Crystal structures of retaining glycosytransferases

[0001] A portion of the disclosure of this patent document contains material that is subject to copyright protection. The copyright owner has no objection to the facsimile reproduction by anyone of the patent document or patent disclosure, as it appears in the Patent and Trademark Office patent file or records, but otherwise reserves all copyright rights whatsoever.

FIELD OF THE INVENTION

[0002] The present invention relates to crystal structure. In particular a crystal comprising a ligand-binding pocket (LBP) of a glycosyltransferase, optionally having a ligand associated therewith. The invention also relates to a crystal of a retaining glycosyltransferase and parts thereof. In particular, the present invention relates to a crystal comprising a ligand binding pocket of a retaining galactosyltransferase optionally in association with a ligand, for example a donor and/or an acceptor molecule or analogue thereof. The crystals may be useful for modeling and/or synthesizing mimetics of a ligand binding pocket, or ligands that associate with the binding pocket. Such mimetics or ligands may be capable of acting as modulators of glycosyltransferase activity, and they may be useful for treating, inhibiting, or preventing diseases associated with or modulated by glycosyltransferases. The structures may be used to determine retaining glycosyltransferase homologs and information about the secondary and tertiary structures of polypeptides which are as yet structurally uncharacterized.

BACKGROUND

[0003] Oligosaccharides are essential to a wide variety of biological functions many of which are crucial for the development, growth, function and survival of an organism (Varki, 1993 Glycobiology 3, 97-130). Lipooligosaccharide (LOS) is the major glycolipid found on the cell surface of gram-negative mucosal pathogens such as Neisseria, Haemophilus, Moraxella, Bordetella and Campylobacter. The LOS structure is made up of a lipid A moiety, 2-keto-3-deoxyoctulosonic acid (KDO) and various terminal oligosaccharides. Bacterial LOS structures can be antigenically and structurally similar to human glycolipids, and thus may camouflage the bacterial surface from recognition by the human immune system. For example, the terminal structures of N. meningitidis and N. gonorrhoea LOS mimic human lacto-N-neotetraose, sialylacto-N-neotetraose and the Pk k blood group glycolipid.

[0004] There have been numerous studies on the genes involved in making the oligosaccharide portion of the LOS structure (Wakarchuk et al, 1996 J. Biol. Chem. 271:19166-19173, Moran et al, 1996 FEMS Immunology and Medical Microbiology 16, 105-115, Kahler & Stephens, 1998 Crit. Rev. Microbiol. 24, 281-334 Biochemical Journal 329, 929-939). An essential aspect of this biosynthesis involves the linking of saccharides with the aid of glycosyltransferases (for classification of the distinct families see Campbell et al., 1997 Biochemical Journal 326, 929-939). These enzymes transfer a sugar, mainly from a nucleotide diphospho-sugar, but also from sugar phosphates, to specific acceptor molecules. α-1, 4-Galactosyltransferase from N. meningitidis (Family 8 in the scheme of Campell et al., 1997 as above), adds an α-galactose from UDPgal (the donor) to a terminal lactose (the acceptor) of the LOS structure creating the Pk blood group glycolipid mimic (FIG. 1a). Interest in understanding this and other bacterial transferases stems, at least in part, from the notion that inhibitors that block the essential formation of LOS biosynthesis in pathogenic bacteria may prove to be useful new antibiotics (Takayama et al, 1999 Bioorganic and Medicinal Chemistry 7, 401-409).

[0005] Based on the relative anomeric stereochemistries of the substrate and product in the reaction catalyzed, glycosyltransferases can be classified mechanistically as either inverting or retaining, (as is also done with the well-studied glycosidase family; Sinnott, 1990, Chem. Rev., 90, 1171-1202; Davies et al., 1997 in Comprehensive Biological Catalysis (Sinnott, M. L., ed) Vol. 1, pp. 119-208, Academic Press, London; Zechel & Withers, 2000 Acc. Chem. Res. 33, 11-18). While this has led to the tacit assumption that similar mechanisms are employed by glycosidases and glycosyltransferases in carrying out their functions, very little has been experimentally verified about the mechanism of the latter.

[0006] By simple analogy with the glycosidase counterpart, inverting glycosyltransferases are believed to follow a direct displacement mechanism with a general base to assist in deprotonating the reactive hydroxyl of the acceptor molecule and possibly a general acid to aid in cleavage of the exocyclic C1—O bond, though a bound metal ion may fulfil this role (FIG. 1b). In the case of retaining transferases, catalysis is believed to proceed via a double displacement mechanism involving the formation and subsequent breakdown of a covalent glycosyl-enzyme intermediate (FIG. 1c). In such a scheme, a nucleophile is required for attack on the anomeric centre of the donor sugar to form the glycosyl-enzyme species. Once again, either an acid catalyst or a metal ion will be required to provide general acid assistance to the cleavage of the exocyclic C1—O bond (in the first step) and a general base will be needed to deprotonate the reactive hydroxyl of the acceptor molecule (in the second step).

[0007] To date the x-ray crystal structures of only four glycosyltransferases have been determined and all catalyze inverting reactions; β-glucosyltransferase from phage T4, (Vrielink et al.,1994 EMBO J. 13, 3413-3422), SpsA from Bacillus subtilis (Charnock and Davies, 1999 Biochemistry. 38, 6380-6385.), bovine β-1,4-galactosyltransferase (Gastinel et al., 1999) and MurG from E. coli (Ha et al, 2000). With the exception of MurG, these structures have been determined in complex with UDP or the donor UDP-sugar. However, electron density for the sugar moiety has not been observed in any of these experiments.

[0008] Despite the fact that the biosynthesis of polysaccharides is of fundamental biological importance, and that a large number of glycosyltransferases have already been described, to date no crystal structures have been provided for retaining glycosyltransferase enzymes, and no crystal structures of any glycosyltransferase enzymes have been provided which give any structural data for the donor and/or acceptor molecule.

[0009] Such crystal structures would be invaluable in understanding the catalytic mechanism of the enzymes and in the rational design of inhibitors.

SUMMARY OF THE INVENTION

[0010] The present invention is based on the finding that it is possible to crystallize a retaining glycosyltransferase, both alone and in combination with a selection of different ligands. More particularly, Applicants have crystallized a retaining glycosyltransferase in complex with a metal cofactor, a donor molecule, and in the presence or absence of an acceptor molecule, and have solved the three-dimensional structure of the enzyme. Solving the crystal structure has enabled the determination of key structural features of retaining glycosyltransferases, particularly the shape of ligand binding pockets (also referred to herein as “LBP”), or parts thereof, that associate with a metal cofactor, donor molecule, and/or acceptor molecule. The crystal structure has also enabled the determination of key structural features in donor molecules and acceptor molecules.

[0011] Binding pockets are of significant utility in drug discovery. The association of natural ligands and substrates with the binding pockets of their corresponding glycosyltransferases is the basis of many biological mechanisms. In addition, many drugs exert their effects through association with the binding pockets of glycosyltransferases. The associations may occur with all or any parts of a binding pocket An understanding of these associations will lead to the design and optimization of drugs having more favorable associations with their target glycosyltransferase and thus provide improved biological effects. Therefore, information about the shape and structure of glycosyltransferases and their ligand-binding pockets is invaluable in designing potential modulators of glycosyltransferases for use in treating diseases and conditions associated with or modulated by the glycosyltransferases.

[0012] Therefore, broadly stated the present invention relates to the secondary, tertiary, and/or quanternary structures of glycosyltransferases, and parts thereof. The glycosyltransferase structure may be the structure the enzyme forms when it is associated with one or more ligands (e.g. an acceptor molecule, a donor molecule, or components thereof). The invention also contemplates a glycosyltransferase structure comprising a the secondary, tertiary, and/or quanternary structure of a glycosyltransferase in association with a ligand. The defined boundaries and properties of the structures and any of the ligands bound to it are pertinent to methods for determining the secondary, tertiary, and/or quanternary structures of polypeptides with unknown structure, and to methods that identify modulators of glycosyltansferases. These modulators are potentially useful as therapeutics for diseases associated with or modulated by glycosytransferases.

[0013] In an embodiment, the invention provides a crystal of a polypeptide corresponding to a retaining glycosyltransferase, or a part thereof (e.g. ligand binding pocket). The invention preferably contemplates the crystal a retaining glycosyltransferase forms when it is complexed with a ligand, including a donor molecule or analogue thereof, an acceptor molecule or analogue thereof, a metal cofactor, and/or heavy metal atom. The crystal form may also comprise one or more ligands (e.g. donor molecule or acceptor molecule).

[0014] A glycosyltransferase structure of the invention may be characterized by the following:

[0015] (a) a ligand binding pocket comprising a core β-sheet containing 7 strands (β33, β2, β1, β4, β6, β8 in FIG. 3) all of which are parallel with the exception of β7; the core β-sheet being further characterized by a nucleotide binding motif composed of four parallel strands sandwiched between helices A and B on one side and helices C and D on the other as illustrated in FIG. 3;

[0016] (b) an antiparallel β-ribbon formed by two strands (β5 and β9) lying almost perpendicular to the core β-sheet, and a substrate binding cleft that lies along the base of the core β-sheet; or

[0017] (c) a C-terminal domain mediating membrane attachment comprising helix M and Helix N in FIG. 3 forming a small pedestal that packs perpendicular to helices A and B of the nucleotide binding motif and to the β-ribbon as shown in FIG. 3.

[0018] The present invention also contemplates molecules or molecular complexes that comprise all or parts of either one or more ligand binding pockets, or homologues of these ligand binding pockets that have similar three-dimensional shapes.

[0019] According to an aspect of the invention there is provided a crystal comprising a ligand binding pocket of a retaining glycosyltransferase.

[0020] A ligand binding pocket may include one or more of the binding domains for a disphosphate group or pyrophosphate of a donor molecule, a nucleotide of a donor molecule, a nitrogeneous heterocyclic base (preferably a pyrimidine base, more preferably uracil) of a donor molecule, a sugar of the nucleotide of a donor molecule, a selected sugar of a donor molecule that is transferred to an acceptor molecule, and/or an acceptor molecule.

[0021] The present invention also provides a crystal comprising a ligand binding pocket of a retaining glycosyltransferase and a donor molecule or analogue thereof from which it is possible to derive structural data for the donor molecule or analogue thereof.

[0022] The present invention also provides a crystal comprising a ligand binding pocket of a retaining glycosyltransferase and an acceptor molecule or analogue thereof from which it is possible to derive structural data for the acceptor molecule or analogue thereof.

[0023] The present invention also provides a crystal comprising the ligand binding pocket of a retaining glycosyltransferase and a metal cofactor.

[0024] In an embodiment a crystal of the invention comprises a ligand binding pocket in association with or complexed with a donor molecule or analogue thereof and/or an acceptor molecule or analogue thereof. In another embodiment the ligand binding pocket is associated with or complexed with a donor molecule, a metal cofactor, and an acceptor molecule. These crystals make it possible to derive structural data for a donor molecule or an acceptor molecule, or analogues thereof.

[0025] The shape and structure of a ligand binding pocket may be defined by selected atomic contacts in the pocket In an embodiment the ligand binding pocket is defined by one or more atomic interactions or enzyme atomic contacts as set forth in Table 3. Each of the atomic interactions is defined in Table 3 by an atomic contact (more preferably, a specific atom where indicated) on the donor molecule or analogue thereof or acceptor molecule or analogue thereof, and an atomic contact (more preferably a specific atom where indicated) on the glycosyltransferase.

[0026] In an embodiment, the ligand binding pocket is an active site binding pocket of a glycosyltransferase. The active site binding pocket refers to the region of a glycosyltransferase where the transfer of a sugar from the donor molecule to the acceptor occurs.

[0027] The invention also provides a method for crystallizing a retaining glycosyltransferase, or a part thereof (e.g. ligand binding pocket), or a complex of a retaining glycosyltransferase or a part thereof and a metal cofactor, donor molecule, and/ or acceptor molecule.

[0028] The crystal structures of the invention enable a model to be produced for a glycosyltransferase and a part thereof, (e.g. a ligand binding pocket), or complexes of the enzyme or parts thereof The models may provide structural information about the donor and/or acceptor molecule and their interactions with the LBP. Models may also be produced for donor and acceptor molecules.

[0029] Therefore the invention also provides a model of a ligand binding pocket designed in accordance with a method of the invention. The invention contemplates a model, crystal, or secondary, tertiary and/or quanternary structure of a glycosyltransferase or ligand binding pocket in association with a ligand or substrate.

[0030] The structures and models of the invention provide information about the atomic contacts involved in the interaction between the enzyme and a known ligand which can be used to screen for unknown ligands. Therefore the present invention provides a method of screening for a ligand capable of binding a glycosyltransferase ligand binding domain, comprising the use of a secondary, tertiary or quanternary structure or a model of the invention. For example, the method may comprise the step of contacting a ligand binding domain with a test compound, and determining if the test compound binds to the ligand.

[0031] A crystal and/or model of the invention may be used in a method of determining the secondary, tertiary, and/or quanternary structures of a polypeptide with incompletely characterised structure. Thus, a method is provided for determining at least a portion of the secondary, tertiary, and/or quanternary structure of molecules or molecular complexes which contain at least some structurally similar features to a retaining glycosyltransferase. This is achieved by using at least some of the structural coordinates set out in Table 4, 5 or 6.

[0032] A structure, crystal and/or model of the invention may be used to design, evaluate, and identity ligands of a glycosyltransferases or homologues thereof. A ligand may be based on the shape and structure of a glycosyltransferase, or a ligand binding pocket or atomic interactions, or atomic contacts thereof. Preferably, a ligand is derived from a ligand binding pocket for a donor molecule or analogue or parts thereof, and/or an acceptor molecule or analogue or parts thereof. The invention also provides modulators that are derived from a DXD motif or the C-terminal binding pocket mediating membrane attachment.

[0033] The present invention also contemplates a ligand identified by a method of the invention. A ligand may be a competitive or non-competitive inhibitor of a glycosyltransferase. Preferably, the ligand is a modulator that is capable of modulating the activity of a glycosyltransferase enzyme. Thus, the methods of the invention permit the identification early in the drug development cycle of compounds that have advantageous properties.

[0034] In an embodiment, the present invention contemplates a method of identifying a modulator of a glycosyltransferase, or a ligand binding pocket, or a part thereof, comprising the step of applying the structural coordinates of a glycosyltransferase, ligand binding pocket, or atomic interactions, or atomic contacts thereof, to computationally evaluate a test ligand for its ability to associate with the glycosyltransferase, or ligand binding pocket, or part thereof. Use of the structural coordinates of a glycosyltransferase structure or ligand binding pocket, or atomic interactions, or atomic contacts thereof to identify a modulator is also provided.

[0035] In an embodiment, the present invention contemplates a method of identifying a modulator of a glycosyltransferase or a ligand binding pocket or binding site thereof, comprising the step of using the structural coordinates of a glycosyltransferase or a ligand binding pocket or binding site thereof, or a model of the invention to computationally evaluate a test compound for its ability to associate with the glycosyltransferase or ligand binding pocket or binding site thereof. Use of the structural coordinates of a glycosyltransferase structure, ligand binding pocket, or binding site thereof, of the invention to identify a ligand or modulator is also provided.

[0036] In another embodiment of the invention, a method is provided for identifying a potential modulator of a glycosyltransferase by determining binding interactions between a test compound and atomic contacts of a ligand binding pocket of a glycosyltransferase defined in accordance with the invention comprising:

[0037] (a) generating the atomic contacts on a computer screen;

[0038] (b) generating test compounds with their spatial structure on the computer screen; and

[0039] (c) determining whether the compounds associate or interact with the atomic contacts defining the glycosyltransferase;

[0040] (d) identifying test compounds that are potential modulators by their ability to enter into, a selected number of atomic contacts.

[0041] Another aspect of the invention provides methods for identifying a potential modulator of a glycosyltransferase function by docking a computer representation of a test compound with a computer representation of a structure of a glycosyltransferase or a ligand binding pocket thereof that is defined as described herein. In an embodiment the method comprises the following steps:

[0042] (a) docking a computer representation of a compound from a computer data base with a computer representation of atomic interactions or atomic contacts of a ligand binding pocket of a glycosyltransferase to obtain a complex;

[0043] (b) determining a conformation of the complex with a favourable geometric fit and favourable complementary interactions; and

[0044] (c) identifying test compounds that best fit the atomic interactions or contacts as potential modulators of the glycosyltransferase.

[0045] In another embodiment the method comprises the following steps:

[0046] (a) modifying a computer representation of a test compound complexed with a ligand binding pocket of a glycosyltransferase by deleting or adding a chemical group or groups;

[0047] (b) determining a conformation of the complex with a favourable geometric fit and favourable complementary interactions; and

[0048] (c) identifying a test compound that best fits the ligand binding pocket as a potential modulator of a glycosyltransferase.

[0049] In still another embodiment the method comprises the following steps:

[0050] (a) generating a computer representation of a test compound complexed with atomic contacts or atomic interactions of a binding pocket of a glycosyltransferase; and

[0051] (b) searching for molecules in a data base that are similar to the test compound using a searching computer program, or replacing portions of the test compound with similar chemical structures from a data base using a compound building computer program.

[0052] The ligands or compounds identified according to the methods of the invention preferably have structures such that they are able to enter into an association with a ligand binding pocket Selected ligands or compounds may be characterized by their suitability for binding to particular ligand binding pockets. A ligand binding pocket or binding site may be regarded as a type of negative template with which the compounds correlate as positives in the manner described herein and thus the compounds are unambiguously defined. Therefore, it is possible to describe the structure of a compound suitable as a modulator of a glycosyltransferase by accurately defining the atomic interactions to which the compound binds to a ligand binding pocket and deriving the structure of the compound from the spacial structure of the target.

[0053] The invention contemplates a method for the design of ligands, in particular modulators, for glycosyltransferase based on the secondary, tertiary or quanternary structure of a donor molecule or acceptor molecule (or part thereof) defined in relation to its spatial association with the three dimensional structure of the glycosyltransferase or a ligand binding pocket thereof. Generally, a method is provided for designing potential inhibitors of a glycosyltransferase comprising the step of using the structural coordinates of a donor molecule or acceptor molecule or part thereof, defined in relation to its spatial association with the secondary, tertiary or quanternary structure or model of a glycosyltransferase or a ligand binding pocket thereof, to generate a compound for associating with the ligand binding pocket of the glycosyltransferase. The following steps are employed in a particular method of the invention: (a) generating a computer representation of a donor molecule or acceptor molecule, or part thereof, defined in relation to its spatial association with the three dimensional structure of a glycosyltransferase or a ligand binding pocket thereof, or defined by the structural coordinates shown in Table 4, 5, or 6; (b) searching for molecules in a data base that are similar to the defined donor molecule or acceptor molecule, or part thereof using a searching computer program, or replacing portions of the compound with similar chemical structures from a database using a compound building computer program.

[0054] Therefore, the invention further contemplates classes of ligands, in particular modulators, of a glycosyltransferase based on the secondary, tertiary or quanternary structure of a donor molecule or acceptor molecule, or part thereof, defined in relation to the donor or acceptor molecule's spatial association with a three dimensional structure of a glycosyltransferase.

[0055] It will be appreciated that a modulator of a glycosyltransferase may be identified by generating an actual secondary or three-dimensional model of a ligand binding pocket, synthesizing a compound, and examining the components to find whether the required interaction occurs.

[0056] A potential ligand or modulator of a glycosyltransferase identified by a method of the present invention may be confirmed as a modulator by synthesizing the compound, and testing its effect on the glycosyltransferase in an assay for that glycosyltransferase's enzymatic activity. Such assays are known in the art. (See for example, Sadler, J. E. et al. Methods Enzymol., 83, 458-514; Schachter, H., et al Methods Enzymol., 179, 351-397; Datti, A., et al Anal.Biochem., 206, 262-266; Palcic, M. M. (1994) Methods Enzymol., 230, 300-316; Fitzgerald, D. K., et al, Anal.Biochem., 36, 43-61; Gosselin, S., et al Anal.Biochem., 220, 92-97; Crawley, S. C., et al Anal.Biochem 185, 112-117; Yan, L., et al, Anal.Biochem., 223, 111-118; Yeh, J. C. and Cummings, R. D. (1996) Anal.Biochem., 236, 126-133; DeBose-Boyd, R. A., et al Arch.Biochem.Biophys., 335, 109-117; Rabina, J., et al, Anal.Biochem., 246, 71-78; Shedletzky, E., et al Anal.Biochem., 249, 88-93; Oubihi, M., et al Anal.Biochem., 257, 169-175; Kanie, Y., et al Anal.Biochem., 263, 240-245.)

[0057] A ligand or modulator of the invention may be converted using customary methods into pharmaceutical compositions. A ligand or modulator may be formulated into a pharmaceutical composition containing a ligand or modulator either alone or together with other active substances.

[0058] Ligands that are modulators that are capable of modulating the activity of glycosyltransferases have therapeutic and prophylactic potential. Therefore, the methods of the invention for identifying ligands or modulators may comprise one or more of the following additional steps:

[0059] (a) testing whether the ligand is a modulator of the activity of a glycosyltransferase, preferably testing the activity of the ligand in cellular assays and animal model assays;

[0060] (b) modifying the ligand;

[0061] (c) optionally rerunning steps (a) or (b); and

[0062] (d) preparing a pharmaceutical composition comprising the ligand.

[0063] Steps (a), (b) (c) and (d) may be carried out in any order, at different points in time, and they need not be sequential.

[0064] Still another aspect of the invention provides a method of conducting a drug discovery business comprising:

[0065] (a) providing one or more systems or methods for identifying modulators based on a model or structure of the present invention, preferably a method using a computer as described herein;

[0066] (b) conducting therapeutic profiling of modulators identified in step (a), or further analogs thereof, for efficacy and toxicity in animals; and

[0067] (c) formulating a pharmaceutical composition including one or more agents identified in step (b) as having an acceptable therapeutic profile.

[0068] In certain embodiments, the subject method may also include a step of establishing a distribution system for distributing the pharmaceutical composition for sale, and may optionally include establishing a sales group for marketing the pharmaceutical composition.

[0069] In yet another aspect of the invention, a method of conducting a target discovery business is provided comprising:

[0070] (a) providing one or more system or method for identifying modulators based on a model or structure of the present invention, preferably a method using a computer as described herein;

[0071] (b) optionally conducting therapeutic profiling of modulators identified in (a) for efficacy and toxicity in animals; and

[0072] (c) licensing to a third party the rights for further drug development and/or sales for agents identified in step (a), or analogs thereof.

[0073] There is also provided a pharmaceutical composition comprising a ligand or modulator, and a method of treating and/or preventing disease associated with a glycosyltransferase comprising the step of administering a ligand or modulator or pharmaceutical composition comprising a modulator to a patient.

[0074] In an aspect, the invention contemplates a method of treating a disease associated with a glycosyltransferase with inappropriate activity in a cellular organism, comprising:

[0075] (a) administering a ligand or modulator identified using the methods of the invention in an acceptable pharmaceutical preparation; and

[0076] (b) activating or inhibiting a glycosyltransferase to treat the disease.

[0077] The invention provides for the use of a ligand or modulator identified by the methods of the invention in the preparation of a medicament to treat or prevent a disease associated with or modulated by a glycosyltransferase in a cellular organism. Use of ligands or modulators of the invention to manufacture a medicament is also provided.

[0078] Another aspect of the invention provides machine readable media encoded with data representing a crystal or model of the invention or the coordinates of a structure of a glycosyltransferase or ligand binding pocket or binding site thereof as defined herein, or the three dimensional structure of a donor molecule or acceptor molecule or part thereof defined in relation to its spatial association with a three dimensional structure of a glycosyltransferase as defined herein. The invention also provides computerized representations of a crystal or model of the invention or the secondary, tertiary or quanternary structures of the invention, including any electronic, magnetic, or electromagnetic storage forms of the data needed to define the structures such that the data will be computer readable for purposes of display and/or manipulation. The invention further provides a computer programmed with a homology model of a ligand binding pocket of a glycosyltransferase. The invention still further contemplates the use of a homology model of the invention as input to a computer programmed for drug design and/or database searching and/or molecular graphic imaging in order to identify new ligands or modulators for glycosyltransferases.

[0079] These and other aspects of the present invention will become evident upon reference to the following detailed description and Tables, and attached drawings.

DESCRIPTION OF THE DRAWINGS

[0080] The present invention will now be described only by way of example, in which reference will be made to the following Figures:

[0081]
FIG. 1. Glycosyl transfer reactions. a) The LgtC catalyzed transfer of galactose from UDP-Gal to the LPS core oligosaccharide of Neisseria. The proposed mechanisms of b) an inverting and c) a retaining α-galactosyltransferase.

[0082]
FIG. 2. An amino acid sequence alignment of Neisseria meningitidis LgtC and related enzymes from glycosyl transferase family 8. Secondary structure elements of LgtC are indicated above the sequence. Invariant residues are shown on blue background and conserved on orange. Sequences from the following organisms were used, their accession numbers in parenthesis. Neisseria meningitidis (P96945), Neisseria gonorrheae (Q50948), Pasturella multocida (AF237927), Haemophilus influenzae (P43947), Escherichia coli (Q92155), Salmonella tryphimurium (P19816), Helicobacter pylori (024967). Residues interacting with the UDP portion of the donor or with the galactose part are marked with filled circles and triangles respectively. Residues coordinating the metal are marked with stars and those that interact with 4-deoxylactose with diamonds.

[0083]
FIG. 3. The overall architecture of LgtC. 3A. A C-α trace of the Lgtc monomer shown in stereo. 3B. The LgtC structure with bound substrate analogues. The substrates are depicted in CPK representation where the acceptor is coloured dark gray, the donor light gray and the manganese pink. Strands and helices are labelled. 3C. View of the LgtC structure showing the substrate binding N-terminal domain and the membrane attaching C-terminal domain. 3D. Topology diagram of LgtC. Helices are coloured blue and strands green.

