.626
19.971
1.00
25.68


ATOM
5035
N
SER
B
836
37.874
26.504
21.552
1.00
28.63


ATOM
5036
CA
SER
B
836
38.926
27.340
22.130
1.00
29.30


ATOM
5037
CB
SER
B
836
38.924
28.734
21.489
1.00
32.06


ATOM
5038
OG
SER
B
836
39.982
29.529
21.996
1.00
32.73


ATOM
5039
C
SER
B
836
38.674
27.454
23.629
1.00
29.51


ATOM
5040
O
SER
B
836
37.718
28.096
24.058
1.00
28.84


ATOM
5041
N
GLU
B
837
39.530
26.825
24.426
1.00
26.81


ATOM
5042
CA
GLU
B
837
39.359
26.846
25.874
1.00
27.10


ATOM
5043
CB
GLU
B
837
40.430
25.972
26.536
1.00
50.60


ATOM
5044
CG
GLU
B
837
41.843
26.245
26.062
1.00
51.48


ATOM
5045
CD
GLU
B
837
42.811
25.145
26.460
1.00
51.89


ATOM
5046
OE1
GLU
B
837
42.985
24.912
27.677
1.00
51.52


ATOM
5047
OE2
GLU
B
837
43.394
24.512
25.552
1.00
51.73


ATOM
5048
C
GLU
B
837
39.348
28.242
26.494
1.00
26.43


ATOM
5049
O
GLU
B
837
38.902
28.413
27.628
1.00
27.28


ATOM
5050
N
ASP
B
838
39.819
29.238
25.749
1.00
24.88


ATOM
5051
CA
ASP
B
838
39.846
30.604
26.254
1.00
25.77


ATOM
5052
CB
ASP
B
838
40.811
31.457
25.428
1.00
38.63


ATOM
5053
CG
ASP
B
838
42.256
31.011
25.582
1.00
39.53


ATOM
5054
OD1
ASP
B
838
42.765
31.036
26.724
1.00
39.53


ATOM
5055
OD2
ASP
B
838
42.877
30.633
24.568
1.00
39.29


ATOM
5056
C
ASP
B
838
38.449
31.226
26.252
1.00
25.03


ATOM
5057
O
ASP
B
838
38.277
32.360
26.699
1.00
25.25


ATOM
5058
N
CYS
B
839
37.464
30.483
25.748
1.00
29.32


ATOM
5059
CA
CYS
B
839
36.073
30.949
25.721
1.00
28.67


ATOM
5060
CB
CYS
B
839
35.383
30.561
24.400
1.00
25.46


ATOM
5061
SG
CYS
B
839
35.809
31.580
22.967
1.00
23.35


ATOM
5062
C
CYS
B
839
35.299
30.342
26.895
1.00
29.69


ATOM
5063
O
CYS
B
839
34.075
30.468
26.984
1.00
29.52


ATOM
5064
N
PHE
B
840
36.023
29.686
27.798
1.00
26.11


ATOM
5065
CA
PHE
B
840
35.405
29.055
28.960
1.00
25.54


ATOM
5066
CB
PHE
B
840
36.467
28.387
29.834
1.00
29.48


ATOM
5067
CG
PHE
B
840
35.916
27.797
31.101
1.00
29.46


ATOM
5068
CD1
PHE
B
840
35.084
26.679
31.060
1.00
29.72


ATOM
5069
CD2
PHE
B
840
36.204
28.373
32.333
1.00
29.95


ATOM
5070
CE1
PHE
B
840
34.546
26.143
32.231
1.00
30.22


ATOM
5071
CE2
PHE
B
840
35.671
27.845
33.512
1.00
29.42


ATOM
5072
CZ
PHE
B
840
34.840
26.729
33.460
1.00
29.68


ATOM
5073
C
PHE
B
840
34.567
29.996
29.831
1.00
26.06


ATOM
5074
O
PHE
B
840
33.531
29.593
30.354
1.00
26.34


ATOM
5075
N
PRO
B
841
35.007
31.253
30.013
1.00
25.13


ATOM
5076
CD
PRO
B
841
36.255
31.904
29.575
1.00
24.36


ATOM
5077
CA
PRO
B
841
34.210
32.164
30.846
1.00
24.99


ATOM
5078
CB
PRO
B
841
34.927
33.502
30.673
1.00
24.78


ATOM
5079
CG
PRO
B
841
36.368
33.073
30.535
1.00
24.46


ATOM
5080
C
PRO
B
841
32.729
32.229
30.446
1.00
24.81


ATOM
5081
O
PRO
B
841
31.865
32.393
31.300
1.00
25.33


ATOM
5082
N
LEU
B
842
32.435
32.096
29.155
1.00
24.08


ATOM
5083
CA
LEU
B
842
31.044
32.143
28.707
1.00
22.49


ATOM
5084
CB
LEU
B
842
30.972
32.171
27.177
1.00
19.33


ATOM
5085
CG
LEU
B
842
31.614
33.377
26.488
1.00
20.20


ATOM
5086
CD1
LEU
B
842
31.712
33.118
24.985
1.00
19.25


ATOM
5087
CD2
LEU
B
842
30.794
34.632
26.783
1.00
20.71


ATOM
5088
C
LEU
B
842
30.260
30.944
29.242
1.00
22.87


ATOM
5089
O
LEU
B
842
29.143
31.088
29.732
1.00
23.13


ATOM
5090
N
LEU
B
843
30.855
29.760
29.158
1.00
22.66


ATOM
5091
CA
LEU
B
843
30.195
28.553
29.640
1.00
22.53


ATOM
5092
CB
LEU
B
843
31.032
27.317
29.298
1.00
33.57


ATOM
5093
CG
LEU
B
843
30.366
25.935
29.275
1.00
34.94


ATOM
5094
CD1
LEU
B
843
31.458
24.882
29.157
1.00
34.20


ATOM
5095
CD2
LEU
B
843
29.540
25.691
30.515
1.00
34.62


ATOM
5096
C
LEU
B
843
30.024
28.635
31.153
1.00
22.75


ATOM
5097
O
LEU
B
843
28.976
28.280
31.690
1.00
22.24


ATOM
5098
N
ASP
B
844
31.068
29.101
31.831
1.00
25.80


ATOM
5099
CA
ASP
B
844
31.061
29.228
33.283
1.00
26.51


ATOM
5100
CB
ASP
B
844
32.425
29.733
33.761
1.00
37.17


ATOM
5101
CG
ASP
B
844
32.584
29.653
35.267
1.00
37.71


ATOM
5102
OD1
ASP
B
844
32.277
28.589
35.844
1.00
37.75


ATOM
5103
OD2
ASP
B
844
33.028
30.654
35.871
1.00
38.29


ATOM
5104
C
ASP
B
844
29.953
30.171
33.750
1.00
26.88


ATOM
5105
O
ASP
B
844
29.215
29.855
34.683
1.00
25.76


ATOM
5106
N
GLY
B
845
29.840
31.323
33.093
1.00
27.19


ATOM
5107
CA
GLY
B
845
28.811
32.281
33.457
1.00
27.20


ATOM
5108
C
GLY
B
845
27.418
31.719
33.239
1.00
27.51


ATOM
5109
O
GLY
B
845
26.511
31.944
34.043
1.00
26.76


ATOM
5110
N
CYS
B
846
27.246
30.982
32.147
1.00
23.86


ATOM
5111
CA
CYS
B
846
25.956
30.381
31.838
1.00
24.52


ATOM
5112
CB
CYS
B
846
26.026
29.636
30.505
1.00
23.78


ATOM
5113
SG
CYS
B
846
24.460
28.924
29.962
1.00
22.31


ATOM
5114
C
CYS
B
846
25.538
29.414
32.938
1.00
24.60


ATOM
5115
O
CYS
B
846
24.388
29.414
33.373
1.00
24.31


ATOM
5116
N
ARG
B
847
26.477
28.589
33.394
1.00
26.53


ATOM
5117
CA
ARG
B
847
26.174
27.621
34.438
1.00
26.50


ATOM
5118
CB
ARG
B
847
27.317
26.605
34.556
1.00
46.23


ATOM
5119
CG
ARG
B
847
27.486
25.797
33.273
1.00
46.99


ATOM
5120
CD
ARG
B
847
28.277
24.507
33.443
1.00
47.45


ATOM
5121
NE
ARG
B
847
29.724
24.700
33.406
1.00
47.23


ATOM
5122
CZ
ARG
B
847
30.594
23.737
33.111
1.00
47.33


ATOM
5123
NH1
ARG
B
847
30.165
22.517
32.822
1.00
47.47


ATOM
5124
NH2
ARG
B
847
31.896
23.989
33.109
1.00
46.97


ATOM
5125
C
ARG
B
847
25.893
28.301
35.776
1.00
26.91


ATOM
5126
O
ARG
B
847
25.046
27.842
36.549
1.00
27.77


ATOM
5127
N
LYS
B
848
26.592
29.400
36.039
1.00
28.28


ATOM
5128
CA
LYS
B
848
26.384
30.155
37.271
1.00
27.83


ATOM
5129
CB
LYS
B
848
27.420
31.277
37.399
1.00
32.07


ATOM
5130
CG
LYS
B
848
28.831
30.798
37.731
1.00
32.23


ATOM
5131
CD
LYS
B
848
29.798
31.975
37.858
1.00
32.55


ATOM
5132
CE
LYS
B
848
31.198
31.513
38.248
1.00
32.52


ATOM
5133
NZ
LYS
B
848
32.179
32.642
38.241
1.00
33.18


ATOM
5134
C
LYS
B
848
24.973
30.740
37.257
1.00
28.34


ATOM
5135
O
LYS
B
848
24.291
30.758
38.282
1.00
28.54


ATOM
5136
N
ASN
B
849
24.525
31.213
36.097
1.00
24.72


ATOM
5137
CA
ASN
B
849
23.179
31.765
36.026
1.00
24.90


ATOM
5138
CB
ASN
B
849
22.975
32.558
34.734
1.00
24.86


ATOM
5139
CG
ASN
B
849
23.561
33.949
34.817
1.00
25.77


ATOM
5140
OD1
ASN
B
849
23.482
34.602
35.865
1.00
26.99


ATOM
5141
ND2
ASN
B
849
24.139
34.422
33.717
1.00
25.44


ATOM
5142
C
ASN
B
849
22.117
30.676
36.149
1.00
24.90


ATOM
5143
O
ASN
B
849
21.041
30.909
36.698
1.00
25.65


ATOM
5144
N
ARG
B
850
22.410
29.484
35.639
1.00
26.25


ATOM
5145
CA
ARG
B
850
21.452
28.392
35.738
1.00
26.05


ATOM
5146
CB
ARG
B
850
21.991
27.128
35.071
1.00
37.42


ATOM
5147
CG
ARG
B
850
21.057
25.945
35.237
1.00
37.84


ATOM
5148
CD
ARG
B
850
21.721
24.635
34.879
1.00
37.92


ATOM
5149
NE
ARG
B
850
20.875
23.509
35.261
1.00
38.86


ATOM
5150
CZ
ARG
B
850
19.666
23.286
34.761
1.00
38.08


ATOM
5151
NH1
ARG
B
850
19.168
24.114
33.854
1.00
39.16


ATOM
5152
NH2
ARG
B
850
18.950
22.247
35.172
1.00
37.88


ATOM
5153
C
ARG
B
850
21.209
28.112
37.217
1.00
26.02


ATOM
5154
O
ARG
B
850
20.087
27.861
37.646
1.00
25.93


ATOM
5155
N
GLN
B
851
22.290
28.148
37.986
1.00
29.35


ATOM
5156
CA
GLN
B
851
22.231
27.915
39.419
1.00
29.80


ATOM
5157
CB
GLN
B
851
23.641
28.042
40.006
1.00
57.33


ATOM
5158
CG
GLN
B
851
23.706
28.453
41.467
1.00
58.18


ATOM
5159
CD
GLN
B
851
25.130
28.731
41.920
1.00
58.63


ATOM
5160
OE1
GLN
B
851
25.355
29.314
42.983
1.00
58.50


ATOM
5161
NE2
GLN
B
851
26.101
28.309
41.114
1.00
58.38


ATOM
5162
C
GLN
B
851
21.289
28.920
40.068
1.00
29.02


ATOM
5163
O
GLN
B
851
20.413
28.550
40.852
1.00
29.23


ATOM
5164
N
LYS
B
852
21.464
30.192
39.724
1.00
28.14


ATOM
5165
CA
LYS
B
852
20.635
31.253
40.283
1.00
28.58


ATOM
5166
CB
LYS
B
852
21.150
32.616
39.815
1.00
42.42


ATOM
5167
CG
LYS
B
852
22.495
33.007
40.409
1.00
42.77


ATOM
5168
CD
LYS
B
852
22.371
33.238
41.906
1.00
42.79


ATOM
5169
CE
LYS
B
852
23.700
33.633
42.527
1.00
43.26


ATOM
5170
NZ
LYS
B
852
23.538
34.014
43.959
1.00
43.16


ATOM
5171
C
LYS
B
852
19.153
31.116
39.941
1.00
28.34


ATOM
5172
O
LYS
B
852
18.296
31.254
40.819
1.00
28.28


ATOM
5173
N
TRP
B
853
18.846
30.854
38.672
1.00
28.99


ATOM
5174
CA
TRP
B
853
17.454
30.709
38.252
1.00
29.17


ATOM
5175
CB
TRP
B
853
17.355
30.629
36.719
1.00
25.14


ATOM
5176
CG
TRP
B
853
17.517
31.963
36.032
1.00
23.87


ATOM
5177
CD2
TRP
B
853
16.695
33.121
36.210
1.00
23.86


ATOM
5178
CE2
TRP
B
853
17.216
34.136
35.377
1.00
23.34


ATOM
5179
CE3
TRP
B
853
15.567
33.400
36.995
1.00
24.36


ATOM
5180
CD1
TRP
B
853
18.475
32.311
35.121
1.00
24.42


ATOM
5181
NE1
TRP
B
853
18.302
33.614
34.725
1.00
24.36


ATOM
5182
CZ2
TRP
B
853
16.648
35.412
35.305
1.00
23.69


ATOM
5183
CZ3
TRP
B
853
15.002
34.669
36.924
1.00
23.64


ATOM
5184
CH2
TRP
B
853
15.545
35.657
36.085
1.00
24.37


ATOM
5185
C
TRP
B
853
16.783
29.488
38.882
1.00
29.77


ATOM
5186
O
TRP
B
853
15.632
29.561
39.309
1.00
29.78


ATOM
5187
N
GLN
B
854
17.504
28.371
38.946
1.00
29.55


ATOM
5188
CA
GLN
B
854
16.951
27.150
39.526
1.00
30.02


ATOM
5189
CB
GLN
B
854
17.937
25.993
39.358
1.00
34.76


ATOM
5190
CG
GLN
B
854
17.451
24.662
39.918
1.00
34.86


ATOM
5191
CD
GLN
B
854
16.141
24.207
39.305
1.00
35.26


ATOM
5192
OE1
GLN
B
854
15.984
24.197
38.085
1.00
35.00


ATOM
5193
NE2
GLN
B
854
15.195
23.815
40.151
1.00
35.46


ATOM
5194
C
GLN
B
854
16.611
27.328
41.005
1.00
30.99


ATOM
5195
O
GLN
B
854
15.559
26.884
41.462
1.00
30.12


ATOM
5196
N
ALA
B
855
17.501
27.976
41.748
1.00
37.27


ATOM
5197
CA
ALA
B
855
17.270
28.206
43.171
1.00
38.24


ATOM
5198
CB
ALA
B
855
18.445
28.958
43.777
1.00
27.97


ATOM
5199
C
ALA
B
855
15.976
28.988
43.380
1.00
38.50


ATOM
5200
O
ALA
B
855
15.308
28.840
44.404
1.00
38.79


ATOM
5201
N
LEU
B
856
15.622
29.817
42.404
1.00
35.46


ATOM
5202
CA
LEU
B
856
14.398
30.613
42.484
1.00
35.13


ATOM
5203
CB
LEU
B
856
14.507
31.858
41.597
1.00
30.40


ATOM
5204
CG
LEU
B
856
15.541
32.924
41.965
1.00
29.57


ATOM
5205
CD1
LEU
B
856
15.493
34.056
40.956
1.00
30.17


ATOM
5206
CD2
LEU
B
856
15.266
33.443
43.367
1.00
30.22


ATOM
5207
C
LEU
B
856
13.179
29.805
42.054
1.00
34.94


ATOM
5208
O
LEU
B
856
12.076
30.012
42.555
1.00
34.78


ATOM
5209
N
ALA
B
857
13.385
28.876
41.127
1.00
36.42


ATOM
5210
CA
ALA
B
857
12.299
28.055
40.609
1.00
36.87


ATOM
5211
CB
ALA
B
857
12.648
27.577
39.206
1.00
33.84


ATOM
5212
C
ALA
B
857
11.926
26.859
41.482
1.00
37.18


ATOM
5213
O
ALA
B
857
10.774
26.429
41.482
1.00
37.43


ATOM
5214
N
GLU
B
858
12.892
26.319
42.216
1.00
41.64


ATOM
5215
CA
GLU
B
858
12.634
25.161
43.069
1.00
42.85


ATOM
5216
CB
GLU
B
858
13.921
24.368
43.295
1.00
56.15


ATOM
5217
CG
GLU
B
858
15.034
25.173
43.930
1.00
56.44


ATOM
5218
CD
GLU
B
858
16.249
24.329
44.252
1.00
56.70


ATOM
5219
OE1
GLU
B
858
16.752
23.629
43.346
1.00
56.58


ATOM
5220
OE2
GLU
B
858
16.700
24.370
45.415
1.00
56.71


ATOM
5221
C
GLU
B
858
12.037
25.541
44.416
1.00
42.83


ATOM
5222
O
GLU
B
858
11.799
26.744
44.645
1.00
42.70


ATOM
5223
OXT
GLU
B
858
11.814
24.618
45.227
1.00
56.34


TER


ATOM
5225
N1
SIL
A
1
−13.215
−5.663
26.629
1.00
24.07


ATOM
5226
C18
SIL
A
1
−13.515
−5.899
27.857
1.00
24.70


ATOM
5227
C19
SIL
A
1
−14.726
−6.742
28.146
1.00
24.74


ATOM
5228
C43
SIL
A
1
−15.702
−6.365
29.114
1.00
25.67


ATOM
5229
O44
SIL
A
1
−15.506
−5.152
29.812
1.00
24.76


ATOM
5230
C45
SIL
A
1
−16.389
−4.626
30.824
1.00
25.28


ATOM
5231
C47
SIL
A
1
−15.790
−3.294
31.325
1.00
25.55


ATOM
5232
C41
SIL
A
1
−16.830
−7.231
29.333
1.00
25.19


ATOM
5233
C39
SIL
A
1
−16.955
−8.443
28.594
1.00
26.15


ATOM
5234
C22
SIL
A
1
−15.963
−8.801
27.633
1.00
25.41


ATOM
5235
S23
SIL
A
1
−16.074
−10.311
26.687
1.00
26.04


ATOM
5236
O38
SIL
A
1
−17.300
−10.973
27.102
1.00
25.69


ATOM
5237
O37
SIL
A
1
−14.845
−11.046
26.958
1.00
26.01


ATOM
5238
N24
SIL
A
1
−16.149
−10.048
25.039
1.00
26.05


ATOM
5239
C35
SIL
A
1
−17.168
−8.998
24.670
1.00
26.28


ATOM
5240
C33
SIL
A
1
−17.218
−8.772
23.126
1.00
26.30


ATOM
5241
N29
SIL
A
1
−15.854
−8.482
22.563
1.00
26.54


ATOM
5242
C31
SIL
A
1
−15.924
−8.260
21.089
1.00
26.02


ATOM
5243
C27
SIL
A
1
−14.887
−9.587
22.889
1.00
26.44


ATOM
5244
C25
SIL
A
1
−14.787
−9.831
24.428
1.00
25.61


ATOM
5245
C20
SIL
A
1
−14.868
−7.946
27.427
1.00
25.44


ATOM
5246
N17
SIL
A
1
−12.749
−5.402
28.877
1.00
24.74


ATOM
5247
C15
SIL
A
1
−11.635
−4.635
28.662
1.00
25.23


ATOM
5248
O16
SIL
A
1
−10.964
−4.202
29.580
1.00
24.95


ATOM
5249
C14
SIL
A
1
−11.266
−4.350
27.234
1.00
25.33


ATOM
5250
N11
SIL
A
1
−10.297
−3.680
26.649
1.00
24.67


ATOM
5251
C12
SIL
A
1
−9.206
−2.961
27.299
1.00
25.39


ATOM
5252
N10
SIL
A
1
−10.467
−3.764
25.300
1.00
25.03


ATOM
5253
C3
SIL
A
1
−11.495
−4.455
25.004
1.00
24.25


ATOM
5254
C4
SIL
A
1
−12.014
−4.783
23.619
1.00
25.73


ATOM
5255
C6
SIL
A
1
−12.905
−3.666
22.952
1.00
26.42


ATOM
5256
C8
SIL
A
1
−13.128
−2.379
23.800
1.00
25.69


ATOM
5257
C2
SIL
A
1
−12.059
−4.866
26.277
1.00
24.93


TER


ATOM
5259
N1
SIL
B
1
15.164
33.812
25.541
1.00
25.10


ATOM
5260
C18
SIL
B
1
14.895
33.565
26.769
1.00
24.27


ATOM
5261
C19
SIL
B
1
13.700
32.702
27.070
1.00
24.84


ATOM
5262
C43
SIL
B
1
12.729
33.045
28.058
1.00
24.56


ATOM
5263
O44
SIL
B
1
12.899
34.250
28.780
1.00
26.57


ATOM
5264
C45
SIL
B
1
12.006
34.722
29.810
1.00
25.69


ATOM
5265
C47
SIL
B
1
12.558
36.064
30.336
1.00
25.09


ATOM
5266
C41
SIL
B
1
11.622
32.157
28.280
1.00
25.59


ATOM
5267
C39
SIL
B
1
11.507
30.960
27.526
1.00
25.77


ATOM
5268
C22
SIL
B
1
12.487
30.633
26.544
1.00
25.79


ATOM
5269
S23
SIL
B
1
12.368
29.137
25.587
1.00
28.36


ATOM
5270
O38
SIL
B
1
11.164
28.457
26.018
1.00
26.14


ATOM
5271
O37
SIL
B
1
13.594
28.402
25.827
1.00
26.31


ATOM
5272
N24
SIL
B
1
12.244
29.398
23.942
1.00
26.57


ATOM
5273
C35
SIL
B
1
11.267
30.495
23.609
1.00
25.93


ATOM
5274
C33
SIL
B
1
11.168
30.716
22.066
1.00
26.61


ATOM
5275
N29
SIL
B
1
12.519
30.913
21.439
1.00
26.95


ATOM
5276
C31
SIL
B
1
12.402
31.132
19.969
1.00
25.72


ATOM
5277
C27
SIL
B
1
13.436
29.763
21.739
1.00
26.60


ATOM
5278
C25
SIL
B
1
13.583
29.525
23.276
1.00
26.54


ATOM
5279
C20
SIL
B
1
13.569
31.507
26.332
1.00
24.95


ATOM
5280
N17
SIL
B
1
15.678
34.063
27.775
1.00
25.01


ATOM
5281
C15
SIL
B
1
16.778
34.843
27.541
1.00
25.62


ATOM
5282
O16
SIL
B
1
17.471
35.279
28.442
1.00
25.56


ATOM
5283
C14
SIL
B
1
17.109
35.142
26.111
1.00
24.85


ATOM
5284
N11
SIL
B
1
18.054
35.828
25.516
1.00
24.72


ATOM
5285
C12
SIL
B
1
19.147
36.556
26.153
1.00
25.78


ATOM
5286
N10
SIL
B
1
17.863
35.755
24.172
1.00
25.21


ATOM
5287
C3
SIL
B
1
16.841
35.056
23.885
1.00
25.43


ATOM
5288
C4
SIL
B
1
16.304
34.734
22.500
1.00
25.15


ATOM
5289
C6
SIL
B
1
15.454
35.880
21.819
1.00
26.50


ATOM
5290
C8
SIL
B
1
15.284
37.187
22.646
1.00
26.25


ATOM
5291
C2
SIL
B
1
16.305
34.627
25.167
1.00
24.69


TER


ATOM
5293
ZN
ZN
A
864
−8.302
0.061
19.726
1.00
33.93


ATOM
5294
MG
MG
A
865
−10.882
−0.915
17.074
1.00
20.57


TER


ATOM
5296
ZN
ZN
B
864
19.969
39.499
18.508
1.00
25.29


ATOM
5297
MG
MG
B
865
0.014
0.254
−1.283
1.00
32.82


END
















TABLE 4










Atomic coordinates for PDE5* apo protein


Atom Number, Atom Type, Residue Type, Residue Number Cartesian


Coordinates X, Y, Z, Atom Occupancy (O), Temperature Factor (B)