[0084]
FIG. 4. Stereo view of the active site. 4A. The ball-and stick models of the donor sugar UDP-Gal is colored as red sticks and the acceptor sugar lactose as green sticks in a refined 2fo-fc map contoured at 1.2 sigma. Amino acids interacting with the substrates are labeled. The loops that fold over the active site, residues 75-80 and 246-251, are colored in green. 4B. Molecular surface representation of the active site. UDP-Gal and 4-deoxylactose are shown in ball-and-stick form. UDP-Gal is almost completely buried in the enzyme while 4-deoxylactose is bound in an open pocket, more accessible to solvent 4C. The hydrogen bonding network of Q189 and the distance and angle to the anomeric carbon C1′.Distances are in Å.

[0085]
FIG. 5. Schematic representation of the interactions between the enzyme and the substrate analogues. Hydrogen bonds (<3.1 Å for all bonds except Cys; <3.5 Å) are indicated with dashed lines. Vdw contacts are shown as nested half circles. Water molecules have not been included.

[0086]
FIG. 6. Possible mechanisms in the LgtC catalyzed reaction. a) 6′-OH of the acceptor substrate and the b) side chain amide oxygen of Gln189 as potential nucleophiles. c) The mechanism of a hexosaminidase in which the amide oxygen of the substrate has been shown to function as the catalytic nucleophile.

DESCRIPTION OF THE TABLES

[0087] The present invention will now be described only by way of example, in which reference will be made to the following Tables:

[0088] Table 1 shows a specific comparison of the specific activity and kinetic parameters of the mutants to the wild-type protein

[0089] Table 2 shows data collection, refinement statistics, and model steriochemistry.

[0090] Table 3 shows atomic interactions of a retaining glycosyltransferase and a donor molecule, and an acceptor molecule.

[0091] Table 4 shows the structural coordinates of a retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with manganese and UDP 2-deoxy-2-fluoro-galactose.

[0092] Table 5 shows the structural coordinates of a retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with manganese, UDP 2-deoxy-2-fluoro-galactose and 4-deoxylactose.

[0093] Table 6 shows the structural coordinates of a retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with manganese and UDP 2-deoxy-2-fluoro-galactose and lactose.

[0094] In Tables 4 through 6 inclusive, from the left, the second column identifies the atom number; the third identifies the atom type; the fourth identifies the amino acid type; the fifth identifies the residue number; the sixth identifies the x coordinates; the seventh identifies the y coordinates; and the eighth identifies the z coordinates.

DETAILED DESCRIPTION OF THE INVENTION

[0095] Unless otherwise indicated, all terms used herein have the same meaning as they would to one skilled in the art of the present invention. Practitioners are particularly directed to Current Protocols in Molecular Biology (Ansubel) for definitions and terms of the art.

[0096] Glycosyltransferase

[0097] The invention generally relates to glycosyltransferases and parts thereof. A glycosyltransferase enzyme is capable of transferring a particular sugar residue from a donor molecule to an acceptor molecule, thus forming a glycosidic linkage. Based on the type of donor sugar transferred, these enzymes are grouped into families, e.g. N-acetylglucosaminyltansferases, N-acetylgalactosaminyltransferases, mannosyltransferases, fucosyltransferases, galactosyltransferases, and sialyltransferases.

[0098] A retaining glycosyltransferases is one which transfers a sugar residue with the retention of anomeric configuration. An inverting glycosyltransferase, on the other hand, is one which transfers a sugar residue with the inversion of anomeric configuration. Campbell et al (1997) (as above) describes a classification of glycosyltransferases based on amino acid sequence similarities. Twenty-six families have been identified altogether, thirteen of which are designated as being inverting enzymes (Families 1, 2, 7, 9, 10, 11, 12, 13, 14, 16, 17, 18 and 23) and eight of which are designated as being retaining enzymes (Families 3, 4, 5, 6, 8, 15, 20 and 21).

[0099] In accordance with certain aspects of the invention, the enzyme is a retaining glycosyltransferase of Family 3, 4, 5, 6, 8, 15, 20 and 21 in the scheme of Campbell et al. In an aspect of the invention the enzyme is capable of catalyzing a step in the biosynthesis of a lipooligosaccharide or lipopolysaccharide. Preferably the glycosyltransferase is a member of Family 8 and has the activities of a lipopolysaccharide galactosyltransferase (EC 2.4.1.44), lipopolysaccharide glucosyltransferase 1 (EC 2.4.1.58), glycogenin glucosyltransferase (EC 2.4.1.186), inositol 1-α galactosyltransferase (EC 2.4.1.123). In a more preferred embodiment, the enzyme is a lipopolysaccharide galactosyltransferase [e.g. SwissProt P27128 (E. coli rfaI) and P19816 (S. typhimurium rfaI)] and in a most preferred embodiment the enzyme is a lipopolysaccharide galactosyltransferase of Neisseria (e.g. meningitidis, gonorrhoeae). A highly preferably enzyme is an α 1,4-galactosyltransferase from Neisseria menigitidis (GenBank Accession No. U65788).

[0100] Glycosyltransferases are derivable from a variety of sources, including viruses, bacteria, fungi, plants and animals. In a preferred embodiment the glycosyltransferase is derivable from a bacterium, in particular a gram-negative bacterium, such as one which is capable of acting as a pathogen. In an aspect of the invention the enzyme is derivable form a gram negative mucosal pathogen. For example, the glycosyltanferase may be found in one (or more) of the following organisms: Neisseria, Escherichia, Salmonella, Haemophilus, Moraxella, Bordatella, and Campylobacter. In a preferred embodiment the enzyme is found in a bacteria of the genus Neisseria, for example N. meningitidis or N. gonorrhea. In a highly preferred embodiment, the enzyme is found in N. meningitidis.

[0101] Preferably the glycosyltransferase is derivable from an organism possessing a lipooligosaccharide (LOS). The lipooligosaccharide may mimic human glycolipids in order to avoid detection by the immune system. For example, the LOS may mimic human lacto-N-neotetraose, sialylacto-N-neotetraose and/or the Pk blood group glycolipid. In a highly preferred embodiment, the enzyme is capable of adding an α-galactose to a terminal lactose of the LOS structure, creating a Pk blood group glycolipid mimic.

[0102] A glycosyltransferase or part thereof in the present invention may be a wild type enzyme, or part thereof, or a mutant, variant or homologue of such an enzyme.

[0103] The term “wild type” refers to a polypeptide having a primary amino acid sequence which is identical with the native enzyme (for example, the bacterial enzyme).

[0104] The term “mutant” refers to a polypeptide having a primary amino acid sequence which differs from the wild type sequence by one or more amino acid additions, substitutions or deletions. Preferably, the mutant has at least 90% sequence identity with the wild type sequence. Preferably, the mutant has 20 mutations or less over the whole wild-type sequence. More preferably the mutant has 10 mutations or less, most preferably 5 mutations or less over the whole wild-type sequence. A mutant may or may not be functional.

[0105] The term “variant” refers to a naturally occurring polypeptide which differs from a wild-type sequence. A variant may be found within the same species (i.e. if there is more than one isoform of the enzyme) or may be found within a different species. Preferably the variant has at least 90% sequence identity with the wild type sequence. Preferably, the variant has 20 mutations or less over the whole wildtype sequence. More preferably, the variant has 10 mutations or less, most preferably 5 mutations or less over the whole wild-type sequence.

[0106] The term “part” indicates that the polypeptide comprises a fraction of the wild-type amino acid sequence. It may comprise one or more large contiguous sections of sequence or a plurality of small sections. The “part” may comprise a ligand binding pocket as described herein. The polypeptide may also comprise other elements of sequence, for example, it may be a fusion protein with another protein (such as one which aids isolation or crystallisation of the polypeptide). Preferably the polypeptide comprises at least 50%, more preferably at least 65%, most preferably at least 80% of the wild-type sequence.

[0107] The term “homologue” means a polypeptide having a degree of homology with the wild-type amino acid sequence. The term “homology” can be equated with “identity”.

[0108] In the present context, a homologous sequence is taken to include an amino acid sequence which may be at least 75, 85 or 90% identical, preferably at least 95 or 98% identical to the wild-type sequence. Typically, the homologues will comprise the same sites (for example LBP) as the subject amino acid sequence. Although homology can also be considered in terms of similarity (i.e. amino acid residues having similar chemical properties/functions), in the context of the present invention it is preferred to express homology in terms of sequence identity.

[0109] Homology comparisons can be conducted by eye, or more usually, with the aid of readily available sequence comparison programs. These commercially available computer programs can calculate % homology between two or more sequences (e.g. Wilbur, W. J. and Lipman, D. J. Proc. Natl. Acad. Sci. USA (1983), 80:726-730).

[0110] 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 is 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.

[0111] 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.

[0112] 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 the default gap penalty for amino acid sequences is −12 for a gap and −4 for each extension.

[0113] Calculation of maximum % 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 offline and online 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. A new tool, called BLAST 2 Sequences is also available for comparing protein and nucleotide sequence (see FEMS Microbiol Lett 1999 174(2): 247-50; FEMS Microbiol Lett 1999 177(1): 187-8 and tatiana@ncbi.nln.nih.gov).

[0114] Although the final % homology can be measured in terms of identity, 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). For some applications, 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.

[0115] Once the software has produced an optimal alignment, it is possible to calculate % homology, preferably % sequence identity. The software typically does this as part of the sequence comparison and generates a numerical result.

[0116] The sequences may have deletions, insertions or substitutions of amino acid residues which produce a silent change and result in a functionally equivalent enzyme. Deliberate amino acid substitutions may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues as long as the secondary binding activity of the substance is retained. For example, negatively charged amino acids include aspartic acid and glutamic acid; positively charged amino acids include lysine and arginine; and amino acids with uncharged polar head groups having similar hydrophilicity values include leucine, isoleucine, valine, glycine, alanine, asparagine, glutamine, serine, threonine, phenylalanine, and tyrosine.

[0117] 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:

1ALIPHATICNon-polarG A PI L VPolar - unchargedC S T MN QPolar - chargedD EK RAROMATICH F W Y

[0118] The polypeptide may also have a homologous substitution (substitution and replacement are both used herein to mean the interchange of an existing amino acid residue, with an alternative residue) i.e. like-for-like substitution such as basic for basic, acidic for acidic, polar for polar etc. Non-homologous substitution may also occur i.e. from one class of residue to another or alternatively involving the inclusion of unnatural amino acids such as ornithine (hereinafter referred to as Z), diaminobutyric acid ornithine (hereinafter referred to as B), norleucine ornithine (hereinafter referred to as O), pyriylalanine, thienylalanine, naphthylalanine and phenylglycine.

[0119] Replacements may also be made by unnatural amino acids include; alpha* and alpha-disubstituted* amino acids, N-alkyl amino acids*, lactic acid*, halide derivatives of natural amino acids such as trifluorotyrosine*, p-Cl-phenylalanine*, p-Br-phenylalanine*, p-I-phenylalanine*, L-allyl-glycine*, β-alanine*, L-a-amino butyric acid*, L-γ-amino butyric acid*, L-α-amino isobutyric acid*, L-ε-amino caproic acid#, 7-amino heptanoic acid*, L-methionine sulfone#*, L-norleucine*, L-norvaline*, p-nitro-L-phenylalanine*, L-hydroxyproline#, L-thioproline*, methyl derivatives of phenylalanine (Phe) such as 4-methyl-Phe*, pentamethyl-Phe*, L-Phe (4-amino), L-Tyr (methyl)*, L-Phe (4-isopropyl)*, L-Tic (1,2,3,4-tetrahydroisoquinoline-3-carboxyl acid)*, L-diaminopropionic acid# and L-Phe (4-benzyl)*. The notation * has been utilised for the purpose of the discussion above (r lating to homologous or non-homologous substitution), to indicate the hydrophobic nature of the derivative whereas # has been utilised to indicate the hydrophilic nature of the derivative, #* indicates amphipathic characteristics.

[0120] Variant amino acid sequences may include suitable spacer groups that may be inserted between any two amino acid residues of the sequence including alkyl groups such as methyl, ethyl or propyl groups in addition to amino acid spacers such as glycine or β-alanine residues. A further form of variation, involving the presence of one or more amino acid residues in peptoid form, will be well understood by those skilled in the art. For the avoidance of doubt, “the peptoid form” is used to refer to variant amino acid residues wherein the α-carbon substituent group is on the residue's nitrogen atom rather than the α-carbon. Processes for preparing peptides in the peptoid form are known in the art, for example Simon R J et al., PNAS (1992) 89(20), 9367-9371 and Horwell D C, Trends Biotechnol. (1995) 13(4), 132-134.

[0121] Crystal

[0122] The invention provides a crystal of a retaining glycosyltransferase or a part or fragment thereof, in particular a ligand binding pocket of a glycosyltransferase.

[0123] As used herein, the term “crystal” or “crystalline” means a structure (such as a three dimensional (3D) solid aggregate) in which the plane faces intersect at definite angles and in which there is a regular structure (such as internal structure) of the constituent chemical species. Thus, the term “crystal” can include any one of: a solid physical crystal form such as an experimentally prepared crystal, a crystal structure derivable from the crystal (including secondary and/or tertiary and/or quaternary structural elements), a 2D and/or 3D model based on the crystal structure, a representation thereof such as a schematic representation thereof or a diagrammatic representation thereof, or a data set thereof for a computer. In one aspect, the crystal is usable in X-ray crystallography techniques. Here, the crystals used can withstand exposure to X-ray beams used to produce a diffraction pattern data necessary to solve the X-ray crystallographic structure. A crystalline form of a glycosyltransferase, may be characterized as being capable of diffracting x-rays in a pattern defined by one of the crystal forms depicted in Blundel et al 1976, Protein Crystallography, Academic Press.

[0124] A crystal of the invention comprises an N-terminal α/β pocket with a central core β-sheet characterized by the following: seven strands (β3, β2, β1, β4, β7, β6, β8) all of which are parallel with the exception of β7; the first 100 residues form a nucleotide binding fold composed of four parallel strands sandwiched between two helices (i.e. A and B) on one side and two helices (i.e. C and D) on the other; and the remainder of the core β-sheet is flanked by three α-helices on one side and five on the other.

[0125] The crystal may also be characterized by an antiparallel β-ribbon formed by β5 and β9 lying almost perpendicular to the core β3-sheet, and a substrate binding cleft that lies along the base of the core β3-sheet.

[0126] The C-terminal domain that mediates membrane attachment of a bacterial glycosyltransferase may be predominantly helical. In particular, it may comprise two helices [i.e. helix M and helix N (which is 310 in nature)] that form a small pedestal that packs perpendicular to the helices of the nucleotide binding motif and to the β-ribbon.

[0127] An illustration of a structure of the invention is shown in FIG. 3.

[0128] In an embodiment, a crystal of a glycosyltransferase of the invention belongs to space group P212121. The term “space group” refers to the lattice and symmetry of the crystal. In a space group designation the capital letter indicates the lattice type and the other symbols represent symmetry operations that can be carried out on the contents of the asymmetric unit without changing its appearance

[0129] A crystal of the invention may comprise a unit cell having the following unit dimensions: a=37.79 (∀0.05) Å, b=76.05 (∀0.05) Å, c=86.84 (∀0.05) Å. The term “unit cell” refers to the smallest and simplest volume element (i.e. parallelpiped-shaped block) of a crystal that is completely representative of the unit of pattern of the crystal. The unit cell axial lengths are represented by a, b, and c. Those of skill in the art understand that a set of atomic coordinates determined by X-ray crystallography is not without standard error.

[0130] In a preferred embodiment, a crystal of the invention has the structural coordinates of the enzyme as shown in Table 4, Table 5, or Table 6. As used herein, the term “structural coordinates” refers to a set of values that define the position of one or more amino acid residues with reference to a system of axes. A data set of structural coordinates defines the three dimensional structure of a molecule or molecules. The term refers to a data set that defines the three dimensional structure of a molecule or molecules (e.g. Cartesian coordinates, temperature factors, and occupancies). Structural co-ordinates can be slightly modified and still render nearly identical three dimensional structures. A measure of a unique set of structural coordinates is the root-mean-square deviation of the resulting structure. Structural coordinates that render three dimensional structures (in particular a three dimensional structure of a ligand binding pocket) that deviate, from one another by a root-mean-square deviation of less than 5 Å, 4 Å, 3 Å, 2 Å, or 1.5 Å may be viewed by a person of ordinary skill in the art as very similar.

[0131] Variations in structural coordinates may be generated because of mathematical manipulations of the. structural coordinates of a glycosyltransferase described herein. For example, the structural coordinates of Table 4, 5, or 6 may be manipulated by crystallographic permutations of the structural coordinates, fractionalization of the structural coordinates, integer additions or substractions to sets of the structural coordinates, inversion of the structural co-ordinates or any combination of the above.

[0132] Variations in the crystal structure due to mutations, additions, substitutions, and/or deletions of the amino acids, or other changes in any of the components that make up the crystal may also account for modifications in structural coordinates. If such modifications are within an acceptable standard error as compared to the original structural coordinates, the resulting structure may be the same. Therefore, a ligand that bound to a ligand binding pocket of an α1,4-galactosyltransferase would also be expected to bind to another ligand binding pocket whose structural coordinates defined a shape that fell within the acceptable error. Such modified structures of a ligand binding pocket thereof are also within the scope of the invention.

[0133] Various computational analyses may be used to determine whether a ligand or a ligand binding pocket thereof is sufficiently similar to all or parts of a ligand or a ligand binding pocket thereof. Such analyses may be carried out using conventional software applications and methods as described herein.

[0134] A crystal of the invention may also be specifically characterised by the parameters, diffraction statistics and/or refinement statistics set out in Table 2.

[0135] A crystal of the invention may comprise the entire sequence of a retaining galactosyltransferase, preferably from glycosyltransferase family 8 (e.g. see FIG. 2), preferably an α1,4-galactosyltransferase, and most preferably an α-1,4-galactosyltransferase (LgtC) derivable from Neisseria meningitidis. A crystal of the invention may comprise a sequence of a retaining galactosyltransferase with a deletion in or around the C-terminus. Preferably the deletion and/or mutation in the C-terminus is sufficient to facilitate crystallisation of the protein. A crystallized enzyme may not include the portion of a bacterial glycosyltransferase enzyme that attaches to the surface of a bacterial membrane. For example, the C-terminal 25 to 50 amino acid residues may be deleted from an α-1,4-galactosyltransferase (LgtC) derivable from Neisseria meningitidis.

[0136] Ligand-Binding Pocket

[0137] In an embodiment the invention provides a crystal comprising a ligand binding pocket.

[0138] “Ligand binding pocket” or “LBP” refers to a region of a molecule or molecular complex that as a result of its shape, favourably associates with a ligand or a part thereof. For example, it may be a region of a glycosyltransferase that is responsible for binding a ligand including a donor molecule, an acceptor molecule and/or a sugar during transfer (e.g. active site binding pocket). With reference to the models and structures of the invention, residues in a ligand binding pocket may be defined by their spatial proximity to a ligand in a model or structure.

[0139] A “ligand” refers to a compound or entity that associates with a ligand binding pocket, including substrates such as acceptor molecules or analogues or parts thereof, donor molecules or analogues or parts thereof A ligand may be designed rationally by using a model according to the present invention. A ligand may be a modulator of a glycosyltransferase including an inhibitor.

[0140] A “donor molecule” or “sugar nucleotide donor” refers to a molecule capable of donating a sugar to an acceptor molecule, via the action of a glycosyltransferase enzyme. The donor molecule may be di- or poly-saccharides, sugar 1-phosphates, or, most commonly, nucleotide diphosphosugars (NDP-sugars), or nucleotide phosphosugars. In a preferred embodiment, the donor molecule is UDP-galactose, UDP glucose, UDP mannose, UDP-N-acetylglucosamine, UDP-N-acetylgalactosamine, UDP-N-acetymannosamine, UDP-glucuronic acid, UDP-galacturonic acid, UDP-fucose, UDP-xylose, UDP-rhamnose, and ADP, GDP and TDP derivatives thereof, and CMP sialic acid.

[0141] An acceptor molecule is capable of accepting a sugar from a donor molecule, via the action of a glycosyltransferase enzyme. It may, for example, comprise a terminal sugar residue for transfer purposes. The acceptor molecule or aglycone can be, for example, a lipid, a protein, a heterocyclic compound, an antibiotic, a peptide, an amino acid, an aromatic or aliphatic alcohol or thiol or another carbohydrate residue. In a preferred embodiment, the donor molecule is or comprises a terminal lactose.

[0142] An analogue of a donor or acceptor molecule is one which mimics the donor or acceptor molecule, binding in the LBP, but which is incapable (or has a significantly reduced capacity) to take part in the transfer reaction. For example, UDP-Gal can act as a donor sugar for a galactosyltransferase. UDP-2Fgal, on the other hand, acts as a donor sugar analogue. The fluorine at the 2-position destabilises the transition state for the transfer reaction, so that effectively no transfer occurs. Similarly, UDPGlcNAc can act as a donor sugar for GnT1 and the methylene phosphonate analogue can act as a donor sugar analogue. By the same token, a terminal lactose can act as an acceptor sugar for a α1,4 galactosyltransferase. 4-deoxylactose is non reactive and is an example of an acceptor molecule analogue.

[0143] The term “ligand binding pocket” (LBP) includes a homologue of the ligand binding pocket or a portion thereof. As used herein, the term “homologue” in reference to a ligand binding pocket refers to ligand binding pocket or a portion thereof which may have deletions, insertions or substitutions of amino acid residues as long as the binding specificity of the molecule is retained. In this regard, deliberate amino acid substitutions may be made on the basis of similarity in polarity, charge, solubility, hydrophobicity, hydrophilicity, and/or the amphipathic nature of the residues as long as the binding specificity of the ligand binding pocket is retained.

[0144] As used herein, the term “portion thereof” means the structural co-ordinates corresponding to a sufficient number of amino acid residues of the glycosyltransferase LBP (or homologues thereof) that are capable of associating or interacting with a ligand. This term includes glycosyltransferase ligand binding pocket amino acid residues having amino acid residues from about 4 Å to about 5 Å of an associated ligand or part thereof. Thus, for example, the structural co-ordinates provided in a crystal structure may contain a subset of the amino acid residues in the LBP which may be useful in the modelling and design of compounds that bind to the LBP.

[0145] A crystal of the invention may comprise a ligand binding pocket and at least part of the pocket which may be involved in attaching the enzyme to the bacterial membrane. Preferably the crystal comprises the entire sequence of the enzyme, optionally with a deletion in or around the C-terminus. Preferably the deletion and/or mutation in the C-terminus is sufficient to facilitate crystallisation of the protein.

[0146] A ligand-binding pocket may comprise an active site binding pocket of a glycosyltransferase. The active site binding pocket refers to the region of a glycosyltransferase where the transfer of a sugar from the donor molecule to the acceptor occurs. In accordance with one aspect, the invention contemplates a crystal of an active site binding pocket of a retaining glycosyltransferase comprising a core β-sheet containing 7 strands (β3, β2, β1, β4, β6, β8 in FIG. 3) all of which are parallel with the exception of β7; the core β-sheet further characterized by a nucleotide binding motif composed of four parallel strands sandwiched between helices A and B on one side and helices C and D on the other as shown in FIG. 3. A polypeptide comprising an active site binding pocket with the shape and structure of an active site binding pocket described herein is also within the scope of the invention.

[0147] The ligand binding pocket may comprise a pocket of a glycosyltransferase structure described herein that is capable of associating with a donor molecule, preferably a nucleotide or portion thereof. A ligand binding pocket may comprise the amino acid residues at the C-terminus of β1 and the N-terminus of helix A of a glycosyltransferase structure as described herein, that are capable of associating with a nucleotide of a donor molecule as described herein. In particular, a ligand-binding pocket may comprise one or both of the loops that associate with a donor molecule or analogue. Such a ligand binding pocket may comprise a loop comprising residues 75-80 and/or a loop comprising residues 246-251 of a glycosyltransferase described herein or a homologue thereof.

[0148] A ligand binding pocket may comprise a cleft at the C-terminal end of a glycosyltransferase β-sheet structure as described herein that is capable of associating with a uridine diphosphate. The ligand binding pocket may comprise a conserved Tyr 11 (Phe in E. coli and Salmonella) of a glycosyltransferase structure as described herein that is capable of stacking with a uracil base.

[0149] When UDP-Gal is capable of acting as a donor molecule for the glycosyltransferase enzyme, preferably the ligand binding pocket may comprise at least one of the residues involved in binding to the UDP portion of UDP-Gal, namely: Tyr 11, Asn 10, Asp 8, Ala 6, Ile 104, Lys 250, Gly 247 and His 78 or a homologue thereof.

[0150] When UDP-Gal is capable of acting as a donor molecule for the glycosyltransferase enzyme, preferably the ligand binding pocket may comprise at least one of the residues involved in binding to the UDP portion of UDP-Gal, namely: Asp 8, Asn 10, Ala 6, Ile 104, Lys 250, Gly 247, and His 78 or a homologue thereof.

[0151] Alternatively, or more preferably in addition, the ligand binding pocket may comprise at least one of the residues involved in shielding the reactive center C1′ atom from water, namely: Ile 76, Asp 103, Asp 153, Ala 154, Gly 155, Tyr 186, Gln 189, His 244, Cys 246 and Gly 247; or a homologue thereof.

[0152] Based on the crystal of LgtC herein, Gln 189 may act as the nucleophile during the transfer reaction. Hence, in an embodiment a crystal of the invention comprises Gln 189 or a homologue thereof. Preferably, the Glnl89 is oriented through hydrogen bonds to both sugar (donation of a hydrogen bond from Nεl to O6 of lactose) and conserved protein side chains (acceptance of a hydrogen bond from the side chain Nε2 of Asn153).

[0153] Alternatively, or more preferably in addition, the ligand binding pocket may comprise at least one of the residues involved in binding to a sugar moiety of a donor molecule such as the galactosyl moiety of UDP-Gal, namely: Asp103, Arg 86, Asp 188, and optionally one or more of Asn 153, Val 79, Thr 83, Gln 187 and Gln 189 or a homologue thereof.

[0154] When lactose is capable of acting as an acceptor molecule for the glycosyltransferase. enzyme, the ligand binding pocket may comprise at least one of the residues involved in binding to lactose, namely: Asp130, Gln 189, Val 76, His 78, Tyr 186, Cys 246, Gly 247, Phe 132, Pro 211, Pro 248, Thr 212 and Cys 246; or a homologue thereof.

[0155] With reference to a crystal of the present invention, residues in the LBP may be defined by their spatial proximity to a ligand in the crystal structure. For example, such may be defined by their proximity to a donor and/or an acceptor molecule.

[0156] A ligand binding pocket may comprise one or more of the residues involved in co-ordination of a Mn2+ ion, namely: His 244, Asp 103 and Asp 105; or a homologue thereof.

[0157] Preferably a LBP comprises at least one DXD motif. A “DXD” sequence motif is common to a wide range of glycosyltransferases, both in prokaryotes and eukaryotes, even though they may not share other sequence similarities. (Campbell et al., 1997 Biochemical Journal 326, 929-939, Breton et al., 1998 Journal of Biochemistry 123, 1000-1009 and Kapitonov and Yu, 1999 Glycobiology 9, 961-978). This motif has been proposed to be involved in the coordination of a divalent cation in the binding of the nucleotide sugar (Busch et al., 1998 The Journal of Biological Chemistry 273, 19566-19572). A number of mutagenesis studies have been carried out in various species on the conserved aspartate residues in the DXD sequence and all have found that enzymatic activity is completely abolished upon removal of the carboxylate (Shibayama et al., 1998 Journal of Bacteriology 180, 5313-5318, Wiggins and Munro, 1998 Proc. Natl. Acad Sci. USA 95, 7945-7950, Busch et al., 1998 (as above) and Hagen et al., 1999 The Journal of Biological Chemistry 274, 6797-6803).

[0158] A ligand binding pocket may comprise one or more of the amino acid residues for a glycosyltransferase structure of the invention identified by atomic contacts on the enzyme for atomic interactions numbers 1 through 17 shown in Table 3.

[0159] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase that associates with a diphosphate of a sugar nucleotide donor molecule is provided comprising one or both of the enzyme atomic contacts of atomic interactions 6 and 7 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the diphosphate group, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket is defined by the atoms of the enzyme atomic contacts of atomic interactions 6 and/or 7 having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0160] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase that associates with a heterocyclic amine base (preferably uracil) of a sugar nucleotide donor molecule is provided comprising one, two, or three of the enzyme atomic contacts of atomic interactions 1,2, and 3 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the heterocyclic amine base, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket is defined by the atoms of the enzyme atomic contacts of atomic interactions 1, 2, and/or 3 having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0161] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase that associates with a sugar of the nucleotide (preferably ribose) of a sugar nucleotide donor molecule is provided comprising one or both of the enzyme atomic contacts of atomic interactions 4 and 5 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the sugar, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket is defined by the atoms of the enzyme atomic contacts of atomic interactions 4 and/or 5 having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0162] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase that associates with a sugar to be transferred (e.g. Gal) of a sugar nucleotide donor molecule is provided comprising one, two, or three enzyme atomic contacts of atomic interactions 8, 9, and 10 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the selected sugar, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket is defined by the atoms of the enzyme atomic contacts of atomic interactions 8, 9, and/or 10 having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0163] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase that associates with a nucleotide (preferably UDP) of a sugar nucleotide donor molecule is provided comprising one, two, three, four, five, six, or seven enzyme atomic contacts of atomic interactions 1 through 7 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the nucleotide, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of a binding pocket is defined by the atoms of one, two, three, four, five, six, or seven enzyme atomic contacts of atomic interactions 1 through 7 having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0164] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase that associates with a sugar nucleotide donor molecule (e.g. UDP-Gal) is provided comprising one, two, three, four, five, six, seven, eight, nine, or ten enzyme atomic contacts of atomic interactions 1 through 10 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the sugar nucleotide donor molecule, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket is defined by the atoms of one, two, three, four, five, six, seven, eight, nine, or ten enzyme atomic contacts of atomic interactions 1 through 10 having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0165] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase that associates with an acceptor molecule (e.g. acceptor with a terminal lactose) is provided comprising one two, three, four, five, or six enzyme atomic contacts of atomic interactions 12 through 17 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the acceptor molecule, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket is defined by the atoms of one, two, three, four, five, or six enzyme atomic contacts of atomic interactions 12 through 17 having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0166] Complexes

[0167] A crystal of the invention includes a crystalline glycosyltransferase or part thereof (e.g. ligand binding pocket) in association with one or more moieties, including heavy-metal atoms i.e. a derivative crystal, a metal cofactor, or one or more ligands or molecules i.e. a co-crystal.

[0168] The term “associate”, “association” or “associating” refers to a condition of proximity between a moiety (i.e. chemical entity or compound or portions or fragments thereof), and a glycosyltransferase, or parts or fragments thereof (e.g. ligand binding pockets). The association may be non-covalent i.e. where the juxtaposition is energetically favoured by for example, hydrogen-bonding, van der Waals, or electrostatic or hydrophobic interactions, or it may be covalent.

[0169] The term “heavy-metal atoms” refers to an atom that can be used to solve an x-ray crystallography phase problem, including but not limited to a transition element, a lanthanide metal, or an actinide metal. Lanthanide metals include elements with atomic numbers between 57 and 71, inclusive. Actinide metals include elements with atomic numbers between 89 and 103, inclusive.

[0170] Multiwavelength anomalous diffraction (MAD) phasing may be used to solve protein structures using selenomethionyl (SeMet) proteins. Therefore, a complex of the invention may comprise a crystalline glycosyltransferase or part thereof (e.g. ligand binding pocket) with selenium associated with the methionine residues of the protein.

[0171] In an embodiment of the invention, a ligand binding pocket is in association with a metal cofactor in the crystal. A “metal cofactor” refers to a metal required for glycosyltransferase activity and/or stability. For example, the metal cofactor may be manganese, and other similar atoms or metals. Different glycosyltransferases may require different cofactors, for example Mn2+, Mg2+, Co2+, Zn2+, Fe2+, and Ca2+. In a preferred embodiment the LBP is in association with manganese.

[0172] A ligand binding pocket in a complex with a cofactor preferably comprises one or more of the residues involved in co-ordination of a Mn2+ ion, namely: His 244, Asp 103 and Asp 105; or a homologue thereof. Preferably the LBP comprises at least one DXD motif.

[0173] A crystal may comprise a complex between a ligand-binding pocket and one or more ligands or molecules. In other words the ligand binding pocket may be associated with one or more ligands or molecules in the crystal. The ligand may be any compound which is capable of stably and specifically associating with the ligand binding pocket A ligand may, for example, be a substrate such as a donor or an acceptor molecule or analogue thereof, and/or the ligand may be a modulator of the glycosyltransferase.

[0174] Therefore, the present invention also provides:

[0175] (a) a crystal comprising a ligand binding pocket of a glycosyltransferase and a donor molecule or analogue thereof;

[0176] (b) a crystal comprising a ligand binding pocket of a glycosyltransferase and an acceptor molecule or analogue thereof;

[0177] (c) a crystal comprising a ligand binding pocket of a glycosyltransferase and a donor molecule or analogue thereof, and an acceptor molecule thereof .

[0178] A complex may comprise one or more of the atomic interactions identified in Table 3. A structure of a complex of the invention may be defined by selected atomic interactions, preferably the atomic interactions as defined in Table 3.

[0179] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase in association with a diphosphate of a sugar nucleotide donor molecule is provided comprising one or both of atomic interactions 6 and 7 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the diphosphate group, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of such a complex is defined by the atoms of the atomic contacts of the atomic interactions having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0180] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase in association with a heterocyclic amine base (preferably uracil) of a sugar nucleotide donor molecule is provided comprising one, two, or three of atomic interactions 1, 2, and 3 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the heterocyclic amine base, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of a such a complex is defined by the atoms of the atomic contacts of the atomic interactions having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0181] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase in association with a sugar of the nucleotide (preferably ribose) of a sugar nucleotide donor molecule is provided comprising one or both of atomic interactions 4 and. 5 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the sugar, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of such a complex is defined by the atoms of the atomic contacts of the atomic interactions having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0182] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase in association with a sugar to be transferred (e.g. Gal) of a sugar nucleotide donor molecule is provided comprising one, two, or three of atomic interactions 8, 9, and 10 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the selected sugar, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of such a complex is defined by the atoms of the atomic contacts of the atomic interactions having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0183] In an embodiment of the invention, a crystal of a ligand binding pocket or secondary, tertiary, and/or quanternary structure of a glycosyltransferase in association with a nucleotide (preferably UDP) of a sugar nucleotide donor molecule is provided comprising one, two, three, four, five, six, or seven of atomic interactions 1 through 7 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the nucleotide, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably, a crystal or secondary, tertiary, and/or quanternary structure of such a complex is defined by the atoms of the atomic contacts of the atomic interactions having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0184] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase in association with a sugar nucleotide donor molecule (e.g. UDP-Gal) is provided comprising one, two, three, four, five, six, seven, eight, nine, or ten of atomic interactions 1 through 10 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the sugar nucleotide donor molecule, and an atomic contact (more preferably, a specific amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably a crystal or secondary, tertiary, and/or quanternary structure of such a complex is defined by the atoms of the atomic contacts of atomic interactions having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0185] In an embodiment of the invention, a crystal or secondary, tertiary, and/or quanternary structure of a ligand binding pocket of a glycosyltransferase in association with an acceptor molecule (e.g. acceptor with a terminal lactose) is provided comprising one two, three, four, five, or six of atomic interactions 12 through 17 identified in Table 3, each atomic interaction defined therein by an atomic contact (more preferably, a specific atom where indicated) on the acceptor molecule, and an atomic contact (more preferably, a specific. amino acid residue where indicated) on the glycosyltransferase (i.e. enzyme atomic contact). Preferably a crystal or secondary, tertiary, and/or quanternary structure of such a complex is defined by the atoms of the atomic contacts of the atomic interactions having the structural coordinates for the atoms listed in Table 4, 5, or 6.

[0186] In an embodiment a crystal of the invention comprises a ligand binding pocket of a galactosyltransferase in association with a donor molecule, such as UDP-2Fgal and/or an acceptor molecule such as 4-deoxylactose or lactose. These complexes may have the structural coordinates shown in Table 4, 5, or 6.

[0187] A crystal of the invention may enable the determination of structural data for the donor molecule or acceptor molecule. In order to be able to derive structural data for the donor/acceptor molecule, it is necessary for the molecule to have sufficiently strong electron density to enable a model of the molecule to be built using standard techniques. For example, there should be sufficient electron density to allow a model to be built using XTALVIEW (McRee 1992 J. Mol. Graphics. 10 44-46).

[0188] Method of Making a Crystal

[0189] The present invention also provides a method of making a crystal according to the invention. The crystal may be formed from an aqueous solution comprising a purified polypeptide comprising a glycosyltransferase or part or fragment thereof (e.g. a catalytic portion, ligand binding pocket). A method may utilize a purified polypeptide comprising a glycosyltransferase ligand binding pocket to form a crystal

[0190] The term “purified” in reference to a polypeptide, does not require absolute purity such as a homogenous preparation rather it represents an indication that the polypeptide is relatively purer than in the natural environment Generally, a purified polypeptide is substantially free of other proteins, lipids, carbohydrates, or other materials with which it is naturally associated, preferably at a functionally significant level for example at least 85% pure, more preferably at least 95% pure, most preferably at least 99% pure. A skilled artisan can purify a polypeptide comprising a glycosyltransferase using standard techniques for protein purification. A substantially pure polypeptide comprising a glycosyltransferase will yield a single major band on a non-reducing polyacrylamide gel. The purity of the glycosyltransferase can also be determined by amino-terminal amino acid sequence analysis.

[0191] A polypeptide used in the method may be chemically synthesized in whole or in part using techniques that are well-known in the art. Alternatively, methods are well known to the skilled artisan to construct expression vectors containing the native or mutated glycosyltransferase coding sequence and appropriate transcriptional/translational control signals. These methods include in vitro recombinant DNA techniques, synthetic techniques, and in vivo recombination/genetic recombination. See for example the techniques described in Sambrook et al. Molecular Cloning: A Laboratory Manual, 2nd Edition, Cold Spring Harbor Laboratory press (1989)), and other laboratory textbooks. (See also Sarker et al, Glycoconjugate 1. 7:380, 1990; Sarker et al, Proc. Natl. Acad, Sci. USA 88:234-238, 1991, Sarker et al, Glycoconjugate J. 11: 204-209, 1994; Hull et al, Biochem Biophys Res Commun 176:608, 1991 and Pownall et al, Genomics 12:699-704, 1992).

[0192] Preferably the polypeptide comprises a glycosyltransferase enzyme or part thereof having a mutation in the part of the enzyme which is involved in attachment to bacterial membranes. In a preferred embodiment the polypeptide comprises a glycosyltransferase enzyme or part thereof having a deletion at or around the C-terminus. In particular, such a deletion may serve to reduce the proportion of basic and/or hydrophobic and/or aromatic residues. The polypeptide may, for example, be missing the C-terminal 25 residues.

[0193] Preferably the polypeptide comprises one or more mutations which serve to reduce or eliminate aggregation of the polypeptide. For example, the polypeptide may comprise one or more mutations (e.g. substitutions or deletions) of cysteine residues.

[0194] Crystals may be grown from an aqueous solution containing the purified glycosyltransferase polypeptide by a variety of conventional processes. These processes include batch, liquid, bridge, dialysis, vapor diffusion, and hanging drop methods. (See for example, McPherson, 1982 John Wiley, New York; McPherson, 1990, Eur. J. Biochem. 189: 1-23; Webber. 1991, Adv. Protein Chem. 41:1-36). Generally, the native crystals of the invention are grown by adding precipitants to the concentrated solution of the glycosyltransferase polypeptide. The precipitants are added at a concentration just below that necessary to precipitate the protein. Water is removed by controlled evaporation to produce precipitating conditions, which are maintained until crystal growth ceases.

[0195] Derivative crystals of the invention can be obtained by soaking native crystals in a solution containing salts of heavy metal atoms. A complex of the invention can be obtained by soaking a native crystal in a solution containing a compound that binds the polypeptide, or they can be obtained by co-crystallizing the polypeptide in the presence of one or more compounds. In order to obtain co-crystals with a compound which binds deep within the tertiary structure of the polypeptide (for example UDP-2FGal is almost entirely buried by LgtC when bound) it is necessary to use the second method.

[0196] In a preferred embodiment, the polypeptide is cocrystallised with a compound which stabilises the polypeptide. For example, the compound may stabilise one or both of the loops made up of residues 75-80 and 246-251. In a highly preferred embodiment the polypeptide is cocrystallised with an inert analogue of the sugar donor, for example UDP 2-deoxy-2-fluorogalactose.

[0197] Once the crystal is grown it can be placed in a glass capillary tube and mounted onto a holding device connected to an X-ray generator and an X-ray detection device. Collection of X-ray diffraction patterns are well documented by those skilled in the art (See for example, Ducruix and Geige, 1992, IRL Press, Oxford, England). A beam of X-rays enter the crystal and diffract from the crystal. An X-ray detection device can be utilized to record the diffraction patterns emanating from the crystal. Suitable devices include the Marr 345 imaging plate detector system with an RU200 rotating anode generator.

[0198] Methods for obtaining the three dimensional structure of the crystalline form of a molecule or complex are described herein and known to those skilled in the art (see Ducruix and Geige 1992, IRL Press, Oxford, England). Generally, the x-ray crystal structure is given by the diffraction patterns. Each diffraction pattern reflection is characterized as a vector and the data collected at this stage determines the amplitude of each vector. The phases of the vectors may be determined by the isomorphous replacement method where heavy atoms soaked into the crystal are used as reference points in the X-ray analysis (see for example, Otwinowski, 1991, Daresbury, United Kingdom, 80-86). The phases of the vectors may also be determined by molecular replacement (see for example, Naraza, 1994, Proteins 11:281-296). The amplitudes and phases of vectors from the crystalline form of a glycosyltransferase determined in accordance with these methods can be used to analyze other related crystalline polypeptides.

[0199] The unit cell dimensions and symmetry, and vector amplitude and phase information can be used in a Fourier transform function to calculate the electron density in the unit cell i.e. to generate an experimental electron density map. This may be accomplished using the PHASES package (Furey, 1990). Amino acid sequence structures are fit to the experimental electron density map (i.e. model building) using computer programs (e.g. Jones, T A. et al, Acta Crystallogr A47, 100-119, 1991). This structure can also be used to calculate a theoretical electron density map. The theoretical and experimental electron density maps can be compared and the agreement between the maps can be described by a parameter referred to as R-factor. A high degree of overlap in the maps is represented by a low value R-factor. The R-factor can be minimized by using computer programs that refine the structure to achieve agreement between the theoretical and observed electron density map. For example, the XPLOR program, developed by Brunger (1992, Nature 355:472-475) can be used for model refinement.

[0200] A three dimensional structure of the molecule or complex may be described by atoms that fit the theoretical electron density characterized by a minimum R value. Files can be created for the structure that defines each atom by co-ordinates in three dimensions.

[0201] Model

[0202] A crystal structure of the present invention may be used to make a model of the glycosyltransferase or a part thereof, (e.g. a ligand-binding pocket). A model may, for example, be a structural model or a computer model. A model may represent the secondary, tertiary and/or quaternary structure of the glycosyltransferase. The model itself may be in two or three dimensions. It is possible for a computer model to be in three dimensions despite the constraints imposed by a conventional computer screen, if it is possible to scroll along at least a pair of axes, causing “rotation” of the image.

[0203] As used herein, the term “modelling” includes the quantitative and qualitative analysis of molecular structure and/or function based on atomic structural information and interaction models. The term “modelling” includes conventional numeric-based molecular dynamic and energy minimization models, interactive computer graphic models, modified molecular mechanics models, distance geometry and other structure-based constraint models.

[0204] Preferably, modelling is performed using a computer and may be further optimized using known methods. This is called modelling optimisation.

[0205] The three dimensional structure of a new crystal may be modelled using molecular replacement The term “molecular replacement” refers to a method that involves generating a preliminary model of a molecule or complex whose structural co-ordinates are unknown, by orienting and positioning a molecule whose structural co-ordinates are known within the unit cell of the unknown crystal, so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal. Lattman, E., “Use of the Rotation and Translation Functions”, in Methods in Enzymology, 115, pp. 55-77 (1985); M. G. Rossmann, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York, (1972).

[0206] Commonly used computer software packages for molecular replacement are X-PLOR (Brunger 1992, Nature 355: 472-475), AMORE (Navaza, 1994, Acta Crystallogr. A50:157-163), the CCP4 package (Collaborative Computational Project, Number 4, “The CCP4 Suite: Programs for Protein Crystallography”, Acta Cryst., Vol. D50, pp. 760-763, 1994), the MERLOT package (P. M. D. Fitzgerald, J. Appl. Cryst., Vol. 21, pp. 273-278, 1988) and XTALVIEW (McCree et al (1992) J. Mol. Graphics 10: 44-46. It is preferable that the resulting structure not exhibit a root-mean-square deviation of more than 3 Å.

[0207] Molecular replacement computer programs generally involve the following steps: (1) determining the number of molecules in the unit cell and defining the angles between them (self rotation function); (2) rotating the known structure against diffraction data to define the orientation of the molecules in the unit cell (rotation function); (3) translating the known structure in three dimensions to correctly position the molecules in the unit cell (translation function); (4) determining the phases of the X-ray diffraction data and calculating an R-factor calculated from the reference data set and from the new data wherein an R-factor between 30-50% indicates that the orientations of the atoms in the unit cell have been reasonably determined by the method; and (5) optionally, decreasing the R-factor to about 20% by refining the new electron density map using iterative refinement techniques known to those skilled in the art (refinement).

[0208] The quality of the model may be analysed using a program such as PROCHECK or 3D-Profiler [Laskowski et al 1993 J. Appl. Cryst. 26:283-291; Luthy R. et al, Nature 356: 83-85, 1992; and Bowie, J. U. et al Science 253: 164-170, 1991]. Once any irregularities have been resolved, the entire structure may be further refined.

[0209] Other molecular modelling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al, “Molecular Modelling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883-894 (1990). See also, Navia, M. A. and M. A. Murcko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992).

[0210] Computer format of Crystals/Models

[0211] Information derivable from the crystal of the present invention (for example the structural coordinates) and/or the model of the present invention may be provided in a computer-readable format.

[0212] Therefore, the invention provides a computer readable medium or a machine readable storage medium which comprises the structural co-ordinates of a retaining glycosyltransferase including all or any parts of the glycosyltransferase (e.g ligand-binding pockets), one or more ligands including substrates, for example, acceptor molecules including portions thereof, or donor molecules including portions thereof. Such storage medium or storage medium encoded with these data are capable of displaying on a computer screen or similar viewing device, a three-dimensional graphical representation of a molecule or molecular complex which comprises the enzyme or ligand binding pockets or similarly shaped homologous enzymes or ligand binding pockets. Thus, the invention also provides computerized representations of a crystal of the invention, including any electronic, magnetic, or electromagnetic storage forms of the data needed to define the structures such that the data will be computer readable for purposes of display and/or manipulation.

[0213] In an aspect the invention provides a computer for producing a three-dimensional representation of a molecule or molecular complex, wherein said molecule or molecular complex comprises a retaining glycosyltransferase or ligand binding pocket thereof defined by structural coordinates of retaining glycosyltransferase amino acids or a ligand binding pocket thereof, or comprises structural coordinates of atoms of a ligand in particular a substrate (e.g. an acceptor or donor molecule), or a three-dimensional representation of a homologue of said molecule or molecular complex, wherein said computer comprises:

[0214] (a) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises the structural coordinates of a retaining glycosyltransferase amino acids according to Table 4, 5, or 6 or a ligand binding pocket thereof, or an acceptor or donor molecule according to Table 4, 5, or 6;

[0215] (b) a working memory for storing instructions for processing said machine-readable data;

[0216] (c) a central-processing unit coupled to said working memory and to said machine-readable data storage medium for processing said machine readable data into said three-dimensional representation; and

[0217] (d) a display coupled to said central-processing unit for displaying said three-dimensional representation.

[0218] A homologue may comprise a glycosyltransferase or ligand binding pocket thereof, or acceptor or donor molecule that has a root mean square deviation from the backbone atoms of not more than 1.5 angstroms.

[0219] The invention also provides a computer for determining at least a portion of the structural coordinates corresponding to an X-ray diffraction pattern of a molecule or molecular complex wherein said computer comprises:

[0220] (a) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises the structural coordinates according to Table 4, 5, or 6;

[0221] (b) a machine-readable data storage medium comprising a data storage material encoded with machine readable data wherein said data comprises an X-ray diffraction pattern of said molecule or molecular complex;

[0222] (c) a working memory for storing instructions for processing said machine-readable data of (a) and (b);

[0223] (d) a central-processing unit coupled to said working memory and to said machine-readable data storage medium of (a) and (b) for performing a Fourier transform of the machine readable data of (a) and for processing said machine readable data of (b) into structural coordinates; and

[0224] (e) a display coupled to said central-processing unit for displaying said structural coordinates of said molecule or molecular complex.

[0225] The invention also contemplates a computer programmed with a model of a ligand binding pocket according to the invention; a machine-readable data-storage medium on which has been stored in machine-readable form a model of a ligand binding pocket of a glycosyltransferase; and the use of a model as input to a computer programmed for drug design and/or database searching and/or molecular graphic imaging in order to identify new ligands or modulators for glycosyltransferases.

[0226] Structural Determinations

[0227] The present invention also provides a method for determining the secondary and/or tertiary structures of a polypeptide by using a crystal, or a model according to the present invention. The polypeptide may be any polypeptide for which the secondary and or tertiary structure is uncharacterised or incompletely characterised. In a preferred embodiment the polypeptide shares (or is predicted to share) some structural or functional homology to the glycosyltransferase of the crystal. For example, the polypeptide may show a degree of structural homology over some or all parts of the primary amino acid sequence. For example the polypeptide may have one or more pockets which shows homology with a glycosyltransferase pocket (Kapitonov and Yu (1999) Glycobiology 9(10): 961-978).

[0228] Two polypeptides are considered to show substantial structural homology when the two peptide sequences, when optimally aligned (such as by the programs GAP or BESTFIT using default gap) share at least 40%, 50%, 60%, 65%, 70%, 75%, 80%, or 85% sequence identity, preferably at least 90 percent sequence identity, more preferably at least 95 percent sequence identity or more. Preferably, residue positions which are not identical differ by conservative amino acid substitutions. For example, the substitution of amino acids having similar chemical properties such as charge or polarity are not likely to affect the properties of a protein. Examples include glutamine for asparagine or glutamic acid for aspartic acid.

[0229] The polypeptide may be a glycosyltransferase with a different specificity for a ligand or portion thereof including a sugar residue, donor molecule or acceptor molecule. The polypeptide may be a glycosyltransferase which requires a different metal cofactor. Alternatively (or in addition) the polypeptide may be a glycosyltransferase enzyme from a different species.

[0230] The polypeptide may be a mutant of the wild-type glycosyltransferase. A mutant may arise naturally, or may be made artificially (for example using molecular biology techniques). The mutant may also not be “made” at all in the conventional sense, but merely tested theoretically using the model of the present invention. A mutant may or may not be functional.

[0231] Thus, using a model of the present invention, the effect of a particular mutation on the overall two and/or three dimensional structure of the glycosyltransferase and/or the interaction between the enzyme and a ligand can be investigated.