X
Y
Z
O
B





















ATOM
1
CB
GLU
A
536
9.887
25.182
24.787
1.00
33.98


ATOM
2
CG
GLU
A
536
11.305
25.697
24.635
1.00
42.32


ATOM
3
CD
GLU
A
536
11.492
27.074
25.245
1.00
47.12


ATOM
4
OE1
GLU
A
536
11.290
27.223
26.470
1.00
54.45


ATOM
5
OE2
GLU
A
536
11.842
28.012
24.499
1.00
51.15


ATOM
6
C
GLU
A
536
7.942
25.044
26.327
1.00
37.22


ATOM
7
O
GLU
A
536
7.222
24.272
25.690
1.00
36.76


ATOM
8
N
GLU
A
536
9.991
23.667
26.752
1.00
36.93


ATOM
9
CA
GLU
A
536
9.456
24.961
26.239
1.00
37.47


ATOM
10
N
THR
A
537
7.463
25.990
27.125
1.00
37.34


ATOM
11
CA
THR
A
537
6.035
26.189
27.289
1.00
36.78


ATOM
12
CB
THR
A
537
5.750
27.235
28.387
1.00
43.61


ATOM
13
OG1
THR
A
537
6.425
28.457
28.069
1.00
45.23


ATOM
14
CG2
THR
A
537
6.241
26.731
29.739
1.00
34.90


ATOM
15
C
THR
A
537
5.452
26.660
25.957
1.00
35.15


ATOM
16
O
THR
A
537
4.239
26.661
25.764
1.00
34.30


ATOM
17
N
ARG
A
538
6.336
27.046
25.040
1.00
32.72


ATOM
18
CA
ARG
A
538
5.943
27.514
23.712
1.00
31.35


ATOM
19
CB
ARG
A
538
7.143
28.133
23.002
1.00
33.78


ATOM
20
CG
ARG
A
538
6.910
28.452
21.531
1.00
42.77


ATOM
21
CD
ARG
A
538
6.041
29.690
21.340
1.00
51.85


ATOM
22
NE
ARG
A
538
4.638
29.475
21.687
1.00
50.21


ATOM
23
CZ
ARG
A
538
3.715
30.433
21.672
1.00
49.57


ATOM
24
NH1
ARG
A
538
4.047
31.673
21.330
1.00
48.08


ATOM
25
NH2
ARG
A
538
2.458
30.154
21.992
1.00
49.14


ATOM
26
C
ARG
A
538
5.405
26.369
22.861
1.00
30.33


ATOM
27
O
ARG
A
538
4.381
26.501
22.187
1.00
28.72


ATOM
28
N
GLU
A
539
6.120
25.250
22.876
1.00
28.94


ATOM
29
CA
GLU
A
539
5.709
24.080
22.115
1.00
25.47


ATOM
30
CB
GLU
A
539
6.807
23.024
22.141
1.00
30.35


ATOM
31
CG
GLU
A
539
8.055
23.426
21.391
1.00
31.75


ATOM
32
CD
GLU
A
539
9.188
22.463
21.628
1.00
31.48


ATOM
33
OE1
GLU
A
539
9.689
22.410
22.771
1.00
46.55


ATOM
34
OE2
GLU
A
539
9.575
21.754
20.676
1.00
57.06


ATOM
35
C
GLU
A
539
4.437
23.511
22.718
1.00
23.49


ATOM
36
O
GLU
A
539
3.599
22.952
22.011
1.00
21.01


ATOM
37
N
LEU
A
540
4.299
23.653
24.032
1.00
22.37


ATOM
38
CA
LEU
A
540
3.114
23.159
24.713
1.00
22.10


ATOM
39
CB
LEU
A
540
3.302
23.223
26.231
1.00
19.44


ATOM
40
CG
LEU
A
540
2.098
22.763
27.059
1.00
22.04


ATOM
41
CD1
LEU
A
540
1.686
21.365
26.627
1.00
19.81


ATOM
42
CD2
LEU
A
540
2.441
22.783
28.539
1.00
38.12


ATOM
43
C
LEU
A
540
1.907
23.995
24.300
1.00
21.23


ATOM
44
O
LEU
A
540
0.844
23.461
23.990
1.00
19.37


ATOM
45
N
GLN
A
541
2.074
25.313
24.283
1.00
20.36


ATOM
46
CA
GLN
A
541
0.972
26.185
23.905
1.00
18.42


ATOM
47
CB
GLN
A
541
1.410
27.651
23.966
1.00
20.67


ATOM
48
CG
GLN
A
541
1.873
28.081
25.350
1.00
24.12


ATOM
49
CD
GLN
A
541
2.356
29.519
25.401
1.00
24.37


ATOM
50
OE1
GLN
A
541
3.047
29.986
24.497
1.00
17.86


ATOM
51
NE2
GLN
A
541
2.008
30.223
26.474
1.00
20.12


ATOM
52
C
GLN
A
541
0.477
25.833
22.505
1.00
17.74


ATOM
53
O
GLN
A
541
−0.726
25.799
22.254
1.00
19.08


ATOM
54
N
SER
A
542
1.404
25.552
21.596
1.00
15.82


ATOM
55
CA
SER
A
542
1.026
25.207
20.231
1.00
18.42


ATOM
56
CB
SER
A
542
2.263
25.179
19.329
1.00
20.91


ATOM
57
OG
SER
A
542
2.857
26.463
19.251
1.00
37.22


ATOM
58
C
SER
A
542
0.320
23.858
20.174
1.00
16.82


ATOM
59
O
SER
A
542
−0.710
23.709
19.520
1.00
17.71


ATOM
60
N
LEU
A
543
0.875
22.874
20.872
1.00
17.64


ATOM
61
CA
LEU
A
543
0.297
21.538
20.878
1.00
17.88


ATOM
62
CB
LEU
A
543
1.269
20.550
21.531
1.00
13.54


ATOM
63
CG
LEU
A
543
0.762
19.113
21.695
1.00
17.02


ATOM
64
CD1
LEU
A
543
0.501
18.504
20.329
1.00
14.15


ATOM
65
CD2
LEU
A
543
1.789
18.284
22.465
1.00
10.59


ATOM
66
C
LEU
A
543
−1.049
21.468
21.592
1.00
18.33


ATOM
67
O
LEU
A
543
−2.013
20.914
21.064
1.00
19.18


ATOM
68
N
ALA
A
544
−1.112
22.038
22.790
1.00
18.60


ATOM
69
CA
ALA
A
544
−2.332
22.003
23.588
1.00
19.09


ATOM
70
CB
ALA
A
544
−2.053
22.573
24.972
1.00
17.83


ATOM
71
C
ALA
A
544
−3.527
22.717
22.967
1.00
21.56


ATOM
72
O
ALA
A
544
−4.667
22.306
23.165
1.00
23.51


ATOM
73
N
ALA
A
545
−3.269
23.782
22.217
1.00
23.98


ATOM
74
CA
ALA
A
545
−4.348
24.547
21.599
1.00
24.34


ATOM
75
CB
ALA
A
545
−3.861
25.952
21.274
1.00
26.53


ATOM
76
C
ALA
A
545
−4.901
23.891
20.341
1.00
25.76


ATOM
77
O
ALA
A
545
−6.065
24.079
19.992
1.00
28.16


ATOM
78
N
ALA
A
546
−4.059
23.115
19.668
1.00
24.74


ATOM
79
CA
ALA
A
546
−4.441
22.443
18.430
1.00
24.22


ATOM
80
CB
ALA
A
546
−3.239
21.701
17.861
1.00
22.00


ATOM
81
C
ALA
A
546
−5.621
21.485
18.529
1.00
21.89


ATOM
82
O
ALA
A
546
−5.803
20.791
19.529
1.00
23.27


ATOM
83
N
VAL
A
547
−6.433
21.464
17.478
1.00
21.72


ATOM
84
CA
VAL
A
547
−7.560
20.548
17.418
1.00
21.65


ATOM
85
CB
VAL
A
547
−8.660
21.045
16.454
1.00
23.33


ATOM
86
CG1
VAL
A
547
−9.754
19.993
16.326
1.00
25.11


ATOM
87
CG2
VAL
A
547
−9.250
22.355
16.965
1.00
23.58


ATOM
88
C
VAL
A
547
−6.925
19.284
16.850
1.00
22.28


ATOM
89
O
VAL
A
547
−6.280
19.329
15.805
1.00
24.96


ATOM
90
N
VAL
A
548
−7.090
18.165
17.542
1.00
21.82


ATOM
91
CA
VAL
A
548
−6.498
16.909
17.098
1.00
19.25


ATOM
92
CB
VAL
A
548
−6.387
15.925
18.278
1.00
19.56


ATOM
93
CG1
VAL
A
548
−5.669
14.659
17.840
1.00
23.78


ATOM
94
CG2
VAL
A
548
−5.656
16.593
19.438
1.00
24.95


ATOM
95
C
VAL
A
548
−7.284
16.241
15.975
1.00
17.26


ATOM
96
O
VAL
A
548
−8.453
15.904
16.146
1.00
19.24


ATOM
97
N
PRO
A
549
−6.646
16.038
14.808
1.00
17.33


ATOM
98
CD
PRO
A
549
−5.293
16.478
14.431
1.00
18.64


ATOM
99
CA
PRO
A
549
−7.315
15.401
13.670
1.00
19.43


ATOM
100
CB
PRO
A
549
−6.245
15.425
12.575
1.00
17.30


ATOM
101
CG
PRO
A
549
−5.420
16.615
12.931
1.00
23.24


ATOM
102
C
PRO
A
549
−7.742
13.982
14.023
1.00
20.23


ATOM
103
O
PRO
A
549
−7.259
13.402
15.001
1.00
16.82


ATOM
104
N
SER
A
550
−8.645
13.431
13.220
1.00
17.57


ATOM
105
CA
SER
A
550
−9.153
12.081
13.432
1.00
20.68


ATOM
106
CB
SER
A
550
−10.343
11.822
12.512
1.00
17.19


ATOM
107
OG
SER
A
550
−9.934
11.861
11.153
1.00
18.60


ATOM
108
C
SER
A
550
−8.075
11.055
13.127
1.00
17.34


ATOM
109
O
SER
A
550
−7.096
11.357
12.443
1.00
16.71


ATOM
110
N
ALA
A
551
−8.257
9.841
13.637
1.00
18.46


ATOM
111
CA
ALA
A
551
−7.304
8.769
13.380
1.00
19.34


ATOM
112
CB
ALA
A
551
−7.706
7.507
14.143
1.00
17.06


ATOM
113
C
ALA
A
551
−7.322
8.502
11.879
1.00
18.62


ATOM
114
O
ALA
A
551
−6.284
8.262
11.261
1.00
20.73


ATOM
115
N
GLN
A
552
−8.518
8.554
11.300
1.00
19.78


ATOM
116
CA
GLN
A
552
−8.700
8.327
9.869
1.00
21.36


ATOM
117
CB
GLN
A
552
−10.175
8.528
9.502
1.00
23.40


ATOM
118
CG
GLN
A
552
−10.541
8.181
8.067
1.00
31.79


ATOM
119
CD
GLN
A
552
−12.026
8.358
7.797
1.00
35.80


ATOM
120
OE1
GLN
A
552
−12.864
7.675
8.390
1.00
46.36


ATOM
121
NE2
GLN
A
552
−12.358
9.283
6.902
1.00
49.03


ATOM
122
C
GLN
A
552
−7.820
9.301
9.086
1.00
21.35


ATOM
123
O
GLN
A
552
−7.040
8.897
8.219
1.00
21.48


ATOM
124
N
THR
A
553
−7.938
10.584
9.408
1.00
19.75


ATOM
125
CA
THR
A
553
−7.151
11.612
8.739
1.00
19.52


ATOM
126
CB
THR
A
553
−7.501
13.017
9.268
1.00
18.18


ATOM
127
OG1
THR
A
553
−8.871
13.318
8.971
1.00
19.96


ATOM
128
CG2
THR
A
553
−6.597
14.066
8.627
1.00
18.92


ATOM
129
C
THR
A
553
−5.654
11.396
8.926
1.00
20.00


ATOM
130
O
THR
A
553
−4.875
11.523
7.980
1.00
19.53


ATOM
131
N
LEU
A
554
−5.260
11.062
10.150
1.00
19.10


ATOM
132
CA
LEU
A
554
−3.855
10.853
10.474
1.00
20.03


ATOM
133
CB
LEU
A
554
−3.650
10.974
11.987
1.00
17.91


ATOM
134
CG
LEU
A
554
−4.091
12.323
12.571
1.00
18.40


ATOM
135
CD1
LEU
A
554
−3.972
12.316
14.082
1.00
16.11


ATOM
136
CD2
LEU
A
554
−3.237
13.436
11.977
1.00
23.68


ATOM
137
C
LEU
A
554
−3.303
9.521
9.970
1.00
19.88


ATOM
138
O
LEU
A
554
−2.093
9.304
9.994
1.00
19.74


ATOM
139
N
LYS
A
555
−4.198
8.637
9.533
1.00
17.37


ATOM
140
CA
LYS
A
555
−3.833
7.327
8.997
1.00
19.69


ATOM
141
CB
LYS
A
555
−3.032
7.523
7.708
1.00
26.45


ATOM
142
CG
LYS
A
555
−3.740
8.429
6.708
1.00
33.54


ATOM
143
CD
LYS
A
555
−2.829
8.837
5.565
1.00
36.95


ATOM
144
CE
LYS
A
555
−3.542
9.803
4.633
1.00
36.53


ATOM
145
NZ
LYS
A
555
−2.645
10.308
3.562
1.00
43.43


ATOM
146
C
LYS
A
555
−3.043
6.454
9.976
1.00
19.45


ATOM
147
O
LYS
A
555
−2.294
5.569
9.565
1.00
18.29


ATOM
148
N
ILE
A
556
−3.227
6.688
11.271
1.00
17.06


ATOM
149
CA
ILE
A
556
−2.501
5.917
12.273
1.00
16.83


ATOM
150
CB
ILE
A
556
−2.475
6.638
13.641
1.00
13.95


ATOM
151
CG2
ILE
A
556
−1.565
7.856
13.569
1.00
16.87


ATOM
152
CG1
ILE
A
556
−3.897
7.017
14.062
1.00
14.93


ATOM
153
CD1
ILE
A
556
−3.981
7.598
15.460
1.00
19.73


ATOM
154
C
ILE
A
556
−3.019
4.496
12.489
1.00
14.60


ATOM
155
O
ILE
A
556
−2.443
3.745
13.271
1.00
12.74


ATOM
156
N
THR
A
557
−4.099
4.125
11.806
1.00
14.27


ATOM
157
CA
THR
A
557
−4.653
2.776
11.938
1.00
15.05


ATOM
158
CB
THR
A
557
−6.187
2.772
11.699
1.00
21.22


ATOM
159
OG1
THR
A
557
−6.813
3.726
12.567
1.00
20.77


ATOM
160
CG2
THR
A
557
−6.773
1.398
11.982
1.00
21.26


ATOM
161
C
THR
A
557
−3.991
1.855
10.907
1.00
14.39


ATOM
162
O
THR
A
557
−4.131
0.631
10.955
1.00
16.89


ATOM
163
N
ASP
A
558
−3.257
2.456
9.979
1.00
14.56


ATOM
164
CA
ASP
A
558
−2.593
1.702
8.923
1.00
14.77


ATOM
165
CB
ASP
A
558
−2.374
2.613
7.713
1.00
20.77


ATOM
166
CG
ASP
A
558
−3.648
3.312
7.274
1.00
30.09


ATOM
167
OD1
ASP
A
558
−4.657
2.616
7.031
1.00
38.75


ATOM
168
OD2
ASP
A
558
−3.642
4.555
7.173
1.00
46.69


ATOM
169
C
ASP
A
558
−1.258
1.086
9.351
1.00
14.68


ATOM
170
O
ASP
A
558
−0.365
1.787
9.829
1.00
13.87


ATOM
171
N
PHE
A
559
−1.124
−0.227
9.175
1.00
13.82


ATOM
172
CA
PHE
A
559
0.119
−0.916
9.526
1.00
13.07


ATOM
173
CB
PHE
A
559
0.000
−2.427
9.283
1.00
14.41


ATOM
174
CG
PHE
A
559
−0.732
−3.175
10.366
1.00
18.21


ATOM
175
CD1
PHE
A
559
−0.289
−3.134
11.680
1.00
14.30


ATOM
176
CD2
PHE
A
559
−1.836
−3.960
10.060
1.00
16.61


ATOM
177
CE1
PHE
A
559
−0.931
−3.866
12.668
1.00
15.41


ATOM
178
CE2
PHE
A
559
−2.482
−4.692
11.043
1.00
15.41


ATOM
179
CZ
PHE
A
559
−2.031
−4.647
12.344
1.00
12.10


ATOM
180
C
PHE
A
559
1.277
−0.386
8.680
1.00
11.71


ATOM
181
O
PHE
A
559
2.431
−0.411
9.109
1.00
12.25


ATOM
182
N
SER
A
560
0.965
0.079
7.473
1.00
13.82


ATOM
183
CA
SER
A
560
1.979
0.597
6.555
1.00
13.86


ATOM
184
CB
SER
A
560
1.538
0.384
5.106
1.00
19.52


ATOM
185
OG
SER
A
560
1.411
−0.996
4.816
1.00
19.35


ATOM
186
C
SER
A
560
2.294
2.071
6.770
1.00
12.88


ATOM
187
O
SER
A
560
2.959
2.698
5.945
1.00
14.29


ATOM
188
N
PHE
A
561
1.815
2.608
7.886
1.00
12.82


ATOM
189
CA
PHE
A
561
2.021
4.009
8.261
1.00
13.63


ATOM
190
CB
PHE
A
561
1.567
4.207
9.713
1.00
14.59


ATOM
191
CG
PHE
A
561
1.835
5.583
10.258
1.00
12.08


ATOM
192
CD1
PHE
A
561
0.956
6.625
10.014
1.00
17.74


ATOM
193
CD2
PHE
A
561
2.967
5.829
11.022
1.00
10.31


ATOM
194
CE1
PHE
A
561
1.199
7.891
10.524
1.00
21.75


ATOM
195
CE2
PHE
A
561
3.220
7.093
11.537
1.00
13.27


ATOM
196
CZ
PHE
A
561
2.333
8.126
11.287
1.00
18.85


ATOM
197
C
PHE
A
561
3.466
4.498
8.125
1.00
14.38


ATOM
198
O
PHE
A
561
4.413
3.791
8.485
1.00
11.10


ATOM
199
N
SER
A
562
3.625
5.716
7.607
1.00
14.38


ATOM
200
CA
SER
A
562
4.939
6.334
7.453
1.00
13.72


ATOM
201
CB
SER
A
562
5.283
6.520
5.972
1.00
15.96


ATOM
202
OG
SER
A
562
6.542
7.159
5.835
1.00
23.25


ATOM
203
C
SER
A
562
4.940
7.695
8.159
1.00
12.53


ATOM
204
O
SER
A
562
4.009
8.490
8.014
1.00
12.55


ATOM
205
N
ASP
A
563
5.992
7.965
8.922
1.00
13.45


ATOM
206
CA
ASP
A
563
6.094
9.223
9.661
1.00
15.79


ATOM
207
CB
ASP
A
563
6.662
8.953
11.050
1.00
13.73


ATOM
208
CG
ASP
A
563
8.166
8.765
11.022
1.00
15.49


ATOM
209
OD1
ASP
A
563
8.895
9.680
11.465
1.00
18.81


ATOM
210
OD2
ASP
A
563
8.625
7.712
10.537
1.00
16.12


ATOM
211
C
ASP
A
563
7.009
10.232
8.974
1.00
16.63


ATOM
212
O
ASP
A
563
7.112
11.383
9.404
1.00
17.82


ATOM
213
N
PHE
A
564
7.673
9.796
7.911
1.00
16.51


ATOM
214
CA
PHE
A
564
8.633
10.635
7.205
1.00
18.23


ATOM
215
CB
PHE
A
564
9.207
9.871
6.011
1.00
15.87


ATOM
216
CG
PHE
A
564
10.446
10.494
5.438
1.00
26.61


ATOM
217
CD1
PHE
A
564
11.599
10.592
6.201
1.00
20.64


ATOM
218
CD2
PHE
A
564
10.458
10.991
4.144
1.00
27.32


ATOM
219
CE1
PHE
A
564
12.742
11.174
5.685
1.00
30.38


ATOM
220
CE2
PHE
A
564
11.599
11.574
3.622
1.00
33.45


ATOM
221
CZ
PHE
A
564
12.742
11.665
4.394
1.00
33.80


ATOM
222
C
PHE
A
564
8.157
12.010
6.740
1.00
18.52


ATOM
223
O
PHE
A
564
8.942
12.959
6.728
1.00
19.54


ATOM
224
N
GLU
A
565
6.885
12.122
6.369
1.00
16.14


ATOM
225
CA
GLU
A
565
6.340
13.391
5.890
1.00
19.03


ATOM
226
CB
GLU
A
565
5.277
13.142
4.813
1.00
18.54


ATOM
227
CG
GLU
A
565
5.708
12.238
3.668
1.00
33.46


ATOM
228
CD
GLU
A
565
6.004
10.818
4.117
1.00
40.92


ATOM
229
OE1
GLU
A
565
5.205
10.258
4.899
1.00
41.02


ATOM
230
OE2
GLU
A
565
7.032
10.259
3.680
1.00
50.71


ATOM
231
C
GLU
A
565
5.710
14.229
7.002
1.00
19.43


ATOM
232
O
GLU
A
565
5.158
15.301
6.740
1.00
20.33


ATOM
233
N
LEU
A
566
5.786
13.746
8.238
1.00
13.91


ATOM
234
CA
LEU
A
566
5.193
14.463
9.362
1.00
15.26


ATOM
235
CB
LEU
A
566
4.515
13.482
10.321
1.00
15.63


ATOM
236
CG
LEU
A
566
3.329
12.669
9.799
1.00
24.63


ATOM
237
CD1
LEU
A
566
2.864
11.698
10.881
1.00
23.72


ATOM
238
CD2
LEU
A
566
2.199
13.607
9.399
1.00
33.15


ATOM
239
C
LEU
A
566
6.187
15.306
10.147
1.00
14.43


ATOM
240
O
LEU
A
566
7.358
14.960
10.265
1.00
17.81


ATOM
241
N
SER
A
567
5.699
16.419
10.685
1.00
14.78


ATOM
242
CA
SER
A
567
6.517
17.317
11.486
1.00
14.98


ATOM
243
CB
SER
A
567
5.928
18.727
11.467
1.00
21.89


ATOM
244
OG
SER
A
567
4.679
18.752
12.144
1.00
17.63


ATOM
245
C
SER
A
567
6.492
16.797
12.922
1.00
13.89


ATOM
246
O
SER
A
567
5.654
15.963
13.268
1.00
13.82


ATOM
247
N
ASP
A
568
7.403
17.289
13.753
1.00
15.43


ATOM
248
CA
ASP
A
568
7.428
16.869
15.149
1.00
15.57


ATOM
249
CB
ASP
A
568
8.536
17.603
15.904
1.00
19.60


ATOM
250
CG
ASP
A
568
9.888
16.947
15.727
1.00
16.75


ATOM
251
OD1
ASP
A
568
9.989
16.021
14.899
1.00
19.05


ATOM
252
OD2
ASP
A
568
10.848
17.355
16.415
1.00
23.47


ATOM
253
C
ASP
A
568
6.076
17.145
15.805
1.00
16.52


ATOM
254
O
ASP
A
568
5.559
16.313
16.556
1.00
15.97


ATOM
255
N
LEU
A
569
5.505
18.311
15.516
1.00
15.09


ATOM
256
CA
LEU
A
569
4.213
18.683
16.076
1.00
15.08


ATOM
257
CB
LEU
A
569
3.815
20.093
15.620
1.00
16.05


ATOM
258
CG
LEU
A
569
2.385
20.516
15.974
1.00
23.47


ATOM
259
CD1
LEU
A
569
2.203
20.527
17.489
1.00
21.65


ATOM
260
CD2
LEU
A
569
2.103
21.896
15.398
1.00
27.54


ATOM
261
C
LEU
A
569
3.136
17.694
15.647
1.00
12.90


ATOM
262
O
LEU
A
569
2.279
17.308
16.441
1.00
16.26


ATOM
263
N
GLU
A
570
3.184
17.281
14.386
1.00
13.40


ATOM
264
CA
GLU
A
570
2.202
16.340
13.869
1.00
14.08


ATOM
265
CB
GLU
A
570
2.354
16.196
12.352
1.00
14.43


ATOM
266
CG
GLU
A
570
1.885
17.432
11.579
1.00
20.85


ATOM
267
CD
GLU
A
570
2.062
17.291
10.081
1.00
23.63


ATOM
268
OE1
GLU
A
570
3.218
17.158
9.632
1.00
21.68


ATOM
269
OE2
GLU
A
570
1.047
17.311
9.352
1.00
28.09


ATOM
270
C
GLU
A
570
2.309
14.978
14.547
1.00
14.43


ATOM
271
O
GLU
A
570
1.293
14.319
14.780
1.00
15.20


ATOM
272
N
THR
A
571
3.529
14.551
14.866
1.00
12.67


ATOM
273
CA
THR
A
571
3.694
13.259
15.538
1.00
12.83


ATOM
274
CB
THR
A
571
5.182
12.816
15.638
1.00
13.30


ATOM
275
OG1
THR
A
571
5.915
13.737
16.452
1.00
12.68


ATOM
276
CG2
THR
A
571
5.817
12.738
14.250
1.00
12.38


ATOM
277
C
THR
A
571
3.110
13.360
16.945
1.00
11.29


ATOM
278
O
THR
A
571
2.589
12.381
17.483
1.00
12.14


ATOM
279
N
ALA
A
572
3.202
14.548
17.538
1.00
12.42


ATOM
280
CA
ALA
A
572
2.659
14.780
18.869
1.00
11.84


ATOM
281
CB
ALA
A
572
3.090
16.142
19.388
1.00
12.18


ATOM
282
C
ALA
A
572
1.136
14.701
18.803
1.00
13.34


ATOM
283
O
ALA
A
572
0.500
14.128
19.683
1.00
11.72


ATOM
284
N
LEU
A
573
0.554
15.283
17.758
1.00
12.67


ATOM
285
CA
LEU
A
573
−0.894
15.244
17.583
1.00
13.98


ATOM
286
CB
LEU
A
573
−1.307
16.104
16.384
1.00
14.33


ATOM
287
CG
LEU
A
573
−1.135
17.619
16.544
1.00
14.55


ATOM
288
CD1
LEU
A
573
−1.445
18.310
15.224
1.00
21.57


ATOM
289
CD2
LEU
A
573
−2.061
18.125
17.647
1.00
20.27


ATOM
290
C
LEU
A
573
−1.338
13.795
17.366
1.00
15.26


ATOM
291
O
LEU
A
573
−2.394
13.378
17.853
1.00
15.01


ATOM
292
N
CYS
A
574
−0.534
13.030
16.632
1.00
13.44


ATOM
293
CA
CYS
A
574
−0.852
11.625
16.385
1.00
13.06


ATOM
294
CB
CYS
A
574
0.187
10.974
15.470
1.00
12.27


ATOM
295
SG
CYS
A
574
0.049
11.382
13.714
1.00
15.24


ATOM
296
C
CYS
A
574
−0.873
10.864
17.703
1.00
12.15


ATOM
297
O
CYS
A
574
−1.710
9.991
17.919
1.00
13.51


ATOM
298
N
THR
A
575
0.066
11.194
18.581
1.00
11.60


ATOM
299
CA
THR
A
575
0.158
10.532
19.872
1.00
12.28


ATOM
300
CB
THR
A
575
1.453
10.949
20.592
1.00
10.90


ATOM
301
OG1
THR
A
575
2.575
10.576
19.777
1.00
13.47


ATOM
302
CG2
THR
A
575
1.565
10.264
21.944
1.00
10.06


ATOM
303
C
THR
A
575
−1.068
10.841
20.726
1.00
11.74


ATOM
304
O
THR
A
575
−1.613
9.952
21.379
1.00
10.78


ATOM
305
N
ILE
A
576
−1.514
12.095
20.717
1.00
12.29


ATOM
306
CA
ILE
A
576
−2.700
12.453
21.484
1.00
11.92


ATOM
307
CB
ILE
A
576
−3.046
13.945
21.354
1.00
11.38


ATOM
308
CG2
ILE
A
576
−4.371
14.222
22.053
1.00
12.83


ATOM
309
CG1
ILE
A
576
−1.933
14.802
21.965
1.00
17.73


ATOM
310
CD1
ILE
A
576
−2.154
16.292
21.798
1.00
13.34


ATOM
311
C
ILE
A
576
−3.880
11.636
20.960
1.00
12.34


ATOM
312
O
ILE
A
576
−4.674
11.103
21.737
1.00
13.64


ATOM
313
N
ARG
A
577
−3.985
11.532
19.638
1.00
13.14


ATOM
314
CA
ARG
A
577
−5.071
10.772
19.032
1.00
13.22


ATOM
315
CB
ARG
A
577
−5.029
10.888
17.503
1.00
12.21


ATOM
316
CG
ARG
A
577
−6.113
10.084
16.795
1.00
12.42


ATOM
317
CD
ARG
A
577
−7.492
10.383
17.365
1.00
10.79


ATOM
318
NE
ARG
A
577
−7.912
11.757
17.111
1.00
18.46


ATOM
319
CZ
ARG
A
577
−9.015
12.304
17.612
1.00
16.47


ATOM
320
NH1
ARG
A
577
−9.319
13.564
17.325
1.00
24.31


ATOM
321
NH2
ARG
A
577
−9.809
11.596
18.405
1.00
18.21


ATOM
322
C
ARG
A
577
−5.029
9.304
19.455
1.00
12.45


ATOM
323
O
ARG
A
577
−6.069
8.675
19.625
1.00
11.98


ATOM
324
N
MET
A
578
−3.831
8.756
19.630
1.00
10.43


ATOM
325
CA
MET
A
578
−3.716
7.367
20.058
1.00
11.28


ATOM
326
CB
MET
A
578
−2.245
6.934
20.090
1.00
11.91


ATOM
327
CG
MET
A
578
−1.605
6.808
18.716
1.00
12.93


ATOM
328
SD
MET
A
578
0.134
6.324
18.830
1.00
16.07


ATOM
329
CE
MET
A
578
0.781
7.021
17.300
1.00
19.76


ATOM
330
C
MET
A
578
−4.332
7.191
21.445
1.00
12.18


ATOM
331
O
MET
A
578
−5.103
6.260
21.675
1.00
11.26


ATOM
332
N
PHE
A
579
−3.982
8.080
22.372
1.00
11.60


ATOM
333
CA
PHE
A
579
−4.521
8.004
23.725
1.00
11.60


ATOM
334
CB
PHE
A
579
−3.921
9.097
24.619
1.00
12.17


ATOM
335
CG
PHE
A
579
−2.584
8.748
25.201
1.00
9.68


ATOM
336
CD1
PHE
A
579
−1.415
9.023
24.510
1.00
13.42


ATOM
337
CD2
PHE
A
579
−2.497
8.148
26.450
1.00
12.49


ATOM
338
CE1
PHE
A
579
−0.178
8.709
25.054
1.00
10.87


ATOM
339
CE2
PHE
A
579
−1.264
7.829
27.000
1.00
13.01


ATOM
340
CZ
PHE
A
579
−0.103
8.113
26.301
1.00
12.83


ATOM
341
C
PHE
A
579
−6.040
8.170
23.708
1.00
12.84


ATOM
342
O
PHE
A
579
−6.765
7.429
24.367
1.00
12.73


ATOM
343
N
THR
A
580
−6.504
9.151
22.943
1.00
15.04


ATOM
344
CA
THR
A
580
−7.926
9.459
22.839
1.00
14.30


ATOM
345
CB
THR
A
580
−8.145
10.702
21.967
1.00
10.78


ATOM
346
OG1
THR
A
580
−7.344
11.780
22.469
1.00
18.08


ATOM
347
CG2
THR
A
580
−9.610
11.115
21.987
1.00
13.16


ATOM
348
C
THR
A
580
−8.772
8.327
22.273
1.00
14.34


ATOM
349
O
THR
A
580
−9.774
7.936
22.871
1.00
14.67


ATOM
350
N
ASP
A
581
−8.367
7.806
21.119
1.00
15.75


ATOM
351
CA
ASP
A
581
−9.106
6.731
20.466
1.00
14.61


ATOM
352
CB
ASP
A
581
−8.724
6.668
18.990
1.00
16.27


ATOM
353
CG
ASP
A
581
−9.398
7.757
18.181
1.00
20.38


ATOM
354
OD1
ASP
A
581
−9.762
8.797
18.776
1.00
15.70


ATOM
355
OD2
ASP
A
581
−9.560
7.580
16.958
1.00
17.57


ATOM
356
C
ASP
A
581
−8.970
5.365
21.123
1.00
15.19


ATOM
357
O
ASP
A
581
−9.627
4.402
20.719
1.00
14.62


ATOM
358
N
LEU
A
582
−8.110
5.275
22.130
1.00
13.55


ATOM
359
CA
LEU
A
582
−7.957
4.032
22.867
1.00
14.36


ATOM
360
CB
LEU
A
582
−6.484
3.739
23.156
1.00
16.24


ATOM
361
CG
LEU
A
582
−5.770
3.024
22.006
1.00
14.56


ATOM
362
CD1
LEU
A
582
−4.272
2.968
22.250
1.00
12.82


ATOM
363
CD2
LEU
A
582
−6.351
1.625
21.865
1.00
12.05


ATOM
364
C
LEU
A
582
−8.739
4.189
24.168
1.00
17.31


ATOM
365
O
LEU
A
582
−8.617
3.378
25.081
1.00
17.82


ATOM
366
N
ASN
A
583
−9.533
5.255
24.246
1.00
17.93


ATOM
367
CA
ASN
A
583
−10.361
5.500
25.420
1.00
21.01


ATOM
368
CB
ASN
A
583
−11.405
4.377
25.525
1.00
22.07


ATOM
369
CG
ASN
A
583
−12.368
4.564
26.682
1.00
34.95


ATOM
370
OD1
ASN
A
583
−12.921
5.645
26.879
1.00
34.93


ATOM
371
ND2
ASN
A
583
−12.589
3.496
27.444
1.00
39.94


ATOM
372
C
ASN
A
583
−9.516
5.575
26.693
1.00
23.16


ATOM
373
O
ASN
A
583
−9.866
4.978
27.713
1.00
27.41


ATOM
374
N
LEU
A
584
−8.406
6.313
26.634
1.00
18.24


ATOM
375
CA
LEU
A
584
−7.517
6.446
27.791
1.00
18.39


ATOM
376
CB
LEU
A
584
−6.060
6.188
27.379
1.00
13.74


ATOM
377
CG
LEU
A
584
−5.713
4.823
26.778
1.00
13.61


ATOM
378
CD1
LEU
A
584
−4.226
4.789
26.412
1.00
16.18


ATOM
379
CD2
LEU
A
584
−6.050
3.726
27.769
1.00
15.78


ATOM
380
C
LEU
A
584
−7.591
7.807
28.486
1.00
18.85


ATOM
381
O
LEU
A
584
−7.377
7.904
29.695
1.00
18.54


ATOM
382
N
VAL
A
585
−7.890
8.853
27.721
1.00
18.53


ATOM
383
CA
VAL
A
585
−7.956
10.211
28.258
1.00
20.90


ATOM
384
CB
VAL
A
585
−8.157
11.234
27.123
1.00
25.63


ATOM
385
CG1
VAL
A
585
−8.083
12.648
27.672
1.00
26.57


ATOM
386
CG2
VAL
A
585
−7.102
11.024
26.054
1.00
26.78


ATOM
387
C
VAL
A
585
−9.049
10.416
29.307
1.00
21.72


ATOM
388
O
VAL
A
585
−8.771
10.839
30.429
1.00
21.94


ATOM
389
N
GLN
A
586
−10.291
10.118
28.945
1.00
22.79


ATOM
390
CA
GLN
A
586
−11.394
10.290
29.881
1.00
25.11


ATOM
391
CB
GLN
A
586
−12.728
10.306
29.131
1.00
34.29


ATOM
392
CG
GLN
A
586
−13.719
11.317
29.678
1.00
39.65


ATOM
393
CD
GLN
A
586
−13.155
12.725
29.663
1.00
50.17


ATOM
394
OE1
GLN
A
586
−12.715
13.218
28.622
1.00
52.20


ATOM
395
NE2
GLN
A
586
−13.160
13.380
30.820
1.00
48.68


ATOM
396
C
GLN
A
586
−11.402
9.172
30.914
1.00
22.36


ATOM
397
O
GLN
A
586
−11.587
9.413
32.108
1.00
23.81


ATOM
398
N
ASN
A
587
−11.195
7.948
30.441
1.00
22.47


ATOM
399
CA
ASN
A
587
−11.181
6.769
31.298
1.00
19.07


ATOM
400
CB
ASN
A
587
−10.651
5.565
30.507
1.00
21.06


ATOM
401
CG
ASN
A
587
−10.944
4.236
31.179
1.00
29.14


ATOM
402
OD1
ASN
A
587
−11.098
4.157
32.397
1.00
21.26


ATOM
403
ND2
ASN
A
587
−11.002
3.174
30.382
1.00
33.44


ATOM
404
C
ASN
A
587
−10.319
6.981
32.542
1.00
20.86


ATOM
405
O
ASN
A
587
−10.727
6.646
33.656
1.00
19.43


ATOM
406
N
PHE
A
588
−9.134
7.553
32.357
1.00
18.57


ATOM
407
CA
PHE
A
588
−8.227
7.753
33.480
1.00
18.65


ATOM
408
CB
PHE
A
588
−6.880
7.109
33.145
1.00
13.88


ATOM
409
CG
PHE
A
588
−6.976
5.624
32.948
1.00
14.75


ATOM
410
CD1
PHE
A
588
−7.272
4.791
34.022
1.00
13.58


ATOM
411
CD2
PHE
A
588
−6.860
5.065
31.686
1.00
12.05


ATOM
412
CE1
PHE
A
588
−7.456
3.431
33.837
1.00
13.16


ATOM
413
CE2
PHE
A
588
−7.044
3.704
31.496
1.00
10.45


ATOM
414
CZ
PHE
A
588
−7.344
2.888
32.576
1.00
16.21


ATOM
415
C
PHE
A
588
−8.063
9.190
33.966
1.00
20.57


ATOM
416
O
PHE
A
588
−7.072
9.538
34.611
1.00
18.90


ATOM
417
N
GLN
A
589
−9.052
10.020
33.662
1.00
21.41


ATOM
418
CA
GLN
A
589
−9.057
11.410
34.110
1.00
23.36


ATOM
419
CB
GLN
A
589
−9.213
11.449
35.634
1.00
28.73


ATOM
420
CG
GLN
A
589
−10.311
10.551
36.194
1.00
40.43


ATOM
421
CD
GLN
A
589
−11.701
11.003
35.797
1.00
42.17


ATOM
422
OE1
GLN
A
589
−12.058
12.167
35.971
1.00
38.12


ATOM
423
NE2
GLN
A
589
−12.498
10.080
35.270
1.00
47.35


ATOM
424
C
GLN
A
589
−7.805
12.201
33.725
1.00
20.90


ATOM
425
O
GLN
A
589
−7.282
12.972
34.531
1.00
21.16


ATOM
426
N
MET
A
590
−7.321
12.019
32.502
1.00
22.12


ATOM
427
CA
MET
A
590
−6.133
12.745
32.069
1.00
21.73


ATOM
428
CB
MET
A
590
−5.463
12.035
30.893
1.00
22.93


ATOM
429
CG
MET
A
590
−4.751
10.752
31.257
1.00
24.06


ATOM
430
SD
MET
A
590
−3.865
10.087
29.838
1.00
19.72


ATOM
431
CE
MET
A
590
−3.631
8.404
30.357
1.00
17.35


ATOM
432
C
MET
A
590
−6.455
14.172
31.654
1.00
22.68


ATOM
433
O
MET
A
590
−7.295
14.398
30.784
1.00
23.69


ATOM
434
N
LYS
A
591
−5.792
15.138
32.278
1.00
20.35


ATOM
435
CA
LYS
A
591
−6.013
16.530
31.919
1.00
20.85


ATOM
436
CB
LYS
A
591
−5.554
17.460
33.045
1.00
22.95


ATOM
437
CG
LYS
A
591
−6.472
17.422
34.262
1.00
28.61


ATOM
438
CD
LYS
A
591
−6.065
18.438
35.315
1.00
37.59


ATOM
439
CE
LYS
A
591
−7.106
18.527
36.423
1.00
42.92


ATOM
440
NZ
LYS
A
591
−8.417
19.026
35.915
1.00
51.43


ATOM
441
C
LYS
A
591
−5.235
16.800
30.636
1.00
20.72


ATOM
442
O
LYS
A
591
−4.048
16.486
30.537
1.00
21.29


ATOM
443
N
HIS
A
592
−5.920
17.375
29.654
1.00
20.84


ATOM
444
CA
HIS
A
592
−5.333
17.670
28.351
1.00
21.11


ATOM
445
CB
HIS
A
592
−6.273
18.577
27.553
1.00
21.39


ATOM
446
CG
HIS
A
592
−5.884
18.737
26.125
1.00
18.05


ATOM
447
CD2
HIS
A
592
−5.427
19.798
25.424
1.00
24.75


ATOM
448
ND1
HIS
A
592
−5.926
17.685
25.213
1.00
22.74


ATOM
449
CE1
HIS
A
592
−5.518
18.102
24.044
1.00
29.20


ATOM
450
NE2
HIS
A
592
−5.204
19.393
24.135
1.00
27.94


ATOM
451
C
HIS
A
592
−3.937
18.295
28.377
1.00
20.49


ATOM
452
O
HIS
A
592
−3.034
17.848
27.661
1.00
19.49


ATOM
453
N
GLU
A
593
−3.765
19.338
29.184
1.00
19.12


ATOM
454
CA
GLU
A
593
−2.481
20.019
29.279
1.00
18.26


ATOM
455
CB
GLU
A
593
−2.592
21.243
30.192
1.00
23.02


ATOM
456
CG
GLU
A
593
−1.267
21.957
30.416
1.00
32.52


ATOM
457
CD
GLU
A
593
−1.422
23.296
31.116
1.00
44.01


ATOM
458
OE1
GLU
A
593
−2.062
24.200
30.535
1.00
41.08


ATOM
459
OE2
GLU
A
593
−0.901
23.446
32.244
1.00
45.85


ATOM
460
C
GLU
A
593
−1.381
19.099
29.793
1.00
18.42


ATOM
461
O
GLU
A
593
−0.230
19.195
29.365
1.00
16.87


ATOM
462
N
VAL
A
594
−1.738
18.209
30.710
1.00
18.22


ATOM
463
CA
VAL
A
594
−0.770
17.275
31.277
1.00
17.13


ATOM
464
CB
VAL
A
594
−1.372
16.506
32.465
1.00
16.16


ATOM
465
CG1
VAL
A
594
−0.314
15.605
33.085
1.00
20.37


ATOM
466
CG2
VAL
A
594
−1.911
17.481
33.491
1.00
22.54


ATOM
467
C
VAL
A
594
−0.299
16.263
30.235
1.00
15.25


ATOM
468
O
VAL
A
594
0.902
16.005
30.101
1.00
16.26


ATOM
469
N
LEU
A
595
−1.246
15.681
29.504
1.00
13.83


ATOM
470
CA
LEU
A
595
−0.897
14.705
28.478
1.00
14.01


ATOM
471
CB
LEU
A
595
−2.163
14.147
27.818
1.00
9.50


ATOM
472
CG
LEU
A
595
−1.969
13.167
26.653
1.00
18.45


ATOM
473
CD1
LEU
A
595
−1.068
12.014
27.076
1.00
12.38


ATOM
474
CD2
LEU
A
595
−3.318
12.643
26.201
1.00
14.12


ATOM
475
C
LEU
A
595
−0.002
15.372
27.438
1.00
13.61


ATOM
476
O
LEU
A
595
1.004
14.804
27.010
1.00
13.98


ATOM
477
N
CYS
A
596
−0.358
16.588
27.037
1.00
14.70


ATOM
478
CA
CYS
A
596
0.448
17.303
26.058
1.00
12.24


ATOM
479
CB
CYS
A
596
−0.191
18.649
25.709
1.00
15.21


ATOM
480
SG
CYS
A
596
−1.702
18.507
24.749
1.00
17.45


ATOM
481
C
CYS
A
596
1.861
17.534
26.586
1.00
12.70


ATOM
482
O
CYS
A
596
2.839
17.327
25.868
1.00
11.06


ATOM
483
N
ARG
A
597
1.970
17.959
27.841
1.00
11.36


ATOM
484
CA
ARG
A
597
3.283
18.211
28.420
1.00
11.51


ATOM
485
CB
ARG
A
597
3.141
18.836
29.815
1.00
14.74


ATOM
486
CG
ARG
A
597
4.463
19.343
30.388
1.00
15.86


ATOM
487
CD
ARG
A
597
4.294
20.067
31.727
1.00
20.22


ATOM
488
NE
ARG
A
597
3.565
21.332
31.614
1.00
21.93


ATOM
489
CZ
ARG
A
597
2.279
21.493
31.916
1.00
27.00


ATOM
490
NH1
ARG
A
597
1.560
20.469
32.357
1.00
22.77


ATOM
491
NH2
ARG
A
597
1.708
22.683
31.782
1.00
30.27


ATOM
492
C
ARG
A
597
4.100
16.919
28.494
1.00
11.80


ATOM
493
O
ARG
A
597
5.287
16.909
28.162
1.00
10.48


ATOM
494
N
TRP
A
598
3.454
15.830
28.905
1.00
11.97


ATOM
495
CA
TRP
A
598
4.112
14.530
29.022
1.00
9.62


ATOM
496
CB
TRP
A
598
3.125
13.488
29.556
1.00
11.57


ATOM
497
CG
TRP
A
598
3.717
12.110
29.702
1.00
10.65


ATOM
498
CD2
TRP
A
598
3.609
11.028
28.771
1.00
9.66


ATOM
499
CE2
TRP
A
598
4.350
9.948
29.298
1.00
8.24


ATOM
500
CE3
TRP
A
598
2.964
10.866
27.541
1.00
11.87


ATOM
501
CD1
TRP
A
598
4.494
11.656
30.728
1.00
9.74


ATOM
502
NE1
TRP
A
598
4.878
10.359
30.492
1.00
11.42


ATOM
503
CZ2
TRP
A
598
4.459
8.720
28.635
1.00
7.38


ATOM
504
CZ3
TRP
A
598
3.075
9.646
26.886
1.00
9.43


ATOM
505
CH2
TRP
A
598
3.818
8.593
27.434
1.00
10.02


ATOM
506
C
TRP
A
598
4.656
14.064
27.670
1.00
12.66


ATOM
507
O
TRP
A
598
5.804
13.617
27.568
1.00
11.33


ATOM
508
N
ILE
A
599
3.823
14.160
26.637
1.00
9.84


ATOM
509
CA
ILE
A
599
4.232
13.748
25.298
1.00
12.03


ATOM
510
CB
ILE
A
599
3.101
13.974
24.270
1.00
11.30


ATOM
511
CG2
ILE
A
599
3.648
13.807
22.856
1.00
13.41


ATOM
512
CG1
ILE
A
599
1.953
13.000
24.546
1.00
13.16


ATOM
513
CD1
ILE
A
599
0.732
13.218
23.668
1.00
13.06


ATOM
514
C
ILE
A
599
5.460
14.533
24.855
1.00
14.21


ATOM
515
O
ILE
A
599
6.414
13.969
24.308
1.00
11.47


ATOM
516
N
LEU
A
600
5.439
15.839
25.094
1.00
14.33


ATOM
517
CA
LEU
A
600
6.566
16.670
24.707
1.00
13.61


ATOM
518
CB
LEU
A
600
6.214
18.151
24.882
1.00
13.53


ATOM
519
CG
LEU
A
600
5.073
18.621
23.971
1.00
12.80


ATOM
520
CD1
LEU
A
600
4.652
20.036
24.336
1.00
15.66


ATOM
521
CD2
LEU
A
600
5.518
18.557
22.520
1.00
13.09


ATOM
522
C
LEU
A
600
7.800
16.297
25.523
1.00
10.78


ATOM
523
O
LEU
A
600
8.917
16.324
25.011
1.00
10.47


ATOM
524
N
SER
A
601
7.601
15.925
26.788
1.00
10.50


ATOM
525
CA
SER
A
601
8.734
15.540
27.624
1.00
8.54


ATOM
526
CB
SER
A
601
8.303
15.398
29.085
1.00
9.00


ATOM
527
OG
SER
A
601
8.036
16.678
29.634
1.00
9.87


ATOM
528
C
SER
A
601
9.342
14.239
27.129
1.00
9.99


ATOM
529
O
SER
A
601
10.563
14.082
27.104
1.00
10.43


ATOM
530
N
VAL
A
602
8.487
13.300
26.739
1.00
10.77


ATOM
531
CA
VAL
A
602
8.968
12.024
26.223
1.00
10.98


ATOM
532
CB
VAL
A
602
7.791
11.081
25.874
1.00
12.52


ATOM
533
CG1
VAL
A
602
8.303
9.856
25.138
1.00
9.22


ATOM
534
CG2
VAL
A
602
7.068
10.658
27.152
1.00
11.71


ATOM
535
C
VAL
A
602
9.794
12.290
24.967
1.00
12.57


ATOM
536
O
VAL
A
602
10.935
11.848
24.855
1.00
11.99


ATOM
537
N
LYS
A
603
9.220
13.043
24.034
1.00
12.97


ATOM
538
CA
LYS
A
603
9.906
13.363
22.792
1.00
11.73


ATOM
539
CB
LYS
A
603
9.025
14.268
21.928
1.00
14.00


ATOM
540
CG
LYS
A
603
9.666
14.688
20.620
1.00
14.56


ATOM
541
CD
LYS
A
603
8.656
15.317
19.686
1.00
16.82


ATOM
542
CE
LYS
A
603
8.088
16.603
20.262
1.00
24.97


ATOM
543
NZ
LYS
A
603
7.169
17.256
19.300
1.00
39.23


ATOM
544
C
LYS
A
603
11.256
14.035
23.042
1.00
11.50


ATOM
545
O
LYS
A
603
12.252
13.694
22.414
1.00
14.04


ATOM
546
N
LYS
A
604
11.279
14.985
23.968
1.00
11.12


ATOM
547
CA
LYS
A
604
12.501
15.714
24.293
1.00
13.84


ATOM
548
CB
LYS
A
604
12.181
16.849
25.274
1.00
16.59


ATOM
549
CG
LYS
A
604
13.403
17.589
25.788
1.00
18.98


ATOM
550
CD
LYS
A
604
13.016
18.673
26.784
1.00
25.53


ATOM
551
CE
LYS
A
604
14.251
19.335
27.391
1.00
31.51


ATOM
552
NZ
LYS
A
604
13.893
20.351
28.424
1.00
29.80


ATOM
553
C
LYS
A
604
13.582
14.824
24.890
1.00
12.98


ATOM
554
O
LYS
A
604
14.776
15.073
24.710
1.00
13.10


ATOM
555
N
ASN
A
605
13.173
13.773
25.587
1.00
12.62


ATOM
556
CA
ASN
A
605
14.146
12.901
26.220
1.00
13.04


ATOM
557
CB
ASN
A
605
13.555
12.336
27.507
1.00
13.13


ATOM
558
CG
ASN
A
605
13.579
13.356
28.638
1.00
32.58


ATOM
559
OD1
ASN
A
605
14.638
13.650
29.197
1.00
25.76


ATOM
560
ND2
ASN
A
605
12.418
13.918
28.962
1.00
30.95


ATOM
561
C
ASN
A
605
14.757
11.809
25.352
1.00
15.12


ATOM
562
O
ASN
A
605
15.342
10.848
25.858
1.00
18.48


ATOM
563
N
TYR
A
606
14.612
11.961
24.042
1.00
10.60


ATOM
564
CA
TYR
A
606
15.233
11.051
23.093
1.00
10.45


ATOM
565
CB
TYR
A
606
14.254
10.645
21.982
1.00
10.34


ATOM
566
CG
TYR
A
606
13.420
9.444
22.358
1.00
11.02


ATOM
567
CD1
TYR
A
606
13.950
8.156
22.297
1.00
8.31


ATOM
568
CE1
TYR
A
606
13.222
7.061
22.752
1.00
8.28


ATOM
569
CD2
TYR
A
606
12.139
9.601
22.874
1.00
12.47


ATOM
570
CE2
TYR
A
606
11.410
8.516
23.335
1.00
15.05


ATOM
571
CZ
TYR
A
606
11.955
7.252
23.275
1.00
15.46


ATOM
572
OH
TYR
A
606
11.227
6.188
23.773
1.00
12.36


ATOM
573
C
TYR
A
606
16.362
11.908
22.539
1.00
11.41


ATOM
574
O
TYR
A
606
16.216
13.129
22.428
1.00
14.91


ATOM
575
N
ARG
A
607
17.499
11.293
22.234
1.00
11.41


ATOM
576
CA
ARG
A
607
18.627
12.042
21.700
1.00
10.90


ATOM
577
CB
ARG
A
607
19.933
11.322
22.034
1.00
12.68


ATOM
578
CG
ARG
A
607
20.078
11.019
23.520
1.00
10.36


ATOM
579
CD
ARG
A
607
21.460
10.489
23.870
1.00
13.25


ATOM
580
NE
ARG
A
607
21.492
9.929
25.221
1.00
9.55


ATOM
581
CZ
ARG
A
607
22.601
9.556
25.854
1.00
18.33


ATOM
582
NH1
ARG
A
607
23.781
9.686
25.262
1.00
13.50


ATOM
583
NH2
ARG
A
607
22.530
9.045
27.077
1.00
17.68


ATOM
584
C
ARG
A
607
18.425
12.150
20.194
1.00
10.45


ATOM
585
O
ARG
A
607
18.616
11.182
19.458
1.00
12.53


ATOM
586
N
LYS
A
608
18.052
13.340
19.738
1.00
11.88


ATOM
587
CA
LYS
A
608
17.755
13.555
18.323
1.00
13.33


ATOM
588
CB
LYS
A
608
17.273
14.993
18.104
1.00
18.33


ATOM
589
CG
LYS
A
608
18.226
16.064
18.574
1.00
34.41


ATOM
590
CD
LYS
A
608
17.558
17.429
18.538
1.00
39.16


ATOM
591
CE
LYS
A
608
18.430
18.485
19.193
1.00
44.56


ATOM
592
NZ
LYS
A
608
19.755
18.595
18.525
1.00
49.34


ATOM
593
C
LYS
A
608
18.837
13.220
17.311
1.00
13.41


ATOM
594
O
LYS
A
608
18.527
12.904
16.164
1.00
14.71


ATOM
595
N
ASN
A
609
20.098
13.272
17.724
1.00
12.65


ATOM
596
CA
ASN
A
609
21.185
12.977
16.804
1.00
15.37


ATOM
597
CB
ASN
A
609
22.383
13.872
17.121
1.00
19.55


ATOM
598
CG
ASN
A
609
22.059
15.347
16.952
1.00
21.29


ATOM
599
OD1
ASN
A
609
21.630
15.779
15.882
1.00
28.72


ATOM
600
ND2
ASN
A
609
22.261
16.126
18.009
1.00
36.76


ATOM
601
C
ASN
A
609
21.593
11.507
16.743
1.00
14.47


ATOM
602
O
ASN
A
609
22.486
11.135
15.981
1.00
15.29


ATOM
603
N
VAL
A
610
20.955
10.670
17.557
1.00
11.89


ATOM
604
CA
VAL
A
610
21.221
9.233
17.511
1.00
11.43


ATOM
605
CB
VAL
A
610
20.696
8.531
18.777
1.00
11.38


ATOM
606
CG1
VAL
A
610
20.649
7.019
18.571
1.00
10.56


ATOM
607
CG2
VAL
A
610
21.608
8.882
19.955
1.00
10.47


ATOM
608
C
VAL
A
610
20.432
8.809
16.272
1.00
12.97


ATOM
609
O
VAL
A
610
19.221
9.025
16.198
1.00
11.59


ATOM
610
N
ALA
A
611
21.131
8.223
15.302
1.00
11.37


ATOM
611
CA
ALA
A
611
20.554
7.833
14.018
1.00
12.77


ATOM
612
CB
ALA
A
611
21.579
7.021
13.223
1.00
12.83


ATOM
613
C
ALA
A
611
19.208
7.117
13.981
1.00
12.88


ATOM
614
O
ALA
A
611
18.305
7.522
13.247
1.00
14.79


ATOM
615
N
TYR
A
612
19.071
6.050
14.756
1.00
12.18


ATOM
616
CA
TYR
A
612
17.830
5.288
14.743
1.00
10.69


ATOM
617
CB
TYR
A
612
18.147
3.824
14.408
1.00
13.15


ATOM
618
CG
TYR
A
612
16.968
2.877
14.509
1.00
12.63


ATOM
619
CD1
TYR
A
612
15.832
3.054
13.729
1.00
19.45


ATOM
620
CE1
TYR
A
612
14.752
2.185
13.833
1.00
24.00


ATOM
621
CD2
TYR
A
612
16.996
1.805
15.392
1.00
13.47


ATOM
622
CE2
TYR
A
612
15.930
0.938
15.503
1.00
24.95


ATOM
623
CZ
TYR
A
612
14.812
1.129
14.722
1.00
24.27


ATOM
624
OH
TYR
A
612
13.761
0.245
14.831
1.00
25.94


ATOM
625
C
TYR
A
612
17.017
5.371
16.028
1.00
11.05


ATOM
626
O
TYR
A
612
15.812
5.632
15.989
1.00
9.25


ATOM
627
N
HIS
A
613
17.667
5.159
17.166
1.00
10.71


ATOM
628
CA
HIS
A
613
16.951
5.199
18.432
1.00
9.46


ATOM
629
CB
HIS
A
613
17.694
4.391
19.499
1.00
12.29


ATOM
630
CG
HIS
A
613
17.706
2.923
19.232
1.00
13.22


ATOM
631
CD2
HIS
A
613
16.742
1.983
19.364
1.00
13.53


ATOM
632
ND1
HIS
A
613
18.811
2.262
18.726
1.00
8.83


ATOM
633
CE1
HIS
A
613
18.523
0.989
18.562
1.00
12.86


ATOM
634
NE2
HIS
A
613
17.268
0.789
18.942
1.00
16.65


ATOM
635
C
HIS
A
613
16.686
6.606
18.936
1.00
11.81


ATOM
636
O
HIS
A
613
17.226
7.023
19.957
1.00
11.26


ATOM
637
N
ASN
A
614
15.859
7.333
18.192
1.00
12.20


ATOM
638
CA
ASN
A
614
15.459
8.685
18.556
1.00
11.65


ATOM
639
CB
ASN
A
614
15.955
9.702
17.516
1.00
19.08


ATOM
640
CG
ASN
A
614
15.631
9.295
16.090
1.00
17.63


ATOM
641
OD1
ASN
A
614
16.529
9.151
15.253
1.00
16.40


ATOM
642
ND2
ASN
A
614
14.349
9.115
15.802
1.00
11.39


ATOM
643
C
ASN
A
614
13.933
8.690
18.644
1.00
11.53


ATOM
644
O
ASN
A
614
13.298
7.647
18.493
1.00
9.32


ATOM
645
N
TRP
A
615
13.342
9.850
18.890
1.00
8.95


ATOM
646
CA
TRP
A
615
11.893
9.929
19.015
1.00
9.02


ATOM
647
CB
TRP
A
615
11.457
11.397
19.127
1.00
9.00


ATOM
648
CG
TRP
A
615
10.002
11.638
18.809
1.00
8.75


ATOM
649
CD2
TRP
A
615
8.860
11.228
19.581
1.00
10.58


ATOM
650
CE2
TRP
A
615
7.709
11.655
18.883
1.00
12.68


ATOM
651
CE3
TRP
A
615
8.698
10.542
20.789
1.00
12.70


ATOM
652
CD1
TRP
A
615
9.504
12.279
17.709
1.00
11.21


ATOM
653
NE1
TRP
A
615
8.132
12.292
17.747
1.00
11.25


ATOM
654
CZ2
TRP
A
615
6.414
11.418
19.354
1.00
12.28


ATOM
655
CZ3
TRP
A
615
7.410
10.307
21.255
1.00
18.15


ATOM
656
CH2
TRP
A
615
6.286
10.744
20.536
1.00
13.05


ATOM
657
C
TRP
A
615
11.090
9.237
17.910
1.00
8.08


ATOM
658
O
TRP
A
615
10.093
8.579
18.197
1.00
9.24


ATOM
659
N
ARG
A
616
11.514
9.365
16.656
1.00
9.61


ATOM
660
CA
ARG
A
616
10.750
8.759
15.570
1.00
11.24


ATOM
661
CB
ARG
A
616
11.346
9.129
14.206
1.00
9.33


ATOM
662
CG
ARG
A
616
11.241
10.630
13.885
1.00
13.33


ATOM
663
CD
ARG
A
616
9.817
11.169
14.120
1.00
11.22


ATOM
664
NE
ARG
A
616
9.705
12.598
13.823
1.00
13.61


ATOM
665
CZ
ARG
A
616
9.119
13.103
12.741
1.00
15.86


ATOM
666
NH1
ARG
A
616
8.577
12.300
11.834
1.00
15.89


ATOM
667
NH2
ARG
A
616
9.073
14.419
12.564
1.00
19.53


ATOM
668
C
ARG
A
616
10.607
7.250
15.705
1.00
9.88


ATOM
669
O
ARG
A
616
9.575
6.692
15.328
1.00
10.40


ATOM
670
N
HIS
A
617
11.625
6.582
16.242
1.00
7.87


ATOM
671
CA
HIS
A
617
11.514
5.141
16.419
1.00
7.37


ATOM
672
CB
HIS
A
617
12.862
4.523
16.782
1.00
11.98


ATOM
673
CG
HIS
A
617
12.742
3.163
17.390
1.00
8.70


ATOM
674
CD2
HIS
A
617
13.043
2.715
18.632
1.00
9.51


ATOM
675
ND1
HIS
A
617
12.206
2.088
16.713
1.00
8.99


ATOM
676
CE1
HIS
A
617
12.183
1.036
17.510
1.00
11.83


ATOM
677
NE2
HIS
A
617
12.684
1.391
18.681
1.00
10.58


ATOM
678
C
HIS
A
617
10.488
4.816
17.506
1.00
8.63


ATOM
679
O
HIS
A
617
9.692
3.888
17.361
1.00
10.24


ATOM
680
N
ALA
A
618
10.498
5.586
18.591
1.00
7.45


ATOM
681
CA
ALA
A
618
9.549
5.358
19.687
1.00
8.54


ATOM
682
CB
ALA
A
618
9.887
6.261
20.864
1.00
11.31


ATOM
683
C
ALA
A
618
8.126
5.637
19.210
1.00
8.39


ATOM
684
O
ALA
A
618
7.184
4.900
19.523
1.00
9.03


ATOM
685
N
PHE
A
619
7.981
6.725
18.465
1.00
8.88


ATOM
686
CA
PHE
A
619
6.695
7.118
17.911
1.00
9.63


ATOM
687
CB
PHE
A
619
6.850
8.418
17.119
1.00
12.92


ATOM
688
CG
PHE
A
619
5.618
8.809
16.357
1.00
10.44


ATOM
689
CD1
PHE
A
619
4.432
9.066
17.021
1.00
18.21


ATOM
690
CD2
PHE
A
619
5.646
8.914
14.974
1.00
12.41


ATOM
691
CE1
PHE
A
619
3.291
9.412
16.324
1.00
14.74


ATOM
692
CE2
PHE
A
619
4.508
9.260
14.270
1.00
13.16


ATOM
693
CZ
PHE
A
619
3.328
9.512
14.947
1.00
11.01


ATOM
694
C
PHE
A
619
6.150
6.017
16.996
1.00
9.52


ATOM
695
O
PHE
A
619
4.975
5.654
17.079
1.00
9.30


ATOM
696
N
ASN
A
620
7.001
5.490
16.119
1.00
10.15


ATOM
697
CA
ASN
A
620
6.583
4.428
15.204
1.00
11.34


ATOM
698
CB
ASN
A
620
7.694
4.123
14.194
1.00
9.10


ATOM
699
CG
ASN
A
620
7.658
5.052
12.999
1.00
17.16


ATOM
700
OD1
ASN
A
620
8.665
5.656
12.634
1.00
19.51


ATOM
701
ND2
ASN
A
620
6.490
5.166
12.382
1.00
12.88


ATOM
702
C
ASN
A
620
6.206
3.161
15.956
1.00
9.23


ATOM
703
O
ASN
A
620
5.273
2.457
15.574
1.00
10.76


ATOM
704
N
THR
A
621
6.936
2.871
17.026
1.00
8.56


ATOM
705
CA
THR
A
621
6.650
1.688
17.819
1.00
9.52


ATOM
706
CB
THR
A
621
7.707
1.509
18.928
1.00
8.96


ATOM
707
OG1
THR
A
621
9.010
1.404
18.328
1.00
9.14


ATOM
708
CG2
THR
A
621
7.428
0.244
19.736
1.00
7.93


ATOM
709
C
THR
A
621
5.252
1.821
18.425
1.00
10.48


ATOM
710
O
THR
A
621
4.455
0.879
18.382
1.00
10.11


ATOM
711
N
ALA
A
622
4.954
2.995
18.978
1.00
8.32


ATOM
712
CA
ALA
A
622
3.644
3.244
19.573
1.00
9.28


ATOM
713
CB
ALA
A
622
3.642
4.583
20.294
1.00
9.90


ATOM
714
C
ALA
A
622
2.567
3.224
18.488
1.00
10.02


ATOM
715
O
ALA
A
622
1.447
2.769
18.721
1.00
8.06


ATOM
716
N
GLN
A
623
2.902
3.708
17.297
1.00
7.82


ATOM
717
CA
GLN
A
623
1.927
3.708
16.211
1.00
10.17


ATOM
718
CB
GLN
A
623
2.456
4.487
15.003
1.00
8.39


ATOM
719
CG
GLN
A
623
1.473
4.578
13.825
1.00
8.23


ATOM
720
CD
GLN
A
623
1.444
3.319
12.967
1.00
13.63


ATOM
721
OE1
GLN
A
623
2.484
2.730
12.682
1.00
12.75


ATOM
722
NE2
GLN
A
623
0.258
2.919
12.535
1.00
11.69


ATOM
723
C
GLN
A
623
1.597
2.278
15.806
1.00
10.35


ATOM
724
O
GLN
A
623
0.449
1.962
15.501
1.00
9.61


ATOM
725
N
CYS
A
624
2.601
1.406
15.802
1.00
9.08


ATOM
726
CA
CYS
A
624
2.355
0.017
15.439
1.00
9.34


ATOM
727
CB
CYS
A
624
3.679
−0.740
15.273
1.00
11.00


ATOM
728
SG
CYS
A
624
3.481
−2.446
14.713
1.00
11.71


ATOM
729
C
CYS
A
624
1.495
−0.625
16.529
1.00
10.17


ATOM
730
O
CYS
A
624
0.631
−1.448
16.239
1.00
10.64


ATOM
731
N
MET
A
625
1.728
−0.238
17.781
1.00
9.06


ATOM
732
CA
MET
A
625
0.933
−0.764
18.892
1.00
9.38


ATOM
733
CB
MET
A
625
1.418
−0.180
20.225
1.00
8.21


ATOM
734
CG
MET
A
625
0.692
−0.718
21.466
1.00
8.16


ATOM
735
SD
MET
A
625
0.904
−2.512
21.728
1.00
11.88


ATOM
736
CE
MET
A
625
2.600
−2.586
22.309
1.00
11.24


ATOM
737
C
MET
A
625
−0.529
−0.376
18.661
1.00
9.31


ATOM
738
O
MET
A
625
−1.434
−1.208
18.757
1.00
10.06


ATOM
739
N
PHE
A
626
−0.757
0.896
18.353
1.00
9.47


ATOM
740
CA
PHE
A
626
−2.112
1.377
18.092
1.00
9.60


ATOM
741
CB
PHE
A
626
−2.077
2.859
17.725
1.00
9.70


ATOM
742
CG
PHE
A
626
−3.432
3.451
17.461
1.00
7.25


ATOM
743
CD1
PHE
A
626
−4.241
3.858
18.509
1.00
13.86


ATOM
744
CD2
PHE
A
626
−3.897
3.598
16.163
1.00
13.47


ATOM
745
CE1
PHE
A
626
−5.491
4.411
18.267
1.00
18.88


ATOM
746
CE2
PHE
A
626
−5.144
4.147
15.917
1.00
11.81


ATOM
747
CZ
PHE
A
626
−5.942
4.552
16.970
1.00
16.53


ATOM
748
C
PHE
A
626
−2.737
0.579
16.940
1.00
10.98


ATOM
749
O
PHE
A
626
−3.862
0.084
17.047
1.00
12.71


ATOM
750
N
ALA
A
627
−1.999
0.455
15.838
1.00
7.24


ATOM
751
CA
ALA
A
627
−2.486
−0.279
14.675
1.00
9.31


ATOM
752
CB
ALA
A
627
−1.454
−0.220
13.549
1.00
14.42


ATOM
753
C
ALA
A
627
−2.803
−1.734
15.024
1.00
11.79


ATOM
754
O
ALA
A
627
−3.815
−2.276
14.583
1.00
11.59


ATOM
755
N
ALA
A
628
−1.945
−2.361
15.824
1.00
10.63


ATOM
756
CA
ALA
A
628
−2.158
−3.749
16.219
1.00
11.00


ATOM
757
CB
ALA
A
628
−0.934
−4.280
16.961
1.00
11.43


ATOM
758
C
ALA
A
628
−3.398
−3.877
17.099
1.00
11.16


ATOM
759
O
ALA
A
628
−4.152
−4.845
16.994
1.00
12.30


ATOM
760
N
LEU
A
629
−3.608
−2.896
17.970
1.00
9.63


ATOM
761
CA
LEU
A
629
−4.765
−2.924
18.856
1.00
9.96


ATOM
762
CB
LEU
A
629
−4.627
−1.858
19.945
1.00
12.79


ATOM
763
CG
LEU
A
629
−3.538
−2.115
20.990
1.00
10.87


ATOM
764
CD1
LEU
A
629
−3.286
−0.859
21.792
1.00
11.38


ATOM
765
CD2
LEU
A
629
−3.956
−3.264
21.897
1.00
14.99


ATOM
766
C
LEU
A
629
−6.051
−2.692
18.073
1.00
12.31


ATOM
767
O
LEU
A
629
−7.084
−3.300
18.364
1.00
11.63


ATOM
768
N
LYS
A
630
−5.973
−1.822
17.070
1.00
11.64


ATOM
769
CA
LYS
A
630
−7.125
−1.479
16.242
1.00
12.87


ATOM
770
CB
LYS
A
630
−6.984
−0.037
15.738
1.00
15.53


ATOM
771
CG
LYS
A
630
−7.084
1.030
16.820
1.00
13.30


ATOM
772
CD
LYS
A
630
−8.495
1.104
17.385
1.00
19.60


ATOM
773
CE
LYS
A
630
−8.698
2.349
18.245
1.00
18.93


ATOM
774
NZ
LYS
A
630
−7.877
2.334
19.481
1.00
40.94


ATOM
775
C
LYS
A
630
−7.323
−2.422
15.049
1.00
13.54


ATOM
776
O
LYS
A
630
−8.122
−3.350
15.107
1.00
12.81


ATOM
777
N
ALA
A
631
−6.597
−2.170
13.967
1.00
13.05


ATOM
778
CA
ALA
A
631
−6.701
−2.997
12.770
1.00
14.94


ATOM
779
CB
ALA
A
631
−5.763
−2.460
11.688
1.00
17.58


ATOM
780
C
ALA
A
631
−6.374
−4.461
13.068
1.00
16.22


ATOM
781
O
ALA
A
631
−6.960
−5.375
12.479
1.00
15.44


ATOM
782
N
GLY
A
632
−5.439
−4.670
13.990
1.00
12.88


ATOM
783
CA
GLY
A
632
−5.028
−6.014
14.359
1.00
13.10


ATOM
784
C
GLY
A
632
−5.995
−6.711
15.298
1.00
13.12


ATOM
785
O
GLY
A
632
−5.850
−7.902
15.576
1.00
15.03


ATOM
786
N
LYS
A
633
−6.968
−5.959
15.803
1.00
13.75


ATOM
787
CA
LYS
A
633
−7.997
−6.497
16.692
1.00
14.20


ATOM
788
CB
LYS
A
633
−8.815
−7.566
15.954
1.00
13.72


ATOM
789
CG
LYS
A
633
−9.438
−7.109
14.631
1.00
23.64


ATOM
790
CD
LYS
A
633
−10.532
−6.072
14.834
1.00
30.20


ATOM
791
CE
LYS
A
633
−11.182
−5.672
13.510
1.00
34.87


ATOM
792
NZ
LYS
A
633
−10.227
−4.989
12.594
1.00
46.21


ATOM
793
C
LYS
A
633
−7.464
−7.085
17.997
1.00
14.18


ATOM
794
O
LYS
A
633
−8.048
−8.024
18.540
1.00
14.72


ATOM
795
N
ILE
A
634
−6.366
−6.536
18.507
1.00
13.07


ATOM
796
CA
ILE
A
634
−5.801
−7.037
19.755
1.00
12.44


ATOM
797
CB
ILE
A
634
−4.262
−6.819
19.799
1.00
13.52


ATOM
798
CG2
ILE
A
634
−3.709
−7.236
21.156
1.00
14.73


ATOM
799
CG1
ILE
A
634
−3.581
−7.632
18.694
1.00
14.10


ATOM
800
CD1
ILE
A
634
−3.757
−9.128
18.829
1.00
14.44


ATOM
801
C
ILE
A
634
−6.439
−6.346
20.967
1.00
12.23


ATOM
802
O
ILE
A
634
−6.456
−6.894
22.067
1.00
12.06


ATOM
803
N
GLN
A
635
−6.990
−5.155
20.752
1.00
13.17


ATOM
804
CA
GLN
A
635
−7.597
−4.377
21.834
1.00
12.59


ATOM
805
CB
GLN
A
635
−8.330
−3.158
21.267
1.00
14.77


ATOM
806
CG
GLN
A
635
−8.796
−2.180
22.345
1.00
17.07


ATOM
807
CD
GLN
A
635
−9.479
−0.949
21.778
1.00
17.87


ATOM
808
OE1
GLN
A
635
−9.080
−0.425
20.741
1.00
15.93


ATOM
809
NE2
GLN
A
635
−10.509
−0.473
22.471
1.00
27.59


ATOM
810
C
GLN
A
635
−8.549
−5.127
22.762
1.00
13.46


ATOM
811
O
GLN
A
635
−8.382
−5.107
23.984
1.00
12.66


ATOM
812
N
ASN
A
636
−9.554
−5.778
22.188
1.00
12.36


ATOM
813
CA
ASN
A
636
−10.533
−6.493
22.996
1.00
15.16


ATOM
814
CB
ASN
A
636
−11.736
−6.872
22.130
1.00
13.54


ATOM
815
CG
ASN
A
636
−12.508
−5.655
21.658
1.00
19.96


ATOM
816
OD1
ASN
A
636
−12.211
−4.526
22.059
1.00
19.43


ATOM
817
ND2
ASN
A
636
−13.506
−5.874
20.810
1.00
20.88


ATOM
818
C
ASN
A
636
−10.002
−7.708
23.743
1.00
14.39


ATOM
819
O
ASN
A
636
−10.720
−8.312
24.539
1.00
17.61


ATOM
820
N
LYS
A
637
−8.744
−8.060
23.500
1.00
13.69


ATOM
821
CA
LYS
A
637
−8.132
−9.194
24.180
1.00
13.94


ATOM
822
CB
LYS
A
637
−7.124
−9.893
23.262
1.00
13.19


ATOM
823
CG
LYS
A
637
−7.667
−10.328
21.910
1.00
16.41


ATOM
824
CD
LYS
A
637
−6.599
−11.079
21.128
1.00
18.79


ATOM
825
CE
LYS
A
637
−7.110
−11.542
19.773
1.00
21.00


ATOM
826
NZ
LYS
A
637
−8.266
−12.467
19.893
1.00
27.72


ATOM
827
C
LYS
A
637
−7.400
−8.708
25.435
1.00
14.29


ATOM
828
O
LYS
A
637
−6.930
−9.514
26.237
1.00
15.91


ATOM
829
N
LEU
A
638
−7.316
−7.391
25.611
1.00
13.88


ATOM
830
CA
LEU
A
638
−6.602
−6.828
26.757
1.00
14.02


ATOM
831
CB
LEU
A
638
−5.426
−5.988
26.256
1.00
14.42


ATOM
832
CG
LEU
A
638
−4.496
−6.595
25.201
1.00
13.65


ATOM
833
CD1
LEU
A
638
−3.405
−5.589
24.860
1.00
13.98


ATOM
834
CD2
LEU
A
638
−3.881
−7.885
25.718
1.00
12.70


ATOM
835
C
LEU
A
638
−7.464
−5.973
27.687
1.00
13.83


ATOM
836
O
LEU
A
638
−8.551
−5.529
27.313
1.00
16.24


ATOM
837
N
THR
A
639
−6.968
−5.745
28.902
1.00
13.04


ATOM
838
CA
THR
A
639
−7.665
−4.913
29.885
1.00
12.97


ATOM
839
CB
THR
A
639
−7.225
−5.244
31.323
1.00
9.72


ATOM
840
OG1
THR
A
639
−5.883
−4.777
31.534
1.00
11.58


ATOM
841
CG2
THR
A
639
−7.284
−6.752
31.574
1.00
13.01


ATOM
842
C
THR
A
639
−7.320
−3.443
29.627
1.00
11.14


ATOM
843
O
THR
A
639
−6.369
−3.147
28.910
1.00
12.39


ATOM
844
N
ASP
A
640
−8.082
−2.524
30.216
1.00
11.83


ATOM
845
CA
ASP
A
640
−7.814
−1.098
30.027
1.00
11.03


ATOM
846
CB
ASP
A
640
−8.846
−0.243
30.774
1.00
9.58


ATOM
847
CG
ASP
A
640
−10.238
−0.368
30.191
1.00
23.27


ATOM
848
OD1
ASP
A
640
−10.357
−0.828
29.037
1.00
21.74


ATOM
849
OD2
ASP
A
640
−11.211
0.011
30.879
1.00
18.96


ATOM
850
C
ASP
A
640
−6.419
−0.724
30.519
1.00
10.85


ATOM
851
O
ASP
A
640
−5.708
0.058
29.881
1.00
11.05


ATOM
852
N
LEU
A
641
−6.031
−1.290
31.655
1.00
11.16


ATOM
853
CA
LEU
A
641
−4.727
−1.004
32.235
1.00
10.51


ATOM
854
CB
LEU
A
641
−4.628
−1.606
33.640
1.00
13.05


ATOM
855
CG
LEU
A
641
−5.633
−1.081
34.674
1.00
13.28


ATOM
856
CD1
LEU
A
641
−5.383
−1.762
36.005
1.00
14.91


ATOM
857
CD2
LEU
A
641
−5.506
0.432
34.813
1.00
12.98


ATOM
858
C
LEU
A
641
−3.593
−1.527
31.359
1.00
10.02


ATOM
859
O
LEU
A
641
−2.550
−0.883
31.237
1.00
9.79


ATOM
860
N
GLU
A
642
−3.791
−2.692
30.748
1.00
9.49


ATOM
861
CA
GLU
A
642
−2.756
−3.253
29.886
1.00
9.55


ATOM
862
CB
GLU
A
642
−3.120
−4.687
29.493
1.00
13.24


ATOM
863
CG
GLU
A
642
−3.215
−5.605
30.705
1.00
17.56


ATOM
864
CD
GLU
A
642
−3.645
−7.021
30.373
1.00
14.47


ATOM
865
OE1
GLU
A
642
−4.411
−7.212
29.404
1.00
12.63


ATOM
866
OE2
GLU
A
642
−3.233
−7.949
31.108
1.00
15.36


ATOM
867
C
GLU
A
642
−2.568
−2.366
28.656
1.00
9.56


ATOM
868
O
GLU
A
642
−1.442
−2.135
28.217
1.00
10.36


ATOM
869
N
ILE
A
643
−3.665
−1.847
28.112
1.00
9.98


ATOM
870
CA
ILE
A
643
−3.585
−0.978
26.945
1.00
11.53


ATOM
871
CB
ILE
A
643
−4.992
−0.683
26.391
1.00
12.52


ATOM
872
CG2
ILE
A
643
−4.915
0.367
25.281
1.00
11.83


ATOM
873
CG1
ILE
A
643
−5.614
−1.984
25.885
1.00
11.82


ATOM
874
CD1
ILE
A
643
−7.089
−1.872
25.553
1.00
18.49


ATOM
875
C
ILE
A
643
−2.883
0.323
27.339
1.00
9.56


ATOM
876
O
ILE
A
643
−1.993
0.806
26.635
1.00
10.76


ATOM
877
N
LEU
A
644
−3.278
0.880
28.479
1.00
9.68


ATOM
878
CA
LEU
A
644
−2.663
2.105
28.974
1.00
9.78


ATOM
879
CB
LEU
A
644
−3.285
2.482
30.321
1.00
11.15


ATOM
880
CG
LEU
A
644
−2.658
3.643
31.093
1.00
14.02


ATOM
881
CD1
LEU
A
644
−2.853
4.946
30.328
1.00
14.15


ATOM
882
CD2
LEU
A
644
−3.315
3.735
32.471
1.00
14.10


ATOM
883
C
LEU
A
644
−1.152
1.899
29.139
1.00
9.98


ATOM
884
O
LEU
A
644
−0.342
2.720
28.694
1.00
9.97


ATOM
885
N
ALA
A
645
−0.778
0.788
29.766
1.00
8.98


ATOM
886
CA
ALA
A
645
0.634
0.492
30.008
1.00
8.84


ATOM
887
CB
ALA
A
645
0.763
−0.724
30.928
1.00
8.17


ATOM
888
C
ALA
A
645
1.414
0.256
28.718
1.00
9.39


ATOM
889
O
ALA
A
645
2.556
0.687
28.598
1.00
9.92


ATOM
890
N
LEU
A
646
0.799
−0.430
27.761
1.00
8.76


ATOM
891
CA
LEU
A
646
1.462
−0.708
26.488
1.00
8.34


ATOM
892
CB
LEU
A
646
0.607
−1.652
25.644
1.00
10.30


ATOM
893
CG
LEU
A
646
0.541
−3.101
26.128
1.00
11.47


ATOM
894
CD1
LEU
A
646
−0.557
−3.832
25.379
1.00
15.28


ATOM
895
CD2
LEU
A
646
1.879
−3.779
25.906
1.00
10.48


ATOM
896
C
LEU
A
646
1.761
0.550
25.682
1.00
7.55


ATOM
897
O
LEU
A
646
2.837
0.676
25.094
1.00
9.05


ATOM
898
N
LEU
A
647
0.812
1.479
25.643
1.00
7.57


ATOM
899
CA
LEU
A
647
1.020
2.713
24.889
1.00
8.87


ATOM
900
CB
LEU
A
647
−0.283
3.516
24.803
1.00
7.82


ATOM
901
CG
LEU
A
647
−0.214
4.722
23.862
1.00
10.06


ATOM
902
CD1
LEU
A
647
0.194
4.251
22.470
1.00
13.81


ATOM
903
CD2
LEU
A
647
−1.560
5.437
23.820
1.00
12.05


ATOM
904
C
LEU
A
647
2.120
3.550
25.540
1.00
8.12


ATOM
905
O
LEU
A
647
3.011
4.070
24.863
1.00
8.78


ATOM
906
N
ILE
A
648
2.056
3.676
26.860
1.00
9.66


ATOM
907
CA
ILE
A
648
3.065
4.429
27.597
1.00
8.86


ATOM
908
CB
ILE
A
648
2.692
4.501
29.100
1.00
10.81


ATOM
909
CG2
ILE
A
648
3.851
5.063
29.917
1.00
7.70


ATOM
910
CG1
ILE
A
648
1.439
5.364
29.266
1.00
11.45


ATOM
911
CD1
ILE
A
648
0.921
5.437
30.688
1.00
9.57


ATOM
912
C
ILE
A
648
4.427
3.756
27.424
1.00
8.38


ATOM
913
O
ILE
A
648
5.439
4.427
27.180
1.00
9.63


ATOM
914
N
ALA
A
649
4.456
2.430
27.536
1.00
9.32


ATOM
915
CA
ALA
A
649
5.710
1.697
27.388
1.00
9.98


ATOM
916
CB
ALA
A
649
5.506
0.214
27.703
1.00
11.64


ATOM
917
C
ALA
A
649
6.285
1.853
25.989
1.00
9.64


ATOM
918
O
ALA
A
649
7.471
2.126
25.831
1.00
10.34


ATOM
919
N
ALA
A
650
5.449
1.680
24.971
1.00
11.02


ATOM
920
CA
ALA
A
650
5.914
1.814
23.591
1.00
9.43


ATOM
921
CB
ALA
A
650
4.747
1.618
22.617
1.00
8.79


ATOM
922
C
ALA
A
650
6.561
3.183
23.359
1.00
8.11


ATOM
923
O
ALA
A
650
7.628
3.292
22.748
1.00
9.60


ATOM
924
N
LEU
A
651
5.914
4.233
23.851
1.00
9.58


ATOM
925
CA
LEU
A
651
6.443
5.582
23.679
1.00
10.27


ATOM
926
CB
LEU
A
651
5.383
6.613
24.066
1.00
9.84


ATOM
927
CG
LEU
A
651
4.198
6.717
23.101
1.00
6.24


ATOM
928
CD1
LEU
A
651
3.038
7.432
23.772
1.00
14.57


ATOM
929
CD2
LEU
A
651
4.637
7.463
21.846
1.00
11.43


ATOM
930
C
LEU
A
651
7.706
5.848
24.488
1.00
10.46


ATOM
931
O
LEU
A
651
8.573
6.611
24.066
1.00
9.75


ATOM
932
N
SER
A
652
7.807
5.194
25.640
1.00
9.58


ATOM
933
CA
SER
A
652
8.935
5.394
26.542
1.00
10.30


ATOM
934
CB
SER
A
652
8.422
5.453
27.983
1.00
9.30


ATOM
935
OG
SER
A
652
7.367
6.379
28.133
1.00
11.78


ATOM
936
C
SER
A
652
10.026
4.334
26.504
1.00
8.64


ATOM
937
O
SER
A
652
11.068
4.520
27.125
1.00
9.90


ATOM
938
N
HIS
A
653
9.805
3.249
25.765
1.00
9.64


ATOM
939
CA
HIS
A
653
10.739
2.128
25.769
1.00
9.99


ATOM
940
CB
HIS
A
653
10.164
0.963
24.952
1.00
8.26


ATOM
941
CG
HIS
A
653
10.546
0.980
23.510
1.00
8.55


ATOM
942
CD2
HIS
A
653
11.529
0.333
22.842
1.00
9.53


ATOM
943
ND1
HIS
A
653
9.881
1.740
22.569
1.00
10.01


ATOM
944
CE1
HIS
A
653
10.440
1.559
21.387
1.00
6.46


ATOM
945
NE2
HIS
A
653
11.444
0.708
21.526
1.00
6.65


ATOM
946
C
HIS
A
653
12.210
2.321
25.412
1.00
10.62


ATOM
947
O
HIS
A
653
13.024
1.459
25.741
1.00
8.86


ATOM
948
N
ASP
A
654
12.559
3.424
24.752
1.00
9.82


ATOM
949
CA
ASP
A
654
13.959
3.673
24.406
1.00
9.46


ATOM
950
CB
ASP
A
654
14.184
3.580
22.889
1.00
10.10


ATOM
951
CG
ASP
A
654
14.509
2.172
22.432
1.00
10.77


ATOM
952
OD1
ASP
A
654
15.159
1.444
23.204
1.00
9.55


ATOM
953
OD2
ASP
A
654
14.141
1.812
21.294
1.00
8.85


ATOM
954
C
ASP
A
654
14.477
5.024
24.896
1.00
9.92


ATOM
955
O
ASP
A
654
15.500
5.507
24.413
1.00
9.67


ATOM
956
N
LEU
A
655
13.783
5.619
25.865
1.00
9.19


ATOM
957
CA
LEU
A
655
14.169
6.922
26.408
1.00
10.06


ATOM
958
CB
LEU
A
655
13.364
7.214
27.677
1.00
8.55


ATOM
959
CG
LEU
A
655
11.900
7.603
27.479
1.00
10.24


ATOM
960
CD1
LEU
A
655
11.151
7.468
28.805
1.00
9.10


ATOM
961
CD2
LEU
A
655
11.819
9.028
26.944
1.00
15.71


ATOM
962
C
LEU
A
655
15.658
7.101
26.713
1.00
10.50


ATOM
963
O
LEU
A
655
16.279
6.268
27.372
1.00
9.92


ATOM
964
N
ASP
A
656
16.215
8.209
26.232
1.00
8.66


ATOM
965
CA
ASP
A
656
17.622
8.542
26.448
1.00
8.66


ATOM
966
CB
ASP
A
656
17.867
8.811
27.941
1.00
11.08


ATOM
967
CG
ASP
A
656
19.211
9.475
28.207
1.00
16.07


ATOM
968
OD1
ASP
A
656
19.576
10.406
27.460
1.00
11.04


ATOM
969
OD2
ASP
A
656
19.897
9.074
29.173
1.00
13.88


ATOM
970
C
ASP
A
656
18.600
7.483
25.939
1.00
8.59


ATOM
971
O
ASP
A
656
19.670
7.288
26.511
1.00
9.89


ATOM
972
N
HIS
A
657
18.242
6.806
24.851
1.00
9.07


ATOM
973
CA
HIS
A
657
19.118
5.790
24.284
1.00
10.63


ATOM
974
CB
HIS
A
657
18.412
5.068
23.137
1.00
9.06


ATOM
975
CG
HIS
A
657
19.095
3.810
22.712
1.00
8.47


ATOM
976
CD2
HIS
A
657
20.347
3.589
22.245
1.00
7.97


ATOM
977
ND1
HIS
A
657
18.480
2.575
22.748
1.00
12.46


ATOM
978
CE1
HIS
A
657
19.322
1.652
22.322
1.00
5.38


ATOM
979
NE2
HIS
A
657
20.464
2.242
22.011
1.00
12.33


ATOM
980
C
HIS
A
657
20.404
6.453
23.778
1.00
11.40


ATOM
981
O
HIS
A
657
20.362
7.404
22.993
1.00
11.45


ATOM
982
N
PRO
A
658
21.567
5.957
24.230
1.00
11.01


ATOM
983
CD
PRO
A
658
21.697
4.963
25.311
1.00
10.94


ATOM
984
CA
PRO
A
658
22.884
6.479
23.850
1.00
10.19


ATOM
985
CB
PRO
A
658
23.792
5.930
24.944
1.00
9.66


ATOM
986
CG
PRO
A
658
23.171
4.618
25.252
1.00
16.61


ATOM
987
C
PRO
A
658
23.386
6.123
22.451
1.00
11.02


ATOM
988
O
PRO
A
658
24.428
6.627
22.021
1.00
12.41


ATOM
989
N
GLY
A
659
22.659
5.265
21.744
1.00
8.82


ATOM
990
CA
GLY
A
659
23.080
4.888
20.405
1.00
8.78


ATOM
991
C
GLY
A
659
24.115
3.781
20.356
1.00
9.97


ATOM
992
O
GLY
A
659
24.750
3.566
19.316
1.00
12.32


ATOM
993
N
VAL
A
660
24.305
3.095
21.480
1.00
8.93


ATOM
994
CA
VAL
A
660
25.248
1.983
21.564
1.00
9.69


ATOM
995
CB
VAL
A
660
26.554
2.387
22.301
1.00
10.19


ATOM
996
CG1
VAL
A
660
27.358
3.355
21.434
1.00
12.07


ATOM
997
CG2
VAL
A
660
26.236
3.020
23.642
1.00
12.93


ATOM
998
C
VAL
A
660
24.545
0.834
22.289
1.00
10.76


ATOM
999
O
VAL
A
660
23.601
1.059
23.052
1.00
10.23


ATOM
1000
N
SER
A
661
25.002
−0.392
22.049
1.00
7.63


ATOM
1001
CA
SER
A
661
24.371
−1.577
22.624
1.00
10.33


ATOM
1002
CB
SER
A
661
24.748
−2.801
21.793
1.00
8.76


ATOM
1003
OG
SER
A
661
26.099
−3.151
22.021
1.00
9.56


ATOM
1004
C
SER
A
661
24.687
−1.864
24.088
1.00
9.36


ATOM
1005
O
SER
A
661
25.549
−1.230
24.696
1.00
10.42


ATOM
1006
N
ASN
A
662
23.969
−2.838
24.643
1.00
10.10


ATOM
1007
CA
ASN
A
662
24.165
−3.261
26.026
1.00
8.94


ATOM
1008
CB
ASN
A
662
23.177
−4.369
26.384
1.00
12.24


ATOM
1009
CG
ASN
A
662
21.832
−3.836
26.824
1.00
11.27


ATOM
1010
OD1
ASN
A
662
20.794
−4.457
26.592
1.00
19.20


ATOM
1011
ND2
ASN
A
662
21.844
−2.689
27.483
1.00
5.90


ATOM
1012
C
ASN
A
662
25.586
−3.781
26.161
1.00
11.89


ATOM
1013
O
ASN
A
662
26.289
−3.459
27.116
1.00
12.39


ATOM
1014
N
GLN
A
663
26.010
−4.598
25.199
1.00
10.34


ATOM
1015
CA
GLN
A
663
27.356
−5.139
25.246
1.00
11.06


ATOM
1016
CB
GLN
A
663
27.578
−6.120
24.083
1.00
14.83


ATOM
1017
CG
GLN
A
663
26.677
−7.373
24.197
1.00
25.28


ATOM
1018
CD
GLN
A
663
25.283
−7.191
23.575
1.00
24.96


ATOM
1019
OE1
GLN
A
663
24.919
−6.113
23.106
1.00
31.10


ATOM
1020
NE2
GLN
A
663
24.497
−8.271
23.572
1.00
46.85


ATOM
1021
C
GLN
A
663
28.422
−4.039
25.236
1.00
13.51


ATOM
1022
O
GLN
A
663
29.439
−4.161
25.921
1.00
12.70


ATOM
1023
N
PHE
A
664
28.184
−2.956
24.504
1.00
12.64


ATOM
1024
CA
PHE
A
664
29.145
−1.852
24.465
1.00
11.20


ATOM
1025
CB
PHE
A
664
28.754
−0.838
23.380
1.00
12.60


ATOM
1026
CG
PHE
A
664
29.669
0.355
23.296
1.00
15.21


ATOM
1027
CD1
PHE
A
664
29.554
1.407
24.198
1.00
13.93


ATOM
1028
CD2
PHE
A
664
30.668
0.409
22.336
1.00
10.34


ATOM
1029
CE1
PHE
A
664
30.419
2.484
24.144
1.00
11.59


ATOM
1030
CE2
PHE
A
664
31.541
1.487
22.275
1.00
16.42


ATOM
1031
CZ
PHE
A
664
31.418
2.527
23.182
1.00
18.27


ATOM
1032
C
PHE
A
664
29.207
−1.171
25.830
1.00
11.75


ATOM
1033
O
PHE
A
664
30.290
−0.818
26.306
1.00
11.28


ATOM
1034
N
LEU
A
665
28.046
−0.980
26.452
1.00
11.17


ATOM
1035
CA
LEU
A
665
27.982
−0.346
27.768
1.00
11.46


ATOM
1036
CB
LEU
A
665
26.524
−0.163
28.204
1.00
11.38


ATOM
1037
CG
LEU
A
665
25.703
0.864
27.420
1.00
9.72


ATOM
1038
CD1
LEU
A
665
24.304
0.959
28.015
1.00
16.35


ATOM
1039
CD2
LEU
A
665
26.399
2.215
27.470
1.00
13.26


ATOM
1040
C
LEU
A
665
28.726
−1.200
28.793
1.00
13.75


ATOM
1041
O
LEU
A
665
29.404
−0.686
29.681
1.00
11.85


ATOM
1042
N
ILE
A
666
28.591
−2.512
28.661
1.00
12.41


ATOM
1043
CA
ILE
A
666
29.259
−3.444
29.559
1.00
13.52


ATOM
1044
CB
ILE
A
666
28.773
−4.887
29.300
1.00
13.10


ATOM
1045
CG2
ILE
A
666
29.667
−5.882
30.020
1.00
13.00


ATOM
1046
CG1
ILE
A
666
27.322
−5.036
29.761
1.00
10.73


ATOM
1047
CD1
ILE
A
666
26.687
−6.346
29.369
1.00
14.67


ATOM
1048
C
ILE
A
666
30.770
−3.381
29.356
1.00
11.71


ATOM
1049
O
ILE
A
666
31.541
−3.297
30.317
1.00
14.40


ATOM
1050
N
ASN
A
667
31.183
−3.408
28.094
1.00
12.52


ATOM
1051
CA
ASN
A
667
32.599
−3.382
27.733
1.00
11.69


ATOM
1052
CB
ASN
A
667
32.745
−3.652
26.232
1.00
15.94


ATOM
1053
CG
ASN
A
667
32.340
−5.065
25.848
1.00
13.91


ATOM
1054
OD1
ASN
A
667
32.138
−5.363
24.669
1.00
17.63


ATOM
1055
ND2
ASN
A
667
32.233
−5.946
26.837
1.00
11.25


ATOM
1056
C
ASN
A
667
33.323
−2.090
28.091
1.00
15.59


ATOM
1057
O
ASN
A
667
34.530
−2.104
28.355
1.00
16.72


ATOM
1058
N
THR
A
668
32.601
−0.974
28.098
1.00
15.05


ATOM
1059
CA
THR
A
668
33.211
0.308
28.428
1.00
16.29


ATOM
1060
CB
THR
A
668
32.670
1.432
27.520
1.00
16.12


ATOM
1061
OG1
THR
A
668
31.237
1.448
27.567
1.00
19.49


ATOM
1062
CG2
THR
A
668
33.133
1.207
26.078
1.00
15.93


ATOM
1063
C
THR
A
668
32.995
0.672
29.895
1.00
18.10


ATOM
1064
O
THR
A
668
33.158
1.830
30.297
1.00
20.65


ATOM
1065
N
ASN
A
669
32.617
−0.330
30.682
1.00
17.75


ATOM
1066
CA
ASN
A
669
32.402
−0.177
32.115
1.00
20.15


ATOM
1067
CB
ASN
A
669
33.749
0.053
32.797
1.00
28.92


ATOM
1068
CG
ASN
A
669
34.791
−0.955
32.361
1.00
34.79


ATOM
1069
OD1
ASN
A
669
34.619
−2.160
32.543
1.00
40.75


ATOM
1070
ND2
ASN
A
669
35.877
−0.468
31.772
1.00
36.76


ATOM
1071
C
ASN
A
669
31.428
0.926
32.515
1.00
20.87


ATOM
1072
O
ASN
A
669
31.690
1.696
33.443
1.00
21.59


ATOM
1073
N
SER
A
670
30.302
0.996
31.819
1.00
17.34


ATOM
1074
CA
SER
A
670
29.286
1.992
32.120
1.00
19.60


ATOM
1075
CB
SER
A
670
28.103
1.836
31.160
1.00
18.96


ATOM
1076
OG
SER
A
670
27.023
2.672
31.535
1.00
22.69


ATOM
1077
C
SER
A
670
28.803
1.787
33.551
1.00
16.24


ATOM
1078
O
SER
A
670
28.755
0.655
34.041
1.00
14.46


ATOM
1079
N
GLU
A
671
28.455
2.879
34.227
1.00
18.45


ATOM
1080
CA
GLU
A
671
27.951
2.775
35.589
1.00
19.69


ATOM
1081
CB
GLU
A
671
27.756
4.154
36.209
1.00
17.48


ATOM
1082
CG
GLU
A
671
28.985
5.024
36.189
1.00
31.14


ATOM
1083
CD
GLU
A
671
28.901
6.156
37.191
1.00
32.78


ATOM
1084
OE1
GLU
A
671
27.830
6.796
37.291
1.00
31.62


ATOM
1085
OE2
GLU
A
671
29.914
6.406
37.875
1.00
26.52


ATOM
1086
C
GLU
A
671
26.611
2.058
35.549
1.00
18.77


ATOM
1087
O
GLU
A
671
26.253
1.332
36.482
1.00
19.75


ATOM
1088
N
LEU
A
672
25.868
2.281
34.466
1.00
17.92


ATOM
1089
CA
LEU
A
672
24.569
1.646
34.279
1.00
15.76


ATOM
1090
CB
LEU
A
672
23.954
2.067
32.942
1.00
12.50


ATOM
1091
CG
LEU
A
672
23.478
3.509
32.771
1.00
18.92


ATOM
1092
CD1
LEU
A
672
23.101
3.741
31.314
1.00
18.65


ATOM
1093
CD2
LEU
A
672
22.292
3.766
33.678
1.00
24.52


ATOM
1094
C
LEU
A
672
24.738
0.130
34.291
1.00
13.50


ATOM
1095
O
LEU
A
672
23.961
−0.586
34.912
1.00
12.92


ATOM
1096
N
ALA
A
673
25.755
−0.358
33.590
1.00
13.11


ATOM
1097
CA
ALA
A
673
26.001
−1.792
33.546
1.00
13.53


ATOM
1098
CB
ALA
A
673
27.169
−2.099
32.594
1.00
11.10


ATOM
1099
C
ALA
A
673
26.318
−2.283
34.956
1.00
13.78


ATOM
1100
O
ALA
A
673
25.925
−3.380
35.354
1.00
12.36


ATOM
1101
N
LEU
A
674
27.028
−1.458
35.718
1.00
15.22


ATOM
1102
CA
LEU
A
674
27.394
−1.829
37.076
1.00
16.65


ATOM
1103
CB
LEU
A
674
28.414
−0.832
37.632
1.00
18.96


ATOM
1104
CG
LEU
A
674
29.225
−1.323
38.832
1.00
26.52


ATOM
1105
CD1
LEU
A
674
29.939
−2.620
38.460
1.00
24.45


ATOM
1106
CD2
LEU
A
674
30.231
−0.258
39.246
1.00
20.57


ATOM
1107
C
LEU
A
674
26.152
−1.866
37.960
1.00
15.94


ATOM
1108
O
LEU
A
674
25.930
−2.818
38.709
1.00
16.86


ATOM
1109
N
MET
A
675
25.335
−0.822
37.851
1.00
19.35


ATOM
1110
CA
MET
A
675
24.107
−0.694
38.627
1.00
18.57


ATOM
1111
CB
MET
A
675
23.413
0.641
38.312
1.00
29.02


ATOM
1112
CG
MET
A
675
24.180
1.882
38.753
1.00
32.86


ATOM
1113
SD
MET
A
675
23.766
3.373
37.785
1.00
38.23


ATOM
1114
CE
MET
A
675
22.129
3.769
38.381
1.00
40.96


ATOM
1115
C
MET
A
675
23.133
−1.830
38.346
1.00
17.83


ATOM
1116
O
MET
A
675
22.529
−2.383
39.265
1.00
17.84


ATOM
1117
N
TYR
A
676
23.000
−2.184
37.073
1.00
15.75


ATOM
1118
CA
TYR
A
676
22.052
−3.212
36.679
1.00
16.85


ATOM
1119
CB
TYR
A
676
21.293
−2.720
35.442
1.00
16.19


ATOM
1120
CG
TYR
A
676
20.619
−1.374
35.668
1.00
20.30


ATOM
1121
CD1
TYR
A
676
19.694
−1.197
36.691
1.00
31.51


ATOM
1122
CE1
TYR
A
676
19.107
0.045
36.922
1.00
18.89


ATOM
1123
CD2
TYR
A
676
20.934
−0.276
34.877
1.00
23.78


ATOM
1124
CE2
TYR
A
676
20.354
0.962
35.097
1.00
27.90


ATOM
1125
CZ
TYR
A
676
19.443
1.117
36.118
1.00
24.78


ATOM
1126
OH
TYR
A
676
18.866
2.354
36.326
1.00
28.03


ATOM
1127
C
TYR
A
676
22.605
−4.623
36.471
1.00
16.48


ATOM
1128
O
TYR
A
676
21.949
−5.478
35.872
1.00
15.88


ATOM
1129
N
ASN
A
677
23.814
−4.863
36.968
1.00
16.14


ATOM
1130
CA
ASN
A
677
24.433
−6.182
36.888
1.00
14.23


ATOM
1131
CB
ASN
A
677
23.666
−7.138
37.812
1.00
21.33


ATOM
1132
CG
ASN
A
677
24.382
−8.452
38.022
1.00
29.37


ATOM
1133
OD1
ASN
A
677
25.570
−8.478
38.349
1.00
38.44


ATOM
1134
ND2
ASN
A
677
23.662
−9.555
37.847
1.00
42.62


ATOM
1135
C
ASN
A
677
24.516
−6.765
35.474
1.00
15.05


ATOM
1136
O
ASN
A
677
24.332
−7.966
35.275
1.00
14.59


ATOM
1137
N
ASP
A
678
24.802
−5.904
34.502
1.00
13.69


ATOM
1138
CA
ASP
A
678
24.926
−6.302
33.100
1.00
16.08


ATOM
1139
CB
ASP
A
678
26.080
−7.293
32.915
1.00
12.96


ATOM
1140
CG
ASP
A
678
27.430
−6.691
33.234
1.00
18.27


ATOM
1141
OD1
ASP
A
678
27.519
−5.452
33.377
1.00
16.21


ATOM
1142
OD2
ASP
A
678
28.406
−7.464
33.334
1.00
20.95


ATOM
1143
C
ASP
A
678
23.667
−6.919
32.499
1.00
16.35


ATOM
1144
O
ASP
A
678
23.731
−7.509
31.420
1.00
17.49


ATOM
1145
N
GLU
A
679
22.534
−6.790
33.184
1.00
14.03


ATOM
1146
CA
GLU
A
679
21.278
−7.358
32.690
1.00
14.39


ATOM
1147
CB
GLU
A
679
20.567
−8.133
33.799
1.00
14.04


ATOM
1148
CG
GLU
A
679
21.314
−9.351
34.300
1.00
22.79


ATOM
1149
CD
GLU
A
679
20.514
−10.128
35.330
1.00
43.42


ATOM
1150
OE1
GLU
A
679
19.464
−10.699
34.964
1.00
51.30


ATOM
1151
OE2
GLU
A
679
20.931
−10.162
36.507
1.00
41.34


ATOM
1152
C
GLU
A
679
20.320
−6.301
32.151
1.00
12.89


ATOM
1153
O
GLU
A
679
19.873
−5.430
32.895
1.00
13.61


ATOM
1154
N
SER
A
680
19.993
−6.401
30.863
1.00
10.87


ATOM
1155
CA
SER
A
680
19.086
−5.456
30.209
1.00
12.50


ATOM
1156
CB
SER
A
680
17.627
−5.787
30.555
1.00
12.08


ATOM
1157
OG
SER
A
680
17.267
−7.087
30.111
1.00
11.26


ATOM
1158
C
SER
A
680
19.409
−4.038
30.663
1.00
11.78


ATOM
1159
O
SER
A
680
18.517
−3.280
31.045
1.00
12.76


ATOM
1160
N
VAL
A
681
20.693
−3.693
30.617
1.00
9.67


ATOM
1161
CA
VAL
A
681
21.183
−2.386
31.049
1.00
7.19


ATOM
1162
CB
VAL
A
681
22.688
−2.248
30.725
1.00
11.97


ATOM
1163
CG1
VAL
A
681
23.219
−0.917
31.245
1.00
10.98


ATOM
1164
CG2
VAL
A
681
23.460
−3.423
31.346
1.00
12.93


ATOM
1165
C
VAL
A
681
20.426
−1.195
30.453
1.00
9.58


ATOM
1166
O
VAL
A
681
19.870
−0.378
31.185
1.00
10.02


ATOM
1167
N
LEU
A
681A
20.420
−1.094
29.128
1.00
9.51


ATOM
1168
CA
LEU
A
681A
19.718
−0.011
28.443
1.00
10.16


ATOM
1169
CB
LEU
A
681A
19.773
−0.216
26.929
1.00
7.24


ATOM
1170
CG
LEU
A
681A
21.079
0.035
26.178
1.00
9.74


ATOM
1171
CD1
LEU
A
681A
20.979
−0.563
24.788
1.00
13.02


ATOM
1172
CD2
LEU
A
681A
21.345
1.526
26.102
1.00
15.84


ATOM
1173
C
LEU
A
681A
18.253
0.049
28.851
1.00
8.34


ATOM
1174
O
LEU
A
681A
17.725
1.118
29.174
1.00
10.62


ATOM
1175
N
GLU
A
682
17.599
−1.110
28.834
1.00
10.08


ATOM
1176
CA
GLU
A
682
16.183
−1.191
29.161
1.00
7.57


ATOM
1177
CB
GLU
A
682
15.667
−2.599
28.855
1.00
6.60


ATOM
1178
CG
GLU
A
682
15.731
−2.954
27.348
1.00
8.78


ATOM
1179
CD
GLU
A
682
17.151
−3.199
26.835
1.00
12.12


ATOM
1180
OE1
GLU
A
682
18.001
−3.693
27.614
1.00
10.38


ATOM
1181
OE2
GLU
A
682
17.418
−2.919
25.646
1.00
10.27


ATOM
1182
C
GLU
A
682
15.867
−0.773
30.594
1.00
8.81


ATOM
1183
O
GLU
A
682
14.829
−0.158
30.854
1.00
7.94


ATOM
1184
N
HIS
A
683
16.752
−1.099
31.526
1.00
9.05


ATOM
1185
CA
HIS
A
683
16.531
−0.677
32.897
1.00
10.40


ATOM
1186
CB
HIS
A
683
17.561
−1.324
33.830
1.00
11.92


ATOM
1187
CG
HIS
A
683
17.161
−2.686
34.296
1.00
10.38


ATOM
1188
CD2
HIS
A
683
17.557
−3.920
33.903
1.00
9.93


ATOM
1189
ND1
HIS
A
683
16.172
−2.888
35.238
1.00
14.33


ATOM
1190
CE1
HIS
A
683
15.977
−4.183
35.400
1.00
7.54


ATOM
1191
NE2
HIS
A
683
16.806
−4.831
34.599
1.00
15.67


ATOM
1192
C
HIS
A
683
16.631
0.846
32.925
1.00
11.08


ATOM
1193
O
HIS
A
683
15.868
1.512
33.621
1.00
10.48


ATOM
1194
N
HIS
A
684
17.553
1.397
32.138
1.00
10.86


ATOM
1195
CA
HIS
A
684
17.710
2.844
32.076
1.00
9.98


ATOM
1196
CB
HIS
A
684
18.941
3.233
31.256
1.00
9.09


ATOM
1197
CG
HIS
A
684
19.229
4.697
31.284
1.00
8.54


ATOM
1198
CD2
HIS
A
684
19.399
5.555
32.322
1.00
5.20


ATOM
1199
ND1
HIS
A
684
19.313
5.467
30.142
1.00
17.15


ATOM
1200
CE1
HIS
A
684
19.518
6.728
30.474
1.00
9.30


ATOM
1201
NE2
HIS
A
684
19.573
6.807
31.795
1.00
15.79


ATOM
1202
C
HIS
A
684
16.473
3.502
31.465
1.00
9.44


ATOM
1203
O
HIS
A
684
16.020
4.542
31.941
1.00
11.75


ATOM
1204
N
HIS
A
685
15.929
2.898
30.411
1.00
9.42


ATOM
1205
CA
HIS
A
685
14.740
3.447
29.757
1.00
7.57


ATOM
1206
CB
HIS
A
685
14.361
2.621
28.521
1.00
14.86


ATOM
1207
CG
HIS
A
685
15.472
2.468
27.521
1.00
7.24


ATOM
1208
CD2
HIS
A
685
15.846
1.402
26.773
1.00
9.32


ATOM
1209
ND1
HIS
A
685
16.299
3.506
27.161
1.00
8.86


ATOM
1210
CE1
HIS
A
685
17.141
3.088
26.227
1.00
14.03


ATOM
1211
NE2
HIS
A
685
16.886
1.819
25.974
1.00
8.62


ATOM
1212
C
HIS
A
685
13.574
3.446
30.747
1.00
9.27


ATOM
1213
O
HIS
A
685
12.798
4.401
30.805
1.00
9.78


ATOM
1214
N
PHE
A
686
13.439
2.376
31.523
1.00
8.10


ATOM
1215
CA
PHE
A
686
12.351
2.314
32.507
1.00
10.05


ATOM
1216
CB
PHE
A
686
12.291
0.923
33.151
1.00
8.82


ATOM
1217
CG
PHE
A
686
11.281
0.808
34.263
1.00
10.55


ATOM
1218
CD1
PHE
A
686
9.937
1.078
34.035
1.00
10.53


ATOM
1219
CD2
PHE
A
686
11.674
0.442
35.538
1.00
11.42


ATOM
1220
CE1
PHE
A
686
9.013
0.985
35.061
1.00
14.12


ATOM
1221
CE2
PHE
A
686
10.754
0.348
36.568
1.00
15.20


ATOM
1222
CZ
PHE
A
686
9.423
0.618
36.328
1.00
13.66


ATOM
1223
C
PHE
A
686
12.554
3.391
33.570
1.00
9.59


ATOM
1224
O
PHE
A
686
11.599
4.036
34.022
1.00
11.10


ATOM
1225
N
ASP
A
687
13.807
3.603
33.965
1.00
10.38


ATOM
1226
CA
ASP
A
687
14.169
4.620
34.950
1.00
13.63


ATOM
1227
CB
ASP
A
687
15.699
4.646
35.147
1.00
15.63


ATOM
1228
CG
ASP
A
687
16.163
5.810
36.032
1.00
35.43


ATOM
1229
OD1
ASP
A
687
15.842
5.812
37.238
1.00
39.21


ATOM
1230
OD2
ASP
A
687
16.855
6.721
35.514
1.00
46.67


ATOM
1231
C
ASP
A
687
13.701
5.983
34.453
1.00
11.19


ATOM
1232
O
ASP
A
687
13.079
6.742
35.191
1.00
12.63


ATOM
1233
N
GLN
A
688
14.026
6.266
33.194
1.00
10.97


ATOM
1234
CA
GLN
A
688
13.664
7.531
32.571
1.00
10.87


ATOM
1235
CB
GLN
A
688
14.331
7.623
31.193
1.00
15.23


ATOM
1236
CG
GLN
A
688
15.844
7.876
31.260
1.00
11.96


ATOM
1237
CD
GLN
A
688
16.179
9.350
31.456
1.00
14.39


ATOM
1238
OE1
GLN
A
688
15.805
10.193
30.640
1.00
20.66


ATOM
1239
NE2
GLN
A
688
16.881
9.663
32.535
1.00
29.50


ATOM
1240
C
GLN
A
688
12.158
7.651
32.455
1.00
10.36


ATOM
1241
O
GLN
A
688
11.587
8.729
32.641
1.00
10.53


ATOM
1242
N
CYS
A
689
11.495
6.536
32.160
1.00
8.48


ATOM
1243
CA
CYS
A
689
10.043
6.517
32.040
1.00
9.59


ATOM
1244
CB
CYS
A
689
9.558
5.097
31.706
1.00
11.54


ATOM
1245
SG
CYS
A
689
7.772
4.940
31.573
1.00
11.98


ATOM
1246
C
CYS
A
689
9.406
7.005
33.343
1.00
10.54


ATOM
1247
O
CYS
A
689
8.559
7.905
33.331
1.00
10.86


ATOM
1248
N
LEU
A
690
9.822
6.417
34.463
1.00
12.43


ATOM
1249
CA
LEU
A
690
9.316
6.786
35.787
1.00
13.70


ATOM
1250
CB
LEU
A
690
9.968
5.912
36.863
1.00
15.35


ATOM
1251
CG
LEU
A
690
9.620
4.423
36.853
1.00
18.35


ATOM
1252
CD1
LEU
A
690
10.326
3.723
38.008
1.00
25.25


ATOM
1253
CD2
LEU
A
690
8.118
4.248
36.969
1.00
17.06


ATOM
1254
C
LEU
A
690
9.605
8.247
36.093
1.00
14.05


ATOM
1255
O
LEU
A
690
8.767
8.975
36.633
1.00
15.63


ATOM
1256
N
MET
A
691
10.817
8.681
35.750
1.00
13.87


ATOM
1257
CA
MET
A
691
11.256
10.042
35.975
1.00
14.41


ATOM
1258
CB
MET
A
691
12.676
10.212
35.411
1.00
14.62


ATOM
1259
CG
MET
A
691
13.371
11.496
35.757
1.00
32.36


ATOM
1260
SD
MET
A
691
12.902
12.755
34.635
1.00
45.55


ATOM
1261
CE
MET
A
691
13.918
12.471
33.200
1.00
37.72


ATOM
1262
C
MET
A
691
10.285
11.024
35.336
1.00
13.72


ATOM
1263
O
MET
A
691
9.863
11.990
35.971
1.00
14.45


ATOM
1264
N
ILE
A
692
9.903
10.758
34.091
1.00
10.48


ATOM
1265
CA
ILE
A
692
8.980
11.644
33.400
1.00
9.98


ATOM
1266
CB
ILE
A
692
8.966
11.371
31.895
1.00
10.00


ATOM
1267
CG2
ILE
A
692
7.909
12.240
31.224
1.00
12.51


ATOM
1268
CG1
ILE
A
692
10.346
11.691
31.315
1.00
14.40


ATOM
1269
CD1
ILE
A
692
10.482
11.400
29.841
1.00
19.81


ATOM
1270
C
ILE
A
692
7.578
11.534
33.973
1.00
10.09


ATOM
1271
O
ILE
A
692
6.906
12.547
34.166
1.00
11.41


ATOM
1272
N
LEU
A
693
7.149
10.316
34.288
1.00
12.13


ATOM
1273
CA
LEU
A
693
5.821
10.111
34.862
1.00
13.85


ATOM
1274
CB
LEU
A
693
5.548
8.615
35.058
1.00
13.96


ATOM
1275
CG
LEU
A
693
5.212
7.826
33.789
1.00
10.33


ATOM
1276
CD1
LEU
A
693
5.183
6.335
34.082
1.00
17.28


ATOM
1277
CD2
LEU
A
693
3.868
8.305
33.243
1.00
9.40


ATOM
1278
C
LEU
A
693
5.644
10.837
36.193
1.00
14.19


ATOM
1279
O
LEU
A
693
4.524
11.179
36.577
1.00
16.64


ATOM
1280
N
ASN
A
694
6.747
11.073
36.893
1.00
16.46


ATOM
1281
CA
ASN
A
694
6.697
11.755
38.183
1.00
16.63


ATOM
1282
CB
ASN
A
694
7.686
11.116
39.159
1.00
20.12


ATOM
1283
CG
ASN
A
694
7.231
9.760
39.641
1.00
24.99


ATOM
1284
OD1
ASN
A
694
7.869
8.742
39.373
1.00
30.33


ATOM
1285
ND2
ASN
A
694
6.115
9.736
40.360
1.00
25.93


ATOM
1286
C
ASN
A
694
6.989
13.247
38.101
1.00
18.31


ATOM
1287
O
ASN
A
694
6.855
13.958
39.093
1.00
18.26


ATOM
1288
N
SER
A
695
7.395
13.721
36.930
1.00
16.05


ATOM
1289
CA
SER
A
695
7.704
15.139
36.755
1.00
17.70


ATOM
1290
CB
SER
A
695
8.321
15.376
35.376
1.00
19.30


ATOM
1291
OG
SER
A
695
9.607
14.793
35.298
1.00
34.04


ATOM
1292
C
SER
A
695
6.471
16.022
36.914
1.00
15.83


ATOM
1293
O
SER
A
695
5.400
15.710
36.406
1.00
17.46


ATOM
1294
N
PRO
A
696
6.611
17.144
37.630
1.00
18.97


ATOM
1295
CD
PRO
A
696
7.779
17.577
38.415
1.00
26.97


ATOM
1296
CA
PRO
A
696
5.480
18.053
37.830
1.00
18.99


ATOM
1297
CB
PRO
A
696
6.113
19.220
38.579
1.00
22.14


ATOM
1298
CG
PRO
A
696
7.154
18.534
39.414
1.00
28.71


ATOM
1299
C
PRO
A
696
4.866
18.480
36.498
1.00
16.02


ATOM
1300
O
PRO
A
696
5.585
18.839
35.564
1.00
18.08


ATOM
1301
N
GLY
A
697
3.539
18.425
36.418
1.00
16.17


ATOM
1302
CA
GLY
A
697
2.843
18.804
35.201
1.00
16.65


ATOM
1303
C
GLY
A
697
2.862
17.725
34.130
1.00
14.72


ATOM
1304
O
GLY
A
697
2.283
17.901
33.060
1.00
15.86


ATOM
1305
N
ASN
A
698
3.511
16.601
34.424
1.00
14.68


ATOM
1306
CA
ASN
A
698
3.621
15.493
33.471
1.00
14.66


ATOM
1307
CB
ASN
A
698
5.099
15.209
33.174
1.00
15.25


ATOM
1308
CG
ASN
A
698
5.760
16.304
32.365
1.00
19.94


ATOM
1309
OD1
ASN
A
698
5.883
16.199
31.146
1.00
13.89


ATOM
1310
ND2
ASN
A
698
6.186
17.367
33.039
1.00
16.33


ATOM
1311
C
ASN
A
698
2.990
14.198
33.973
1.00
14.82


ATOM
1312
O
ASN
A
698
3.044
13.174
33.293
1.00
13.20


ATOM
1313
N
GLN
A
699
2.379
14.243
35.151
1.00
13.46


ATOM
1314
CA
GLN
A
699
1.807
13.041
35.749
1.00
14.53


ATOM
1315
CB
GLN
A
699
1.652
13.281
37.251
1.00
16.25


ATOM
1316
CG
GLN
A
699
2.957
13.713
37.902
1.00
17.08


ATOM
1317
CD
GLN
A
699
2.787
14.103
39.350
1.00
37.15


ATOM
1318
OE1
GLN
A
699
2.147
15.105
39.661
1.00
41.13


ATOM
1319
NE2
GLN
A
699
3.357
13.307
40.248
1.00
41.91


ATOM
1320
C
GLN
A
699
0.499
12.522
35.158
1.00
13.96


ATOM
1321
O
GLN
A
699
−0.567
12.676
35.754
1.00
15.67


ATOM
1322
N
ILE
A
700
0.582
11.867
34.003
1.00
13.44


ATOM
1323
CA
ILE
A
700
−0.617
11.348
33.356
1.00
14.25


ATOM
1324
CB
ILE
A
700
−0.345
10.974
31.881
1.00
15.57


ATOM
1325
CG2
ILE
A
700
0.010
12.222
31.086
1.00
15.78


ATOM
1326
CG1
ILE
A
700
0.777
9.941
31.793
1.00
16.74


ATOM
1327
CD1
ILE
A
700
0.940
9.361
30.407
1.00
12.98


ATOM
1328
C
ILE
A
700
−1.262
10.151
34.064
1.00
13.88


ATOM
1329
O
ILE
A
700
−2.342
9.709
33.673
1.00
14.53


ATOM
1330
N
LEU
A
701
−0.609
9.624
35.098
1.00
11.60


ATOM
1331
CA
LEU
A
701
−1.169
8.495
35.845
1.00
14.58


ATOM
1332
CB
LEU
A
701
−0.150
7.358
35.965
1.00
13.85


ATOM
1333
CG
LEU
A
701
0.310
6.673
34.677
1.00
11.07


ATOM
1334
CD1
LEU
A
701
1.270
5.539
35.031
1.00
13.34


ATOM
1335
CD2
LEU
A
701
−0.895
6.128
33.921
1.00
12.89


ATOM
1336
C
LEU
A
701
−1.612
8.914
37.247
1.00
13.75


ATOM
1337
O
LEU
A
701
−2.053
8.084
38.040
1.00
15.74


ATOM
1338
N
SER
A
702
−1.497
10.201
37.547
1.00
15.74


ATOM
1339
CA
SER
A
702
−1.872
10.717
38.860
1.00
18.36


ATOM
1340
CB
SER
A
702
−1.573
12.217
38.949
1.00
20.19


ATOM
1341
OG
SER
A
702
−2.446
12.958
38.113
1.00
21.94


ATOM
1342
C
SER
A
702
−3.347
10.490
39.176
1.00
19.34


ATOM
1343
O
SER
A
702
−3.754
10.559
40.336
1.00
20.75


ATOM
1344
N
GLY
A
703
−4.144
10.224
38.148
1.00
18.92


ATOM
1345
CA
GLY
A
703
−5.565
10.012
38.359
1.00
20.40


ATOM
1346
C
GLY
A
703
−5.944
8.600
38.764
1.00
21.19


ATOM
1347
O
GLY
A
703
−7.036
8.369
39.284
1.00
20.43


ATOM
1348
N
LEU
A
704
−5.045
7.649
38.539
1.00
16.00


ATOM
1349
CA
LEU
A
704
−5.326
6.259
38.876
1.00
15.59


ATOM
1350
CB
LEU
A
704
−4.262
5.335
38.278
1.00
9.29


ATOM
1351
CG
LEU
A
704
−4.459
4.921
36.823
1.00
14.10


ATOM
1352
CD1
LEU
A
704
−4.510
6.143
35.926
1.00
17.73


ATOM
1353
CD2
LEU
A
704
−3.312
3.998
36.418
1.00
11.19


ATOM
1354
C
LEU
A
704
−5.419
5.993
40.368
1.00
16.40


ATOM
1355
O
LEU
A
704
−4.773
6.659
41.178
1.00
16.88


ATOM
1356
N
SER
A
705
−6.233
5.004
40.721
1.00
15.43


ATOM
1357
CA
SER
A
705
−6.395
4.621
42.111
1.00
15.96


ATOM
1358
CB
SER
A
705
−7.556
3.640
42.268
1.00
15.57


ATOM
1359
OG
SER
A
705
−7.242
2.402
41.658
1.00
15.44


ATOM
1360
C
SER
A
705
−5.092
3.947
42.515
1.00
16.32


ATOM
1361
O
SER
A
705
−4.280
3.583
41.662
1.00
17.25


ATOM
1362
N
ILE
A
706
−4.886
3.782
43.812
1.00
17.56


ATOM
1363
CA
ILE
A
706
−3.666
3.164
44.292
1.00
16.88


ATOM
1364
CB
ILE
A
706
−3.679
3.086
45.836
1.00
21.33


ATOM
1365
CG2
ILE
A
706
−2.466
2.331
46.335
1.00
23.53


ATOM
1366
CG1
ILE
A
706
−3.712
4.507
46.411
1.00
21.96


ATOM
1367
CD1
ILE
A
706
−3.892
4.577
47.918
1.00
22.24


ATOM
1368
C
ILE
A
706
−3.415
1.782
43.685
1.00
16.48


ATOM
1369
O
ILE
A
706
−2.291
1.470
43.291
1.00
18.62


ATOM
1370
N
GLU
A
707
−4.456
0.962
43.584
1.00
15.92


ATOM
1371
CA
GLU
A
707
−4.304
−0.376
43.019
1.00
14.53


ATOM
1372
CB
GLU
A
707
−5.509
−1.250
43.378
1.00
19.33


ATOM
1373
CG
GLU
A
707
−5.518
−1.682
44.836
1.00
24.82


ATOM
1374
CD
GLU
A
707
−4.269
−2.460
45.214
1.00
31.26


ATOM
1375
OE1
GLU
A
707
−4.029
−3.525
44.610
1.00
34.47


ATOM
1376
OE2
GLU
A
707
−3.525
−2.006
46.110
1.00
30.79


ATOM
1377
C
GLU
A
707
−4.093
−0.385
41.507
1.00
14.27


ATOM
1378
O
GLU
A
707
−3.283
−1.156
41.002
1.00
15.02


ATOM
1379
N
GLU
A
708
−4.818
0.458
40.782
1.00
11.81


ATOM
1380
CA
GLU
A
708
−4.644
0.495
39.337
1.00
12.49


ATOM
1381
CB
GLU
A
708
−5.756
1.317
38.673
1.00
14.73


ATOM
1382
CG
GLU
A
708
−7.134
0.663
38.813
1.00
11.98


ATOM
1383
CD
GLU
A
708
−8.088
1.020
37.683
1.00
18.01


ATOM
1384
OE1
GLU
A
708
−8.121
2.196
37.274
1.00
19.76


ATOM
1385
OE2
GLU
A
708
−8.816
0.120
37.216
1.00
22.22


ATOM
1386
C
GLU
A
708
−3.264
1.054
38.996
1.00
14.00


ATOM
1387
O
GLU
A
708
−2.624
0.607
38.047
1.00
12.79


ATOM
1388
N
TYR
A
709
−2.798
2.018
39.784
1.00
12.70


ATOM
1389
CA
TYR
A
709
−1.482
2.604
39.551
1.00
13.42


ATOM
1390
CB
TYR
A
709
−1.204
3.724
40.557
1.00
12.05


ATOM
1391
CG
TYR
A
709
0.129
4.407
40.339
1.00
19.13


ATOM
1392
CD1
TYR
A
709
0.311
5.302
39.296
1.00
14.81


ATOM
1393
CE1
TYR
A
709
1.530
5.928
39.091
1.00
15.81


ATOM
1394
CD2
TYR
A
709
1.207
4.149
41.174
1.00
17.39


ATOM
1395
CE2
TYR
A
709
2.427
4.767
40.978
1.00
18.97


ATOM
1396
CZ
TYR
A
709
2.583
5.658
39.934
1.00
17.67


ATOM
1397
OH
TYR
A
709
3.793
6.284
39.737
1.00
18.77


ATOM
1398
C
TYR
A
709
−0.424
1.515
39.708
1.00
15.44


ATOM
1399
O
TYR
A
709
0.452
1.348
38.855
1.00
15.06


ATOM
1400
N
LYS
A
710
−0.520
0.774
40.808
1.00
15.25


ATOM
1401
CA
LYS
A
710
0.409
−0.311
41.095
1.00
15.31


ATOM
1402
CB
LYS
A
710
−0.020
−1.026
42.379
1.00
22.10


ATOM
1403
CG
LYS
A
710
0.809
−2.249
42.716
1.00
23.74


ATOM
1404
CD
LYS
A
710
0.299
−2.931
43.978
1.00
33.24


ATOM
1405
CE
LYS
A
710
0.996
−4.263
44.204
1.00
39.08


ATOM
1406
NZ
LYS
A
710
2.478
−4.117
44.248
1.00
42.37


ATOM
1407
C
LYS
A
710
0.474
−1.309
39.939
1.00
14.94


ATOM
1408
O
LYS
A
710
1.555
−1.645
39.448
1.00
12.87


ATOM
1409
N
THR
A
711
−0.692
−1.777
39.506
1.00
13.50


ATOM
1410
CA
THR
A
711
−0.783
−2.736
38.411
1.00
12.45


ATOM
1411
CB
THR
A
711
−2.249
−3.092
38.128
1.00
17.44


ATOM
1412
OG1
THR
A
711
−2.791
−3.792
39.255
1.00
21.96


ATOM
1413
CG2
THR
A
711
−2.365
−3.953
36.872
1.00
16.75


ATOM
1414
C
THR
A
711
−0.161
−2.198
37.129
1.00
11.72


ATOM
1415
O
THR
A
711
0.597
−2.896
36.442
1.00
13.19


ATOM
1416
N
THR
A
712
−0.487
−0.954
36.809
1.00
11.15


ATOM
1417
CA
THR
A
712
0.015
−0.319
35.599
1.00
13.99


ATOM
1418
CB
THR
A
712
−0.598
1.081
35.424
1.00
9.97


ATOM
1419
OG1
THR
A
712
−2.029
0.967
35.357
1.00
14.40


ATOM
1420
CG2
THR
A
712
−0.088
1.729
34.133
1.00
12.92


ATOM
1421
C
THR
A
712
1.541
−0.221
35.556
1.00
12.77


ATOM
1422
O
THR
A
712
2.158
−0.596
34.559
1.00
12.54


ATOM
1423
N
LEU
A
713
2.156
0.275
36.625
1.00
12.50


ATOM
1424
CA
LEU
A
713
3.612
0.384
36.638
1.00
11.02


ATOM
1425
CB
LEU
A
713
4.105
1.023
37.940
1.00
13.58


ATOM
1426
CG
LEU
A
713
3.889
2.528
38.100
1.00
22.03


ATOM
1427
CD1
LEU
A
713
4.754
3.042
39.250
1.00
21.64


ATOM
1428
CD2
LEU
A
713
4.261
3.241
36.809
1.00
27.88


ATOM
1429
C
LEU
A
713
4.298
−0.967
36.438
1.00
13.04


ATOM
1430
O
LEU
A
713
5.340
−1.048
35.785
1.00
12.26


ATOM
1431
N
LYS
A
714
3.718
−2.026
36.995
1.00
11.66


ATOM
1432
CA
LYS
A
714
4.304
−3.356
36.852
1.00
12.24


ATOM
1433
CB
LYS
A
714
3.540
−4.383
37.690
1.00
17.46


ATOM
1434
CG
LYS
A
714
3.582
−4.123
39.182
1.00
27.51


ATOM
1435
CD
LYS
A
714
2.878
−5.236
39.939
1.00
33.99


ATOM
1436
CE
LYS
A
714
2.899
−4.988
41.433
1.00
42.93


ATOM
1437
NZ
LYS
A
714
2.222
−6.092
42.168
1.00
46.33


ATOM
1438
C
LYS
A
714
4.284
−3.784
35.390
1.00
12.70


ATOM
1439
O
LYS
A
714
5.259
−4.338
34.886
1.00
12.91


ATOM
1440
N
ILE
A
715
3.168
−3.525
34.717
1.00
10.95


ATOM
1441
CA
ILE
A
715
3.023
−3.869
33.308
1.00
10.57


ATOM
1442
CB
ILE
A
715
1.586
−3.590
32.820
1.00
11.39


ATOM
1443
CG2
ILE
A
715
1.468
−3.896
31.339
1.00
11.35


ATOM
1444
CG1
ILE
A
715
0.596
−4.450
33.613
1.00
12.69


ATOM
1445
CD1
ILE
A
715
−0.854
−4.130
33.332
1.00
13.44


ATOM
1446
C
ILE
A
715
4.017
−3.052
32.482
1.00
10.34


ATOM
1447
O
ILE
A
715
4.676
−3.581
31.588
1.00
11.86


ATOM
1448
N
ILE
A
716
4.133
−1.762
32.793
1.00
10.78


ATOM
1449
CA
ILE
A
716
5.069
−0.886
32.081
1.00
9.90


ATOM
1450
CB
ILE
A
716
4.989
0.563
32.621
1.00
10.08


ATOM
1451
CG2
ILE
A
716
6.171
1.387
32.115
1.00
10.86


ATOM
1452
CG1
ILE
A
716
3.661
1.197
32.189
1.00
10.91


ATOM
1453
CD1
ILE
A
716
3.413
2.564
32.792
1.00
11.27


ATOM
1454
C
ILE
A
716
6.508
−1.393
32.196
1.00
8.77


ATOM
1455
O
ILE
A
716
7.229
−1.487
31.199
1.00
9.34


ATOM
1456
N
LYS
A
717
6.926
−1.724
33.413
1.00
9.18


ATOM
1457
CA
LYS
A
717
8.275
−2.235
33.623
1.00
10.88


ATOM
1458
CB
LYS
A
717
8.489
−2.606
35.087
1.00
12.47


ATOM
1459
CG
LYS
A
717
9.790
−3.366
35.337
1.00
14.78


ATOM
1460
CD
LYS
A
717
9.865
−3.864
36.775
1.00
17.70


ATOM
1461
CE
LYS
A
717
11.045
−4.809
36.977
1.00
29.85


ATOM
1462
NZ
LYS
A
717
11.082
−5.374
38.355
1.00
25.71


ATOM
1463
C
LYS
A
717
8.540
−3.469
32.752
1.00
10.54


ATOM
1464
O
LYS
A
717
9.536
−3.524
32.041
1.00
10.05


ATOM
1465
N
GLN
A
718
7.647
−4.451
32.847
1.00
11.40


ATOM
1466
CA
GLN
A
718
7.774
−5.682
32.067
1.00
11.80


ATOM
1467
CB
GLN
A
718
6.635
−6.628
32.434
1.00
11.33


ATOM
1468
CG
GLN
A
718
6.683
−6.965
33.899
1.00
14.75


ATOM
1469
CD
GLN
A
718
7.954
−7.691
34.293
1.00
35.80


ATOM
1470
OE1
GLN
A
718
8.774
−7.176
35.053
1.00
49.66


ATOM
1471
NE2
GLN
A
718
8.115
−8.909
33.784
1.00
43.62


ATOM
1472
C
GLN
A
718
7.778
−5.422
30.559
1.00
9.82


ATOM
1473
O
GLN
A
718
8.559
−6.027
29.831
1.00
9.86


ATOM
1474
N
ALA
A
719
6.920
−4.518
30.108
1.00
8.83


ATOM
1475
CA
ALA
A
719
6.842
−4.205
28.686
1.00
10.49


ATOM
1476
CB
ALA
A
719
5.657
−3.292
28.436
1.00
5.96


ATOM
1477
C
ALA
A
719
8.129
−3.560
28.186
1.00
9.98


ATOM
1478
O
ALA
A
719
8.618
−3.892
27.101
1.00
9.19


ATOM
1479
N
ILE
A
720
8.688
−2.641
28.971
1.00
7.25


ATOM
1480
CA
ILE
A
720
9.920
−1.988
28.548
1.00
8.66


ATOM
1481
CB
ILE
A
720
10.233
−0.753
29.426
1.00
10.86


ATOM
1482
CG2
ILE
A
720
11.616
−0.193
29.086
1.00
11.64


ATOM
1483
CG1
ILE
A
720
9.164
0.320
29.181
1.00
11.59


ATOM
1484
CD1
ILE
A
720
9.367
1.605
29.976
1.00
12.21


ATOM
1485
C
ILE
A
720
11.085
−2.974
28.580
1.00
10.02


ATOM
1486
O
ILE
A
720
11.883
−3.040
27.641
1.00
8.95


ATOM
1487
N
LEU
A
721
11.178
−3.762
29.643
1.00
8.10


ATOM
1488
CA
LEU
A
721
12.264
−4.733
29.719
1.00
8.45


ATOM
1489
CB
LEU
A
721
12.251
−5.446
31.077
1.00
10.55


ATOM
1490
CG
LEU
A
721
12.613
−4.553
32.267
1.00
13.26


ATOM
1491
CD1
LEU
A
721
12.539
−5.350
33.574
1.00
15.78


ATOM
1492
CD2
LEU
A
721
14.006
−3.991
32.059
1.00
24.08


ATOM
1493
C
LEU
A
721
12.173
−5.750
28.576
1.00
9.96


ATOM
1494
O
LEU
A
721
13.195
−6.196
28.049
1.00
8.91


ATOM
1495
N
ALA
A
722
10.948
−6.082
28.175
1.00
8.77


ATOM
1496
CA
ALA
A
722
10.715
−7.047
27.100
1.00
8.74


ATOM
1497
CB
ALA
A
722
9.219
−7.218
26.879
1.00
9.06


ATOM
1498
C
ALA
A
722
11.383
−6.648
25.786
1.00
10.10


ATOM
1499
O
ALA
A
722
11.704
−7.507
24.965
1.00
13.26


ATOM
1500
N
THR
A
723
11.598
−5.350
25.585
1.00
8.97


ATOM
1501
CA
THR
A
723
12.213
−4.884
24.344
1.00
10.94


ATOM
1502
CB
THR
A
723
11.943
−3.374
24.127
1.00
8.53


ATOM
1503
OG1
THR
A
723
12.542
−2.615
25.181
1.00
8.41


ATOM
1504
CG2
THR
A
723
10.437
−3.114
24.118
1.00
8.22


ATOM
1505
C
THR
A
723
13.713
−5.187
24.203
1.00
9.21


ATOM
1506
O
THR
A
723
14.327
−4.862
23.186
1.00
12.03


ATOM
1507
N
ASP
A
724
14.308
−5.797
25.223
1.00
9.75


ATOM
1508
CA
ASP
A
724
15.710
−6.203
25.133
1.00
7.82


ATOM
1509
CB
ASP
A
724
16.257
−6.533
26.525
1.00
12.18


ATOM
1510
CG
ASP
A
724
17.648
−7.147
26.490
1.00
8.16


ATOM
1511
OD1
ASP
A
724
18.232
−7.299
25.394
1.00
11.70


ATOM
1512
OD2
ASP
A
724
18.161
−7.481
27.581
1.00
11.61


ATOM
1513
C
ASP
A
724
15.600
−7.475
24.293
1.00
8.26


ATOM
1514
O
ASP
A
724
15.022
−8.459
24.742
1.00
10.28


ATOM
1515
N
LEU
A
725
16.127
−7.452
23.073
1.00
9.50


ATOM
1516
CA
LEU
A
725
16.037
−8.611
22.189
1.00
8.83


ATOM
1517
CB
LEU
A
725
16.791
−8.343
20.883
1.00
11.33


ATOM
1518
CG
LEU
A
725
16.365
−9.236
19.717
1.00
16.17


ATOM
1519
CD1
LEU
A
725
14.910
−8.953
19.367
1.00
12.02


ATOM
1520
CD2
LEU
A
725
17.262
−8.974
18.516
1.00
20.09


ATOM
1521
C
LEU
A
725
16.573
−9.880
22.849
1.00
12.30


ATOM
1522
O
LEU
A
725
16.179
−10.994
22.498
1.00
11.52


ATOM
1523
N
ALA
A
726
17.476
−9.712
23.806
1.00
11.08


ATOM
1524
CA
ALA
A
726
18.028
−10.855
24.517
1.00
12.63


ATOM
1525
CB
ALA
A
726
19.104
−10.394
25.489
1.00
21.41


ATOM
1526
C
ALA
A
726
16.918
−11.583
25.274
1.00
12.40


ATOM
1527
O
ALA
A
726
16.914
−12.813
25.354
1.00
13.56


ATOM
1528
N
LEU
A
727
15.985
−10.823
25.843
1.00
12.79


ATOM
1529
CA
LEU
A
727
14.884
−11.421
26.591
1.00
14.99


ATOM
1530
CB
LEU
A
727
14.206
−10.380
27.485
1.00
11.71


ATOM
1531
CG
LEU
A
727
15.096
−9.856
28.612
1.00
16.19


ATOM
1532
CD1
LEU
A
727
14.302
−8.925
29.511
1.00
13.74


ATOM
1533
CD2
LEU
A
727
15.631
−11.036
29.409
1.00
19.43


ATOM
1534
C
LEU
A
727
13.868
−12.045
25.646
1.00
15.02


ATOM
1535
O
LEU
A
727
13.173
−12.996
26.005
1.00
15.57


ATOM
1536
N
TYR
A
728
13.777
−11.500
24.438
1.00
12.38


ATOM
1537
CA
TYR
A
728
12.862
−12.038
23.435
1.00
12.71


ATOM
1538
CB
TYR
A
728
12.844
−11.136
22.194
1.00
10.64


ATOM
1539
CG
TYR
A
728
12.303
−11.823
20.960
1.00
12.57


ATOM
1540
CD1
TYR
A
728
10.966
−12.197
20.875
1.00
14.71


ATOM
1541
CE1
TYR
A
728
10.473
−12.854
19.752
1.00
12.42


ATOM
1542
CD2
TYR
A
728
13.139
−12.124
19.888
1.00
13.44


ATOM
1543
CE2
TYR
A
728
12.659
−12.777
18.763
1.00
13.13


ATOM
1544
CZ
TYR
A
728
11.329
−13.142
18.699
1.00
15.27


ATOM
1545
OH
TYR
A
728
10.857
−13.801
17.580
1.00
18.62


ATOM
1546
C
TYR
A
728
13.350
−13.430
23.041
1.00
12.62


ATOM
1547
O
TYR
A
728
12.588
−14.401
23.028
1.00
14.23


ATOM
1548
N
ILE
A
729
14.636
−13.522
22.723
1.00
12.98


ATOM
1549
CA
ILE
A
729
15.232
−14.788
22.327
1.00
13.19


ATOM
1550
CB
ILE
A
729
16.723
−14.595
21.983
1.00
14.56


ATOM
1551
CG2
ILE
A
729
17.395
−15.942
21.797
1.00
19.39


ATOM
1552
CG1
ILE
A
729
16.849
−13.727
20.727
1.00
18.02


ATOM
1553
CD1
ILE
A
729
18.268
−13.309
20.406
1.00
26.38


ATOM
1554
C
ILE
A
729
15.088
−15.826
23.439
1.00
15.70


ATOM
1555
O
ILE
A
729
14.830
−17.001
23.178
1.00
14.36


ATOM
1556
N
LYS
A
730
15.227
−15.375
24.681
1.00
15.21


ATOM
1557
CA
LYS
A
730
15.127
−16.257
25.837
1.00
16.44


ATOM
1558
CB
LYS
A
730
15.657
−15.528
27.075
1.00
21.43


ATOM
1559
CG
LYS
A
730
15.494
−16.291
28.376
1.00
27.38


ATOM
1560
CD
LYS
A
730
16.133
−15.528
29.523
1.00
31.22


ATOM
1561
CE
LYS
A
730
15.975
−16.267
30.839
1.00
36.43


ATOM
1562
NZ
LYS
A
730
16.672
−15.556
31.947
1.00
41.27


ATOM
1563
C
LYS
A
730
13.727
−16.802
26.133
1.00
16.48


ATOM
1564
O
LYS
A
730
13.573
−17.972
26.498
1.00
17.06


ATOM
1565
N
ARG
A
731
12.707
−15.969
25.968
1.00
14.55


ATOM
1566
CA
ARG
A
731
11.347
−16.395
26.283
1.00
15.57


ATOM
1567
CB
ARG
A
731
10.622
−15.291
27.060
1.00
19.59


ATOM
1568
CG
ARG
A
731
11.309
−14.842
28.335
1.00
18.25


ATOM
1569
CD
ARG
A
731
10.437
−13.846
29.086
1.00
33.93


ATOM
1570
NE
ARG
A
731
9.209
−14.462
29.588
1.00
32.78


ATOM
1571
CZ
ARG
A
731
8.168
−13.781
30.058
1.00
29.98


ATOM
1572
NH1
ARG
A
731
8.197
−12.456
30.091
1.00
30.21


ATOM
1573
NH2
ARG
A
731
7.097
−14.426
30.501
1.00
36.09


ATOM
1574
C
ARG
A
731
10.461
−16.807
25.118
1.00
12.75


ATOM
1575
O
ARG
A
731
9.436
−17.454
25.325
1.00
15.30


ATOM
1576
N
ARG
A
732
10.841
−16.445
23.897
1.00
13.21


ATOM
1577
CA
ARG
A
732
10.002
−16.759
22.751
1.00
11.06


ATOM
1578
CB
ARG
A
732
10.589
−16.162
21.474
1.00
10.97


ATOM
1579
CG
ARG
A
732
11.872
−16.812
21.021
1.00
12.09


ATOM
1580
CD
ARG
A
732
12.325
−16.192
19.724
1.00
12.79


ATOM
1581
NE
ARG
A
732
13.525
−16.822
19.193
1.00
13.80


ATOM
1582
CZ
ARG
A
732
13.919
−16.704
17.930
1.00
20.20


ATOM
1583
NH1
ARG
A
732
13.201
−15.980
17.077
1.00
23.11


ATOM
1584
NE2
ARG
A
732
15.025
−17.307
17.518
1.00
22.17


ATOM
1585
C
ARG
A
732
9.751
−18.245
22.549
1.00
11.37


ATOM
1586
O
ARG
A
732
8.704
−18.625
22.031
1.00
11.95


ATOM
1587
N
GLY
A
733
10.703
−19.078
22.962
1.00
13.25


ATOM
1588
CA
GLY
A
733
10.543
−20.512
22.804
1.00
13.40


ATOM
1589
C
GLY
A
733
9.298
−21.009
23.508
1.00
14.10


ATOM
1590
O
GLY
A
733
8.543
−21.823
22.970
1.00
15.18


ATOM
1591
N
GLU
A
734
9.080
−20.512
24.719
1.00
11.89


ATOM
1592
CA
GLU
A
734
7.919
−20.900
25.505
1.00
14.43


ATOM
1593
CB
GLU
A
734
7.988
−20.264
26.895
1.00
14.05


ATOM
1594
CG
GLU
A
734
6.675
−20.312
27.661
1.00
18.08


ATOM
1595
CD
GLU
A
734
6.810
−19.828
29.091
1.00
21.97


ATOM
1596
OE1
GLU
A
734
7.742
−19.048
29.372
1.00
19.31


ATOM
1597
OE2
GLU
A
734
5.977
−20.221
29.932
1.00
32.96


ATOM
1598
C
GLU
A
734
6.632
−20.478
24.806
1.00
14.65


ATOM
1599
O
GLU
A
734
5.663
−21.235
24.760
1.00
14.67


ATOM
1600
N
PHE
A
735
6.631
−19.264
24.267
1.00
15.01


ATOM
1601
CA
PHE
A
735
5.470
−18.729
23.566
1.00
11.90


ATOM
1602
CB
PHE
A
735
5.743
−17.278
23.157
1.00
11.17


ATOM
1603
CG
PHE
A
735
4.632
−16.635
22.366
1.00
16.06


ATOM
1604
CD1
PHE
A
735
3.354
−16.515
22.892
1.00
16.32


ATOM
1605
CD2
PHE
A
735
4.885
−16.102
21.111
1.00
13.68


ATOM
1606
CE1
PHE
A
735
2.355
−15.869
22.178
1.00
13.80


ATOM
1607
CE2
PHE
A
735
3.897
−15.458
20.400
1.00
12.16


ATOM
1608
CZ
PHE
A
735
2.631
−15.340
20.931
1.00
14.03


ATOM
1609
C
PHE
A
735
5.142
−19.566
22.329
1.00
13.78


ATOM
1610
O
PHE
A
735
3.989
−19.946
22.117
1.00
13.01


ATOM
1611
N
PHE
A
736
6.156
−19.853
21.517
1.00
12.56


ATOM
1612
CA
PHE
A
736
5.952
−20.632
20.299
1.00
14.09


ATOM
1613
CB
PHE
A
736
7.242
−20.691
19.472
1.00
15.66


ATOM
1614
CG
PHE
A
736
7.752
−19.342
19.031
1.00
17.77


ATOM
1615
CD1
PHE
A
736
6.888
−18.268
18.894
1.00
16.30


ATOM
1616
CD2
PHE
A
736
9.092
−19.166
18.701
1.00
14.18


ATOM
1617
CE1
PHE
A
736
7.345
−17.040
18.435
1.00
13.31


ATOM
1618
CE2
PHE
A
736
9.558
−17.939
18.242
1.00
13.12


ATOM
1619
CZ
PHE
A
736
8.686
−16.877
18.106
1.00
17.60


ATOM
1620
C
PHE
A
736
5.483
−22.054
20.598
1.00
14.02


ATOM
1621
O
PHE
A
736
4.653
−22.608
19.874
1.00
15.27


ATOM
1622
N
GLU
A
737
6.022
−22.640
21.661
1.00
15.53


ATOM
1623
CA
GLU
A
737
5.667
−24.000
22.047
1.00
16.49


ATOM
1624
CB
GLU
A
737
6.598
−24.493
23.155
1.00
18.16


ATOM
1625
CG
GLU
A
737
6.296
−25.908
23.623
1.00
32.20


ATOM
1626
CD
GLU
A
737
7.266
−26.397
24.685
1.00
44.41


ATOM
1627
OE1
GLU
A
737
7.368
−25.748
25.748
1.00
43.95


ATOM
1628
OE2
GLU
A
737
7.926
−27.433
24.457
1.00
45.00


ATOM
1629
C
GLU
A
737
4.219
−24.105
22.505
1.00
16.86


ATOM
1630
O
GLU
A
737
3.517
−25.050
22.137
1.00
18.64


ATOM
1631
N
LEU
A
738
3.774
−23.144
23.308
1.00
15.93


ATOM
1632
CA
LEU
A
738
2.396
−23.140
23.791
1.00
14.96


ATOM
1633
CB
LEU
A
738
2.137
−21.910
24.665
1.00
13.51


ATOM
1634
CG
LEU
A
738
2.817
−21.890
26.037
1.00
13.44


ATOM
1635
CD1
LEU
A
738
2.813
−20.474
26.589
1.00
14.08


ATOM
1636
CD2
LEU
A
738
2.103
−22.844
26.987
1.00
21.77


ATOM
1637
C
LEU
A
738
1.435
−23.137
22.610
1.00
15.65


ATOM
1638
O
LEU
A
738
0.431
−23.854
22.610
1.00
17.64


ATOM
1639
N
ILE
A
739
1.743
−22.323
21.604
1.00
13.75


ATOM
1640
CA
ILE
A
739
0.904
−22.236
20.415
1.00
14.28


ATOM
1641
CB
ILE
A
739
1.388
−21.112
19.464
1.00
12.79


ATOM
1642
CG2
ILE
A
739
0.686
−21.224
18.118
1.00
23.84


ATOM
1643
CG1
ILE
A
739
1.122
−19.744
20.096
1.00
16.58


ATOM
1644
CD1
ILE
A
739
1.656
−18.576
19.279
1.00
13.81


ATOM
1645
C
ILE
A
739
0.925
−23.557
19.654
1.00
16.17


ATOM
1646
O
ILE
A
739
−0.126
−24.107
19.309
1.00
18.24


ATOM
1647
N
ARG
A
740
2.124
−24.075
19.410
1.00
15.35


ATOM
1648
CA
ARG
A
740
2.274
−25.322
18.671
1.00
18.48


ATOM
1649
CB
ARG
A
740
3.758
−25.648
18.474
1.00
23.15


ATOM
1650
CG
ARG
A
740
3.996
−26.804
17.508
1.00
35.46


ATOM
1651
CD
ARG
A
740
5.475
−27.059
17.224
1.00
39.66


ATOM
1652
NE
ARG
A
740
6.174
−27.694
18.340
1.00
40.53


ATOM
1653
CZ
ARG
A
740
6.703
−27.043
19.371
1.00
42.20


ATOM
1654
NH1
ARG
A
740
6.623
−25.721
19.441
1.00
52.88


ATOM
1655
NH2
ARG
A
740
7.317
−27.718
20.335
1.00
44.19


ATOM
1656
C
ARG
A
740
1.582
−26.495
19.360
1.00
19.41


ATOM
1657
O
ARG
A
740
1.093
−27.410
18.698
1.00
18.06


ATOM
1658
N
LYS
A
741
1.539
−26.470
20.686
1.00
18.03


ATOM
1659
CA
LYS
A
741
0.906
−27.553
21.430
1.00
18.11


ATOM
1660
CB
LYS
A
741
1.696
−27.853
22.699
1.00
14.50


ATOM
1661
CG
LYS
A
741
3.074
−28.426
22.451
1.00
21.67


ATOM
1662
CD
LYS
A
741
3.717
−28.812
23.763
1.00
23.36


ATOM
1663
CE
LYS
A
741
5.087
−29.430
23.558
1.00
27.38


ATOM
1664
NZ
LYS
A
741
5.715
−29.747
24.871
1.00
23.91


ATOM
1665
C
LYS
A
741
−0.540
−27.248
21.798
1.00
17.80


ATOM
1666
O
LYS
A
741
−1.134
−27.940
22.623
1.00
18.63


ATOM
1667
N
ASN
A
742
−1.102
−26.214
21.183
1.00
17.40


ATOM
1668
CA
ASN
A
742
−2.478
−25.822
21.456
1.00
17.84


ATOM
1669
CB
ASN
A
742
−3.443
−26.841
20.849
1.00
16.88


ATOM
1670
CG
ASN
A
742
−3.442
−26.801
19.335
1.00
15.02


ATOM
1671
OD1
ASN
A
742
−3.741
−25.772
18.733
1.00
28.97


ATOM
1672
ND2
ASN
A
742
−3.100
−27.923
18.709
1.00
20.44


ATOM
1673
C
ASN
A
742
−2.734
−25.671
22.949
1.00
17.96


ATOM
1674
O
ASN
A
742
−3.727
−26.174
23.486
1.00
17.06


ATOM
1675
N
GLN
A
743
−1.827
−24.964
23.615
1.00
16.68


ATOM
1676
CA
GLN
A
743
−1.937
−24.727
25.045
1.00
17.92


ATOM
1677
CB
GLN
A
743
−0.738
−25.338
25.777
1.00
20.38


ATOM
1678
CG
GLN
A
743
−0.461
−26.787
25.408
1.00
28.60


ATOM
1679
CD
GLN
A
743
0.746
−27.350
26.131
1.00
30.94


ATOM
1680
OE1
GLN
A
743
1.775
−26.682
26.255
1.00
32.52


ATOM
1681
NE2
GLN
A
743
0.634
−28.588
26.602
1.00
20.21


ATOM
1682
C
GLN
A
743
−2.002
−23.233
25.341
1.00
16.35


ATOM
1683
O
GLN
A
743
−2.175
−22.836
26.490
1.00
18.44


ATOM
1684
N
PHE
A
744
−1.877
−22.407
24.307
1.00
16.26


ATOM
1685
CA
PHE
A
744
−1.916
−20.959
24.501
1.00
19.79


ATOM
1686
CB
PHE
A
744
−1.627
−20.229
23.184
1.00
21.58


ATOM
1687
CG
PHE
A
744
−1.465
−18.740
23.340
1.00
17.97


ATOM
1688
CD1
PHE
A
744
−0.441
−18.216
24.117
1.00
20.04


ATOM
1689
CD2
PHE
A
744
−2.345
−17.865
22.720
1.00
24.29


ATOM
1690
CE1
PHE
A
744
−0.298
−16.847
24.271
1.00
24.80


ATOM
1691
CE2
PHE
A
744
−2.208
−16.499
22.869
1.00
20.38


ATOM
1692
CZ
PHE
A
744
−1.184
−15.988
23.647
1.00
26.24


ATOM
1693
C
PHE
A
744
−3.265
−20.515
25.060
1.00
19.74


ATOM
1694
O
PHE
A
744
−4.316
−20.860
24.526
1.00
21.03


ATOM
1695
N
ASN
A
745
−3.221
−19.746
26.142
1.00
19.11


ATOM
1696
CA
ASN
A
745
−4.427
−19.260
26.791
1.00
18.83


ATOM
1697
CB
ASN
A
745
−4.893