[0232] Alternatively, the polypeptide may perform an analogous function or be suspected to show a similar catalytic mechanism to the glycosyltransferase enzyme. For example the polypeptide may remove, transport, or add on a sugar residue. If the glycosyltransferase of the crystal is a retaining glycosyltransferase, the polypeptide under investigation may be known or suspected to function via a double-displacement mechanism.

[0233] The polypeptide may also be the same as the polypeptide of the crystal, but in association with a different ligand (for example, donor molecule, acceptor molecule analogue, modulator or inhibitor) or cofactor. In this way it is possible to investigate the effect of altering the ligand or compound with which the polypeptide is associated on the structure of the LBP.

[0234] Secondary or tertiary structure may be determined by applying the structural coordinates of the crystal or model of the present invention to other data such as an amino acid sequence, X-ray crystallographic diffraction data, or nuclear magnetic resonance (NMR) data. Homology modeling, molecular replacement, and nuclear magnetic resonance methods using these other data sets are described below.

[0235] Homology modeling (also known as comparative modeling or knowledge-based modeling) methods develop a three dimensional model from a polypeptide sequence based on the structures of known proteins (i.e. the glycosyltransferase of the crystal). The method utilizes a computer model of the crystal of the present invention (the “known structure”), a computer representation of the amino acid sequence of the polypeptide with an unknown structure, and standard computer representations of the structures of amino acids. The method in particular comprises the steps of; (a) identifying structurally conserved and variable regions in the known structure; (b) aligning the amino acid sequences of the known structure and unknown structure (c) generating coordinates of main chain atoms and side chain atoms in structurally conserved and variable regions of the unknown structure based on the coordinates of the known structure thereby obtaining a homology model; and (d) refining the homology model to obtain a three dimensional structure for the unknown structure. This method is well known to those skilled in the art (Greer, 1985, Science 228, 1055; Bundell et al 1988, Eur. J. Biochem. 172, 513; Knighton et al., 1992, Science 258:130-135, http://biochem.vt.edu/courses/modeling/homology.htn). Computer programs that can be used in homology modelling are Quanta and the Homology module in the Insight II modelling package distributed by Molecular Simulations Inc, or MODELLER (Rockefeller University, www.iucr.ac.uk/sinris-top/logical/prg-modeller.html).

[0236] In step (a) of the homology modelling method, the known glycosyltransferase structure is examined to identify the structurally conserved regions (SCRs) from which an average structure, or framework, can be constructed for these regions of the protein. Variable regions (VRs), in which known structures may differ in conformation, also must be identified. SCRs generally correspond to the elements of secondary structure, such as alpha-helices and beta-sheets, and to ligand- and substrate-binding sites (e.g. acceptor and donor binding sites). The VRs usually lie on the surface of the proteins and form the loops where the main chain turns.

[0237] Many methods are available for sequence alignment of known structures and unknown structures. Sequence alignments generally are based on the dynamic programming algorithm of Needleman and Wunsch [J. Mol. Biol. 48: 442453, 1970]. Current methods include FASTA, Smith-Waterman, and BLASTP, with the BLASTP method differing from the other two in not allowing gaps. Scoring of alignments typically involves construction of a 20×20 matrix in which identical amino acids and those of similar character (i.e., conservative substitutions) may be scored higher than those of different character. Substitution schemes which may be used to score alignments include the scoring matrices PAM (Dayhoff et al., Meth. Enzymol. 91: 524-545, 1983), and BLOSUM (Henilcoff and Henikoff, Proc. Nat. Acad. Sci. USA 89: 10915-10919, 1992), and the matrices based on alignments derived from three-dimensional structures including that of Johnson and Overington (JO matrices) (J. Mol. Biol. 233: 716-738, 1993).

[0238] Alignment based solely on sequence may be used; however, other structural features also may be taken into account. In Quanta, multiple sequence alignment algorithms are available that may be used when aligning a sequence of the unknown with the known structures. Four scoring systems (i.e. sequence homology, secondary structure homology, residue accessibility homology, CA-CA distance homology) are available, each of which may be evaluated during an alignment so that relative statistical weights may be assigned.

[0239] When generating co-ordinates for the unknown structure, main chain atoms and side chain atoms, both in SCRs and VRs need to be modelled. A variety of approaches known to those skilled in the art may be used to assign coordinates to the unknown. In particular, the coordinates of the main chain atoms of SCRs will be transferred to the unknown structure. VRs correspond most often to the loops on the surface of the polypeptide and if a loop in the known structure is a good model for the unknown, then the main chain coordinates of the known structure may be copied. Side chain coordinates of SCRs and VRs are copied if the residue type in the unknown is identical to or very similar to that in the known structure. For other side chain coordinates, a side chain rotamer library may be used to define the side chain coordinates. When a good model for a loop cannot be found fragment databases may be searched for loops in other proteins that may provide a suitable model for the unknown. If desired, the loop may then be subjected to conformational searching to identify low energy conformers if desired.

[0240] Once a homology model has been generated it is analyzed to determine its correctness. A computer program available to assist in this analysis is the Protein Health module in Quanta which provides a variety of tests. Other programs that provide structure analysis along with output include PROCHECK and 3D-Profiler [Luthy R. et al, Nature 356: 83-85, 1992; and Bowie, J. U. et al, Science 253: 164-170, 1991]. Once any irregularities have been resolved, the entire structure may be further refined. Refinement may consist of energy minimization with restraints, especially for the SCRs. Restraints may be gradually removed for subsequent minimizations. Molecular dynamics may also be applied in conjunction with energy minimization.

[0241] Molecular replacement involves applying a known structure to solve the X-ray crystallographic data set of a polypeptide of unknown structure. The method can be used to define the phases describing the X-ray diffraction data of a polypeptide of unknown structure when only the amplitudes are known. Thus in an embodiment of the invention, a method is provided for determining three dimensional structures of polypeptides with unknown structure by applying the structural coordinates of the crystal of the present invention to provide an X-ray crystallographic data set for a polypeptide of unknown structure, and (b) determining a low energy conformation of the resulting structure.

[0242] The structural coordinates of the crystal of the present invention may be applied to nuclear magnetic resonance (NMR) data to determine the three dimensional structures of polypeptides with uncharacterised or incompletely characterised structure. (See for example, Wuthrich, 1986, John Wiley and Sons, New York: 176-199; Pflugrath et al., 1986, J. Molecular Biology 189: 383-386; Kline et al., 1986 J. Molecular Biology 189:377-382). While the secondary structure of a polypeptide may often be determined by NMR data, the spatial connections between individual pieces of secondary structure are not as readily determined. The structural co-ordinates of a polypeptide defined by X-ray crystallography can guide the NMR spectroscopist to an understanding of the spatial interactions between secondary structural elements in a polypeptide of related structure. Information on spatial interactions between secondary structural elements can greatly simplify Nuclear Overhauser Effect (NOE) data from two-dimensional NMR experiments. In addition, applying the structural co-ordinates after the determination of secondary structure by NMR techniques simplifies the assignment of NOE's relating to particular amino acids in the polypeptide sequence and does not greatly bias the NMR analysis of polypeptide structure.

[0243] In an embodiment, the invention relates to a method of determining three dimensional structures of polypeptides with unknown structures, by applying the structural coordinates of a crystal of the present invention to nuclear magnetic resonance (NMR) data of the unknown structure. This method comprises the steps of: (a) determining the secondary structure of an unknown structure using NMR data; and (b) simplifying the assignment of through-space interactions of amino acids. The term “through-space interactions” defines the orientation of the secondary structural elements in the three dimensional structure and the distances between amino acids from different portions of the amino acid sequence. The term “assignment” defines a method of analyzing NMR data and identifying which amino acids give rise to signals in the NMR spectrum.

[0244] Screening Method

[0245] The present invention also provides a method of screening for a ligand that associates with a ligand binding pocket and/or modulates the function of a glycosyltransferase, by using a crystal or a model according to the present invention. The method may involve investigating whether a test compound is capable of associating with or binding a ligand binding pocket.

[0246] As used herein, the term “test compound” refers to any compound which is potentially capable of associating with a ligand binding pocket and/or modulating the function of a glycosyltransferase. If, after testing, it is determined that a test compound does bind to a LBP, it is known as a “ligand”.

[0247] A “test compound” includes but is not limited to, a compound which may be obtainable from or produced by any suitable source, whether natural or not. The test compound may be designed or obtained from a library of compounds which may comprise peptides, as well as other compounds, such as small organic molecules and particularly new lead compounds. By way of example, the test compound may be a natural substance, a biological macromolecule, or an extract made from biological materials such as bacteria, fungi, or animal (particularly mammalian) cells or tissues, an organic or an inorganic molecule, a synthetic test compound, a semi-synthetic test compound, a carbohydrate, a monosaccharide, an oligosaccharide or polysaccharide, a glycolipid, a glycopeptide, a saponin, a heterocyclic compound, a structural or functional mimetic, a peptide, a peptidomimetic, a derivatised test compound, a peptide cleaved from a whole protein, or a peptides synthesised synthetically (such as, by way of example, either using a peptide synthesizer or by recombinant techniques or combinations thereof), a recombinant test compound, a natural or a non-natural test compound, a fusion protein or equivalent thereof and mutants, derivatives or combinations thereof.

[0248] The test compound may be screened as part of a library or a data base of molecules. Data bases which may be used include ACD (Molecular Designs Limited), NCI (National Cancer Institute), CCDC (Cambridge Crystallographic Data Center), CAST (Chemical Abstract Service), Derwent (Derwent Information Limited), Maybridge (Maybridge Chemical Company Ltd), Aldrich (Aldrich Chemical Company), DOCK (University of California in San Francisco), and the Directory of Natural Products (Chapman & Hall). Computer programs such as CONCORD (Tripos Associates) or DB-Converter (Molecular Simulations Limited) can be used to convert a data set represented in two dimensions to one represented in three dimensions.

[0249] Test compounds may be tested for their capacity to fit spatially into the glycosyltransferase LBP. As used herein, the term “fits spatially” means that the three-dimensional structure of the test compound is accommodated geometrically in a cavity or pocket of the glycosyltransferase LBP. The test compound can then be considered to be a ligand.

[0250] A favourable geometric fit occurs when the surface areas of the test compound are in close proximity with the surface area of the cavity or pocket without forming unfavorable interactions. A favourable complementary interaction occurs where the test compound interacts by hydrophobic, aromatic, ionic, dipolar, or hydrogen donating and accepting forces. Unfavourable interactions may be steric hindrance between atoms in the test compound and atoms in the binding site.

[0251] In an embodiment of the invention, a method is provided for identifying potential modulators of a glycosyltransferase function. The method utilizes the structural coordinates or model of a glycosyltransferase three dimensional structure, or binding pocket thereof. The method comprises the steps of (a) docking a computer representation of a test compound from a computer data base with a computer model of a ligand binding pocket of a glycosyltransferase; (b) determining a conformation of a complex between the test compound and binding pocket with a favourable geometric fit or favorable complementary interactions; and (c) identifying test compounds that best fit the glycosyltransferase ligand binding pocket as potential modulators of glycosyltransferase function. The initial glycosyltransferase structure may or may not have ligands including substrates bound to it. A favourable complementary interaction occurs where a compound in a compound-glycosyltransferase complex interacts by hydrophobic, ionic, or hydrogen donating and accepting forces, with the active-site or binding pocket of a glycosyltransferase without forming unfavorable interactions.

[0252] If a model of the present invention is a computer model, the test compounds may be positioned in an LBP through computational docking. If, on the other hand, the model of the present invention is a structural model, the test compounds may be positioned in the LBP by, for example, manual docking.

[0253] As used herein the term “docking” refers to a process of placing a compound in close proximity with a glycosyltransferase LBP, or a process of finding low energy conformations of a test compound/glycosyltransferase complex.

[0254] A screening method of the present invention may comprise the following steps:

[0255] (i) generating a computer model of a glycosyltransferase or a ligand binding pocket thereof using a crystal according to the invention;

[0256] (ii) docking a computer representation of a test compound with the computer model;

[0257] (iii) analysing the fit of the compound in the glycosyltransferase or ligand binding pocket.

[0258] The method may be applied to a plurality of test compounds, to identify those that best fit the enzyme or ligand binding pocket.

[0259] In an aspect of the invention a method is provided comprising the following steps:

[0260] (a) docking a computer representation of a structure of a test compound into a computer representation of a ligand binding pocket of a glycosyltransferase defined in accordance with the invention using a computer program, or by interactively moving the representation of the test compound into the representation of the binding pocket;

[0261] (b) characterizing the geometry and the complementary interactions formed between the atoms of the ligand binding pocket and the compound; optionally

[0262] (c) searching libraries for molecular fragments which can fit into the empty space between the compound and ligand binding pocket and can be linked to the compound; and

[0263] (d) linking the fragments found in (c) to the compound and evaluating the new modified compound.

[0264] In an embodiment of the invention a method is provided which comprises the following steps:

[0265] (a) docking a computer representation of a test compound from a computer data base with a computer representation of a selected site (e.g. an inhibitor binding pocket) on a glycosyltransferase structure or model defined in accordance with the invention to obtain a complex;

[0266] (b) determining a conformation of the complex with a favourable geometric fit and favourable complementary interactions; and

[0267] (c) identifying test compounds that best fit the selected site as potential modulators of the glycosyltransferase.

[0268] The model used in the screening method may comprise the ligand-binding pocket of a glycosyltransferase enzyme either alone or in association with one or more ligands and/or cofactors. For example, the model may comprise the ligand-binding pocket in association with a donor molecule (or analogue thereof) and/or an acceptor molecule (or analogue thereof).

[0269] If the model comprises an unassociated ligand binding pocket, then the selected site under investigation may be the LBP itself. The test compound may, for example, mimic a known substrate for the enzyme (such as a donor or acceptor molecule) in order to interact with the LBP. The selected site may alternatively be another site on the enzyme (for example a site involved in attachment to the bacterial membrane).

[0270] If the model comprises an associated LBP, for example an LBP in association with a donor molecule or analogue thereof, the selected site may be the LBP or a site made up of the LBP and the complexed ligand, or a site on the ligand itself. The test compound may be investigated for its capacity to modulate the interaction with the associated molecule.

[0271] A test compound (or plurality of test compounds) may be selected on the basis of its similarity to a known ligand for the glycosyltransferase. For example, the screening method may comprise the following steps:

[0272] (i) generating a computer model of the LBP of a glycosyltransferase in complex with a ligand;

[0273] (ii) searching for a test compound with a similar three dimensional structure and/or similar chemical groups; and

[0274] (iii) evaluating the fit of the test compound in the LBP.

[0275] Searching may be carried out using a database of computer representations of potential compounds, using methods known in the art.

[0276] The present invention also provides a method for designing ligands for a glycosyltransferase. It is well known in the art to use a screening method as described above to identify a test compound with promising fit, but then to use this test compound as a starting point to design a ligand with improved fit to the model. Such techniques are known as “structure-based ligand design” (See Kuntz et al., 1994, Ace. Chem. Res. 27:117; Guida, 1994, Current Opinion in Struc. Biol. 4: 777; and Colman, 1994, Current Opinion in Struc. Biol. 4: 868, for reviews of structure-based drug design and identification;and Kuntz et al 1982, J. Mol. Biol. 162:269; Kuntz et al., 1994, Acc. Chem. Res. 27: 117; Meng et al., 1992, J. Compt. Chem. 13: 505; Bohm, 1994, J. Comp. Aided Molec. Design 8: 623 for methods of structure-based modulator design).

[0277] Examples of computer programs that may be used for structure-based ligand design are CAVEAT (Bartlett et al., 1989, in “Chemical and Biological Problems in Molecular Recognition”, Roberts, S. M. Ley, S. V.; Campbell, N. M. eds; Royal Society of Chemistry: Cambridge, pp 182-196); FLOG Miller et al., 1994, J. Comp. Aided Molec. Design 8:153); PRO Modulator (Clark et al., 1995 J. Comp. Aided Molec. Design 9:13); MCSS (Miranker and Karplus, 1991, Proteins: Structure, Function, and Genetics 8:195); and, GRID (Goodford, 1985, J. Med. Chem. 28:849).

[0278] The method may comprise the following steps:

[0279] (i) docking a model of a test compound with a model of a selected site;

[0280] (ii) identifying one or more groups on the test compound which may be modified to improve their fit in the selected site;

[0281] (iii) replacing one or more identified groups to produce a modified test compound model; and

[0282] (iv) docking the modified test compound model with the model of the selected site.

[0283] Evaluation of fit may comprise the following steps:

[0284] (a) mapping chemical features of a test compound such as by hydrogen bond donors or acceptors, hydrophobic/lipophilic sites, positively ionizable sites, or negatively ionizable sites; and

[0285] (b) adding geometric constraints to selected mapped features.

[0286] The fit of the modified test compound may then be evaluated using the same criteria.

[0287] The chemical modification of a group may either enhance or reduce hydrogen bonding interaction, charge interaction, hydrophobic interaction, Van Der Waals interaction or dipole interaction between the test compound and the key amino acid residue(s) of the selected site. Preferably the group modifications involve the addition, removal, or replacement of substituents onto the test compound such that the substituents are positioned to collide or to bind preferentially with one or more amino acid residues that correspond to the key amino acid residues of the selected site.

[0288] Identified groups in a test compound may be substituted with, for example, alkyl, alkoxy, hydroxyl, aryl, cycloalkyl, alkenyl, alkynyl, thiol, thioalkyl, thioaryl, amino, or halo groups. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided.

[0289] If a modified test compound model has an improved fit, then it may bind to the selected site and be considered to be a “ligand”. Rational modification of groups may be made with the aid of libraries of molecular fragments which may be screened for their capacity to fit into the available space and to interact with the appropriate atoms. Databases of computer representations of libraries of chemical groups are available commercially, for this purpose.

[0290] The test compound may also be modified “in situ” (i.e. once docked into the potential binding site), enabling immediate evaluation of the effect of replacing selected groups. The computer representation of the test compound may be modified by deleting a chemical group or groups, or by adding a chemical group or groups. After each modification to a compound, the atoms of the modified compound and potential binding site can be shifted in conformation and the distance between the compound and the active site atoms may be scored on the basis of geometric fit and favourable complementary interactions between the molecules. This technique is described in detail in Molecular Simulations User Manual, 1995 in LUDI.

[0291] Examples of ligand building and/or searching computer include programs in the Molecular Simulations Package (Catalyst), ISIS/HOST, ISIS/BASE, and ISIS/DRAW (Molecular Designs Limited), and UNITY (Tripos Associates).

[0292] The “starting point” for rational ligand design may be a known ligand for the enzyme. For example, in order to identify potential modulators of the glycosyltransferase, a logical approach would be to start with a known ligand (for example a donor or acceptor molecule) to produce a molecule which mimics the binding of the ligand. Such a molecule may, for example, act as a competitive inhibitor for the true ligand, or may bind so strongly that the interaction (and inhibition) is effectively irreversible.

[0293] Such a method may comprise the following steps:

[0294] (i) generating a computer model of a LBP of a glycosyltransferase in complex with a ligand;

[0295] (ii) replacing one or more groups on the ligand model to produce a modified ligand; and

[0296] (iii) evaluating the fit of the modified ligand in the LBP.

[0297] The replacement groups could be selected and replaced using a compound construction program which replaces computer representations of chemical groups with groups from a computer database, where the representations of the compounds are defined by structural co-ordinates.

[0298] In an embodiment, a screening method is provided for identifying a ligand of a glycosyltransferase comprising the step of using the structural co-ordinates of a donor molecule or acceptor molecule or component thereof, defined in relation to its spatial association with a glycosyltransferase structure or a ligand binding pocket of the invention, to generate a compound that is capable of associating with the glycosyltransferase or ligand binding pocket.

[0299] The screening methods of the present invention may be used to identify compounds or entities that associate with a molecule that associates with a glycosyltransferase enzyme (for example, a substrate molecule).

[0300] In an embodiment of the invention, a screening method is provided for identifying a ligand of a glycosyltransferase comprising the step of using the structural co-ordinates of uridine, uracil, or UDP listed in Table 4, 5, or 6 to generate a compound for associating with the active site binding pocket of a glycosyltransferase as described herein. The following steps are employed in a particular method of the invention: (a) generating a computer representation of uridine, uracil, or UDP, defined by its structural coordinates listed in Table 4, 5, or 6; (b) searching for molecules in a data base that are structurally or chemically similar to the defined uridine, uracil, or UDP, using a searching computer program, or replacing portions of the compound with similar chemical structures from a database using a compound building computer program.

[0301] In another embodiment of the invention, a screening method is provided for identifying a ligand of a glycosyltransferase comprising the step of using the structural co-ordinates of UDP-Gal listed in Table 4, 5, or 6 to generate a compound for associating with the active site of a glycosyltransferase of the invention. The following steps are employed in a particular method of the invention: (a) generating a computer representation of UDP-Gal defined by its structural co-ordinates listed in Table 4, 5, or 6; and (b) searching for molecules in a data base that are structurally or chemically similar to the defined UDP-Gal using a searching computer program, or replacing portions of the compound with similar chemical structures from a database using a compound building computer program.

[0302] In another embodiment of the invention, a method is provided for designing potential inhibitors of a glycosyltransferase comprising the step of using the structural coordinates of a lactose molecule in Table 5, to generate a compound for associating with the active site of a glycosyltransferase.

[0303] The following steps are employed in a particular method of the invention: (a) generating a computer representation of a lactose acceptor defined by its structural coordinates listed in Table 4, 5, or 6; and (b) searching for molecules in a data base that are structurally or chemically similar to the defined lactose acceptor using a searching computer program, or replacing portions of the compound with similar chemical structures from a database using a compound building computer program.

[0304] The screening methods of the present invention may be used to identify compounds or entities that associate with a molecule that associates with a glycosyltransferase enzyme (for example, a donor or acceptor molecule).

[0305] Compounds and entities (e.g. ligands) of glycosyltransferases identified using the above-described methods may be prepared using methods described in standard reference sources utilized by those skilled in the art. For example, organic compounds may be prepared by organic synthetic methods described in references such as March, 1994, Advanced Organic Chemistry: Reactions, Mechanisms, and Structure, New York, McGraw Hill.

[0306] Test compounds and ligands which are identified using a model of the present invention can be screened in assays such as those well known in the art. Screening can be, for example, in vitro, in cell culture, and/or in vivo. Biological screening assays preferably centre on activity-based response models, binding assays (which measure how well a compound binds), and bacterial, yeast and animal cell lines (which measure the biological effect of a compound in a cell). The assays can be automated for high capacity-high throughput screening (HTS) in which large numbers of compounds can be tested to identify compounds with the desired activity. The biological assay, may also be an assay for the ligand binding activity of a compound that selectively binds to the ligand binding domain compared to other enzymes.

[0307] Ligands/Compounds/Modulators

[0308] The present invention provides a ligand or compound or entity identified by a screening method of the present invention. A ligand or compound may have been designed rationally by using a model according to the present invention. A ligand or compound identified using the screening methods of the invention specifically associate with a target compound. In the present invention the target compound may be the glycosyltransferase enzyme or a molecule that is capable of associating with the glycosyltransferase enzyme (for example a donor or acceptor molecule). In a preferred embodiment the ligand is capable of binding to the LBP of a glycosyltransferase.

[0309] A ligand or compound identified using a screening method of the invention may act as a “modulator”, i.e. a compound which affects the activity of a glycosyltransferase. A modulator may reduce, enhance or alter the biological function of a glycosyltransferase. For example a modulator may modulate the capacity of the enzyme to transfer a sugar from donor to acceptor. Alternatively, or in addition, it may modulate the capacity of the enzyme to attach to bacterial membranes. An alteration in biological function may be characterised by a change in specificity. For example, a modulator may cause the enzyme to accept a different acceptor or donor molecule, to transfer a different sugar, or to work with a different metal cofactor. In order to exert its function, the modulator commonly binds to the ligand binding pocket.

[0310] A “modulator” which is capable of reducing the biological function of the enzyme may also be known as an inhibitor. Preferably an inhibitor reduces or blocks the capacity of the enzyme to transfer a sugar from donor to acceptor. The inhibitor may mimic the binding of a donor or acceptor molecule, for example, it may be a donor or acceptor analogue. A donor or acceptor analogue may be designed by considering the interactions between the donor or acceptor molecule and the enzyme (for example by using information derivable from the crystal of the invention) and specifically altering one or more groups (as described above). Examples of donor and acceptor molecule analogues for LgtC are UDP-2Fgal and 4-deoxylactose respectively. Acceptor molecule analogues are also illustrated in Example 2.

[0311] In a highly preferred embodiment a modulator acts as an inhibitor of the glycosyltransferase and is capable of inhibiting lipooligosaccharide biosynthesis. Such an inhibitor may be useful as an antibiotic, because inhibition of LOS synthesis will prevent the bacterium from escaping detection by the human immune system by minicing human glycoproteins.

[0312] The present invention also provides a method for modulating the activity of a glycosyltransferase within a bacterial cell using a modulator according to the present invention. It would be possible to monitor the expression of LOS on the bacterial surface following such treatment by a number of methods known in the art (for example by detecting expression with an LOS-specific antibody).

[0313] In another preferred embodiment, the modulator is capable of causing or preventing oxidation of Cys 246. It is thought that oxidation of Cys 246 results in impaired donor and acceptor binding.

[0314] In another preferred embodiment, the modulator modulates the catalytic mechanism of the enzyme. For example it may affect the capacity of the side-chain oxygen of Gln 189 to act as a nucleophile in the double displacement mechanism.

[0315] A modulator may be an agonist, partial agonist, partial inverse agonist or antagonist of the glucosyltransferase.

[0316] As used herein, the term “agonist” means any ligand, which is capable of binding to a ligand binding pocket and which is capable of increasing a proportion of the enzyme that is in an active form, resulting in an increased biological response. The term includes partial agonists and inverse agonists.

[0317] As used herein, the term “partial agonist” means an agonist that is unable to evoke the maximal response of a biological system, even at a concentration sufficient to saturate the specific receptors.