−20.270
27.839
1.00
14.11


ATOM
1698
CG
ASN
A
745
−6.067
−19.764
28.653
1.00
17.45


ATOM
1699
OD1
ASN
A
745
−6.924
−19.042
28.143
1.00
22.19


ATOM
1700
ND2
ASN
A
745
−6.120
−20.152
29.921
1.00
30.84


ATOM
1701
C
ASN
A
745
−4.183
−17.906
27.446
1.00
17.46


ATOM
1702
O
ASN
A
745
−3.518
−17.818
28.481
1.00
17.84


ATOM
1703
N
LEU
A
746
−4.720
−16.857
26.826
1.00
16.56


ATOM
1704
CA
LEU
A
746
−4.573
−15.497
27.323
1.00
18.48


ATOM
1705
CB
LEU
A
746
−5.163
−14.495
26.323
1.00
15.11


ATOM
1706
CG
LEU
A
746
−4.319
−14.192
25.082
1.00
17.98


ATOM
1707
CD1
LEU
A
746
−5.031
−13.165
24.217
1.00
16.50


ATOM
1708
CD2
LEU
A
746
−2.960
−13.664
25.507
1.00
17.71


ATOM
1709
C
LEU
A
746
−5.212
−15.284
28.688
1.00
21.08


ATOM
1710
O
LEU
A
746
−4.911
−14.304
29.366
1.00
20.60


ATOM
1711
N
GLU
A
747
−6.098
−16.192
29.089
1.00
21.14


ATOM
1712
CA
GLU
A
747
−6.748
−16.075
30.389
1.00
21.90


ATOM
1713
CB
GLU
A
747
−7.916
−17.058
30.504
1.00
20.33


ATOM
1714
CG
GLU
A
747
−9.179
−16.586
29.813
1.00
31.82


ATOM
1715
CD
GLU
A
747
−10.324
−17.569
29.959
1.00
40.12


ATOM
1716
OE1
GLU
A
747
−10.550
−18.057
31.086
1.00
43.30


ATOM
1717
OE2
GLU
A
747
−11.003
−17.846
28.949
1.00
40.94


ATOM
1718
C
GLU
A
747
−5.740
−16.331
31.498
1.00
22.98


ATOM
1719
O
GLU
A
747
−5.885
−15.826
32.612
1.00
23.46


ATOM
1720
N
ASP
A
748
−4.719
−17.124
31.188
1.00
21.44


ATOM
1721
CA
ASP
A
748
−3.670
−17.424
32.151
1.00
21.15


ATOM
1722
CB
ASP
A
748
−2.800
−18.579
31.651
1.00
19.25


ATOM
1723
CG
ASP
A
748
−1.656
−18.899
32.595
1.00
19.90


ATOM
1724
OD1
ASP
A
748
−0.710
−18.088
32.692
1.00
26.86


ATOM
1725
OD2
ASP
A
748
−1.704
−19.962
33.246
1.00
42.46


ATOM
1726
C
ASP
A
748
−2.819
−16.171
32.314
1.00
20.94


ATOM
1727
O
ASP
A
748
−2.240
−15.677
31.351
1.00
19.01


ATOM
1728
N
PRO
A
749
−2.742
−15.637
33.541
1.00
18.53


ATOM
1729
CD
PRO
A
749
−3.443
−16.108
34.750
1.00
26.08


ATOM
1730
CA
PRO
A
749
−1.958
−14.432
33.825
1.00
19.83


ATOM
1731
CB
PRO
A
749
−2.009
−14.346
35.347
1.00
25.90


ATOM
1732
CG
PRO
A
749
−3.377
−14.896
35.654
1.00
25.60


ATOM
1733
C
PRO
A
749
−0.528
−14.476
33.286
1.00
17.96


ATOM
1734
O
PRO
A
749
−0.047
−13.506
32.708
1.00
18.09


ATOM
1735
N
HIS
A
750
0.149
−15.603
33.475
1.00
17.27


ATOM
1736
CA
HIS
A
750
1.520
−15.737
32.998
1.00
16.70


ATOM
1737
CB
HIS
A
750
2.138
−17.039
33.509
1.00
14.57


ATOM
1738
CG
HIS
A
750
3.506
−17.301
32.975
1.00
13.17


ATOM
1739
CD2
HIS
A
750
4.710
−16.780
33.299
1.00
15.22


ATOM
1740
ND1
HIS
A
750
3.748
−18.181
31.933
1.00
20.55


ATOM
1741
CE1
HIS
A
750
5.030
−18.183
31.649
1.00
21.44


ATOM
1742
NE2
HIS
A
750
5.644
−17.338
32.465
1.00
27.33


ATOM
1743
C
HIS
A
750
1.615
−15.691
31.475
1.00
16.04


ATOM
1744
O
HIS
A
750
2.521
−15.069
30.925
1.00
16.50


ATOM
1745
N
GLU
A
751
0.680
−16.346
30.794
1.00
14.76


ATOM
1746
CA
GLU
A
751
0.689
−16.359
29.333
1.00
14.97


ATOM
1747
CB
GLU
A
751
−0.269
−17.427
28.798
1.00
11.89


ATOM
1748
CG
GLU
A
751
0.173
−18.848
29.123
1.00
16.94


ATOM
1749
CD
GLU
A
751
−0.601
−19.892
28.354
1.00
17.06


ATOM
1750
OE1
GLU
A
751
−0.804
−19.697
27.140
1.00
17.15


ATOM
1751
OE2
GLU
A
751
−0.993
−20.912
28.959
1.00
27.83


ATOM
1752
C
GLU
A
751
0.325
−14.988
28.764
1.00
14.11


ATOM
1753
O
GLU
A
751
0.782
−14.616
27.685
1.00
14.18


ATOM
1754
N
LYS
A
752
−0.501
−14.248
29.498
1.00
13.06


ATOM
1755
CA
LYS
A
752
−0.900
−12.910
29.092
1.00
11.63


ATOM
1756
CB
LYS
A
752
−1.984
−12.370
30.041
1.00
11.74


ATOM
1757
CG
LYS
A
752
−2.200
−10.865
29.981
1.00
11.33


ATOM
1758
CD
LYS
A
752
−2.667
−10.402
28.608
1.00
18.51


ATOM
1759
CE
LYS
A
752
−3.921
−11.138
28.184
1.00
31.49


ATOM
1760
NZ
LYS
A
752
−4.536
−10.523
26.978
1.00
47.29


ATOM
1761
C
LYS
A
752
0.362
−12.047
29.176
1.00
14.58


ATOM
1762
O
LYS
A
752
0.665
−11.293
28.249
1.00
11.11


ATOM
1763
N
GLU
A
753
1.093
−12.196
30.270
1.00
12.46


ATOM
1764
CA
GLU
A
753
2.315
−11.409
30.445
1.00
13.89


ATOM
1765
CB
GLU
A
753
2.939
−11.745
31.801
1.00
15.41


ATOM
1766
CG
GLU
A
753
4.187
−10.950
32.098
1.00
17.51


ATOM
1767
CD
GLU
A
753
4.946
−11.478
33.300
1.00
36.21


ATOM
1768
OE1
GLU
A
753
4.335
−11.579
34.384
1.00
28.23


ATOM
1769
OE2
GLU
A
753
6.150
−11.782
33.162
1.00
36.81


ATOM
1770
C
GLU
A
753
3.267
−11.729
29.313
1.00
14.45


ATOM
1771
O
GLU
A
753
3.852
−10.839
28.671
1.00
11.34


ATOM
1772
N
LEU
A
754
3.441
−13.018
29.035
1.00
12.90


ATOM
1773
CA
LEU
A
754
4.329
−13.471
27.974
1.00
13.51


ATOM
1774
CB
LEU
A
754
4.377
−15.011
27.908
1.00
13.76


ATOM
1775
CG
LEU
A
754
5.196
−15.682
26.793
1.00
15.32


ATOM
1776
CD1
LEU
A
754
6.663
−15.286
26.877
1.00
15.56


ATOM
1777
CD2
LEU
A
754
5.044
−17.193
26.930
1.00
14.90


ATOM
1778
C
LEU
A
754
3.915
−12.900
26.616
1.00
12.21


ATOM
1779
O
LEU
A
754
4.765
−12.478
25.821
1.00
11.37


ATOM
1780
N
PHE
A
755
2.613
−12.867
26.351
1.00
11.00


ATOM
1781
CA
PHE
A
755
2.119
−12.336
25.088
1.00
9.92


ATOM
1782
CB
PHE
A
755
0.609
−12.551
24.966
1.00
12.44


ATOM
1783
CG
PHE
A
755
0.002
−11.867
23.780
1.00
11.67


ATOM
1784
CD1
PHE
A
755
0.338
−12.259
22.492
1.00
13.36


ATOM
1785
CD2
PHE
A
755
−0.858
−10.792
23.948
1.00
9.93


ATOM
1786
CE1
PHE
A
755
−0.170
−11.590
21.393
1.00
14.56


ATOM
1787
CE2
PHE
A
755
−1.369
−10.118
22.854
1.00
13.93


ATOM
1788
CZ
PHE
A
755
−1.021
−10.517
21.574
1.00
18.65


ATOM
1789
C
PHE
A
755
2.431
−10.840
24.972
1.00
9.95


ATOM
1790
O
PHE
A
755
2.856
−10.367
23.916
1.00
10.28


ATOM
1791
N
LEU
A
756
2.225
−10.099
26.057
1.00
9.98


ATOM
1792
CA
LEU
A
756
2.489
−8.664
26.034
1.00
9.03


ATOM
1793
CB
LEU
A
756
2.102
−8.017
27.370
1.00
9.14


ATOM
1794
CG
LEU
A
756
0.610
−8.119
27.706
1.00
13.27


ATOM
1795
CD1
LEU
A
756
0.331
−7.487
29.065
1.00
21.21


ATOM
1796
CD2
LEU
A
756
−0.198
−7.432
26.613
1.00
18.57


ATOM
1797
C
LEU
A
756
3.959
−8.410
25.721
1.00
9.36


ATOM
1798
O
LEU
A
756
4.291
−7.437
25.045
1.00
8.42


ATOM
1799
N
ALA
A
757
4.844
−9.285
26.197
1.00
7.41


ATOM
1800
CA
ALA
A
757
6.267
−9.118
25.915
1.00
10.17


ATOM
1801
CB
ALA
A
757
7.096
−10.112
26.720
1.00
10.57


ATOM
1802
C
ALA
A
757
6.514
−9.315
24.421
1.00
9.99


ATOM
1803
O
ALA
A
757
7.254
−8.548
23.798
1.00
10.22


ATOM
1804
N
MET
A
758
5.890
−10.341
23.845
1.00
8.41


ATOM
1805
CA
MET
A
758
6.046
−10.627
22.422
1.00
8.55


ATOM
1806
CB
MET
A
758
5.348
−11.946
22.061
1.00
8.57


ATOM
1807
CG
MET
A
758
5.898
−13.175
22.783
1.00
9.97


ATOM
1808
SD
MET
A
758
7.613
−13.597
22.367
1.00
15.99


ATOM
1809
CE
MET
A
758
7.436
−14.226
20.702
1.00
36.66


ATOM
1810
C
MET
A
758
5.469
−9.499
21.572
1.00
9.31


ATOM
1811
O
MET
A
758
6.035
−9.134
20.534
1.00
8.67


ATOM
1812
N
LEU
A
759
4.334
−8.962
22.008
1.00
10.68


ATOM
1813
CA
LEU
A
759
3.682
−7.877
21.290
1.00
7.26


ATOM
1814
CB
LEU
A
759
2.348
−7.536
21.954
1.00
6.70


ATOM
1815
CG
LEU
A
759
1.521
−6.419
21.316
1.00
9.88


ATOM
1816
CD1
LEU
A
759
1.217
−6.751
19.858
1.00
13.46


ATOM
1817
CD2
LEU
A
759
0.232
−6.241
22.103
1.00
8.91


ATOM
1818
C
LEU
A
759
4.589
−6.650
21.269
1.00
10.65


ATOM
1819
O
LEU
A
759
4.677
−5.945
20.259
1.00
8.66


ATOM
1820
N
MET
A
760
5.258
−6.388
22.387
1.00
8.87


ATOM
1821
CA
MET
A
760
6.168
−5.251
22.454
1.00
9.10


ATOM
1822
CB
MET
A
760
6.760
−5.114
23.859
1.00
9.37


ATOM
1823
CG
MET
A
760
5.831
−4.491
24.889
1.00
7.94


ATOM
1824
SD
MET
A
760
5.392
−2.762
24.513
1.00
11.15


ATOM
1825
CE
MET
A
760
6.981
−1.951
24.748
1.00
10.58


ATOM
1826
C
MET
A
760
7.292
−5.445
21.444
1.00
9.36


ATOM
1827
O
MET
A
760
7.693
−4.501
20.757
1.00
8.44


ATOM
1828
N
THR
A
761
7.812
−6.667
21.359
1.00
8.62


ATOM
1829
CA
THR
A
761
8.890
−6.948
20.416
1.00
9.46


ATOM
1830
CB
THR
A
761
9.442
−8.379
20.597
1.00
12.42


ATOM
1831
OG1
THR
A
761
9.916
−8.540
21.940
1.00
11.86


ATOM
1832
CG2
THR
A
761
10.598
−8.636
19.620
1.00
9.90


ATOM
1833
C
THR
A
761
8.389
−6.785
18.984
1.00
10.31


ATOM
1834
O
THR
A
761
9.088
−6.238
18.128
1.00
10.55


ATOM
1835
N
ALA
A
762
7.172
−7.254
18.722
1.00
10.42


ATOM
1836
CA
ALA
A
762
6.598
−7.148
17.389
1.00
7.73


ATOM
1837
CB
ALA
A
762
5.202
−7.777
17.362
1.00
10.79


ATOM
1838
C
ALA
A
762
6.524
−5.689
16.948
1.00
9.57


ATOM
1839
O
ALA
A
762
6.794
−5.370
15.787
1.00
9.59


ATOM
1840
N
CYS
A
763
6.161
−4.801
17.872
1.00
7.53


ATOM
1841
CA
CYS
A
763
6.063
−3.378
17.551
1.00
7.89


ATOM
1842
CB
CYS
A
763
5.237
−2.641
18.611
1.00
11.70


ATOM
1843
SG
CYS
A
763
3.503
−3.143
18.670
1.00
11.19


ATOM
1844
C
CYS
A
763
7.441
−2.744
17.443
1.00
9.03


ATOM
1845
O
CYS
A
763
7.689
−1.911
16.574
1.00
10.26


ATOM
1846
N
ASP
A
764
8.340
−3.157
18.329
1.00
8.73


ATOM
1847
CA
ASP
A
764
9.703
−2.641
18.352
1.00
10.03


ATOM
1848
CB
ASP
A
764
10.448
−3.269
19.541
1.00
11.85


ATOM
1849
CG
ASP
A
764
11.766
−2.585
19.840
1.00
12.03


ATOM
1850
OD1
ASP
A
764
11.963
−1.451
19.361
1.00
11.46


ATOM
1851
OD2
ASP
A
764
12.592
−3.176
20.571
1.00
15.03


ATOM
1852
C
ASP
A
764
10.447
−2.924
17.036
1.00
10.20


ATOM
1853
O
ASP
A
764
11.225
−2.097
16.562
1.00
11.71


ATOM
1854
N
LEU
A
765
10.194
−4.086
16.442
1.00
11.54


ATOM
1855
CA
LEU
A
765
10.867
−4.474
15.202
1.00
11.71


ATOM
1856
CB
LEU
A
765
11.208
−5.965
15.252
1.00
13.42


ATOM
1857
CG
LEU
A
765
12.017
−6.454
16.453
1.00
15.02


ATOM
1858
CD1
LEU
A
765
12.233
−7.957
16.348
1.00
13.91


ATOM
1859
CD2
LEU
A
765
13.345
−5.721
16.499
1.00
16.31


ATOM
1860
C
LEU
A
765
10.049
−4.221
13.941
1.00
12.10


ATOM
1861
O
LEU
A
765
10.490
−4.560
12.837
1.00
11.30


ATOM
1862
N
SER
A
766
8.881
−3.606
14.101
1.00
12.76


ATOM
1863
CA
SER
A
766
7.965
−3.383
12.983
1.00
10.86


ATOM
1864
CB
SER
A
766
6.672
−2.733
13.488
1.00
8.49


ATOM
1865
OG
SER
A
766
6.902
−1.438
13.991
1.00
14.83


ATOM
1866
C
SER
A
766
8.446
−2.657
11.729
1.00
7.60


ATOM
1867
O
SER
A
766
7.782
−2.735
10.700
1.00
9.56


ATOM
1868
N
ALA
A
767
9.575
−1.956
11.787
1.00
8.02


ATOM
1869
CA
ALA
A
767
10.073
−1.296
10.581
1.00
9.45


ATOM
1870
CB
ALA
A
767
11.364
−0.522
10.881
1.00
11.41


ATOM
1871
C
ALA
A
767
10.340
−2.377
9.521
1.00
10.04


ATOM
1872
O
ALA
A
767
10.253
−2.124
8.319
1.00
10.04


ATOM
1873
N
ILE
A
768
10.655
−3.586
9.976
1.00
9.49


ATOM
1874
CA
ILE
A
768
10.942
−4.694
9.066
1.00
12.99


ATOM
1875
CB
ILE
A
768
11.555
−5.894
9.840
1.00
9.64


ATOM
1876
CG2
ILE
A
768
10.473
−6.631
10.612
1.00
7.91


ATOM
1877
CG1
ILE
A
768
12.270
−6.836
8.868
1.00
12.83


ATOM
1878
CD1
ILE
A
768
13.471
−6.199
8.190
1.00
15.69


ATOM
1879
C
ILE
A
768
9.704
−5.173
8.296
1.00
11.57


ATOM
1880
O
ILE
A
768
9.812
−5.986
7.376
1.00
12.45


ATOM
1881
N
THR
A
769
8.530
−4.665
8.662
1.00
12.70


ATOM
1882
CA
THR
A
769
7.286
−5.062
7.999
1.00
10.88


ATOM
1883
CB
THR
A
769
6.167
−5.326
9.025
1.00
13.25


ATOM
1884
OG1
THR
A
769
5.760
−4.083
9.617
1.00
12.15


ATOM
1885
CG2
THR
A
769
6.654
−6.271
10.124
1.00
16.86


ATOM
1886
C
THR
A
769
6.762
−3.991
7.036
1.00
12.18


ATOM
1887
O
THR
A
769
5.795
−4.223
6.308
1.00
13.18


ATOM
1888
N
LYS
A
770
7.402
−2.824
7.043
1.00
12.64


ATOM
1889
CA
LYS
A
770
6.986
−1.686
6.216
1.00
10.43


ATOM
1890
CB
LYS
A
770
7.684
−0.413
6.714
1.00
12.22


ATOM
1891
CG
LYS
A
770
7.375
−0.029
8.165
1.00
7.87


ATOM
1892
CD
LYS
A
770
5.948
0.457
8.330
1.00
13.33


ATOM
1893
CE
LYS
A
770
5.644
0.766
9.794
1.00
14.40


ATOM
1894
NZ
LYS
A
770
4.263
1.293
9.973
1.00
14.45


ATOM
1895
C
LYS
A
770
7.247
−1.829
4.716
1.00
11.91


ATOM
1896
O
LYS
A
770
8.069
−2.638
4.290
1.00
13.63


ATOM
1897
N
PRO
A
771
6.529
−1.041
3.892
1.00
11.52


ATOM
1898
CD
PRO
A
771
5.408
−0.150
4.240
1.00
14.60


ATOM
1899
CA
PRO
A
771
6.718
−1.096
2.441
1.00
12.80


ATOM
1900
CB
PRO
A
771
5.914
0.099
1.950
1.00
15.88


ATOM
1901
CG
PRO
A
771
4.751
0.098
2.886
1.00
11.15


ATOM
1902
C
PRO
A
771
8.206
−0.933
2.183
1.00
14.66


ATOM
1903
O
PRO
A
771
8.880
−0.201
2.908
1.00
15.01


ATOM
1904
N
TRP
A
772
8.711
−1.604
1.156
1.00
14.26


ATOM
1905
CA
TRP
A
772
10.133
−1.555
0.827
1.00
15.34


ATOM
1906
CB
TRP
A
772
10.367
−2.121
−0.578
1.00
14.10


ATOM
1907
CG
TRP
A
772
11.809
−2.101
−1.009
1.00
17.47


ATOM
1908
CD2
TRP
A
772
12.931
−2.659
−0.307
1.00
17.61


ATOM
1909
CE2
TRP
A
772
14.079
−2.404
−1.086
1.00
19.63


ATOM
1910
CE3
TRP
A
772
13.076
−3.348
0.901
1.00
16.69


ATOM
1911
CD1
TRP
A
772
12.313
−1.547
−2.152
1.00
16.69


ATOM
1912
NE1
TRP
A
772
13.675
−1.725
−2.204
1.00
24.41


ATOM
1913
CZ2
TRP
A
772
15.354
−2.816
−0.694
1.00
24.29


ATOM
1914
CZ3
TRP
A
772
14.344
−3.755
1.289
1.00
17.48


ATOM
1915
CH2
TRP
A
772
15.466
−3.488
0.493
1.00
21.25


ATOM
1916
C
TRP
A
772
10.820
−0.190
0.952
1.00
17.78


ATOM
1917
O
TRP
A
772
11.834
−0.070
1.639
1.00
15.81


ATOM
1918
N
PRO
A
773
10.286
0.853
0.291
1.00
19.35


ATOM
1919
CD
PRO
A
773
9.132
0.877
−0.624
1.00
18.85


ATOM
1920
CA
PRO
A
773
10.909
2.180
0.377
1.00
18.24


ATOM
1921
CB
PRO
A
773
9.926
3.068
−0.382
1.00
21.17


ATOM
1922
CG
PRO
A
773
9.386
2.138
−1.422
1.00
23.60


ATOM
1923
C
PRO
A
773
11.129
2.654
1.814
1.00
16.33


ATOM
1924
O
PRO
A
773
12.167
3.235
2.140
1.00
16.01


ATOM
1925
N
ILE
A
774
10.143
2.406
2.668
1.00
16.23


ATOM
1926
CA
ILE
A
774
10.228
2.805
4.066
1.00
15.30


ATOM
1927
CB
ILE
A
774
8.851
2.670
4.751
1.00
15.99


ATOM
1928
CG2
ILE
A
774
8.977
2.922
6.250
1.00
13.24


ATOM
1929
CG1
ILE
A
774
7.867
3.658
4.110
1.00
20.68


ATOM
1930
CD1
ILE
A
774
6.441
3.501
4.588
1.00
21.74


ATOM
1931
C
ILE
A
774
11.264
1.958
4.804
1.00
16.31


ATOM
1932
O
ILE
A
774
12.133
2.491
5.497
1.00
15.63


ATOM
1933
N
GLN
A
775
11.173
0.640
4.650
1.00
13.80


ATOM
1934
CA
GLN
A
775
12.120
−0.274
5.279
1.00
12.85


ATOM
1935
CB
GLN
A
775
11.786
−1.727
4.901
1.00
13.34


ATOM
1936
CG
GLN
A
775
12.987
−2.688
4.921
1.00
14.20


ATOM
1937
CD
GLN
A
775
13.582
−2.897
6.305
1.00
21.70


ATOM
1938
OE1
GLN
A
775
14.663
−3.472
6.441
1.00
13.81


ATOM
1939
NE2
GLN
A
775
12.880
−2.440
7.336
1.00
14.50


ATOM
1940
C
GLN
A
775
13.549
0.057
4.877
1.00
13.13


ATOM
1941
O
GLN
A
775
14.458
0.060
5.694
1.00
12.67


ATOM
1942
N
GLN
A
776
13.749
0.352
3.590
1.00
10.04


ATOM
1943
CA
GLN
A
776
15.068
0.674
3.090
1.00
12.84


ATOM
1944
CB
GLN
A
776
15.004
0.820
1.564
1.00
19.00


ATOM
1945
CG
GLN
A
776
16.326
0.943
0.890
1.00
25.33


ATOM
1946
CD
GLN
A
776
16.172
0.760
−0.595
1.00
36.37


ATOM
1947
OE1
GLN
A
776
15.258
1.315
−1.209
1.00
39.80


ATOM
1948
NE2
GLN
A
776
17.058
−0.023
−1.186
1.00
41.16


ATOM
1949
C
GLN
A
776
15.627
1.934
3.738
1.00
10.61


ATOM
1950
O
GLN
A
776
16.796
1.988
4.109
1.00
13.39


ATOM
1951
N
ARG
A
777
14.776
2.946
3.922
1.00
10.52


ATOM
1952
CA
ARG
A
777
15.199
4.197
4.534
1.00
11.43


ATOM
1953
CB
ARG
A
777
14.090
5.253
4.419
1.00
15.26


ATOM
1954
CG
ARG
A
777
14.487
6.607
4.948
1.00
20.06


ATOM
1955
CD
ARG
A
777
13.343
7.586
4.765
1.00
25.19


ATOM
1956
NE
ARG
A
777
12.206
7.273
5.627
1.00
34.37


ATOM
1957
CZ
ARG
A
777
12.232
7.359
6.954
1.00
35.62


ATOM
1958
NH1
ARG
A
777
13.340
7.747
7.575
1.00
37.87


ATOM
1959
NH2
ARG
A
777
11.149
7.068
7.661
1.00
29.66


ATOM
1960
C
ARG
A
777
15.560
3.979
5.997
1.00
10.83


ATOM
1961
O
ARG
A
777
16.601
4.447
6.472
1.00
13.15


ATOM
1962
N
ILE
A
778
14.715
3.238
6.705
1.00
12.38


ATOM
1963
CA
ILE
A
778
14.953
2.944
8.112
1.00
13.18


ATOM
1964
CB
ILE
A
778
13.753
2.209
8.744
1.00
15.50


ATOM
1965
CG2
ILE
A
778
14.091
1.788
10.170
1.00
13.56


ATOM
1966
CG1
ILE
A
778
12.516
3.108
8.721
1.00
22.29


ATOM
1967
CD1
ILE
A
778
12.685
4.399
9.478
1.00
26.81


ATOM
1968
C
ILE
A
778
16.198
2.086
8.305
1.00
12.49


ATOM
1969
O
ILE
A
778
16.963
2.298
9.245
1.00
12.70


ATOM
1970
N
ALA
A
779
16.399
1.117
7.417
1.00
12.47


ATOM
1971
CA
ALA
A
779
17.563
0.242
7.510
1.00
13.19


ATOM
1972
CB
ALA
A
779
17.538
−0.789
6.391
1.00
14.05


ATOM
1973
C
ALA
A
779
18.856
1.051
7.452
1.00
13.71


ATOM
1974
O
ALA
A
779
19.839
0.700
8.106
1.00
11.99


ATOM
1975
N
GLU
A
780
18.858
2.131
6.672
1.00
14.86


ATOM
1976
CA
GLU
A
780
20.048
2.976
6.560
1.00
13.62


ATOM
1977
CB
GLU
A
780
19.860
4.053
5.487
1.00
17.29


ATOM
1978
CG
GLU
A
780
19.742
3.519
4.075
1.00
30.45


ATOM
1979
CD
GLU
A
780
19.744
4.628
3.038
1.00
42.90


ATOM
1980
OE1
GLU
A
780
20.761
5.347
2.939
1.00
42.08


ATOM
1981
OE2
GLU
A
780
18.728
4.783
2.326
1.00
56.88


ATOM
1982
C
GLU
A
780
20.350
3.649
7.897
1.00
13.45


ATOM
1983
O
GLU
A
780
21.506
3.791
8.277
1.00
14.75


ATOM
1984
N
LEU
A
781
19.303
4.074
8.597
1.00
12.82


ATOM
1985
CA
LEU
A
781
19.464
4.716
9.898
1.00
10.66


ATOM
1986
CB
LEU
A
781
18.113
5.215
10.410
1.00
12.60


ATOM
1987
CG
LEU
A
781
17.428
6.296
9.574
1.00
15.49


ATOM
1988
CD1
LEU
A
781
16.101
6.670
10.215
1.00
14.52


ATOM
1989
CD2
LEU
A
781
18.339
7.513
9.475
1.00
17.00


ATOM
1990
C
LEU
A
781
20.032
3.704
10.887
1.00
12.39


ATOM
1991
O
LEU
A
781
20.935
4.014
11.673
1.00
11.98


ATOM
1992
N
VAL
A
782
19.490
2.490
10.839
1.00
9.90


ATOM
1993
CA
VAL
A
782
19.933
1.418
11.719
1.00
9.65


ATOM
1994
CB
VAL
A
782
19.116
0.126
11.463
1.00
10.42


ATOM
1995
CG1
VAL
A
782
19.714
−1.029
12.240
1.00
13.17


ATOM
1996
CG2
VAL
A
782
17.657
0.339
11.868
1.00
16.63


ATOM
1997
C
VAL
A
782
21.418
1.154
11.477
1.00
10.70


ATOM
1998
O
VAL
A
782
22.210
1.068
12.418
1.00
13.37


ATOM
1999
N
ALA
A
783
21.793
1.053
10.206
1.00
11.25


ATOM
2000
CA
ALA
A
783
23.185
0.810
9.839
1.00
11.83


ATOM
2001
CB
ALA
A
783
23.299
0.632
8.337
1.00
15.10


ATOM
2002
C
ALA
A
783
24.074
1.961
10.298
1.00
12.03


ATOM
2003
O
ALA
A
783
25.170
1.746
10.820
1.00
12.81


ATOM
2004
N
THR
A
784
23.599
3.187
10.099
1.00
11.94


ATOM
2005
CA
THR
A
784
24.358
4.359
10.504
1.00
10.90


ATOM
2006
CB
THR
A
784
23.572
5.659
10.211
1.00
12.78


ATOM
2007
OG1
THR
A
784
23.359
5.778
8.797
1.00
15.62


ATOM
2008
CG2
THR
A
784
24.341
6.883
10.706
1.00
13.70


ATOM
2009
C
THR
A
784
24.676
4.282
11.995
1.00
11.74


ATOM
2010
O
THR
A
784
25.819
4.490
12.408
1.00
10.51


ATOM
2011
N
GLU
A
785
23.670
3.969
12.805
1.00
10.01


ATOM
2012
CA
GLU
A
785
23.881
3.880
14.243
1.00
10.75


ATOM
2013
CB
GLU
A
785
22.549
3.669
14.968
1.00
7.51


ATOM
2014
CG
GLU
A
785
22.675
3.740
16.483
1.00
9.65


ATOM
2015
CD
GLU
A
785
21.335
3.755
17.178
1.00
7.52


ATOM
2016
OE1
GLU
A
785
20.415
4.436
16.674
1.00
10.93


ATOM
2017
OE2
GLU
A
785
21.208
3.099
18.236
1.00
12.56


ATOM
2018
C
GLU
A
785
24.847
2.760
14.612
1.00
11.99


ATOM
2019
O
GLU
A
785
25.737
2.948
15.440
1.00
11.68


ATOM
2020
N
PHE
A
786
24.671
1.594
13.997
1.00
9.83


ATOM
2021
CA
PHE
A
786
25.541
0.464
14.285
1.00
10.39


ATOM
2022
CB
PHE
A
786
25.069
−0.794
13.550
1.00
11.58


ATOM
2023
CG
PHE
A
786
23.876
−1.455
14.176
1.00
16.59


ATOM
2024
CD1
PHE
A
786
23.632
−1.327
15.533
1.00
18.18


ATOM
2025
CD2
PHE
A
786
23.034
−2.254
13.419
1.00
19.90


ATOM
2026
CE1
PHE
A
786
22.570
−1.986
16.125
1.00
25.35


ATOM
2027
CE2
PHE
A
786
21.972
−2.916
14.004
1.00
17.12


ATOM
2028
CZ
PHE
A
786
21.740
−2.781
15.360
1.00
16.84


ATOM
2029
C
PHE
A
786
26.985
0.760
13.898
1.00
9.62


ATOM
2030
O
PHE
A
786
27.907
0.444
14.652
1.00
10.46


ATOM
2031
N
PHE
A
787
27.183
1.348
12.720
1.00
8.90


ATOM
2032
CA
PHE
A
787
28.531
1.680
12.273
1.00
9.83


ATOM
2033
CB
PHE
A
787
28.515
2.141
10.809
1.00
10.96


ATOM
2034
CG
PHE
A
787
28.116
1.056
9.849
1.00
8.28


ATOM
2035
CD1
PHE
A
787
28.335
−0.276
10.172
1.00
10.72


ATOM
2036
CD2
PHE
A
787
27.546
1.357
8.626
1.00
11.47


ATOM
2037
CE1
PHE
A
787
27.993
−1.287
9.296
1.00
12.45


ATOM
2038
CE2
PHE
A
787
27.201
0.344
7.739
1.00
12.21


ATOM
2039
CZ
PHE
A
787
27.424
−0.977
8.075
1.00
8.97


ATOM
2040
C
PHE
A
787
29.165
2.747
13.149
1.00
12.00


ATOM
2041
O
PHE
A
787
30.387
2.787
13.311
1.00
11.70


ATOM
2042
N
ASP
A
788
28.340
3.620
13.713
1.00
10.51


ATOM
2043
CA
ASP
A
788
28.867
4.655
14.583
1.00
13.07


ATOM
2044
CB
ASP
A
788
27.770
5.654
14.953
1.00
9.28


ATOM
2045
CG
ASP
A
788
28.275
6.751
15.869
1.00
17.65


ATOM
2046
OD1
ASP
A
788
27.862
6.784
17.046
1.00
22.26


ATOM
2047
OD2
ASP
A
788
29.097
7.575
15.414
1.00
23.70


ATOM
2048
C
ASP
A
788
29.427
3.975
15.832
1.00
11.61


ATOM
2049
O
ASP
A
788
30.491
4.349
16.324
1.00
11.23


ATOM
2050
N
GLN
A
789
28.719
2.965
16.338
1.00
10.39


ATOM
2051
CA
GLN
A
789
29.201
2.243
17.515
1.00
10.66


ATOM
2052
CB
GLN
A
789
28.185
1.199
17.979
1.00
14.04


ATOM
2053
CG
GLN
A
789
28.667
0.416
19.191
1.00
13.95


ATOM
2054
CD
GLN
A
789
27.696
−0.652
19.641
1.00
13.88


ATOM
2055
OE1
GLN
A
789
26.488
−0.445
19.641
1.00
10.68


ATOM
2056
NE2
GLN
A
789
28.226
−1.799
20.051
1.00
10.88


ATOM
2057
C
GLN
A
789
30.509
1.541
17.155
1.00
12.25


ATOM
2058
O
GLN
A
789
31.452
1.504
17.952
1.00
12.92


ATOM
2059
N
GLY
A
790
30.552
0.979
15.950
1.00
12.27


ATOM
2060
CA
GLY
A
790
31.746
0.292
15.493
1.00
13.69


ATOM
2061
C
GLY
A
790
32.948
1.218
15.519
1.00
12.41


ATOM
2062
O
GLY
A
790
34.050
0.805
15.885
1.00
14.19


ATOM
2063
N
ASP
A
791
32.743
2.476
15.135
1.00
13.24


ATOM
2064
CA
ASP
A
791
33.837
3.448
15.135
1.00
15.89


ATOM
2065
CB
ASP
A
791
33.383
4.802
14.582
1.00
11.78


ATOM
2066
CG
ASP
A
791
33.022
4.748
13.108
1.00
11.72


ATOM
2067
OD1
ASP
A
791
33.525
3.853
12.401
1.00
16.07


ATOM
2068
OD2
ASP
A
791
32.249
5.619
12.657
1.00
16.56


ATOM
2069
C
ASP
A
791
34.350
3.653
16.554
1.00
15.06


ATOM
2070
O
ASP
A
791
35.555
3.751
16.794
1.00
15.97


ATOM
2071
N
ARG
A
792
33.423
3.723
17.496
1.00
16.00


ATOM
2072
CA
ARG
A
792
33.783
3.925
18.885
1.00
13.38


ATOM
2073
CB
ARG
A
792
32.544
4.308
19.680
1.00
15.67


ATOM
2074
CG
ARG
A
792
32.056
5.689
19.304
1.00
20.98


ATOM
2075
CD
ARG
A
792
30.791
6.043
20.014
1.00
22.55


ATOM
2076
NE
ARG
A
792
30.929
6.004
21.465
1.00
21.96


ATOM
2077
CZ
ARG
A
792
29.945
6.332
22.290
1.00
19.00


ATOM
2078
NH1
ARG
A
792
28.782
6.726
21.791
1.00
18.95


ATOM
2079
NH2
ARG
A
792
30.105
6.236
23.601
1.00
23.88


ATOM
2080
C
ARG
A
792
34.466
2.716
19.501
1.00
13.13


ATOM
2081
O
ARG
A
792
35.296
2.865
20.390
1.00
14.33


ATOM
2082
N
GLU
A
793
34.112
1.522
19.036
1.00
14.11


ATOM
2083
CA
GLU
A
793
34.730
0.305
19.545
1.00
12.55


ATOM
2084
CB
GLU
A
793
33.969
−0.932
19.051
1.00
12.93


ATOM
2085
CG
GLU
A
793
32.531
−0.986
19.543
1.00
15.09


ATOM
2086
CD
GLU
A
793
31.816
−2.269
19.165
1.00
17.10


ATOM
2087
OE1
GLU
A
793
32.105
−2.807
18.078
1.00
14.75


ATOM
2088
OE2
GLU
A
793
30.951
−2.728
19.949
1.00
13.37


ATOM
2089
C
GLU
A
793
36.184
0.251
19.080
1.00
13.70


ATOM
2090
O
GLU
A
793
37.073
−0.143
19.837
1.00
14.48


ATOM
2091
N
ARG
A
794
36.429
0.655
17.838
1.00
12.88


ATOM
2092
CA
ARG
A
794
37.792
0.647
17.318
1.00
16.50


ATOM
2093
CB
ARG
A
794
37.828
1.083
15.847
1.00
16.91


ATOM
2094
CG
ARG
A
794
37.330
0.047
14.838
1.00
16.40


ATOM
2095
CD
ARG
A
794
37.399
0.609
13.422
1.00
20.95


ATOM
2096
NE
ARG
A
794
36.790
−0.268
12.422
1.00
21.25


ATOM
2097
CZ
ARG
A
794
37.323
−1.407
11.996
1.00
16.41


ATOM
2098
NH1
ARG
A
794
38.486
−1.822
12.480
1.00
26.91


ATOM
2099
NH2
ARG
A
794
36.691
−2.134
11.082
1.00
18.30


ATOM
2100
C
ARG
A
794
38.648
1.603
18.141
1.00
17.48


ATOM
2101
O
ARG
A
794
39.781
1.287
18.503
1.00
18.61


ATOM
2102
N
LYS
A
795
38.087
2.769
18.443
1.00
19.00


ATOM
2103
CA
LYS
A
795
38.793
3.795
19.199
1.00
19.03


ATOM
2104
CB
LYS
A
795
38.146
5.161
18.947
1.00
22.77


ATOM
2105
CG
LYS
A
795
38.839
6.312
19.661
1.00
30.54


ATOM
2106
CD
LYS
A
795
38.128
7.633
19.410
1.00
38.45


ATOM
2107
CE
LYS
A
795
38.902
8.796
20.009
1.00
34.57


ATOM
2108
NZ
LYS
A
795
40.267
8.886
19.424
1.00
42.21


ATOM
2109
C
LYS
A
795
38.866
3.554
20.704
1.00
19.86


ATOM
2110
O
LYS
A
795
39.923
3.716
21.310
1.00
21.68


ATOM
2111
N
GLU
A
796
37.747
3.166
21.304
1.00
17.50


ATOM
2112
CA
GLU
A
796
37.696
2.953
22.745
1.00
18.20


ATOM
2113
CB
GLU
A
796
36.286
3.272
23.255
1.00
16.63


ATOM
2114
CG
GLU
A
796
35.872
4.722
23.048
1.00
19.55


ATOM
2115
CD
GLU
A
796
34.425
4.982
23.414
1.00
17.22


ATOM
2116
OE1
GLU
A
796
33.986
4.520
24.489
1.00
17.11


ATOM
2117
OE2
GLU
A
796
33.729
5.660
22.629
1.00
17.31


ATOM
2118
C
GLU
A
796
38.116
1.568
23.238
1.00
18.82


ATOM
2119
O
GLU
A
796
38.604
1.432
24.359
1.00
19.88


ATOM
2120
N
LEU
A
797
37.936
0.544
22.408
1.00
17.76


ATOM
2121
CA
LEU
A
797
38.279
−0.817
22.809
1.00
17.55


ATOM
2122
CB
LEU
A
797
37.032
−1.708
22.732
1.00
14.21


ATOM
2123
CG
LEU
A
797
35.816
−1.230
23.535
1.00
21.04


ATOM
2124
CD1
LEU
A
797
34.655
−2.194
23.333
1.00
19.81


ATOM
2125
CD2
LEU
A
797
36.177
−1.134
25.008
1.00
22.47


ATOM
2126
C
LEU
A
797
39.400
−1.441
21.980
1.00
18.06


ATOM
2127
O
LEU
A
797
39.899
−2.518
22.312
1.00
18.10


ATOM
2128
N
ASN
A
798
39.795
−0.760
20.910
1.00
17.87


ATOM
2129
CA
ASN
A
798
40.846
−1.244
20.016
1.00
17.14


ATOM
2130
CB
ASN
A
798
42.202
−1.278
20.732
1.00
18.53


ATOM
2131
CG
ASN
A
798
43.357
−1.501
19.770
1.00
19.84


ATOM
2132
OD1
ASN
A
798
43.497
−0.774
18.788
1.00
22.65


ATOM
2133
ND2
ASN
A
798
44.186
−2.507
20.043
1.00
17.46


ATOM
2134
C
ASN
A
798
40.522
−2.632
19.472
1.00
19.40


ATOM
2135
O
ASN
A
798
41.400
−3.485
19.352
1.00
18.37


ATOM
2136
N
ILE
A
799
39.254
−2.852
19.141
1.00
18.23


ATOM
2137
CA
ILE
A
799
38.816
−4.134
18.603
1.00
20.72


ATOM
2138
CB
ILE
A
799
37.779
−4.811
19.529
1.00
23.69


ATOM
2139
CG2
ILE
A
799
38.348
−4.970
20.930
1.00
25.12


ATOM
2140
CG1
ILE
A
799
36.500
−3.968
19.570
1.00
27.29


ATOM
2141
CD1
ILE
A
799
35.381
−4.581
20.373
1.00
23.09


ATOM
2142
C
ILE
A
799
38.158
−3.926
17.243
1.00
20.66


ATOM
2143
O
ILE
A
799
37.636
−2.846
16.956
1.00
20.48


ATOM
2144
N
GLU
A
800
38.199
−4.951
16.399
1.00
20.84


ATOM
2145
CA
GLU
A
800
37.558
−4.855
15.096
1.00
19.43


ATOM
2146
CB
GLU
A
800
38.162
−5.856
14.109
1.00
25.89


ATOM
2147
CG
GLU
A
800
37.507
−5.813
12.735
1.00
37.89


ATOM
2148
CD
GLU
A
800
38.245
−6.637
11.699
1.00
48.08


ATOM
2149
OE1
GLU
A
800
38.421
−7.856
11.915
1.00
47.23


ATOM
2150
OE2
GLU
A
800
38.647
−6.063
10.663
1.00
52.27


ATOM
2151
C
GLU
A
800
36.095
−5.188
15.345
1.00
16.86


ATOM
2152
O
GLU
A
800
35.774
−6.249
15.879
1.00
20.00


ATOM
2153
N
PRO
A
801
35.186
−4.277
14.979
1.00
16.72


ATOM
2154
CD
PRO
A
801
35.413
−2.971
14.340
1.00
13.94


ATOM
2155
CA
PRO
A
801
33.755
−4.518
15.188
1.00
15.17


ATOM
2156
CB
PRO
A
801
33.101
−3.242
14.651
1.00
11.35


ATOM
2157
CG
PRO
A
801
34.189
−2.204
14.760
1.00
18.39


ATOM
2158
C
PRO
A
801
33.249
−5.750
14.446
1.00
14.88


ATOM
2159
O
PRO
A
801
33.836
−6.168
13.437
1.00
14.57


ATOM
2160
N
THR
A
802
32.166
−6.333
14.952
1.00
13.89


ATOM
2161
CA
THR
A
802
31.554
−7.473
14.282
1.00
13.70


ATOM
2162
CB
THR
A
802
30.367
−8.057
15.090
1.00
18.66


ATOM
2163
OG1
THR
A
802
29.339
−7.067
15.227
1.00
22.82


ATOM
2164
CG2
THR
A
802
30.824
−8.491
16.475
1.00
28.52


ATOM
2165
C
THR
A
802
31.028
−6.886
12.974
1.00
13.06


ATOM
2166
O
THR
A
802
30.896
−5.666
12.853
1.00
13.12


ATOM
2167
N
ASP
A
803
30.730
−7.737
11.997
1.00
13.68


ATOM
2168
CA
ASP
A
803
30.239
−7.260
10.706
1.00
13.10


ATOM
2169
CB
ASP
A
803
29.784
−8.436
9.840
1.00
15.94


ATOM
2170
CG
ASP
A
803
30.942
−9.281
9.340
1.00
19.70


ATOM
2171
OD1
ASP
A
803
32.108
−8.965
9.661
1.00
16.86


ATOM
2172
OD2
ASP
A
803
30.681
−10.265
8.619
1.00
17.57


ATOM
2173
C
ASP
A
803
29.092
−6.262
10.829
1.00
14.26


ATOM
2174
O
ASP
A
803
29.071
−5.239
10.141
1.00
15.59


ATOM
2175
N
LEU
A
804
28.142
−6.561
11.706
1.00
12.76


ATOM
2176
CA
LEU
A
804
26.982
−5.700
11.907
1.00
13.21


ATOM
2177
CB
LEU
A
804
26.116
−6.251
13.042
1.00
14.65


ATOM
2178
CG
LEU
A
804
24.861
−5.430
13.347
1.00
15.24


ATOM
2179
CD1
LEU
A
804
24.020
−5.317
12.092
1.00
16.29


ATOM
2180
CD2
LEU
A
804
24.068
−6.089
14.461
1.00
23.77


ATOM
2181
C
LEU
A
804
27.356
−4.252
12.214
1.00
13.48


ATOM
2182
O
LEU
A
804
26.646
−3.317
11.825
1.00
13.22


ATOM
2183
N
MET
A
805
28.476
−4.067
12.904
1.00
12.28


ATOM
2184
CA
MET
A
805
28.909
−2.725
13.276
1.00
11.75


ATOM
2185
CB
MET
A
805
29.141
−2.671
14.790
1.00
13.28


ATOM
2186
CG
MET
A
805
27.859
−2.865
15.589
1.00
33.42


ATOM
2187
SD
MET
A
805
28.125
−3.166
17.338
1.00
47.91


ATOM
2188
CE
MET
A
805
26.447
−3.244
17.925
1.00
28.62


ATOM
2189
C
MET
A
805
30.160
−2.268
12.542
1.00
11.31


ATOM
2190
O
MET
A
805
30.761
−1.259
12.908
1.00
12.42


ATOM
2191
N
ASN
A
806
30.530
−2.992
11.490
1.00
11.94


ATOM
2192
CA
ASN
A
806
31.726
−2.673
10.712
1.00
13.21


ATOM
2193
CB
ASN
A
806
32.537
−3.954
10.471
1.00
13.42


ATOM
2194
CG
ASN
A
806
33.907
−3.676
9.876
1.00
16.11


ATOM
2195
OD1
ASN
A
806
34.209
−2.549
9.484
1.00
17.92


ATOM
2196
ND2
ASN
A
806
34.740
−4.706
9.802
1.00
15.54


ATOM
2197
C
ASN
A
806
31.371
−2.023
9.374
1.00
14.20


ATOM
2198
O
ASN
A
806
30.988
−2.715
8.430
1.00
14.08


ATOM
2199
N
ARG
A
807
31.508
−0.699
9.296
1.00
12.56


ATOM
2200
CA
ARG
A
807
31.189
0.037
8.075
1.00
14.91


ATOM
2201
CB
ARG
A
807
31.410
1.543
8.275
1.00
16.99


ATOM
2202
CG
ARG
A
807
30.891
2.385
7.116
1.00
25.83


ATOM
2203
CD
ARG
A
807
31.162
3.881
7.280
1.00
30.30


ATOM
2204
NE
ARG
A
807
30.520
4.470
8.457
1.00
20.02


ATOM
2205
CZ
ARG
A
807
31.078
4.525
9.662
1.00
16.27


ATOM
2206
NH1
ARG
A
807
32.290
4.025
9.854
1.00
20.90


ATOM
2207
NH2
ARG
A
807
30.431
5.095
10.670
1.00
15.75


ATOM
2208
C
ARG
A
807
32.021
−0.442
6.889
1.00
13.89


ATOM
2209
O
ARG
A
807
31.573
−0.392
5.736
1.00
13.84


ATOM
2210
N
GLU
A
808
33.228
−0.910
7.177
1.00
11.68


ATOM
2211
CA
GLU
A
808
34.122
−1.397
6.137
1.00
17.06


ATOM
2212
CB
GLU
A
808
35.502
−1.675
6.731
1.00
16.87


ATOM
2213
CG
GLU
A
808
36.256
−0.394
7.085
1.00
22.64


ATOM
2214
CD
GLU
A
808
37.556
−0.645
7.819
1.00
24.85


ATOM
2215
OE1
GLU
A
808
38.293
−1.576
7.430
1.00
26.32


ATOM
2216
OE2
GLU
A
808
37.846
0.100
8.780
1.00
36.15


ATOM
2217
C
GLU
A
808
33.565
−2.641
5.461
1.00
15.58


ATOM
2218
O
GLU
A
808
33.929
−2.956
4.329
1.00
15.69


ATOM
2219
N
LYS
A
809
32.677
−3.343
6.156
1.00
14.84


ATOM
2220
CA
LYS
A
809
32.062
−4.544
5.600
1.00
16.67


ATOM
2221
CB
LYS
A
809
32.381
−5.765
6.478
1.00
12.30


ATOM
2222
CG
LYS
A
809
33.845
−6.184
6.405
1.00
13.87


ATOM
2223
CD
LYS
A
809
34.151
−7.408
7.259
1.00
14.82


ATOM
2224
CE
LYS
A
809
33.430
−8.641
6.745
1.00
25.64


ATOM
2225
NZ
LYS
A
809
33.789
−9.854
7.534
1.00
21.95


ATOM
2226
C
LYS
A
809
30.555
−4.363
5.445
1.00
15.95


ATOM
2227
O
LYS
A
809
29.770
−5.281
5.693
1.00
18.05


ATOM
2228
N
LYS
A
810
30.156
−3.167
5.022
1.00
15.13


ATOM
2229
CA
LYS
A
810
28.742
−2.867
4.828
1.00
16.24


ATOM
2230
CB
LYS
A
810
28.549
−1.383
4.494
1.00
14.35


ATOM
2231
CG
LYS
A
810
29.347
−0.869
3.312
1.00
24.48


ATOM
2232
CD
LYS
A
810
29.222
0.647
3.226
1.00
29.64


ATOM
2233
CE
LYS
A
810
29.994
1.224
2.049
1.00
35.68


ATOM
2234
NZ
LYS
A
810
29.432
0.786
0.746
1.00
42.39


ATOM
2235
C
LYS
A
810
28.139
−3.744
3.734
1.00
14.42


ATOM
2236
O
LYS
A
810
26.921
−3.843
3.607
1.00
14.44


ATOM
2237
N
ASN
A
811
28.995
−4.389
2.950
1.00
13.62


ATOM
2238
CA
ASN
A
811
28.511
−5.270
1.893
1.00
13.60


ATOM
2239
CB
ASN
A
811
29.680
−5.746
1.016
1.00
18.14


ATOM
2240
CG
ASN
A
811
30.815
−6.340
1.826
1.00
21.65


ATOM
2241
OD1
ASN
A
811
30.936
−7.559
1.958
1.00
17.54


ATOM
2242
ND2
ASN
A
811
31.651
−5.472
2.388
1.00
13.93


ATOM
2243
C
ASN
A
811
27.777
−6.474
2.487
1.00
14.60


ATOM
2244
O
ASN
A
811
27.084
−7.197
1.777
1.00
13.25


ATOM
2245
N
LYS
A
812
27.922
−6.677
3.796
1.00
14.05


ATOM
2246
CA
LYS
A
812
27.279
−7.797
4.478
1.00
15.17


ATOM
2247
CB
LYS
A
812
28.057
−8.150
5.753
1.00
15.23


ATOM
2248
CG
LYS
A
812
29.401
−8.803
5.500
1.00
20.27


ATOM
2249
CD
LYS
A
812
29.198
−10.137
4.817
1.00
28.44


ATOM
2250
CE
LYS
A
812
30.497
−10.886
4.658
1.00
35.44


ATOM
2251
NZ
LYS
A
812
30.257
−12.223
4.048
1.00
38.51


ATOM
2252
C
LYS
A
812
25.818
−7.542
4.859
1.00
15.78


ATOM
2253
O
LYS
A
812
25.109
−8.475
5.258
1.00
13.98


ATOM
2254
N
ILE
A
813
25.366
−6.297
4.724
1.00
14.64


ATOM
2255
CA
ILE
A
813
24.012
−5.964
5.144
1.00
14.83


ATOM
2256
CB
ILE
A
813
23.770
−4.460
5.007
1.00
15.21


ATOM
2257
CG2
ILE
A
813
22.264
−4.158
5.091
1.00
15.81


ATOM
2258
CG1
ILE
A
813
24.616
−3.740
6.073
1.00
13.99


ATOM
2259
CD1
ILE
A
813
24.445
−2.265
6.070
1.00
27.43


ATOM
2260
C
ILE
A
813
22.862
−6.792
4.546
1.00
14.67


ATOM
2261
O
ILE
A
813
22.042
−7.309
5.270
1.00
13.44


ATOM
2262
N
PRO
A
814
22.807
−6.936
3.224
1.00
12.07


ATOM
2263
CD
PRO
A
814
23.603
−6.274
2.191
1.00
14.86


ATOM
2264
CA
PRO
A
814
21.709
−7.724
2.623
1.00
14.39


ATOM
2265
CB
PRO
A
814
22.060
−7.714
1.152
1.00
13.45


ATOM
2266
CG
PRO
A
814
22.693
−6.351
1.001
1.00
14.67


ATOM
2267
C
PRO
A
814
21.605
−9.144
3.185
1.00
11.82


ATOM
2268
O
PRO
A
814
20.525
−9.603
3.570
1.00
12.87


ATOM
2269
N
SER
A
815
22.730
−9.846
3.215
1.00
11.71


ATOM
2270
CA
SER
A
815
22.730
−11.205
3.729
1.00
13.13


ATOM
2271
CB
SER
A
815
24.102
−11.863
3.526
1.00
14.66


ATOM
2272
OG
SER
A
815
25.124
−11.185
4.233
1.00
27.24


ATOM
2273
C
SER
A
815
22.366
−11.220
5.212
1.00
14.09


ATOM
2274
O
SER
A
815
21.677
−12.120
5.682
1.00
14.61


ATOM
2275
N
MET
A
816
22.809
−10.211
5.937
1.00
14.82


ATOM
2276
CA
MET
A
816
22.498
−10.197
7.353
1.00
14.08


ATOM
2277
CB
MET
A
816
23.449
−9.254
8.079
1.00
16.95


ATOM
2278
CG
MET
A
816
24.829
−9.872
8.232
1.00
19.08


ATOM
2279
SD
MET
A
816
26.019
−8.905
9.168
1.00
23.16


ATOM
2280
CE
MET
A
816
25.502
−9.310
10.812
1.00
29.41


ATOM
2281
C
MET
A
816
21.057
−9.838
7.628
1.00
12.78


ATOM
2282
O
MET
A
816
20.477
−10.281
8.613
1.00
13.06


ATOM
2283
N
GLN
A
817
20.464
−9.010
6.765
1.00
11.62


ATOM
2284
CA
GLN
A
817
19.061
−8.637
6.915
1.00
11.33


ATOM
2285
CB
GLN
A
817
18.666
−7.547
5.899
1.00
12.94


ATOM
2286
CG
GLN
A
817
19.186
−6.179
6.283
1.00
11.95


ATOM
2287
CD
GLN
A
817
18.469
−5.624
7.500
1.00
17.94


ATOM
2288
OE1
GLN
A
817
18.544
−6.183
8.595
1.00
34.56


ATOM
2289
NE2
GLN
A
817
17.759
−4.523
7.309
1.00
34.13


ATOM
2290
C
GLN
A
817
18.202
−9.882
6.714
1.00
13.31


ATOM
2291
O
GLN
A
817
17.254
−10.116
7.472
1.00
10.14


ATOM
2292
N
VAL
A
818
18.537
−10.698
5.715
1.00
12.18


ATOM
2293
CA
VAL
A
818
17.774
−11.918
5.479
1.00
11.53


ATOM
2294
CB
VAL
A
818
18.252
−12.659
4.210
1.00
13.56


ATOM
2295
CG1
VAL
A
818
17.500
−13.972
4.063
1.00
10.58


ATOM
2296
CG2
VAL
A
818
18.032
−11.781
2.982
1.00
17.92


ATOM
2297
C
VAL
A
818
17.903
−12.858
6.678
1.00
11.51


ATOM
2298
O
VAL
A
818
16.930
−13.494
7.090
1.00
12.55


ATOM
2299
N
GLY
A
819
19.110
−12.934
7.231
1.00
11.44


ATOM
2300
CA
GLY
A
819
19.356
−13.791
8.376
1.00
12.74


ATOM
2301
C
GLY
A
819
18.556
−13.335
9.579
1.00
13.96


ATOM
2302
O
GLY
A
819
18.068
−14.149
10.360
1.00
13.49


ATOM
2303
N
PHE
A
820
18.430
−12.022
9.725
1.00
14.20


ATOM
2304
CA
PHE
A
820
17.682
−11.426
10.825
1.00
11.70


ATOM
2305
CB
PHE
A
820
17.927
−9.913
10.833
1.00
11.32


ATOM
2306
CG
PHE
A
820
17.122
−9.167
11.858
1.00
9.99


ATOM
2307
CD1
PHE
A
820
17.268
−9.436
13.209
1.00
23.52


ATOM
2308
CD2
PHE
A
820
16.225
−8.184
11.466
1.00
17.26


ATOM
2309
CE1
PHE
A
820
16.529
−8.740
14.151
1.00
19.87


ATOM
2310
CE2
PHE
A
820
15.485
−7.488
12.403
1.00
16.59


ATOM
2311
CZ
PHE
A
820
15.640
−7.767
13.746
1.00
17.66


ATOM
2312
C
PHE
A
820
16.191
−11.731
10.651
1.00
12.70


ATOM
2313
O
PHE
A
820
15.498
−12.103
11.604
1.00
10.72


ATOM
2314
N
ILE
A
821
15.697
−11.571
9.429
1.00
10.04


ATOM
2315
CA
ILE
A
821
14.298
−11.850
9.150
1.00
9.29


ATOM
2316
CB
ILE
A
821
13.957
−11.540
7.679
1.00
10.14


ATOM
2317
CG2
ILE
A
821
12.617
−12.166
7.307
1.00
12.87


ATOM
2318
CG1
ILE
A
821
13.931
−10.022
7.479
1.00
12.03


ATOM
2319
CD1
ILE
A
821
13.795
−9.580
6.037
1.00
14.77


ATOM
2320
C
ILE
A
821
13.991
−13.311
9.462
1.00
11.67


ATOM
2321
O
ILE
A
821
13.012
−13.617
10.140
1.00
11.27


ATOM
2322
N
ASP
A
822
14.841
−14.215
8.985
1.00
11.97


ATOM
2323
CA
ASP
A
822
14.634
−15.637
9.237
1.00
14.30


ATOM
2324
CB
ASP
A
822
15.630
−16.479
8.428
1.00
17.59


ATOM
2325
CG
ASP
A
822
15.317
−16.499
6.942
1.00
17.92


ATOM
2326
OD1
ASP
A
822
14.177
−16.153
6.564
1.00
15.98


ATOM
2327
OD2
ASP
A
822
16.212
−16.880
6.152
1.00
13.97


ATOM
2328
C
ASP
A
822
14.759
−16.021
10.714
1.00
15.42


ATOM
2329
O
ASP
A
822
13.876
−16.671
11.275
1.00
16.53


ATOM
2330
N
ALA
A
823
15.849
−15.608
11.345
1.00
13.55


ATOM
2331
CA
ALA
A
823
16.101
−15.971
12.737
1.00
15.03


ATOM
2332
CB
ALA
A
823
17.580
−15.756
13.058
1.00
13.84


ATOM
2333
C
ALA
A
823
15.254
−15.299
13.810
1.00
15.13


ATOM
2334
O
ALA
A
823
14.907
−15.928
14.810
1.00
17.91


ATOM
2335
N
ILE
A
824
14.914
−14.032
13.606
1.00
13.91


ATOM
2336
CA
ILE
A
824
14.169
−13.281
14.611
1.00
14.87


ATOM
2337
CB
ILE
A
824
14.929
−11.971
14.966
1.00
16.51


ATOM
2338
CG2
ILE
A
824
14.085
−11.106
15.891
1.00
11.92


ATOM
2339
CG1
ILE
A
824
16.291
−12.293
15.589
1.00
19.03


ATOM
2340
CD1
ILE
A
824
16.211
−12.966
16.938
1.00
17.79


ATOM
2341
C
ILE
A
824
12.736
−12.872
14.271
1.00
15.38


ATOM
2342
O
ILE
A
824
11.817
−13.051
15.077
1.00
15.58


ATOM
2343
N
CYS
A
825
12.548
−12.332
13.074
1.00
11.66


ATOM
2344
CA
CYS
A
825
11.248
−11.798
12.682
1.00
10.83


ATOM
2345
CB
CYS
A
825
11.470
−10.717
11.629
1.00
14.06


ATOM
2346
SG
CYS
A
825
12.684
−9.498
12.156
1.00
12.72


ATOM
2347
C
CYS
A
825
10.094
−12.685
12.231
1.00
12.83


ATOM
2348
O
CYS
A
825
9.003
−12.606
12.792
1.00
11.78


ATOM
2349
N
LEU
A
826
10.312
−13.508
11.213
1.00
10.64


ATOM
2350
CA
LEU
A
826
9.230
−14.343
10.699
1.00
12.29


ATOM
2351
CB
LEU
A
826
9.759
−15.291
9.621
1.00
17.45


ATOM
2352
CG
LEU
A
826
10.132
−14.585
8.314
1.00
14.44


ATOM
2353
CD1
LEU
A
826
10.756
−15.585
7.355
1.00
19.69


ATOM
2354
CD2
LEU
A
826
8.884
−13.965
7.693
1.00
17.13


ATOM
2355
C
LEU
A
826
8.428
−15.131
11.735
1.00
11.75


ATOM
2356
O
LEU
A
826
7.194
−15.094
11.728
1.00
12.87


ATOM
2357
N
GLN
A
827
9.115
−15.842
12.620
1.00
9.56


ATOM
2358
CA
GLN
A
827
8.426
−16.637
13.632
1.00
10.96


ATOM
2359
CB
GLN
A
827
9.438
−17.368
14.507
1.00
9.95


ATOM
2360
CG
GLN
A
827
10.207
−18.465
13.805
1.00
14.60


ATOM
2361
CD
GLN
A
827
11.365
−18.949
14.646
1.00
27.21


ATOM
2362
OE1
GLN
A
827
12.420
−18.312
14.695
1.00
20.68


ATOM
2363
NE2
GLN
A
827
11.169
−20.068
15.335
1.00
24.19


ATOM
2364
C
GLN
A
827
7.516
−15.798
14.524
1.00
13.14


ATOM
2365
O
GLN
A
827
6.428
−16.235
14.906
1.00
13.21


ATOM
2366
N
LEU
A
828
7.966
−14.596
14.862
1.00
10.02


ATOM
2367
CA
LEU
A
828
7.182
−13.713
15.720
1.00
10.78


ATOM
2368
CB
LEU
A
828
8.037
−12.521
16.166
1.00
9.67


ATOM
2369
CG
LEU
A
828
7.315
−11.431
16.966
1.00
14.41


ATOM
2370
CD1
LEU
A
828
6.653
−12.048
18.185
1.00
16.13


ATOM
2371
CD2
LEU
A
828
8.300
−10.351
17.389
1.00
14.03


ATOM
2372
C
LEU
A
828
5.902
−13.218
15.036
1.00
11.55


ATOM
2373
O
LEU
A
828
4.814
−13.290
15.609
1.00
12.50


ATOM
2374
N
TYR
A
829
6.024
−12.717
13.812
1.00
10.38


ATOM
2375
CA
TYR
A
829
4.851
−12.217
13.109
1.00
11.38


ATOM
2376
CB
TYR
A
829
5.286
−11.392
11.892
1.00
9.07


ATOM
2377
CG
TYR
A
829
5.967
−10.112
12.324
1.00
13.32


ATOM
2378
CD1
TYR
A
829
5.298
−9.189
13.118
1.00
8.62


ATOM
2379
CE1
TYR
A
829
5.926
−8.037
13.569
1.00
10.58


ATOM
2380
CD2
TYR
A
829
7.290
−9.849
11.989
1.00
10.78


ATOM
2381
CE2
TYR
A
829
7.930
−8.699
12.440
1.00
8.02


ATOM
2382
CZ
TYR
A
829
7.241
−7.800
13.228
1.00
8.64


ATOM
2383
OH
TYR
A
829
7.867
−6.659
13.688
1.00
10.63


ATOM
2384
C
TYR
A
829
3.908
−13.349
12.731
1.00
12.07


ATOM
2385
O
TYR
A
829
2.704
−13.140
12.594
1.00
14.07


ATOM
2386
N
GLU
A
830
4.452
−14.555
12.585
1.00
14.19


ATOM
2387
CA
GLU
A
830
3.614
−15.709
12.274
1.00
14.53


ATOM
2388
CB
GLU
A
830
4.469
−16.919
11.881
1.00
15.21


ATOM
2389
CG
GLU
A
830
5.196
−16.751
10.557
1.00
18.48


ATOM
2390
CD
GLU
A
830
6.057
−17.948
10.208
1.00
27.35


ATOM
2391
OE1
GLU
A
830
6.422
−18.701
11.133
1.00
25.55


ATOM
2392
OE2
GLU
A
830
6.380
−18.127
9.014
1.00
25.64


ATOM
2393
C
GLU
A
830
2.806
−16.027
13.531
1.00
15.34


ATOM
2394
O
GLU
A
830
1.594
−16.245
13.462
1.00
15.05


ATOM
2395
N
ALA
A
831
3.484
−16.037
14.679
1.00
12.88


ATOM
2396
CA
ALA
A
831
2.836
−16.319
15.958
1.00
13.60


ATOM
2397
CB
ALA
A
831
3.877
−16.341
17.080
1.00
14.75


ATOM
2398
C
ALA
A
831
1.764
−15.279
16.264
1.00
14.36


ATOM
2399
O
ALA
A
831
0.666
−15.617
16.714
1.00
13.70


ATOM
2400
N
LEU
A
832
2.085
−14.010
16.026
1.00
11.70


ATOM
2401
CA
LEU
A
832
1.135
−12.935
16.276
1.00
12.90


ATOM
2402
CB
LEU
A
832
1.800
−11.577
16.030
1.00
12.02


ATOM
2403
CG
LEU
A
832
0.935
−10.334
16.256
1.00
13.07


ATOM
2404
CD1
LEU
A
832
0.367
−10.354
17.670
1.00
16.97


ATOM
2405
CD2
LEU
A
832
1.764
−9.076
16.018
1.00
12.70


ATOM
2406
C
LEU
A
832
−0.093
−13.098
15.382
1.00
13.07


ATOM
2407
O
LEU
A
832
−1.221
−12.851
15.811
1.00
12.63


ATOM
2408
N
THR
A
833
0.125
−13.522
14.140
1.00
10.33


ATOM
2409
CA
THR
A
833
−0.985
−13.720
13.213
1.00
11.65


ATOM
2410
CB
THR
A
833
−0.471
−14.019
11.798
1.00
15.54


ATOM
2411
OG1
THR
A
833
0.250
−12.881
11.309
1.00
13.44


ATOM
2412
CG2
THR
A
833
−1.631
−14.319
10.856
1.00
20.09


ATOM
2413
C
THR
A
833
−1.856
−14.875
13.709
1.00
13.24


ATOM
2414
O
THR
A
833
−3.070
−14.879
13.512
1.00
14.62


ATOM
2415
N
HIS
A
834
−1.233
−15.855
14.358
1.00
12.04


ATOM
2416
CA
HIS
A
834
−1.974
−16.988
14.901
1.00
15.35


ATOM
2417
CB
HIS
A
834
−1.010
−18.045
15.451
1.00
17.31


ATOM
2418
CG
HIS
A
834
−1.686
−19.161
16.174
1.00
21.70


ATOM
2419
CD2
HIS
A
834
−2.005
−20.422
15.792
1.00
27.35


ATOM
2420
ND1
HIS
A
834
−2.158
−19.040
17.471
1.00
27.23


ATOM
2421
CE1
HIS
A
834
−2.728
−20.162
17.843
1.00
22.73


ATOM
2422
NE2
HIS
A
834
−2.650
−21.026
16.836
1.00
26.03


ATOM
2423
C
HIS
A
834
−2.907
−16.495
16.011
1.00
16.43


ATOM
2424
O
HIS
A
834
−4.061
−16.917
16.101
1.00
16.32


ATOM
2425
N
VAL
A
835
−2.402
−15.600
16.852
1.00
14.39


ATOM
2426
CA
VAL
A
835
−3.201
−15.042
17.940
1.00
16.17


ATOM
2427
CB
VAL
A
835
−2.329
−14.177
18.879
1.00
20.06


ATOM
2428
CG1
VAL
A
835
−3.203
−13.433
19.878
1.00
26.18


ATOM
2429
CG2
VAL
A
835
−1.336
−15.067
19.616
1.00
22.85


ATOM
2430
C
VAL
A
835
−4.345
−14.196
17.376
1.00
18.30


ATOM
2431
O
VAL
A
835
−5.462
−14.219
17.899
1.00
16.68


ATOM
2432
N
SER
A
836
−4.061
−13.461
16.302
1.00
15.55


ATOM
2433
CA
SER
A
836
−5.060
−12.620
15.646
1.00
15.62


ATOM
2434
CB
SER
A
836
−5.081
−11.222
16.267
1.00
18.44


ATOM
2435
OG
SER
A
836
−6.092
−10.430
15.665
1.00
24.05


ATOM
2436
C
SER
A
836
−4.744
−12.516
14.153
1.00
15.03


ATOM
2437
O
SER
A
836
−3.754
−11.901
13.759
1.00
14.82


ATOM
2438
N
GLU
A
837
−5.596
−13.123
13.334
1.00
16.29


ATOM
2439
CA
GLU
A
837
−5.423
−13.139
11.886
1.00
16.40


ATOM
2440
CB
GLU
A
837
−6.578
−13.922
11.244
1.00
19.29


ATOM
2441
CG
GLU
A
837
−6.524
−14.017
9.722
1.00
30.56


ATOM
2442
CD
GLU
A
837
−5.259
−14.685
9.213
1.00
40.78


ATOM
2443
OE1
GLU
A
837
−4.925
−15.785
9.704
1.00
33.63


ATOM
2444
OE2
GLU
A
837
−4.603
−14.112
8.316
1.00
45.55


ATOM
2445
C
GLU
A
837
−5.324
−11.749
11.256
1.00
14.00


ATOM
2446
O
GLU
A
837
−4.672
−11.574
10.227
1.00
16.56


ATOM
2447
N
ASP
A
838
−5.967
−10.762
11.871
1.00
14.38


ATOM
2448
CA
ASP
A
838
−5.938
−9.402
11.349
1.00
12.78


ATOM
2449
CB
ASP
A
838
−6.990
−8.547
12.060
1.00
12.80


ATOM
2450
CG
ASP
A
838
−8.410
−8.929
11.669
1.00
31.66


ATOM
2451
OD1
ASP
A
838
−8.770
−8.750
10.487
1.00
25.15


ATOM
2452
OD2
ASP
A
838
−9.162
−9.414
12.540
1.00
29.94


ATOM
2453
C
ASP
A
838
−4.558
−8.751
11.468
1.00
11.81


ATOM
2454
O
ASP
A
838
−4.355
−7.625
11.017
1.00
12.87


ATOM
2455
N
CYS
A
839
−3.610
−9.456
12.080
1.00
14.34


ATOM
2456
CA
CYS
A
839
−2.254
−8.929
12.203
1.00
14.23


ATOM
2457
CB
CYS
A
839
−1.619
−9.354
13.533
1.00
12.27


ATOM
2458
SG
CYS
A
839
−2.115
−8.349
14.969
1.00
12.53


ATOM
2459
C
CYS
A
839
−1.412
−9.440
11.038
1.00
15.74


ATOM
2460
O
CYS
A
839
−0.222
−9.142
10.941
1.00
13.52


ATOM
2461
N
PHE
A
840
−2.044
−10.209
10.152
1.00
14.15


ATOM
2462
CA
PHE
A
840
−1.364
−10.765
8.983
1.00
14.85


ATOM
2463
CB
PHE
A
840
−2.370
−11.451
8.052
1.00
18.01


ATOM
2464
CG
PHE
A
840
−1.760
−11.926
6.764
1.00
16.92


ATOM
2465
CD1
PHE
A
840
−0.886
−13.001
6.751
1.00
13.52


ATOM
2466
CD2
PHE
A
840
−2.010
−11.257
5.575
1.00
19.38


ATOM
2467
CE1
PHE
A
840
−0.269
−13.398
5.575
1.00
23.30


ATOM
2468
CE2
PHE
A
840
−1.397
−11.649
4.396
1.00
23.75


ATOM
2469
CZ
PHE
A
840
−0.525
−12.720
4.397
1.00
22.76


ATOM
2470
C
PHE
A
840
−0.541
−9.768
8.155
1.00
13.70


ATOM
2471
O
PHE
A
840
0.546
−10.105
7.678
1.00
13.33


ATOM
2472
N
PRO
A
841
−1.049
−8.537
7.958
1.00
12.97


ATOM
2473
CD
PRO
A
841
−2.369
−8.002
8.339
1.00
14.47


ATOM
2474
CA
PRO
A
841
−0.294
−7.557
7.168
1.00
12.84


ATOM
2475
CB
PRO
A
841
−1.127
−6.287
7.312
1.00
14.37


ATOM
2476
CG
PRO
A
841
−2.533
−6.826
7.391
1.00
14.58


ATOM
2477
C
PRO
A
841
1.151
−7.367
7.630
1.00
14.54


ATOM
2478
O
PRO
A
841
2.034
−7.065
6.826
1.00
13.75


ATOM
2479
N
LEU
A
842
1.393
−7.530
8.926
1.00
11.66


ATOM
2480
CA
LEU
A
842
2.747
−7.384
9.444
1.00
12.35


ATOM
2481
CB
LEU
A
842
2.732
−7.430
10.977
1.00
11.85


ATOM
2482
CG
LEU
A
842
2.039
−6.228
11.624
1.00
12.78


ATOM
2483
CD1
LEU
A
842
1.900
−6.434
13.131
1.00
14.23


ATOM
2484
CD2
LEU
A
842
2.837
−4.975
11.321
1.00
14.25


ATOM
2485
C
LEU
A
842
3.613
−8.513
8.880
1.00
13.95


ATOM
2486
O
LEU
A
842
4.741
−8.290
8.444
1.00
13.84


ATOM
2487
N
LEU
A
843
3.067
−9.727
8.882
1.00
11.90


ATOM
2488
CA
LEU
A
843
3.779
−10.889
8.359
1.00
11.64


ATOM
2489
CB
LEU
A
843
2.995
−12.161
8.670
1.00
10.07


ATOM
2490
CG
LEU
A
843
3.532
−13.468
8.084
1.00
9.50


ATOM
2491
CD1
LEU
A
843
4.940
−13.735
8.588
1.00
13.64


ATOM
2492
CD2
LEU
A
843
2.597
−14.608
8.466
1.00
12.37


ATOM
2493
C
LEU
A
843
3.971
−10.751
6.847
1.00
11.74


ATOM
2494
O
LEU
A
843
5.054
−11.003
6.319
1.00
13.14


ATOM
2495
N
ASP
A
844
2.909
−10.342
6.160
1.00
13.31


ATOM
2496
CA
ASP
A
844
2.943
−10.154
4.711
1.00
14.45


ATOM
2497
CB
ASP
A
844
1.573
−9.639
4.245
1.00
18.19


ATOM
2498
CG
ASP
A
844
1.354
−9.771
2.739
1.00
13.51


ATOM
2499
OD1
ASP
A
844
2.141
−10.459
2.057
1.00
18.86


ATOM
2500
OD2
ASP
A
844
0.367
−9.187
2.243
1.00
17.91


ATOM
2501
C
ASP
A
844
4.053
−9.153
4.366
1.00
13.87


ATOM
2502
O
ASP
A
844
4.854
−9.386
3.460
1.00
13.07


ATOM
2503
N
GLY
A
845
4.100
−8.046
5.104
1.00
12.67


ATOM
2504
CA
GLY
A
845
5.115
−7.035
4.862
1.00
11.69


ATOM
2505
C
GLY
A
845
6.529
−7.540
5.097
1.00
11.05


ATOM
2506
O
GLY
A
845
7.447
−7.240
4.330
1.00
12.51


ATOM
2507
N
CYS
A
846
6.704
−8.314
6.161
1.00
10.28


ATOM
2508
CA
CYS
A
846
8.005
−8.882
6.507
1.00
10.93


ATOM
2509
CB
CYS
A
846
7.889
−9.643
7.831
1.00
14.58


ATOM
2510
SG
CYS
A
846
9.443
−10.273
8.485
1.00
12.82


ATOM
2511
C
CYS
A
846
8.497
−9.821
5.398
1.00
11.92


ATOM
2512
O
CYS
A
846
9.661
−9.762
4.985
1.00
11.24


ATOM
2513
N
ARG
A
847
7.605
−10.683
4.914
1.00
12.77


ATOM
2514
CA
ARG
A
847
7.953
−11.618
3.853
1.00
13.72


ATOM
2515
CB
ARG
A
847
6.762
−12.527
3.535
1.00
11.63


ATOM
2516
CG
ARG
A
847
6.457
−13.545
4.619
1.00
13.10


ATOM
2517
CD
ARG
A
847
5.180
−14.308
4.316
1.00
17.35


ATOM
2518
NE
ARG
A
847
4.978
−15.402
5.262
1.00
19.23


ATOM
2519
CZ
ARG
A
847
3.840
−16.077
5.389
1.00
21.47


ATOM
2520
NH1
ARG
A
847
2.796
−15.769
4.632
1.00
24.29


ATOM
2521
NH2
ARG
A
847
3.750
−17.059
6.275
1.00
27.21


ATOM
2522
C
ARG
A
847
8.371
−10.870
2.592
1.00
13.53


ATOM
2523
O
ARG
A
847
9.320
−11.265
1.906
1.00
13.20


ATOM
2524
N
LYS
A
848
7.659
−9.793
2.283
1.00
12.35


ATOM
2525
CA
LYS
A
848
7.977
−9.007
1.099
1.00
14.65


ATOM
2526
CB
LYS
A
848
6.925
−7.915
0.880
1.00
16.22


ATOM
2527
CG
LYS
A
848
5.567
−8.447
0.413
1.00
14.77


ATOM
2528
CD
LYS
A
848
4.579
−7.308
0.195
1.00
19.65


ATOM
2529
CE
LYS
A
848
3.210
−7.817
−0.206
1.00
19.42


ATOM
2530
NZ
LYS
A
848
2.214
−6.709
−0.212
1.00
23.11


ATOM
2531
C
LYS
A
848
9.364
−8.392
1.229
1.00
14.80


ATOM
2532
O
LYS
A
848
10.112
−8.319
0.253
1.00
13.12


ATOM
2533
N
ASN
A
849
9.713
−7.953
2.435
1.00
13.42


ATOM
2534
CA
ASN
A
849
11.034
−7.369
2.648
1.00
13.07


ATOM
2535
CB
ASN
A
849
11.086
−6.646
3.995
1.00
13.67


ATOM
2536
CG
ASN
A
849
10.412
−5.288
3.950
1.00
17.85


ATOM
2537
OD1
ASN
A
849
9.863
−4.821
4.949
1.00
16.87


ATOM
2538
ND2
ASN
A
849
10.461
−4.638
2.790
1.00
13.21


ATOM
2539
C
ASN
A
849
12.122
−8.434
2.568
1.00
12.00


ATOM
2540
O
ASN
A
849
13.252
−8.148
2.165
1.00
11.88


ATOM
2541
N
ARG
A
850
11.797
−9.667
2.945
1.00
11.53


ATOM
2542
CA
ARG
A
850
12.793
−10.729
2.860
1.00
11.98


ATOM
2543
CB
ARG
A
850
12.285
−12.037
3.473
1.00
14.13


ATOM
2544
CG
ARG
A
850
13.373
−13.110
3.508
1.00
13.55


ATOM
2545
CD
ARG
A
850
12.838
−14.511
3.781
1.00
18.02


ATOM
2546
NE
ARG
A
850
13.930
−15.457
4.001
1.00
16.95


ATOM
2547
CZ
ARG
A
850
14.743
−15.919
3.052
1.00
14.40


ATOM
2548
NH1
ARG
A
850
14.595
−15.533
1.790
1.00
16.03


ATOM
2549
NH2
ARG
A
850
15.727
−16.754
3.373
1.00
12.51


ATOM
2550
C
ARG
A
850
13.138
−10.972
1.399
1.00
13.81


ATOM
2551
O
ARG
A
850
14.304
−11.151
1.054
1.00
15.14


ATOM
2552
N
GLN
A
851
12.118
−10.985
0.542
1.00
16.03


ATOM
2553
CA
GLN
A
851
12.317
−11.193
−0.892
1.00
15.42


ATOM
2554
CB
GLN
A
851
10.969
−11.156
−1.622
1.00
17.30


ATOM
2555
CG
GLN
A
851
11.039
−11.399
−3.127
1.00
30.46


ATOM
2556
CD
GLN
A
851
11.475
−10.174
−3.912
1.00
34.81


ATOM
2557
OE1
GLN
A
851
10.862
−9.110
−3.814
1.00
37.41


ATOM
2558
NE2
GLN
A
851
12.534
−10.320
−4.704
1.00
40.89


ATOM
2559
C
GLN
A
851
13.229
−10.109
−1.436
1.00
16.49


ATOM
2560
O
GLN
A
851
14.151
−10.371
−2.208
1.00
15.70


ATOM
2561
N
LYS
A
852
12.953
−8.867
−1.014
1.00
15.86


ATOM
2562
CA
LYS
A
852
13.705
−7.685
−1.428
1.00
16.63


ATOM
2563
CB
LYS
A
852
13.065
−6.405
−0.838
1.00
13.58


ATOM
2564
CG
LYS
A
852
11.802
−6.008
−1.561
1.00
18.37


ATOM
2565
CD
LYS
A
852
12.183
−5.582
−2.958
1.00
31.95


ATOM
2566
CE
LYS
A
852
11.002
−5.087
−3.751
1.00
37.83


ATOM
2567
NZ
LYS
A
852
11.421
−4.599
−5.099
1.00
41.92


ATOM
2568
C
LYS
A
852
15.175
−7.754
−1.037
1.00
15.46


ATOM
2569
O
LYS
A
852
16.055
−7.542
−1.874
1.00
14.58


ATOM
2570
N
TRP
A
853
15.446
−8.063
0.225
1.00
12.99


ATOM
2571
CA
TRP
A
853
16.821
−8.168
0.705
1.00
12.72


ATOM
2572
CB
TRP
A
853
16.843
−8.299
2.228
1.00
11.94


ATOM
2573
CG
TRP
A
853
16.640
−7.011
2.957
1.00
11.40


ATOM
2574
CD2
TRP
A
853
17.485
−5.864
2.913
1.00
14.74


ATOM
2575
CE2
TRP
A
853
16.929
−4.888
3.763
1.00
12.41


ATOM
2576
CE3
TRP
A
853
18.675
−5.554
2.236
1.00
10.90


ATOM
2577
CD1
TRP
A
853
15.618
−6.701
3.813
1.00
11.02


ATOM
2578
NE1
TRP
A
853
15.781
−5.429
4.303
1.00
14.15


ATOM
2579
CZ2
TRP
A
853
17.502
−3.638
3.958
1.00
12.03


ATOM
2580
CZ3
TRP
A
853
19.246
−4.312
2.427
1.00
13.77


ATOM
2581
CH2
TRP
A
853
18.663
−3.370
3.280
1.00
16.08


ATOM
2582
C
TRP
A
853
17.543
−9.357
0.074
1.00
13.55


ATOM
2583
O
TRP
A
853
18.722
−9.265
−0.282
1.00
13.19


ATOM
2584
N
GLN
A
854
16.836
−10.472
−0.062
1.00
12.06


ATOM
2585
CA
GLN
A
854
17.427
−11.667
−0.657
1.00
13.49


ATOM
2586
CB
GLN
A
854
16.426
−12.822
−0.630
1.00
13.86


ATOM
2587
CG
GLN
A
854
16.934
−14.128
−1.242
1.00
15.91


ATOM
2588
CD
GLN
A
854
18.267
−14.585
−0.665
1.00
23.66


ATOM
2589
OE1
GLN
A
854
18.544
−14.404
0.520
1.00
20.44


ATOM
2590
NE2
GLN
A
854
19.091
−15.199
−1.504
1.00
26.84


ATOM
2591
C
GLN
A
854
17.869
−11.400
−2.094
1.00
13.14


ATOM
2592
O
GLN
A
854
18.920
−11.880
−2.524
1.00
15.55


ATOM
2593
N
ALA
A
855
17.069
−10.635
−2.832
1.00
14.63


ATOM
2594
CA
ALA
A
855
17.408
−10.318
−4.219
1.00
15.08


ATOM
2595
CB
ALA
A
855
16.264
−9.563
−4.884
1.00
17.06


ATOM
2596
C
ALA
A
855
18.697
−9.504
−4.303
1.00
16.23


ATOM
2597
O
ALA
A
855
19.439
−9.611
−5.278
1.00
17.06


ATOM
2598
N
LEU
A
856
18.959
−8.689
−3.287
1.00
15.11


ATOM
2599
CA
LEU
A
856
20.178
−7.889
−3.261
1.00
17.23


ATOM
2600
CB
LEU
A
856
20.031
−6.715
−2.284
1.00
11.53


ATOM
2601
CG
LEU
A
856
18.968
−5.676
−2.643
1.00
15.60


ATOM
2602
CD1
LEU
A
856
18.996
−4.549
−1.634
1.00
19.73


ATOM
2603
CD2
LEU
A
856
19.226
−5.145
−4.047
1.00
12.95


ATOM
2604
C
LEU
A
856
21.362
−8.754
−2.835
1.00
17.35


ATOM
2605
O
LEU
A
856
22.478
−8.601
−3.337
1.00
17.30


ATOM
2606
N
ALA
A
857
21.109
−9.674
−1.911
1.00
16.52


ATOM
2607
CA
ALA
A
857
22.156
−10.545
−1.396
1.00
17.82


ATOM
2608
CB
ALA
A
857
21.708
−11.155
−0.079
1.00
15.78


ATOM
2609
C
ALA
A
857
22.616
−11.651
−2.339
1.00
19.95


ATOM
2610
O
ALA
A
857
23.781
−12.048
−2.305
1.00
21.30


ATOM
2611
N
GLU
A
858
21.715
−12.144
−3.181
1.00
19.75


ATOM
2612
CA
GLU
A
858
22.059
−13.233
−4.091
1.00
23.14


ATOM
2613
CB
GLU
A
858
20.798
−14.008
−4.475
1.00
28.23


ATOM
2614
CG
GLU
A
858
19.735
−13.155
−5.139
1.00
35.46


ATOM
2615
CD
GLU
A
858
18.516
−13.957
−5.548
1.00
41.30


ATOM
2616
OE1
GLU
A
858
17.928
−14.635
−4.679
1.00
46.06


ATOM
2617
OE2
GLU
A
858
18.144
−13.905
−6.739
1.00
53.40


ATOM
2618
C
GLU
A
858
22.773
−12.775
−5.356
1.00
24.66


ATOM
2619
O
GLU
A
858
22.769
−11.561
−5.640
1.00
27.06


ATOM
2620
OXT
GLU
A
858
23.319
−13.654
−6.053
1.00
33.90


TER
2621

GLU
A
858


ATOM
2622
O
HOH
W
1
14.659
12.373
18.930
1.00
11.90


ATOM
2623
O
HOH
W
2
9.029
0.616
15.467
1.00
15.60


ATOM
2624
O
HOH
W
3
17.339
−0.310
24.269
1.00
9.87


ATOM
2625
O
HOH
W
4
17.787
8.492
22.312
1.00
9.91


ATOM
2626
O
HOH
W
5
22.322
0.101
41.405
1.00
10.58


ATOM
2627
O
HOH
W
6
7.037
−4.929
2.938
1.00
15.52


ATOM
2628
O
HOH
W
7
24.844
0.942
17.890
1.00
12.19


ATOM
2629
O
HOH
W
8
17.812
−5.285
21.940
1.00
13.09


ATOM
2630
O
HOH
W
9
19.355
−1.244
21.749
1.00
11.09


ATOM
2631
O
HOH
W
10
11.998
−15.929
13.123
1.00
15.08


ATOM
2632
O
HOH
W
11
17.595
6.868
5.858
1.00
17.40


ATOM
2633
O
HOH
W
12
20.522
−8.124
28.490
1.00
16.30


ATOM
2634
O
HOH
W
13
7.122
8.426
30.706
1.00
12.74


ATOM
2635
O
HOH
W
14
14.281
−0.736
24.882
1.00
10.20


ATOM
2636
O
HOH
W
15
27.778
−4.812
7.714
1.00
14.34


ATOM
2637
O
HOH
W
16
45.697
−5.856
19.373
1.00
13.79


ATOM
2638
O
HOH
W
17
32.028
0.851
11.859
1.00
12.49


ATOM
2639
O
HOH
W
18
12.716
−7.833
22.260
1.00
11.62


ATOM
2640
O
HOH
W
19
20.770
−7.019
24.953
1.00
13.66


ATOM
2641
O
HOH
W
20
9.679
−8.387
30.457
1.00
18.04


ATOM
2642
O
HOH
W
21
20.996
−1.566
19.584
1.00
15.27


ATOM
2643
O
HOH
W
22
5.367
−8.570
29.548
1.00
17.36


ATOM
2644
O
HOH
W
23
25.138
−9.337
1.725
1.00
17.63


ATOM
2645
O
HOH
W
24
−9.020
−0.116
43.708
1.00
15.91


ATOM
2646
O
HOH
W
25
22.657
−6.174
29.194
1.00
17.18


ATOM
2647
O
HOH
W
26
−4.280
19.557
21.192
1.00
19.85


ATOM
2648
O
HOH
W
27
14.289
6.604
13.852
1.00
14.85


ATOM
2649
O
HOH
W
28
11.411
−1.302
13.935
1.00
12.80


ATOM
2650
O
HOH
W
29
11.700
13.882
15.200
1.00
14.97


ATOM
2651
O
HOH
W
30
18.410
10.076
12.196
1.00
19.59


ATOM
2652
O
HOH
W
31
26.709
7.571
23.378
1.00
17.44


ATOM
2653
O
HOH
W
32
25.420
5.805
17.773
1.00
17.40


ATOM
2654
O
HOH
W
33
11.087
10.589
10.070
1.00
17.81


ATOM
2655
O
HOH
W
34
11.500
−19.954
26.231
1.00
16.07


ATOM
2656
O
HOH
W
35
−5.204
−5.042
34.106
1.00
17.24


ATOM
2657
O
HOH
W
36
1.941
9.940
36.428
1.00
13.95


ATOM
2658
O
HOH
W
37
23.916
7.238
15.924
1.00
14.00


ATOM
2659
O
HOH
W
38
4.522
21.473
19.911
1.00
20.60


ATOM
2660
O
HOH
W
39
7.654
32.374
24.586
1.00
19.77


ATOM
2661
O
HOH
W
40
−11.105
8.617
12.732
1.00
20.19


ATOM
2662
O
HOH
W
41
14.266
14.289
20.855
1.00
16.50


ATOM
2663
O
HOH
W
42
27.797
−9.140
13.072
1.00
17.28


ATOM
2664
O
HOH
W
43
13.361
−5.781
20.636
1.00
17.62


ATOM
2665
O
HOH
W
44
9.439
17.952
22.920
1.00
20.34


ATOM
2666
O
HOH
W
45
13.506
−19.339
23.851
1.00
17.51


ATOM
2667
O
HOH
W
46
−9.608
−2.484
44.794
1.00
18.03


ATOM
2668
O
HOH
W
47
19.179
−3.517
23.479
1.00
14.63


ATOM
2669
O
HOH
W
48
20.825
−1.771
7.357
1.00
15.56


ATOM
2670
O
HOH
W
49
3.953
−2.401
8.103
1.00
15.98


ATOM
2671
O
HOH
W
50
5.164
2.828
12.389
1.00
17.57


ATOM
2672
O
HOH
W
51
22.475
−6.004
8.390
1.00
20.31


ATOM
2673
O
HOH
W
52
−1.505
−7.713
3.922
1.00
20.93


ATOM
2674
O
HOH
W
53
16.030
13.344
15.066
1.00
22.86


ATOM
2675
O
HOH
W
54
3.120
33.114
17.327
1.00
18.81


ATOM
2676
O
HOH
W
55
6.517
19.676
19.112
1.00
20.43


ATOM
2677
O
HOH
W
56
27.812
5.941
11.269
1.00
19.39


ATOM
2678
O
HOH
W
57
14.704
9.138
12.638
1.00
17.37


ATOM
2679
O
HOH
W
58
10.813
−19.129
28.734
1.00
23.50


ATOM
2680
O
HOH
W
59
9.603
−13.958
1.403
1.00
20.05


ATOM
2681
O
HOH
W
60
46.209
−3.550
17.835
1.00
18.22


ATOM
2682
O
HOH
W
61
24.760
−2.396
10.006
1.00
20.80


ATOM
2683
O
HOH
W
62
11.077
3.087
12.585
1.00
21.05


ATOM
2684
O
HOH
W
63
10.534
−10.726
28.998
1.00
21.18


ATOM
2685
O
HOH
W
64
−0.961
−11.064
33.440
1.00
18.63


ATOM
2686
O
HOH
W
65
20.890
0.577
15.388
1.00
19.77


ATOM
2687
O
HOH
W
66
21.685
13.866
20.281
1.00
24.54


ATOM
2688
O
HOH
W
67
−5.012
−3.878
8.180
1.00
21.24


ATOM
2689
O
HOH
W
68
−10.443
9.371
15.194
1.00
19.03


ATOM
2690
O
HOH
W
69
26.635
8.578
39.152
1.00
19.48


ATOM
2691
O
HOH
W
70
21.837
−4.044
23.094
1.00
14.46


ATOM
2692
O
HOH
W
71
18.979
0.534
3.275
1.00
19.32


ATOM
2693
O
HOH
W
72
−7.687
−4.529
35.484
1.00
19.76


ATOM
2694
O
HOH
W
73
−4.441
9.972
35.483
1.00
21.75


ATOM
2695
O
HOH
W
74
22.147
0.611
18.233
1.00
21.06


ATOM
2696
O
HOH
W
75
25.625
7.694
19.834
1.00
17.79


ATOM
2697
O
HOH
W
76
−9.716
14.941
11.027
1.00
20.22


ATOM
2698
O
HOH
W
77
14.015
−1.710
16.866
1.00
19.03


ATOM
2699
O
HOH
W
78
21.861
−3.953
20.354
1.00
17.68


ATOM
2700
O
HOH
W
79
21.854
−11.471
10.659
1.00
21.05


ATOM
2701
O
HOH
W
80
15.795
−5.944
−4.295
1.00
17.34


ATOM
2702
O
HOH
W
81
26.427
−5.333
20.748
1.00
28.65


ATOM
2703
O
HOH
W
82
0.806
16.637
36.547
1.00
22.11


ATOM
2704
O
HOH
W
83
28.883
5.909
33.300
1.00
35.99


ATOM
2705
O
HOH
W
84
0.615
−5.836
36.804
1.00
21.63


ATOM
2706
O
HOH
W
85
14.416
−12.696
−3.692
1.00
22.36


ATOM
2707
O
HOH
W
86
−4.841
7.644
43.980
1.00
19.92


ATOM
2708
O
HOH
W
87
−6.059
5.564
10.293
1.00
22.49


ATOM
2709
O
HOH
W
88
7.210
1.031
13.002
1.00
19.78


ATOM
2710
O
HOH
W
89
−5.786
−6.329
9.023
1.00
20.32


ATOM
2711
O
HOH
W
90
19.117
4.909
35.027
1.00
17.30


ATOM
2712
O
HOH
W
91
10.592
13.017
38.293
1.00
23.66


ATOM
2713
O
HOH
W
92
−9.801
5.234
16.132
1.00
20.64


ATOM
2714
O
HOH
W
93
−6.370
−17.172
24.540
1.00
23.65


ATOM
2715
O
HOH
W
94
−6.833
1.342
45.207
1.00
17.92


ATOM
2716
O
HOH
W
95
33.715
−7.279
11.000
1.00
17.67


ATOM
2717
O
HOH
W
96
5.722
31.659
29.252
1.00
19.35


ATOM
2718
O
HOH
W
97
14.155
−2.890
10.083
1.00
16.30


ATOM
2719
O
HOH
W
98
19.709
−5.898
20.414
1.00
27.45


ATOM
2720
O
HOH
W
99
4.418
−3.958
2.629
1.00
23.70


ATOM
2721
O
HOH
W
100
5.739
5.419
41.566
1.00
26.30


ATOM
2722
O
HOH
W
101
1.882
−10.334
12.547
1.00
21.56


ATOM
2723
O
HOH
W
102
1.506
9.558
7.516
1.00
21.76


ATOM
2724
O
HOH
W
103
23.211
1.757
4.698
1.00
23.21


ATOM
2725
O
HOH
W
104
36.282
2.363
9.440
1.00
27.13


ATOM
2726
O
HOH
W
105
27.600
−11.267
2.472
1.00
18.59


ATOM
2727
O
HOH
W
106
16.305
16.757
22.862
1.00
25.14


ATOM
2728
O
HOH
W
107
21.223
−0.443
4.807
1.00
20.51


ATOM
2729
O
HOH
W
108
12.939
13.840
12.680
1.00
26.10


ATOM
2730
O
HOH
W
109
10.191
−9.652
24.549
1.00
17.97


ATOM
2731
O
HOH
W
110
9.527
−19.990
11.160
1.00
34.52


ATOM
2732
O
HOH
W
111
2.300
−4.117
6.982
1.00
21.40


ATOM
2733
O
HOH
W
112
31.807
5.599
25.384
1.00
19.28


ATOM
2734
O
HOH
W
113
11.858
5.625
12.858
1.00
18.80


ATOM
2735
O
HOH
W
114
2.975
3.851
3.583
1.00
28.02


ATOM
2736
O
HOH
W
115
22.328
−3.325
9.278
1.00
18.13


ATOM
2737
O
HOH
W
116
7.581
21.278
17.210
1.00
26.33


ATOM
2738
O
HOH
W
117
−8.959
18.330
19.702
1.00
25.41


ATOM
2739
O
HOH
W
118
−7.913
−3.625
46.688
1.00
16.16


ATOM
2740
O
HOH
W
119
29.369
−4.122
35.016
1.00
21.35


ATOM
2741
O
HOH
W
120
−10.313
4.301
39.676
1.00
20.84


ATOM
2742
O
HOH
W
121
36.288
−8.163
10.383
1.00
29.41


ATOM
2743
O
HOH
W
122
−5.305
0.154
7.066
1.00
32.03


ATOM
2744
O
HOH
W
123
15.892
9.345
6.948
1.00
31.98


ATOM
2745
O
HOH
W
124
−7.934
−11.981
26.594
1.00
24.88


ATOM
2746
O
HOH
W
125
−7.700
−14.762
14.417
1.00
27.16


ATOM
2747
O
HOH
W
126
7.924
19.345
32.073
1.00
27.10


ATOM
2748
O
HOH
W
127
22.963
−15.271
−0.194
1.00
34.57


ATOM
2749
O
HOH
W
128
14.018
4.418
0.344
1.00
27.94


ATOM
2750
O
HOH
W
129
13.334
16.377
17.301
1.00
27.05


ATOM
2751
O
HOH
W
130
30.641
−11.391
0.176
1.00
21.79


ATOM
2752
O
HOH
W
131
−5.143
−9.116
6.397
1.00
26.22


ATOM
2753
O
HOH
W
132
44.452
2.118
22.189
1.00
25.35


ATOM
2754
O
HOH
W
133
−0.942
−8.268
32.526
1.00
21.73


ATOM
2755
O
HOH
W
134
32.286
8.100
17.531
1.00
30.18


ATOM
2756
O
HOH
W
135
4.471
−22.268
17.254
1.00
22.18


ATOM
2757
O
HOH
W
136
20.964
−7.154
10.051
1.00
23.34


ATOM
2758
O
HOH
W
137
−6.984
26.107
22.746
1.00
26.33


ATOM
2759
O
HOH
W
138
17.856
14.348
24.807
1.00
20.33


ATOM
2760
O
HOH
W
139
10.038
−5.546
41.193
1.00
26.62


ATOM
2761
O
HOH
W
140
13.989
13.837
16.687
1.00
27.53


ATOM
2762
O
HOH
W
141
23.629
−13.084
9.502
1.00
28.21


ATOM
2763
O
HOH
W
142
31.635
7.713
14.307
1.00
30.30


ATOM
2764
O
HOH
W
143
6.811
−2.344
−0.868
1.00
24.47


ATOM
2765
O
HOH
W
144
7.278
−9.981
30.756
1.00
27.03


ATOM
2766
O
HOH
W
145
−6.981
7.089
6.281
1.00
26.94


ATOM
2767
O
HOH
W
146
−8.635
18.558
29.861
1.00
27.91


ATOM
2768
O
HOH
W
147
30.525
−1.680
34.334
1.00
24.09


ATOM
2769
O
HOH
W
148
2.251
−13.867
2.121
1.00
25.49


ATOM
2770
O
HOH
W
149
−8.063
−9.740
29.191
1.00
24.34


ATOM
2771
O
HOH
W
150
−1.333
15.279
37.020
1.00
28.81


ATOM
2772
O
HOH
W
151
18.429
15.610
21.408
1.00
22.50


ATOM
2773
O
HOH
W
152
13.471
−4.264
12.528
1.00
19.38


ATOM
2774
O
HOH
W
153
18.621
−17.600
7.222
1.00
21.52


ATOM
2775
O
HOH
W
154
19.181
−5.396
13.023
1.00
33.83


ATOM
2776
O
HOH
W
155
−3.698
−11.419
33.622
1.00
22.32


ATOM
2777
O
HOH
W
156
24.773
−7.687
26.828
1.00
25.23


ATOM
2778
O
HOH
W
157
11.338
6.981
10.450
1.00
25.98


ATOM
2779
O
HOH
W
158
7.187
4.097
9.722
1.00
25.73


ATOM
2780
O
HOH
W
159
10.571
18.276
18.940
1.00
26.56


ATOM
2781
O
HOH
W
160
29.444
8.138
18.655
1.00
25.10


ATOM
2782
O
HOH
W
161
−4.733
−16.782
12.321
1.00
23.51


ATOM
2783
O
HOH
W
162
24.194
7.218
40.602
1.00
28.88


ATOM
2784
O
HOH
W
163
13.925
−7.040
−5.961
1.00
29.58


ATOM
2785
O
HOH
W
164
−8.456
17.425
10.469
1.00
25.03


ATOM
2786
O
HOH
W
165
20.283
7.809
6.109
1.00
25.58


ATOM
2787
O
HOH
W
166
11.226
1.360
14.389
1.00
28.28


ATOM
2788
O
HOH
W
167
17.600
11.985
25.766
1.00
28.21


ATOM
2789
O
HOH
W
168
−1.369
0.364
6.150
1.00
26.61


ATOM
2790
O
HOH
W
169
1.250
6.912
6.112
1.00
22.96


ATOM
2791
O
HOH
W
170
13.982
16.820
19.827
1.00
26.70


ATOM
2792
O
HOH
W
171
8.401
6.117
8.285
1.00
29.37


ATOM
2793
O
HOH
W
172
1.561
32.980
20.315
1.00
25.71


ATOM
2794
O
HOH
W
173
8.687
−4.960
0.724
1.00
20.63


ATOM
2795
O
HOH
W
174
16.762
−8.584
32.541
1.00
22.53


ATOM
2796
O
HOH
W
175
−8.928
23.790
25.122
1.00
26.68


ATOM
2797
O
HOH
W
176
30.774
−10.692
12.781
1.00
29.33


ATOM
2798
O
HOH
W
177
−4.491
−0.583
48.435
1.00
27.59


ATOM
2799
O
HOH
W
178
−10.254
8.887
25.677
1.00
27.41


ATOM
2800
O
HOH
W
179
12.487
−14.347
0.366
1.00
29.02


ATOM
2801
O
HOH
W
180
−2.194
−3.193
5.572
1.00
37.26


ATOM
2802
O
HOH
W
181
21.240
−14.747
4.723
1.00
24.12


ATOM
2803
O
HOH
W
182
25.238
15.872
21.083
1.00
33.15


ATOM
2804
O
HOH
W
183
27.650
8.541
12.497
1.00
23.15


ATOM
2805
O
HOH
W
184
35.303
3.837
26.688
1.00
23.28


ATOM
2806
O
HOH
W
185
−3.730
14.555
34.107
1.00
23.34


ATOM
2807
O
HOH
W
186
−8.927
−4.660
10.381
1.00
28.70


ATOM
2808
O
HOH
W
187
40.695
−1.179
15.166
1.00
31.35


ATOM
2809
O
HOH
W
188
−0.356
−22.615
31.607
1.00
35.28


ATOM
2810
O
HOH
W
189
3.463
34.674
22.382
1.00
27.20


ATOM
2811
O
HOH
W
190
8.911
2.196
11.376
1.00
19.30


ATOM
2812
O
HOH
W
191
−2.598
−24.115
28.861
1.00
26.04


ATOM
2813
O
HOH
W
192
8.418
−15.510
34.179
1.00
38.02


ATOM
2814
O
HOH
W
193
15.703
−17.633
−0.060
1.00
35.88


ATOM
2815
O
HOH
W
194
32.518
0.997
3.614
1.00
34.25


ATOM
2816
O
HOH
W
195
19.062
−16.798
10.198
1.00
27.69


ATOM
2817
O
HOH
W
196
13.216
8.976
10.392
1.00
27.61


ATOM
2818
O
HOH
W
197
2.647
−0.086
12.019
1.00
23.91


ATOM
2819
O
HOH
W
198
−1.276
−7.561
35.325
1.00
25.96


ATOM
2820
O
HOH
W
199
4.267
−22.362
30.170
1.00
35.68


ATOM
2821
O
HOH
W
200
21.787
10.595
30.558
1.00
32.19


ATOM
2822
O
HOH
W
201
21.638
20.389
14.210
1.00
43.09


ATOM
2823
O
HOH
W
202
5.373
−10.297
38.927
1.00
36.29


ATOM
2824
O
HOH
W
203
29.035
−9.588
1.139
1.00
25.61


ATOM
2825
O
HOH
W
204
0.403
−17.629
11.462
1.00
25.52


ATOM
2826
O
HOH
W
205
15.896
−2.824
23.429
1.00
9.81


ATOM
2827
O
HOH
W
206
13.783
−1.283
21.923
1.00
12.03


ATOM
2828
O
HOH
W
207
16.854
−0.738
21.328
1.00
11.76


ATOM
2829
O
HOH
W
208
14.946
−0.465
19.263
1.00
10.55


ATOM
2830
O
HOH
W
209
−5.566
−9.500
29.835
1.00
34.12


ATOM
2831
O
HOH
W
210
11.435
14.251
33.693
1.00
48.96


ATOM
2832
O
HOH
W
211
3.944
31.281
18.816
1.00
43.83


ATOM
2833
O
HOH
W
212
21.511
8.201
40.401
1.00
42.14


ATOM
2834
O
HOH
W
213
44.825
1.178
19.793
1.00
52.54


ATOM
2835
O
HOH
W
214
9.397
20.244
23.958
1.00
30.91


ATOM
2836
O
HOH
W
215
18.636
−1.182
15.865
1.00
23.82


ATOM
2837
O
HOH
W
216
18.955
−2.693
17.957
1.00
28.82


ATOM
2838
O
HOH
W
217
26.248
−9.541
27.965
1.00
25.10


ATOM
2839
O
HOH
W
218
24.703
−9.867
30.146
1.00
25.52


ATOM
2840
O
HOH
W
219
22.600
−9.260
25.832
1.00
26.71


ATOM
2841
O
HOH
W
220
1.825
10.054
39.457
1.00
25.12


ATOM
2842
O
HOH
W
221
3.585
4.590
45.058
1.00
28.59


ATOM
2843
O
HOH
W
222
3.777
−6.424
30.447
1.00
24.42


TER
2844

HOH
W
222


ATOM
2845
ZN
ZN
B
864
13.210
0.069
20.406
1.00
15.15


ATOM
2846
MG
MG
B
865
15.487
−0.725
23.006
1.00
8.84


TER
2847

MG
B
865


END
















TABLE 5










Atomic coordinates for PDE5* complex with UK-088, 800


Atom Number, Atom Type, Residue Type, Residue Number Cartesian Coordinates


X, Y, Z, Atom Occupancy (O), Temperature Factor (B) and Atom Type













X
Y
Z
O
B





















ATOM
1
CB
GLU
A
536
9.887
25.182
24.787
1.00
33.98


ATOM
2
CG
GLU
A
536
11.305
25.697
24.635
1.00
42.32


ATOM
3
CD
GLU
A
536
11.492
27.074
25.245
1.00
47.12


ATOM
4
OE1
GLU
A
536
11.290
27.223
26.470
1.00
54.45


ATOM
5
OE2
GLU
A
536
11.842
28.012
24.499
1.00
51.15


ATOM
6
C
GLU
A
536
7.942
25.044
26.327
1.00
37.22


ATOM
7
O
GLU
A
536
7.222
24.272
25.690
1.00
36.76


ATOM
8
N
GLU
A
536
9.991
23.667
26.752
1.00
36.93


ATOM
9
CA
GLU
A
536
9.456
24.961
26.239
1.00
37.47


ATOM
10
N
THR
A
537
7.463
25.990
27.125
1.00
37.34


ATOM
11
CA
THR
A
537
6.035
26.189
27.289
1.00
36.78


ATOM
12
CB
THR
A
537
5.750
27.235
28.387
1.00
43.61


ATOM
13
OG1
THR
A
537
6.425
28.457
28.069
1.00
45.23


ATOM
14
CG2
THR
A
537
6.241
26.731
29.739
1.00
34.90


ATOM
15
C
THR
A
537
5.452
26.660
25.957
1.00
35.15


ATOM
16
O
THR
A
537
4.239
26.661
25.764
1.00
34.30


ATOM
17
N
ARG
A
538
6.336
27.046
25.040
1.00
32.72


ATOM
18
CA
ARG
A
538
5.943
27.514
23.712
1.00
31.35


ATOM
19
CB
ARG
A
538
7.143
28.133
23.002
1.00
33.78


ATOM
20
CG
ARG
A
538
6.910
28.452
21.531
1.00
42.77


ATOM
21
CD
ARG
A
538
6.041
29.690
21.340
1.00
51.85


ATOM
22
NE
ARG
A
538
4.638
29.475
21.687
1.00
50.21


ATOM
23
CZ
ARG
A
538
3.715
30.433
21.672
1.00
49.57


ATOM
24
NH1
ARG
A
538
4.047
31.673
21.330
1.00
48.08


ATOM
25
NH2
ARG
A
538
2.458
30.154
21.992
1.00
49.14


ATOM
26
C
ARG
A
538
5.405
26.369
22.861
1.00
30.33


ATOM
27
O
ARG
A
538
4.381
26.501
22.187
1.00
28.72


ATOM
28
N
GLU
A
539
6.120
25.250
22.876
1.00
28.94


ATOM
29
CA
GLU
A
539
5.709
24.080
22.115
1.00
25.47


ATOM
30
CB
GLU
A
539
6.807
23.024
22.141
1.00
30.35


ATOM
31
CG
GLU
A
539
8.055
23.426
21.391
1.00
31.75


ATOM
32
CD
GLU
A
539
9.188
22.463
21.628
1.00
31.48


ATOM
33
OE1
GLU
A
539
9.689
22.410
22.771
1.00
46.55


ATOM
34
OE2
GLU
A
539
9.575
21.754
20.676
1.00
57.06


ATOM
35
C
GLU
A
539
4.437
23.511
22.718
1.00
23.49


ATOM
36
O
GLU
A
539
3.599
22.952
22.011
1.00
21.01


ATOM
37
N
LEU
A
540
4.299
23.653
24.032
1.00
22.37


ATOM
38
CA
LEU
A
540
3.114
23.159
24.713
1.00
22.10


ATOM
39
CB
LEU
A
540
3.302
23.223
26.231
1.00
19.44


ATOM
40
CG
LEU
A
540
2.098
22.763
27.059
1.00
22.04


ATOM
41
CD1
LEU
A
540
1.686
21.365
26.627
1.00
19.81


ATOM
42
CD2
LEU
A
540
2.441
22.783
28.539
1.00
38.12


ATOM
43
C
LEU
A
540
1.907
23.995
24.300
1.00
21.23


ATOM
44
O
LEU
A
540
0.844
23.461
23.990
1.00
19.37


ATOM
45
N
GLN
A
541
2.074
25.313
24.283
1.00
20.36


ATOM
46
CA
GLN
A
541
0.972
26.185
23.905
1.00
18.42


ATOM
47
CB
GLN
A
541
1.410
27.651
23.966
1.00
20.67


ATOM
48
CG
GLN
A
541
1.873
28.081
25.350
1.00
24.12


ATOM
49
CD
GLN
A
541
2.356
29.519
25.401
1.00
24.37


ATOM
50
OE1
GLN
A
541
3.047
29.986
24.497
1.00
17.86


ATOM
51
NE2
GLN
A
541
2.008
30.223
26.474
1.00
20.12


ATOM
52
C
GLN
A
541
0.477
25.833
22.505
1.00
17.74


ATOM
53
O
GLN
A
541
−0.726
25.799
22.254
1.00
19.08


ATOM
54
N
SER
A
542
1.404
25.552
21.596
1.00
15.82


ATOM
55
CA
SER
A
542
1.026
25.207
20.231
1.00
18.42


ATOM
56
CB
SER
A
542
2.263
25.179
19.329
1.00
20.91


ATOM
57
OG
SER
A
542
2.857
26.463
19.251
1.00
37.22


ATOM
58
C
SER
A
542
0.320
23.858
20.174
1.00
16.82


ATOM
59
O
SER
A
542
−0.710
23.709
19.520
1.00
17.71


ATOM
60
N
LEU
A
543
0.875
22.874
20.872
1.00
17.64


ATOM
61
CA
LEU
A
543
0.297
21.538
20.878
1.00
17.88


ATOM
62
CB
LEU
A
543
1.269
20.550
21.531
1.00
13.54


ATOM
63
CG
LEU
A
543
0.762
19.113
21.695
1.00
17.02


ATOM
64
CD1
LEU
A
543
0.501
18.504
20.329
1.00
14.15


ATOM
65
CD2
LEU
A
543
1.789
18.284
22.465
1.00
10.59


ATOM
66
C
LEU
A
543
−1.049
21.468
21.592
1.00
18.33


ATOM
67
O
LEU
A
543
−2.013
20.914
21.064
1.00
19.18


ATOM
68
N
ALA
A
544
−1.112
22.038
22.790
1.00
18.60


ATOM
69
CA
ALA
A
544
−2.332
22.003
23.588
1.00
19.09


ATOM
70
CB
ALA
A
544
−2.053
22.573
24.972
1.00
17.83


ATOM
71
C
ALA
A
544
−3.527
22.717
22.967
1.00
21.56


ATOM
72
O
ALA
A
544
−4.667
22.306
23.165
1.00
23.51


ATOM
73
N
ALA
A
545
−3.269
23.782
22.217
1.00
23.98


ATOM
74
CA
ALA
A
545
−4.348
24.547
21.599
1.00
24.34


ATOM
75
CB
ALA
A
545
−3.861
25.952
21.274
1.00
26.53


ATOM
76
C
ALA
A
545
−4.901
23.891
20.341
1.00
25.76


ATOM
77
O
ALA
A
545
−6.065
24.079
19.992
1.00
28.16


ATOM
78
N
ALA
A
546
−4.059
23.115
19.668
1.00
24.74


ATOM
79
CA
ALA
A
546
−4.441
22.443
18.430
1.00
24.22


ATOM
80
CB
ALA
A
546
−3.239
21.701
17.861
1.00
22.00


ATOM
81
C
ALA
A
546
−5.621
21.485
18.529
1.00
21.89


ATOM
82
O
ALA
A
546
−5.803
20.791
19.529
1.00
23.27


ATOM
83
N
VAL
A
547
−6.433
21.464
17.478
1.00
21.72


ATOM
84
CA
VAL
A
547
−7.560
20.548
17.418
1.00
21.65


ATOM
85
CB
VAL
A
547
−8.660
21.045
16.454
1.00
23.33


ATOM
86
CG1
VAL
A
547
−9.754
19.993
16.326
1.00
25.11


ATOM
87
CG2
VAL
A
547
−9.250
22.355
16.965
1.00
23.58


ATOM
88
C
VAL
A
547
−6.925
19.284
16.850
1.00
22.28


ATOM
89
O
VAL
A
547
−6.280
19.329
15.805
1.00
24.96


ATOM
90
N
VAL
A
548
−7.090
18.165
17.542
1.00
21.82


ATOM
91
CA
VAL
A
548
−6.498
16.909
17.098
1.00
19.25


ATOM
92
CB
VAL
A
548
−6.387
15.925
18.278
1.00
19.56


ATOM
93
CG1
VAL
A
548
−5.669
14.659
17.840
1.00
23.78


ATOM
94
CG2
VAL
A
548
−5.656
16.593
19.438
1.00
24.95


ATOM
95
C
VAL
A
548
−7.284
16.241
15.975
1.00
17.26


ATOM
96
O
VAL
A
548
−8.453
15.904
16.146
1.00
19.24


ATOM
97
N
PRO
A
549
−6.646
16.038
14.808
1.00
17.33


ATOM
98
CD
PRO
A
549
−5.293
16.478
14.431
1.00
18.64


ATOM
99
CA
PRO
A
549
−7.315
15.401
13.670
1.00
19.43


ATOM
100
CB
PRO
A
549
−6.245
15.425
12.575
1.00
17.30


ATOM
101
CG
PRO
A
549
−5.420
16.615
12.931
1.00
23.24


ATOM
102
C
PRO
A
549
−7.742
13.982
14.023
1.00
20.23


ATOM
103
O
PRO
A
549
−7.259
13.402
15.001
1.00
16.82


ATOM
104
N
SER
A
550
−8.645
13.431
13.220
1.00
17.57


ATOM
105
CA
SER
A
550
−9.153
12.081
13.432
1.00
20.68


ATOM
106
CB
SER
A
550
−10.343
11.822
12.512
1.00
17.19


ATOM
107
OG
SER
A
550
−9.934
11.861
11.153
1.00
18.60


ATOM
108
C
SER
A
550
−8.075
11.055
13.127
1.00
17.34


ATOM
109
O
SER
A
550
−7.096
11.357
12.443
1.00
16.71


ATOM
110
N
ALA
A
551
−8.257
9.841
13.637
1.00
18.46


ATOM
111
CA
ALA
A
551
−7.304
8.769
13.380
1.00
19.34


ATOM
112
CB
ALA
A
551
−7.706
7.507
14.143
1.00
17.06


ATOM
113
C
ALA
A
551
−7.322
8.502
11.879
1.00
18.62


ATOM
114
O
ALA
A
551
−6.284
8.262
11.261
1.00
20.73


ATOM
115
N
GLN
A
552
−8.518
8.554
11.300
1.00
19.78


ATOM
116
CA
GLN
A
552
−8.700
8.327
9.869
1.00
21.36


ATOM
117
CB
GLN
A
552
−10.175
8.528
9.502
1.00
23.40


ATOM
118
CG
GLN
A
552
−10.541
8.181
8.067
1.00
31.79


ATOM
119
CD
GLN
A
552
−12.026
8.358
7.797
1.00
35.80


ATOM
120
OE1
GLN
A
552
−12.864
7.675
8.390
1.00
46.36


ATOM
121
NE2
GLN
A
552
−12.358
9.283
6.902
1.00
49.03


ATOM
122
C
GLN
A
552
−7.820
9.301
9.086
1.00
21.35


ATOM
123
O
GLN
A
552
−7.040
8.897
8.219
1.00
21.48


ATOM
124
N
THR
A
553
−7.938
10.584
9.408
1.00
19.75


ATOM
125
CA
THR
A
553
−7.151
11.612
8.739
1.00
19.52


ATOM
126
CB
THR
A
553
−7.501
13.017
9.268
1.00
18.18


ATOM
127
OG1
THR
A
553
−8.871
13.318
8.971
1.00
19.96


ATOM
128
CG2
THR
A
553
−6.597
14.066
8.627
1.00
18.92


ATOM
129
C
THR
A
553
−5.654
11.396
8.926
1.00
20.00


ATOM
130
O
THR
A
553
−4.875
11.523
7.980
1.00
19.53


ATOM
131
N
LEU
A
554
−5.260
11.062
10.150
1.00
19.10


ATOM
132
CA
LEU
A
554
−3.855
10.853
10.474
1.00
20.03


ATOM
133
CB
LEU
A
554
−3.650
10.974
11.987
1.00
17.91


ATOM
134
CG
LEU
A
554
−4.091
12.323
12.571
1.00
18.40


ATOM
135
CD1
LEU
A
554
−3.972
12.316
14.082
1.00
16.11


ATOM
136
CD2
LEU
A
554
−3.237
13.436
11.977
1.00
23.68


ATOM
137
C
LEU
A
554
−3.303
9.521
9.970
1.00
19.88


ATOM
138
O
LEU
A
554
−2.093
9.304
9.994
1.00
19.74


ATOM
139
N
LYS
A
555
−4.198
8.637
9.533
1.00
17.37


ATOM
140
CA
LYS
A
555
−3.833
7.327
8.997
1.00
19.69


ATOM
141
CB
LYS
A
555
−3.032
7.523
7.708
1.00
26.45


ATOM
142
CG
LYS
A
555
−3.740
8.429
6.708
1.00
33.54


ATOM
143
CD
LYS
A
555
−2.829
8.837
5.565
1.00
36.95


ATOM
144
CE
LYS
A
555
−3.542
9.803
4.633
1.00
36.53


ATOM
145
NZ
LYS
A
555
−2.645
10.308
3.562
1.00
43.43


ATOM
146
C
LYS
A
555
−3.043
6.454
9.976
1.00
19.45


ATOM
147
O
LYS
A
555
−2.294
5.569
9.565
1.00
18.29


ATOM
148
N
ILE
A
556
−3.227
6.688
11.271
1.00
17.06


ATOM
149
CA
ILE
A
556
−2.501
5.917
12.273
1.00
16.83


ATOM
150
CB
ILE
A
556
−2.475
6.638
13.641
1.00
13.95


ATOM
151
CG2
ILE
A
556
−1.565
7.856
13.569
1.00
16.87


ATOM
152
CG1
ILE
A
556
−3.897
7.017
14.062
1.00
14.93


ATOM
153
CD1
ILE
A
556
−3.981
7.598
15.460
1.00
19.73


ATOM
154
C
ILE
A
556
−3.019
4.496
12.489
1.00
14.60


ATOM
155
O
ILE
A
556
−2.443
3.745
13.271
1.00
12.74


ATOM
156
N
THR
A
557
−4.099
4.125
11.806
1.00
14.27


ATOM
157
CA
THR
A
557
−4.653
2.776
11.938
1.00
15.05


ATOM
158
CB
THR
A
557
−6.187
2.772
11.699
1.00
21.22


ATOM
159
OG1
THR
A
557
−6.813
3.726
12.567
1.00
20.77


ATOM
160
CG2
THR
A
557
−6.773
1.398
11.982
1.00
21.26


ATOM
161
C
THR
A
557
−3.991
1.855
10.907
1.00
14.39


ATOM
162
O
THR
A
557
−4.131
0.631
10.955
1.00
16.89


ATOM
163
N
ASP
A
558
−3.257
2.456
9.979
1.00
14.56


ATOM
164
CA
ASP
A
558
−2.593
1.702
8.923
1.00
14.77


ATOM
165
CB
ASP
A
558
−2.374
2.613
7.713
1.00
20.77


ATOM
166
CG
ASP
A
558
−3.648
3.312
7.274
1.00
30.09


ATOM
167
OD1
ASP
A
558
−4.657
2.616
7.031
1.00
38.75


ATOM
168
OD2
ASP
A
558
−3.642
4.555
7.173
1.00
46.69


ATOM
169
C
ASP
A
558
−1.258
1.086
9.351
1.00
14.68


ATOM
170
O
ASP
A
558
−0.365
1.787
9.829
1.00
13.87


ATOM
171
N
PHE
A
559
−1.124
−0.227
9.175
1.00
13.82


ATOM
172
CA
PHE
A
559
0.119
−0.916
9.526
1.00
13.07


ATOM
173
CB
PHE
A
559
0.000
−2.427
9.283
1.00
14.41


ATOM
174
CG
PHE
A
559
−0.732
−3.175
10.366
1.00
18.21


ATOM
175
CD1
PHE
A
559
−0.289
−3.134
11.680
1.00
14.30


ATOM
176
CD2
PHE
A
559
−1.836
−3.960
10.060
1.00
16.61


ATOM
177
CE1
PHE
A
559
−0.931
−3.866
12.668
1.00
15.41


ATOM
178
CE2
PHE
A
559
−2.482
−4.692
11.043
1.00
15.41


ATOM
179
CZ
PHE
A
559
−2.031
−4.647
12.344
1.00
12.10


ATOM
180
C
PHE
A
559
1.277
−0.386
8.680
1.00
11.71


ATOM
181
O
PHE
A
559
2.431
−0.411
9.109
1.00
12.25


ATOM
182
N
SER
A
560
0.965
0.079
7.473
1.00
13.82


ATOM
183
CA
SER
A
560
1.979
0.597
6.555
1.00
13.86


ATOM
184
CB
SER
A
560
1.538
0.384
5.106
1.00
19.52


ATOM
185
OG
SER
A
560
1.411
−0.996
4.816
1.00
19.35


ATOM
186
C
SER
A
560
2.294
2.071
6.770
1.00
12.88


ATOM
187
O
SER
A
560
2.959
2.698
5.945
1.00
14.29


ATOM
188
N
PHE
A
561
1.815
2.608
7.886
1.00
12.82


ATOM
189
CA
PHE
A
561
2.021
4.009
8.261
1.00
13.63


ATOM
190
CB
PHE
A
561
1.567
4.207
9.713
1.00
14.59


ATOM
191
CG
PHE
A
561
1.835
5.583
10.258
1.00
12.08


ATOM
192
CD1
PHE
A
561
0.956
6.625
10.014
1.00
17.74


ATOM
193
CD2
PHE
A
561
2.967
5.829
11.022
1.00
10.31


ATOM
194
CE1
PHE
A
561
1.199
7.891
10.524
1.00
21.75


ATOM
195
CE2
PHE
A
561
3.220
7.093
11.537
1.00
13.27


ATOM
196
CZ
PHE
A
561
2.333
8.126
11.287
1.00
18.85


ATOM
197
C
PHE
A
561
3.466
4.498
8.125
1.00
14.38


ATOM
198
O
PHE
A
561
4.413
3.791
8.485
1.00
11.10


ATOM
199
N
SER
A
562
3.625
5.716
7.607
1.00
14.38


ATOM
200
CA
SER
A
562
4.939
6.334
7.453
1.00
13.72


ATOM
201
CB
SER
A
562
5.283
6.520
5.972
1.00
15.96


ATOM
202
OG
SER
A
562
6.542
7.159
5.835
1.00
23.25


ATOM
203
C
SER
A
562
4.940
7.695
8.159
1.00
12.53


ATOM
204
O
SER
A
562
4.009
8.490
8.014
1.00
12.55


ATOM
205
N
ASP
A
563
5.992
7.965
8.922
1.00
13.45


ATOM
206
CA
ASP
A
563
6.094
9.223
9.661
1.00
15.79


ATOM
207
CB
ASP
A
563
6.662
8.953
11.050
1.00
13.73


ATOM
208
CG
ASP
A
563
8.166
8.765
11.022
1.00
15.49


ATOM
209
OD1
ASP
A
563
8.895
9.680
11.465
1.00
18.81


ATOM
210
OD2
ASP
A
563
8.625
7.712
10.537
1.00
16.12


ATOM
211
C
ASP
A
563
7.009
10.232
8.974
1.00
16.63


ATOM
212
O
ASP
A
563
7.112
11.383
9.404
1.00
17.82


ATOM
213
N
PHE
A
564
7.673
9.796
7.911
1.00
16.51


ATOM
214
CA
PHE
A
564
8.633
10.635
7.205
1.00
18.23


ATOM
215
CB
PHE
A
564
9.207
9.871
6.011
1.00
15.87


ATOM
216
CG
PHE
A
564
10.446
10.494
5.438
1.00
26.61


ATOM
217
CD1
PHE
A
564
11.599
10.592
6.201
1.00
20.64


ATOM
218
CD2
PHE
A
564
10.458
10.991
4.144
1.00
27.32


ATOM
219
CE1
PHE
A
564
12.742
11.174
5.685
1.00
30.38


ATOM
220
CE2
PHE
A
564
11.599
11.574
3.622
1.00
33.45


ATOM
221
CZ
PHE
A
564
12.742
11.665
4.394
1.00
33.80


ATOM
222
C
PHE
A
564
8.157
12.010
6.740
1.00
18.52


ATOM
223
O
PHE
A
564
8.942
12.959
6.728
1.00
19.54


ATOM
224
N
GLU
A
565
6.885
12.122
6.369
1.00
16.14


ATOM
225
CA
GLU
A
565
6.340
13.391
5.890
1.00
19.03


ATOM
226
CB
GLU
A
565
5.277
13.142
4.813
1.00
18.54


ATOM
227
CG
GLU
A
565
5.708
12.238
3.668
1.00
33.46


ATOM
228
CD
GLU
A
565
6.004
10.818
4.117
1.00
40.92


ATOM
229
OE1
GLU
A
565
5.205
10.258
4.899
1.00
41.02


ATOM
230
OE2
GLU
A
565
7.032
10.259
3.680
1.00
50.71


ATOM
231
C
GLU
A
565
5.710
14.229
7.002
1.00
19.43


ATOM
232
O
GLU
A
565
5.158
15.301
6.740
1.00
20.33


ATOM
233
N
LEU
A
566
5.786
13.746
8.238
1.00
13.91


ATOM
234
CA
LEU
A
566
5.193
14.463
9.362
1.00
15.26


ATOM
235
CB
LEU
A
566
4.515
13.482
10.321
1.00
15.63


ATOM
236
CG
LEU
A
566
3.329
12.669
9.799
1.00
24.63


ATOM
237
CD1
LEU
A
566
2.864
11.698
10.881
1.00
23.72


ATOM
238
CD2
LEU
A
566
2.199
13.607
9.399
1.00
33.15


ATOM
239
C
LEU
A
566
6.187
15.306
10.147
1.00
14.43


ATOM
240
O
LEU
A
566
7.358
14.960
10.265
1.00
17.81


ATOM
241
N
SER
A
567
5.699
16.419
10.685
1.00
14.78


ATOM
242
CA
SER
A
567
6.517
17.317
11.486
1.00
14.98


ATOM
243
CB
SER
A
567
5.928
18.727
11.467
1.00
21.89


ATOM
244
OG
SER
A
567
4.679
18.752
12.144
1.00
17.63


ATOM
245
C
SER
A
567
6.492
16.797
12.922
1.00
13.89


ATOM
246
O
SER
A
567
5.654
15.963
13.268
1.00
13.82


ATOM
247
N
ASP
A
568
7.403
17.289
13.753
1.00
15.43


ATOM
248
CA
ASP
A
568
7.428
16.869
15.149
1.00
15.57


ATOM
249
CB
ASP
A
568
8.536
17.603
15.904
1.00
19.60


ATOM
250
CG
ASP
A
568
9.888
16.947
15.727
1.00
16.75


ATOM
251
OD1
ASP
A
568
9.989
16.021
14.899
1.00
19.05


ATOM
252
OD2
ASP
A
568
10.848
17.355
16.415
1.00
23.47


ATOM
253
C
ASP
A
568
6.076
17.145
15.805
1.00
16.52


ATOM
254
O
ASP
A
568
5.559
16.313
16.556
1.00
15.97


ATOM
255
N
LEU
A
569
5.505
18.311
15.516
1.00
15.09


ATOM
256
CA
LEU
A
569
4.213
18.683
16.076
1.00
15.08


ATOM
257
CB
LEU
A
569
3.815
20.093
15.620
1.00
16.05


ATOM
258
CG
LEU
A
569
2.385
20.516
15.974
1.00
23.47


ATOM
259
CD1
LEU
A
569
2.203
20.527
17.489
1.00
21.65


ATOM
260
CD2
LEU
A
569
2.103
21.896
15.398
1.00
27.54


ATOM
261
C
LEU
A
569
3.136
17.694
15.647
1.00
12.90


ATOM
262
O
LEU
A
569
2.279
17.308
16.441
1.00
16.26


ATOM
263
N
GLU
A
570
3.184
17.281
14.386
1.00
13.40


ATOM
264
CA
GLU
A
570
2.202
16.340
13.869
1.00
14.08


ATOM
265
CB
GLU
A
570
2.354
16.196
12.352
1.00
14.43


ATOM
266
CG
GLU
A
570
1.885
17.432
11.579
1.00
20.85


ATOM
267
CD
GLU
A
570
2.062
17.291
10.081
1.00
23.63


ATOM
268
OE1
GLU
A
570
3.218
17.158
9.632
1.00
21.68


ATOM
269
OE2
GLU
A
570
1.047
17.311
9.352
1.00
28.09


ATOM
270
C
GLU
A
570
2.309
14.978
14.547
1.00
14.43


ATOM
271
O
GLU
A
570
1.293
14.319
14.780
1.00
15.20


ATOM
272
N
THR
A
571
3.529
14.551
14.866
1.00
12.67


ATOM
273
CA
THR
A
571
3.694
13.259
15.538
1.00
12.83


ATOM
274
CB
THR
A
571
5.182
12.816
15.638
1.00
13.30


ATOM
275
OG1
THR
A
571
5.915
13.737
16.452
1.00
12.68


ATOM
276
CG2
THR
A
571
5.817
12.738
14.250
1.00
12.38


ATOM
277
C
THR
A
571
3.110
13.360
16.945
1.00
11.29


ATOM
278
O
THR
A
571
2.589
12.381
17.483
1.00
12.14


ATOM
279
N
ALA
A
572
3.202
14.548
17.538
1.00
12.42


ATOM
280
CA
ALA
A
572
2.659
14.780
18.869
1.00
11.84


ATOM
281
CB
ALA
A
572
3.090
16.142
19.388
1.00
12.18


ATOM
282
C
ALA
A
572
1.136
14.701
18.803
1.00
13.34


ATOM
283
O
ALA
A
572
0.500
14.128
19.683
1.00
11.72


ATOM
284
N
LEU
A
573
0.554
15.283
17.758
1.00
12.67


ATOM
285
CA
LEU
A
573
−0.894
15.244
17.583
1.00
13.98


ATOM
286
CB
LEU
A
573
−1.307
16.104
16.384
1.00
14.33


ATOM
287
CG
LEU
A
573
−1.135
17.619
16.544
1.00
14.55


ATOM
288
CD1
LEU
A
573
−1.445
18.310
15.224
1.00
21.57


ATOM
289
CD2
LEU
A
573
−2.061
18.125
17.647
1.00
20.27


ATOM
290
C
LEU
A
573
−1.338
13.795
17.366
1.00
15.26


ATOM
291
O
LEU
A
573
−2.394
13.378
17.853
1.00
15.01


ATOM
292
N
CYS
A
574
−0.534
13.030
16.632
1.00
13.44


ATOM
293
CA
CYS
A
574
−0.852
11.625
16.385
1.00
13.06


ATOM
294
CB
CYS
A
574
0.187
10.974
15.470
1.00
12.27


ATOM
295
SG
CYS
A
574
0.049
11.382
13.714
1.00
15.24


ATOM
296
C
CYS
A
574
−0.873
10.864
17.703
1.00
12.15


ATOM
297
O
CYS
A
574
−1.710
9.991
17.919
1.00
13.51


ATOM
298
N
THR
A
575
0.066
11.194
18.581
1.00
11.60


ATOM
299
CA
THR
A
575
0.158
10.532
19.872
1.00
12.28


ATOM
300
CB
THR
A
575
1.453
10.949
20.592
1.00
10.90


ATOM
301
OG1
THR
A
575
2.575
10.576
19.777
1.00
13.47


ATOM
302
CG2
THR
A
575
1.565
10.264
21.944
1.00
10.06


ATOM
303
C
THR
A
575
−1.068
10.841
20.726
1.00
11.74


ATOM
304
O
THR
A
575
−1.613
9.952
21.379
1.00
10.78


ATOM
305
N
ILE
A
576
−1.514
12.095
20.717
1.00
12.29


ATOM
306
CA
ILE
A
576
−2.700
12.453
21.484
1.00
11.92


ATOM
307
CB
ILE
A
576
−3.046
13.945
21.354
1.00
11.38


ATOM
308
CG2
ILE
A
576
−4.371
14.222
22.053
1.00
12.83


ATOM
309
CG1
ILE
A
576
−1.933
14.802
21.965
1.00
17.73


ATOM
310
CD1
ILE
A
576
−2.154
16.292
21.798
1.00
13.34


ATOM
311
C
ILE
A
576
−3.880
11.636
20.960
1.00
12.34


ATOM
312
O
ILE
A
576
−4.674
11.103
21.737
1.00
13.64


ATOM
313
N
ARG
A
577
−3.985
11.532
19.638
1.00
13.14


ATOM
314
CA
ARG
A
577
−5.071
10.772
19.032
1.00
13.22


ATOM
315
CB
ARG
A
577
−5.029
10.888
17.503
1.00
12.21


ATOM
316
CG
ARG
A
577
−6.113
10.084
16.795
1.00
12.42


ATOM
317
CD
ARG
A
577
−7.492
10.383
17.365
1.00
10.79


ATOM
318
NE
ARG
A
577
−7.912
11.757
17.111
1.00
18.46


ATOM
319
CZ
ARG
A
577
−9.015
12.304
17.612
1.00
16.47


ATOM
320
NH1
ARG
A
577
−9.319
13.564
17.325
1.00
24.31


ATOM
321
NH2
ARG
A
577
−9.809
11.596
18.405
1.00
18.21


ATOM
322
C
ARG
A
577
−5.029
9.304
19.455
1.00
12.45


ATOM
323
O
ARG
A
577
−6.069
8.675
19.625
1.00
11.98


ATOM
324
N
MET
A
578
−3.831
8.756
19.630
1.00
10.43


ATOM
325
CA
MET
A
578
−3.716
7.367
20.058
1.00
11.28


ATOM
326
CB
MET
A
578
−2.245
6.934
20.090
1.00
11.91


ATOM
327
CG
MET
A
578
−1.605
6.808
18.716
1.00
12.93


ATOM
328
SD
MET
A
578
0.134
6.324
18.830
1.00
16.07


ATOM
329
CE
MET
A
578
0.781
7.021
17.300
1.00
19.76


ATOM
330
C
MET
A
578
−4.332
7.191
21.445
1.00
12.18


ATOM
331
O
MET
A
578
−5.103
6.260
21.675
1.00
11.26


ATOM
332
N
PHE
A
579
−3.982
8.080
22.372
1.00
11.60


ATOM
333
CA
PHE
A
579
−4.521
8.004
23.725
1.00
11.60


ATOM
334
CB
PHE
A
579
−3.921
9.097
24.619
1.00
12.17


ATOM
335
CG
PHE
A
579
−2.584
8.748
25.201
1.00
9.68


ATOM
336
CD1
PHE
A
579
−1.415
9.023
24.510
1.00
13.42


ATOM
337
CD2
PHE
A
579
−2.497
8.148
26.450
1.00
12.49


ATOM
338
CE1
PHE
A
579
−0.178
8.709
25.054
1.00
10.87


ATOM
339
CE2
PHE
A
579
−1.264
7.829
27.000
1.00
13.01


ATOM
340
CZ
PHE
A
579
−0.103
8.113
26.301
1.00
12.83


ATOM
341
C
PHE
A
579
−6.040
8.170
23.708
1.00
12.84


ATOM
342
O
PHE
A
579
−6.765
7.429
24.367
1.00
12.73


ATOM
343
N
THR
A
580
−6.504
9.151
22.943
1.00
15.04


ATOM
344
CA
THR
A
580
−7.926
9.459
22.839
1.00
14.30


ATOM
345
CB
THR
A
580
−8.145
10.702
21.967
1.00
10.78


ATOM
346
OG1
THR
A
580
−7.344
11.780
22.469
1.00
18.08


ATOM
347
CG2
THR
A
580
−9.610
11.115
21.987
1.00
13.16


ATOM
348
C
THR
A
580
−8.772
8.327
22.273
1.00
14.34


ATOM
349
O
THR
A
580
−9.774
7.936
22.871
1.00
14.67


ATOM
350
N
ASP
A
581
−8.367
7.806
21.119
1.00
15.75


ATOM
351
CA
ASP
A
581
−9.106
6.731
20.466
1.00
14.61


ATOM
352
CB
ASP
A
581
−8.724
6.668
18.990
1.00
16.27


ATOM
353
CG
ASP
A
581
−9.398
7.757
18.181
1.00
20.38


ATOM
354
OD1
ASP
A
581
−9.762
8.797
18.776
1.00
15.70


ATOM
355
OD2
ASP
A
581
−9.560
7.580
16.958
1.00
17.57


ATOM
356
C
ASP
A
581
−8.970
5.365
21.123
1.00
15.19


ATOM
357
O
ASP
A
581
−9.627
4.402
20.719
1.00
14.62


ATOM
358
N
LEU
A
582
−8.110
5.275
22.130
1.00
13.55


ATOM
359
CA
LEU
A
582
−7.957
4.032
22.867
1.00
14.36


ATOM
360
CB
LEU
A
582
−6.484
3.739
23.156
1.00
16.24


ATOM
361
CG
LEU
A
582
−5.770
3.024
22.006
1.00
14.56


ATOM
362
CD1
LEU
A
582
−4.272
2.968
22.250
1.00
12.82


ATOM
363
CD2
LEU
A
582
−6.351
1.625
21.865
1.00
12.05


ATOM
364
C
LEU
A
582
−8.739
4.189
24.168
1.00
17.31


ATOM
365
O
LEU
A
582
−8.617
3.378
25.081
1.00
17.82


ATOM
366
N
ASN
A
583
−9.533
5.255
24.246
1.00
17.93


ATOM
367
CA
ASN
A
583
−10.361
5.500
25.420
1.00
21.01


ATOM
368
CB
ASN
A
583
−11.405
4.377
25.525
1.00
22.07


ATOM
369
CG
ASN
A
583
−12.368
4.564
26.682
1.00
34.95


ATOM
370
OD1
ASN
A
583
−12.921
5.645
26.879
1.00
34.93


ATOM
371
ND2
ASN
A
583
−12.589
3.496
27.444
1.00
39.94


ATOM
372
C
ASN
A
583
−9.516
5.575
26.693
1.00
23.16


ATOM
373
O
ASN
A
583
−9.866
4.978
27.713
1.00
27.41


ATOM
374
N
LEU
A
584
−8.406
6.313
26.634
1.00
18.24


ATOM
375
CA
LEU
A
584
−7.517
6.446
27.791
1.00
18.39


ATOM
376
CB
LEU
A
584
−6.060
6.188
27.379
1.00
13.74


ATOM
377
CG
LEU
A
584
−5.713
4.823
26.778
1.00
13.61


ATOM
378
CD1
LEU
A
584
−4.226
4.789
26.412
1.00
16.18


ATOM
379
CD2
LEU
A
584
−6.050
3.726
27.769
1.00
15.78


ATOM
380
C
LEU
A
584
−7.591
7.807
28.486
1.00
18.85


ATOM
381
O
LEU
A
584
−7.377
7.904
29.695
1.00
18.54


ATOM
382
N
VAL
A
585
−7.890
8.853
27.721
1.00
18.53


ATOM
383
CA
VAL
A
585
−7.956
10.211
28.258
1.00
20.90


ATOM
384
CB
VAL
A
585
−8.157
11.234
27.123
1.00
25.63


ATOM
385
CG1
VAL
A
585
−8.083
12.648
27.672
1.00
26.57


ATOM
386
CG2
VAL
A
585
−7.102
11.024
26.054
1.00
26.78


ATOM
387
C
VAL
A
585
−9.049
10.416
29.307
1.00
21.72


ATOM
388
O
VAL
A
585
−8.771
10.839
30.429
1.00
21.94


ATOM
389
N
GLN
A
586
−10.291
10.118
28.945
1.00
22.79


ATOM
390
CA
GLN
A
586
−11.394
10.290
29.881
1.00
25.11


ATOM
391
CB
GLN
A
586
−12.728
10.306
29.131
1.00
34.29


ATOM
392
CG
GLN
A
586
−13.719
11.317
29.678
1.00
39.65


ATOM
393
CD
GLN
A
586
−13.155
12.725
29.663
1.00
50.17


ATOM
394
OE1
GLN
A
586
−12.715
13.218
28.622
1.00
52.20


ATOM
395
NE2
GLN
A
586
−13.160
13.380
30.820
1.00
48.68


ATOM
396
C
GLN
A
586
−11.402
9.172
30.914
1.00
22.36


ATOM
397
O
GLN
A
586
−11.587
9.413
32.108
1.00
23.81


ATOM
398
N
ASN
A
587
−11.195
7.948
30.441
1.00
22.47


ATOM
399
CA
ASN
A
587
−11.181
6.769
31.298
1.00
19.07


ATOM
400
CB
ASN
A
587
−10.651
5.565
30.507
1.00
21.06


ATOM
401
CG
ASN
A
587
−10.944
4.236
31.179
1.00
29.14


ATOM
402
OD1
ASN
A
587
−11.098
4.157
32.397
1.00
21.26


ATOM
403
ND2
ASN
A
587
−11.002
3.174
30.382
1.00
33.44


ATOM
404
C
ASN
A
587
−10.319
6.981
32.542
1.00
20.86


ATOM
405
O
ASN
A
587
−10.727
6.646
33.656
1.00
19.43


ATOM
406
N
PHE
A
588
−9.134
7.553
32.357
1.00
18.57


ATOM
407
CA
PHE
A
588
−8.227
7.753
33.480
1.00
18.65


ATOM
408
CB
PHE
A
588
−6.880
7.109
33.145
1.00
13.88


ATOM
409
CG
PHE
A
588
−6.976
5.624
32.948
1.00
14.75


ATOM
410
CD1
PHE
A
588
−7.272
4.791
34.022
1.00
13.58


ATOM
411
CD2
PHE
A
588
−6.860
5.065
31.686
1.00
12.05


ATOM
412
CE1
PHE
A
588
−7.456
3.431
33.837
1.00
13.16


ATOM
413
CE2
PHE
A
588
−7.044
3.704
31.496
1.00
10.45


ATOM
414
CZ
PHE
A
588
−7.344
2.888
32.576
1.00
16.21


ATOM
415
C
PHE
A
588
−8.063
9.190
33.966
1.00
20.57


ATOM
416
O
PHE
A
588
−7.072
9.538
34.611
1.00
18.90


ATOM
417
N
GLN
A
589
−9.052
10.020
33.662
1.00
21.41


ATOM
418
CA
GLN
A
589
−9.057
11.410
34.110
1.00
23.36


ATOM
419
CB
GLN
A
589
−9.213
11.449
35.634
1.00
28.73


ATOM
420
CG
GLN
A
589
−10.311
10.551
36.194
1.00
40.43


ATOM
421
CD
GLN
A
589
−11.701
11.003
35.797
1.00
42.17


ATOM
422
OE1
GLN
A
589
−12.058
12.167
35.971
1.00
38.12


ATOM
423
NE2
GLN
A
589
−12.498
10.080
35.270
1.00
47.35


ATOM
424
C
GLN
A
589
−7.805
12.201
33.725
1.00
20.90


ATOM
425
O
GLN
A
589
−7.282
12.972
34.531
1.00
21.16


ATOM
426
N
MET
A
590
−7.321
12.019
32.502
1.00
22.12


ATOM
427
CA
MET
A
590
−6.133
12.745
32.069
1.00
21.73


ATOM
428
CB
MET
A
590
−5.463
12.035
30.893
1.00
22.93


ATOM
429
CG
MET
A
590
−4.751
10.752
31.257
1.00
24.06


ATOM
430
SD
MET
A
590
−3.865
10.087
29.838
1.00
19.72


ATOM
431
CE
MET
A
590
−3.631
8.404
30.357
1.00
17.35


ATOM
432
C
MET
A
590
−6.455
14.172
31.654
1.00
22.68


ATOM
433
O
MET
A
590
−7.295
14.398
30.784
1.00
23.69


ATOM
434
N
LYS
A
591
−5.792
15.138
32.278
1.00
20.35


ATOM
435
CA
LYS
A
591
−6.013
16.530
31.919
1.00
20.85


ATOM
436
CB
LYS
A
591
−5.554
17.460
33.045
1.00
22.95


ATOM
437
CG
LYS
A
591
−6.472
17.422
34.262
1.00
28.61


ATOM
438
CD
LYS
A
591
−6.065
18.438
35.315
1.00
37.59


ATOM
439
CE
LYS
A
591
−7.106
18.527
36.423
1.00
42.92


ATOM
440
NZ
LYS
A
591
−8.417
19.026
35.915
1.00
51.43


ATOM
441
C
LYS
A
591
−5.235
16.800
30.636
1.00
20.72


ATOM
442
O
LYS
A
591
−4.048
16.486
30.537
1.00
21.29


ATOM
443
N
HIS
A
592
−5.920
17.375
29.654
1.00
20.84


ATOM
444
CA
HIS
A
592
−5.333
17.670
28.351
1.00
21.11


ATOM
445
CB
HIS
A
592
−6.273
18.577
27.553
1.00
21.39


ATOM
446
CG
HIS
A
592
−5.884
18.737
26.125
1.00
18.05


ATOM
447
CD2
HIS
A
592
−5.427
19.798
25.424
1.00
24.75


ATOM
448
ND1
HIS
A
592
−5.926
17.685
25.213
1.00
22.74


ATOM
449
CE1
HIS
A
592
−5.518
18.102
24.044
1.00
29.20


ATOM
450
NE2
HIS
A
592
−5.204
19.393
24.135
1.00
27.94


ATOM
451
C
HIS
A
592
−3.937
18.295
28.377
1.00
20.49


ATOM
452
O
HIS
A
592
−3.034
17.848
27.661
1.00
19.49


ATOM
453
N
GLU
A
593
−3.765
19.338
29.184
1.00
19.12


ATOM
454
CA
GLU
A
593
−2.481
20.019
29.279
1.00
18.26


ATOM
455
CB
GLU
A
593
−2.592
21.243
30.192
1.00
23.02


ATOM
456
CG
GLU
A
593
−1.267
21.957
30.416
1.00
32.52


ATOM
457
CD
GLU
A
593
−1.422
23.296
31.116
1.00
44.01


ATOM
458
OE1
GLU
A
593
−2.062
24.200
30.535
1.00
41.08


ATOM
459
OE2
GLU
A
593
−0.901
23.446
32.244
1.00
45.85


ATOM
460
C
GLU
A
593
−1.381
19.099
29.793
1.00
18.42


ATOM
461
O
GLU
A
593
−0.230
19.195
29.365
1.00
16.87


ATOM
462
N
VAL
A
594
−1.738
18.209
30.710
1.00
18.22


ATOM
463
CA
VAL
A
594
−0.770
17.275
31.277
1.00
17.13


ATOM
464
CB
VAL
A
594
−1.372
16.506
32.465
1.00
16.16


ATOM
465
CG1
VAL
A
594
−0.314
15.605
33.085
1.00
20.37


ATOM
466
CG2
VAL
A
594
−1.911
17.481
33.491
1.00
22.54


ATOM
467
C
VAL
A
594
−0.299
16.263
30.235
1.00
15.25


ATOM
468
O
VAL
A
594
0.902
16.005
30.101
1.00
16.26


ATOM
469
N
LEU
A
595
−1.246
15.681
29.504
1.00
13.83


ATOM
470
CA
LEU
A
595
−0.897
14.705
28.478
1.00
14.01


ATOM
471
CB
LEU
A
595
−2.163
14.147
27.818
1.00
9.50


ATOM
472
CG
LEU
A
595
−1.969
13.167
26.653
1.00
18.45


ATOM
473
CD1
LEU
A
595
−1.068
12.014
27.076
1.00
12.38


ATOM
474
CD2
LEU
A
595
−3.318
12.643
26.201
1.00
14.12


ATOM
475
C
LEU
A
595
−0.002
15.372
27.438
1.00
13.61


ATOM
476
O
LEU
A
595
1.004
14.804
27.010
1.00
13.98


ATOM
477
N
CYS
A
596
−0.358
16.588
27.037
1.00
14.70


ATOM
478
CA
CYS
A
596
0.448
17.303
26.058
1.00
12.24


ATOM
479
CB
CYS
A
596
−0.191
18.649
25.709
1.00
15.21


ATOM
480
SG
CYS
A
596
−1.702
18.507
24.749
1.00
17.45


ATOM
481
C
CYS
A
596
1.861
17.534
26.586
1.00
12.70


ATOM
482
O
CYS
A
596
2.839
17.327
25.868
1.00
11.06


ATOM
483
N
ARG
A
597
1.970
17.959
27.841
1.00
11.36


ATOM
484
CA
ARG
A
597
3.283
18.211
28.420
1.00
11.51


ATOM
485
CB
ARG
A
597
3.141
18.836
29.815
1.00
14.74


ATOM
486
CG
ARG
A
597
4.463
19.343
30.388
1.00
15.86


ATOM
487
CD
ARG
A
597
4.294
20.067
31.727
1.00
20.22


ATOM
488
NE
ARG
A
597
3.565
21.332
31.614
1.00
21.93


ATOM
489
CZ
ARG
A
597
2.279
21.493
31.916
1.00
27.00


ATOM
490
NH1
ARG
A
597
1.560
20.469
32.357
1.00
22.77


ATOM
491
NH2
ARG
A
597
1.708
22.683
31.782
1.00
30.27


ATOM
492
C
ARG
A
597
4.100
16.919
28.494
1.00
11.80


ATOM
493
O
ARG
A
597
5.287
16.909
28.162
1.00
10.48


ATOM
494
N
TRP
A
598
3.454
15.830
28.905
1.00
11.97


ATOM
495
CA
TRP
A
598
4.112
14.530
29.022
1.00
9.62


ATOM
496
CB
TRP
A
598
3.125
13.488
29.556
1.00
11.57


ATOM
497
CG
TRP
A
598
3.717
12.110
29.702
1.00
10.65


ATOM
498
CD2
TRP
A
598
3.609
11.028
28.771
1.00
9.66


ATOM
499
CE2
TRP
A
598
4.350
9.948
29.298
1.00
8.24


ATOM
500
CE3
TRP
A
598
2.964
10.866
27.541
1.00
11.87


ATOM
501
CD1
TRP
A
598
4.494
11.656
30.728
1.00
9.74


ATOM
502
NE1
TRP
A
598
4.878
10.359
30.492
1.00
11.42


ATOM
503
CZ2
TRP
A
598
4.459
8.720
28.635
1.00
7.38


ATOM
504
CZ3
TRP
A
598
3.075
9.646
26.886
1.00
9.43


ATOM
505
CH2
TRP
A
598
3.818
8.593
27.434
1.00
10.02


ATOM
506
C
TRP
A
598
4.656
14.064
27.670
1.00
12.66


ATOM
507
O
TRP
A
598
5.804
13.617
27.568
1.00
11.33


ATOM
508
N
ILE
A
599
3.823
14.160
26.637
1.00
9.84


ATOM
509
CA
ILE
A
599
4.232
13.748
25.298
1.00
12.03


ATOM
510
CB
ILE
A
599
3.101
13.974
24.270
1.00
11.30


ATOM
511
CG2
ILE
A
599
3.648
13.807
22.856
1.00
13.41


ATOM
512
CG1
ILE
A
599
1.953
13.000
24.546
1.00
13.16


ATOM
513
CD1
ILE
A
599
0.732
13.218
23.668
1.00
13.06


ATOM
514
C
ILE
A
599
5.460
14.533
24.855
1.00
14.21


ATOM
515
O
ILE
A
599
6.414
13.969
24.308
1.00
11.47


ATOM
516
N
LEU
A
600
5.439
15.839
25.094
1.00
14.33


ATOM
517
CA
LEU
A
600
6.566
16.670
24.707
1.00
13.61


ATOM
518
CB
LEU
A
600
6.214
18.151
24.882
1.00
13.53


ATOM
519
CG
LEU
A
600
5.073
18.621
23.971
1.00
12.80


ATOM
520
CD1
LEU
A
600
4.652
20.036
24.336
1.00
15.66


ATOM
521
CD2
LEU
A
600
5.518
18.557
22.520
1.00
13.09


ATOM
522
C
LEU
A
600
7.800
16.297
25.523
1.00
10.78


ATOM
523
O
LEU
A
600
8.917
16.324
25.011
1.00
10.47


ATOM
524
N
SER
A
601
7.601
15.925
26.788
1.00
10.50


ATOM
525
CA
SER
A
601
8.734
15.540
27.624
1.00
8.54


ATOM
526
CB
SER
A
601
8.303
15.398
29.085
1.00
9.00


ATOM
527
OG
SER
A
601
8.036
16.678
29.634
1.00
9.87


ATOM
528
C
SER
A
601
9.342
14.239
27.129
1.00
9.99


ATOM
529
O
SER
A
601
10.563
14.082
27.104
1.00
10.43


ATOM
530
N
VAL
A
602
8.487
13.300
26.739
1.00
10.77


ATOM
531
CA
VAL
A
602
8.968
12.024
26.223
1.00
10.98


ATOM
532
CB
VAL
A
602
7.791
11.081
25.874
1.00
12.52


ATOM
533
CG1
VAL
A
602
8.303
9.856
25.138
1.00
9.22


ATOM
534
CG2
VAL
A
602
7.068
10.658
27.152
1.00
11.71


ATOM
535
C
VAL
A
602
9.794
12.290
24.967
1.00
12.57


ATOM
536
O
VAL
A
602
10.935
11.848
24.855
1.00
11.99


ATOM
537
N
LYS
A
603
9.220
13.043
24.034
1.00
12.97


ATOM
538
CA
LYS
A