[0318] As used herein, the term “partial inverse agonist” is an inverse agonist that evokes a submaximal response to a biological system, even at a concentration sufficient to saturate the specific receptors. At high concentrations, it will diminish the actions of a full inverse agonist.

[0319] The invention relates to a glycosyltransferase ligand binding pocket antagonist, wherein said ligand binding pocket is that defined by the amino acid structural coordinates described herein. For example the ligand may antagonise the inhibition of glycosyltransferase by an inhibitor.

[0320] As used herein, the term “antagonist” means any agent that reduces the action of another agent, such as an agonist. The antagonist may act at the same site as the agonist (competitive antagonism). The antagonistic action may result from a combination of the substance being antagonised (chemical antagonism) or the production of an opposite effect through a different receptor (functional antagonism or physiological antagonism) or as a consequence of competition for the binding site of an intermediate that links receptor activation to the effect observed (indirect antagonism).

[0321] As used herein, the term “competitive antagonism” refers to the competition between an agonist and an antagonist for a receptor that occurs when the binding of agonist and antagonist becomes mutually exclusive. This may be because the agonist and antagonist compete for the same binding site or combine with adjacent but overlapping sites. A third possibility is that different sites are involved but that they influence the receptor macromolecules in such a way that agonist and antagonist molecules cannot be bound at the same time. If the agonist and antagonist form only short lived combinations with the receptor so that equilibrium between agonist, antagonist and receptor is reached during the presence of the agonist, the antagonism will be surmountable over a wide range of concentrations. In contrast, some antagonists, when in close enough proximity to their binding site, may form a stable covalent bond with it and the antagonism becomes insurmountable when no spare receptors remain.

[0322] As mentioned above, an identified ligand or compound may act as a ligand model (for example, a template) for the development of other compounds. A modulator may be a mimetic of a ligand or ligand binding pocket A mimetic of a ligand (e.g an acceptor or donor molecule or part thereof) may compete with a natural ligand for a glycosyltransferase and antagonize a physiological effect of the enzyme in an animal. A mimetic of a ligand may be an organically synthesized compound. A mimetic of a ligand binding pocket, may be either a peptide or other biopharmaceutical (such as an organically synthesized compound) that specifically binds to a natural acceptor or donor molecule for a glycosyltransferase and antagonizes a physiological effect of the enzyme in an animal.

[0323] Once a ligand has been optimally selected or designed, substitutions may then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds may then be analyzed for efficiency of fit to a glycosyltransferase ligand binding pocket by the same computer methods described above. Preferably, positions for substitution are selected based on the predicted binding orientation of a ligand to a glycosyltransferase ligand binding pocket.

[0324] A modulator may be one or a variety of different sorts of molecule. For example, a modulator may be a peptide, member of random peptide libraries and combinatorial chemistry-derived molecular libraries, phosphopeptide (including members of random or partially degenerate, directed phosphopeptide libraries), a carbohydrate, a monosaccharide, an oligosaccharide or polysaccharide, a glycolipid, a glycopeptide, a saponin, a heterocyclic compound antibody, carbohydrate, nucleoside or nucleotide or part thereof, and small organic or inorganic molecule. A modulator may be an endogenous physiological compound, or it may be a natural or synthetic compound. The modulators of the present invention may be natural or synthetic. The term “modulator” also refers to a chemically modified ligand or compound.

[0325] A technique suitable for preparing a modulator will depend on its chemical nature. For example, peptides can be synthesized by solid phase techniques (Roberge J Y et al (1995) Science 269: 202-204) and automated synthesis may be achieved, for example, using the ABI 43 1 A Peptide Synthesizer (Perlin Elmer) in accordance with the instructions provided by the manufacturer. Once cleaved from the resin, the peptide may be 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.). The composition of the synthetic peptides may be confirmed by amino acid analysis or sequencing (e.g., the Edman degradation procedure; Creighton, supra).

[0326] If a modulator is a nucleotide, or a polypeptide expressable therefrom, it may be synthesized, in whole or in part, using chemical methods well known in the art (see Caruthers M H et al (1980) Nuc Acids Res Symp Ser 215-23, Horn T et al (1980) Nuc Acids Res Symp Ser 225-232), or it may be prepared using recombinant techniques well known in the art.

[0327] Organic compounds may be prepared by organic synthetic methods described in references (e.g. March, 1994, Advanced Organic Chemistry: Reactions, Mechanisms, and Structure, New York, McGraw Hill).

[0328] The invention also relates to classes of modulators of glycosyltransferases based on the structure and shape of a ligand, in particular, a substrate including a donor molecule, or component thereof, or an acceptor molecule or component thereof, defined in relation to the ligand's spatial association with a glycosyltransferase structure of the invention or part thereof. Therefore, a modulator may comprise a ligand, in particular a donor molecule or an acceptor molecule, having the shape or structure, preferably the structural coordinates, of the ligand in the active site binding pocket of a reaction catalyzed by a glycosyltransferase.

[0329] A class of modulators of glycosyltransferases may comprise a compound containing a structure of uracil, uridine, ribose, pyrophosphate, or UDP, and having one or more, preferably all, of the structural coordinates of uracil, uridine, ribose, pyrophosphate, or UDP of Table 4, 5, or 6. In an embodiment, modulators are provided comprising the structure of UDP-Gal and having one or more, preferably all, of the structural co-ordinates of UDP-Gal of Table 4, 5, or 6. Functional groups in the uracil, uridine, ribose, pyrophosphate, UDP, or UDP-Gal modulators may be substituted with, for example, alkyl, alkoxy, hydroxyl, aryl, cycloalkyl, alkenyl, allynyl, thiol, thioalkyl, thioaryl, amino, or halo, or they may be modified using techniques known in the art. Substituents will be selected to optimize the activity of the modulator.

[0330] Modulators are also contemplated that comprise the structure of an acceptor molecule with the structural co-ordinates of lactose in Table 5 or 6. Functional groups in an acceptor structure may be substituted with, for example, alkyl, alkoxy, hydroxyl, aryl, cycloalkyl, alkenyl, alkynyl, thiol, thioalkyl, thioaryl, amino, or halo, or they may be modified using techniques known in the art. Substituents will b selected to optimize the activity of the modulator.

[0331] A class of modulators defined by the invention are compounds comprising the structural coordinates of UDP-Gal in the active site binding pocket of a reaction catalyzed by a glycosyltransferase. The UDP-Gal adopts a folded conformation in which the UDP moiety is bound in an extended manner and the galactose tucks back under the phosphates such that the plane of the galactose ring is almost parallel to the plane of the diphosphate (FIGS. 3).

[0332] Another class of modulators of the invention are compounds comprising a uridine diphosphate group having the structural co-ordinates of uridine diphosphate in the active site binding pocket of a reaction catalyzed by a glycosyltransferase.

[0333] Yet another class of modulators defined by the invention are compounds comprising the structural co-ordinates of lactose or an analogue thereof (4-deoxylactose, see also Example 2) in the active site binding pocket of a reaction catalyzed by a glycosyltransferase. The moieties of the lactose adopt a full chair conformation.

[0334] A class of modulators contemplated by the present invention are donor-acceptor complexes based on the spatial arrangement of a donor molecule and acceptor molecule in a transition state in a glycosyltransferase reaction. While not wishing to be bound by any particular theory, a retaining glycosyltransferase of the present invention may follow an SNi mechanism involving a direct displacement of the leaving group by the nucleophile, but from the front face of the sugar. Thus both the 4-hydroxyl of the lactose acceptor (the nucleophile) and the phosphate moiety of the UDP leaving group are located on the alpha face of the sugar. Reaction proceeds via a very dissociative (oxocarbenium ion-like) transition state. Precedent exists for this type of mechanism. (See J. Org Chem. (1994) 59, 1849; J. Org Chem. (1989) 54, 761;J. Org Chem. (1993), 58, 2822; see J. Amer Chem Soc (1980) 102, 2026:J. Amer. Chem. Soc. (1990) 10 113, 7958 re sugar systems). Based on this mechanism, the invention contemplates the following classes of modulators:

[0335] The invention contemplates all optical isomers and racemic forms of the modulators of the invention.

[0336] Pharmaceutical Composition

[0337] The present invention also provides the use of a ligand, in particular a modulator according to the invention, in the manufacture of a medicament to treat and/or prevent a disease in a mammalian patient. There is also provided a pharmaceutical composition comprising such a ligand or modulator and a method of treating and/or preventing a disease comprising the step of administering such a ligand or modulator or pharmaceutical composition to a mammalian patient.

[0338] The pharmaceutical compositions may be for human or animal usage in human and veterinary medicine and will typically comprise a pharmaceutically acceptable carrier, diluent, excipient, adjuvant or combination thereof.

[0339] Acceptable carriers or diluents for therapeutic use are well known in the pharmaceutical art, and are described, for example, in Remington's Pharmaceutical Sciences, Mack Publishing Co. (A. R. Gennaro edit. 1985). The choice of pharmaceutical carrier, excipient or diluent can be selected with regard to the intended route of administration and standard pharmaceutical practice. The pharmaceutical compositions may comprise in addition to the carrier, excipient or diluent any suitable binder(s), lubricant(s), suspending agent(s), coating agent(s), and solubilising agent(s).

[0340] Preservatives, stabilizers, dyes and even flavouring agents may be provided in the pharmaceutical composition. Examples of preservatives include sodium benzoate, sorbic acid and esters of p-hydroxybenzoic acid Antioxidants and suspending agents may be also used.

[0341] The routes for admininstration (delivery) include, but are not limited to, one or more of: oral (e.g. as a tablet, capsule, or as an ingestable solution), topical, mucosal (e.g. as a nasal spray or aerosol for inhalation), nasal, parenteral (e.g. by an injectable form), gastrointestinal, intraspinal, intraperitoneal, intramuscular, intravenous, intrauterine, intraocular, intradermal, intracranial, intratracheal, intravaginal, intracerebroventricular, intracerebral, subcutaneous, ophthalmic (including intravitreal or intracameral), transdermal, rectal, buccal, vaginal, epidural, sublingual.

[0342] Where the pharmaceutical composition is to be delivered mucosally through the gastrointestinal mucosa, it should be able to remain stable during transit though the gastrointestinal tract; for example, it should be resistant to proteolytic degradation, stable at acid pH and resistant to the detergent effects of bile.

[0343] Where appropriate, the pharmaceutical compositions can be administered by inhalation, in the form of a suppository or pessary, topically in the form of a lotion, gel, hydrogel, solution, cream, ointment or dusting powder, by use of a skin patch, orally in the form of tablets containing excipients such as starch or lactose or chalk, or in capsules or ovules either alone or in admixture with excipients, or in the form of elixirs, solutions or suspensions containing flavouring or colouring agents, or they can be injected parenterally, for example intravenously, intramuscularly or subcutaneously. For parenteral administration, the compositions may be best used in the form of a sterile aqueous solution which may contain other substances, for example enough salts or monosaccharides 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.

[0344] If the agent of the present invention is administered parenterally, then examples of such administration include one or more of: intravenously, intra-arterially, intraperitoneally, intrathecally, intraventricularly, intraurethrally, intrasternally, intracranially, intramuscularly or subcutaneously administering the agent; and/or by using infusion techniques.

[0345] For buccal or sublingual administration the compositions may be administered in the form of tablets or lozenges which can be formulated in a conventional manner.

[0346] The tablets may contain excipients such as microcrystalline cellulose, lactose, sodium citrate, calcium carbonate, dibasic calcium phosphate and glycine, disintegrants such as starch (preferably corn, potato or tapioca starch), sodium starch glycollate, croscarmellose sodium and certain complex silicates, and granulation binders such as polyvinylpyrrolidone, hydroxypropylmethylcellulose (HPMC), hydroxypropylcellulose (HPC), sucrose, gelatin and acacia. Additionally, lubricating agents such as magnesium stearate, stearic acid, glyceryl behenate, and talc may be included.

[0347] Solid compositions of a similar type may also be employed as fillers in gelatin capsules. Preferred excipients in this regard include lactose, starch, cellulose, milk sugar, or high molecular weight polyethylene glycols. For aqueous suspensions and/or elixirs, the agent 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.

[0348] As indicated, a therapeutic agent of the present invention can be administered intranasally or by inhalation and is 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™m) 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 the agent and a suitable powder base such as lactose or starch.

[0349] Therapeutic administration of polypeptide ligands (e.g. modulators) may also be accomplished using gene therapy. A nucleic acid including a promoter operatively linked to a heterologous polypeptide may be used to produce high-level expression of the polypeptide in cells transfected with the nucleic acid. DNA or isolated nucleic acids may be introduced into cells of a subject by conventional nucleic acid delivery systems. Suitable delivery systems include liposomes, naked DNA, and receptor-mediated delivery systems, and viral vectors such as retroviruses, herpes viruses, and adenoviruses.

[0350] The invention further provides a method of treating a mammal, the method comprising administering to a mammal a ligand (e.g. modulator) or pharmaceutical composition of the present invention.

[0351] Typically, a physician will determine the actual dosage which will be most suitable for an individual subject and it will vary with the age, weight and response of the particular patient and severity of the condition. The dosages below are exemplary of the average case. There can, of course, be individual instances where higher or lower dosage ranges are merited.

[0352] The specific dose level and frequency of dosage for any particular patient may be varied and will depend upon a variety of factors including the activity of the specific compound employed, the metabolic stability and length of action of that compound, the age, body weight, general health, sex, diet, mode and time of administration, rate of excretion, drug combination, the severity of the particular condition, and the individual undergoing therapy. By way of example, the pharmaceutical composition of the present invention may be administered in accordance with a regimen of 1 to 10 times per day, such as once or twice per day.

[0353] For oral and parenteral administration to human patients, the daily dosage level of the agent may be in single or divided doses.

[0354] Applications

[0355] As mentioned above, some glycosyltransferases are involved in the biosynthesis of bacterial lipooligosaccharide (LOS) which is thought to be essential for the pathogen to attach to host receptors and to evade the immune response (Kahler C M, Stephens D S, Crit Rev Microbiol 1998;24(4):281-334). A ligand or modulator may be able to modulate the activity of a glycosyltransferase within a bacterial cell. Hence a ligand or modulator according to the present invention may be capable of modulating LOS synthesis and therefore modulating bacterial attachment and/or recognition by the immune system.

[0356] Lipooligosaccharides (LOSs) are expressed on mucosal Gram-negative bacteria, including members of the genera Neisseria, Haemophilus, Bordetella, and Branhamella. They can also be expressed on some enteric bacteria such as Campylobacter jejuni and Campylobacter coli strains. LOSs share similar lipid A structures with an identical array of functional activities as LPSs. LOSs lack O-antigen units with the LOS oligosaccharide structures limited to 10 saccharide units. The LOS species of pathogenic Neisseria can play a major role in pathogenesis through enhancing the resistance of the organism to killing by normal human serum. Other distinguishing characteristics of LOS are the structural and antigenic similarity of some LOS species to human glycolipids and the potential for certain LOSs to be modified in vivo by host substances or secretions. These modifications of LOS in different environments of the host result in synthesis of new LOS structures that probably benefit the survival of the pathogen. The LOS of N. gonorrhoeae can act as a ligand of human receptors, promoting invasion of host cells.

[0357] Therefore, a ligand or modulator of the invention may be used to treat diseases caused by the following pathogenic organisms that have a LOS/LPS involvement in disease: Neisseria (meningitidis and gonnhorea) Haemophilus (influenzae and ducreyii), Branhanella (Moraxella), Canplyobacter, and Helicobacter. In a preferred embodiment the disease is associated with infection by a bacterium from the species Neisseria In a highly preferred embodiment the disease is associated with infection by Neisseria meningitidis, such diseases include, but are not limited to meningitis.

[0358] Meningococcal LOS is a critical virulence factor in N. meningitidis infections and is involved in many aspects of pathogenesis, including the colonization of the human nasopharynx, survival after bloodstream invasion, and the inflammation associated with the morbidity and mortality of meningococcemia and meningitis. Meningococcal LOS, which is a component of serogroup B meningococcal vaccines currently in clinical trials, has been proposed as a candidate for a new generation of meningococcal vaccines. (FEMS Immunol Med Microbiol 1996 Dec 1;16(2):105-15 Moran A P, Prendergast M M, Appelmelk B J)

[0359] LOS of pathogenic Neisseria spp. mimic the carbohydrate moieties of glycosphingolipids present on human cells. Such mimicry may serve to camouflage the bacterial surface from the host The LOS component is antigenically and/or chemically identical to lactoneoseries glycosphingolipids and can become sialylated in Neisseria gonorrhoeae when the bacterium is grown in the presence of cytidine 5′-monophospho-N-acetylneuraminic acid, the nucleotide sugar of sialic acid Strains of Neisseria meningitidis and Haemophilus influenzae also express similarly sialylated LPS. Sialylation of the LOS influences susceptibility to bactericidal antibody, may decrease or prevent phagocytosis, cause down-regulation of complement activation, and decrease adherence to neutrophils and the subsequent oxidative burst response. The core oligosaccharides of LPS of Campylobacter jejuni serotypes which are associated with the development of the neurological disorder, Guillain-Barre syndrome (GBS), exhibit mimicry of gangliosides. Cross-reactive antibodies between C. jejuni LPS and gangliosides are considered to play an important role in GBS pathogenesis. In contrast, the O-chain of a number of Helicobacter pylori strains exhibit mimicry of Lewis(x) and Lewis(y) blood group antigens. The role of this mimicry may play a role in bacterial camouflage, the induction of autoimmunity and immune suppression in H. pylori-associated disease. ( Crit Rev Microbiol 1996;22(3):139-8 Preston A, Mandrell R E, Gibson B W, Apicella M A)

[0360] Bordetella, does not use molecular mimicry but has either LOS or LPS as a critical virulence factor. (Infect Immun 2000 Dec;68(12):6720 Harvill E T, Preston A, Cotter P A, Allen A G, Maskell D J, Miller J F). Bordetella pertussis, Bordetella parapertussis, and Bordetella bronchiseptica are closely related subspecies that cause respiratory tract infections in humans and other mammals and express many similar virulence factors. Therefore, a ligand (e.g. modulator) of the invention may be used in preventing or treating diseases associated with Bordetella.

[0361] The following non-limiting examples are illustrative of the present invention:

EXAMPLES

Example 1

[0362] Material and Methods

[0363] Expression and Purification:

[0364] Recombinant LgtC-25 was over expressed in E. coli (AD202) as described previously (ref. 6). Briefly, the protein was first purified on a Q-sepharose fast flow column followed by a Superdex200 column (Pharmacia). Selenomethionyl LgtC was expressed in E. coli BL21 in minimal media supplemented with glucose and MgCl2. When the cultures reached OD600=0.6, selenomethionine (50 mg 1−1) was added and at the same time the synthesis of methionine was down-regulated by the addition of 100 mg 1−1 phenylalanine, threonine, lysine and 50 mg 1−1 leucine, isoleucine, valine and proline (ref 41). After an additional 15 minutes, expression was induced with 0.5 mM IPTG after which the culture was grown for 6 hours. Selenomethionyl protein was purified following the same protocol with the exception that 5 mM DTT was included in all buffers. Incorporation of selenomethionine was confirmed by mass spectrometry. The structure was determined using a double cysteine mutant C128/174S from which more reproducible crystals could be produced than from the wildtype.

[0365] Site-directed Mutagenesis Via PCR.

[0366] All mutations were constructed in pCWlgtC-25 (ref. 6). A two stage PCR mutagenesis protocol was used. Two separate PCR reactions were performed, to generate two overlapping gene fragments, one of which contains the mutation. The primers were from the 5′ (primer 1) and (primer 2) 3′ ends of the gene as well as two internal primers. One internal primer contained the mutation and the other was chosen such that the 2 PCR products would overlap by 100 bp. These two products were gel purified, and then used as template for a third PCR reaction containing primers 1 and 2. This produced the fall length version of the gene with the mutation incorporated. Primers 1 and 2 contain BamHI and HindIII restriction sites which were used to subclone the final PCR product into pCW. Constructs were sequenced to verify the presence of only the mutation of interest.

[0367] Kinetic Assays

[0368] Synthesis of UDP-2Fgal was achieved essentially as described previously (ref. 19). Syntheses of 4′-deoxylactose, 6′-deoxylactose and galactosyl β-1,6-lactose will be described elsewhere. Kinetic studies were performed at 30° C. in 20 mM HEPES, pH 7.5 containing 0.1% bovine serum albumin, 50 mM KCl, 5 mM MnCl2 and 5 mM DTT. The reaction was monitored via a continuous coupled assay similar to that described by Gosselin et al (ref. 42), in which UDP release is coupled to the oxidation of NADH (λ=340 nm, ε=6.22 nM−1cm−1). The change in absorbance was measured by means of a UNICAM 8700 UV-Vis spectrophotometer equipped with a circulating water bath. Kinetic parameters were calculated by direct fit of the initial rates to the respective equations using Grafit version 3.0 (ref.43).

[0369] Crystallization and Data Collection:

[0370] For crystallization 3 mM TCEP, 3 mM MnCl2 and 5 mM UDP-2FGal was added to the protein (10 mg ml−1) in 50 mM NH4OAc, pH 7.0. The protein solution was further mixed in equal amounts with reservoir solution containing 50 mM NaOAc pH 5.0 and 5-20% PEG monomethylether 2000 and incubated on ice for 30 min before the solution was spun. Drops (6 μl) were allowed to equilibrate against the well solution as hanging drops and were streak seeded to induce crystallization. Orthorhombic LgtC crystals grow within a few hours of seeding and contain one molecule in the asymmetric unit (VM=2.0 Å3 Da−1) in space group P212121 with unit cell dimensions a=39.79 Å b=76.05 Å c=86.84 Å.

[0371] A 2.0 Å MAD dataset, using four wavelengths, was collected at the Stanford Synchrotron Radiation Laboratory, beamline 1-5 using a Quantum Q4 CCD detector. For the deoxylactose complex, selenomethionyl crystals were soaked in 10 mM 4′-deoxylactose for 24 hours prior to data collection. Data were collected on a local Rigaka RU200 rotation anode equipped with OSMIC mirrors. All data were collected at 100K using mother liquor supplemented with 20% PEG 400 as cryoprotectant. All data was processed with DENZO and SCALEPACK (ref. 44). Statistics for data collection and processing are summarized in Table 2.

[0372] Structure Determination and Refinement:

[0373] The seven Se atom positions were determined using SOLVE (ref. 45). Phases and electron density maps were improved with DM (ref. 46). The initial density maps were of excellent quality and the model was easily built using XTALVIEW (ref. 47). The sequence differs from the published sequence (p96945) in three positions; an additional Gly was added at position 57, Ser 248 was exchanged for Pro and Gly 268 exchanged for Ala. These sequence differences were confirmed with DNA sequencing. The LgtC structure (with solvent, Mn and UDP-Gal removed) was used as the starting model for the 4-deoxylactose complex. Both complexes were refined with CNS 1.0 (ref. 48) where 5% of the data were flagged for the Rfree calculation. The parameters described by Engh and Huber (ref. 49) were used and the dictionaries for the substrates were generated by XPLO2D (ref. 50). All model building was performed using XTALVIEW. The quality of the models was analyzed with the program PROCHECK (ref. 51). Details of the refinement statistics are given in Table 2. Two regions with weak or no density have been excluded from the model, residues 218-221 between helix K and L, and the four C-terminal residues.

[0374] Structural Analysis and Figure Preparation:

[0375] Surfaces were calculated with the CCP4 program AREAIMOL using a probe with a 1.4 Å radius . (ref. 34). Superpositions were done with the program TOP (ref. 18). FIGS. 1 and 6 were prepared with ChemDraw; FIGS. 3, 4c and 5 were prepared with MOLSCRIPT52 and rendered with Raster3D 53. FIG. 4b was prepared with GRASP (ref 54).

[0376] Results and Discussion

[0377] Overall Fold:

[0378] The galactosyl transferase structure determined here is that of a deletion mutant of LgtC missing the C-terminal 25 residues. This was necessary since the C-terminal 50 residues of LgtC have been proposed to be involved in attachment of LgtC (and other related sugar transferases) to the surface of the bacterial membrane (ref. 6), and the full length protein is less stable. As shown in FIG. 2 the deleted part of the enzyme is very rich in basic residues (Arg 287, Lys 292, Arg 293, Arg 297, Arg 299, Arg 300, Lys 301, Arg 305, Arg 308, Lys 309) which would be complementary to the negatively charged phospholipids in the membrane. There are also several hydrophobic and aromatic residues (Ala 283, Val 284, Met 288, Phe 289, Met 294, Leu 295, Trp 298. Leu 302, Ala 304, Phe 306, Leu 307, Ile 310, Tyr 311), which suggests that the C-terminus associates with the membrane via hydrophobic as well as electrostatic interactions. A sequence alignment of seven bacterial enzymes, all belonging to glycosyltransferase family 8, reveals that they are relatively conserved in terms of sequence and size in both the substrate binding and membrane association domains (FIG. 2). It was also necessary to replace several cysteine residues that were believed to be responsible for (reversible) aggregation of the protein in order to produce a protein that crystallized. X-ray quality crystals were then produced reliably only in the presence of an inert analogue of the sugar donor, namely UDP 2-deoxy-2-fluoro-α-D-galactopyranose (UDP-2FGal).

[0379] The structure determined is that of a monomer comprising 286 residues that form a large N-terminal α/β domain which contains the active site and a smaller helical C-terminal domain which mediates membrane attachment The overall fold is presented in FIG. 3. A central β-sheet forms the core of the α/β-domain. The sheet contains seven strands (β3, β2, β1, β4, β7, β6, β8) all of which are parallel with the exception of β7. The first 100 residues provide a nucleotide binding fold composed of four parallel strands. sandwiched between helices A and B on one side and helices C and D on the other. Helix C and the N-terminal part of helix D are both of 310 character. The remainder of the central β-sheet is flanked by four α-helices on each side. In addition, an antiparallel β-ribbon formed by β5 and β9 lies almost perpendicular to the sheet The substrate binding cleft is an extended, largely occluded groove that lies along the base of the central β-sheet.

[0380] The small C-terminal domain of LgtC, residues 248-282 (the last four residues are disordered), is mainly helical, with helix M and helix N (which is 310 in nature) forming a small pedestal that packs perpendicular to helices A and B of the nucleotide binding motif and to the β-ribbon (FIG. 3c).

[0381] A structural homology search using the TOP server (ref. 18) indicates that only the N-terminal nucleotide binding motif of LgtC shares significant structural similarity with other protein structures in the PDB. The remaining segment, residues 101-282, displays limited identity with other known folds. The top hit is the inverting glycosyltransferase bovine β-1,4-galactosyltransferase (ref. 14). Despite the low sequence identity (˜14%), superposition of the structure of this enzyme with that of LgtC yields a root mean square (rms) deviation of 2.1 Å on 83 common C-α atoms (with portions of elements β1,2,3,4,5,7,8 and helices A, D, H, J, K and M having the closest similarity). The glycosyl transferase SpsA from Bacillus subtilis (ref. 13) also has some structural similarity with LgtC (rms deviation of 2.1 Å on 76 common C-α atoms with portions of elements β1,2,3,5,7,9 and helices A, C, D, J and L having the closest similarity). A significant difference between LgtC and the inverting transferases (SpsA, B4G and phage T4-transferase) is that the donor UDP-Gal is bound in a much more shallow, solvent-exposed binding cleft in comparison to the deep, solvent-shielded cleft of LgtC. This may well reflect a greater need to exclude solvent from the active site of an enzyme that forms a reactive glycosyl-enzyme intermediate.

[0382] UDP-sugar Binding Mode

[0383] The structure of LgtC was solved in complex with Mn2+ and a non-cleavable analogue of the donor sugar, UDP-Gal in which the hydroxyl at the 2 position of the galactose has been substituted by a fluorine. The fluorine at the 2-position serves to inductively destabilize the oxacarbenium ion-like transition states for the reaction catalyzed, thereby slowing the reaction dramatically. Indeed linetic studies showed that no transfer occurs from UDP-2FGal, but that it acts as an excellent inhibitor, with a Ki value of 2 μM (competitive with respect to UDP-Gal) as compared to the Km value of 18 μM measured for UDP-Gal (Table 1). This fluorine substitution approach has been used previously to dramatically slow reaction rates in studies on glycosidases and on the mechanistically analogous glycogen phosphorylase10 and indeed UDP-2FGal has been synthesized previously and shown to inhibit two other galactosyltransferases19.

[0384] Most of the interactions between the enzyme and the nucleotide are formed by residues located at the C-terminus of β1 and the N-terminus of helix A. Two loops, from opposite sides of the groove, fold over the UDP-2FGal as a tight lid (FIGS. 3b, 4). The first loop, residues 75-80, is a part of the nucleotide binding motif and connects helix C with helix D. The second loop consists of residues 246-251 and is also part of a hinge between the N-terminal and the C-terminal domain. In the UDP-2FGal complex, the conformations of these two loops are stabilized primarily by interactions with the donor substrate in conjunction with additional intramolecular van der Waals (Vdw) interactions observed between His 78 and Pro 248. The structure indicates that these loops would likely be disordered or would adopt alternative conformations in the absence of the donor UDP-sugar. This may explain the inability to crystallize LgtC in the absence of UDP-2FGal.

[0385] The UDP-2FGal is almost entirely buried by the enzyme, leaving only 10 Å2 or 1.5% of the molecule exposed to solvent (FIG. 4b). The donor sugar is highly ordered (Table 2) and adopts an unusual folded conformation in which the UDP moiety is bound in an extended manner but the galactose tucks back under the phosphates such that the plane of the galactose ring is almost parallel to the plane of the diphosphate (FIGS. 3, 4, 5). In other UDP-Gal complexes in the PDB, (for example in UDP-galactose 4-epimerase (ref. 20)), the UDP-Gal (or UDP-Glc) are bound in fully extended forms. As a measure of this conformation, a torsion angle calculated on PA and PB of the diphosphate and C1′ and C4′ of the galactose ring in LgtC is −10° compared to −160° in the epimerase structure. Interestingly, the conformation of the galactose-1-phosphate portion of the molecule is quite reminiscent of the conformation of glucose-1-phosphate or its analogues bound to glycogen phosphorylase (ref. 21). This is possibly quite relevant since glycogen phosphorylase is also a retaining glycosyltransferase.

[0386] The uridine diphosphate portion of UDP-2FGal binds in a cleft at the C-terminal end of the β-sheet while the uracil base stacks with conserved Tyr 11 (Phe in E. coli and Salmonella). The uracil carbonyl O4 forms a hydrogen bond with the ND2 group of Asn 10 while N3 of the base donates a hydrogen bond to OD1 of Asp 8. O2 of uracil is also within hydrogen bonding distance of the main chain nitrogen atom of Asp 8. The ribose ring adopts a C3-endo conformation in which 02 interacts with the carbonyl oxygen of Ala 6 and O3 with the main chain amide of Ile104. Both phosphates form hydrogen bonds with the protein, O2A with conserved Lys 250 (NZ) and O2B with Gly 247 (N) and His 78 (NE2).

[0387] The galactosyl moiety of the donor sugar is highly ordered within the LgtC active site (Table 2). The ring adopts a standard 4C1 chair conformation similar to that of other UDP-galactose molecules in the PDB. O3′ forms hydrogen bonds to the side chain atoms of the invariant residues Asp 103 and Arg 86. O4′ and O6′ both hydrogen bond with the side chain carboxylate of the conserved Asp 188 indicating an important role for this residue in binding and probably in catalysis also. Such bidentate hydrogen bonding of a carboxyl group with vicinal hydroxyl groups on an active site sugar is well known, as in cyclodextrin glycosyltransferases and α-amylases (both family 13 ‘hydrolases’) where an aspartic acid residue bridges O2 and O3 of the substrate (ref. 22,23). F2 engages in only very weak interactions with a single active site residue (Asn 153), thereby possibly explaining why the binding constants of UDP-2Fgal and UDP-Gal are so similar. However, as a consequence of the folded conformation of the UDP-sugar, it engages in a relatively short interaction with an oxygen atom of the adjacent phosphate moiety. Presumably a hydroxyl group at the 2-position forms a hydrogen bond here, which likely becomes much stronger at the transition state as the glycosidic bond is cleaved and negative charge accumulates on the phosphate oxygens. This would stabilise the transition state, thus promoting catalysis. An additional hydrogen bond is formed between O6′ and the amide oxygen of the conserved Gln 189. There are also several Vdw interactions with the side chain atoms of Val 79, Thr 83, Gln 187 and Gln 189.

[0388] Manganese Binding

[0389] A “DXD” sequence motif is common to a wide range of glycosyltransferases, both in prokaryotes and eukaryotes, even though they may not share other sequence similarities (ref. 5,24,25). This motif has been proposed to be involved in the co-ordination of a divalent cation in the binding of the nucleotide sugar (ref. 26), though it may also show up in other contexts. Indeed, a number of mutagenesis studies have been carried out in various species on the conserved aspartate residues in the DXD sequence and all have found that enzymatic activity is completely abolished upon removal of the carboxylate, consistent with an important role in these cases (ref. 26-29). Interestingly, LgtC has four DXD motifs but only two are located within the active site of the enzyme. One is indeed shown to have important binding interactions with the metal ion while the role of the other is primarily in the binding of the acceptor sugar. Not surprisingly, these are also the only two served DXD motifs amongst the members of family 8. Based on these observations, it is clear that a DXD sequence is not always indicative of a metal binding site in glycosyltransferases and therefore should not be used as such. However, it is interesting to note that on the basis of the DXD sequence, an interesting glycosyltransferase activity was identified in the Fringe protein and this was shown to be responsible for modulating the activity of Notch receptors (ref. 30,31).

[0390] Earlier work has shown that manganese is required for enzyme stability and activity in LgtC, as in other related glycosyltransferases (ref. 6,32). It has been presumed that the metal functions to stabilize the UDP leaving group during bond cleavage. In the structure described herein, a single well-ordered Mn2+ ion is observed coordinated by the two phosphate oxygens of UDP as well as by the side chain atoms of three protein residues conserved throughout the family 8 glycosyltransferases, His 244, Asp 103 and Asp 105 (the latter two forming the DXD motif; FIG. 4). Asp 103 provides one liganding side-chain oxygen and Asp 105 provides a bidentate interaction. The co-ordination of the Mn2+ ion exhibits standard octahedral geometry with characteristic ligand distances ranging from 2.2 to 2.4 Å33. Consistent with studies on DXD motifs in other systems, when Asp 103 is mutated to Asn or Glu activities drop dramatically, the kcat values of the mutant being 2400-fold and 3500-fold lower compared to the wild type (Table 1). The bidentate ligand, Asp 105, is also essential for full activity; when substituted by Asn or Glu the mutated LgtC expresses very poorly.

[0391] Acceptor Binding:

[0392] The acceptor analog, 4-deoxylactose, in which the nucleophilic hydroxyl at the 4′ position has been replaced by hydrogen, cannot function as a substrate for LgtC, but does still act as an inhibitor Ki=16 mM with respect to lactose). Its binding is very similar to that of lactose (Km=20 mM) indicating that interactions at the 4-position are not crucial for ground state binding. Highly ordered electron density for both donor and acceptor molecules is observed from data collected on LgtC/UDP-2FGal crystals into which the 4-deoxylactose was soaked. The non-reactive acceptor analogue is bound in a large open pocket on the C-terminal end of the α/β domain adjacent to the galactose moiety of the donor sugar. The pocket is formed by the loop between helices C and D, the domain hinge, helices F, I, J and K, (FIGS. 3, 4). The acceptor sugar is significantly more accessible to solvent than the donor, 141 Å2 or 28% of the entire molecular surface. The non-reducing terminal galactose moiety of the lactose adopts a full chair conformation. A hydrogen bond is formed from O2 to a water molecule and from O6 to Asp 130 (OD2) and Gln 189 (NE2). Binding is also stabilised by Vdw interactions with the side chain atoms of Val 76, His 78, Tyr 186, Cys 246 and Gly 247. Mutation of Asp 130 to an alanine severely limits protein expression, perhaps reflecting the intricate structural role this amino acid plays, with hydrogen bonds to the side chain nitrogen of the conserved Asn 153 and to the main chain amide of Val 133 as well as to the lactose O6. A mutant Y186F, was also generated to address the possibility of a role for its OH group in binding or catalysis upon rotation of its side chain hydroxyl closer to the reactive centre. However, the mutation affects neither expression nor kinetic parameters (Table 1) suggesting that such an important role is unlikely though Vdw interactions of its ring atoms with the lactose are probably important.

[0393] The reducing end glucose moiety of the lactose also adopts a full chair conformation, binding of the ring being stabilized by hydrophobic stacking interactions with Phe 132 and Vdw interactions with the side chain atoms of Pro 211 and Pro 248 (FIGS. 4, 5). Hydrogen bonds from O3′ to the Thr 212 hydroxyl and main chain nitrogen (via a water molecule) and a direct hydrogen bond to the side chain of Cys 246 are also observed. Biochemical studies have shown that full LgtC activity is dependent on the presence of reducing agents (ref. 6). The structure described herein clearly shows that no cysteine residues are at a suitable distance from each other to form a disulfide bridge. However, the structure does suggest that oxidation of Cys 246, located on one of the two loops that envelop the donor sugar and within hydrogen bonding distance to the acceptor sugar, could result in impaired donor and acceptor binding.

[0394] The LgtC/UDP-2FGal structure is minimally changed upon acceptor binding (r.m.s of 0.16 Å on 282 C-α atoms). All hydrogen bonds between the donor and the enzyme are maintained, with additional bonds observed from O2A of the phosphate, to Tyr 11 (OH) and the carbonyl of His 78 via a water molecule. Furthermore, in the donor/acceptor complex, the side chain of Cys 246 adopts a new conformation to form a hydrogen bond with the lactose O3′ atom. In the LgtC/UDP-2FGal complex an acetate ion is bound between sp 130 and Gln 189. Upon acceptor binding the acetate is displaced by the deoxylactose with the O6 atom forming hydrogen bonds to the side chain carboxylate of Asp 130 and the side chain amide of Gln 189.

[0395] Implications for Catalysis:

[0396] LgtC has been shown to follow an ordered bi-bi kinetic mechanism in which UDP-Gal binds first, followed by lactose. Bond rearrangement then occurs and product trisaccharide is released first, followed by UDP. The structure determined is completely consistent with this mechanism since the UDP-2Fgal is deeply buried by two loops that fold over the active site. Acceptor sugar is not required to form this complex, and indeed no significant changes in the structure of this complex are seen upon binding of 4-deoxylactose. Importantly the 2-fluorogalactose moiety is highly ordered, with multiple hydrogen bonds and Vdw interactions from conserved active site residues. Although the order of Mn2+ binding has not been determined kinetically in this enzyme, the structure suggests that the metal ion remains bound to the protein throughout, consistent with the fact that addition of exogenous Mn2+ is not essential for catalysis. Its location in the active site, coordinating to oxygens of the α- and β-phosphate moieties of UDP-2Fgal, is typical, and is consistent with a role of the cation as an acid catalyst.

[0397] Efficient catalysis of galactosyl transfer requires that water be excluded from the active site, or at least carefully controlled therein, in order to ensure that hydrolysis does not occur. The close packing and occluded nature of the donor sugar in the LgtC structure limits the binding of ordered water molecules in the active site (FIG. 4b). In the UDP-2Fgal structure, only a single water molecule is within 5 Å of the reactive center C1′ of the donor galactose (4.4 Å) and this water is displaced by the O2 hydroxyl of deoxylactose upon formation of the ternary complex. Within this complex, the reactive center C1′ atom is entirely buried by residues Ile 76, Asp 103, Asp 130, Asp 153, Ala 154, Gly 155, Tyr 186, Gln 189, His 244, Cys 246, Gly 247 and by the acceptor sugar (as calculated with CONTACT34 using a 6 Å cutoff). The closest water molecule in this complex is 7.3 Å away from the anomeric C1′ atom. Thus the enzyme has apparently evolved to exclude water, as would be expected.

[0398] As noted earlier, the stereochemical outcome of the reaction catalyzed suggests, by analogy with retaining glycosidases, that a double-displacement mechanism via a glycosyl-enzyme intermediate is occurring. If this is indeed true, then a suitable nucleophile should be located close to the anomeric carbon (C1′) of the UDP-2Fgal, and on the correct (β) face to allow direct displacement of the UDP leaving group.

[0399] Analysis of the LgtC structure indicates that the only polar atoms within 5 Å of the reactive center C1′ come from either the acceptor sugar (the lactose hydroxyl O3 (3.2 Å) and hydroxymethyl O6 (4.6 Å)) or from the side chain oxygen atom of Gln 189 (3.5 Å), and the side chain nitrogen atom of Asn 153 (4.2 Å). However, of these only the lactose O6 and the side chain oxygen atom of Gln 189 are located on the β-face on a reasonable trajectory. In light of experience with retaining glycosidases, this is surprising, since the carboxylate side chain of an Asp or Glu residue might have been anticipated on that basis. The two choices were therefore considered and evaluated separately, as follows.

[0400] The possibility of the 6-hydroxyl of lactose functioning in this fashion was initially intriguing, as this would have involved the enzyme first forming a tightly bound intermediate galactosyl β-1,6-lactose species. After movement away of the released UDP the 4-hydroxyl of the lactose could then attack the anomeric center from the α-face, forming the desired Gal α-1,4-lactose product (FIG. 6a). A particularly attractive component of this mechanism is the fact that it inherently demands formation of a ternary complex prior to the generation of a reactive intermediate, thereby minimizing the possibility of unwanted hydrolysis. Less attractive is the fact that the intermediate would not itself be inherently reactive, being a simple glycoside. The mechanism was probed experimentally in two ways. Firstly 6-deoxylactose, in which the putatively nucleophilic 6-hydroxyl had been removed, was synthesized and shown not to function as a substrate, which would be consistent with this mechanism. However, neither did it act as an inhibitor, thereby rendering its inactivity as a substrate meaningless. It does, however, indicate that binding interactions at that position, probably primarily with Asp 130, are quite important. More definitive results suggesting that this was not the likely mechanism come from the finding that galactosyl β-1,6-lactose, synthesized chemically, does not function as a substrate when incubated with LgtC in the presence of UDP plus the usual buffer components. Therefore, unless binding of this potential intermediate is too slow to permit measurable turnover, this mechanism is unlikely.

[0401] The alternative mechanism, in which the oxygen of Gln 189 attacks at the anomeric center to form an imidic ester intermediate (FIG. 6b) is initially unattractive given the fact that amides are notoriously poor nucleophiles. However, the reaction is entirely precedented, even within the field of glycosidases, since a chemically equivalent intermediate has been demonstrated to form during catalysis by N-acetylhexosaminidases from glycosidase families 18 and 20 (see ref. 10,11 for reviews). In those cases the substrate's own amide functionality attacks to form an oxazolinium ion intermediate (FIG. 6c) that is charge stabilized by an invariant carboxylate side chain close to the substrate nitrogen atom. In LgtC the oxygen atom of the side chain amide is well-positioned to perform a nucleophilic attack on C1′ both in terms of distance (3.5 Å) and in terms of the direction and angle of attack: the Cδ-Oε1-C1′ angle is 106.2° in good agreement with ideal values (FIG. 4c)35. This identical position is seen in the complex with UDP-2Fgal (r.m.s of 0.14 Å on the 9 atoms of the residue), as might be expected for a pre-organised nucleophile. Gln 189 is contained within the invariant D/EQD motif (Helix J) found in all family 8 retaining glycosyltransferases (FIG. 3) (ref. 5). The side chain amide of Glnl 89 is fully buried in the donor/acceptor complex, and is oriented through several hydrogen bonds to both sugar (donation of a hydrogen bond from Nε1 to O6 of the lactose) and conserved protein side chains (acceptance of a hydrogen bond from the side chain Nε2 of Asn 153 (itself an invariant residue found within the NAG motif in all family 8 glycosyltransferases) and the main-chain NH of Ala 154, FIG. 4c). Furthermore, charge stabilization could be provided by the nearby (4.0 Å) carboxylate side chain of Asp 130.

[0402] Interestingly a mechanism of this type has been hinted at previously for another glycosyltransferase, glycogen phosphorylase, on the basis of structures of complexes with a suspected transition state analogue inhibitor, deoxynojirimycin tetrazole (ref. 36), and of a ternary complex with a thiooligosaccharide plus phosphate (ref. 37). In both cases the group identified as being closest to the anomeric center of the sugar to be transferred, and in the best position to function as catalytic nucleophile, is the main chain oxygen of the backbone amide of His 377. Similar to LgtC, stabilization of the developing positive charge on the nitrogen in this case can be afforded by the nearby aspartate (Asp 307) located within 4 Å of the amide nitrogen. Given the parallels in the reaction catalysed and the similarity in 3-dimensional structure with other transferases (ref. 38,39) this could indicate similar roles for these two amide carbonyl groups of LgtC and glycogen phosphorylase.

[0403] This mechanistic hypothesis was tested in LgtC through mutagenesis and kinetic analysis of the resultant mutants. The mutant Q189A has a kcat value equaling 3% of that of the wild type enzyme (based on kcat values measured with varying UDP-Gal), and a very similar Km value for UDP-Gal. Interestingly, the Km value for lactose was considerably (6-7 fold) higher than that for the wild type enzyme, consistent with the presence of a hydrogen bond between Nε1 of Gln 189 and 06 of lactose. Importantly this confirms that the activity measured is indeed that of the mutant, and not due to contaminating wild type enzyme (itself unlikely since considerable precautions were taking during purification, including the use of new column packing materials for purification of this mutant). However, this relatively high residual activity renders a role for Gln 189 as the catalytic nucleophile somewhat unlikely given the presumed crucial importance of such a residue. Indeed, equivalent mutations of catalytic nucleophiles in retaining glycosidases typically reduce kcat values by at least 105 fold (ref. 10,11). The possibility that the mutant catalyses hydrolysis rather than transfer as a consequence of water binding in the site vacated by the side chain of Gln 189 was evaluated by product analysis. Only transfer products were observed, not galactose. Possible ‘rescue’ of activity by added small molecules that could bind in the cavity created, as has been seen for retaining glycosidases (ref. 11,40) was also probed. No rate increases were observed with any of the added reagents (formate, acetate, formamide, azide, acetamide), although modeling suggests that binding of these molecules in the Q189A mutation may be sterically unfavorable. Another possibility that cannot be ruled out is that an adjacent residue substitutes for Gln 189 within this mutant, but with lower efficiency.

[0404] Given the fact that definitive evidence of a double displacement mechanism remains elusive, a third possibility, but one with only limited chemical precedent, is that the reaction proceeds via a front side SN2-like attack, otherwise known as an SNi mechanism. In this scenario, approach of the nucleophile (the reactive hydroxyl of the acceptor sugar) towards the reactive centre would occur from the same side from which the UDP leaving group would depart and reaction would most likely proceed via a highly dissociative (oxocarbenium ion-like) transition state. Such a mechanism has been proposed previously for glycogen phosphorylase (ref. 9), but no experimental support has yet been accumulated.

[0405] Conclusions:

[0406] Determination of this first three-dimensional structure of a retaining nucleotide sugar-dependent glycosyl transferase in a complex with analogues of both substrates for the enzyme provides unique insights into the structure and mechanism of this important class of enzymes. Partial commonality of fold with those of several inverting transferases suggest that common structural elements are employed in the construction of a glycosyl transfer site, irrespective of the stereochemical outcome of the reaction.

[0407] This is the first structure of a glycosyltransferase to provide any structural information about the donor and acceptor sugars, and the first crystal structure of a retaining transferase, and is invaluable for rational inhibitor design.

Example 2

[0408] Synthesis of Alternate Acceptor Substrates:

[0409] 2,2′,3,3′,4′,6,6′-Hepta-O-acetyl-α-lactosyl Bromide (1)

[0410] To a 0° C. solution of per-O-acetylated β-D-lactose (4.7 g, 6.87 mmol) in anhydrous CH2Cl2 (15 mL) under nitrogen was added 45% HBr/AcOH (5.3 mL). The reaction vessel was then sealed and the solution was allowed to stir at room temperature. After 2.5 h, the reaction mixture was poured into chilled water (80 mL) and diluted with CH2Cl2 (60 mL). Solid NaHCO3 was added to neutralize the excess acid and the layers were separated. The aqueous layer was further extracted with CH2Cl2 (2×80 mL) and the combined organic extracts were washed with water (2×80 mL), aq. NaHCO3 (50 mL) and brine (50 mL). Evaporation of the solvent under reduced pressure after drying over MgSO4 yielded 1 (4.5 g, 93%) as a white brittle solid. 1H NMR (CDCl3, 400 MHz): δ 6.5 (d, 1 H, J1,2 4.0 Hz, H-1), 5.53 (dd, 1 H, J3,2 9.6, J3,4 9.6 Hz, H-3), 5.33 (dd, 1 H, J4′,3′ 3.4, J4′,5′ 0.9 Hz, H-4′), 5.11 (dd, 1 H, J2′,3′ 10.4, J2′,1′ 7.9 Hz, H-2′), 4.94 (dd, 1 H, J3′,2′ 10.4, J3′3,4′3.4 Hz, H-3′), 4.74 (dd, 1 H, J2,3 9.6, J2,1 4.0 Hz, H-2), 4.49 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 4.47 (dd, 1 H, J6a,6b 12.0, J6a,5 1.7 Hz, H-6a), 4.02-4.23 (m, 4 H, H-5, H-6b, H-6a′, H-6b′), 3.86 (ddd, 1 H, J5′,6b′ 7.3, J5′,6a′ 6.4, J5′,4′ 0.9 Hz, H-5′), 3.83 (dd, 1 H, J4,5 9.8, J4,3 9.6 Hz, H-4), 2.13, 2.10, 2.06, 2.04, 2.03, 2.02, 1.94 (s, 21 H, 7×OAc).

[0411] Benzyl 2,2′,3,3′,4′,6,6′-hepta-O-acetyl-β-lactoside (2)

[0412] 1 (2.6 g, 3.69 mmol) was stirred in anhydrous CH2Cl2 (25 mL) containing 4 Å sieves under an atmosphere of nitrogen when benzyl alcohol (1.9 mL, 18.47 mmol) and AgCO3 (2.0 g, 7.39 mmol) were added, along with a crystal of iodine. The reaction mixture was covered and stirred at room temperature overnight before it was filtered through Celite®. The filtrate was evaporated in vacuo and the residue was chromatographed over silica gel (PE:EtOAc, 3:2 to 1:1). Crystallization from PE/EtOAc yielded 2 (2.0 g, 75%) as a white solid. 1H NMR (CDCl3, 400 MHz): δ 7.22-7.35 (m, 5H, Ar), 5.32 (dd, 1 H, J4′,3′ 3.3, J4′,5′ 0.8 Hz, H-4′), 5.16 (dd, 1 H, J3,2 9.3, J3,4 9.2 Hz, H-3), 5.08 (dd, 1 H, J2′,3′ 10.4, J2′,1′ 7.9 Hz, H-2′), 4.99 (dd, 1 H, J2,3 9.3, J2,1 7.9 Hz, H-2), 4.93 (dd, 1 H, J3′,2′ 10.4, J3′,4′ 3.3 Hz, H-3′), 4.86 (d, 1 H, J 12.3 Hz, PhCH), 4.58 (d, 1 H, J 12.3 Hz, PhCH), 4.50 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 4.48 (d, 1 H, J1,2 7.9 Hz, H-1), 4.48-4.52 (m, 1 H, H-6a), 4.00-4.15 (m, 3 H, H-6b, H-6a′, H-6b′), 3.84 (ddd, 1 H, J5′,6b′ 7.4, J5′,6a′ 6.3, J5′,4′ 0.8 Hz, h-5′), 3.79 (dd, 1 H, J4,5 9.6, J4,3 9.2 Hz, H-4), 3.56 (ddd, 1 H, J5,4 9.6, J5,6b 5.0, J5,6a 2.0 Hz, H-5), 2.12, 2.11, 2.02, 2.01, 2.00, 1.98, 1.94 (s, 21H, 7×OAc).