603
9.906
13.363
22.792
1.00
11.73


ATOM
539
CB
LYS
A
603
9.025
14.268
21.928
1.00
14.00


ATOM
540
CG
LYS
A
603
9.666
14.688
20.620
1.00
14.56


ATOM
541
CD
LYS
A
603
8.656
15.317
19.686
1.00
16.82


ATOM
542
CE
LYS
A
603
8.088
16.603
20.262
1.00
24.97


ATOM
543
NZ
LYS
A
603
7.169
17.256
19.300
1.00
39.23


ATOM
544
C
LYS
A
603
11.256
14.035
23.042
1.00
11.50


ATOM
545
O
LYS
A
603
12.252
13.694
22.414
1.00
14.04


ATOM
546
N
LYS
A
604
11.279
14.985
23.968
1.00
11.12


ATOM
547
CA
LYS
A
604
12.501
15.714
24.293
1.00
13.84


ATOM
548
CB
LYS
A
604
12.181
16.849
25.274
1.00
16.59


ATOM
549
CG
LYS
A
604
13.403
17.589
25.788
1.00
18.98


ATOM
550
CD
LYS
A
604
13.016
18.673
26.784
1.00
25.53


ATOM
551
CE
LYS
A
604
14.251
19.335
27.391
1.00
31.51


ATOM
552
NZ
LYS
A
604
13.893
20.351
28.424
1.00
29.80


ATOM
553
C
LYS
A
604
13.582
14.824
24.890
1.00
12.98


ATOM
554
O
LYS
A
604
14.776
15.073
24.710
1.00
13.10


ATOM
555
N
ASN
A
605
13.173
13.773
25.587
1.00
12.62


ATOM
556
CA
ASN
A
605
14.146
12.901
26.220
1.00
13.04


ATOM
557
CB
ASN
A
605
13.555
12.336
27.507
1.00
13.13


ATOM
558
CG
ASN
A
605
13.579
13.356
28.638
1.00
32.58


ATOM
559
OD1
ASN
A
605
14.638
13.650
29.197
1.00
25.76


ATOM
560
ND2
ASN
A
605
12.418
13.918
28.962
1.00
30.95


ATOM
561
C
ASN
A
605
14.757
11.809
25.352
1.00
15.12


ATOM
562
O
ASN
A
605
15.342
10.848
25.858
1.00
18.48


ATOM
563
N
TYR
A
606
14.612
11.961
24.042
1.00
10.60


ATOM
564
CA
TYR
A
606
15.233
11.051
23.093
1.00
10.45


ATOM
565
CB
TYR
A
606
14.254
10.645
21.982
1.00
10.34


ATOM
566
CG
TYR
A
606
13.420
9.444
22.358
1.00
11.02


ATOM
567
CD1
TYR
A
606
13.950
8.156
22.297
1.00
8.31


ATOM
568
CE1
TYR
A
606
13.222
7.061
22.752
1.00
8.28


ATOM
569
CD2
TYR
A
606
12.139
9.601
22.874
1.00
12.47


ATOM
570
CE2
TYR
A
606
11.410
8.516
23.335
1.00
15.05


ATOM
571
CZ
TYR
A
606
11.955
7.252
23.275
1.00
15.46


ATOM
572
OH
TYR
A
606
11.227
6.188
23.773
1.00
12.36


ATOM
573
C
TYR
A
606
16.362
11.908
22.539
1.00
11.41


ATOM
574
O
TYR
A
606
16.216
13.129
22.428
1.00
14.91


ATOM
575
N
ARG
A
607
17.499
11.293
22.234
1.00
11.41


ATOM
576
CA
ARG
A
607
18.627
12.042
21.700
1.00
10.90


ATOM
577
CB
ARG
A
607
19.933
11.322
22.034
1.00
12.68


ATOM
578
CG
ARG
A
607
20.078
11.019
23.520
1.00
10.36


ATOM
579
CD
ARG
A
607
21.460
10.489
23.870
1.00
13.25


ATOM
580
NE
ARG
A
607
21.492
9.929
25.221
1.00
9.55


ATOM
581
CZ
ARG
A
607
22.601
9.556
25.854
1.00
18.33


ATOM
582
NH1
ARG
A
607
23.781
9.686
25.262
1.00
13.50


ATOM
583
NH2
ARG
A
607
22.530
9.045
27.077
1.00
17.68


ATOM
584
C
ARG
A
607
18.425
12.150
20.194
1.00
10.45


ATOM
585
O
ARG
A
607
18.616
11.182
19.458
1.00
12.53


ATOM
586
N
LYS
A
608
18.052
13.340
19.738
1.00
11.88


ATOM
587
CA
LYS
A
608
17.755
13.555
18.323
1.00
13.33


ATOM
588
CB
LYS
A
608
17.273
14.993
18.104
1.00
18.33


ATOM
589
CG
LYS
A
608
18.226
16.064
18.574
1.00
34.41


ATOM
590
CD
LYS
A
608
17.558
17.429
18.538
1.00
39.16


ATOM
591
CE
LYS
A
608
18.430
18.485
19.193
1.00
44.56


ATOM
592
NZ
LYS
A
608
19.755
18.595
18.525
1.00
49.34


ATOM
593
C
LYS
A
608
18.837
13.220
17.311
1.00
13.41


ATOM
594
O
LYS
A
608
18.527
12.904
16.164
1.00
14.71


ATOM
595
N
ASN
A
609
20.098
13.272
17.724
1.00
12.65


ATOM
596
CA
ASN
A
609
21.185
12.977
16.804
1.00
15.37


ATOM
597
CB
ASN
A
609
22.383
13.872
17.121
1.00
19.55


ATOM
598
CG
ASN
A
609
22.059
15.347
16.952
1.00
21.29


ATOM
599
OD1
ASN
A
609
21.630
15.779
15.882
1.00
28.72


ATOM
600
ND2
ASN
A
609
22.261
16.126
18.009
1.00
36.76


ATOM
601
C
ASN
A
609
21.593
11.507
16.743
1.00
14.47


ATOM
602
O
ASN
A
609
22.486
11.135
15.981
1.00
15.29


ATOM
603
N
VAL
A
610
20.955
10.670
17.557
1.00
11.89


ATOM
604
CA
VAL
A
610
21.221
9.233
17.511
1.00
11.43


ATOM
605
CB
VAL
A
610
20.696
8.531
18.777
1.00
11.38


ATOM
606
CG1
VAL
A
610
20.649
7.019
18.571
1.00
10.56


ATOM
607
CG2
VAL
A
610
21.608
8.882
19.955
1.00
10.47


ATOM
608
C
VAL
A
610
20.432
8.809
16.272
1.00
12.97


ATOM
609
O
VAL
A
610
19.221
9.025
16.198
1.00
11.59


ATOM
610
N
ALA
A
611
21.131
8.223
15.302
1.00
11.37


ATOM
611
CA
ALA
A
611
20.554
7.833
14.018
1.00
12.77


ATOM
612
CB
ALA
A
611
21.579
7.021
13.223
1.00
12.83


ATOM
613
C
ALA
A
611
19.208
7.117
13.981
1.00
12.88


ATOM
614
O
ALA
A
611
18.305
7.522
13.247
1.00
14.79


ATOM
615
N
TYR
A
612
19.071
6.050
14.756
1.00
12.18


ATOM
616
CA
TYR
A
612
17.830
5.288
14.743
1.00
10.69


ATOM
617
CB
TYR
A
612
18.147
3.824
14.408
1.00
13.15


ATOM
618
CG
TYR
A
612
16.968
2.877
14.509
1.00
12.63


ATOM
619
CD1
TYR
A
612
15.832
3.054
13.729
1.00
19.45


ATOM
620
CE1
TYR
A
612
14.752
2.185
13.833
1.00
24.00


ATOM
621
CD2
TYR
A
612
16.996
1.805
15.392
1.00
13.47


ATOM
622
CE2
TYR
A
612
15.930
0.938
15.503
1.00
24.95


ATOM
623
CZ
TYR
A
612
14.812
1.129
14.722
1.00
24.27


ATOM
624
OH
TYR
A
612
13.761
0.245
14.831
1.00
25.94


ATOM
625
C
TYR
A
612
17.017
5.371
16.028
1.00
11.05


ATOM
626
O
TYR
A
612
15.812
5.632
15.989
1.00
9.25


ATOM
627
N
HIS
A
613
17.667
5.159
17.166
1.00
10.71


ATOM
628
CA
HIS
A
613
16.951
5.199
18.432
1.00
9.46


ATOM
629
CB
HIS
A
613
17.694
4.391
19.499
1.00
12.29


ATOM
630
CG
HIS
A
613
17.706
2.923
19.232
1.00
13.22


ATOM
631
CD2
HIS
A
613
16.742
1.983
19.364
1.00
13.53


ATOM
632
ND1
HIS
A
613
18.811
2.262
18.726
1.00
8.83


ATOM
633
CE1
HIS
A
613
18.523
0.989
18.562
1.00
12.86


ATOM
634
NE2
HIS
A
613
17.268
0.789
18.942
1.00
16.65


ATOM
635
C
HIS
A
613
16.686
6.606
18.936
1.00
11.81


ATOM
636
O
HIS
A
613
17.226
7.023
19.957
1.00
11.26


ATOM
637
N
ASN
A
614
15.859
7.333
18.192
1.00
12.20


ATOM
638
CA
ASN
A
614
15.459
8.685
18.556
1.00
11.65


ATOM
639
CB
ASN
A
614
15.955
9.702
17.516
1.00
19.08


ATOM
640
CG
ASN
A
614
15.631
9.295
16.090
1.00
17.63


ATOM
641
OD1
ASN
A
614
16.529
9.151
15.253
1.00
16.40


ATOM
642
ND2
ASN
A
614
14.349
9.115
15.802
1.00
11.39


ATOM
643
C
ASN
A
614
13.933
8.690
18.644
1.00
11.53


ATOM
644
O
ASN
A
614
13.298
7.647
18.493
1.00
9.32


ATOM
645
N
TRP
A
615
13.342
9.850
18.890
1.00
8.95


ATOM
646
CA
TRP
A
615
11.893
9.929
19.015
1.00
9.02


ATOM
647
CB
TRP
A
615
11.457
11.397
19.127
1.00
9.00


ATOM
648
CG
TRP
A
615
10.002
11.638
18.809
1.00
8.75


ATOM
649
CD2
TRP
A
615
8.860
11.228
19.581
1.00
10.58


ATOM
650
CE2
TRP
A
615
7.709
11.655
18.883
1.00
12.68


ATOM
651
CE3
TRP
A
615
8.698
10.542
20.789
1.00
12.70


ATOM
652
CD1
TRP
A
615
9.504
12.279
17.709
1.00
11.21


ATOM
653
NE1
TRP
A
615
8.132
12.292
17.747
1.00
11.25


ATOM
654
CZ2
TRP
A
615
6.414
11.418
19.354
1.00
12.28


ATOM
655
CZ3
TRP
A
615
7.410
10.307
21.255
1.00
18.15


ATOM
656
CH2
TRP
A
615
6.286
10.744
20.536
1.00
13.05


ATOM
657
C
TRP
A
615
11.090
9.237
17.910
1.00
8.08


ATOM
658
O
TRP
A
615
10.093
8.579
18.197
1.00
9.24


ATOM
659
N
ARG
A
616
11.514
9.365
16.656
1.00
9.61


ATOM
660
CA
ARG
A
616
10.750
8.759
15.570
1.00
11.24


ATOM
661
CB
ARG
A
616
11.346
9.129
14.206
1.00
9.33


ATOM
662
CG
ARG
A
616
11.241
10.630
13.885
1.00
13.33


ATOM
663
CD
ARG
A
616
9.817
11.169
14.120
1.00
11.22


ATOM
664
NE
ARG
A
616
9.705
12.598
13.823
1.00
13.61


ATOM
665
CZ
ARG
A
616
9.119
13.103
12.741
1.00
15.86


ATOM
666
NH1
ARG
A
616
8.577
12.300
11.834
1.00
15.89


ATOM
667
NH2
ARG
A
616
9.073
14.419
12.564
1.00
19.53


ATOM
668
C
ARG
A
616
10.607
7.250
15.705
1.00
9.88


ATOM
669
O
ARG
A
616
9.575
6.692
15.328
1.00
10.40


ATOM
670
N
HIS
A
617
11.625
6.582
16.242
1.00
7.87


ATOM
671
CA
HIS
A
617
11.514
5.141
16.419
1.00
7.37


ATOM
672
CB
HIS
A
617
12.862
4.523
16.782
1.00
11.98


ATOM
673
CG
HIS
A
617
12.742
3.163
17.390
1.00
8.70


ATOM
674
CD2
HIS
A
617
13.043
2.715
18.632
1.00
9.51


ATOM
675
ND1
HIS
A
617
12.206
2.088
16.713
1.00
8.99


ATOM
676
CE1
HIS
A
617
12.183
1.036
17.510
1.00
11.83


ATOM
677
NE2
HIS
A
617
12.684
1.391
18.681
1.00
10.58


ATOM
678
C
HIS
A
617
10.488
4.816
17.506
1.00
8.63


ATOM
679
O
HIS
A
617
9.692
3.888
17.361
1.00
10.24


ATOM
680
N
ALA
A
618
10.498
5.586
18.591
1.00
7.45


ATOM
681
CA
ALA
A
618
9.549
5.358
19.687
1.00
8.54


ATOM
682
CB
ALA
A
618
9.887
6.261
20.864
1.00
11.31


ATOM
683
C
ALA
A
618
8.126
5.637
19.210
1.00
8.39


ATOM
684
O
ALA
A
618
7.184
4.900
19.523
1.00
9.03


ATOM
685
N
PHE
A
619
7.981
6.725
18.465
1.00
8.88


ATOM
686
CA
PHE
A
619
6.695
7.118
17.911
1.00
9.63


ATOM
687
CB
PHE
A
619
6.850
8.418
17.119
1.00
12.92


ATOM
688
CG
PHE
A
619
5.618
8.809
16.357
1.00
10.44


ATOM
689
CD1
PHE
A
619
4.432
9.066
17.021
1.00
18.21


ATOM
690
CD2
PHE
A
619
5.646
8.914
14.974
1.00
12.41


ATOM
691
CE1
PHE
A
619
3.291
9.412
16.324
1.00
14.74


ATOM
692
CE2
PHE
A
619
4.508
9.260
14.270
1.00
13.16


ATOM
693
CZ
PHE
A
619
3.328
9.512
14.947
1.00
11.01


ATOM
694
C
PHE
A
619
6.150
6.017
16.996
1.00
9.52


ATOM
695
O
PHE
A
619
4.975
5.654
17.079
1.00
9.30


ATOM
696
N
ASN
A
620
7.001
5.490
16.119
1.00
10.15


ATOM
697
CA
ASN
A
620
6.583
4.428
15.204
1.00
11.34


ATOM
698
CB
ASN
A
620
7.694
4.123
14.194
1.00
9.10


ATOM
699
CG
ASN
A
620
7.658
5.052
12.999
1.00
17.16


ATOM
700
OD1
ASN
A
620
8.665
5.656
12.634
1.00
19.51


ATOM
701
ND2
ASN
A
620
6.490
5.166
12.382
1.00
12.88


ATOM
702
C
ASN
A
620
6.206
3.161
15.956
1.00
9.23


ATOM
703
O
ASN
A
620
5.273
2.457
15.574
1.00
10.76


ATOM
704
N
THR
A
621
6.936
2.871
17.026
1.00
8.56


ATOM
705
CA
THR
A
621
6.650
1.688
17.819
1.00
9.52


ATOM
706
CB
THR
A
621
7.707
1.509
18.928
1.00
8.96


ATOM
707
OG1
THR
A
621
9.010
1.404
18.328
1.00
9.14


ATOM
708
CG2
THR
A
621
7.428
0.244
19.736
1.00
7.93


ATOM
709
C
THR
A
621
5.252
1.821
18.425
1.00
10.48


ATOM
710
O
THR
A
621
4.455
0.879
18.382
1.00
10.11


ATOM
711
N
ALA
A
622
4.954
2.995
18.978
1.00
8.32


ATOM
712
CA
ALA
A
622
3.644
3.244
19.573
1.00
9.28


ATOM
713
CB
ALA
A
622
3.642
4.583
20.294
1.00
9.90


ATOM
714
C
ALA
A
622
2.567
3.224
18.488
1.00
10.02


ATOM
715
O
ALA
A
622
1.447
2.769
18.721
1.00
8.06


ATOM
716
N
GLN
A
623
2.902
3.708
17.297
1.00
7.82


ATOM
717
CA
GLN
A
623
1.927
3.708
16.211
1.00
10.17


ATOM
718
CB
GLN
A
623
2.456
4.487
15.003
1.00
8.39


ATOM
719
CG
GLN
A
623
1.473
4.578
13.825
1.00
8.23


ATOM
720
CD
GLN
A
623
1.444
3.319
12.967
1.00
13.63


ATOM
721
OE1
GLN
A
623
2.484
2.730
12.682
1.00
12.75


ATOM
722
NE2
GLN
A
623
0.258
2.919
12.535
1.00
11.69


ATOM
723
C
GLN
A
623
1.597
2.278
15.806
1.00
10.35


ATOM
724
O
GLN
A
623
0.449
1.962
15.501
1.00
9.61


ATOM
725
N
CYS
A
624
2.601
1.406
15.802
1.00
9.08


ATOM
726
CA
CYS
A
624
2.355
0.017
15.439
1.00
9.34


ATOM
727
CB
CYS
A
624
3.679
−0.740
15.273
1.00
11.00


ATOM
728
SG
CYS
A
624
3.481
−2.446
14.713
1.00
11.71


ATOM
729
C
CYS
A
624
1.495
−0.625
16.529
1.00
10.17


ATOM
730
O
CYS
A
624
0.631
−1.448
16.239
1.00
10.64


ATOM
731
N
MET
A
625
1.728
−0.238
17.781
1.00
9.06


ATOM
732
CA
MET
A
625
0.933
−0.764
18.892
1.00
9.38


ATOM
733
CB
MET
A
625
1.418
−0.180
20.225
1.00
8.21


ATOM
734
CG
MET
A
625
0.692
−0.718
21.466
1.00
8.16


ATOM
735
SD
MET
A
625
0.904
−2.512
21.728
1.00
11.88


ATOM
736
CE
MET
A
625
2.600
−2.586
22.309
1.00
11.24


ATOM
737
C
MET
A
625
−0.529
−0.376
18.661
1.00
9.31


ATOM
738
O
MET
A
625
−1.434
−1.208
18.757
1.00
10.06


ATOM
739
N
PHE
A
626
−0.757
0.896
18.353
1.00
9.47


ATOM
740
CA
PHE
A
626
−2.112
1.377
18.092
1.00
9.60


ATOM
741
CB
PHE
A
626
−2.077
2.859
17.725
1.00
9.70


ATOM
742
CG
PHE
A
626
−3.432
3.451
17.461
1.00
7.25


ATOM
743
CD1
PHE
A
626
−4.241
3.858
18.509
1.00
13.86


ATOM
744
CD2
PHE
A
626
−3.897
3.598
16.163
1.00
13.47


ATOM
745
CE1
PHE
A
626
−5.491
4.411
18.267
1.00
18.88


ATOM
746
CE2
PHE
A
626
−5.144
4.147
15.917
1.00
11.81


ATOM
747
CZ
PHE
A
626
−5.942
4.552
16.970
1.00
16.53


ATOM
748
C
PHE
A
626
−2.737
0.579
16.940
1.00
10.98


ATOM
749
O
PHE
A
626
−3.862
0.084
17.047
1.00
12.71


ATOM
750
N
ALA
A
627
−1.999
0.455
15.838
1.00
7.24


ATOM
751
CA
ALA
A
627
−2.486
−0.279
14.675
1.00
9.31


ATOM
752
CB
ALA
A
627
−1.454
−0.220
13.549
1.00
14.42


ATOM
753
C
ALA
A
627
−2.803
−1.734
15.024
1.00
11.79


ATOM
754
O
ALA
A
627
−3.815
−2.276
14.583
1.00
11.59


ATOM
755
N
ALA
A
628
−1.945
−2.361
15.824
1.00
10.63


ATOM
756
CA
ALA
A
628
−2.158
−3.749
16.219
1.00
11.00


ATOM
757
CB
ALA
A
628
−0.934
−4.280
16.961
1.00
11.43


ATOM
758
C
ALA
A
628
−3.398
−3.877
17.099
1.00
11.16


ATOM
759
O
ALA
A
628
−4.152
−4.845
16.994
1.00
12.30


ATOM
760
N
LEU
A
629
−3.608
−2.896
17.970
1.00
9.63


ATOM
761
CA
LEU
A
629
−4.765
−2.924
18.856
1.00
9.96


ATOM
762
CB
LEU
A
629
−4.627
−1.858
19.945
1.00
12.79


ATOM
763
CG
LEU
A
629
−3.538
−2.115
20.990
1.00
10.87


ATOM
764
CD1
LEU
A
629
−3.286
−0.859
21.792
1.00
11.38


ATOM
765
CD2
LEU
A
629
−3.956
−3.264
21.897
1.00
14.99


ATOM
766
C
LEU
A
629
−6.051
−2.692
18.073
1.00
12.31


ATOM
767
O
LEU
A
629
−7.084
−3.300
18.364
1.00
11.63


ATOM
768
N
LYS
A
630
−5.973
−1.822
17.070
1.00
11.64


ATOM
769
CA
LYS
A
630
−7.125
−1.479
16.242
1.00
12.87


ATOM
770
CB
LYS
A
630
−6.984
−0.037
15.738
1.00
15.53


ATOM
771
CG
LYS
A
630
−7.084
1.030
16.820
1.00
13.30


ATOM
772
CD
LYS
A
630
−8.495
1.104
17.385
1.00
19.60


ATOM
773
CE
LYS
A
630
−8.698
2.349
18.245
1.00
18.93


ATOM
774
NZ
LYS
A
630
−7.877
2.334
19.481
1.00
40.94


ATOM
775
C
LYS
A
630
−7.323
−2.422
15.049
1.00
13.54


ATOM
776
O
LYS
A
630
−8.122
−3.350
15.107
1.00
12.81


ATOM
777
N
ALA
A
631
−6.597
−2.170
13.967
1.00
13.05


ATOM
778
CA
ALA
A
631
−6.701
−2.997
12.770
1.00
14.94


ATOM
779
CB
ALA
A
631
−5.763
−2.460
11.688
1.00
17.58


ATOM
780
C
ALA
A
631
−6.374
−4.461
13.068
1.00
16.22


ATOM
781
O
ALA
A
631
−6.960
−5.375
12.479
1.00
15.44


ATOM
782
N
GLY
A
632
−5.439
−4.670
13.990
1.00
12.88


ATOM
783
CA
GLY
A
632
−5.028
−6.014
14.359
1.00
13.10


ATOM
784
C
GLY
A
632
−5.995
−6.711
15.298
1.00
13.12


ATOM
785
O
GLY
A
632
−5.850
−7.902
15.576
1.00
15.03


ATOM
786
N
LYS
A
633
−6.968
−5.959
15.803
1.00
13.75


ATOM
787
CA
LYS
A
633
−7.997
−6.497
16.692
1.00
14.20


ATOM
788
CB
LYS
A
633
−8.815
−7.566
15.954
1.00
13.72


ATOM
789
CG
LYS
A
633
−9.438
−7.109
14.631
1.00
23.64


ATOM
790
CD
LYS
A
633
−10.532
−6.072
14.834
1.00
30.20


ATOM
791
CE
LYS
A
633
−11.182
−5.672
13.510
1.00
34.87


ATOM
792
NZ
LYS
A
633
−10.227
−4.989
12.594
1.00
46.21


ATOM
793
C
LYS
A
633
−7.464
−7.085
17.997
1.00
14.18


ATOM
794
O
LYS
A
633
−8.048
−8.024
18.540
1.00
14.72


ATOM
795
N
ILE
A
634
−6.366
−6.536
18.507
1.00
13.07


ATOM
796
CA
ILE
A
634
−5.801
−7.037
19.755
1.00
12.44


ATOM
797
CB
ILE
A
634
−4.262
−6.819
19.799
1.00
13.52


ATOM
798
CG2
ILE
A
634
−3.709
−7.236
21.156
1.00
14.73


ATOM
799
CG1
ILE
A
634
−3.581
−7.632
18.694
1.00
14.10


ATOM
800
CD1
ILE
A
634
−3.757
−9.128
18.829
1.00
14.44


ATOM
801
C
ILE
A
634
−6.439
−6.346
20.967
1.00
12.23


ATOM
802
O
ILE
A
634
−6.456
−6.894
22.067
1.00
12.06


ATOM
803
N
GLN
A
635
−6.990
−5.155
20.752
1.00
13.17


ATOM
804
CA
GLN
A
635
−7.597
−4.377
21.834
1.00
12.59


ATOM
805
CB
GLN
A
635
−8.330
−3.158
21.267
1.00
14.77


ATOM
806
CG
GLN
A
635
−8.796
−2.180
22.345
1.00
17.07


ATOM
807
CD
GLN
A
635
−9.479
−0.949
21.778
1.00
17.87


ATOM
808
OE1
GLN
A
635
−9.080
−0.425
20.741
1.00
15.93


ATOM
809
NE2
GLN
A
635
−10.509
−0.473
22.471
1.00
27.59


ATOM
810
C
GLN
A
635
−8.549
−5.127
22.762
1.00
13.46


ATOM
811
O
GLN
A
635
−8.382
−5.107
23.984
1.00
12.66


ATOM
812
N
ASN
A
636
−9.554
−5.778
22.188
1.00
12.36


ATOM
813
CA
ASN
A
636
−10.533
−6.493
22.996
1.00
15.16


ATOM
814
CB
ASN
A
636
−11.736
−6.872
22.130
1.00
13.54


ATOM
815
CG
ASN
A
636
−12.508
−5.655
21.658
1.00
19.96


ATOM
816
OD1
ASN
A
636
−12.211
−4.526
22.059
1.00
19.43


ATOM
817
ND2
ASN
A
636
−13.506
−5.874
20.810
1.00
20.88


ATOM
818
C
ASN
A
636
−10.002
−7.708
23.743
1.00
14.39


ATOM
819
O
ASN
A
636
−10.720
−8.312
24.539
1.00
17.61


ATOM
820
N
LYS
A
637
−8.744
−8.060
23.500
1.00
13.69


ATOM
821
CA
LYS
A
637
−8.132
−9.194
24.180
1.00
13.94


ATOM
822
CB
LYS
A
637
−7.124
−9.893
23.262
1.00
13.19


ATOM
823
CG
LYS
A
637
−7.667
−10.328
21.910
1.00
16.41


ATOM
824
CD
LYS
A
637
−6.599
−11.079
21.128
1.00
18.79


ATOM
825
CE
LYS
A
637
−7.110
−11.542
19.773
1.00
21.00


ATOM
826
NZ
LYS
A
637
−8.266
−12.467
19.893
1.00
27.72


ATOM
827
C
LYS
A
637
−7.400
−8.708
25.435
1.00
14.29


ATOM
828
O
LYS
A
637
−6.930
−9.514
26.237
1.00
15.91


ATOM
829
N
LEU
A
638
−7.316
−7.391
25.611
1.00
13.88


ATOM
830
CA
LEU
A
638
−6.602
−6.828
26.757
1.00
14.02


ATOM
831
CB
LEU
A
638
−5.426
−5.988
26.256
1.00
14.42


ATOM
832
CG
LEU
A
638
−4.496
−6.595
25.201
1.00
13.65


ATOM
833
CD1
LEU
A
638
−3.405
−5.589
24.860
1.00
13.98


ATOM
834
CD2
LEU
A
638
−3.881
−7.885
25.718
1.00
12.70


ATOM
835
C
LEU
A
638
−7.464
−5.973
27.687
1.00
13.83


ATOM
836
O
LEU
A
638
−8.551
−5.529
27.313
1.00
16.24


ATOM
837
N
THR
A
639
−6.968
−5.745
28.902
1.00
13.04


ATOM
838
CA
THR
A
639
−7.665
−4.913
29.885
1.00
12.97


ATOM
839
CB
THR
A
639
−7.225
−5.244
31.323
1.00
9.72


ATOM
840
OG1
THR
A
639
−5.883
−4.777
31.534
1.00
11.58


ATOM
841
CG2
THR
A
639
−7.284
−6.752
31.574
1.00
13.01


ATOM
842
C
THR
A
639
−7.320
−3.443
29.627
1.00
11.14


ATOM
843
O
THR
A
639
−6.369
−3.147
28.910
1.00
12.39


ATOM
844
N
ASP
A
640
−8.082
−2.524
30.216
1.00
11.83


ATOM
845
CA
ASP
A
640
−7.814
−1.098
30.027
1.00
11.03


ATOM
846
CB
ASP
A
640
−8.846
−0.243
30.774
1.00
9.58


ATOM
847
CG
ASP
A
640
−10.238
−0.368
30.191
1.00
23.27


ATOM
848
OD1
ASP
A
640
−10.357
−0.828
29.037
1.00
21.74


ATOM
849
OD2
ASP
A
640
−11.211
0.011
30.879
1.00
18.96


ATOM
850
C
ASP
A
640
−6.419
−0.724
30.519
1.00
10.85


ATOM
851
O
ASP
A
640
−5.708
0.058
29.881
1.00
11.05


ATOM
852
N
LEU
A
641
−6.031
−1.290
31.655
1.00
11.16


ATOM
853
CA
LEU
A
641
−4.727
−1.004
32.235
1.00
10.51


ATOM
854
CB
LEU
A
641
−4.628
−1.606
33.640
1.00
13.05


ATOM
855
CG
LEU
A
641
−5.633
−1.081
34.674
1.00
13.28


ATOM
856
CD1
LEU
A
641
−5.383
−1.762
36.005
1.00
14.91


ATOM
857
CD2
LEU
A
641
−5.506
0.432
34.813
1.00
12.98


ATOM
858
C
LEU
A
641
−3.593
−1.527
31.359
1.00
10.02


ATOM
859
O
LEU
A
641
−2.550
−0.883
31.237
1.00
9.79


ATOM
860
N
GLU
A
642
−3.791
−2.692
30.748
1.00
9.49


ATOM
861
CA
GLU
A
642
−2.756
−3.253
29.886
1.00
9.55


ATOM
862
CB
GLU
A
642
−3.120
−4.687
29.493
1.00
13.24


ATOM
863
CG
GLU
A
642
−3.215
−5.605
30.705
1.00
17.56


ATOM
864
CD
GLU
A
642
−3.645
−7.021
30.373
1.00
14.47


ATOM
865
OE1
GLU
A
642
−4.411
−7.212
29.404
1.00
12.63


ATOM
866
OE2
GLU
A
642
−3.233
−7.949
31.108
1.00
15.36


ATOM
867
C
GLU
A
642
−2.568
−2.366
28.656
1.00
9.56


ATOM
868
O
GLU
A
642
−1.442
−2.135
28.217
1.00
10.36


ATOM
869
N
ILE
A
643
−3.665
−1.847
28.112
1.00
9.98


ATOM
870
CA
ILE
A
643
−3.585
−0.978
26.945
1.00
11.53


ATOM
871
CB
ILE
A
643
−4.992
−0.683
26.391
1.00
12.52


ATOM
872
CG2
ILE
A
643
−4.915
0.367
25.281
1.00
11.83


ATOM
873
CG1
ILE
A
643
−5.614
−1.984
25.885
1.00
11.82


ATOM
874
CD1
ILE
A
643
−7.089
−1.872
25.553
1.00
18.49


ATOM
875
C
ILE
A
643
−2.883
0.323
27.339
1.00
9.56


ATOM
876
O
ILE
A
643
−1.993
0.806
26.635
1.00
10.76


ATOM
877
N
LEU
A
644
−3.278
0.880
28.479
1.00
9.68


ATOM
878
CA
LEU
A
644
−2.663
2.105
28.974
1.00
9.78


ATOM
879
CB
LEU
A
644
−3.285
2.482
30.321
1.00
11.15


ATOM
880
CG
LEU
A
644
−2.658
3.643
31.093
1.00
14.02


ATOM
881
CD1
LEU
A
644
−2.853
4.946
30.328
1.00
14.15


ATOM
882
CD2
LEU
A
644
−3.315
3.735
32.471
1.00
14.10


ATOM
883
C
LEU
A
644
−1.152
1.899
29.139
1.00
9.98


ATOM
884
O
LEU
A
644
−0.342
2.720
28.694
1.00
9.97


ATOM
885
N
ALA
A
645
−0.778
0.788
29.766
1.00
8.98


ATOM
886
CA
ALA
A
645
0.634
0.492
30.008
1.00
8.84


ATOM
887
CB
ALA
A
645
0.763
−0.724
30.928
1.00
8.17


ATOM
888
C
ALA
A
645
1.414
0.256
28.718
1.00
9.39


ATOM
889
O
ALA
A
645
2.556
0.687
28.598
1.00
9.92


ATOM
890
N
LEU
A
646
0.799
−0.430
27.761
1.00
8.76


ATOM
891
CA
LEU
A
646
1.462
−0.708
26.488
1.00
8.34


ATOM
892
CB
LEU
A
646
0.607
−1.652
25.644
1.00
10.30


ATOM
893
CG
LEU
A
646
0.541
−3.101
26.128
1.00
11.47


ATOM
894
CD1
LEU
A
646
−0.557
−3.832
25.379
1.00
15.28


ATOM
895
CD2
LEU
A
646
1.879
−3.779
25.906
1.00
10.48


ATOM
896
C
LEU
A
646
1.761
0.550
25.682
1.00
7.55


ATOM
897
O
LEU
A
646
2.837
0.676
25.094
1.00
9.05


ATOM
898
N
LEU
A
647
0.812
1.479
25.643
1.00
7.57


ATOM
899
CA
LEU
A
647
1.020
2.713
24.889
1.00
8.87


ATOM
900
CB
LEU
A
647
−0.283
3.516
24.803
1.00
7.82


ATOM
901
CG
LEU
A
647
−0.214
4.722
23.862
1.00
10.06


ATOM
902
CD1
LEU
A
647
0.194
4.251
22.470
1.00
13.81


ATOM
903
CD2
LEU
A
647
−1.560
5.437
23.820
1.00
12.05


ATOM
904
C
LEU
A
647
2.120
3.550
25.540
1.00
8.12


ATOM
905
O
LEU
A
647
3.011
4.070
24.863
1.00
8.78


ATOM
906
N
ILE
A
648
2.056
3.676
26.860
1.00
9.66


ATOM
907
CA
ILE
A
648
3.065
4.429
27.597
1.00
8.86


ATOM
908
CB
ILE
A
648
2.692
4.501
29.100
1.00
10.81


ATOM
909
CG2
ILE
A
648
3.851
5.063
29.917
1.00
7.70


ATOM
910
CG1
ILE
A
648
1.439
5.364
29.266
1.00
11.45


ATOM
911
CD1
ILE
A
648
0.921
5.437
30.688
1.00
9.57


ATOM
912
C
ILE
A
648
4.427
3.756
27.424
1.00
8.38


ATOM
913
O
ILE
A
648
5.439
4.427
27.180
1.00
9.63


ATOM
914
N
ALA
A
649
4.456
2.430
27.536
1.00
9.32


ATOM
915
CA
ALA
A
649
5.710
1.697
27.388
1.00
9.98


ATOM
916
CB
ALA
A
649
5.506
0.214
27.703
1.00
11.64


ATOM
917
C
ALA
A
649
6.285
1.853
25.989
1.00
9.64


ATOM
918
O
ALA
A
649
7.471
2.126
25.831
1.00
10.34


ATOM
919
N
ALA
A
650
5.449
1.680
24.971
1.00
11.02


ATOM
920
CA
ALA
A
650
5.914
1.814
23.591
1.00
9.43


ATOM
921
CB
ALA
A
650
4.747
1.618
22.617
1.00
8.79


ATOM
922
C
ALA
A
650
6.561
3.183
23.359
1.00
8.11


ATOM
923
O
ALA
A
650
7.628
3.292
22.748
1.00
9.60


ATOM
924
N
LEU
A
651
5.914
4.233
23.851
1.00
9.58


ATOM
925
CA
LEU
A
651
6.443
5.582
23.679
1.00
10.27


ATOM
926
CB
LEU
A
651
5.383
6.613
24.066
1.00
9.84


ATOM
927
CG
LEU
A
651
4.198
6.717
23.101
1.00
6.24


ATOM
928
CD1
LEU
A
651
3.038
7.432
23.772
1.00
14.57


ATOM
929
CD2
LEU
A
651
4.637
7.463
21.846
1.00
11.43


ATOM
930
C
LEU
A
651
7.706
5.848
24.488
1.00
10.46


ATOM
931
O
LEU
A
651
8.573
6.611
24.066
1.00
9.75


ATOM
932
N
SER
A
652
7.807
5.194
25.640
1.00
9.58


ATOM
933
CA
SER
A
652
8.935
5.394
26.542
1.00
10.30


ATOM
934
CB
SER
A
652
8.422
5.453
27.983
1.00
9.30


ATOM
935
OG
SER
A
652
7.367
6.379
28.133
1.00
11.78


ATOM
936
C
SER
A
652
10.026
4.334
26.504
1.00
8.64


ATOM
937
O
SER
A
652
11.068
4.520
27.125
1.00
9.90


ATOM
938
N
HIS
A
653
9.805
3.249
25.765
1.00
9.64


ATOM
939
CA
HIS
A
653
10.739
2.128
25.769
1.00
9.99


ATOM
940
CB
HIS
A
653
10.164
0.963
24.952
1.00
8.26


ATOM
941
CG
HIS
A
653
10.546
0.980
23.510
1.00
8.55


ATOM
942
CD2
HIS
A
653
11.529
0.333
22.842
1.00
9.53


ATOM
943
ND1
HIS
A
653
9.881
1.740
22.569
1.00
10.01


ATOM
944
CE1
HIS
A
653
10.440
1.559
21.387
1.00
6.46


ATOM
945
NE2
HIS
A
653
11.444
0.708
21.526
1.00
6.65


ATOM
946
C
HIS
A
653
12.210
2.321
25.412
1.00
10.62


ATOM
947
O
HIS
A
653
13.024
1.459
25.741
1.00
8.86


ATOM
948
N
ASP
A
654
12.559
3.424
24.752
1.00
9.82


ATOM
949
CA
ASP
A
654
13.959
3.673
24.406
1.00
9.46


ATOM
950
CB
ASP
A
654
14.184
3.580
22.889
1.00
10.10


ATOM
951
CG
ASP
A
654
14.509
2.172
22.432
1.00
10.77


ATOM
952
OD1
ASP
A
654
15.159
1.444
23.204
1.00
9.55


ATOM
953
OD2
ASP
A
654
14.141
1.812
21.294
1.00
8.85


ATOM
954
C
ASP
A
654
14.477
5.024
24.896
1.00
9.92


ATOM
955
O
ASP
A
654
15.500
5.507
24.413
1.00
9.67


ATOM
956
N
LEU
A
655
13.783
5.619
25.865
1.00
9.19


ATOM
957
CA
LEU
A
655
14.169
6.922
26.408
1.00
10.06


ATOM
958
CB
LEU
A
655
13.364
7.214
27.677
1.00
8.55


ATOM
959
CG
LEU
A
655
11.900
7.603
27.479
1.00
10.24


ATOM
960
CD1
LEU
A
655
11.151
7.468
28.805
1.00
9.10


ATOM
961
CD2
LEU
A
655
11.819
9.028
26.944
1.00
15.71


ATOM
962
C
LEU
A
655
15.658
7.101
26.713
1.00
10.50


ATOM
963
O
LEU
A
655
16.279
6.268
27.372
1.00
9.92


ATOM
964
N
ASP
A
656
16.215
8.209
26.232
1.00
8.66


ATOM
965
CA
ASP
A
656
17.622
8.542
26.448
1.00
8.66


ATOM
966
CB
ASP
A
656
17.867
8.811
27.941
1.00
11.08


ATOM
967
CG
ASP
A
656
19.211
9.475
28.207
1.00
16.07


ATOM
968
OD1
ASP
A
656
19.576
10.406
27.460
1.00
11.04


ATOM
969
OD2
ASP
A
656
19.897
9.074
29.173
1.00
13.88


ATOM
970
C
ASP
A
656
18.600
7.483
25.939
1.00
8.59


ATOM
971
O
ASP
A
656
19.670
7.288
26.511
1.00
9.89


ATOM
972
N
HIS
A
657
18.242
6.806
24.851
1.00
9.07


ATOM
973
CA
HIS
A
657
19.118
5.790
24.284
1.00
10.63


ATOM
974
CB
HIS
A
657
18.412
5.068
23.137
1.00
9.06


ATOM
975
CG
HIS
A
657
19.095
3.810
22.712
1.00
8.47


ATOM
976
CD2
HIS
A
657
20.347
3.589
22.245
1.00
7.97


ATOM
977
ND1
HIS
A
657
18.480
2.575
22.748
1.00
12.46


ATOM
978
CE1
HIS
A
657
19.322
1.652
22.322
1.00
5.38


ATOM
979
NE2
HIS
A
657
20.464
2.242
22.011
1.00
12.33


ATOM
980
C
HIS
A
657
20.404
6.453
23.778
1.00
11.40


ATOM
981
O
HIS
A
657
20.362
7.404
22.993
1.00
11.45


ATOM
982
N
PRO
A
658
21.567
5.957
24.230
1.00
11.01


ATOM
983
CD
PRO
A
658
21.697
4.963
25.311
1.00
10.94


ATOM
984
CA
PRO
A
658
22.884
6.479
23.850
1.00
10.19


ATOM
985
CB
PRO
A
658
23.792
5.930
24.944
1.00
9.66


ATOM
986
CG
PRO
A
658
23.171
4.618
25.252
1.00
16.61


ATOM
987
C
PRO
A
658
23.386
6.123
22.451
1.00
11.02


ATOM
988
O
PRO
A
658
24.428
6.627
22.021
1.00
12.41


ATOM
989
N
GLY
A
659
22.659
5.265
21.744
1.00
8.82


ATOM
990
CA
GLY
A
659
23.080
4.888
20.405
1.00
8.78


ATOM
991
C
GLY
A
659
24.115
3.781
20.356
1.00
9.97


ATOM
992
O
GLY
A
659
24.750
3.566
19.316
1.00
12.32


ATOM
993
N
VAL
A
660
24.305
3.095
21.480
1.00
8.93


ATOM
994
CA
VAL
A
660
25.248
1.983
21.564
1.00
9.69


ATOM
995
CB
VAL
A
660
26.554
2.387
22.301
1.00
10.19


ATOM
996
CG1
VAL
A
660
27.358
3.355
21.434
1.00
12.07


ATOM
997
CG2
VAL
A
660
26.236
3.020
23.642
1.00
12.93


ATOM
998
C
VAL
A
660
24.545
0.834
22.289
1.00
10.76


ATOM
999
O
VAL
A
660
23.601
1.059
23.052
1.00
10.23


ATOM
1000
N
SER
A
661
25.002
−0.392
22.049
1.00
7.63


ATOM
1001
CA
SER
A
661
24.371
−1.577
22.624
1.00
10.33


ATOM
1002
CB
SER
A
661
24.748
−2.801
21.793
1.00
8.76


ATOM
1003
OG
SER
A
661
26.099
−3.151
22.021
1.00
9.56


ATOM
1004
C
SER
A
661
24.687
−1.864
24.088
1.00
9.36


ATOM
1005
O
SER
A
661
25.549
−1.230
24.696
1.00
10.42


ATOM
1006
N
ASN
A
662
23.969
−2.838
24.643
1.00
10.10


ATOM
1007
CA
ASN
A
662
24.165
−3.261
26.026
1.00
8.94


ATOM
1008
CB
ASN
A
662
23.177
−4.369
26.384
1.00
12.24


ATOM
1009
CG
ASN
A
662
21.832
−3.836
26.824
1.00
11.27


ATOM
1010
OD1
ASN
A
662
20.794
−4.457
26.592
1.00
19.20


ATOM
1011
ND2
ASN
A
662
21.844
−2.689
27.483
1.00
5.90


ATOM
1012
C
ASN
A
662
25.586
−3.781
26.161
1.00
11.89


ATOM
1013
O
ASN
A
662
26.289
−3.459
27.116
1.00
12.39


ATOM
1014
N
GLN
A
663
26.010
−4.598
25.199
1.00
10.34


ATOM
1015
CA
GLN
A
663
27.356
−5.139
25.246
1.00
11.06


ATOM
1016
CB
GLN
A
663
27.578
−6.120
24.083
1.00
14.83


ATOM
1017
CG
GLN
A
663
26.677
−7.373
24.197
1.00
25.28


ATOM
1018
CD
GLN
A
663
25.283
−7.191
23.575
1.00
24.96


ATOM
1019
OE1
GLN
A
663
24.919
−6.113
23.106
1.00
31.10


ATOM
1020
NE2
GLN
A
663
24.497
−8.271
23.572
1.00
46.85


ATOM
1021
C
GLN
A
663
28.422
−4.039
25.236
1.00
13.51


ATOM
1022
O
GLN
A
663
29.439
−4.161
25.921
1.00
12.70


ATOM
1023
N
PHE
A
664
28.184
−2.956
24.504
1.00
12.64


ATOM
1024
CA
PHE
A
664
29.145
−1.852
24.465
1.00
11.20


ATOM
1025
CB
PHE
A
664
28.754
−0.838
23.380
1.00
12.60


ATOM
1026
CG
PHE
A
664
29.669
0.355
23.296
1.00
15.21


ATOM
1027
CD1
PHE
A
664
29.554
1.407
24.198
1.00
13.93


ATOM
1028
CD2
PHE
A
664
30.668
0.409
22.336
1.00
10.34


ATOM
1029
CE1
PHE
A
664
30.419
2.484
24.144
1.00
11.59


ATOM
1030
CE2
PHE
A
664
31.541
1.487
22.275
1.00
16.42


ATOM
1031
CZ
PHE
A
664
31.418
2.527
23.182
1.00
18.27


ATOM
1032
C
PHE
A
664
29.207
−1.171
25.830
1.00
11.75


ATOM
1033
O
PHE
A
664
30.290
−0.818
26.306
1.00
11.28


ATOM
1034
N
LEU
A
665
28.046
−0.980
26.452
1.00
11.17


ATOM
1035
CA
LEU
A
665
27.982
−0.346
27.768
1.00
11.46


ATOM
1036
CB
LEU
A
665
26.524
−0.163
28.204
1.00
11.38


ATOM
1037
CG
LEU
A
665
25.703
0.864
27.420
1.00
9.72


ATOM
1038
CD1
LEU
A
665
24.304
0.959
28.015
1.00
16.35


ATOM
1039
CD2
LEU
A
665
26.399
2.215
27.470
1.00
13.26


ATOM
1040
C
LEU
A
665
28.726
−1.200
28.793
1.00
13.75


ATOM
1041
O
LEU
A
665
29.404
−0.686
29.681
1.00
11.85


ATOM
1042
N
ILE
A
666
28.591
−2.512
28.661
1.00
12.41


ATOM
1043
CA
ILE
A
666
29.259
−3.444
29.559
1.00
13.52


ATOM
1044
CB
ILE
A
666
28.773
−4.887
29.300
1.00
13.10


ATOM
1045
CG2
ILE
A
666
29.667
−5.882
30.020
1.00
13.00


ATOM
1046
CG1
ILE
A
666
27.322
−5.036
29.761
1.00
10.73


ATOM
1047
CD1
ILE
A
666
26.687
−6.346
29.369
1.00
14.67


ATOM
1048
C
ILE
A
666
30.770
−3.381
29.356
1.00
11.71


ATOM
1049
O
ILE
A
666
31.541
−3.297
30.317
1.00
14.40


ATOM
1050
N
ASN
A
667
31.183
−3.408
28.094
1.00
12.52


ATOM
1051
CA
ASN
A
667
32.599
−3.382
27.733
1.00
11.69


ATOM
1052
CB
ASN
A
667
32.745
−3.652
26.232
1.00
15.94


ATOM
1053
CG
ASN
A
667
32.340
−5.065
25.848
1.00
13.91


ATOM
1054
OD1
ASN
A
667
32.138
−5.363
24.669
1.00
17.63


ATOM
1055
ND2
ASN
A
667
32.233
−5.946
26.837
1.00
11.25


ATOM
1056
C
ASN
A
667
33.323
−2.090
28.091
1.00
15.59


ATOM
1057
O
ASN
A
667
34.530
−2.104
28.355
1.00
16.72


ATOM
1058
N
THR
A
668
32.601
−0.974
28.098
1.00
15.05


ATOM
1059
CA
THR
A
668
33.211
0.308
28.428
1.00
16.29


ATOM
1060
CB
THR
A
668
32.670
1.432
27.520
1.00
16.12


ATOM
1061
OG1
THR
A
668
31.237
1.448
27.567
1.00
19.49


ATOM
1062
CG2
THR
A
668
33.133
1.207
26.078
1.00
15.93


ATOM
1063
C
THR
A
668
32.995
0.672
29.895
1.00
18.10


ATOM
1064
O
THR
A
668
33.158
1.830
30.297
1.00
20.65


ATOM
1065
N
ASN
A
669
32.617
−0.330
30.682
1.00
17.75


ATOM
1066
CA
ASN
A
669
32.402
−0.177
32.115
1.00
20.15


ATOM
1067
CB
ASN
A
669
33.749
0.053
32.797
1.00
28.92


ATOM
1068
CG
ASN
A
669
34.791
−0.955
32.361
1.00
34.79


ATOM
1069
OD1
ASN
A
669
34.619
−2.160
32.543
1.00
40.75


ATOM
1070
ND2
ASN
A
669
35.877
−0.468
31.772
1.00
36.76


ATOM
1071
C
ASN
A
669
31.428
0.926
32.515
1.00
20.87


ATOM
1072
O
ASN
A
669
31.690
1.696
33.443
1.00
21.59


ATOM
1073
N
SER
A
670
30.302
0.996
31.819
1.00
17.34


ATOM
1074
CA
SER
A
670
29.286
1.992
32.120
1.00
19.60


ATOM
1075
CB
SER
A
670
28.103
1.836
31.160
1.00
18.96


ATOM
1076
OG
SER
A
670
27.023
2.672
31.535
1.00
22.69


ATOM
1077
C
SER
A
670
28.803
1.787
33.551
1.00
16.24


ATOM
1078
O
SER
A
670
28.755
0.655
34.041
1.00
14.46


ATOM
1079
N
GLU
A
671
28.455
2.879
34.227
1.00
18.45


ATOM
1080
CA
GLU
A
671
27.951
2.775
35.589
1.00
19.69


ATOM
1081
CB
GLU
A
671
27.756
4.154
36.209
1.00
17.48


ATOM
1082
CG
GLU
A
671
28.985
5.024
36.189
1.00
31.14


ATOM
1083
CD
GLU
A
671
28.901
6.156
37.191
1.00
32.78


ATOM
1084
OE1
GLU
A
671
27.830
6.796
37.291
1.00
31.62


ATOM
1085
OE2
GLU
A
671
29.914
6.406
37.875
1.00
26.52


ATOM
1086
C
GLU
A
671
26.611
2.058
35.549
1.00
18.77


ATOM
1087
O
GLU
A
671
26.253
1.332
36.482
1.00
19.75


ATOM
1088
N
LEU
A
672
25.868
2.281
34.466
1.00
17.92


ATOM
1089
CA
LEU
A
672
24.569
1.646
34.279
1.00
15.76


ATOM
1090
CB
LEU
A
672
23.954
2.067
32.942
1.00
12.50


ATOM
1091
CG
LEU
A
672
23.478
3.509
32.771
1.00
18.92


ATOM
1092
CD1
LEU
A
672
23.101
3.741
31.314
1.00
18.65


ATOM
1093
CD2
LEU
A
672
22.292
3.766
33.678
1.00
24.52


ATOM
1094
C
LEU
A
672
24.738
0.130
34.291
1.00
13.50


ATOM
1095
O
LEU
A
672
23.961
−0.586
34.912
1.00
12.92


ATOM
1096
N
ALA
A
673
25.755
−0.358
33.590
1.00
13.11


ATOM
1097
CA
ALA
A
673
26.001
−1.792
33.546
1.00
13.53


ATOM
1098
CB
ALA
A
673
27.169
−2.099
32.594
1.00
11.10


ATOM
1099
C
ALA
A
673
26.318
−2.283
34.956
1.00
13.78


ATOM
1100
O
ALA
A
673
25.925
−3.380
35.354
1.00
12.36


ATOM
1101
N
LEU
A
674
27.028
−1.458
35.718
1.00
15.22


ATOM
1102
CA
LEU
A
674
27.394
−1.829
37.076
1.00
16.65


ATOM
1103
CB
LEU
A
674
28.414
−0.832
37.632
1.00
18.96


ATOM
1104
CG
LEU
A
674
29.225
−1.323
38.832
1.00
26.52


ATOM
1105
CD1
LEU
A
674
29.939
−2.620
38.460
1.00
24.45


ATOM
1106
CD2
LEU
A
674
30.231
−0.258
39.246
1.00
20.57


ATOM
1107
C
LEU
A
674
26.152
−1.866
37.960
1.00
15.94


ATOM
1108
O
LEU
A
674
25.930
−2.818
38.709
1.00
16.86


ATOM
1109
N
MET
A
675
25.335
−0.822
37.851
1.00
19.35


ATOM
1110
CA
MET
A
675
24.107
−0.694
38.627
1.00
18.57


ATOM
1111
CB
MET
A
675
23.413
0.641
38.312
1.00
29.02


ATOM
1112
CG
MET
A
675
24.180
1.882
38.753
1.00
32.86


ATOM
1113
SD
MET
A
675
23.766
3.373
37.785
1.00
38.23


ATOM
1114
CE
MET
A
675
22.129
3.769
38.381
1.00
40.96


ATOM
1115
C
MET
A
675
23.133
−1.830
38.346
1.00
17.83


ATOM
1116
O
MET
A
675
22.529
−2.383
39.265
1.00
17.84


ATOM
1117
N
TYR
A
676
23.000
−2.184
37.073
1.00
15.75


ATOM
1118
CA
TYR
A
676
22.052
−3.212
36.679
1.00
16.85


ATOM
1119
CB
TYR
A
676
21.293
−2.720
35.442
1.00
16.19


ATOM
1120
CG
TYR
A
676
20.619
−1.374
35.668
1.00
20.30


ATOM
1121
CD1
TYR
A
676
19.694
−1.197
36.691
1.00
31.51


ATOM
1122
CE1
TYR
A
676
19.107
0.045
36.922
1.00
18.89


ATOM
1123
CD2
TYR
A
676
20.934
−0.276
34.877
1.00
23.78


ATOM
1124
CE2
TYR
A
676
20.354
0.962
35.097
1.00
27.90


ATOM
1125
CZ
TYR
A
676
19.443
1.117
36.118
1.00
24.78


ATOM
1126
OH
TYR
A
676
18.866
2.354
36.326
1.00
28.03


ATOM
1127
C
TYR
A
676
22.605
−4.623
36.471
1.00
16.48


ATOM
1128
O
TYR
A
676
21.949
−5.478
35.872
1.00
15.88


ATOM
1129
N
ASN
A
677
23.814
−4.863
36.968
1.00
16.14


ATOM
1130
CA
ASN
A
677
24.433
−6.182
36.888
1.00
14.23


ATOM
1131
CB
ASN
A
677
23.666
−7.138
37.812
1.00
21.33


ATOM
1132
CG
ASN
A
677
24.382
−8.452
38.022
1.00
29.37


ATOM
1133
OD1
ASN
A
677
25.570
−8.478
38.349
1.00
38.44


ATOM
1134
ND2
ASN
A
677
23.662
−9.555
37.847
1.00
42.62


ATOM
1135
C
ASN
A
677
24.516
−6.765
35.474
1.00
15.05


ATOM
1136
O
ASN
A
677
24.332
−7.966
35.275
1.00
14.59


ATOM
1137
N
ASP
A
678
24.802
−5.904
34.502
1.00
13.69


ATOM
1138
CA
ASP
A
678
24.926
−6.302
33.100
1.00
16.08


ATOM
1139
CB
ASP
A
678
26.080
−7.293
32.915
1.00
12.96


ATOM
1140
CG
ASP
A
678
27.430
−6.691
33.234
1.00
18.27


ATOM
1141
OD1
ASP
A
678
27.519
−5.452
33.377
1.00
16.21


ATOM
1142
OD2
ASP
A
678
28.406
−7.464
33.334
1.00
20.95


ATOM
1143
C
ASP
A
678
23.667
−6.919
32.499
1.00
16.35


ATOM
1144
O
ASP
A
678
23.731
−7.509
31.420
1.00
17.49


ATOM
1145
N
GLU
A
679
22.534
−6.790
33.184
1.00
14.03


ATOM
1146
CA
GLU
A
679
21.278
−7.358
32.690
1.00
14.39


ATOM
1147
CB
GLU
A
679
20.567
−8.133
33.799
1.00
14.04


ATOM
1148
CG
GLU
A
679
21.314
−9.351
34.300
1.00
22.79


ATOM
1149
CD
GLU
A
679
20.514
−10.128
35.330
1.00
43.42


ATOM
1150
OE1
GLU
A
679
19.464
−10.699
34.964
1.00
51.30


ATOM
1151
OE2
GLU
A
679
20.931
−10.162
36.507
1.00
41.34


ATOM
1152
C
GLU
A
679
20.320
−6.301
32.151
1.00
12.89


ATOM
1153
O
GLU
A
679
19.873
−5.430
32.895
1.00
13.61


ATOM
1154
N
SER
A
680
19.993
−6.401
30.863
1.00
10.87


ATOM
1155
CA
SER
A
680
19.086
−5.456
30.209
1.00
12.50


ATOM
1156
CB
SER
A
680
17.627
−5.787
30.555
1.00
12.08


ATOM
1157
OG
SER
A
680
17.267
−7.087
30.111
1.00
11.26


ATOM
1158
C
SER
A
680
19.409
−4.038
30.663
1.00
11.78


ATOM
1159
O
SER
A
680
18.517
−3.280
31.045
1.00
12.76


ATOM
1160
N
VAL
A
681
20.693
−3.693
30.617
1.00
9.67


ATOM
1161
CA
VAL
A
681
21.183
−2.386
31.049
1.00
7.19


ATOM
1162
CB
VAL
A
681
22.688
−2.248
30.725
1.00
11.97


ATOM
1163
CG1
VAL
A
681
23.219
−0.917
31.245
1.00
10.98


ATOM
1164
CG2
VAL
A
681
23.460
−3.423
31.346
1.00
12.93


ATOM
1165
C
VAL
A
681
20.426
−1.195
30.453
1.00
9.58


ATOM
1166
O
VAL
A
681
19.870
−0.378
31.185
1.00
10.02


ATOM
1167
N
LEU
A
681A
20.420
−1.094
29.128
1.00
9.51


ATOM
1168
CA
LEU
A
681A
19.718
−0.011
28.443
1.00
10.16


ATOM
1169
CB
LEU
A
681A
19.773
−0.216
26.929
1.00
7.24


ATOM
1170
CG
LEU
A
681A
21.079
0.035
26.178
1.00
9.74


ATOM
1171
CD1
LEU
A
681A
20.979
−0.563
24.788
1.00
13.02


ATOM
1172
CD2
LEU
A
681A
21.345
1.526
26.102
1.00
15.84


ATOM
1173
C
LEU
A
681A
18.253
0.049
28.851
1.00
8.34


ATOM
1174
O
LEU
A
681A
17.725
1.118
29.174
1.00
10.62


ATOM
1175
N
GLU
A
682
17.599
−1.110
28.834
1.00
10.08


ATOM
1176
CA
GLU
A
682
16.183
−1.191
29.161
1.00
7.57


ATOM
1177
CB
GLU
A
682
15.667
−2.599
28.855
1.00
6.60


ATOM
1178
CG
GLU
A
682
15.731
−2.954
27.348
1.00
8.78


ATOM
1179
CD
GLU
A
682
17.151
−3.199
26.835
1.00
12.12


ATOM
1180
OE1
GLU
A
682
18.001
−3.693
27.614
1.00
10.38


ATOM
1181
OE2
GLU
A
682
17.418
−2.919
25.646
1.00
10.27


ATOM
1182
C
GLU
A
682
15.867
−0.773
30.594
1.00
8.81


ATOM
1183
O
GLU
A
682
14.829
−0.158
30.854
1.00
7.94


ATOM
1184
N
HIS
A
683
16.752
−1.099
31.526
1.00
9.05


ATOM
1185
CA
HIS
A
683
16.531
−0.677
32.897
1.00
10.40


ATOM
1186
CB
HIS
A
683
17.561
−1.324
33.830
1.00
11.92


ATOM
1187
CG
HIS
A
683
17.161
−2.686
34.296
1.00
10.38


ATOM
1188
CD2
HIS
A
683
17.557
−3.920
33.903
1.00
9.93


ATOM
1189
ND1
HIS
A
683
16.172
−2.888
35.238
1.00
14.33


ATOM
1190
CE1
HIS
A
683
15.977
−4.183
35.400
1.00
7.54


ATOM
1191
NE2
HIS
A
683
16.806
−4.831
34.599
1.00
15.67


ATOM
1192
C
HIS
A
683
16.631
0.846
32.925
1.00
11.08


ATOM
1193
O
HIS
A
683
15.868
1.512
33.621
1.00
10.48


ATOM
1194
N
HIS
A
684
17.553
1.397
32.138
1.00
10.86


ATOM
1195
CA
HIS
A
684
17.710
2.844
32.076
1.00
9.98


ATOM
1196
CB
HIS
A
684
18.941
3.233
31.256
1.00
9.09


ATOM
1197
CG
HIS
A
684
19.229
4.697
31.284
1.00
8.54


ATOM
1198
CD2
HIS
A
684
19.399
5.555
32.322
1.00
5.20


ATOM
1199
ND1
HIS
A
684
19.313
5.467
30.142
1.00
17.15


ATOM
1200
CE1
HIS
A
684
19.518
6.728
30.474
1.00
9.30


ATOM
1201
NE2
HIS
A
684
19.573
6.807
31.795
1.00
15.79


ATOM
1202
C
HIS
A
684
16.473
3.502
31.465
1.00
9.44


ATOM
1203
O
HIS
A
684
16.020
4.542
31.941
1.00
11.75


ATOM
1204
N
HIS
A
685
15.929
2.898
30.411
1.00
9.42


ATOM
1205
CA
HIS
A
685
14.740
3.447
29.757
1.00
7.57


ATOM
1206
CB
HIS
A
685
14.361
2.621
28.521
1.00
14.86


ATOM
1207
CG
HIS
A
685
15.472
2.468
27.521
1.00
7.24


ATOM
1208
CD2
HIS
A
685
15.846
1.402
26.773
1.00
9.32


ATOM
1209
ND1
HIS
A
685
16.299
3.506
27.161
1.00
8.86


ATOM
1210
CE1
HIS
A
685
17.141
3.088
26.227
1.00
14.03


ATOM
1211
NE2
HIS
A
685
16.886
1.819
25.974
1.00
8.62


ATOM
1212
C
HIS
A
685
13.574
3.446
30.747
1.00
9.27


ATOM
1213
O
HIS
A
685
12.798
4.401
30.805
1.00
9.78


ATOM
1214
N
PHE
A
686
13.439
2.376
31.523
1.00
8.10


ATOM
1215
CA
PHE
A
686
12.351
2.314
32.507
1.00
10.05


ATOM
1216
CB
PHE
A
686
12.291
0.923
33.151
1.00
8.82


ATOM
1217
CG
PHE
A
686
11.281
0.808
34.263
1.00
10.55


ATOM
1218
CD1
PHE
A
686
9.937
1.078
34.035
1.00
10.53


ATOM
1219
CD2
PHE
A
686
11.674
0.442
35.538
1.00
11.42


ATOM
1220
CE1
PHE
A
686
9.013
0.985
35.061
1.00
14.12


ATOM
1221
CE2
PHE
A
686
10.754
0.348
36.568
1.00
15.20


ATOM
1222
CZ
PHE
A
686
9.423
0.618
36.328
1.00
13.66


ATOM
1223
C
PHE
A
686
12.554
3.391
33.570
1.00
9.59


ATOM
1224
O
PHE
A
686
11.599
4.036
34.022
1.00
11.10


ATOM
1225
N
ASP
A
687
13.807
3.603
33.965
1.00
10.38


ATOM
1226
CA
ASP
A
687
14.169
4.620
34.950
1.00
13.63


ATOM
1227
CB
ASP
A
687
15.699
4.646
35.147
1.00
15.63


ATOM
1228
CG
ASP
A
687
16.163
5.810
36.032
1.00
35.43


ATOM
1229
OD1
ASP
A
687
15.842
5.812
37.238
1.00
39.21


ATOM
1230
OD2
ASP
A
687
16.855
6.721
35.514
1.00
46.67


ATOM
1231
C
ASP
A
687
13.701
5.983
34.453
1.00
11.19


ATOM
1232
O
ASP
A
687
13.079
6.742
35.191
1.00
12.63


ATOM
1233
N
GLN
A
688
14.026
6.266
33.194
1.00
10.97


ATOM
1234
CA
GLN
A
688
13.664
7.531
32.571
1.00
10.87


ATOM
1235
CB
GLN
A
688
14.331
7.623
31.193
1.00
15.23


ATOM
1236
CG
GLN
A
688
15.844
7.876
31.260
1.00
11.96


ATOM
1237
CD
GLN
A
688
16.179
9.350
31.456
1.00
14.39


ATOM
1238
OE1
GLN
A
688
15.805
10.193
30.640
1.00
20.66


ATOM
1239
NE2
GLN
A
688
16.881
9.663
32.535
1.00
29.50


ATOM
1240
C
GLN
A
688
12.158
7.651
32.455
1.00
10.36


ATOM
1241
O
GLN
A
688
11.587
8.729
32.641
1.00
10.53


ATOM
1242
N
CYS
A
689
11.495
6.536
32.160
1.00
8.48


ATOM
1243
CA
CYS
A
689
10.043
6.517
32.040
1.00
9.59


ATOM
1244
CB
CYS
A
689
9.558
5.097
31.706
1.00
11.54


ATOM
1245
SG
CYS
A
689
7.772
4.940
31.573
1.00
11.98


ATOM
1246
C
CYS
A
689
9.406
7.005
33.343
1.00
10.54


ATOM
1247
O
CYS
A
689
8.559
7.905
33.331
1.00
10.86


ATOM
1248
N
LEU
A
690
9.822
6.417
34.463
1.00
12.43


ATOM
1249
CA
LEU
A
690
9.316
6.786
35.787
1.00
13.70


ATOM
1250
CB
LEU
A
690
9.968
5.912
36.863
1.00
15.35


ATOM
1251
CG
LEU
A
690
9.620
4.423
36.853
1.00
18.35


ATOM
1252
CD1
LEU
A
690
10.326
3.723
38.008
1.00
25.25


ATOM
1253
CD2
LEU
A
690
8.118
4.248
36.969
1.00
17.06


ATOM
1254
C
LEU
A
690
9.605
8.247
36.093
1.00
14.05


ATOM
1255
O
LEU
A
690
8.767
8.975
36.633
1.00
15.63


ATOM
1256
N
MET
A
691
10.817
8.681
35.750
1.00
13.87


ATOM
1257
CA
MET
A
691
11.256
10.042
35.975
1.00
14.41


ATOM
1258
CB
MET
A
691
12.676
10.212
35.411
1.00
14.62


ATOM
1259
CG
MET
A
691
13.371
11.496
35.757
1.00
32.36


ATOM
1260
SD
MET
A
691
12.902
12.755
34.635
1.00
45.55


ATOM
1261
CE
MET
A
691
13.918
12.471
33.200
1.00
37.72


ATOM
1262
C
MET
A
691
10.285
11.024
35.336
1.00
13.72


ATOM
1263
O
MET
A
691
9.863
11.990
35.971
1.00
14.45


ATOM
1264
N
ILE
A
692
9.903
10.758
34.091
1.00
10.48


ATOM
1265
CA
ILE
A
692
8.980
11.644
33.400
1.00
9.98


ATOM
1266
CB
ILE
A
692
8.966
11.371
31.895
1.00
10.00


ATOM
1267
CG2
ILE
A
692
7.909
12.240
31.224
1.00
12.51


ATOM
1268
CG1
ILE
A
692
10.346
11.691
31.315
1.00
14.40


ATOM
1269
CD1
ILE
A
692
10.482
11.400
29.841
1.00
19.81


ATOM
1270
C
ILE
A
692
7.578
11.534
33.973
1.00
10.09


ATOM
1271
O
ILE
A
692
6.906
12.547
34.166
1.00
11.41


ATOM
1272
N
LEU
A
693
7.149
10.316
34.288
1.00
12.13


ATOM
1273
CA
LEU
A
693
5.821
10.111
34.862
1.00
13.85


ATOM
1274
CB
LEU
A
693
5.548
8.615
35.058
1.00
13.96


ATOM
1275
CG
LEU
A
693
5.212
7.826
33.789
1.00
10.33


ATOM
1276
CD1
LEU
A
693
5.183
6.335
34.082
1.00
17.28


ATOM
1277
CD2
LEU
A
693
3.868
8.305
33.243
1.00
9.40


ATOM
1278
C
LEU
A
693
5.644
10.837
36.193
1.00
14.19


ATOM
1279
O
LEU
A
693
4.524
11.179
36.577
1.00
16.64


ATOM
1280
N
ASN
A
694
6.747
11.073
36.893
1.00
16.46


ATOM
1281
CA
ASN
A
694
6.697
11.755
38.183
1.00
16.63


ATOM
1282
CB
ASN
A
694
7.686
11.116
39.159
1.00
20.12


ATOM
1283
CG
ASN
A
694
7.231
9.760
39.641
1.00
24.99


ATOM
1284
OD1
ASN
A
694
7.869
8.742
39.373
1.00
30.33


ATOM
1285
ND2
ASN
A
694
6.115
9.736
40.360
1.00
25.93


ATOM
1286
C
ASN
A
694
6.989
13.247
38.101
1.00
18.31


ATOM
1287
O
ASN
A
694
6.855
13.958
39.093
1.00
18.26


ATOM
1288
N
SER
A
695
7.395
13.721
36.930
1.00
16.05


ATOM
1289
CA
SER
A
695
7.704
15.139
36.755
1.00
17.70


ATOM
1290
CB
SER
A
695
8.321
15.376
35.376
1.00
19.30


ATOM
1291
OG
SER
A
695
9.607
14.793
35.298
1.00
34.04


ATOM
1292
C
SER
A
695
6.471
16.022
36.914
1.00
15.83


ATOM
1293
O
SER
A
695
5.400
15.710
36.406
1.00
17.46


ATOM
1294
N
PRO
A
696
6.611
17.144
37.630
1.00
18.97


ATOM
1295
CD
PRO
A
696
7.779
17.577
38.415
1.00
26.97


ATOM
1296
CA
PRO
A
696
5.480
18.053
37.830
1.00
18.99


ATOM
1297
CB
PRO
A
696
6.113
19.220
38.579
1.00
22.14


ATOM
1298
CG
PRO
A
696
7.154
18.534
39.414
1.00
28.71


ATOM
1299
C
PRO
A
696
4.866
18.480
36.498
1.00
16.02


ATOM
1300
O
PRO
A
696
5.585
18.839
35.564
1.00
18.08


ATOM
1301
N
GLY
A
697
3.539
18.425
36.418
1.00
16.17


ATOM
1302
CA
GLY
A
697
2.843
18.804
35.201
1.00
16.65


ATOM
1303
C
GLY
A
697
2.862
17.725
34.130
1.00
14.72


ATOM
1304
O
GLY
A
697
2.283
17.901
33.060
1.00
15.86


ATOM
1305
N
ASN
A
698
3.511
16.601
34.424
1.00
14.68


ATOM
1306
CA
ASN
A
698
3.621
15.493
33.471
1.00
14.66


ATOM
1307
CB
ASN
A
698
5.099
15.209
33.174
1.00
15.25


ATOM
1308
CG
ASN
A
698
5.760
16.304
32.365
1.00
19.94


ATOM
1309
OD1
ASN
A
698
5.883
16.199
31.146
1.00
13.89


ATOM
1310
ND2
ASN
A
698
6.186
17.367
33.039
1.00
16.33


ATOM
1311
C
ASN
A
698
2.990
14.198
33.973
1.00
14.82


ATOM
1312
O
ASN
A
698
3.044
13.174
33.293
1.00
13.20


ATOM
1313
N
GLN
A
699
2.379
14.243
35.151
1.00
13.46


ATOM
1314
CA
GLN
A
699
1.807
13.041
35.749
1.00
14.53


ATOM
1315
CB
GLN
A
699
1.652
13.281
37.251
1.00
16.25


ATOM
1316
CG
GLN
A
699
2.957
13.713
37.902
1.00
17.08


ATOM
1317
CD
GLN
A
699
2.787
14.103
39.350
1.00
37.15


ATOM
1318
OE1
GLN
A
699
2.147
15.105
39.661
1.00
41.13


ATOM
1319
NE2
GLN
A
699
3.357
13.307
40.248
1.00
41.91


ATOM
1320
C
GLN
A
699
0.499
12.522
35.158
1.00
13.96


ATOM
1321
O
GLN
A
699
−0.567
12.676
35.754
1.00
15.67


ATOM
1322
N
ILE
A
700
0.582
11.867
34.003
1.00
13.44


ATOM
1323
CA
ILE
A
700
−0.617
11.348
33.356
1.00
14.25


ATOM
1324
CB
ILE
A
700
−0.345
10.974
31.881
1.00
15.57


ATOM
1325
CG2
ILE
A
700
0.010
12.222
31.086
1.00
15.78


ATOM
1326
CG1
ILE
A
700
0.777
9.941
31.793
1.00
16.74


ATOM
1327
CD1
ILE
A
700
0.940
9.361
30.407
1.00
12.98


ATOM
1328
C
ILE
A
700
−1.262
10.151
34.064
1.00
13.88


ATOM
1329
O
ILE
A
700
−2.342
9.709
33.673
1.00
14.53


ATOM
1330
N
LEU
A
701
−0.609
9.624
35.098
1.00
11.60


ATOM
1331
CA
LEU
A
701
−1.169
8.495
35.845
1.00
14.58


ATOM
1332
CB
LEU
A
701
−0.150
7.358
35.965
1.00
13.85


ATOM
1333
CG
LEU
A
701
0.310
6.673
34.677
1.00
11.07


ATOM
1334
CD1
LEU
A
701
1.270
5.539
35.031
1.00
13.34


ATOM
1335
CD2
LEU
A
701
−0.895
6.128
33.921
1.00
12.89


ATOM
1336
C
LEU
A
701
−1.612
8.914
37.247
1.00
13.75


ATOM
1337
O
LEU
A
701
−2.053
8.084
38.040
1.00
15.74


ATOM
1338
N
SER
A
702
−1.497
10.201
37.547
1.00
15.74


ATOM
1339
CA
SER
A
702
−1.872
10.717
38.860
1.00
18.36


ATOM
1340
CB
SER
A
702
−1.573
12.217
38.949
1.00
20.19


ATOM
1341
OG
SER
A
702
−2.446
12.958
38.113
1.00
21.94


ATOM
1342
C
SER
A
702
−3.347
10.490
39.176
1.00
19.34


ATOM
1343
O
SER
A
702
−3.754
10.559
40.336
1.00
20.75


ATOM
1344
N
GLY
A
703
−4.144
10.224
38.148
1.00
18.92


ATOM
1345
CA
GLY
A
703
−5.565
10.012
38.359
1.00
20.40


ATOM
1346
C
GLY
A
703
−5.944
8.600
38.764
1.00
21.19


ATOM
1347
O
GLY
A
703
−7.036
8.369
39.284
1.00
20.43


ATOM
1348
N
LEU
A
704
−5.045
7.649
38.539
1.00
16.00


ATOM
1349
CA
LEU
A
704
−5.326
6.259
38.876
1.00
15.59


ATOM
1350
CB
LEU
A
704
−4.262
5.335
38.278
1.00
9.29


ATOM
1351
CG
LEU
A
704
−4.459
4.921
36.823
1.00
14.10


ATOM
1352
CD1
LEU
A
704
−4.510
6.143
35.926
1.00
17.73


ATOM
1353
CD2
LEU
A
704
−3.312
3.998
36.418
1.00
11.19


ATOM
1354
C
LEU
A
704
−5.419
5.993
40.368
1.00
16.40


ATOM
1355
O
LEU
A
704
−4.773
6.659
41.178
1.00
16.88


ATOM
1356
N
SER
A
705
−6.233
5.004
40.721
1.00
15.43


ATOM
1357
CA
SER
A
705
−6.395
4.621
42.111
1.00
15.96


ATOM
1358
CB
SER
A
705
−7.556
3.640
42.268
1.00
15.57


ATOM
1359
OG
SER
A
705
−7.242
2.402
41.658
1.00
15.44


ATOM
1360
C
SER
A
705
−5.092
3.947
42.515
1.00
16.32


ATOM
1361
O
SER
A
705
−4.280
3.583
41.662
1.00
17.25


ATOM
1362
N
ILE
A
706
−4.886
3.782
43.812
1.00
17.56


ATOM
1363
CA
ILE
A
706
−3.666
3.164
44.292
1.00
16.88


ATOM
1364
CB
ILE
A
706
−3.679
3.086
45.836
1.00
21.33


ATOM
1365
CG2
ILE
A
706
−2.466
2.331
46.335
1.00
23.53


ATOM
1366
CG1
ILE
A
706
−3.712
4.507
46.411
1.00
21.96


ATOM
1367
CD1
ILE
A
706
−3.892
4.577
47.918
1.00
22.24


ATOM
1368
C
ILE
A
706
−3.415
1.782
43.685
1.00
16.48


ATOM
1369
O
ILE
A
706
−2.291
1.470
43.291
1.00
18.62


ATOM
1370
N
GLU
A
707
−4.456
0.962
43.584
1.00
15.92


ATOM
1371
CA
GLU
A
707
−4.304
−0.376
43.019
1.00
14.53


ATOM
1372
CB
GLU
A
707
−5.509
−1.250
43.378
1.00
19.33


ATOM
1373
CG
GLU
A
707
−5.518
−1.682
44.836
1.00
24.82


ATOM
1374
CD
GLU
A
707
−4.269
−2.460
45.214
1.00
31.26


ATOM
1375
OE1
GLU
A
707
−4.029
−3.525
44.610
1.00
34.47


ATOM
1376
OE2
GLU
A
707
−3.525
−2.006
46.110
1.00
30.79


ATOM
1377
C
GLU
A
707
−4.093
−0.385
41.507
1.00
14.27


ATOM
1378
O
GLU
A
707
−3.283
−1.156
41.002
1.00
15.02


ATOM
1379
N
GLU
A
708
−4.818
0.458
40.782
1.00
11.81


ATOM
1380
CA
GLU
A
708
−4.644
0.495
39.337
1.00
12.49


ATOM
1381
CB
GLU
A
708
−5.756
1.317
38.673
1.00
14.73


ATOM
1382
CG
GLU
A
708
−7.134
0.663
38.813
1.00
11.98


ATOM
1383
CD
GLU
A
708
−8.088
1.020
37.683
1.00
18.01


ATOM
1384
OE1
GLU
A
708
−8.121
2.196
37.274
1.00
19.76


ATOM
1385
OE2
GLU
A
708
−8.816
0.120
37.216
1.00
22.22


ATOM
1386
C
GLU
A
708
−3.264
1.054
38.996
1.00
14.00


ATOM
1387
O
GLU
A
708
−2.624
0.607
38.047
1.00
12.79


ATOM
1388
N
TYR
A
709
−2.798
2.018
39.784
1.00
12.70


ATOM
1389
CA
TYR
A
709
−1.482
2.604
39.551
1.00
13.42


ATOM
1390
CB
TYR
A
709
−1.204
3.724
40.557
1.00
12.05


ATOM
1391
CG
TYR
A
709
0.129
4.407
40.339
1.00
19.13


ATOM
1392
CD1
TYR
A
709
0.311
5.302
39.296
1.00
14.81


ATOM
1393
CE1
TYR
A
709
1.530
5.928
39.091
1.00
15.81


ATOM
1394
CD2
TYR
A
709
1.207
4.149
41.174
1.00
17.39


ATOM
1395
CE2
TYR
A
709
2.427
4.767
40.978
1.00
18.97


ATOM
1396
CZ
TYR
A
709
2.583
5.658
39.934
1.00
17.67


ATOM
1397
OH
TYR
A
709
3.793
6.284
39.737
1.00
18.77


ATOM
1398
C
TYR
A
709
−0.424
1.515
39.708
1.00
15.44


ATOM
1399
O
TYR
A
709
0.452
1.348
38.855
1.00
15.06


ATOM
1400
N
LYS
A
710
−0.520
0.774
40.808
1.00
15.25


ATOM
1401
CA
LYS
A
710
0.409
−0.311
41.095
1.00
15.31


ATOM
1402
CB
LYS
A
710
−0.020
−1.026
42.379
1.00
22.10


ATOM
1403
CG
LYS
A
710
0.809
−2.249
42.716
1.00
23.74


ATOM
1404
CD
LYS
A
710
0.299
−2.931
43.978
1.00
33.24


ATOM
1405
CE
LYS
A
710
0.996
−4.263
44.204
1.00
39.08


ATOM
1406
NZ
LYS
A
710
2.478
−4.117
44.248
1.00
42.37


ATOM
1407
C
LYS
A
710
0.474
−1.309
39.939
1.00
14.94


ATOM
1408
O
LYS
A
710
1.555
−1.645
39.448
1.00
12.87


ATOM
1409
N
THR
A
711
−0.692
−1.777
39.506
1.00
13.50


ATOM
1410
CA
THR
A
711
−0.783
−2.736
38.411
1.00
12.45


ATOM
1411
CB
THR
A
711
−2.249
−3.092
38.128
1.00
17.44


ATOM
1412
OG1
THR
A
711
−2.791
−3.792
39.255
1.00
21.96


ATOM
1413
CG2
THR
A
711
−2.365
−3.953
36.872
1.00
16.75


ATOM
1414
C
THR
A
711
−0.161
−2.198
37.129
1.00
11.72


ATOM
1415
O
THR
A
711
0.597
−2.896
36.442
1.00
13.19


ATOM
1416
N
THR
A
712
−0.487
−0.954
36.809
1.00
11.15


ATOM
1417
CA
THR
A
712
0.015
−0.319
35.599
1.00
13.99


ATOM
1418
CB
THR
A
712
−0.598
1.081
35.424
1.00
9.97


ATOM
1419
OG1
THR
A
712
−2.029
0.967
35.357
1.00
14.40


ATOM
1420
CG2
THR
A
712
−0.088
1.729
34.133
1.00
12.92


ATOM
1421
C
THR
A
712
1.541
−0.221
35.556
1.00
12.77


ATOM
1422
O
THR
A
712
2.158
−0.596
34.559
1.00
12.54


ATOM
1423
N
LEU
A
713
2.156
0.275
36.625
1.00
12.50


ATOM
1424
CA
LEU
A
713
3.612
0.384
36.638
1.00
11.02


ATOM
1425
CB
LEU
A
713
4.105
1.023
37.940
1.00
13.58


ATOM
1426
CG
LEU
A
713
3.889
2.528
38.100
1.00
22.03


ATOM
1427
CD1
LEU
A
713
4.754
3.042
39.250
1.00
21.64


ATOM
1428
CD2
LEU
A
713
4.261
3.241
36.809
1.00
27.88


ATOM
1429
C
LEU
A
713
4.298
−0.967
36.438
1.00
13.04


ATOM
1430
O
LEU
A
713
5.340
−1.048
35.785
1.00
12.26


ATOM
1431
N
LYS
A
714
3.718
−2.026
36.995
1.00
11.66


ATOM
1432
CA
LYS
A
714
4.304
−3.356
36.852
1.00
12.24


ATOM
1433
CB
LYS
A
714
3.540
−4.383
37.690
1.00
17.46


ATOM
1434
CG
LYS
A
714
3.582
−4.123
39.182
1.00
27.51


ATOM
1435
CD
LYS
A
714
2.878
−5.236
39.939
1.00
33.99


ATOM
1436
CE
LYS
A
714
2.899
−4.988
41.433
1.00
42.93


ATOM
1437
NZ
LYS
A
714
2.222
−6.092
42.168
1.00
46.33


ATOM
1438
C
LYS
A
714
4.284
−3.784
35.390
1.00
12.70


ATOM
1439
O
LYS
A
714
5.259
−4.338
34.886
1.00
12.91


ATOM
1440
N
ILE
A
715
3.168
−3.525
34.717
1.00
10.95


ATOM
1441
CA
ILE
A
715
3.023
−3.869
33.308
1.00
10.57


ATOM
1442
CB
ILE
A
715
1.586
−3.590
32.820
1.00
11.39


ATOM
1443
CG2
ILE
A
715
1.468
−3.896
31.339
1.00
11.35


ATOM
1444
CG1
ILE
A
715
0.596
−4.450
33.613
1.00
12.69


ATOM
1445
CD1
ILE
A
715
−0.854
−4.130
33.332
1.00
13.44


ATOM
1446
C
ILE
A
715
4.017
−3.052
32.482
1.00
10.34


ATOM
1447
O
ILE
A
715
4.676
−3.581
31.588
1.00
11.86


ATOM
1448
N
ILE
A
716
4.133
−1.762
32.793
1.00
10.78


ATOM
1449
CA
ILE
A
716
5.069
−0.886
32.081
1.00
9.90


ATOM
1450
CB
ILE
A
716
4.989
0.563
32.621
1.00
10.08


ATOM
1451
CG2
ILE
A
716
6.171
1.387
32.115
1.00
10.86


ATOM
1452
CG1
ILE
A
716
3.661
1.197
32.189
1.00
10.91


ATOM
1453
CD1
ILE
A
716
3.413
2.564
32.792
1.00
11.27


ATOM
1454
C
ILE
A
716
6.508
−1.393
32.196
1.00
8.77


ATOM
1455
O
ILE
A
716
7.229
−1.487
31.199
1.00
9.34


ATOM
1456
N
LYS
A
717
6.926
−1.724
33.413
1.00
9.18


ATOM
1457
CA
LYS
A
717
8.275
−2.235
33.623
1.00
10.88


ATOM
1458
CB
LYS
A
717
8.489
−2.606
35.087
1.00
12.47


ATOM
1459
CG
LYS
A
717
9.790
−3.366
35.337
1.00
14.78


ATOM
1460
CD
LYS
A
717
9.865
−3.864
36.775
1.00
17.70


ATOM
1461
CE
LYS
A
717
11.045
−4.809
36.977
1.00
29.85


ATOM
1462
NZ
LYS
A
717
11.082
−5.374
38.355
1.00
25.71


ATOM
1463
C
LYS
A
717
8.540
−3.469
32.752
1.00
10.54


ATOM
1464
O
LYS
A
717
9.536
−3.524
32.041
1.00
10.05


ATOM
1465
N
GLN
A
718
7.647
−4.451
32.847
1.00
11.40


ATOM
1466
CA
GLN
A
718
7.774
−5.682
32.067
1.00
11.80


ATOM
1467
CB
GLN
A
718
6.635
−6.628
32.434
1.00
11.33


ATOM
1468
CG
GLN
A
718
6.683
−6.965
33.899
1.00
14.75


ATOM
1469
CD
GLN
A
718
7.954
−7.691
34.293
1.00
35.80


ATOM
1470
OE1
GLN
A
718
8.774
−7.176
35.053
1.00
49.66


ATOM
1471
NE2
GLN
A
718
8.115
−8.909
33.784
1.00
43.62


ATOM
1472
C
GLN
A
718
7.778
−5.422
30.559
1.00
9.82


ATOM
1473
O
GLN
A
718
8.559
−6.027
29.831
1.00
9.86


ATOM
1474
N
ALA
A
719
6.920
−4.518
30.108
1.00
8.83


ATOM
1475
CA
ALA
A
719
6.842
−4.205
28.686
1.00
10.49


ATOM
1476
CB
ALA
A
719
5.657
−3.292
28.436
1.00
5.96


ATOM
1477
C
ALA
A
719
8.129
−3.560
28.186
1.00
9.98


ATOM
1478
O
ALA
A
719
8.618
−3.892
27.101
1.00
9.19


ATOM
1479
N
ILE
A
720
8.688
−2.641
28.971
1.00
7.25


ATOM
1480
CA
ILE
A
720
9.920
−1.988
28.548
1.00
8.66


ATOM
1481
CB
ILE
A
720
10.233
−0.753
29.426
1.00
10.86


ATOM
1482
CG2
ILE
A
720
11.616
−0.193
29.086
1.00
11.64


ATOM
1483
CG1
ILE
A
720
9.164
0.320
29.181
1.00
11.59


ATOM
1484
CD1
ILE
A
720
9.367
1.605
29.976
1.00
12.21


ATOM
1485
C
ILE
A
720
11.085
−2.974
28.580
1.00
10.02


ATOM
1486
O
ILE
A
720
11.883
−3.040
27.641
1.00
8.95


ATOM
1487
N
LEU
A
721
11.178
−3.762
29.643
1.00
8.10


ATOM
1488
CA
LEU
A
721
12.264
−4.733
29.719
1.00
8.45


ATOM
1489
CB
LEU
A
721
12.251
−5.446
31.077
1.00
10.55


ATOM
1490
CG
LEU
A
721
12.613
−4.553
32.267
1.00
13.26


ATOM
1491
CD1
LEU
A
721
12.539
−5.350
33.574
1.00
15.78


ATOM
1492
CD2
LEU
A
721
14.006
−3.991
32.059
1.00
24.08


ATOM
1493
C
LEU
A
721
12.173
−5.750
28.576
1.00
9.96


ATOM
1494
O
LEU
A
721
13.195
−6.196
28.049
1.00
8.91


ATOM
1495
N
ALA
A
722
10.948
−6.082
28.175
1.00
8.77


ATOM
1496
CA
ALA
A
722
10.715
−7.047
27.100
1.00
8.74


ATOM
1497
CB
ALA
A
722
9.219
−7.218
26.879
1.00
9.06


ATOM
1498
C
ALA
A
722
11.383
−6.648
25.786
1.00
10.10


ATOM
1499
O
ALA
A
722
11.704
−7.507
24.965
1.00
13.26


ATOM
1500
N
THR
A
723
11.598
−5.350
25.585
1.00
8.97


ATOM
1501
CA
THR
A
723
12.213
−4.884
24.344
1.00
10.94


ATOM
1502
CB
THR
A
723
11.943
−3.374
24.127
1.00
8.53


ATOM
1503
OG1
THR
A
723
12.542
−2.615
25.181
1.00
8.41


ATOM
1504
CG2
THR
A
723
10.437
−3.114
24.118
1.00
8.22


ATOM
1505
C
THR
A
723
13.713
−5.187
24.203
1.00
9.21


ATOM
1506
O
THR
A
723
14.327
−4.862
23.186
1.00
12.03


ATOM
1507
N
ASP
A
724
14.308
−5.797
25.223
1.00
9.75


ATOM
1508
CA
ASP
A
724
15.710
−6.203
25.133
1.00
7.82


ATOM
1509
CB
ASP
A
724
16.257
−6.533
26.525
1.00
12.18


ATOM
1510
CG
ASP
A
724
17.648
−7.147
26.490
1.00
8.16


ATOM
1511
OD1
ASP
A
724
18.232
−7.299
25.394
1.00
11.70


ATOM
1512
OD2
ASP
A
724
18.161
−7.481
27.581
1.00
11.61


ATOM
1513
C
ASP
A
724
15.600
−7.475
24.293
1.00
8.26


ATOM
1514
O
ASP
A
724
15.022
−8.459
24.742
1.00
10.28


ATOM
1515
N
LEU
A
725
16.127
−7.452
23.073
1.00
9.50


ATOM
1516
CA
LEU
A
725
16.037
−8.611
22.189
1.00
8.83


ATOM
1517
CB
LEU
A
725
16.791
−8.343
20.883
1.00
11.33


ATOM
1518
CG
LEU
A
725
16.365
−9.236
19.717
1.00
16.17


ATOM
1519
CD1
LEU
A
725
14.910
−8.953
19.367
1.00
12.02


ATOM
1520
CD2
LEU
A
725
17.262
−8.974
18.516
1.00
20.09


ATOM
1521
C
LEU
A
725
16.573
−9.880
22.849
1.00
12.30


ATOM
1522
O
LEU
A
725
16.179
−10.994
22.498
1.00
11.52


ATOM
1523
N
ALA
A
726
17.476
−9.712
23.806
1.00
11.08


ATOM
1524
CA
ALA
A
726
18.028
−10.855
24.517
1.00
12.63


ATOM
1525
CB
ALA
A
726
19.104
−10.394
25.489
1.00
21.41


ATOM
1526
C
ALA
A
726
16.918
−11.583
25.274
1.00
12.40


ATOM
1527
O
ALA
A
726
16.914
−12.813
25.354
1.00
13.56


ATOM
1528
N
LEU
A
727
15.985
−10.823
25.843
1.00
12.79


ATOM
1529
CA
LEU
A
727
14.884
−11.421
26.591
1.00
14.99


ATOM
1530
CB
LEU
A
727
14.206
−10.380
27.485
1.00
11.71


ATOM
1531
CG
LEU
A
727
15.096
−9.856
28.612
1.00
16.19


ATOM
1532
CD1
LEU
A
727
14.302
−8.925
29.511
1.00
13.74


ATOM
1533
CD2
LEU
A
727
15.631
−11.036
29.409
1.00
19.43


ATOM
1534
C
LEU
A
727
13.868
−12.045
25.646
1.00
15.02


ATOM
1535
O
LEU
A
727
13.173
−12.996
26.005
1.00
15.57


ATOM
1536
N
TYR
A
728
13.777
−11.500
24.438
1.00
12.38


ATOM
1537
CA
TYR
A
728
12.862
−12.038
23.435
1.00
12.71


ATOM
1538
CB
TYR
A
728
12.844
−11.136
22.194
1.00
10.64


ATOM
1539
CG
TYR
A
728
12.303
−11.823
20.960
1.00
12.57


ATOM
1540
CD1
TYR
A
728
10.966
−12.197
20.875
1.00
14.71


ATOM
1541
CE1
TYR
A
728
10.473
−12.854
19.752
1.00
12.42


ATOM
1542
CD2
TYR
A
728
13.139
−12.124
19.888
1.00
13.44


ATOM
1543
CE2
TYR
A
728
12.659
−12.777
18.763
1.00
13.13


ATOM
1544
CZ
TYR
A
728
11.329
−13.142
18.699
1.00
15.27


ATOM
1545
OH
TYR
A
728
10.857
−13.801
17.580
1.00
18.62


ATOM
1546
C
TYR
A
728
13.350
−13.430
23.041
1.00
12.62


ATOM
1547
O
TYR
A
728
12.588
−14.401
23.028
1.00
14.23


ATOM
1548
N
ILE
A
729
14.636
−13.522
22.723
1.00
12.98


ATOM
1549
CA
ILE
A
729
15.232
−14.788
22.327
1.00
13.19


ATOM
1550
CB
ILE
A
729
16.723
−14.595
21.983
1.00
14.56


ATOM
1551
CG2
ILE
A
729
17.395
−15.942
21.797
1.00
19.39


ATOM
1552
CG1
ILE
A
729
16.849
−13.727
20.727
1.00
18.02


ATOM
1553
CD1
ILE
A
729
18.268
−13.309
20.406
1.00
26.38


ATOM
1554
C
ILE
A
729
15.088
−15.826
23.439
1.00
15.70


ATOM
1555
O
ILE
A
729
14.830
−17.001
23.178
1.00
14.36


ATOM
1556
N
LYS
A
730
15.227
−15.375
24.681
1.00
15.21


ATOM
1557
CA
LYS
A
730
15.127
−16.257
25.837
1.00
16.44


ATOM
1558
CB
LYS
A
730
15.657
−15.528
27.075
1.00
21.43


ATOM
1559
CG
LYS
A
730
15.494
−16.291
28.376
1.00
27.38


ATOM
1560
CD
LYS
A
730
16.133
−15.528
29.523
1.00
31.22


ATOM
1561
CE
LYS
A
730
15.975
−16.267
30.839
1.00
36.43


ATOM
1562
NZ
LYS
A
730
16.672
−15.556
31.947
1.00
41.27


ATOM
1563
C
LYS
A
730
13.727
−16.802
26.133
1.00
16.48


ATOM
1564
O
LYS
A
730
13.573
−17.972
26.498
1.00
17.06


ATOM
1565
N
ARG
A
731
12.707
−15.969
25.968
1.00
14.55


ATOM
1566
CA
ARG
A
731
11.347
−16.395
26.283
1.00
15.57


ATOM
1567
CB
ARG
A
731
10.622
−15.291
27.060
1.00
19.59


ATOM
1568
CG
ARG
A
731
11.309
−14.842
28.335
1.00
18.25


ATOM
1569
CD
ARG
A
731
10.437
−13.846
29.086
1.00
33.93


ATOM
1570
NE
ARG
A
731
9.209
−14.462
29.588
1.00
32.78


ATOM
1571
CZ
ARG
A
731
8.168
−13.781
30.058
1.00
29.98


ATOM
1572
NH1
ARG
A
731
8.197
−12.456
30.091
1.00
30.21


ATOM
1573
NH2
ARG
A
731
7.097
−14.426
30.501
1.00
36.09


ATOM
1574
C
ARG
A
731
10.461
−16.807
25.118
1.00
12.75


ATOM
1575
O
ARG
A
731
9.436
−17.454
25.325
1.00
15.30


ATOM
1576
N
ARG
A
732
10.841
−16.445
23.897
1.00
13.21


ATOM
1577
CA
ARG
A
732
10.002
−16.759
22.751
1.00
11.06


ATOM
1578
CB
ARG
A
732
10.589
−16.162
21.474
1.00
10.97


ATOM
1579
CG
ARG
A
732
11.872
−16.812
21.021
1.00
12.09


ATOM
1580
CD
ARG
A
732
12.325
−16.192
19.724
1.00
12.79


ATOM
1581
NE
ARG
A
732
13.525
−16.822
19.193
1.00
13.80


ATOM
1582
CZ
ARG
A
732
13.919
−16.704
17.930
1.00
20.20


ATOM
1583
NH1
ARG
A
732
13.201
−15.980
17.077
1.00
23.11


ATOM
1584
NH2
ARG
A
732
15.025
−17.307
17.518
1.00
22.17


ATOM
1585
C
ARG
A
732
9.751
−18.245
22.549
1.00
11.37


ATOM
1586
O
ARG
A
732
8.704
−18.625
22.031
1.00
11.95


ATOM
1587
N
GLY
A
733
10.703
−19.078
22.962
1.00
13.25


ATOM
1588
CA
GLY
A
733
10.543
−20.512
22.804
1.00
13.40


ATOM
1589
C
GLY
A
733
9.298
−21.009
23.508
1.00
14.10


ATOM
1590
O
GLY
A
733
8.543
−21.823
22.970
1.00
15.18


ATOM
1591
N
GLU
A
734
9.080
−20.512
24.719
1.00
11.89


ATOM
1592
CA
GLU
A
734
7.919
−20.900
25.505
1.00
14.43


ATOM
1593
CB
GLU
A
734
7.988
−20.264
26.895
1.00
14.05


ATOM
1594
CG
GLU
A
734
6.675
−20.312
27.661
1.00
18.08


ATOM
1595
CD
GLU
A
734
6.810
−19.828
29.091
1.00
21.97


ATOM
1596
OE1
GLU
A
734
7.742
−19.048
29.372
1.00
19.31


ATOM
1597
OE2
GLU
A
734
5.977
−20.221
29.932
1.00
32.96


ATOM
1598
C
GLU
A
734
6.632
−20.478
24.806
1.00
14.65


ATOM
1599
O
GLU
A
734
5.663
−21.235
24.760
1.00
14.67


ATOM
1600
N
PHE
A
735
6.631
−19.264
24.267
1.00
15.01


ATOM
1601
CA
PHE
A
735
5.470
−18.729
23.566
1.00
11.90


ATOM
1602
CB
PHE
A
735
5.743
−17.278
23.157
1.00
11.17


ATOM
1603
CG
PHE
A
735
4.632
−16.635
22.366
1.00
16.06


ATOM
1604
CD1
PHE
A
735
3.354
−16.515
22.892
1.00
16.32


ATOM
1605
CD2
PHE
A
735
4.885
−16.102
21.111
1.00
13.68


ATOM
1606
CE1
PHE
A
735
2.355
−15.869
22.178
1.00
13.80


ATOM
1607
CE2
PHE
A
735
3.897
−15.458
20.400
1.00
12.16


ATOM
1608
CZ
PHE
A
735
2.631
−15.340
20.931
1.00
14.03


ATOM
1609
C
PHE
A
735
5.142
−19.566
22.329
1.00
13.78


ATOM
1610
O
PHE
A
735
3.989
−19.946
22.117
1.00
13.01


ATOM
1611
N
PHE
A
736
6.156
−19.853
21.517
1.00
12.56


ATOM
1612
CA
PHE
A
736
5.952
−20.632
20.299
1.00
14.09


ATOM
1613
CB
PHE
A
736
7.242
−20.691
19.472
1.00
15.66


ATOM
1614
CG
PHE
A
736
7.752
−19.342
19.031
1.00
17.77


ATOM
1615
CD1
PHE
A
736
6.888
−18.268
18.894
1.00
16.30


ATOM
1616
CD2
PHE
A
736
9.092
−19.166
18.701
1.00
14.18


ATOM
1617
CE1
PHE
A
736
7.345
−17.040
18.435
1.00
13.31


ATOM
1618
CE2
PHE
A
736
9.558
−17.939
18.242
1.00
13.12


ATOM
1619
CZ
PHE
A
736
8.686
−16.877
18.106
1.00
17.60


ATOM
1620
C
PHE
A
736
5.483
−22.054
20.598
1.00
14.02


ATOM
1621
O
PHE
A
736
4.653
−22.608
19.874
1.00
15.27


ATOM
1622
N
GLU
A
737
6.022
−22.640
21.661
1.00
15.53


ATOM
1623
CA
GLU
A
737
5.667
−24.000
22.047
1.00
16.49


ATOM
1624
CB
GLU
A
737
6.598
−24.493
23.155
1.00
18.16


ATOM
1625
CG
GLU
A
737
6.296
−25.908
23.623
1.00
32.20


ATOM
1626
CD
GLU
A
737
7.266
−26.397
24.685
1.00
44.41


ATOM
1627
OE1
GLU
A
737
7.368
−25.748
25.748
1.00
43.95


ATOM
1628
OE2
GLU
A
737
7.926
−27.433
24.457
1.00
45.00


ATOM
1629
C
GLU
A
737
4.219
−24.105
22.505
1.00
16.86


ATOM
1630
O
GLU
A
737
3.517
−25.050
22.137
1.00
18.64


ATOM
1631
N
LEU
A
738
3.774
−23.144
23.308
1.00
15.93


ATOM
1632
CA
LEU
A
738
2.396
−23.140
23.791
1.00
14.96


ATOM
1633
CB
LEU
A
738
2.137
−21.910
24.665
1.00
13.51


ATOM
1634
CG
LEU
A
738
2.817
−21.890
26.037
1.00
13.44


ATOM
1635
CD1
LEU
A
738
2.813
−20.474
26.589
1.00
14.08


ATOM
1636
CD2
LEU
A
738
2.103
−22.844
26.987
1.00
21.77


ATOM
1637
C
LEU
A
738
1.435
−23.137
22.610
1.00
15.65


ATOM
1638
O
LEU
A
738
0.431
−23.854
22.610
1.00
17.64


ATOM
1639
N
ILE
A
739
1.743
−22.323
21.604
1.00
13.75


ATOM
1640
CA
ILE
A
739
0.904
−22.236
20.415
1.00
14.28


ATOM
1641
CB
ILE
A
739
1.388
−21.112
19.464
1.00
12.79


ATOM
1642
CG2
ILE
A
739
0.686
−21.224
18.118
1.00
23.84


ATOM
1643
CG1
ILE
A
739
1.122
−19.744
20.096
1.00
16.58


ATOM
1644
CD1
ILE
A
739
1.656
−18.576
19.279
1.00
13.81


ATOM
1645
C
ILE
A
739
0.925
−23.557
19.654
1.00
16.17


ATOM
1646
O
ILE
A
739
−0.126
−24.107
19.309
1.00
18.24


ATOM
1647
N
ARG
A
740
2.124
−24.075
19.410
1.00
15.35


ATOM
1648
CA
ARG
A
740
2.274
−25.322
18.671
1.00
18.48


ATOM
1649
CB
ARG
A
740
3.758
−25.648
18.474
1.00
23.15


ATOM
1650
CG
ARG
A
740
3.996
−26.804
17.508
1.00
35.46


ATOM
1651
CD
ARG
A
740
5.475
−27.059
17.224
1.00
39.66


ATOM
1652
NE
ARG
A
740
6.174
−27.694
18.340
1.00
40.53


ATOM
1653
CZ
ARG
A
740
6.703
−27.043
19.371
1.00
42.20


ATOM
1654
NH1
ARG
A
740
6.623
−25.721
19.441
1.00
52.88


ATOM
1655
NH2
ARG
A
740
7.317
−27.718
20.335
1.00
44.19


ATOM
1656
C
ARG
A
740
1.582
−26.495
19.360
1.00
19.41


ATOM
1657
O
ARG
A
740
1.093
−27.410
18.698
1.00
18.06


ATOM
1658
N
LYS
A
741
1.539
−26.470
20.686
1.00
18.03


ATOM
1659
CA
LYS
A
741
0.906
−27.553
21.430
1.00
18.11


ATOM
1660
CB
LYS
A
741
1.696
−27.853
22.699
1.00
14.50


ATOM
1661
CG
LYS
A
741
3.074
−28.426
22.451
1.00
21.67


ATOM
1662
CD
LYS
A
741
3.717
−28.812
23.763
1.00
23.36


ATOM
1663
CE
LYS
A
741
5.087
−29.430
23.558
1.00
27.38


ATOM
1664
NZ
LYS
A
741
5.715
−29.747
24.871
1.00
23.91


ATOM
1665
C
LYS
A
741
−0.540
−27.248
21.798
1.00
17.80


ATOM
1666
O
LYS
A
741
−1.134
−27.940
22.623
1.00
18.63


ATOM
1667
N
ASN
A
742
−1.102
−26.214
21.183
1.00
17.40


ATOM
1668
CA
ASN
A
742
−2.478
−25.822
21.456
1.00
17.84


ATOM
1669
CB
ASN
A
742
−3.443
−26.841
20.849
1.00
16.88


ATOM
1670
CG
ASN
A
742
−3.442
−26.801
19.335
1.00
15.02


ATOM
1671
OD1
ASN
A
742
−3.741
−25.772
18.733
1.00
28.97


ATOM
1672
ND2
ASN
A
742
−3.100
−27.923
18.709
1.00
20.44


ATOM
1673
C
ASN
A
742
−2.734
−25.671
22.949
1.00
17.96


ATOM
1674
O
ASN
A
742
−3.727
−26.174
23.486
1.00
17.06


ATOM
1675
N
GLN
A
743
−1.827
−24.964
23.615
1.00
16.68


ATOM
1676
CA
GLN
A
743
−1.937
−24.727
25.045
1.00
17.92


ATOM
1677
CB
GLN
A
743
−0.738
−25.338
25.777
1.00
20.38


ATOM
1678
CG
GLN
A
743
−0.461
−26.787
25.408
1.00
28.60


ATOM
1679
CD
GLN
A
743
0.746
−27.350
26.131
1.00
30.94


ATOM
1680
OE1
GLN
A
743
1.775
−26.682
26.255
1.00
32.52


ATOM
1681
NE2
GLN
A
743
0.634
−28.588
26.602
1.00
20.21


ATOM
1682
C
GLN
A
743
−2.002
−23.233
25.341
1.00
16.35


ATOM
1683
O
GLN
A
743
−2.175
−22.836
26.490
1.00
18.44


ATOM
1684
N
PHE
A
744
−1.877
−22.407
24.307
1.00
16.26


ATOM
1685
CA
PHE
A
744
−1.916
−20.959
24.501
1.00
19.79


ATOM
1686
CB
PHE
A
744
−1.627
−20.229
23.184
1.00
21.58


ATOM
1687
CG
PHE
A
744
−1.465
−18.740
23.340
1.00
17.97


ATOM
1688
CD1
PHE
A
744
−0.441
−18.216
24.117
1.00
20.04


ATOM
1689
CD2
PHE
A
744
−2.345
−17.865
22.720
1.00
24.29


ATOM
1690
CE1
PHE
A
744
−0.298
−16.847
24.271
1.00
24.80


ATOM
1691
CE2
PHE
A
744
−2.208
−16.499
22.869
1.00
20.38


ATOM
1692
CZ
PHE
A
744
−1.184
−15.988
23.647
1.00
26.24


ATOM
1693
C
PHE
A
744
−3.265
−20.515
25.060
1.00
19.74


ATOM
1694
O
PHE
A
744
−4.316
−20.860
24.526
1.00
21.03


ATOM
1695
N
ASN
A
745
−3.221
−19.746
26.142
1.00
19.11


ATOM
1696
CA
ASN
A
745
−4.427
−19.260
26.791
1.00
18.83


ATOM
1697
CB
ASN
A
745
−4.893
−20.270
27.839
1.00
14.11


ATOM
1698
CG
ASN
A
745
−6.067
−19.764
28.653
1.00
17.45


ATOM
1699
OD1
ASN
A
745
−6.924
−19.042
28.143
1.00
22.19


ATOM
1700
ND2
ASN
A
745
−6.120
−20.152
29.921
1.00
30.84


ATOM
1701
C
ASN
A
745
−4.183
−17.906
27.446
1.00
17.46


ATOM
1702
O
ASN
A
745
−3.518
−17.818
28.481
1.00
17.84


ATOM
1703
N
LEU
A
746
−4.720
−16.857
26.826
1.00
16.56


ATOM
1704
CA
LEU
A
746
−4.573
−15.497
27.323
1.00
18.48


ATOM
1705
CB
LEU
A
746
−5.163
−14.495
26.323
1.00
15.11


ATOM
1706
CG
LEU
A
746
−4.319
−14.192
25.082
1.00
17.98


ATOM
1707
CD1
LEU
A
746
−5.031
−13.165
24.217
1.00
16.50


ATOM
1708
CD2
LEU
A
746
−2.960
−13.664
25.507
1.00
17.71


ATOM
1709
C
LEU
A
746
−5.212
−15.284
28.688
1.00
21.08


ATOM
1710
O
LEU
A
746
−4.911
−14.304
29.366
1.00
20.60


ATOM
1711
N
GLU
A
747
−6.098
−16.192
29.089
1.00
21.14


ATOM
1712
CA
GLU
A
747
−6.748
−16.075
30.389
1.00
21.90


ATOM
1713
CB
GLU
A
747
−7.916
−17.058
30.504
1.00
20.33


ATOM
1714
CG
GLU
A
747
−9.179
−16.586
29.813
1.00
31.82


ATOM
1715
CD
GLU
A
747
−10.324
−17.569
29.959
1.00
40.12


ATOM
1716
OE1
GLU
A
747
−10.550
−18.057
31.086
1.00
43.30


ATOM
1717
OE2
GLU
A
747
−11.003
−17.846
28.949
1.00
40.94


ATOM
1718
C
GLU
A
747
−5.740
−16.331
31.498
1.00
22.98


ATOM
1719
O
GLU
A
747
−5.885
−15.826
32.612
1.00
23.46


ATOM
1720
N
ASP
A
748
−4.719
−17.124
31.188
1.00
21.44


ATOM
1721
CA
ASP
A
748
−3.670
−17.424
32.151
1.00
21.15


ATOM
1722
CB
ASP
A
748
−2.800
−18.579
31.651
1.00
19.25


ATOM
1723
CG
ASP
A
748
−1.656
−18.899
32.595
1.00
19.90


ATOM
1724
OD1
ASP
A
748
−0.710
−18.088
32.692
1.00
26.86


ATOM
1725
OD2
ASP
A
748
−1.704
−19.962
33.246
1.00
42.46


ATOM
1726
C
ASP
A
748
−2.819
−16.171
32.314
1.00
20.94


ATOM
1727
O
ASP
A
748
−2.240
−15.677
31.351
1.00
19.01


ATOM
1728
N
PRO
A
749
−2.742
−15.637
33.541
1.00
18.53


ATOM
1729
CD
PRO
A
749
−3.443
−16.108
34.750
1.00
26.08


ATOM
1730
CA
PRO
A
749
−1.958
−14.432
33.825
1.00
19.83


ATOM
1731
CB
PRO
A
749
−2.009
−14.346
35.347
1.00
25.90


ATOM
1732
CG
PRO
A
749
−3.377
−14.896
35.654
1.00
25.60


ATOM
1733
C
PRO
A
749
−0.528
−14.476
33.286
1.00
17.96


ATOM
1734
O
PRO
A
749
−0.047
−13.506
32.708
1.00
18.09


ATOM
1735
N
HIS
A
750
0.149
−15.603
33.475
1.00
17.27


ATOM
1736
CA
HIS
A
750
1.520
−15.737
32.998
1.00
16.70


ATOM
1737
CB
HIS
A
750
2.138
−17.039
33.509
1.00
14.57


ATOM
1738
CG
HIS
A
750
3.506
−17.301
32.975
1.00
13.17


ATOM
1739
CD2
HIS
A
750
4.710
−16.780
33.299
1.00
15.22


ATOM
1740
ND1
HIS
A
750
3.748
−18.181
31.933
1.00
20.55


ATOM
1741
CE1
HIS
A
750
5.030
−18.183
31.649
1.00
21.44


ATOM
1742
NE2
HIS
A
750
5.644
−17.338
32.465
1.00
27.33


ATOM
1743
C
HIS
A
750
1.615
−15.691
31.475
1.00
16.04


ATOM
1744
O
HIS
A
750
2.521
−15.069
30.925
1.00
16.50


ATOM
1745
N
GLU
A
751
0.680
−16.346
30.794
1.00
14.76


ATOM
1746
CA
GLU
A
751
0.689
−16.359
29.333
1.00
14.97


ATOM
1747
CB
GLU
A
751
−0.269
−17.427
28.798
1.00
11.89


ATOM
1748
CG
GLU
A
751
0.173
−18.848
29.123
1.00
16.94


ATOM
1749
CD
GLU
A
751
−0.601
−19.892
28.354
1.00
17.06


ATOM
1750
OE1
GLU
A
751
−0.804
−19.697
27.140
1.00
17.15


ATOM
1751
OE2
GLU
A
751
−0.993
−20.912
28.959
1.00
27.83


ATOM
1752
C
GLU
A
751
0.325
−14.988
28.764
1.00
14.11


ATOM
1753
O
GLU
A
751
0.782
−14.616
27.685
1.00
14.18


ATOM
1754
N
LYS
A
752
−0.501
−14.248
29.498
1.00
13.06


ATOM
1755
CA
LYS
A
752
−0.900
−12.910
29.092
1.00
11.63


ATOM
1756
CB
LYS
A
752
−1.984
−12.370
30.041
1.00
11.74


ATOM
1757
CG
LYS
A
752
−2.200
−10.865
29.981
1.00
11.33


ATOM
1758
CD
LYS
A
752
−2.667
−10.402
28.608
1.00
18.51


ATOM
1759
CE
LYS
A
752
−3.921
−11.138
28.184
1.00
31.49


ATOM
1760
NZ
LYS
A
752
−4.536
−10.523
26.978
1.00
47.29


ATOM
1761
C
LYS
A
752
0.362
−12.047
29.176
1.00
14.58


ATOM
1762
O
LYS
A
752
0.665
−11.293
28.249
1.00
11.11


ATOM
1763
N
GLU
A
753
1.093
−12.196
30.270
1.00
12.46


ATOM
1764
CA
GLU
A
753
2.315
−11.409
30.445
1.00
13.89


ATOM
1765
CB
GLU
A
753
2.939
−11.745
31.801
1.00
15.41


ATOM
1766
CG
GLU
A
753
4.187
−10.950
32.098
1.00
17.51


ATOM
1767
CD
GLU
A
753
4.946
−11.478
33.300
1.00
36.21


ATOM
1768
OE1
GLU
A
753
4.335
−11.579
34.384
1.00
28.23


ATOM
1769
OE2
GLU
A
753
6.150
−11.782
33.162
1.00
36.81


ATOM
1770
C
GLU
A
753
3.267
−11.729
29.313
1.00
14.45


ATOM
1771
O
GLU
A
753
3.852
−10.839
28.671
1.00
11.34


ATOM
1772
N
LEU
A
754
3.441
−13.018
29.035
1.00
12.90


ATOM
1773
CA
LEU
A
754
4.329
−13.471
27.974
1.00
13.51


ATOM
1774
CB
LEU
A
754
4.377
−15.011
27.908
1.00
13.76


ATOM
1775
CG
LEU
A
754
5.196
−15.682
26.793
1.00
15.32


ATOM
1776
CD1
LEU
A
754
6.663
−15.286
26.877
1.00
15.56


ATOM
1777
CD2
LEU
A
754
5.044
−17.193
26.930
1.00
14.90


ATOM
1778
C
LEU
A
754
3.915
−12.900
26.616
1.00
12.21


ATOM
1779
O
LEU
A
754
4.765
−12.478
25.821
1.00
11.37


ATOM
1780
N
PHE
A
755
2.613
−12.867
26.351
1.00
11.00


ATOM
1781
CA
PHE
A
755
2.119
−12.336
25.088
1.00
9.92


ATOM
1782
CB
PHE
A
755
0.609
−12.551
24.966
1.00
12.44


ATOM
1783
CG
PHE
A
755
0.002
−11.867
23.780
1.00
11.67


ATOM
1784
CD1
PHE
A
755
0.338
−12.259
22.492
1.00
13.36


ATOM
1785
CD2
PHE
A
755
−0.858
−10.792
23.948
1.00
9.93


ATOM
1786
CE1
PHE
A
755
−0.170
−11.590
21.393
1.00
14.56


ATOM
1787
CE2
PHE
A
755
−1.369
−10.118
22.854
1.00
13.93


ATOM
1788
CZ
PHE
A
755
−1.021
−10.517
21.574
1.00
18.65


ATOM
1789
C
PHE
A
755
2.431
−10.840
24.972
1.00
9.95


ATOM
1790
O
PHE
A
755
2.856
−10.367
23.916
1.00
10.28


ATOM
1791
N
LEU
A
756
2.225
−10.099
26.057
1.00
9.98


ATOM
1792
CA
LEU
A
756
2.489
−8.664
26.034
1.00
9.03


ATOM
1793
CB
LEU
A
756
2.102
−8.017
27.370
1.00
9.14


ATOM
1794
CG
LEU
A
756
0.610
−8.119
27.706
1.00
13.27


ATOM
1795
CD1
LEU
A
756
0.331
−7.487
29.065
1.00
21.21


ATOM
1796
CD2
LEU
A
756
−0.198
−7.432
26.613
1.00
18.57


ATOM
1797
C
LEU
A
756
3.959
−8.410
25.721
1.00
9.36


ATOM
1798
O
LEU
A
756
4.291
−7.437
25.045
1.00
8.42


ATOM
1799
N
ALA
A
757
4.844
−9.285
26.197
1.00
7.41


ATOM
1800
CA
ALA
A
757
6.267
−9.118
25.915
1.00
10.17


ATOM
1801
CB
ALA
A
757
7.096
−10.112
26.720
1.00
10.57


ATOM
1802
C
ALA
A
757
6.514
−9.315
24.421
1.00
9.99


ATOM
1803
O
ALA
A
757
7.254
−8.548
23.798
1.00
10.22


ATOM
1804
N
MET
A
758
5.890
−10.341
23.845
1.00
8.41


ATOM
1805
CA
MET
A
758
6.046
−10.627
22.422
1.00
8.55


ATOM
1806
CB
MET
A
758
5.348
−11.946
22.061
1.00
8.57


ATOM
1807
CG
MET
A
758
5.898
−13.175
22.783
1.00
9.97


ATOM
1808
SD
MET
A
758
7.613
−13.597
22.367
1.00
15.99


ATOM
1809
CE
MET
A
758
7.436
−14.226
20.702
1.00
36.66


ATOM
1810
C
MET
A
758
5.469
−9.499
21.572
1.00
9.31


ATOM
1811
O
MET
A
758
6.035
−9.134
20.534
1.00
8.67


ATOM
1812
N
LEU
A
759
4.334
−8.962
22.008
1.00
10.68


ATOM
1813
CA
LEU
A
759
3.682
−7.877
21.290
1.00
7.26


ATOM
1814
CB
LEU
A
759
2.348
−7.536
21.954
1.00
6.70


ATOM
1815
CG
LEU
A
759
1.521
−6.419
21.316
1.00
9.88


ATOM
1816
CD1
LEU
A
759
1.217
−6.751
19.858
1.00
13.46


ATOM
1817
CD2
LEU
A
759
0.232
−6.241
22.103
1.00
8.91


ATOM
1818
C
LEU
A
759
4.589
−6.650
21.269
1.00
10.65


ATOM
1819
O
LEU
A
759
4.677
−5.945
20.259
1.00
8.66


ATOM
1820
N
MET
A
760
5.258
−6.388
22.387
1.00
8.87


ATOM
1821
CA
MET
A
760
6.168
−5.251
22.454
1.00
9.10


ATOM
1822
CB
MET
A
760
6.760
−5.114
23.859
1.00
9.37


ATOM
1823
CG
MET
A
760
5.831
−4.491
24.889
1.00
7.94


ATOM
1824
SD
MET
A
760
5.392
−2.762
24.513
1.00
11.15


ATOM
1825
CE
MET
A
760
6.981
−1.951
24.748
1.00
10.58


ATOM
1826
C
MET
A
760
7.292
−5.445
21.444
1.00
9.36


ATOM
1827
O
MET
A
760
7.693
−4.501
20.757
1.00
8.44


ATOM
1828
N
THR
A
761
7.812
−6.667
21.359
1.00
8.62


ATOM
1829
CA
THR
A
761
8.890
−6.948
20.416
1.00
9.46


ATOM
1830
CB
THR
A
761
9.442
−8.379
20.597
1.00
12.42


ATOM
1831
OG1
THR
A
761
9.916
−8.540
21.940
1.00
11.86


ATOM
1832
CG2
THR
A
761
10.598
−8.636
19.620
1.00
9.90


ATOM
1833
C
THR
A
761
8.389
−6.785
18.984
1.00
10.31


ATOM
1834
O
THR
A
761
9.088
−6.238
18.128
1.00
10.55


ATOM
1835
N
ALA
A
762
7.172
−7.254
18.722
1.00
10.42


ATOM
1836
CA
ALA
A
762
6.598
−7.148
17.389
1.00
7.73


ATOM
1837
CB
ALA
A
762
5.202
−7.777
17.362
1.00
10.79


ATOM
1838
C
ALA
A
762
6.524
−5.689
16.948
1.00
9.57


ATOM
1839
O
ALA
A
762
6.794
−5.370
15.787
1.00
9.59


ATOM
1840
N
CYS
A
763
6.161
−4.801
17.872
1.00
7.53


ATOM
1841
CA
CYS
A
763
6.063
−3.378
17.551
1.00
7.89


ATOM
1842
CB
CYS
A
763
5.237
−2.641
18.611
1.00
11.70


ATOM
1843
SG
CYS
A
763
3.503
−3.143
18.670
1.00
11.19


ATOM
1844
C
CYS
A
763
7.441
−2.744
17.443
1.00
9.03


ATOM
1845
O
CYS
A
763
7.689
−1.911
16.574
1.00
10.26


ATOM
1846
N
ASP
A
764
8.340
−3.157
18.329
1.00
8.73


ATOM
1847
CA
ASP
A
764
9.703
−2.641
18.352
1.00
10.03


ATOM
1848
CB
ASP
A
764
10.448
−3.269
19.541
1.00
11.85


ATOM
1849
CG
ASP
A
764
11.766
−2.585
19.840
1.00
12.03


ATOM
1850
OD1
ASP
A
764
11.963
−1.451
19.361
1.00
11.46


ATOM
1851
OD2
ASP
A
764
12.592
−3.176
20.571
1.00
15.03


ATOM
1852
C
ASP
A
764
10.447
−2.924
17.036
1.00
10.20


ATOM
1853
O
ASP
A
764
11.225
−2.097
16.562
1.00
11.71


ATOM
1854
N
LEU
A
765
10.194
−4.086
16.442
1.00
11.54


ATOM
1855
CA
LEU
A
765
10.867
−4.474
15.202
1.00
11.71


ATOM
1856
CB
LEU
A
765
11.208
−5.965
15.252
1.00
13.42


ATOM
1857
CG
LEU
A
765
12.017
−6.454
16.453
1.00
15.02


ATOM
1858
CD1
LEU
A
765
12.233
−7.957
16.348
1.00
13.91


ATOM
1859
CD2
LEU
A
765
13.345
−5.721
16.499
1.00
16.31


ATOM
1860
C
LEU
A
765
10.049
−4.221
13.941
1.00
12.10


ATOM
1861
O
LEU
A
765
10.490
−4.560
12.837
1.00
11.30


ATOM
1862
N
SER
A
766
8.881
−3.606
14.101
1.00
12.76


ATOM
1863
CA
SER
A
766
7.965
−3.383
12.983
1.00
10.86


ATOM
1864
CB
SER
A
766
6.672
−2.733
13.488
1.00
8.49


ATOM
1865
OG
SER
A
766
6.902
−1.438
13.991
1.00
14.83


ATOM
1866
C
SER
A
766
8.446
−2.657
11.729
1.00
7.60


ATOM
1867
O
SER
A
766
7.782
−2.735
10.700
1.00
9.56


ATOM
1868
N
ALA
A
767
9.575
−1.956
11.787
1.00
8.02


ATOM
1869
CA
ALA
A
767
10.073
−1.296
10.581
1.00
9.45


ATOM
1870
CB
ALA
A
767
11.364
−0.522
10.881
1.00
11.41


ATOM
1871
C
ALA
A
767
10.340
−2.377
9.521
1.00
10.04


ATOM
1872
O
ALA
A
767
10.253
−2.124
8.319
1.00
10.04


ATOM
1873
N
ILE
A
768
10.655
−3.586
9.976
1.00
9.49


ATOM
1874
CA
ILE
A
768
10.942
−4.694
9.066
1.00
12.99


ATOM
1875
CB
ILE
A
768
11.555
−5.894
9.840
1.00
9.64


ATOM
1876
CG2
ILE
A
768
10.473
−6.631
10.612
1.00
7.91


ATOM
1877
CG1
ILE
A
768
12.270
−6.836
8.868
1.00
12.83


ATOM
1878
CD1
ILE
A
768
13.471
−6.199
8.190
1.00
15.69


ATOM
1879
C
ILE
A
768
9.704
−5.173
8.296
1.00
11.57


ATOM
1880
O
ILE
A
768
9.812
−5.986
7.376
1.00
12.45


ATOM
1881
N
THR
A
769
8.530
−4.665
8.662
1.00
12.70


ATOM
1882
CA
THR
A
769
7.286
−5.062
7.999
1.00
10.88


ATOM
1883
CB
THR
A
769
6.167
−5.326
9.025
1.00
13.25


ATOM
1884
OG1
THR
A
769
5.760
−4.083
9.617
1.00
12.15


ATOM
1885
CG2
THR
A
769
6.654
−6.271
10.124
1.00
16.86


ATOM
1886
C
THR
A
769
6.762
−3.991
7.036
1.00
12.18


ATOM
1887
O
THR
A
769
5.795
−4.223
6.308
1.00
13.18


ATOM
1888
N
LYS
A
770
7.402
−2.824
7.043
1.00
12.64


ATOM
1889
CA
LYS
A
770
6.986
−1.686
6.216
1.00
10.43


ATOM
1890
CB
LYS
A
770
7.684
−0.413
6.714
1.00
12.22


ATOM
1891
CG
LYS
A
770
7.375
−0.029
8.165
1.00
7.87


ATOM
1892
CD
LYS
A
770
5.948
0.457
8.330
1.00
13.33


ATOM
1893
CE
LYS
A
770
5.644
0.766
9.794
1.00
14.40


ATOM
1894
NZ
LYS
A
770
4.263
1.293
9.973
1.00
14.45


ATOM
1895
C
LYS
A
770
7.247
−1.829
4.716
1.00
11.91


ATOM
1896
O
LYS
A
770
8.069
−2.638
4.290
1.00
13.63


ATOM
1897
N
PRO
A
771
6.529
−1.041
3.892
1.00
11.52


ATOM
1898
CD
PRO
A
771
5.408
−0.150
4.240
1.00
14.60


ATOM
1899
CA
PRO
A
771
6.718
−1.096
2.441
1.00
12.80


ATOM
1900
CB
PRO
A
771
5.914
0.099
1.950
1.00
15.88


ATOM
1901
CG
PRO
A
771
4.751
0.098
2.886
1.00
11.15


ATOM
1902
C
PRO
A
771
8.206
−0.933
2.183
1.00
14.66


ATOM
1903
O
PRO
A
771
8.880
−0.201
2.908
1.00
15.01


ATOM
1904
N
TRP
A
772
8.711
−1.604
1.156
1.00
14.26


ATOM
1905
CA
TRP
A
772
10.133
−1.555
0.827
1.00
15.34


ATOM
1906
CB
TRP
A
772
10.367
−2.121
−0.578
1.00
14.10


ATOM
1907
CG
TRP
A
772
11.809
−2.101
−1.009
1.00
17.47


ATOM
1908
CD2
TRP
A
772
12.931
−2.659
−0.307
1.00
17.61


ATOM
1909
CE2
TRP
A
772
14.079
−2.404
−1.086
1.00
19.63


ATOM
1910
CE3
TRP
A
772
13.076
−3.348
0.901
1.00
16.69


ATOM
1911
CD1
TRP
A
772
12.313
−1.547
−2.152
1.00
16.69


ATOM
1912
NE1
TRP
A
772
13.675
−1.725
−2.204
1.00
24.41


ATOM
1913
CZ2
TRP
A
772
15.354
−2.816
−0.694
1.00
24.29


ATOM
1914
CZ3
TRP
A
772
14.344
−3.755
1.289
1.00
17.48


ATOM
1915
CH2
TRP
A
772
15.466
−3.488
0.493
1.00
21.25


ATOM
1916
C
TRP
A
772
10.820
−0.190
0.952
1.00
17.78


ATOM
1917
O
TRP
A
772
11.834
−0.070
1.639
1.00
15.81


ATOM
1918
N
PRO
A
773
10.286
0.853
0.291
1.00
19.35


ATOM
1919
CD
PRO
A
773
9.132
0.877
−0.624
1.00
18.85


ATOM
1920
CA
PRO
A
773
10.909
2.180
0.377
1.00
18.24


ATOM
1921
CB
PRO
A
773
9.926
3.068
−0.382
1.00
21.17


ATOM
1922
CG
PRO
A
773
9.386
2.138
−1.422
1.00
23.60


ATOM
1923
C
PRO
A
773
11.129
2.654
1.814
1.00
16.33


ATOM
1924
O
PRO
A
773
12.167
3.235
2.140
1.00
16.01


ATOM
1925
N
ILE
A
774
10.143
2.406
2.668
1.00
16.23


ATOM
1926
CA
ILE
A
774
10.228
2.805
4.066
1.00
15.30


ATOM
1927
CB
ILE
A
774
8.851
2.670
4.751
1.00
15.99


ATOM
1928
CG2
ILE
A
774
8.977
2.922
6.250
1.00
13.24


ATOM
1929
CG1
ILE
A
774
7.867
3.658
4.110
1.00
20.68


ATOM
1930
CD1
ILE
A
774
6.441
3.501
4.588
1.00
21.74


ATOM
1931
C
ILE
A
774
11.264
1.958
4.804
1.00
16.31


ATOM
1932
O
ILE
A
774
12.133
2.491
5.497
1.00
15.63


ATOM
1933
N
GLN
A
775
11.173
0.640
4.650
1.00
13.80


ATOM
1934
CA
GLN
A
775
12.120
−0.274
5.279
1.00
12.85


ATOM
1935
CB
GLN
A
775
11.786
−1.727
4.901
1.00
13.34


ATOM
1936
CG
GLN
A
775
12.987
−2.688
4.921
1.00
14.20


ATOM
1937
CD
GLN
A
775
13.582
−2.897
6.305
1.00
21.70


ATOM
1938
OE1
GLN
A
775
14.663
−3.472
6.441
1.00
13.81


ATOM
1939
NE2
GLN
A
775
12.880
−2.440
7.336
1.00
14.50


ATOM
1940
C
GLN
A
775
13.549
0.057
4.877
1.00
13.13


ATOM
1941
O
GLN
A
775
14.458
0.060
5.694
1.00
12.67


ATOM
1942
N
GLN
A
776
13.749
0.352
3.590
1.00
10.04


ATOM
1943
CA
GLN
A
776
15.068
0.674
3.090
1.00
12.84


ATOM
1944
CB
GLN
A
776
15.004
0.820
1.564
1.00
19.00


ATOM
1945
CG
GLN
A
776
16.326
0.943
0.890
1.00
25.33


ATOM
1946
CD
GLN
A
776
16.172
0.760
−0.595
1.00
36.37


ATOM
1947
OE1
GLN
A
776
15.258
1.315
−1.209
1.00
39.80


ATOM
1948
NE2
GLN
A
776
17.058
−0.023
−1.186
1.00
41.16


ATOM
1949
C
GLN
A
776
15.627
1.934
3.738
1.00
10.61


ATOM
1950
O
GLN
A
776
16.796
1.988
4.109
1.00
13.39


ATOM
1951
N
ARG
A
777
14.776
2.946
3.922
1.00
10.52


ATOM
1952
CA
ARG
A
777
15.199
4.197
4.534
1.00
11.43


ATOM
1953
CB
ARG
A
777
14.090
5.253
4.419
1.00
15.26


ATOM
1954
CG
ARG
A
777
14.487
6.607
4.948
1.00
20.06


ATOM
1955
CD
ARG
A
777
13.343
7.586
4.765
1.00
25.19


ATOM
1956
NE
ARG
A
777
12.206
7.273
5.627
1.00
34.37


ATOM
1957
CZ
ARG
A
777
12.232
7.359
6.954
1.00
35.62


ATOM
1958
NH1
ARG
A
777
13.340
7.747
7.575
1.00
37.87


ATOM
1959
NH2
ARG
A
777
11.149
7.068
7.661
1.00
29.66


ATOM
1960
C
ARG
A
777
15.560
3.979
5.997
1.00
10.83


ATOM
1961
O
ARG
A
777
16.601
4.447
6.472
1.00
13.15


ATOM
1962
N
ILE
A
778
14.715
3.238
6.705
1.00
12.38


ATOM
1963
CA
ILE
A
778
14.953
2.944
8.112
1.00
13.18


ATOM
1964
CB
ILE
A
778
13.753
2.209
8.744
1.00
15.50


ATOM
1965
CG2
ILE
A
778
14.091
1.788
10.170
1.00
13.56


ATOM
1966
CG1
ILE
A
778
12.516
3.108
8.721
1.00
22.29


ATOM
1967
CD1
ILE
A
778
12.685
4.399
9.478
1.00
26.81


ATOM
1968
C
ILE
A
778
16.198
2.086
8.305
1.00
12.49


ATOM
1969
O
ILE
A
778
16.963
2.298
9.245
1.00
12.70


ATOM
1970
N
ALA
A
779
16.399
1.117
7.417
1.00
12.47


ATOM
1971
CA
ALA
A
779
17.563
0.242
7.510
1.00
13.19


ATOM
1972
CB
ALA
A
779
17.538
−0.789
6.391
1.00
14.05


ATOM
1973
C
ALA
A
779
18.856
1.051
7.452
1.00
13.71


ATOM
1974
O
ALA
A
779
19.839
0.700
8.106
1.00
11.99


ATOM
1975
N
GLU
A
780
18.858
2.131
6.672
1.00
14.86


ATOM
1976
CA
GLU
A
780
20.048
2.976
6.560
1.00
13.62


ATOM
1977
CB
GLU
A
780
19.860
4.053
5.487
1.00
17.29


ATOM
1978
CG
GLU
A
780
19.742
3.519
4.075
1.00
30.45


ATOM
1979
CD
GLU
A
780
19.744
4.628
3.038
1.00
42.90


ATOM
1980
OE1
GLU
A
780
20.761
5.347
2.939
1.00
42.08


ATOM
1981
OE2
GLU
A
780
18.728
4.783
2.326
1.00
56.88


ATOM
1982
C
GLU
A
780
20.350
3.649
7.897
1.00
13.45


ATOM
1983
O
GLU
A
780
21.506
3.791
8.277
1.00
14.75


ATOM
1984
N
LEU
A
781
19.303
4.074
8.597
1.00
12.82


ATOM
1985
CA
LEU
A
781
19.464
4.716
9.898
1.00
10.66


ATOM
1986
CB
LEU
A
781
18.113
5.215
10.410
1.00
12.60


ATOM
1987
CG
LEU
A
781
17.428
6.296
9.574
1.00
15.49


ATOM
1988
CD1
LEU
A
781
16.101
6.670
10.215
1.00
14.52


ATOM
1989
CD2
LEU
A
781
18.339
7.513
9.475
1.00
17.00


ATOM
1990
C
LEU
A
781
20.032
3.704
10.887
1.00
12.39


ATOM
1991
O
LEU
A
781
20.935
4.014
11.673
1.00
11.98


ATOM
1992
N
VAL
A
782
19.490
2.490
10.839
1.00
9.90


ATOM
1993
CA
VAL
A
782
19.933
1.418
11.719
1.00
9.65


ATOM
1994
CB
VAL
A
782
19.116
0.126
11.463
1.00
10.42


ATOM
1995
CG1
VAL
A
782
19.714
−1.029
12.240
1.00
13.17


ATOM
1996
CG2
VAL
A
782
17.657
0.339
11.868
1.00
16.63


ATOM
1997
C
VAL
A
782
21.418
1.154
11.477
1.00
10.70


ATOM
1998
O
VAL
A
782
22.210
1.068
12.418
1.00
13.37


ATOM
1999
N
ALA
A
783
21.793
1.053
10.206
1.00
11.25


ATOM
2000
CA
ALA
A
783
23.185
0.810
9.839
1.00
11.83


ATOM
2001
CB
ALA
A
783
23.299
0.632
8.337
1.00
15.10


ATOM
2002
C
ALA
A
783
24.074
1.961
10.298
1.00
12.03


ATOM
2003
O
ALA
A
783
25.170
1.746
10.820
1.00
12.81


ATOM
2004
N
THR
A
784
23.599
3.187
10.099
1.00
11.94


ATOM
2005
CA
THR
A
784
24.358
4.359
10.504
1.00
10.90


ATOM
2006
CB
THR
A
784
23.572
5.659
10.211
1.00
12.78


ATOM
2007
OG1
THR
A
784
23.359
5.778
8.797
1.00
15.62


ATOM
2008
CG2
THR
A
784
24.341
6.883
10.706
1.00
13.70


ATOM
2009
C
THR
A
784
24.676
4.282
11.995
1.00
11.74


ATOM
2010
O
THR
A
784
25.819
4.490
12.408
1.00
10.51


ATOM
2011
N
GLU
A
785
23.670
3.969
12.805
1.00
10.01


ATOM
2012
CA
GLU
A
785
23.881
3.880
14.243
1.00
10.75


ATOM
2013
CB
GLU
A
785
22.549
3.669
14.968
1.00
7.51


ATOM
2014
CG
GLU
A
785
22.675
3.740
16.483
1.00
9.65


ATOM
2015
CD
GLU
A
785
21.335
3.755
17.178
1.00
7.52


ATOM
2016
OE1
GLU
A
785
20.415
4.436
16.674
1.00
10.93


ATOM
2017
OE2
GLU
A
785
21.208
3.099
18.236
1.00
12.56


ATOM
2018
C
GLU
A
785
24.847
2.760
14.612
1.00
11.99


ATOM
2019
O
GLU
A
785
25.737
2.948
15.440
1.00
11.68


ATOM
2020
N
PHE
A
786
24.671
1.594
13.997
1.00
9.83


ATOM
2021
CA
PHE
A
786
25.541
0.464
14.285
1.00
10.39


ATOM
2022
CB
PHE
A
786
25.069
−0.794
13.550
1.00
11.58


ATOM
2023
CG
PHE
A
786
23.876
−1.455
14.176
1.00
16.59


ATOM
2024
CD1
PHE
A
786
23.632
−1.327
15.533
1.00
18.18


ATOM
2025
CD2
PHE
A
786
23.034
−2.254
13.419
1.00
19.90


ATOM
2026
CE1
PHE
A
786
22.570
−1.986
16.125
1.00
25.35


ATOM
2027
CE2
PHE
A
786
21.972
−2.916
14.004
1.00
17.12


ATOM
2028
CZ
PHE
A
786
21.740
−2.781
15.360
1.00
16.84


ATOM
2029
C
PHE
A
786
26.985
0.760
13.898
1.00
9.62


ATOM
2030
O
PHE
A
786
27.907
0.444
14.652
1.00
10.46


ATOM
2031
N
PHE
A
787
27.183
1.348
12.720
1.00
8.90


ATOM
2032
CA
PHE
A
787
28.531
1.680
12.273
1.00
9.83


ATOM
2033
CB
PHE
A
787
28.515
2.141
10.809
1.00
10.96


ATOM
2034
CG
PHE
A
787
28.116
1.056
9.849
1.00
8.28


ATOM
2035
CD1
PHE
A
787
28.335
−0.276
10.172
1.00
10.72


ATOM
2036
CD2
PHE
A
787
27.546
1.357
8.626
1.00
11.47


ATOM
2037
CE1
PHE
A
787
27.993
−1.287
9.296
1.00
12.45


ATOM
2038
CE2
PHE
A
787
27.201
0.344
7.739
1.00
12.21


ATOM
2039
CZ
PHE
A
787
27.424
−0.977
8.075
1.00
8.97


ATOM
2040
C
PHE
A
787
29.165
2.747
13.149
1.00
12.00


ATOM
2041
O
PHE
A
787
30.387
2.787
13.311
1.00
11.70


ATOM
2042
N
ASP
A
788
28.340
3.620
13.713
1.00
10.51


ATOM
2043
CA
ASP
A
788
28.867
4.655
14.583
1.00
13.07


ATOM
2044
CB
ASP
A
788
27.770
5.654
14.953
1.00
9.28


ATOM
2045
CG
ASP
A
788
28.275
6.751
15.869
1.00
17.65


ATOM
2046
OD1
ASP
A
788
27.862
6.784
17.046
1.00
22.26


ATOM
2047
OD2
ASP
A
788
29.097
7.575
15.414
1.00
23.70


ATOM
2048
CA
ASP
A
788
29.427
3.975
15.832
1.00
11.61


ATOM
2049
O
ASP
A
788
30.491
4.349
16.324
1.00
11.23


ATOM
2050
N
GLN
A
789
28.719
2.965
16.338
1.00
10.39


ATOM
2051
CA
GLN
A
789
29.201
2.243
17.515
1.00
10.66


ATOM
2052
CB
GLN
A
789
28.185
1.199
17.979
1.00
14.04


ATOM
2053
CG
GLN
A
789
28.667
0.416
19.191
1.00
13.95


ATOM
2054
CD
GLN
A
789
27.696
−0.652
19.641
1.00
13.88


ATOM
2055
OE1
GLN
A
789
26.488
−0.445
19.641
1.00
10.68


ATOM
2056
NE2
GLN
A
789
28.226
−1.799
20.051
1.00
10.88


ATOM
2057
C
GLN
A
789
30.509
1.541
17.155
1.00
12.25


ATOM
2058
O
GLN
A
789
31.452
1.504
17.952
1.00
12.92


ATOM
2059
N
GLY
A
790
30.552
0.979
15.950
1.00
12.27


ATOM
2060
CA
GLY
A
790
31.746
0.292
15.493
1.00
13.69


ATOM
2061
C
GLY
A
790
32.948
1.218
15.519
1.00
12.41


ATOM
2062
O
GLY
A
790
34.050
0.805
15.885
1.00
14.19


ATOM
2063
N
ASP
A
791
32.743
2.476
15.135
1.00
13.24


ATOM
2064
CA
ASP
A
791
33.837
3.448
15.135
1.00
15.89


ATOM
2065
CB
ASP
A
791
33.383
4.802
14.582
1.00
11.78


ATOM
2066
CG
ASP
A
791
33.022
4.748
13.108
1.00
11.72


ATOM
2067
OD1
ASP
A
791
33.525
3.853
12.401
1.00
16.07


ATOM
2068
OD2
ASP
A
791
32.249
5.619
12.657
1.00
16.56


ATOM
2069
C
ASP
A
791
34.350
3.653
16.554
1.00
15.06


ATOM
2070
O
ASP
A
791
35.555
3.751
16.794
1.00
15.97


ATOM
2071
N
ARG
A
792
33.423
3.723
17.496
1.00
16.00


ATOM
2072
CA
ARG
A
792
33.783
3.925
18.885
1.00
13.38


ATOM
2073
CB
ARG
A
792
32.544
4.308
19.680
1.00
15.67


ATOM
2074
CG
ARG
A
792
32.056
5.689
19.304
1.00
20.98


ATOM
2075
CD
ARG
A
792
30.791
6.043
20.014
1.00
22.55


ATOM
2076
NE
ARG
A
792
30.929
6.004
21.465
1.00
21.96


ATOM
2077
CZ
ARG
A
792
29.945
6.332
22.290
1.00
19.00


ATOM
2078
NH1
ARG
A
792
28.782
6.726
21.791
1.00
18.95


ATOM
2079
NH2
ARG
A
792
30.105
6.236
23.601
1.00
23.88


ATOM
2080
C
ARG
A
792
34.466
2.716
19.501
1.00
13.13


ATOM
2081
O
ARG
A
792
35.296
2.865
20.390
1.00
14.33


ATOM
2082
N
GLU
A
793
34.112
1.522
19.036
1.00
14.11


ATOM
2083
CA
GLU
A
793
34.730
0.305
19.545
1.00
12.55


ATOM
2084
CB
GLU
A
793
33.969
−0.932
19.051
1.00
12.93


ATOM
2085
CG
GLU
A
793
32.531
−0.986
19.543
1.00
15.09


ATOM
2086
CD
GLU
A
793
31.816
−2.269
19.165
1.00
17.10


ATOM
2087
OE1
GLU
A
793
32.105
−2.807
18.078
1.00
14.75


ATOM
2088
OE2
GLU
A
793
30.951
−2.728
19.949
1.00
13.37


ATOM
2089
C
GLU
A
793
36.184
0.251
19.080
1.00
13.70


ATOM
2090
O
GLU
A
793
37.073
−0.143
19.837
1.00
14.48


ATOM
2091
N
ARG
A
794
36.429
0.655
17.838
1.00
12.88


ATOM
2092
CA
ARG
A
794
37.792
0.647
17.318
1.00
16.50


ATOM
2093
CB
ARG
A
794
37.828
1.083
15.847
1.00
16.91


ATOM
2094
CG
ARG
A
794
37.330
0.047
14.838
1.00
16.40


ATOM
2095
CD
ARG
A
794
37.399
0.609
13.422
1.00
20.95


ATOM
2096
NE
ARG
A
794
36.790
−0.268
12.422
1.00
21.25


ATOM
2097
CZ
ARG
A
794
37.323
−1.407
11.996
1.00
16.41


ATOM
2098
NH1
ARG
A
794
38.486
−1.822
12.480
1.00
26.91


ATOM
2099
NH2
ARG
A
794
36.691
−2.134
11.082
1.00
18.30


ATOM
2100
C
ARG
A
794
38.648
1.603
18.141
1.00
17.48


ATOM
2101
O
ARG
A
794
39.781
1.287
18.503
1.00
18.61


ATOM
2102
N
LYS
A
795
38.087
2.769
18.443
1.00
19.00


ATOM
2103
CA
LYS
A
795
38.793
3.795
19.199
1.00
19.03


ATOM
2104
CB
LYS
A
795
38.146
5.161
18.947
1.00
22.77


ATOM
2105
CG
LYS
A
795
38.839
6.312
19.661
1.00
30.54


ATOM
2106
CD
LYS
A
795
38.128
7.633
19.410
1.00
38.45


ATOM
2107
CE
LYS
A
795
38.902
8.796
20.009
1.00
34.57


ATOM
2108
NZ
LYS
A
795
40.267
8.886
19.424
1.00
42.21


ATOM
2109
C
LYS
A
795
38.866
3.554
20.704
1.00
19.86


ATOM
2110
O
LYS
A
795
39.923
3.716
21.310
1.00
21.68


ATOM
2111
N
GLU
A
796
37.747
3.166
21.304
1.00
17.50


ATOM
2112
CA
GLU
A
796
37.696
2.953
22.745
1.00
18.20


ATOM
2113
CB
GLU
A
796
36.286
3.272
23.255
1.00
16.63


ATOM
2114
CG
GLU
A
796
35.872
4.722
23.048
1.00
19.55


ATOM
2115
CD
GLU
A
796
34.425
4.982
23.414
1.00
17.22


ATOM
2116
OE1
GLU
A
796
33.986
4.520
24.489
1.00
17.11


ATOM
2117
OE2
GLU
A
796
33.729
5.660
22.629
1.00
17.31


ATOM
2118
C
GLU
A
796
38.116
1.568
23.238
1.00
18.82


ATOM
2119
O
GLU
A
796
38.604
1.432
24.359
1.00
19.88


ATOM
2120
N
LEU
A
797
37.936
0.544
22.408
1.00
17.76


ATOM
2121
CA
LEU
A
797
38.279
−0.817
22.809
1.00
17.55


ATOM
2122
CB
LEU
A
797
37.032
−1.708
22.732
1.00
14.21


ATOM
2123
CG
LEU
A
797
35.816
−1.230
23.535
1.00
21.04


ATOM
2124
CD1
LEU
A
797
34.655
−2.194
23.333
1.00
19.81


ATOM
2125
CD2
LEU
A
797
36.177
−1.134
25.008
1.00
22.47


ATOM
2126
C
LEU
A
797
39.400
−1.441
21.980
1.00
18.06


ATOM
2127
O
LEU
A
797
39.899
−2.518
22.312
1.00
18.10


ATOM
2128
N
ASN
A
798
39.795
−0.760
20.910
1.00
17.87


ATOM
2129
CA
ASN
A
798
40.846
−1.244
20.016
1.00
17.14


ATOM
2130
CB
ASN
A
798
42.202
−1.278
20.732
1.00
18.53


ATOM
2131
CG
ASN
A
798
43.357
−1.501
19.770
1.00
19.84


ATOM
2132
OD1
ASN
A
798
43.497
−0.774
18.788
1.00
22.65


ATOM
2133
ND2
ASN
A
798
44.186
−2.507
20.043
1.00
17.46


ATOM
2134
C
ASN
A
798
40.522
−2.632
19.472
1.00
19.40


ATOM
2135
O
ASN
A
798
41.400
−3.485
19.352
1.00
18.37


ATOM
2136
N
ILE
A
799
39.254
−2.852
19.141
1.00
18.23


ATOM
2137
CA
ILE
A
799
38.816
−4.134
18.603
1.00
20.72


ATOM
2138
CB
ILE
A
799
37.779
−4.811
19.529
1.00
23.69


ATOM
2139
CG2
ILE
A
799
38.348
−4.970
20.930
1.00
25.12


ATOM
2140
CG1
ILE
A
799
36.500
−3.968
19.570
1.00
27.29


ATOM
2141
CD1
ILE
A
799
35.381
−4.581
20.373
1.00
23.09


ATOM
2142
C
ILE
A
799
38.158
−3.926
17.243
1.00
20.66


ATOM
2143
O
ILE
A
799
37.636
−2.846
16.956
1.00
20.48


ATOM
2144
N
GLU
A
800
38.199
−4.951
16.399
1.00
20.84


ATOM
2145
CA
GLU
A
800
37.558
−4.855
15.096
1.00
19.43


ATOM
2146
CB
GLU
A
800
38.162
−5.856
14.109
1.00
25.89


ATOM
2147
CG
GLU
A
800
37.507
−5.813
12.735
1.00
37.89


ATOM
2148
CD
GLU
A
800
38.245
−6.637
11.699
1.00
48.08


ATOM
2149
OE1
GLU
A
800
38.421
−7.856
11.915
1.00
47.23


ATOM
2150
OE2
GLU
A
800
38.647
−6.063
10.663
1.00
52.27


ATOM
2151
C
GLU
A
800
36.095
−5.188
15.345
1.00
16.86


ATOM
2152
O
GLU
A
800
35.774
−6.249
15.879
1.00
20.00


ATOM
2153
N
PRO
A
801
35.186
−4.277
14.979
1.00
16.72


ATOM
2154
CD
PRO
A
801
35.413
−2.971
14.340
1.00
13.94


ATOM
2155
CA
PRO
A
801
33.755
−4.518
15.188
1.00
15.17


ATOM
2156
CB
PRO
A
801
33.101
−3.242
14.651
1.00
11.35


ATOM
2157
CG
PRO
A
801
34.189
−2.204
14.760
1.00
18.39


ATOM
2158
C
PRO
A
801
33.249
−5.750
14.446
1.00
14.88


ATOM
2159
O
PRO
A
801
33.836
−6.168
13.437
1.00
14.57


ATOM
2160
N
THR
A
802
32.166
−6.333
14.952
1.00
13.89


ATOM
2161
CA
THR
A
802
31.554
−7.473
14.282
1.00
13.70


ATOM
2162
CB
THR
A
802
30.367
−8.057
15.090
1.00
18.66


ATOM
2163
OG1
THR
A
802
29.339
−7.067
15.227
1.00
22.82


ATOM
2164
CG2
THR
A
802
30.824
−8.491
16.475
1.00
28.52


ATOM
2165
C
THR
A
802
31.028
−6.886
12.974
1.00
13.06


ATOM
2166
O
THR
A
802
30.896
−5.666
12.853
1.00
13.12


ATOM
2167
N
ASP
A
803
30.730
−7.737
11.997
1.00
13.68


ATOM
2168
CA
ASP
A
803
30.239
−7.260
10.706
1.00
13.10


ATOM
2169
CB
ASP
A
803
29.784
−8.436
9.840
1.00
15.94


ATOM
2170
CG
ASP
A
803
30.942
−9.281
9.340
1.00
19.70


ATOM
2171
OD1
ASP
A
803
32.108
−8.965
9.661
1.00
16.86


ATOM
2172
OD2
ASP
A
803
30.681
−10.265
8.619
1.00
17.57


ATOM
2173
C
ASP
A
803
29.092
−6.262
10.829
1.00
14.26


ATOM
2174
O
ASP
A
803
29.071
−5.239
10.141
1.00
15.59


ATOM
2175
N
LEU
A
804
28.142
−6.561
11.706
1.00
12.76


ATOM
2176
CA
LEU
A
804
26.982
−5.700
11.907
1.00
13.21


ATOM
2177
CB
LEU
A
804
26.116
−6.251
13.042
1.00
14.65


ATOM
2178
CG
LEU
A
804
24.861
−5.430
13.347
1.00
15.24


ATOM
2179
CD1
LEU
A
804
24.020
−5.317
12.092
1.00
16.29


ATOM
2180
CD2
LEU
A
804
24.068
−6.089
14.461
1.00
23.77


ATOM
2181
C
LEU
A
804
27.356
−4.252
12.214
1.00
13.48


ATOM
2182
O
LEU
A
804
26.646
−3.317
11.825
1.00
13.22


ATOM
2183
N
MET
A
805
28.476
−4.067
12.904
1.00
12.28


ATOM
2184
CA
MET
A
805
28.909
−2.725
13.276
1.00
11.75


ATOM
2185
CB
MET
A
805
29.141
−2.671
14.790
1.00
13.28


ATOM
2186
CG
MET
A
805
27.859
−2.865
15.589
1.00
33.42


ATOM
2187
SD
MET
A
805
28.125
−3.166
17.338
1.00
47.91


ATOM
2188
CE
MET
A
805
26.447
−3.244
17.925
1.00
28.62


ATOM
2189
C
MET
A
805
30.160
−2.268
12.542
1.00
11.31


ATOM
2190
O
MET
A
805
30.761
−1.259
12.908
1.00
12.42


ATOM
2191
N
ASN
A
806
30.530
−2.992
11.490
1.00
11.94


ATOM
2192
CA
ASN
A
806
31.726
−2.673
10.712
1.00
13.21


ATOM
2193
CB
ASN
A
806
32.537
−3.954
10.471
1.00
13.42


ATOM
2194
CG
ASN
A
806
33.907
−3.676
9.876
1.00
16.11


ATOM
2195
OD1
ASN
A
806
34.209
−2.549
9.484
1.00
17.92


ATOM
2196
ND2
ASN
A
806
34.740
−4.706
9.802
1.00
15.54


ATOM
2197
C
ASN
A
806
31.371
−2.023
9.374
1.00
14.20


ATOM
2198
O
ASN
A
806
30.988
−2.715
8.430
1.00
14.08


ATOM
2199
N
ARG
A
807
31.508
−0.699
9.296
1.00
12.56


ATOM
2200
CA
ARG
A
807
31.189
0.037
8.075
1.00
14.91


ATOM
2201
CB
ARG
A
807
31.410
1.543
8.275
1.00
16.99


ATOM
2202
CG
ARG
A
807
30.891
2.385
7.116
1.00
25.83


ATOM
2203
CD
ARG
A
807
31.162
3.881
7.280
1.00
30.30


ATOM
2204
NE
ARG
A
807
30.520
4.470
8.457
1.00
20.02


ATOM
2205
CZ
ARG
A
807
31.078
4.525
9.662
1.00
16.27


ATOM
2206
NH1
ARG
A
807
32.290
4.025
9.854
1.00
20.90


ATOM
2207
NH2
ARG
A
807
30.431
5.095
10.670
1.00
15.75


ATOM
2208
C
ARG
A
807
32.021
−0.442
6.889
1.00
13.89


ATOM
2209
O
ARG
A
807
31.573
−0.392
5.736
1.00
13.84


ATOM
2210
N
GLU
A
808
33.228
−0.910
7.177
1.00
11.68


ATOM
2211
CA
GLU
A
808
34.122
−1.397
6.137
1.00
17.06


ATOM
2212
CB
GLU
A
808
35.502
−1.675
6.731
1.00
16.87


ATOM
2213
CG
GLU
A
808
36.256
−0.394
7.085
1.00
22.64


ATOM
2214
CD
GLU
A
808
37.556
−0.645
7.819
1.00
24.85


ATOM
2215
OE1
GLU
A
808
38.293
−1.576
7.430
1.00
26.32


ATOM
2216
OE2
GLU
A
808
37.846
0.100
8.780
1.00
36.15


ATOM
2217
C
GLU
A
808
33.565
−2.641
5.461
1.00
15.58


ATOM
2218
O
GLU
A
808
33.929
−2.956
4.329
1.00
15.69


ATOM
2219
N
LYS
A
809
32.677
−3.343
6.156
1.00
14.84


ATOM
2220
CA
LYS
A
809
32.062
−4.544
5.600
1.00
16.67


ATOM
2221
CB
LYS
A
809
32.381
−5.765
6.478
1.00
12.30


ATOM
2222
CG
LYS
A
809
33.845
−6.184
6.405
1.00
13.87


ATOM
2223
CD
LYS