[0413] Anal. Calcd. for C33H42O18: C, 54.54; H, 5.83. Found: C, 54.50; H, 5.93.

[0414] Benzyl β-lactoside (3)

[0415] To a solution of 2 (1.24 g, 1.71 mmol) in anhydrous MeOH (30 mL) under nitrogen was added a catalytic amount of sodium methoxide until the pH of the solution was around 10. The reaction mixture was then stirred overnight at room temperature before it was neutralized with acidic Amberlyte® resin. After evaporation of the solvent, crystallization of the resulting residue from MeOH/EtOAc yielded 3 (0.64 g, 87%) as a white solid. 1H NMR (D2O, 400 MHz) selected data only: δ 7.30-7.60 (m, 5 H, Ar), 4.90 (d, 1 H, J 11.4 Hz, PhCH), 4.52 (d, 1 H, J1′,2′ 8.0 Hz, H-1′), 4.41 (d, 1 H, J1,2 7.8 Hz, H-1), 3.95 (dd, 1 H, J6a,6b 12.3, J6a,5 2.1 Hz; H-6a), 3.88 (d, 1 H, J4′,3′ 3.3 Hz, H-4′), 3.32 (dd, 1 H, J4,5 8.7, J4,3 8.4 Hz, H-4).

[0416] Anal. Calcd. for C19H28O11: C, 52.77; H, 6.53. Found: C, 52.47; H, 6.63.

[0417] Allyl 2,2′,3,3′,4′, 6,6′-hepta-O-acetyl-β-lactoside (4)

[0418] 1 (0.5 g, 0.69 mmol) was stirred in anhydrous CH2Cl2 (5 mL) containing 4 Å sieves under an atmosphere of nitrogen when allyl alcohol (0.24 mL, 3.46 mmol) and Ag2CO3 (0.4 g, 1.38 mmol) were added along with a crystal of iodine. The reaction was covered and stirred at room temperature for 9 h before it was filtered through Celite®. The filtrate was evaporated in vacuo and the residue was chromatographed over silica gel (PE:EtOAc, 3:2 to 1: 1) to yield 4 (0.35 g, 76%) as a white solid. 1H NMR (CDCl3, 400 MHz): δ 5.81 (m, 1 H, OCH2CH=CH2), 5.32 (dd, 1 H, J4′,3′ 3.4, J4′,5′ 0.9 Hz, H-4′), 5.23 (ddd, 1 H, Jtrans 17.3, J 3.2, Jgem 1.6 Hz, OCH2CH=CHtrans), 5.17 (dd, 1 H, J3,2 9.3, J3,4 9.2 Hz, H-3), 5.17 (ddd, 1 H, Jcis 10.5, J 2.8, Jgem 1.6 Hz, OCH2CH═CHcis), 5.08 (dd, 1 H, J2′,3′ 10.4, J2′,1′ 7.9 Hz, H-2′), 4.93 (dd, 1 H, J3′,2′ 10.4, J3′,4′ 3.4 Hz, H-3′), 4.90 (dd, 1 H, J2,3 9.3, J2,1 7.9 Hz, H-2), 4.50 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 4.46 (d, 1 H, J1,2 7.9 Hz, H-1), 4.44-4.50 (m, 1 H, H-6a), 4.27 (ddt, 1 H, J 13.2, J 4.9, J 1.5 Hz, OCR), 4.01-4.14 (m, 4 H, H-6b, H-6a′, H-6b′, OCH), 3.84 (ddd, 1 H, J5′,6b′ 7.2, J5′,6a′ 6.4, J5′,4′ 0.9 Hz, H-5′), 3.78 (dd, 1 H, J4,5 9.7, J4,3 9.2 Hz, H-4), 3.57 (ddd, 1 H, J5,4 9.7, J5,6b 5.0, J5,6a 2.0 Hz, H-5), 2.13, 2.10, 2.03, 2.01, 1.94 (s, 21 H, 7×OAc).

[0419] Allyl β-lactoside (5)

[0420] 4 (0.14 g, 0.21 mmol) was dissolved in anhydrous MeOH at 0° C. under an atmosphere of nitrogen when gaseous ammonia was bubbled into the solution. After 5 min, both the ammonia source and ice bath were removed and the reaction mixture was stirred overnight at room temperature. Evaporation of the solvent in vacuo followed by chromatography over silica gel (EtOAc:MeOH:H2O, 15:4:1) yielded 5 (47.5 mg, 60%) as a white solid. 1H NMR (D2O, 400 MHz) selected data only: δ 5.95 (m, 1 H, OCH2CH═CH2), 5.35 (dd, 1 H, Jtrans 17.3, Jgem 1.4 Hz, CH═CHtrans), 5.26 (d, 1 H, Jcis 8.4 Hz, CH═CHcis), 4.50 (d, 1 H, J1′,2′ 8.0 Hz, H-1′), 4.42 (d, 1 H, J1,2 7.7 Hz, H-1), 4.37 (m, 1H, OCH), 4.20 (m, 1 H, OCH), 3.95 (dd, 1 H, J6a,6b 12.2, J6a,5 1.7 Hz, H-6a), 3.89 (d, 1 H, J4′,3′ 3.1 Hz, H-4′), 3.52 (dd, 1 H, J4,5 9.8, J4,3 7.8 Hz, H-4).

[0421] Anal. Calcd. for C15H26O11.½H2O: C, 46.03; H, 6.95. Found: C, 46.52; H, 6.85.

[0422] 4-Pentenyl 2,2′,3,3′,4′,6,6′-hepta-Oacetyl-β-lactoside (6)

[0423] 1 (0.5 g, 0.72 mmol) was stirred in anhydrous CH2Cl2 (5 mL) containing 4 Å sieves under an atmosphere of nitrogen when 4-penten-1-ol (0.37 mL, 3.60 mmol) and Hg(CN)2 (0.3 g, 1.08 mmol) were added along with a crystal of iodine. The reaction mixture was covered and stirred at room temperature for 13.5 h before it was filtered through Celite®. The filtrate was evaporated in vacuo and the residue was chromatographed over silica gel (PE:EtOAc, 3:2 to 1:1) to yield 6 (0.21 g, 41%) as a colourless gum. 1H NMR (CDCl3, 400 MHz): δ 5.75 (m, 1 H, CH═CH,), 5.32 (dd, 1 H, J4′,3′ 3.4, J4′,5′ 0.8 Hz, H4′), 5.17 (dd, 1 H, J3,2 9.4, J3,4 9.2 Hz, H-3), 5.08 (dd, 1 H, J2′,3′ 10.4, J2′,1′ 7.9 Hz, H-2′), 4.98 (ddd, 1 H, Jtrans 17.1, J 3.4, Jgem 1.7 Hz, CH═CHtrans), 4.93 (dd, 1 H, J3′,2′ 10.4, J3′,4′ 3.4 Hz, H-3′), 4.92-4.96 (m, 1 H, CH═CHcis), 4.87 (dd, 1 H, J2,3 9.4, J2,1 8.0 Hz, H-2), 4.46 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 4.43 (d, 1 H, J1,2 8.0 Hz, H-1), 4.42-4.46 (m, 1 H, H-6a), 4.02-4.14 (m, 3 H, H-6b, H-6a′, H-6b′), 3.87 (dd, 1 H, J4,5 9.7, J4,3 9.2 Hz, H4), 3.84 (m, 1 H, H-5′), 3.81 (dt, 1 H, J 9.8, J 6.2 Hz, OCH), 3.57 (ddd, 1 H, J5,4 9.7, J5,6b 5.1, J5,6a 2.0 Hz, H-5), 3.45 (dt, 1 H, J 9.8, J6.7 Hz, OCH), 2.14,2.12, 2.09,2.03, 2.02, 2.01, 1.94 (s, 21 H, 7×OAc), 1.52-1.70 (m, 4 H, CH2CH2).

[0424] 4-Pentenyl β-lactoside (7)

[0425] To a solution of 6 (0.45 g, 0.63 mmol) in anhydrous MeOH (20 mL) under nitrogen was added a catalytic amount of sodium methoxide until the pH of the solution was around 10. The reaction mixture was then stirred overnight at room temperature before it was neutralized with acidic Amberlyte® resin. After the solvent was evaporated in vacuo, chromatography of the resulting residue over silica gel (EtOAc:MeOH:H2O, 15:4:1) yielded 7 (0.17 g, 67%) as a white powder. 1H NMR (D2O, 400 MHz) selected data only: δ 5.89 (m, 1 H, CH═CH2), 5.06 (dd, 1 H, Jtrans17.3, Jgem 1.0 Hz, CH═CHtrans), 5.00 (dd, 1 H, Jcis 9.3, Jgem 1.0 Hz, CH═CHcis), 4.45 (d, 1 H, J1′,2′ 7.8 Hz, H-1′), 4.42 (d, 1 H, J1,2 7.6 Hz, H-1), 2.07-2.17 (m, 2 H, CH2CH═CH2), 1.65-1.75 (m, 2 H, OCH2—CH2).

[0426] Anal. Calcd. for C17H30O11.½H2O: C, 48.68; H, 7.45. Found: C, 48.98; H, 7.14.

[0427] 2,3-Dihydroxypropyl 2,2′,3,3′,4′,6,6′-hepta-O-acetyl-β-lactoside (8)

[0428] N-Methylmorpholino N-oxide (0.02 g, 0.18 mmol) was dissolved in a solution of 4:1 acetone:water (1.5 mL) under an atmosphere of nitrogen at 0° C. when a catalytic amount of osmium tetroxide in t-butanol was added. To this was added a solution of 4 (0.11 g, 0.16 mmol) in acetone (0.5 mL) and the reaction mixture was stirred overnight. Sodium bisulfite (0.06 g, 0.55 mmol) in water (1 mL) was then added to the reaction and stirring was continued for 1 h. The reaction was poured into brine (10 mL) and extracted with CH2Cl2 (2×10 mL). Evaporation of the combined organic layers after drying over MgSO4 yielded 8 (0.11 g, 96%) as a white solid. 1H NMR (CDCl3, 400 MHz) selected data only: δ 5.35 (d, 1 H, J4′.,3′ 3.3 Hz, H-4′), 5.18 (dd, 1 H, J3,2 9.5, J3,4 9.1 HZ, H-3), 5.08 (dd, 1 H, J2′,3′ 10.4, J2′,1′ 7.9 Hz, H-2′), 4.94 (dd, 1 H, J3′,2′ 10.4, J3′,4′ 3.3 Hz, H-3′), 4.87 (dd, 1 H, J2,3 9.5, J2,1 8.0 Hz, H-2), 4.53 (ddd, 1 H, J 12.1, J 5.3, J 2.1 Hz, OCH), 4.44 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 4.42 (d, 1 H, J1,2 8.0 Hz, H-1), 2.17, 2.13, 2.05, 2.03, 2.02, 1.94 (s, 21 H, 7×OAc).

[0429] 2,3-Dihydroxypropyl β-lactoside (9)

[0430] To a solution of 8 (0.10 g, 0.15 mmol) in anhydrous MeOH (20 mL) under nitrogen was added a catalytic amount of sodium methoxide until the pH of the solution was around 10. The reaction mixture was then stirred overnight at room temperature before it was neutralized with acidic Amberlyte® resin. After evaporation of the solvent, crystalization of the resulting residue from MeOH yielded 9 (34.5 mg, 57%) as a white solid. 1H NMR (D2O, 400 MHz) selected data only: δ 4.47 (d, 1 H, J1,2 8.0 Hz, H-1), 4.42 (d, 1 H, J1′,2′ 8.0 Hz, H-1′).

[0431] Anal. Calcd. for C15H28O13: C, 43.27; H, 6.78. Found: C, 43.30; H, 6.92.

[0432] Synthesis of UDP-2FGal:

[0433] 3,4,6-Tri-O-acetyl-2-deoxy-2-fluoro-D-galactopyranose (10)

[0434] 3,4,6-Tri-O-acetyl-D-galactal (0.912 g, 3.349 mmol) was dissolved in DMF (15 mL), then water (6 mL) and Selectfluor™ (N-fluoro-N-chloromethyltriethylenediamine bis(tetrafluoroborate), 4.20 g, 11.80 mmol) from Air Products and Chemicals Inc. were added and the reaction mixture was stirred at 50° C. After 24 h, the reaction was shown to be complete by TLC (PE:EtOAc, 3:2). To the reaction mixture was added water (40 mL) and this was then extracted with CH2Cl2 (3×50 mL). The combined organic layers were washed with water (3×50 mL), dried over MgSO4 and the solvent was removed under reduced pressure. Chromatography of the resulting residue over silica gel (PE:EtOAc, 3:2 to 1: 1) yielded 10 (0.36 g, 35%) as a colourless gum. 1H NMR (CDCl3, 400 MHz) for the α anomer: δ 5.52 (d, 1 H, J1,2 3.8 Hz, H-1), 5.38-5.50 (m, 2 H, H-3, H-4), 4.75 (ddd, 1 H, J2,F 49.9, J2,3 10.0, J2,1 3.8 Hz, H-2), 4.47 (m, 1 H, H-5), 4.00-4.15 (m, 2 H H-6a, H-6b), 2.10, 2.00, 1.99 (s, 9 H, 3×OAc). 19FNMR(CDCl3, 188 MHz): δ-131.1 (dd, JF,2 49.9, JF,3 14.5 Hz).

[0435] 1,3,4,6-Tetra-O-acetyl-2-deoxy-2-fluoro-β-galactopyranose (11)

[0436] To a solution of 10 (0.88 g, 2.84 mmol) in pyridine (7 mL) was added acetic anhydride (3.5 mL) and the reaction was stirred at room temperature overnight The pyridine and acetic anhydride were then removed by evaporation under reduced pressure and the residue was then taken up in 10% v/v HCl (80 mL) and extracted with CH2Cl2 (3×70 mL). The combined organic extracts were washed with 10% v/v HCl (70 mL), aq. NaHCO3 (70 mL), water (70 mL) and brine (70 mL), dried over MgSO4 and the solvent was evaporated in vacuo to yield the desired compound as a mixture of anomers. The residue was then dissolved in anhydrous CH2Cl2 (10 mL) under an atmosphere of argon and the temperature was brought to 0° C. To this was added a solution of 45% HBr/AcOH after which the argon source was removed and the reaction vessel was sealed and allowed to warm to room temperature. After 4 h, the reaction was poured into ice water (80 mL) and diluted with CH2Cl2 (80 mL). Solid NaHCO3 was added to neutralize the excess acid and the layers were separated. The aqueous layer was further extracted with CH2Cl2 (2×70 mL). The organic layers were subsequently combined and washed with aq. NaHCO3 (2×70 mL), water (100 mL) and brine (70 mL) and dried over MgSO4. Evaporation of the solvent under reduced pressure yielded a beige gum to which acetic acid (35 mL) and Hg(OAc)2 (1.87 g, 5.97 mmol) were added. The reaction was allowed to stir at room temperature under an atmosphere of argon. After 3 h, the reaction was poured into water (100 mL) and then extracted with CH2Cl2 (3×80 mL). The combined organic extracts were washed with aq. NaHCO3 (3×80 mL), water (80 mL) and brine (80 mL). After drying over MgSO4, the solvent was removed in vacuo and the residue was chromatographed over silica gel (PE:EtOAc, 3:1 to 5:2) to yield 11 (0.83 g, 83%) as a white solid. 1H NMR (CDCl3, 400 MHz): δ 5.77 (dd, 1 H, J1,2 8.1, J1,F 4.1 Hz, H-1), 5.43 (m, 1 H, H-4), 5.15 (ddd, 1 H, J3,F 13.2, J3,2 9.8, J3,4 3.6 Hz, H-3), 4.62 (ddd, 1H, J2,F 51.6, J2,3 9.8, J2,1 8.1 Hz, H-2), 4.05-4.20 (m, 3 H, H-5, H-6a, H6b), 2.18, 2.14, 2.05, 2.03 (s, 12 H, 4×OAc). 19F NMR (CDCl3, 188 MHz): δ-132.1 (ddd, JF,2 51.6, JF,3 13.2, JF,1 4.1 Hz).

[0437] 2-Deoxy-2-fluoro-α-D-galactopyranose-1-phosphate, mono(tri-n-octyl)ammonium Salt (12)

[0438] Anhydrous H3PO4 (0.31 g, 3.17 mmol) was dried under vacuum for 24 h before it was melted at 50° C. 11 (0.14 g, 0.40 mmol) was then added and the reaction mixture was stirred under reduced pressure (20 mm Hg) for 9 h. After this time, THF (1 mL) and a solution of 2 M LiOH (6 mL) were added and the reaction mixture was allowed to stir at room temperature overnight After filtering through Celite® and washing with 0.01 M LiOH, the solvent was evaporated in vacuo. The residue was then dissolved in water and passed through a column of Bio-Rad AG 50W-X2, 200-400 mesh, sulfonic acid cation exchanger (H+ form). The desired fractions were pooled and the solvent volume was decreased by evaporation under reduced pressure. Tri-n-octylamine (0.14 g, 0.40 mmol) was added and the solution was lyophilized yielding 12 (0.28 g) as a colourless syrup. 1H NMR (CDCl3, 400 MHz): δ 5.74 (dd, 1 H, J1,P 5-9, J1,2 3.6 Hz, H-1), 4.63 (m, 1 H, H-2), 4.23 (m, 1 H, H-3), 3.72-4.15 (m, 4 H, H-4, H-5, H-6a, H-6b), 2.80 (m, 6 H, NCH2), 1.65 (m, 6 H, NCCH2), 1.30 (m, 30 H, CH2), 0.85 (t, 9 H, CH3). 19F NMR (CDCl3, 188 MHz, proton decoupled): δ-132.4. 31P NMR (CDCl3, 81 MHz proton decoupled): δ 0.01.

[0439] Uridine 5′-diphospho-(2-deoxy-2-fluoro)-α-D-galactopyranose, di-ammonium Salt (13)

[0440] To 12 (0.25 g, 0.40 mmol) was added anhydrous pyridine (5 mL) which was then evaporated. This procedure was repeated twice before UMP-morpholidate (0.33 g, 0.48 mmol) was added. Evaporation with anhydrous pyridine (5 mL) was again repeated three times. 1H tetrazole (0.07 g, 1.01 mmol) and anhydrous pyridine (3 mL) were then added and the reaction mixture was stirred at room temperature. An aliquot of the reaction mixture was transferred into an NMR tube containing a capillary of DMSO-d6 so that the progress of the reaction could be monitored via 31P NMR. After 27 days, the reaction mixture was diluted with water and evaporated under reduced pressure. After repeating this four times, the residue was taken up in 100 mM NH4HCO3 (5 mL) and the tri-n-octylamine was extracted with diethyl ether (3×5 mL). The aqueous layer was lyophilized to yield the crude product Purification was afforded by size exclusion chromatography through a column of Bio-Gel P2 extra fine resin (1×45 cm) using a Beckman Biosepra ProSys Workstation. The product was eluted with 250 mM NH4HCO3 at a flow rate of 0.1 mL/min. The desired fractions were pooled and lyophilized to yield 13 (90.0 mg, 37%) as a white powdery solid. 1H NMR (D2O, 400 MHz) selected data only: δ 7.91 (d, 1 H, J6,5 6.1 HZ H-6), 5.93 (m, 2 H, H-1′, H5), 5.76 (dd, 1 H J1″,P 7.1, J1″,2 3.6, H-1″). 19F NMR (D2O, 188 MHz): δ-132.4 (dd, J2″,F 49.9, J3″,F 11.1 Hz). 31P NMR (D2O, 81 MHz, proton decoupled): δ-9.10 (d, JPβ,Pα 19.9 Hz, Pβ), −10.8 (d, JPα,Pβ 19.9 Hz, Pα).

[0441] Anal. Calcd. for C15H29FN4O16P2: C, 29.91; H, 4.85; N, 9.30. Found: C, 30.37; H, 5.34; N, 9.89.

[0442] Synthesis of Incompetent Acceptor Substrates:

[0443] 1,2,2′,3,3′,6-Hexa-O-acelyl-4′,6′-O-benzylidene-α-lactose (14)

[0444] To a suspension of lactose (45 g, 124.90 mmol) in DMF (110 mL) was added benzaldehyde dimethyl acetal (20.6 mL, 137.40 mmol) followed by a catalytic amount of p-toluenesulphonic acid (0.47 g, 2.5 mmol). The reaction mixture was then stirred under reduced pressure (20 mm Hg) for 4 d at 60° C. After this time, water (200 mL) was added and unreacted benzaldehyde dimethyl acetal was extracted with EtOAc (2×200 mL). The aqueous layer was evaporated in vacuo following which, pyridine (200 mL) and acetic anhydride (100 mL) were then added to the resulting residue. The reaction mixture was allowed to stir overnight before the volume was decreased by evaporation under reduced pressure. To the remaining residue was added ice water (300 mL) and the crude product was then extracted with CH2Cl2 (2×250 mL). The combined organic layers were washed with 10% v/v HCl (3×200 mL), water (2×200 mL) and brine (1×250 mL), dried over MgSO4 and the solvent was evaporated under reduced pressure. Crystallization from EtOAc/Hexane yielded 14 as a slightly yellowish solid (8 g, 10%). 1H NMR (CDCl3, 200 MHz): δ 7.30-7.55 (m, 5 H, Ar), 6.45 (d, 1 H, J1,2 3.7 Hz, H-1), 5.48 (s, 1 H, PhCH), 5.45 (dd, 1 H, J3,2 10.4, J3,4 9.9 Hz, H-3), 5.35 (dd, 1 H, J2′,3′ 10.3, J2′,1′ 7.9 Hz, H-2′), 5.05 (dd, 1 H, J2,3 10.4, J2,1 3.7 Hz, H-2), 4.87 (dd, 1 H, J3′,2′ 10.3, J3′,4′ 3.5 Hz, H-3′), 4.45 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 4.30-4.55 (m, 1 H, H-5), 4.15-4.45 (m, 2 H, H6a, H-6b), 4.13 (dd, 1 H, J6a′,6b′ 8.2, J6a′,5′ 4.1 Hz, H-6a′), 4.08 (dd, 1 H, J4′,3′ 3.5, J4′,5′ 1.6 Hz, H-4), 3.95-4.05 (m, 2 H, H-5′, H-6b′), 3.80 (dd, 1 H, J4,3 9.9, J4,5 9.3 Hz, H-4), 2.17, 2.11, 2.15, 2.14, 2.00 (s, 18 H, 6×OAc).

[0445] 1,2,2′,3,3′,6-Hexa-O-acetyl-6′-O-benzyl-α-lactose (15)

[0446] 14 (3.5 g, 5.13 mmol) was dissolved in anhydrous THF (120 mL) when sodium cyanoborohydride (3.2 g, 51.27 mmol) was added. A saturated solution of HCl in diethyl ether was then cannulated into the reaction mixture in portions until the evolution of gas had ceased. Within 0.5 h, the reaction was judged to be complete by TLC (PE:EtOAc, 1:1). At this time, the reaction mixture was added to water (100 mL) and the crude product was extracted with CH2Cl2 (2×100 mL). The combined organic layers were washed with aq NaHCO3 (2×100 mL) and water (100 mL), dried over MgSO4 and evaporated in vacuo. Chromatography over silica gel (PE:EtOAc, 4:5) yielded 15 as a white solid (2.66 g, 76%). 1H NMR (CDCl3, 200 MHz) selected data only: δ 7.30-7.45 (m, 5 H, Ar), 6.25 (d, 1 H, J1,2 3.7 Hz, H-1), 5.43 (dd, 1 H, J3,2 10.2, J3,4 9.1 Hz, H-3), 5.19 (dd, 1 H, J2′,3′ 10.1, J2′,1′ 7.8 Hz, H-2′), 5.02 (dd, 1 H, J2,3 10.2, J2,1 3.7 Hz, H-2), 4.89 (dd, 1H, J3′,2′ 10.1, J3′,4′ 3.1 Hz, H-3′), 4.52 (s, 2 H, PhCH2), 4.45 (d, 1 H, J1′,2′ 7.8 Hz, H-1′), 2.15, 2.10, 2.07, 2.04, 2.01,2.00 (s, 18 H, 6×OAc).

[0447] 1,2,2′,3,3′,6-Hexa-O-acetyl-6′-O-benzyl-4′-deoxy-4′-iodo-α-cellobiose (16)

[0448] A stirring solution of 15 (1.32 g, 1.93 mmol) in anhydrous CH2Cl2 (15 mL) under argon was cooled to −20° C. before pyridine (5 mL) and triflic anhydride (0.88 mL, 5.20 mmol) were added The reaction mixture was then warmed to room temperature and stirred for 2 h prior to the addition of aq NaHCO3 (50 mL). The crude material was extracted with CH2Cl2 (2×35 mL) and the combined organic extracts were subsequently washed with water (2×80 mL). Coevaporation of the organic layer with MeCN under reduced pressure yielded a yellow foamy gum, which was then dissolved in anhydrous DMF (25 mL). After the addition of Nal (1.44 g, 9.63 mmol), the reaction mixture was allowed to stir at room temperature overnight under an atmosphere of argon before being added to aq NaHCO3 (100 mL) and extracted with CH2Cl2 (3×125 mL). After the combined organic layers were washed with water (2×75 mL), dried over MgSO4 and evaporated under reduced pressure, the resulting residue was crystallized from EtOAc/Hexane to yield 16 (0.94 g, 62%) as a cotton-like solid. 1H NMR (CDCl3, 200 MHz) selected data only: δ 7.30-7.45 (m, 5 H, Ar), 6.24 (d, 1 H, J1,2 3.7 Hz, H-1), 5.42 (dd, 1 H, J3,2 10.3, J3,4 9.3 Hz, H-3), 5.25 (dd, 1 H, J3′,2′ 9.2, J3′,4′ 11.0 Hz, H-3′), 5.00 (dd, 1 H, J23 10.3, J2,1 3.7 Hz, H-2), 4.78 (dd, 1 H, J2′,3′ 9.2, J2′,1′ 8.1 Hz, H-2′), 4.50 (s, 2 H, PhCH2), 4.48 (d, 1 H, J1′,2′ 8.1 Hz, H-1′), 2.12,2.09,2.06,2.01, 2.00 (s, 18 H, 6×OAc).