A
809
34.151
−7.408
7.259
1.00
14.82


ATOM
2224
CE
LYS
A
809
33.430
−8.641
6.745
1.00
25.64


ATOM
2225
NZ
LYS
A
809
33.789
−9.854
7.534
1.00
21.95


ATOM
2226
C
LYS
A
809
30.555
−4.363
5.445
1.00
15.95


ATOM
2227
O
LYS
A
809
29.770
−5.281
5.693
1.00
18.05


ATOM
2228
N
LYS
A
810
30.156
−3.167
5.022
1.00
15.13


ATOM
2229
CA
LYS
A
810
28.742
−2.867
4.828
1.00
16.24


ATOM
2230
CB
LYS
A
810
28.549
−1.383
4.494
1.00
14.35


ATOM
2231
CG
LYS
A
810
29.347
−0.869
3.312
1.00
24.48


ATOM
2232
CD
LYS
A
810
29.222
0.647
3.226
1.00
29.64


ATOM
2233
CE
LYS
A
810
29.994
1.224
2.049
1.00
35.68


ATOM
2234
NZ
LYS
A
810
29.432
0.786
0.746
1.00
42.39


ATOM
2235
C
LYS
A
810
28.139
−3.744
3.734
1.00
14.42


ATOM
2236
O
LYS
A
810
26.921
−3.843
3.607
1.00
14.44


ATOM
2237
N
ASN
A
811
28.995
−4.389
2.950
1.00
13.62


ATOM
2238
CA
ASN
A
811
28.511
−5.270
1.893
1.00
13.60


ATOM
2239
CB
ASN
A
811
29.680
−5.746
1.016
1.00
18.14


ATOM
2240
CG
ASN
A
811
30.815
−6.340
1.826
1.00
21.65


ATOM
2241
OD1
ASN
A
811
30.936
−7.559
1.958
1.00
17.54


ATOM
2242
ND2
ASN
A
811
31.651
−5.472
2.388
1.00
13.93


ATOM
2243
C
ASN
A
811
27.777
−6.474
2.487
1.00
14.60


ATOM
2244
O
ASN
A
811
27.084
−7.197
1.777
1.00
13.25


ATOM
2245
N
LYS
A
812
27.922
−6.677
3.796
1.00
14.05


ATOM
2246
CA
LYS
A
812
27.279
−7.797
4.478
1.00
15.17


ATOM
2247
CB
LYS
A
812
28.057
−8.150
5.753
1.00
15.23


ATOM
2248
CG
LYS
A
812
29.401
−8.803
5.500
1.00
20.27


ATOM
2249
CD
LYS
A
812
29.198
−10.137
4.817
1.00
28.44


ATOM
2250
CE
LYS
A
812
30.497
−10.886
4.658
1.00
35.44


ATOM
2251
NZ
LYS
A
812
30.257
−12.223
4.048
1.00
38.51


ATOM
2252
C
LYS
A
812
25.818
−7.542
4.859
1.00
15.78


ATOM
2253
O
LYS
A
812
25.109
−8.475
5.258
1.00
13.98


ATOM
2254
N
ILE
A
813
25.366
−6.297
4.724
1.00
14.64


ATOM
2255
CA
ILE
A
813
24.012
−5.964
5.144
1.00
14.83


ATOM
2256
CB
ILE
A
813
23.770
−4.460
5.007
1.00
15.21


ATOM
2257
CG2
ILE
A
813
22.264
−4.158
5.091
1.00
15.81


ATOM
2258
CG1
ILE
A
813
24.616
−3.740
6.073
1.00
13.99


ATOM
2259
CD1
ILE
A
813
24.445
−2.265
6.070
1.00
27.43


ATOM
2260
C
ILE
A
813
22.862
−6.792
4.546
1.00
14.67


ATOM
2261
O
ILE
A
813
22.042
−7.309
5.270
1.00
13.44


ATOM
2262
N
PRO
A
814
22.807
−6.936
3.224
1.00
12.07


ATOM
2263
CD
PRO
A
814
23.603
−6.274
2.191
1.00
14.86


ATOM
2264
CA
PRO
A
814
21.709
−7.724
2.623
1.00
14.39


ATOM
2265
CB
PRO
A
814
22.060
−7.714
1.152
1.00
13.45


ATOM
2266
CG
PRO
A
814
22.693
−6.351
1.001
1.00
14.67


ATOM
2267
C
PRO
A
814
21.605
−9.144
3.185
1.00
11.82


ATOM
2268
O
PRO
A
814
20.525
−9.603
3.570
1.00
12.87


ATOM
2269
N
SER
A
815
22.730
−9.846
3.215
1.00
11.71


ATOM
2270
CA
SER
A
815
22.730
−11.205
3.729
1.00
13.13


ATOM
2271
CB
SER
A
815
24.102
−11.863
3.526
1.00
14.66


ATOM
2272
OG
SER
A
815
25.124
−11.185
4.233
1.00
27.24


ATOM
2273
C
SER
A
815
22.366
−11.220
5.212
1.00
14.09


ATOM
2274
O
SER
A
815
21.677
−12.120
5.682
1.00
14.61


ATOM
2275
N
MET
A
816
22.809
−10.211
5.937
1.00
14.82


ATOM
2276
CA
MET
A
816
22.498
−10.197
7.353
1.00
14.08


ATOM
2277
CB
MET
A
816
23.449
−9.254
8.079
1.00
16.95


ATOM
2278
CG
MET
A
816
24.829
−9.872
8.232
1.00
19.08


ATOM
2279
SD
MET
A
816
26.019
−8.905
9.168
1.00
23.16


ATOM
2280
CE
MET
A
816
25.502
−9.310
10.812
1.00
29.41


ATOM
2281
C
MET
A
816
21.057
−9.838
7.628
1.00
12.78


ATOM
2282
O
MET
A
816
20.477
−10.281
8.613
1.00
13.06


ATOM
2283
N
GLN
A
817
20.464
−9.010
6.765
1.00
11.62


ATOM
2284
CA
GLN
A
817
19.061
−8.637
6.915
1.00
11.33


ATOM
2285
CB
GLN
A
817
18.666
−7.547
5.899
1.00
12.94


ATOM
2286
CG
GLN
A
817
19.186
−6.179
6.283
1.00
11.95


ATOM
2287
CD
GLN
A
817
18.469
−5.624
7.500
1.00
17.94


ATOM
2288
OE1
GLN
A
817
18.544
−6.183
8.595
1.00
34.56


ATOM
2289
NE2
GLN
A
817
17.759
−4.523
7.309
1.00
34.13


ATOM
2290
C
GLN
A
817
18.202
−9.882
6.714
1.00
13.31


ATOM
2291
O
GLN
A
817
17.254
−10.116
7.472
1.00
10.14


ATOM
2292
N
VAL
A
818
18.537
−10.698
5.715
1.00
12.18


ATOM
2293
CA
VAL
A
818
17.774
−11.918
5.479
1.00
11.53


ATOM
2294
CB
VAL
A
818
18.252
−12.659
4.210
1.00
13.56


ATOM
2295
CG1
VAL
A
818
17.500
−13.972
4.063
1.00
10.58


ATOM
2296
CG2
VAL
A
818
18.032
−11.781
2.982
1.00
17.92


ATOM
2297
C
VAL
A
818
17.903
−12.858
6.678
1.00
11.51


ATOM
2298
O
VAL
A
818
16.930
−13.494
7.090
1.00
12.55


ATOM
2299
N
GLY
A
819
19.110
−12.934
7.231
1.00
11.44


ATOM
2300
CA
GLY
A
819
19.356
−13.791
8.376
1.00
12.74


ATOM
2301
C
GLY
A
819
18.556
−13.335
9.579
1.00
13.96


ATOM
2302
O
GLY
A
819
18.068
−14.149
10.360
1.00
13.49


ATOM
2303
N
PHE
A
820
18.430
−12.022
9.725
1.00
14.20


ATOM
2304
CA
PHE
A
820
17.682
−11.426
10.825
1.00
11.70


ATOM
2305
CB
PHE
A
820
17.927
−9.913
10.833
1.00
11.32


ATOM
2306
CG
PHE
A
820
17.122
−9.167
11.858
1.00
9.99


ATOM
2307
CD1
PHE
A
820
17.268
−9.436
13.209
1.00
23.52


ATOM
2308
CD2
PHE
A
820
16.225
−8.184
11.466
1.00
17.26


ATOM
2309
CE1
PHE
A
820
16.529
−8.740
14.151
1.00
19.87


ATOM
2310
CE2
PHE
A
820
15.485
−7.488
12.403
1.00
16.59


ATOM
2311
CZ
PHE
A
820
15.640
−7.767
13.746
1.00
17.66


ATOM
2312
C
PHE
A
820
16.191
−11.731
10.651
1.00
12.70


ATOM
2313
O
PHE
A
820
15.498
−12.103
11.604
1.00
10.72


ATOM
2314
N
ILE
A
821
15.697
−11.571
9.429
1.00
10.04


ATOM
2315
CA
ILE
A
821
14.298
−11.850
9.150
1.00
9.29


ATOM
2316
CB
ILE
A
821
13.957
−11.540
7.679
1.00
10.14


ATOM
2317
CG2
ILE
A
821
12.617
−12.166
7.307
1.00
12.87


ATOM
2318
CG1
ILE
A
821
13.931
−10.022
7.479
1.00
12.03


ATOM
2319
CD1
ILE
A
821
13.795
−9.580
6.037
1.00
14.77


ATOM
2320
C
ILE
A
821
13.991
−13.311
9.462
1.00
11.67


ATOM
2321
O
ILE
A
821
13.012
−13.617
10.140
1.00
11.27


ATOM
2322
N
ASP
A
822
14.841
−14.215
8.985
1.00
11.97


ATOM
2323
CA
ASP
A
822
14.634
−15.637
9.237
1.00
14.30


ATOM
2324
CB
ASP
A
822
15.630
−16.479
8.428
1.00
17.59


ATOM
2325
CG
ASP
A
822
15.317
−16.499
6.942
1.00
17.92


ATOM
2326
OD1
ASP
A
822
14.177
−16.153
6.564
1.00
15.98


ATOM
2327
OD2
ASP
A
822
16.212
−16.880
6.152
1.00
13.97


ATOM
2328
C
ASP
A
822
14.759
−16.021
10.714
1.00
15.42


ATOM
2329
O
ASP
A
822
13.876
−16.671
11.275
1.00
16.53


ATOM
2330
N
ALA
A
823
15.849
−15.608
11.345
1.00
13.55


ATOM
2331
CA
ALA
A
823
16.101
−15.971
12.737
1.00
15.03


ATOM
2332
CB
ALA
A
823
17.580
−15.756
13.058
1.00
13.84


ATOM
2333
C
ALA
A
823
15.254
−15.299
13.810
1.00
15.13


ATOM
2334
O
ALA
A
823
14.907
−15.928
14.810
1.00
17.91


ATOM
2335
N
ILE
A
824
14.914
−14.032
13.606
1.00
13.91


ATOM
2336
CA
ILE
A
824
14.169
−13.281
14.611
1.00
14.87


ATOM
2337
CB
ILE
A
824
14.929
−11.971
14.966
1.00
16.51


ATOM
2338
CG2
ILE
A
824
14.085
−11.106
15.891
1.00
11.92


ATOM
2339
CG1
ILE
A
824
16.291
−12.293
15.589
1.00
19.03


ATOM
2340
CD1
ILE
A
824
16.211
−12.966
16.938
1.00
17.79


ATOM
2341
C
ILE
A
824
12.736
−12.872
14.271
1.00
15.38


ATOM
2342
O
ILE
A
824
11.817
−13.051
15.077
1.00
15.58


ATOM
2343
N
CYS
A
825
12.548
−12.332
13.074
1.00
11.66


ATOM
2344
CA
CYS
A
825
11.248
−11.798
12.682
1.00
10.83


ATOM
2345
CB
CYS
A
825
11.470
−10.717
11.629
1.00
14.06


ATOM
2346
SG
CYS
A
825
12.684
−9.498
12.156
1.00
12.72


ATOM
2347
C
CYS
A
825
10.094
−12.685
12.231
1.00
12.83


ATOM
2348
O
CYS
A
825
9.003
−12.606
12.792
1.00
11.78


ATOM
2349
N
LEU
A
826
10.312
−13.508
11.213
1.00
10.64


ATOM
2350
CA
LEU
A
826
9.230
−14.343
10.699
1.00
12.29


ATOM
2351
CB
LEU
A
826
9.759
−15.291
9.621
1.00
17.45


ATOM
2352
CG
LEU
A
826
10.132
−14.585
8.314
1.00
14.44


ATOM
2353
CD1
LEU
A
826
10.756
−15.585
7.355
1.00
19.69


ATOM
2354
CD2
LEU
A
826
8.884
−13.965
7.693
1.00
17.13


ATOM
2355
C
LEU
A
826
8.428
−15.131
11.735
1.00
11.75


ATOM
2356
O
LEU
A
826
7.194
−15.094
11.728
1.00
12.87


ATOM
2357
N
GLN
A
827
9.115
−15.842
12.620
1.00
9.56


ATOM
2358
CA
GLN
A
827
8.426
−16.637
13.632
1.00
10.96


ATOM
2359
CB
GLN
A
827
9.438
−17.368
14.507
1.00
9.95


ATOM
2360
CG
GLN
A
827
10.207
−18.465
13.805
1.00
14.60


ATOM
2361
CD
GLN
A
827
11.365
−18.949
14.646
1.00
27.21


ATOM
2362
OE1
GLN
A
827
12.420
−18.312
14.695
1.00
20.68


ATOM
2363
NE2
GLN
A
827
11.169
−20.068
15.335
1.00
24.19


ATOM
2364
C
GLN
A
827
7.516
−15.798
14.524
1.00
13.14


ATOM
2365
O
GLN
A
827
6.428
−16.235
14.906
1.00
13.21


ATOM
2366
N
LEU
A
828
7.966
−14.596
14.862
1.00
10.02


ATOM
2367
CA
LEU
A
828
7.182
−13.713
15.720
1.00
10.78


ATOM
2368
CB
LEU
A
828
8.037
−12.521
16.166
1.00
9.67


ATOM
2369
CG
LEU
A
828
7.315
−11.431
16.966
1.00
14.41


ATOM
2370
CD1
LEU
A
828
6.653
−12.048
18.185
1.00
16.13


ATOM
2371
CD2
LEU
A
828
8.300
−10.351
17.389
1.00
14.03


ATOM
2372
C
LEU
A
828
5.902
−13.218
15.036
1.00
11.55


ATOM
2373
O
LEU
A
828
4.814
−13.290
15.609
1.00
12.50


ATOM
2374
N
TYR
A
829
6.024
−12.717
13.812
1.00
10.38


ATOM
2375
CA
TYR
A
829
4.851
−12.217
13.109
1.00
11.38


ATOM
2376
CB
TYR
A
829
5.286
−11.392
11.892
1.00
9.07


ATOM
2377
CG
TYR
A
829
5.967
−10.112
12.324
1.00
13.32


ATOM
2378
CD1
TYR
A
829
5.298
−9.189
13.118
1.00
8.62


ATOM
2379
CE1
TYR
A
829
5.926
−8.037
13.569
1.00
10.58


ATOM
2380
CD2
TYR
A
829
7.290
−9.849
11.989
1.00
10.78


ATOM
2381
CE2
TYR
A
829
7.930
−8.699
12.440
1.00
8.02


ATOM
2382
CZ
TYR
A
829
7.241
−7.800
13.228
1.00
8.64


ATOM
2383
OH
TYR
A
829
7.867
−6.659
13.688
1.00
10.63


ATOM
2384
C
TYR
A
829
3.908
−13.349
12.731
1.00
12.07


ATOM
2385
O
TYR
A
829
2.704
−13.140
12.594
1.00
14.07


ATOM
2386
N
GLU
A
830
4.452
−14.555
12.585
1.00
14.19


ATOM
2387
CA
GLU
A
830
3.614
−15.709
12.274
1.00
14.53


ATOM
2388
CB
GLU
A
830
4.469
−16.919
11.881
1.00
15.21


ATOM
2389
CG
GLU
A
830
5.196
−16.751
10.557
1.00
18.48


ATOM
2390
CD
GLU
A
830
6.057
−17.948
10.208
1.00
27.35


ATOM
2391
OE1
GLU
A
830
6.422
−18.701
11.133
1.00
25.55


ATOM
2392
OE2
GLU
A
830
6.380
−18.127
9.014
1.00
25.64


ATOM
2393
C
GLU
A
830
2.806
−16.027
13.531
1.00
15.34


ATOM
2394
O
GLU
A
830
1.594
−16.245
13.462
1.00
15.05


ATOM
2395
N
ALA
A
831
3.484
−16.037
14.679
1.00
12.88


ATOM
2396
CA
ALA
A
831
2.836
−16.319
15.958
1.00
13.60


ATOM
2397
CB
ALA
A
831
3.877
−16.341
17.080
1.00
14.75


ATOM
2398
C
ALA
A
831
1.764
−15.279
16.264
1.00
14.36


ATOM
2399
O
ALA
A
831
0.666
−15.617
16.714
1.00
13.70


ATOM
2400
N
LEU
A
832
2.085
−14.010
16.026
1.00
11.70


ATOM
2401
CA
LEU
A
832
1.135
−12.935
16.276
1.00
12.90


ATOM
2402
CB
LEU
A
832
1.800
−11.577
16.030
1.00
12.02


ATOM
2403
CG
LEU
A
832
0.935
−10.334
16.256
1.00
13.07


ATOM
2404
CD1
LEU
A
832
0.367
−10.354
17.670
1.00
16.97


ATOM
2405
CD2
LEU
A
832
1.764
−9.076
16.018
1.00
12.70


ATOM
2406
C
LEU
A
832
−0.093
−13.098
15.382
1.00
13.07


ATOM
2407
O
LEU
A
832
−1.221
−12.851
15.811
1.00
12.63


ATOM
2408
N
THR
A
833
0.125
−13.522
14.140
1.00
10.33


ATOM
2409
CA
THR
A
833
−0.985
−13.720
13.213
1.00
11.65


ATOM
2410
CB
THR
A
833
−0.471
−14.019
11.798
1.00
15.54


ATOM
2411
OG1
THR
A
833
0.250
−12.881
11.309
1.00
13.44


ATOM
2412
CG2
THR
A
833
−1.631
−14.319
10.856
1.00
20.09


ATOM
2413
C
THR
A
833
−1.856
−14.875
13.709
1.00
13.24


ATOM
2414
O
THR
A
833
−3.070
−14.879
13.512
1.00
14.62


ATOM
2415
N
HIS
A
834
−1.233
−15.855
14.358
1.00
12.04


ATOM
2416
CA
HIS
A
834
−1.974
−16.988
14.901
1.00
15.35


ATOM
2417
CB
HIS
A
834
−1.010
−18.045
15.451
1.00
17.31


ATOM
2418
CG
HIS
A
834
−1.686
−19.161
16.174
1.00
21.70


ATOM
2419
CD2
HIS
A
834
−2.005
−20.422
15.792
1.00
27.35


ATOM
2420
ND1
HIS
A
834
−2.158
−19.040
17.471
1.00
27.23


ATOM
2421
CE1
HIS
A
834
−2.728
−20.162
17.843
1.00
22.73


ATOM
2422
NE2
HIS
A
834
−2.650
−21.026
16.836
1.00
26.03


ATOM
2423
C
HIS
A
834
−2.907
−16.495
16.011
1.00
16.43


ATOM
2424
O
HIS
A
834
−4.061
−16.917
16.101
1.00
16.32


ATOM
2425
N
VAL
A
835
−2.402
−15.600
16.852
1.00
14.39


ATOM
2426
CA
VAL
A
835
−3.201
−15.042
17.940
1.00
16.17


ATOM
2427
CB
VAL
A
835
−2.329
−14.177
18.879
1.00
20.06


ATOM
2428
CG1
VAL
A
835
−3.203
−13.433
19.878
1.00
26.18


ATOM
2429
CG2
VAL
A
835
−1.336
−15.067
19.616
1.00
22.85


ATOM
2430
C
VAL
A
835
−4.345
−14.196
17.376
1.00
18.30


ATOM
2431
O
VAL
A
835
−5.462
−14.219
17.899
1.00
16.68


ATOM
2432
N
SER
A
836
−4.061
−13.461
16.302
1.00
15.55


ATOM
2433
CA
SER
A
836
−5.060
−12.620
15.646
1.00
15.62


ATOM
2434
CB
SER
A
836
−5.081
−11.222
16.267
1.00
18.44


ATOM
2435
OG
SER
A
836
−6.092
−10.430
15.665
1.00
24.05


ATOM
2436
C
SER
A
836
−4.744
−12.516
14.153
1.00
15.03


ATOM
2437
O
SER
A
836
−3.754
−11.901
13.759
1.00
14.82


ATOM
2438
N
GLU
A
837
−5.596
−13.123
13.334
1.00
16.29


ATOM
2439
CA
GLU
A
837
−5.423
−13.139
11.886
1.00
16.40


ATOM
2440
CB
GLU
A
837
−6.578
−13.922
11.244
1.00
19.29


ATOM
2441
CG
GLU
A
837
−6.524
−14.017
9.722
1.00
30.56


ATOM
2442
CD
GLU
A
837
−5.259
−14.685
9.213
1.00
40.78


ATOM
2443
OE1
GLU
A
837
−4.925
−15.785
9.704
1.00
33.63


ATOM
2444
OE2
GLU
A
837
−4.603
−14.112
8.316
1.00
45.55


ATOM
2445
C
GLU
A
837
−5.324
−11.749
11.256
1.00
14.00


ATOM
2446
O
GLU
A
837
−4.672
−11.574
10.227
1.00
16.56


ATOM
2447
N
ASP
A
838
−5.967
−10.762
11.871
1.00
14.38


ATOM
2448
CA
ASP
A
838
−5.938
−9.402
11.349
1.00
12.78


ATOM
2449
CB
ASP
A
838
−6.990
−8.547
12.060
1.00
12.80


ATOM
2450
CG
ASP
A
838
−8.410
−8.929
11.669
1.00
31.66


ATOM
2451
OD1
ASP
A
838
−8.770
−8.750
10.487
1.00
25.15


ATOM
2452
OD2
ASP
A
838
−9.162
−9.414
12.540
1.00
29.94


ATOM
2453
C
ASP
A
838
−4.558
−8.751
11.468
1.00
11.81


ATOM
2454
O
ASP
A
838
−4.355
−7.625
11.017
1.00
12.87


ATOM
2455
N
CYS
A
839
−3.610
−9.456
12.080
1.00
14.34


ATOM
2456
CA
CYS
A
839
−2.254
−8.929
12.203
1.00
14.23


ATOM
2457
CB
CYS
A
839
−1.619
−9.354
13.533
1.00
12.27


ATOM
2458
SG
CYS
A
839
−2.115
−8.349
14.969
1.00
12.53


ATOM
2459
C
CYS
A
839
−1.412
−9.440
11.038
1.00
15.74


ATOM
2460
O
CYS
A
839
−0.222
−9.142
10.941
1.00
13.52


ATOM
2461
N
PHE
A
840
−2.044
−10.209
10.152
1.00
14.15


ATOM
2462
CA
PHE
A
840
−1.364
−10.765
8.983
1.00
14.85


ATOM
2463
CB
PHE
A
840
−2.370
−11.451
8.052
1.00
18.01


ATOM
2464
CG
PHE
A
840
−1.760
−11.926
6.764
1.00
16.92


ATOM
2465
CD1
PHE
A
840
−0.886
−13.001
6.751
1.00
13.52


ATOM
2466
CD2
PHE
A
840
−2.010
−11.257
5.575
1.00
19.38


ATOM
2467
CE1
PHE
A
840
−0.269
−13.398
5.575
1.00
23.30


ATOM
2468
CE2
PHE
A
840
−1.397
−11.649
4.396
1.00
23.75


ATOM
2469
CZ
PHE
A
840
−0.525
−12.720
4.397
1.00
22.76


ATOM
2470
C
PHE
A
840
−0.541
−9.768
8.155
1.00
13.70


ATOM
2471
O
PHE
A
840
0.546
−10.105
7.678
1.00
13.33


ATOM
2472
N
PRO
A
841
−1.049
−8.537
7.958
1.00
12.97


ATOM
2473
CD
PRO
A
841
−2.369
−8.002
8.339
1.00
14.47


ATOM
2474
CA
PRO
A
841
−0.294
−7.557
7.168
1.00
12.84


ATOM
2475
CB
PRO
A
841
−1.127
−6.287
7.312
1.00
14.37


ATOM
2476
CG
PRO
A
841
−2.533
−6.826
7.391
1.00
14.58


ATOM
2477
C
PRO
A
841
1.151
−7.367
7.630
1.00
14.54


ATOM
2478
O
PRO
A
841
2.034
−7.065
6.826
1.00
13.75


ATOM
2479
N
LEU
A
842
1.393
−7.530
8.926
1.00
11.66


ATOM
2480
CA
LEU
A
842
2.747
−7.384
9.444
1.00
12.35


ATOM
2481
CB
LEU
A
842
2.732
−7.430
10.977
1.00
11.85


ATOM
2482
CG
LEU
A
842
2.039
−6.228
11.624
1.00
12.78


ATOM
2483
CD1
LEU
A
842
1.900
−6.434
13.131
1.00
14.23


ATOM
2484
CD2
LEU
A
842
2.837
−4.975
11.321
1.00
14.25


ATOM
2485
C
LEU
A
842
3.613
−8.513
8.880
1.00
13.95


ATOM
2486
O
LEU
A
842
4.741
−8.290
8.444
1.00
13.84


ATOM
2487
N
LEU
A
843
3.067
−9.727
8.882
1.00
11.90


ATOM
2488
CA
LEU
A
843
3.779
−10.889
8.359
1.00
11.64


ATOM
2489
CB
LEU
A
843
2.995
−12.161
8.670
1.00
10.07


ATOM
2490
CG
LEU
A
843
3.532
−13.468
8.084
1.00
9.50


ATOM
2491
CD1
LEU
A
843
4.940
−13.735
8.588
1.00
13.64


ATOM
2492
CD2
LEU
A
843
2.597
−14.608
8.466
1.00
12.37


ATOM
2493
C
LEU
A
843
3.971
−10.751
6.847
1.00
11.74


ATOM
2494
O
LEU
A
843
5.054
−11.003
6.319
1.00
13.14


ATOM
2495
N
ASP
A
844
2.909
−10.342
6.160
1.00
13.31


ATOM
2496
CA
ASP
A
844
2.943
−10.154
4.711
1.00
14.45


ATOM
2497
CB
ASP
A
844
1.573
−9.639
4.245
1.00
18.19


ATOM
2498
CG
ASP
A
844
1.354
−9.771
2.739
1.00
13.51


ATOM
2499
OD1
ASP
A
844
2.141
−10.459
2.057
1.00
18.86


ATOM
2500
OD2
ASP
A
844
0.367
−9.187
2.243
1.00
17.91


ATOM
2501
C
ASP
A
844
4.053
−9.153
4.366
1.00
13.87


ATOM
2502
O
ASP
A
844
4.854
−9.386
3.460
1.00
13.07


ATOM
2503
N
GLY
A
845
4.100
−8.046
5.104
1.00
12.67


ATOM
2504
CA
GLY
A
845
5.115
−7.035
4.862
1.00
11.69


ATOM
2505
C
GLY
A
845
6.529
−7.540
5.097
1.00
11.05


ATOM
2506
O
GLY
A
845
7.447
−7.240
4.330
1.00
12.51


ATOM
2507
N
CYS
A
846
6.704
−8.314
6.161
1.00
10.28


ATOM
2508
CA
CYS
A
846
8.005
−8.882
6.507
1.00
10.93


ATOM
2509
CB
CYS
A
846
7.889
−9.643
7.831
1.00
14.58


ATOM
2510
SG
CYS
A
846
9.443
−10.273
8.485
1.00
12.82


ATOM
2511
C
CYS
A
846
8.497
−9.821
5.398
1.00
11.92


ATOM
2512
O
CYS
A
846
9.661
−9.762
4.985
1.00
11.24


ATOM
2513
N
ARG
A
847
7.605
−10.683
4.914
1.00
12.77


ATOM
2514
CA
ARG
A
847
7.953
−11.618
3.853
1.00
13.72


ATOM
2515
CB
ARG
A
847
6.762
−12.527
3.535
1.00
11.63


ATOM
2516
CG
ARG
A
847
6.457
−13.545
4.619
1.00
13.10


ATOM
2517
CD
ARG
A
847
5.180
−14.308
4.316
1.00
17.35


ATOM
2518
NE
ARG
A
847
4.978
−15.402
5.262
1.00
19.23


ATOM
2519
CZ
ARG
A
847
3.840
−16.077
5.389
1.00
21.47


ATOM
2520
NH1
ARG
A
847
2.796
−15.769
4.632
1.00
24.29


ATOM
2521
NH2
ARG
A
847
3.750
−17.059
6.275
1.00
27.21


ATOM
2522
C
ARG
A
847
8.371
−10.870
2.592
1.00
13.53


ATOM
2523
O
ARG
A
847
9.320
−11.265
1.906
1.00
13.20


ATOM
2524
N
LYS
A
848
7.659
−9.793
2.283
1.00
12.35


ATOM
2525
CA
LYS
A
848
7.977
−9.007
1.099
1.00
14.65


ATOM
2526
CB
LYS
A
848
6.925
−7.915
0.880
1.00
16.22


ATOM
2527
CG
LYS
A
848
5.567
−8.447
0.413
1.00
14.77


ATOM
2528
CD
LYS
A
848
4.579
−7.308
0.195
1.00
19.65


ATOM
2529
CE
LYS
A
848
3.210
−7.817
−0.206
1.00
19.42


ATOM
2530
NZ
LYS
A
848
2.214
−6.709
−0.212
1.00
23.11


ATOM
2531
C
LYS
A
848
9.364
−8.392
1.229
1.00
14.80


ATOM
2532
O
LYS
A
848
10.112
−8.319
0.253
1.00
13.12


ATOM
2533
N
ASN
A
849
9.713
−7.953
2.435
1.00
13.42


ATOM
2534
CA
ASN
A
849
11.034
−7.369
2.648
1.00
13.07


ATOM
2535
CB
ASN
A
849
11.086
−6.646
3.995
1.00
13.67


ATOM
2536
CG
ASN
A
849
10.412
−5.288
3.950
1.00
17.85


ATOM
2537
OD1
ASN
A
849
9.863
−4.821
4.949
1.00
16.87


ATOM
2538
ND2
ASN
A
849
10.461
−4.638
2.790
1.00
13.21


ATOM
2539
C
ASN
A
849
12.122
−8.434
2.568
1.00
12.00


ATOM
2540
O
ASN
A
849
13.252
−8.148
2.165
1.00
11.88


ATOM
2541
N
ARG
A
850
11.797
−9.667
2.945
1.00
11.53


ATOM
2542
CA
ARG
A
850
12.793
−10.729
2.860
1.00
11.98


ATOM
2543
CB
ARG
A
850
12.285
−12.037
3.473
1.00
14.13


ATOM
2544
CG
ARG
A
850
13.373
−13.110
3.508
1.00
13.55


ATOM
2545
CD
ARG
A
850
12.838
−14.511
3.781
1.00
18.02


ATOM
2546
NE
ARG
A
850
13.930
−15.457
4.001
1.00
16.95


ATOM
2547
CZ
ARG
A
850
14.743
−15.919
3.052
1.00
14.40


ATOM
2548
NH1
ARG
A
850
14.595
−15.533
1.790
1.00
16.03


ATOM
2549
NH2
ARG
A
850
15.727
−16.754
3.373
1.00
12.51


ATOM
2550
C
ARG
A
850
13.138
−10.972
1.399
1.00
13.81


ATOM
2551
O
ARG
A
850
14.304
−11.151
1.054
1.00
15.14


ATOM
2552
N
GLN
A
851
12.118
−10.985
0.542
1.00
16.03


ATOM
2553
CA
GLN
A
851
12.317
−11.193
−0.892
1.00
15.42


ATOM
2554
CB
GLN
A
851
10.969
−11.156
−1.622
1.00
17.30


ATOM
2555
CG
GLN
A
851
11.039
−11.399
−3.127
1.00
30.46


ATOM
2556
CD
GLN
A
851
11.475
−10.174
−3.912
1.00
34.81


ATOM
2557
OE1
GLN
A
851
10.862
−9.110
−3.814
1.00
37.41


ATOM
2558
NE2
GLN
A
851
12.534
−10.320
−4.704
1.00
40.89


ATOM
2559
C
GLN
A
851
13.229
−10.109
−1.436
1.00
16.49


ATOM
2560
O
GLN
A
851
14.151
−10.371
−2.208
1.00
15.70


ATOM
2561
N
LYS
A
852
12.953
−8.867
−1.014
1.00
15.86


ATOM
2562
CA
LYS
A
852
13.705
−7.685
−1.428
1.00
16.63


ATOM
2563
CB
LYS
A
852
13.065
−6.405
−0.838
1.00
13.58


ATOM
2564
CG
LYS
A
852
11.802
−6.008
−1.561
1.00
18.37


ATOM
2565
CD
LYS
A
852
12.183
−5.582
−2.958
1.00
31.95


ATOM
2566
CE
LYS
A
852
11.002
−5.087
−3.751
1.00
37.83


ATOM
2567
NZ
LYS
A
852
11.421
−4.599
−5.099
1.00
41.92


ATOM
2568
C
LYS
A
852
15.175
−7.754
−1.037
1.00
15.46


ATOM
2569
O
LYS
A
852
16.055
−7.542
−1.874
1.00
14.58


ATOM
2570
N
TRP
A
853
15.446
−8.063
0.225
1.00
12.99


ATOM
2571
CA
TRP
A
853
16.821
−8.168
0.705
1.00
12.72


ATOM
2572
CB
TRP
A
853
16.843
−8.299
2.228
1.00
11.94


ATOM
2573
CG
TRP
A
853
16.640
−7.011
2.957
1.00
11.40


ATOM
2574
CD2
TRP
A
853
17.485
−5.864
2.913
1.00
14.74


ATOM
2575
CE2
TRP
A
853
16.929
−4.888
3.763
1.00
12.41


ATOM
2576
CE3
TRP
A
853
18.675
−5.554
2.236
1.00
10.90


ATOM
2577
CD1
TRP
A
853
15.618
−6.701
3.813
1.00
11.02


ATOM
2578
NE1
TRP
A
853
15.781
−5.429
4.303
1.00
14.15


ATOM
2579
CZ2
TRP
A
853
17.502
−3.638
3.958
1.00
12.03


ATOM
2580
CZ3
TRP
A
853
19.246
−4.312
2.427
1.00
13.77


ATOM
2581
CH2
TRP
A
853
18.663
−3.370
3.280
1.00
16.08


ATOM
2582
C
TRP
A
853
17.543
−9.357
0.074
1.00
13.55


ATOM
2583
O
TRP
A
853
18.722
−9.265
−0.282
1.00
13.19


ATOM
2584
N
GLN
A
854
16.836
−10.472
−0.062
1.00
12.06


ATOM
2585
CA
GLN
A
854
17.427
−11.667
−0.657
1.00
13.49


ATOM
2586
CB
GLN
A
854
16.426
−12.822
−0.630
1.00
13.86


ATOM
2587
CG
GLN
A
854
16.934
−14.128
−1.242
1.00
15.91


ATOM
2588
CD
GLN
A
854
18.267
−14.585
−0.665
1.00
23.66


ATOM
2589
OE1
GLN
A
854
18.544
−14.404
0.520
1.00
20.44


ATOM
2590
NE2
GLN
A
854
19.091
−15.199
−1.504
1.00
26.84


ATOM
2591
C
GLN
A
854
17.869
−11.400
−2.094
1.00
13.14


ATOM
2592
O
GLN
A
854
18.920
−11.880
−2.524
1.00
15.55


ATOM
2593
N
ALA
A
855
17.069
−10.635
−2.832
1.00
14.63


ATOM
2594
CA
ALA
A
855
17.408
−10.318
−4.219
1.00
15.08


ATOM
2595
CB
ALA
A
855
16.264
−9.563
−4.884
1.00
17.06


ATOM
2596
C
ALA
A
855
18.697
−9.504
−4.303
1.00
16.23


ATOM
2597
O
ALA
A
855
19.439
−9.611
−5.278
1.00
17.06


ATOM
2598
N
LEU
A
856
18.959
−8.689
−3.287
1.00
15.11


ATOM
2599
CA
LEU
A
856
20.178
−7.889
−3.261
1.00
17.23


ATOM
2600
CB
LEU
A
856
20.031
−6.715
−2.284
1.00
11.53


ATOM
2601
CG
LEU
A
856
18.968
−5.676
−2.643
1.00
15.60


ATOM
2602
CD1
LEU
A
856
18.996
−4.549
−1.634
1.00
19.73


ATOM
2603
CD2
LEU
A
856
19.226
−5.145
−4.047
1.00
12.95


ATOM
2604
C
LEU
A
856
21.362
−8.754
−2.835
1.00
17.35


ATOM
2605
O
LEU
A
856
22.478
−8.601
−3.337
1.00
17.30


ATOM
2606
N
ALA
A
857
21.109
−9.674
−1.911
1.00
16.52


ATOM
2607
CA
ALA
A
857
22.156
−10.545
−1.396
1.00
17.82


ATOM
2608
CB
ALA
A
857
21.708
−11.155
−0.079
1.00
15.78


ATOM
2609
C
ALA
A
857
22.616
−11.651
−2.339
1.00
19.95


ATOM
2610
O
ALA
A
857
23.781
−12.048
−2.305
1.00
21.30


ATOM
2611
N
GLU
A
858
21.715
−12.144
−3.181
1.00
19.75


ATOM
2612
CA
GLU
A
858
22.059
−13.233
−4.091
1.00
23.14


ATOM
2613
CB
GLU
A
858
20.798
−14.008
−4.475
1.00
28.23


ATOM
2614
CG
GLU
A
858
19.735
−13.155
−5.139
1.00
35.46


ATOM
2615
CD
GLU
A
858
18.516
−13.957
−5.548
1.00
41.30


ATOM
2616
OE1
GLU
A
858
17.928
−14.635
−4.679
1.00
46.06


ATOM
2617
OE2
GLU
A
858
18.144
−13.905
−6.739
1.00
53.40


ATOM
2618
C
GLU
A
858
22.773
−12.775
−5.356
1.00
24.66


ATOM
2619
O
GLU
A
858
22.769
−11.561
−5.640
1.00
27.06


ATOM
2620
OXT
GLU
A
858
23.319
−13.654
−6.053
1.00
33.90


TER
2621

GLU
A
858


ATOM
2622
O
HOH
W
1
14.659
12.373
18.930
1.00
11.90


ATOM
2623
O
HOH
W
2
9.029
0.616
15.467
1.00
15.60


ATOM
2624
O
HOH
W
3
17.339
−0.310
24.269
1.00
9.87


ATOM
2625
O
HOH
W
4
17.787
8.492
22.312
1.00
9.91


ATOM
2626
O
HOH
W
5
22.322
0.101
41.405
1.00
10.58


ATOM
2627
O
HOH
W
6
7.037
−4.929
2.938
1.00
15.52


ATOM
2628
O
HOH
W
7
24.844
0.942
17.890
1.00
12.19


ATOM
2629
O
HOH
W
8
17.812
−5.285
21.940
1.00
13.09


ATOM
2630
O
HOH
W
9
19.355
−1.244
21.749
1.00
11.09


ATOM
2631
O
HOH
W
10
11.998
−15.929
13.123
1.00
15.08


ATOM
2632
O
HOH
W
11
17.595
6.868
5.858
1.00
17.40


ATOM
2633
O
HOH
W
12
20.522
−8.124
28.490
1.00
16.30


ATOM
2634
O
HOH
W
13
7.122
8.426
30.706
1.00
12.74


ATOM
2635
O
HOH
W
14
14.281
−0.736
24.882
1.00
10.20


ATOM
2636
O
HOH
W
15
27.778
−4.812
7.714
1.00
14.34


ATOM
2637
O
HOH
W
16
45.697
−5.856
19.373
1.00
13.79


ATOM
2638
O
HOH
W
17
32.028
0.851
11.859
1.00
12.49


ATOM
2639
O
HOH
W
18
12.716
−7.833
22.260
1.00
11.62


ATOM
2640
O
HOH
W
19
20.770
−7.019
24.953
1.00
13.66


ATOM
2641
O
HOH
W
20
9.679
−8.387
30.457
1.00
18.04


ATOM
2642
O
HOH
W
21
20.996
−1.566
19.584
1.00
15.27


ATOM
2643
O
HOH
W
22
5.367
−8.570
29.548
1.00
17.36


ATOM
2644
O
HOH
W
23
25.138
−9.337
1.725
1.00
17.63


ATOM
2645
O
HOH
W
24
−9.020
−0.116
43.708
1.00
15.91


ATOM
2646
O
HOH
W
25
22.657
−6.174
29.194
1.00
17.18


ATOM
2647
O
HOH
W
26
−4.280
19.557
21.192
1.00
19.85


ATOM
2648
O
HOH
W
27
14.289
6.604
13.852
1.00
14.85


ATOM
2649
O
HOH
W
28
11.411
−1.302
13.935
1.00
12.80


ATOM
2650
O
HOH
W
29
11.700
13.882
15.200
1.00
14.97


ATOM
2651
O
HOH
W
30
18.410
10.076
12.196
1.00
19.59


ATOM
2652
O
HOH
W
31
26.709
7.571
23.378
1.00
17.44


ATOM
2653
O
HOH
W
32
25.420
5.805
17.773
1.00
17.40


ATOM
2654
O
HOH
W
33
11.087
10.589
10.070
1.00
17.81


ATOM
2655
O
HOH
W
34
11.500
−19.954
26.231
1.00
16.07


ATOM
2656
O
HOH
W
35
−5.204
−5.042
34.106
1.00
17.24


ATOM
2657
O
HOH
W
36
1.941
9.940
36.428
1.00
13.95


ATOM
2658
O
HOH
W
37
23.916
7.238
15.924
1.00
14.00


ATOM
2659
O
HOH
W
38
4.522
21.473
19.911
1.00
20.60


ATOM
2660
O
HOH
W
39
7.654
32.374
24.586
1.00
19.77


ATOM
2661
O
HOH
W
40
−11.105
8.617
12.732
1.00
20.19


ATOM
2662
O
HOH
W
41
14.266
14.289
20.855
1.00
16.50


ATOM
2663
O
HOH
W
42
27.797
−9.140
13.072
1.00
17.28


ATOM
2664
O
HOH
W
43
13.361
−5.781
20.636
1.00
17.62


ATOM
2665
O
HOH
W
44
9.439
17.952
22.920
1.00
20.34


ATOM
2666
O
HOH
W
45
13.506
−19.339
23.851
1.00
17.51


ATOM
2667
O
HOH
W
46
−9.608
−2.484
44.794
1.00
18.03


ATOM
2668
O
HOH
W
47
19.179
−3.517
23.479
1.00
14.63


ATOM
2669
O
HOH
W
48
20.825
−1.771
7.357
1.00
15.56


ATOM
2670
O
HOH
W
49
3.953
−2.401
8.103
1.00
15.98


ATOM
2671
O
HOH
W
50
5.164
2.828
12.389
1.00
17.57


ATOM
2672
O
HOH
W
51
22.475
−6.004
8.390
1.00
20.31


ATOM
2673
O
HOH
W
52
−1.505
−7.713
3.922
1.00
20.93


ATOM
2674
O
HOH
W
53
16.030
13.344
15.066
1.00
22.86


ATOM
2675
O
HOH
W
54
3.120
33.114
17.327
1.00
18.81


ATOM
2676
O
HOH
W
55
6.517
19.676
19.112
1.00
20.43


ATOM
2677
O
HOH
W
56
27.812
5.941
11.269
1.00
19.39


ATOM
2678
O
HOH
W
57
14.704
9.138
12.638
1.00
17.37


ATOM
2679
O
HOH
W
58
10.813
−19.129
28.734
1.00
23.50


ATOM
2680
O
HOH
W
59
9.603
−13.958
1.403
1.00
20.05


ATOM
2681
O
HOH
W
60
46.209
−3.550
17.835
1.00
18.22


ATOM
2682
O
HOH
W
61
24.760
−2.396
10.006
1.00
20.80


ATOM
2683
O
HOH
W
62
11.077
3.087
12.585
1.00
21.05


ATOM
2684
O
HOH
W
63
10.534
−10.726
28.998
1.00
21.18


ATOM
2685
O
HOH
W
64
−0.961
−11.064
33.440
1.00
18.63


ATOM
2686
O
HOH
W
65
20.890
0.577
15.388
1.00
19.77


ATOM
2687
O
HOH
W
66
21.685
13.866
20.281
1.00
24.54


ATOM
2688
O
HOH
W
67
−5.012
−3.878
8.180
1.00
21.24


ATOM
2689
O
HOH
W
68
−10.443
9.371
15.194
1.00
19.03


ATOM
2690
O
HOH
W
69
26.635
8.578
39.152
1.00
19.48


ATOM
2691
O
HOH
W
70
21.837
−4.044
23.094
1.00
14.46


ATOM
2692
O
HOH
W
71
18.979
0.534
3.275
1.00
19.32


ATOM
2693
O
HOH
W
72
−7.687
−4.529
35.484
1.00
19.76


ATOM
2694
O
HOH
W
73
−4.441
9.972
35.483
1.00
21.75


ATOM
2695
O
HOH
W
74
22.147
0.611
18.233
1.00
21.06


ATOM
2696
O
HOH
W
75
25.625
7.694
19.834
1.00
17.79


ATOM
2697
O
HOH
W
76
−9.716
14.941
11.027
1.00
20.22


ATOM
2698
O
HOH
W
77
14.015
−1.710
16.866
1.00
19.03


ATOM
2699
O
HOH
W
78
21.861
−3.953
20.354
1.00
17.68


ATOM
2700
O
HOH
W
79
21.854
−11.471
10.659
1.00
21.05


ATOM
2701
O
HOH
W
80
15.795
−5.944
−4.295
1.00
17.34


ATOM
2702
O
HOH
W
81
26.427
−5.333
20.748
1.00
28.65


ATOM
2703
O
HOH
W
82
0.806
16.637
36.547
1.00
22.11


ATOM
2704
O
HOH
W
83
28.883
5.909
33.300
1.00
35.99


ATOM
2705
O
HOH
W
84
0.615
−5.836
36.804
1.00
21.63


ATOM
2706
O
HOH
W
85
14.416
−12.696
−3.692
1.00
22.36


ATOM
2707
O
HOH
W
86
−4.841
7.644
43.980
1.00
19.92


ATOM
2708
O
HOH
W
87
−6.059
5.564
10.293
1.00
22.49


ATOM
2709
O
HOH
W
88
7.210
1.031
13.002
1.00
19.78


ATOM
2710
O
HOH
W
89
−5.786
−6.329
9.023
1.00
20.32


ATOM
2711
O
HOH
W
90
19.117
4.909
35.027
1.00
17.30


ATOM
2712
O
HOH
W
91
10.592
13.017
38.293
1.00
23.66


ATOM
2713
O
HOH
W
92
−9.801
5.234
16.132
1.00
20.64


ATOM
2714
O
HOH
W
93
−6.370
−17.172
24.540
1.00
23.65


ATOM
2715
O
HOH
W
94
−6.833
1.342
45.207
1.00
17.92


ATOM
2716
O
HOH
W
95
33.715
−7.279
11.000
1.00
17.67


ATOM
2717
O
HOH
W
96
5.722
31.659
29.252
1.00
19.35


ATOM
2718
O
HOH
W
97
14.155
−2.890
10.083
1.00
16.30


ATOM
2719
O
HOH
W
98
19.709
−5.898
20.414
1.00
27.45


ATOM
2720
O
HOH
W
99
4.418
−3.958
2.629
1.00
23.70


ATOM
2721
O
HOH
W
100
5.739
5.419
41.566
1.00
26.30


ATOM
2722
O
HOH
W
101
1.882
−10.334
12.547
1.00
21.56


ATOM
2723
O
HOH
W
102
1.506
9.558
7.516
1.00
21.76


ATOM
2724
O
HOH
W
103
23.211
1.757
4.698
1.00
23.21


ATOM
2725
O
HOH
W
104
36.282
2.363
9.440
1.00
27.13


ATOM
2726
O
HOH
W
105
27.600
−11.267
2.472
1.00
18.59


ATOM
2727
O
HOH
W
106
16.305
16.757
22.862
1.00
25.14


ATOM
2728
O
HOH
W
107
21.223
−0.443
4.807
1.00
20.51


ATOM
2729
O
HOH
W
108
12.939
13.840
12.680
1.00
26.10


ATOM
2730
O
HOH
W
109
10.191
−9.652
24.549
1.00
17.97


ATOM
2731
O
HOH
W
110
9.527
−19.990
11.160
1.00
34.52


ATOM
2732
O
HOH
W
111
2.300
−4.117
6.982
1.00
21.40


ATOM
2733
O
HOH
W
112
31.807
5.599
25.384
1.00
19.28


ATOM
2734
O
HOH
W
113
11.858
5.625
12.858
1.00
18.80


ATOM
2735
O
HOH
W
114
2.975
3.851
3.583
1.00
28.02


ATOM
2736
O
HOH
W
115
22.328
−3.325
9.278
1.00
18.13


ATOM
2737
O
HOH
W
116
7.581
21.278
17.210
1.00
26.33


ATOM
2738
O
HOH
W
117
−8.959
18.330
19.702
1.00
25.41


ATOM
2739
O
HOH
W
118
−7.913
−3.625
46.688
1.00
16.16


ATOM
2740
O
HOH
W
119
29.369
−4.122
35.016
1.00
21.35


ATOM
2741
O
HOH
W
120
−10.313
4.301
39.676
1.00
20.84


ATOM
2742
O
HOH
W
121
36.288
−8.163
10.383
1.00
29.41


ATOM
2743
O
HOH
W
122
−5.305
0.154
7.066
1.00
32.03


ATOM
2744
O
HOH
W
123
15.892
9.345
6.948
1.00
31.98


ATOM
2745
O
HOH
W
124
−7.934
−11.981
26.594
1.00
24.88


ATOM
2746
O
HOH
W
125
−7.700
−14.762
14.417
1.00
27.16


ATOM
2747
O
HOH
W
126
7.924
19.345
32.073
1.00
27.10


ATOM
2748
O
HOH
W
127
22.963
−15.271
−0.194
1.00
34.57


ATOM
2749
O
HOH
W
128
14.018
4.418
0.344
1.00
27.94


ATOM
2750
O
HOH
W
129
13.334
16.377
17.301
1.00
27.05


ATOM
2751
O
HOH
W
130
30.641
−11.391
0.176
1.00
21.79


ATOM
2752
O
HOH
W
131
−5.143
−9.116
6.397
1.00
26.22


ATOM
2753
O
HOH
W
132
44.452
2.118
22.189
1.00
25.35


ATOM
2754
O
HOH
W
133
−0.942
−8.268
32.526
1.00
21.73


ATOM
2755
O
HOH
W
134
32.286
8.100
17.531
1.00
30.18


ATOM
2756
O
HOH
W
135
4.471
−22.268
17.254
1.00
22.18


ATOM
2757
O
HOH
W
136
20.964
−7.154
10.051
1.00
23.34


ATOM
2758
O
HOH
W
137
−6.984
26.107
22.746
1.00
26.33


ATOM
2759
O
HOH
W
138
17.856
14.348
24.807
1.00
20.33


ATOM
2760
O
HOH
W
139
10.038
−5.546
41.193
1.00
26.62


ATOM
2761
O
HOH
W
140
13.989
13.837
16.687
1.00
27.53


ATOM
2762
O
HOH
W
141
23.629
−13.084
9.502
1.00
28.21


ATOM
2763
O
HOH
W
142
31.635
7.713
14.307
1.00
30.30


ATOM
2764
O
HOH
W
143
6.811
−2.344
−0.868
1.00
24.47


ATOM
2765
O
HOH
W
144
7.278
−9.981
30.756
1.00
27.03


ATOM
2766
O
HOH
W
145
−6.981
7.089
6.281
1.00
26.94


ATOM
2767
O
HOH
W
146
−8.635
18.558
29.861
1.00
27.91


ATOM
2768
O
HOH
W
147
30.525
−1.680
34.334
1.00
24.09


ATOM
2769
O
HOH
W
148
2.251
−13.867
2.121
1.00
25.49


ATOM
2770
O
HOH
W
149
−8.063
−9.740
29.191
1.00
24.34


ATOM
2771
O
HOH
W
150
−1.333
15.279
37.020
1.00
28.81


ATOM
2772
O
HOH
W
151
18.429
15.610
21.408
1.00
22.50


ATOM
2773
O
HOH
W
152
13.471
−4.264
12.528
1.00
19.38


ATOM
2774
O
HOH
W
153
18.621
−17.600
7.222
1.00
21.52


ATOM
2775
O
HOH
W
154
19.181
−5.396
13.023
1.00
33.83


ATOM
2776
O
HOH
W
155
−3.698
−11.419
33.622
1.00
22.32


ATOM
2777
O
HOH
W
156
24.773
−7.687
26.828
1.00
25.23


ATOM
2778
O
HOH
W
157
11.338
6.981
10.450
1.00
25.98


ATOM
2779
O
HOH
W
158
7.187
4.097
9.722
1.00
25.73


ATOM
2780
O
HOH
W
159
10.571
18.276
18.940
1.00
26.56


ATOM
2781
O
HOH
W
160
29.444
8.138
18.655
1.00
25.10


ATOM
2782
O
HOH
W
161
−4.733
−16.782
12.321
1.00
23.51


ATOM
2783
O
HOH
W
162
24.194
7.218
40.602
1.00
28.88


ATOM
2784
O
HOH
W
163
13.925
−7.040
−5.961
1.00
29.58


ATOM
2785
O
HOH
W
164
−8.456
17.425
10.469
1.00
25.03


ATOM
2786
O
HOH
W
165
20.283
7.809
6.109
1.00
25.58


ATOM
2787
O
HOH
W
166
11.226
1.360
14.389
1.00
28.28


ATOM
2788
O
HOH
W
167
17.600
11.985
25.766
1.00
28.21


ATOM
2789
O
HOH
W
168
−1.369
0.364
6.150
1.00
26.61


ATOM
2790
O
HOH
W
169
1.250
6.912
6.112
1.00
22.96


ATOM
2791
O
HOH
W
170
13.982
16.820
19.827
1.00
26.70


ATOM
2792
O
HOH
W
171
8.401
6.117
8.285
1.00
29.37


ATOM
2793
O
HOH
W
172
1.561
32.980
20.315
1.00
25.71


ATOM
2794
O
HOH
W
173
8.687
−4.960
0.724
1.00
20.63


ATOM
2795
O
HOH
W
174
16.762
−8.584
32.541
1.00
22.53


ATOM
2796
O
HOH
W
175
−8.928
23.790
25.122
1.00
26.68


ATOM
2797
O
HOH
W
176
30.774
−10.692
12.781
1.00
29.33


ATOM
2798
O
HOH
W
177
−4.491
−0.583
48.435
1.00
27.59


ATOM
2799
O
HOH
W
178
−10.254
8.887
25.677
1.00
27.41


ATOM
2800
O
HOH
W
179
12.487
−14.347
0.366
1.00
29.02


ATOM
2801
O
HOH
W
180
−2.194
−3.193
5.572
1.00
37.26


ATOM
2802
O
HOH
W
181
21.240
−14.747
4.723
1.00
24.12


ATOM
2803
O
HOH
W
182
25.238
15.872
21.083
1.00
33.15


ATOM
2804
O
HOH
W
183
27.650
8.541
12.497
1.00
23.15


ATOM
2805
O
HOH
W
184
35.303
3.837
26.688
1.00
23.28


ATOM
2806
O
HOH
W
185
−3.730
14.555
34.107
1.00
23.34


ATOM
2807
O
HOH
W
186
−8.927
−4.660
10.381
1.00
28.70


ATOM
2808
O
HOH
W
187
40.695
−1.179
15.166
1.00
31.35


ATOM
2809
O
HOH
W
188
−0.356
−22.615
31.607
1.00
35.28


ATOM
2810
O
HOH
W
189
3.463
34.674
22.382
1.00
27.20


ATOM
2811
O
HOH
W
190
8.911
2.196
11.376
1.00
19.30


ATOM
2812
O
HOH
W
191
−2.598
−24.115
28.861
1.00
26.04


ATOM
2813
O
HOH
W
192
8.418
−15.510
34.179
1.00
38.02


ATOM
2814
O
HOH
W
193
15.703
−17.633
−0.060
1.00
35.88


ATOM
2815
O
HOH
W
194
32.518
0.997
3.614
1.00
34.25


ATOM
2816
O
HOH
W
195
19.062
−16.798
10.198
1.00
27.69


ATOM
2817
O
HOH
W
196
13.216
8.976
10.392
1.00
27.61


ATOM
2818
O
HOH
W
197
2.647
−0.086
12.019
1.00
23.91


ATOM
2819
O
HOH
W
198
−1.276
−7.561
35.325
1.00
25.96


ATOM
2820
O
HOH
W
199
4.267
−22.362
30.170
1.00
35.68


ATOM
2821
O
HOH
W
200
21.787
10.595
30.558
1.00
32.19


ATOM
2822
O
HOH
W
201
21.638
20.389
14.210
1.00
43.09


ATOM
2823
O
HOH
W
202
5.373
−10.297
38.927
1.00
36.29


ATOM
2824
O
HOH
W
203
29.035
−9.588
1.139
1.00
25.61


ATOM
2825
O
HOH
W
204
0.403
−17.629
11.462
1.00
25.52


ATOM
2826
O
HOH
W
205
15.896
−2.824
23.429
1.00
9.81


ATOM
2827
O
HOH
W
206
13.783
−1.283
21.923
1.00
12.03


ATOM
2828
O
HOH
W
207
16.854
−0.738
21.328
1.00
11.76


ATOM
2829
O
HOH
W
208
14.946
−0.465
19.263
1.00
10.55


ATOM
2830
O
HOH
W
209
−5.566
−9.500
29.835
1.00
34.12


ATOM
2831
O
HOH
W
210
11.435
14.251
33.693
1.00
48.96


ATOM
2832
O
HOH
W
211
3.944
31.281
18.816
1.00
43.83


ATOM
2833
O
HOH
W
212
21.511
8.201
40.401
1.00
42.14


ATOM
2834
O
HOH
W
213
44.825
1.178
19.793
1.00
52.54


ATOM
2835
O
HOH
W
214
9.397
20.244
23.958
1.00
30.91


ATOM
2836
O
HOH
W
215
18.636
−1.182
15.865
1.00
23.82


ATOM
2837
O
HOH
W
216
18.955
−2.693
17.957
1.00
28.82


ATOM
2838
O
HOH
W
217
26.248
−9.541
27.965
1.00
25.10


ATOM
2839
O
HOH
W
218
24.703
−9.867
30.146
1.00
25.52


ATOM
2840
O
HOH
W
219
22.600
−9.260
25.832
1.00
26.71


ATOM
2841
O
HOH
W
220
1.825
10.054
39.457
1.00
25.12


ATOM
2842
O
HOH
W
221
3.585
4.590
45.058
1.00
28.59


ATOM
2843
O
HOH
W
222
3.777
−6.424
30.447
1.00
24.42


TER
2844

HOH
W
222


ATOM
2845
ZN
ZN
B
864
13.210
0.069
20.406
1.00
15.15


ATOM
2846
MG
MG
B
865
15.487
−0.725
23.006
1.00
8.84


TER
2847

MG
B
865


END










References
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Abbreviations

cAMPcyclic adenosine monophosphatecGMPcyclic guanosine monophosphatePDEphosphodiesterasePGKprotein kinase GMADmulti-wavelength anomalous dispersionPCRpolymerase chain reaction2YT16 g tryptone, 10 g yeast extract, 5 g NaCl per litresolutionTristris[hydroxymethyl]amino-methaneE-64epoxysuccinyl-l-leucylamido-(4-guanidino) butaneDTTDL-dithiothreitolβ-MEβ-mercaptoethanolIPTGβ-D-isopropyl-thiogalactopyranosideEDTAethylenediamine tetraacetic acidBis-Trisbis[2-hydroxyethyl]imino-tris[hydroxymethyl]methanePEGpolyethylene glycolPEG2KMMEpolyethylene glycol 2000 monomethyl etherrmsdroot mean square deviationrpmrevolutions per minuteMoimultiplicity of infectionSildenafil5-[2-ethoxy-5-(4-methyl-1-piperazinylsulphonyl)phenyl]-1-methyl-3-n-propyl-1,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one, which is also known as 1-[[3-(6,7-dihydro-1-methyl-7-oxo-3-propyl-1H-pyrazolo[4,3-d]pyrimidin-5-yl)-4-ethoxyphenyl]sulphonyl]-4-methylpiperazine(see EP-A-0463756)UK-092,480see “Sildenafil”UK-088,8005-(2-ethoxyphenyl)-1-methyl-3-propyl-1,6-dihydro-7H-pyrazolo[4,3-d]pyrimidin-7-one.


List of Sequences

Wild-type PDE5 “loop region”HRGVNNSYIQRSEHPLAQLYCHSIMESEQ ID NO: 1Wild-type PDE5 catalytic domainEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLESEQ ID NO: 2TALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEKPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKLKNKIPSMQVGFDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRNFull length wild-type PDE5 sequenceERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWSEQ ID NO: 3DFTFSYFVRLKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHRGVNNSYIQRSEHPLAQLYCHSIMEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEQQEKMLINGESGQAKRNWild-type PDE4 “loop region”HPGVSNQFLINTNSELALMYNDESVLESEQ ID NO: 4Loop-swapped PDE5 catalytic domain =PDE5*EEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLESEQ ID NO: 5TALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDLHPGVSNQFLINTNSELALMYNDESVLEHHHDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAEFull length PDE5 sequence comprisingPDE5*ERAGPSFGQQRQQQQPQQQKQQQRDQDSVEAWLDDHWSEQ ID NO: 6DFTFSYFVRKATREMVNAWFAERVHTIPVCKEGIRGHTESCSCPLQQSPRADNSVPGTPTRKISASEFDRPLRPIVVKDSEGTVSFLSDSEKKEQMPLTPPRFDHDEGDQCSRLLELVKDISSHLDVTALCHKIFLHIHGLISADRYSLFLVCEDSSNDKFLISRLFDVAEGSTLEEVSNNCIRLEWNKGIVGHVAALGEPLNIKDAYEDPRFNAEVDQITGYKTQSILCMPIKNHREEVVGVAQAINKKSGNGGTFTEKDEKDFAAYLAFCGIVLHNAQLYETSLLENKRNQVLLDLASLIFEEQQSLEVILKKIAATIISFMQVQKCTIFIVDEDCSDSFSSVFHMECEELEKSSDTLTREHDANKINYMYAQYVKNTMEPLNIPDVSKDKRFPWTTENTGNVNQQCIRSLLCTPIKNGKKNKVIGVCQLVNKMEENTGKVKPFNRNDEQFLEAFVIFCGLGIQNTQMYEAVERAMAKQMVTLEVLSYHASAAEEETRELQSLAAAVVPSAQTLKITDFSFSDFELSDLETALCTIRMFTDLNLVQNFQMKHEVLCRWILSVKKNYRKNVAYHNWRHAFNTAQCMFAALKAGKIQNKLTDLEILALLIAALSHDLDHPGVSNQFLNTNSELALMYNDESVLEHHHFDQCLMILNSPGNQILSGLSIEEYKTTLKIIKQAILATDLALYIKRRGEFFELIRKNQFNLEDPHQKELFLAMLMTACDLSAITKPWPIQQRIAELVATEFFDQGDRERKELNIEPTDLMNREKKNKIPSMQVGFIDAICLQLYEALTHVSEDCFPLLDGCRKNRQKWQALAECGTGAATTCATGGAGGAAGAAACAAGAGAGCTACSEQ ID NO: 7CGTTCTAGACTATCAGTTCCGCTTGGCCTGGCCGCTTSEQ ID NO: 8TCCCCCGTGAATTCATGCATCATCATCATCATCATCTTCTGGSEQ ID NO: 9TTCCGCGTGGATCTGCGCCCGAGGAAGAAACAAGAGAGCTACCAAAGAAAGTTCTGAATTTGTGTTGATGAGAAACTGASEQ ID NO: 10TTGGAGACTCCAGGATGATCCAAATCGTGGCTTAGATCAACACAAATTCAGAACTTGCTTTGATGTATAATGSEQ ID NO: 11ATGAATCTGTGTTGGAACACCATCATTTTGACCAGCGTTCTAGACTATCATTCTGCAAGGGCCTGCCATTTCSEQ ID NO: 12TGCGTCATATGGAGGAAGAAACAAGAGAGCTACSEQ ID NO: 13CGTCTCGAGCTATCATTCTGCAAGGGCCTGCCATTTCSEQ ID NO: 14TG


Claims
  • 1. A crystal of a PDE5 protein comprising SEQ ID NO: 4 or a sequence having 95% identity thereto into which a ligand is capable of being soaked such that the ligand is bound to the active site of the protein.
  • 2. A crystal of claim 1 wherein said protein comprises SEQ ID NO:4.
  • 3. A crystal of claim 1 wherein said ligand is a compound of the formula represented in FIG. 4.
  • 4. A crystal of a PDE5 protein comprising SEQ ID NO: 5 or a sequence having 95% identity thereto into which a ligand is capable of being soaked such that the ligand is bound to the active site of the protein.
  • 5. A crystal of claim 4 wherein said protein comprises SEQ ID NO: 5.
  • 6. A crystal of claim 4 wherein said ligand is a compound of the Formula represented in FIG. 4.
  • 7. A crystal according to one of claim 1 or claim 4 which is grown in a buffer in the pH range of 6.5 to 8.0.
  • 8. A crystal according to one of claim 1 or claim 4 which is grown in the presence of an alcohol.
  • 9. A crystal according to one of claim 1 or claim 4 which is grown in a solution containing HEPES buffer, polyethylene glycol 4000 and iso-propanol.
  • 10. A PDE5 protein crystal comprising one or more of the following characteristics: (a) a space group C2; (b) unit cell dimensions a˜56 ű1%, b˜77 ű1%, c˜81 ű1%, α=γ=90°, β=103°±1%; (c) one molecule per asymmetric unit; (d) a protein of a molecular weight of approximately 40 kDa±2 kDa; (e) a calculated solvent content of approximately 44±5%; and/or (f) a monoclinic crystal system.
  • 11. A crystal of a PDE5 protein including SEQ ID NO:4 or SEQ ID NO:5 or a sequence having 95% identity to SEQ ID NO:4 or SEQ ID NO:5 wherein the protein has an active site within the third sub-domain of the protein which is bounded by Helices 15 (H15 813-824) and 14 (H14 772-797), the C-terminus of Helix 13 (H13 749-765), and the C-terminus of Helix 11 (H11 706-721) along with the loop region between Helices 11 and 12a (H12a 725-731) as shown in FIG. 2.
  • 12. A crystal as recited in claim 11 wherein said crystal is soakable.
  • 13. A crystal of claim 11 wherein the protein has an active site within the third sub-domain of the protein and comprises Leu 765, Ala 767 and Ile 768 and one or more of Phe 820, Val 782, Phe 786, Tyr 612, Leu 804, Ala 779, Ala 783, Ile 813, Met 816 and Gln 817 or functional substituents thereof.
  • 14. A crystal according to one of claim 1 or claim 4, wherein the protein has a three-dimensional structure characterized by the atomic co-ordinates set out in Table 4 or a derivative set as expressed in any reference frame thereof.
  • 15. A crystal according to one of claim 1 or claim 4, wherein a PDE5 ligand has been soaked in.
  • 16. A crystal according to claim 14, wherein the protein has a three-dimensional structure characterized by the atomic co-ordinates set out in Table 5 or a derivative set as expressed in any reference frame thereof.
  • 17. A heavy atom derivative of a crystal according to one of claim 1 or claim 4.
  • 18. A method of using the atomic co-ordinates determined from a crystal according to one of claim 1 or claim 4 for deriving a three-dimensional structure of a PDE5 or a mutant, derivative, variant, analogue, homologue, sub-domain or fragment thereof.
  • 19. A method according to claim 18, wherein the sub-domain is the catalytic domain.
  • 20. A method of identifying a compound which is a ligand of PDE5 comprising the following steps: (a) providing a PDE5 crystal including SEQ ID NO: 4 or SEQ ID NO:5 or a sequence having 95% identity to SEQ ID NO:4 or SEQ ID NO:5, (b) contacting the crystal with the compound under conditions conducive to soaking the compound into the crystal, (c) determining, by X-ray diffraction and structure solution, whether or not the compound is bound to the active site of the protein in the resultant soaked crystal, (d) optionally assaying the ligand to determine whether it is an inhibitor of PDE5.
  • 21. A method according to claim 20 wherein the compound is based on the structural template as shown in FIG. 4.
  • 22. A method of designing a compound capable of associating with PDE5, comprising the following steps: (a) computationally creating a three-dimensional representation of the structure of the protein present in a PDE5 crystal including SEQ ID NO: 4 or SEQ ID NO: 5 or a sequence having 95% identity to SEQ ID NO:4 or SEQ ID NO:5, or a fragment or subdomain thereof, (b) computationally creating a three-dimensional representation of the structure of a compound, (c) co-displaying the three-dimensional representation of the compound structure with the three-dimensional representation of the protein structure, (d) assessing whether the three-dimensional representation of the compound structure fits the three-dimensional representation of an active site of the protein structure, (e) optionally making assaying the ligand to determine whether it is an inhibitor of PDE5.
  • 23. A method of selecting a PDE5 ligand from a group of potential PDE5 ligands, comprising the following steps: (a) computationally creating a three-dimensional representation of the structure of the protein present in a PDE5 crystal including SEQ ID NO:4 or SEQ ID NO:5 or a sequence having 95% identity to SEQ ID NO:4 or SEQ ID NO:5, or a fragment or subdomain thereof, (b) computationally creating a three-dimensional representation of the structure of the ligand, (c) co-displaying the three-dimensional representation of the ligand structure with the three-dimensional representation of the protein structure, (d) assessing whether the three-dimensional representation of the ligand structure fits the three-dimensional representation of an active site of the protein structure, (e) optionally making and assaying the ligand to determine whether it is an inhibitor of PDE5.
  • 24. A method of using of the three-dimensional structure as derivable according to claim 23 to design site-directed mutants of PDE5.
  • 25. A method of selecting a PDE5 ligand from a group of potential PDE5 ligands, comprising the following steps: (a) computationally creating a three-dimensional representation of the structure of the protein present in the PDE5 crystal, including SEQ ID NO:4 or SEQ ID NO:5 or a sequence having 95% identity to SEQ ID NO:4 or SEQ ID NO:5, or a fragment or subdomain thereof, (b) computationally creating a three-dimensional representation of the structure of the ligand, (c) co-displaying the three-dimensional representation of the ligand with the three-dimensional representation of the protein structure, (d) assessing whether the three-dimensional representation of the ligand fits the three-dimensional representation of an active site of the protein structure, (e) optionally making and assaying the ligand to determine whether it is an inhibitor of PDE5.
  • 26. A method of soaking a ligand into a crystal according to one of claims 1 or 4 comprising the following steps: (a) incubating the crystal in an aqueous stabilising solution comprising buffer and polyethylene glycol; (b) combining the compound with the stabilising solution; and (c) optionally adding a cryo-protectant to the stabilising solution.
Priority Claims (3)
Number Date Country Kind
0310058.3 May 2003 GB national
PCT/IB02/04426 Oct 2002 WO international
0126417.5 Nov 2001 GB national
RELATED APPLICATIONS AND PRIORITY CLAIMS THERETO

This application is a continuation-in-part of U.S. application Ser. No. 10/427,222 filed May 1, 2003 which is a continuation-in-part of U.S. application Ser. No. 10,415,839, filed on Apr. 30, 2003, which is the National Stage Application of International Application No. PCT/EB02/04426 filed on Oct. 24, 2002, having designated the United States. The subject matter of each of the co-pending U.S. application Ser. No. 10/415,839 and co-pending U.S. application Ser. No. 10/472,222 and International Application No. PCT/EB02/04426 is incorporated-by-reference in their entirety herein. This application claims priority under 35 USC §119, 120 and 365 to the following patent applications: Application No. GB0126417.5 filed in the United Kingdom on Nov. 2, 2001; Application No. UK 0310058.3 filed May 1, 2003; International Application No. PCT/IB02/04426 filed in the WO on Oct. 24, 2002 and having designated the U.S. as a receiving country; U.S. application Ser. No. 10/415,839 filed on Apr. 30, 2003 and U.S. application Ser. No. 10/427,222 filed on May 1, 2003.

Continuation in Parts (2)
Number Date Country
Parent 10427222 May 2003 US
Child 10837081 Apr 2004 US
Parent 10415839 Oct 2003 US
Child 10837081 Apr 2004 US