[0449] 1,2,2′,3,3′,6-Hexa-O-acetyl-6′-O-benzyl-4′-deoxy-α-lactose (17)

[0450] To a solution of 16 (0.90 g, 1.13 mmol) in anhydrous benzene (30 mL) under argon was added tributyltin hydride (1.65 g, 5.67 mmol) and a catalytic amount of AIBN. The reaction mixture was then refluxed for 45 min after which time the solvent was evaporated in vacuo. The residue was dissolved in MeCN (120 mL) and washed with hexane (3×70 mL). Evaporation of the MeCN layer followed by crystallization from EtOAc/Hexane yielded 17 (0.87 g, 85%) as a white fluffy solid. 1H NMR (CDCl3, 400 MHz): δ 7.25-7.40 (m, S H, Ar), 6.24 (d, 1 H, J1,2 3.7 Hz, H-1), 5.42 (dd, 1 H, J3,2 10.1, J3,4 9.4 H, H-3), 4.99 (dd, 1 H, J23 10.1, J2,1 3.7 HZ, H-2), 4.91 (ddd, 1 H, J3′,4′ax 11.3, J3′,2′ 9.6, J3′,4′eq 5.4 Hz, H-3′), 4.80 (dd, 1 H, J2′,3′ 9.6, J2′,1′ 7.8 Hz, H-1′), 4.50 (s, 2 H, PhCH2), 4.43 (dd, 1 H, J6a,6b 12.2, J6a,5 2.0 Hz, H-6a), 4.36 (d, 1 H, J1′,2+ 7.8 Hz, H-1′), 4.12 (dd, 1 H, J6b,6a 12.2, J6b,5 4.3 Hz, H-6b), 3.97 (ddd, 1 H, J5,4 10.1, J5,6b 4.3, J5,6a 2.0 Hz, H-5), 3.78 (dd, 1 H, J4,5 10.1, J4,3 9.4 Hz, H-4), 3.60-3.67 (m, 1 H, H-5′), 3.56 (dd, 1 H, J6a′,6b′ 9.8, J6a′,5′ 5.3 Hz, H-6a′), 3.45 (dd, 1 H, J6b′,6a′ 9.8, J6b′,5′ 4.8 Hz, H-6b′), 2.14, 2.08, 2.01, 1.98 (s, 18 H, 6×OAc), 2.00-2.10 (m, 1 H, H4′eq), 1.50-1.64 (m, 1 H, H-4′ax).

[0451] 1,2,2′,3,3′,6-Hexa-O-acetyl-4′-deoxy-α-lactose (18)

[0452] 17 (0.23 g, 0.34 mmol) was dissolved in EtOH (4 mL) when cyclohexene (1.39 mL, 13.76 mmol) and 20% Pd(OH)2/C (0.06 g) were added and the reaction mixture was refluxed. After 2 h, the catalyst was removed by filtration through Celite® and the filtrate was evaporated in vacuo. Crystallization from EtOH yielded 18 (0.13 g, 63%) as a white fluffy solid. 1H NMR (CDCl3, 400 MHz): δ 6.24 (d, 1 H, J1,2 3.7 Hz, H-1), 5.45 (dd, 1 H, J3,2 10.0, J3,4 9.2 Hz, H-3), 5.01 (dd, 1 H, J2,3 10.0, J2,1 3.8 Hz, H-2), 4.94 (ddd, 1 H, J3′,4′ax 11.5, J3′,2′ 9.5, J3′,4′eq 5.4 Hz, H-3′), 4.81 (dd, 1 H, J2′,3′ 9.5, J2′,1′ 7.7 Hz, H-2′), 4.47 (d, 1 H, J1′,2′ 7.7 Hz, H-1′), 4.44 (dd, 1 H, J6a,6b 12.5, J6a,5 2.0 Hz, H-6a), 4.08 (dd, 1 H, J6b,6a 12.5, J6b,5 4.5 Hz, H-6b), 4.00 (ddd, 1 H, J5,4 10.0, J5,6b 4.5, J5,6a 2.0 Hz, H-5), 3.83 (dd, 1 H, J4,5 10.0, J4,3 9.2 Hz, H-4), 3.52-3.68 (m, 3 H, H-5′, H-6a′, H-6b′), 2.15, 2.08, 2.06, 2.04, 1.98, 1.97 (s, 18 H, 6×OAc), 2.00-2.10 (m, 1 H, H-4′eq), 1.50-1.64 (m, 1 H, H-4′ax).

[0453] 4′-Deoxylactose (19)

[0454] To a stirring solution of 18 (0.50 g, 0.87 mmol) in anhydrous MeOH (8 mL) under argon was added a catalytic amount of sodium methoxide until the solution was slightly basic. The reaction mixture was allowed to stir at room temperature overnight prior to being neutralized with Amberlyte® IR-120 acidic resin. After filtration, evaporation of the solvent under reduced pressure yielded 19 (0.24 g, 85%) as a white solid. 1H NMR (D2O, 400 MHz) selected data only for β anomer: δ 4.63 (d, 1 H, J1,2 8.0 Hz, H-1), 4.40 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 3.22-3.29 (m, 1 H, H-5), 3.19 (ddd, 1 H, J5′,4′ax 11.2, J5′,6a′ 8.0, J5′,6b′ 3.2 Hz, H-5′), 1.95 (dd, 1 H, J4′eq,4′ax 12.0, J4′eq,3′ 4.4 Hz, H-4′eq), 1.42 (ddd, 1 H, J4′ax,4′eq 12.0, J4′ax,3′ 11.9, J4′ax,5′ 11.2 Hz, H-4′ax).

[0455] Anal. Calcd. for C12H22O10: C, 44.17; H, 6.80. Found: C, 43.87; H, 6.91.

[0456] 2,2′,3,3′,4′,6,6′-Hepta-O-acetyl-α-cellobiosyl Bromide (20)

[0457] A solution of octa-O-acetylcellobiose (10.95 g, 16.10 mmol) in anhydrous CH2Cl2 (35 mL) under an atmosphere of nitrogen was cooled to 0° C. prior to the addition of 45% w/v HBr/AcOH (13 mL). The reaction vessel was then sealed and the reaction mixture was allowed to warm to room temperature. After 4 h, the reaction mixture was diluted with CH2Cl2 (100 mL) and the solution was added to ice water (200 mL) whereupon it was neutralized with solid NaHCO3. Upon separation of the two phases, the aqueous layer was further extracted with CH2Cl2 (2×100 mL) and the combined organic extracts were washed with aq. NaHCO3 (2×75 mL), water (75 mL) and brine (75 mL). Removal of the solvent under reduced pressure after drying over MgSO4 yielded 20 as a white solid (11.12 g, 99%). 1H NMR (CDCl3, 400 MH): δ 6.50 (d, 1 H, J1,2 4.1 Hz, H-1), 5.50 (dd, 1 H, J3,2 9.7, J3,4 9.7 Hz, H-3), 5.13 (dd, 1 H, J3′,4′ 9.3, J3′,2′ 9.2 Hz, H-3′), 5.05 (dd, 1 H, J4′,5′ 9.7, J4′,3′ 9.3 Hz, H-4′), 4.91 (dd, 1 H, J6a′,6b′ 12.5, J6a′,5′ 4.5 Hz, H-6a′), 4.11-4.23 (m, 2 H, H-5, H-6b), 4.03 (dd, 1 H, J6b′,6a′ 12.5, J6b′,5′ 2.3 Hz, H-6b′), 3.81 (dd, 1 H, J4,3 9.7, J4,5 9.7 Hz, H-4), 3.65 (ddd, 1 H, J5′,4′ 9.7, J5′,6a′ 4.5, J5′,6b′ 2.3 Hz, H-5′), 2.11, 2.06, 2.01, 2.00, 1.98, 1.96 (s,21 H, 7×OAc).

[0458] Benzyl 2,2′,3,3′,4′,6,6′-hepta-O-acetyl-β-cellobioside (21)

[0459] To a solution of 20 (9.99 g, 14.29 mmol) in anhydrous CH2Cl2 (100 mL) containing 4 Å molecular sieves under an atmosphere of nitrogen was added benzyl alcohol (7.39 mL, 71.44 mmol) and silver carbonate (7.88 g, 28.58 mmol). A crystal of iodine was added and the reaction vessel was shielded from the light and stirred at room temperature overnight After this time, the reaction mixture was filtered through Celite® and washed with CH2Cl2. The solvent was then evaporated in vacuo and the residue was crystallized from EtOAc/Hex to yield 21 (6.91 g, 66%) as a white fluffy solid. 1H NMR (CDCl3, 400 MHz): δ 7.20-7.35 (m, 5 H, Ar), 5.11 (dd, 2 H, J3,2/3′,2′ 9.3, J3,4/3′,4′ 9.3 Hz, H-3, H-3′), 5.03 (dd, 1 H, J4′,5′ 9.8, J4′,3′ 9.3 Hz, H-4′), 4.94 (dd, 1 H, J2′,3′ 9.6, J2′,1′ 7.9 Hz, H-2′), 4.89 (dd, 1 H, J2,3 9.3, J2,1 8.0 Hz, H-2), 4.83 (d, 1 H, J 12.3 Hz, PhCH). 4.56 (d, 1 H, J 12.3 Hz, PhCH), 4.51 (dd, 1 H, J6a,6b 12.0, J6a,5 2.0 Hz, H-6a), 4.49 (d, 1 H, J1,2 8.0 Hz, H-1), 4.48 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 4.33 (dd, 1 H, J6a′,6b′ 12.5, J6a′,5′ 4.5 Hz, H-6a′), 4.08 (dd, 1 H, J6b,6a 12.0, J6b,5 5.0 Hz, H-6b), 4.01 (dd, 1 H, J6b′,6a′ 12.5, J6b′,5′ 2.3 Hz, H-6b′), 3.77 (dd, 1 H, J4,5 9.6, J4,3 9.3 Hz, H-4), 3.63 (ddd, 1 H, J5′,4′ 9.8, J5′,6b′ 4.5, J5′,6b′ 2.3 Hz, H-S′), 3.54 (ddd, 1 H, J5,4 9.6, J5,6b 5.0, J5,6a 2.0 Hz, H-5), 2.12, 2.05, 2.00, 1.98, 1.97, 1.95 (s, 21 H, 7×OAc).

[0460] Benzyl β-cellobioside (22)

[0461] 21 (6.33 g, 8.71 mmol) was suspended in anhydrous MeOH under nitrogen when a catalytic amount of sodium methoxide was added until a basic pH was obtained. After 24 h, the reaction mixture was neutralized with acidic Amberlyte® resin. Removal of the solvent under reduced pressure yielded 22 (3.91, g) quantitatively as a white solid. 1H NMR (D2O, 400 MHz) selected data only: δ 7.35-7.50 (m, 5 H, Ar), 4.90 (d, 1H, J 11.6 Hz, PhCH), 4.75 (d, 1 H, J 11.6 Hz, PhCH), 4.56 (d, 1 H, J1,2 8.0 Hz, H-1), 4.47 (d, 1 H, J1′,2′ 7.8 Hz, H-1′), 3.96 (dd, 1 H, J6a,6b 12.1, J6a,5 2.0 Hz, H-6a), 3.88 (dd, 1 H, J6a′,6b′ 12.6, J6′,5′ 2.2 Hz, H-6a′), 3.79 (dd, 1 H, J6b,6a 12.1, J6b,5 5.0 Hz H-6b), 3.70 (dd, 1 H, J6b′,6a′ 12.6, J6′,5′ 5.6 Hz, H-6b′).

[0462] Benzyl 2,2′,3,3′,6-penta-O-acetyl-4′,6′-O-p-methoxybenzylidene-β-cellobioside (23)

[0463] To a suspension of 22 (3.64 g, 8.42 mmol) in DMF (100 mL) was added p-anisaldehyde dimethyl acetal (1.72 mL, 10.10 mmol) followed by a catalytic amount of toluenesulphonic acid (0.03 g, 0.17 mmol). The reaction mixture was then stirred under reduced pressure (20 mm Hg) for 10 d at 60° C. After this time, solid NaHCO3 was added to neutralize the reaction and the solvent was evaporated in vacuo. To the resulting residue was added pyridine (30 mL) and acetic anhydride (15 mL) and the mixture was stirred overnight. The volume of pyridine and acetic anhydride was then decreased by evaporation under reduced pressure and the resulting syrup was taken up in 10% v/v HCl and extracted with CH2Cl2 (3×80 mL). The combined organic extracts were washed with 10% v/v HCl (2×50 mL), aq. NaHCO3 (50 mL) and water (50 mL), dried over MgSO4 and the solvent was evaporated in vacuo. The residue was crystallized from EtOAc/Hexanes to yield 23 (3.72 g, 58%) as a white solid. 1H NMR (CDCl3, 400 MHz): δ 7.20-7.35 (m, 7 H. Ar), 6.80-6.90 (m, 2 H, Ar), 5.40 (s, 1 H, MeOPhCH), 5.22 (dd, 1 H, J3,2 9.4, J3,4 9.3 Hz, H-3), 5.11 (dd, 1 H, J3′,4′ 9.3, J3′,2′ 9.2 Hz, H-3′), 4.94 (dd, 1 H, J2,3 7.9 Hz, H-2), 4.88 (dd, 1 H, J2′,3′ 9.2, J2′,1′ 7.8 Hz, H-2′), 4.84 (d, 1 H, J 12.3 Hz, PhCH), 4.57 (d, 1 H, J1,2 7.9 Hz, H-1), 4.56 (d, 1 H, J 12.3 Hz, PhCH), 4.50 (dd, 1 H, J6a,6b 11.9, J6a,5 1.9 Hz, H-6a), 4.49 (d, 1 H, J1′,2′ 7.8 Hz, H-1′), 4.31 (dd, 1 H, J4′,3′ 9.3, J4′,5′ 4.9 Hz, H-4′), 4.07 (dd, 1 H, J6b,6a 11.9, J6b,6a 4.7 Hz, H-6b), 3.75-3.90 (m, 4 H, H-4, OCH3), 3.66 (dd, 1 H, J6a′,6b′ 10.2, J6a′,5′ 9.6 Hz, H-6a′), 3.64 (dd, 1 H, J6b′,6a′ 10.2, J6b′,5′ 9.3 Hz, H-6b′), 3.53 (ddd, 1 H, J5,4 9.8, J5,6b 4.7, J5,6a 1.9 Hz, H-5), 3.43 (ddd, 1 H, J5′,6a′ 9.6, J5′,6b′ 9.3, J5′,4′4.9 Hz, H-5′), 2.12, 2.03, 2.00, 1.99, 1.97 (s, 15 H, 5×OAc).

[0464] Benzyl 2,2′,3,3′,6-penta-O-acetyl-6′-O-p-methoxybenzyl-β-cellobioside (24)

[0465] 23 (1.17 g, 1.54 mmol) was dissolved in anhydrous DMF (12 mL) when NaCNBH3 (0.49 g, 7.72 mmol) was added. A solution of TFA (1.20 mL, 15.43 mmol) in anhydrous DMF (8 mL) was then added dropwise to the reaction mixture and the solution was allowed to stir at room temperature overnight. The reaction mixture was then filtered through Celite® and washed with CH2Cl2. The filtrate was added to aq NaHCO3 (100 mL) and extracted with additional portions of CH2Cl2 (3×75 mL). The combined organic extracts were then washed with aq NaHCO3 (100 mL), water (2×100 mL) and brine (100 mL), dried over MgSO4 and the solvent was removed under reduced pressure. Chromatography over silica gel (PE:EtOAc, 1:1) afforded 24 (0.85 g, 72%) as a white solid. 1H NMR (CDCl3, 400 MHz): δ 7.15-7.35 (m, 7 H, Ar), 6.80-6.90 (m, 2 H, Ar), 5.09 (dd, 1 H, J3,2 9.3, J3,4 9.2 Hz, H-3), 4.95 (dd, 1 H, J3′,2′ 9.4, J3′,4′ 9.3 Hz, H-3′), 4.93 (dd, 1 H, J2,3 9.3, J2,1 7.9 Hz, H-2), 4.82 (d, 1 H, J 12.3 Hz, PhCH), 4.80 (dd, 1 H, J2′,3′ 9.4, J2′,1′ 7.9 Hz, H-2′), 4.55 (d, 1 H, J 12.3 Hz, PhCH), 4.50 (dd, 1 H, J6a,6b 12.0, J6a,5 2.0 Hz, H-6a), 4.47 (d, 1 H, J 11.2 Hz, MeOPhCH), 4.46 (d, 1 H, J1,2 7.9 Hz, H-1), 4.44 (d, 1 H, J1′,2′ 7.9 Hz, H-1′), 4.41 (d, 1 H, J 11.2 Hz, MeOPhCH), 4.06 (dd, 1 H, J6b,6a 12.0, J6b,5 5.0 Hz, H-6b), 3.67-3.76 (m, 3 H, H-4, H-4′, H-6a′), 3.64 (dd, 1 H, J6b′,6a′ 9.9, J6b′,5′ 4.8 Hz, H-6b′), 3.52 (ddd, 1 H, J5,4 9.8, J5,6b 5.0, J5,6a 2.0 Hz, H-5), 3.39-3.45 (m, 1 H, H-5′), 2.10, 2.03, 2.00, 1.97, 1.94 (s, 15 H, 5×OAc).

[0466] Benzyl 2,2′,3,3′,6-penta-O-acetyl-4′-deoxy-4′-fluoro-β-lactoside (25)

[0467] A solution of 24 (0.11 g, 0.15 mmol) in anhydrous CH2Cl2 (5 mL) under an atmosphere of argon was cooled to −20° C. before trilic anhydride (66.4 μL, 0.40 mmol) was added dropwise to the solution. The reaction mixture was stirred at room temperature for 1 h and was then diluted with 10% v/v HCl (20 mL). The mixture was extracted with CH2Cl2 (3×20 mL) and the combined organic layers were washed with an additional portion of 10% v/v HCl (20 mL), water (2×20 mL) and brine. After drying over MgSO4, the solvent was evaporated under reduced pressure. The resulting residue was then dissolved in anhydrous CH2Cl2 and the solution was cooled to −10° C. prior to the addition of tris(dimethylamino)sulfur (trimethylsilyl)difluoride (0.12 g, 0.44 mmol). The reaction was then refluxed for 0.5 h after which time water (20 mL) was added and the reaction was extracted with CH2Cl2 (3×20 mL). The combined organic extracts were washed with water (2×20 mL), dried over MgSO4 and the solvent was removed in vacua. Chromatography over silica gel (PE:EtOAc, 2:3) yielded 25 (40.3 mg, 43%) as a white solid. 1H NMR (CDCl3, 500 MHz): δ 7.25-7.35 (m, 5 H, Ar), 5.15 (dd, 1 H, J2′,3′ 10.3, J2′,1′ 8.0 Hz, H-2′), 5.12 (dd, 1 H, J3,2 9.2, J3,4 9.2 Hz, H-3), 4.96 (dd, 1 H, J2,s 9.2, J2,1 7.8 Hz, H-2), 4.89 (ddd, 1 H, J3′,F 27.6, J3′,2′ 10.4, J3′,4′ 2.7 Hz, H-3′), 4.84 (d, 1 H, J 12.1 Hz, PhCH), 4.80 (dd, 1 H, J4′,F 50.3, J4′,3′ 2.7 Hz, H4′), 4.57 (d, 1 H, J12.3 Hz, PhCH), 4.52 (d, 1H, J1′,2′ 7.4 Hz, H-1′), 4.51 (dd, 1 H, J6a,6b 11.9, J6a,5 2.2 Hz, H-6a), 4.49 (d, 1 H, J1,2 7.8 Hz, H-1), 4.07 (dd, 1 H, J6b,6a 11.9, J6b,5 5.2 Hz, H-6b), 3.87 (ddd, 1 H, J6a′,6b′ 11.5, J6a′,5′ 7.5, J6a′,F 1.0 Hz, H-6a′), 3.85 (dd, 1 H, J4,3 9.2, J4,5 9.3 Hz, H4), 3.72 (dd, 1 H, J6b′,6a′ 11.5, J6b′,5′ 4.9 Hz, H-6b′), 3.61 (ddd, 1 H, J5′,F 26.4, J5,6a′7.5, J5′,6b′ 4.9 Hz, H-5′),. 3.55-3.59 (m, 1 H, H-5), 2.11, 2.06, 2.04, 2.03, 1.98 (s, 15 H, 5×OAc). 19F NMR (CDCl3, 188 MHz): δ-140.0 (ddd, JF,4′ 50.3, JF,3′ 27.6, JF,5′ 26.4 Hz).

[0468] Anal. Calcd. for C29H37FO: C, 54.04; H, 5.79. Found: C, 54.32; H,5.78.

[0469] Benzyl 4′-deoxy-4′-fluoro-β-lactoside (26)

[0470] A solution of 25 (0.09 g, 0.14 mmol) in anhydrous MeOH (5 mL) under argon was made basic through the addition of a catalytic amount of sodium methoxide. The reaction mixture was stirred at room temperature overnight before it was neutralized with acidic Amberlyte® resin. Removal of the resin by filtration followed by evaporation of the solvent in vacuo gave a quantitative yield of 26 (60 mg) as a white solid. 1H NMR (D2O, 400 MHz) selected data only: δ 7.35-7.55 (m, 5 H, Ar), 4.91 (d, 1 H, J 11.6 Hz, PhCH), 4.54 (d, 1 H, J1′,2′ 7.8 Hz, H-1′), 4.51 (d, 1 H, J1,2 6.0 Hz, H-1), 3.98 (dd, 1 H, J6a,6b 12.3, J6a,5 1.9 Hz, H-6a), 3.33 (dd, 1 H, J4,3 8.6, J4,5 8.4 Hz, H4). 19F NMR (D2O, 188 MHz): δ-141.2 (ddd, JF,4′ 51.0, JF,3′ 30.0, JF,5′ 30.0 Hz).

[0471] Anal. Calcd. for C19H27FO10: C, 52.53; H, 6.26. Found: C, 52.33; H, 6.31.

[0472] Benzyl 2,2′,3,3′,6-penta-O-acetyl-4′-deoxy-4′-iodo-6′-O-p-methoxybenzyl-β-lactoside (27)

[0473] To a stirred solution of 24 (1.22 g, 1.60 mmol) in anhydrous CH2Cl2 (20 mL) under argon at −20° C. was added pyridine (1.1 mL, 13.47 mmol) followed by triflic anhydride (0.73 mL, 4.33 mmol). After 5 min, the reaction mixture was allowed to warm to room temperature and then was stirred at this temperature for an additional hour. After dilution with 10% v/v HCl (65 mL), the reaction was then extracted with CH2Cl2 (3×65 mL). The combined organic extracts were washed with 10% v/v HCl (65 mL), water (65 mL) and brine (65 mL), dried over MgSO4 and the solvent was evaporated under reduced pressure. The residue was dissolved in anhydrous DMF (20 mL), Nal (1.20 g, 8.02 mmol) was added and the reaction mixture was stirred at room temperature overnight. After diluting with water (75 mL) and extracting with CH2Cl2 (3×75 mL), the combined organic layers were then washed with water (4×75 mL) and brine (75 mL), dried over MgSO4 and the solvent was evaporated in vacuo. The residue was chromatographed over silica gel (PE:EtOAc, 3:2) and the desired fractions were pooled and recrystallized from EtOAc/Hex to yield 27 (0.54 g, 38%) as a white solid. 1H NMR (CDCl3, 400 MHz): δ 7.20-7.35 (m, 7 H, Ar), 6.85-6.90 (m, 2 H, Ar), 5.15 (dd, 1 H, J2′,3′ 9.9, J2′,1′ 7.8 Hz, H-2′), 5.10 (dd, 1 H, J3,2 9.5, J3,4 9.3 Hz, H-3), 4.95 (dd, 1 H, J2,3 9.5, J2,1 7.9 Hz, H-2), 4.83 (d, 1 H, J 12.3 Hz, PhCH), 4.64 (dd, 1 H, J4′,3′ 4.2, J4′,5′ 1.1 Hz, H-4′), 4.56 (d, 1 H, J 12.3 Hz, PhCH), 4.47 (d, 1 H, J1′,2′ 7.8 Hz, H-1′), 4.43-4.49 (m, 2 H, MeOPhCH2), 4.43 (d, 1 H, J1,2 7.9 Hz, H-1), 4.43 (dd, 1 H, J6a,6b 11.9, J6a,5 2.0 Hz, H-6a), 4.25 (dd, 1 H, J3′,2′ 9.9, J3′,4′ 4.2 Hz, H-3′), 4.05 (dd, 1 H, J6b,6a 11.9, J6b,5 5.0 Hz, H-6b), 3.72-3.80 (m, 4 H, H-4, OCH3), 3.62 (dd, 1 H, J6a′,6b′ 9.4, J6a′,5′ 5.5 Hz, H-6a′), 3.53 (ddd, 1 H, J5,4 9.9, J5,6b 5.0, J5,6a 2.0 Hz, H-5), 3.45 (dd, 1 H, J6b′,6a′ 9.4, J6b′,5′ 7.0 Hz, H-6b′), 2.91 (ddd, 1 H, J5′,6b′ 7.0, J5′,6a′ 5.5, J5′,4′ 1.1 Hz, H-5′), 2.09, 2.05, 2.01, 1.98, 1.97 (s, 15 H, 5×OAc).

[0474] Benzyl 2,2′,3,3′,6-penta-O-acetyl-4′-deoxy-6′-O-p-methoxybenzyl-,β-lactoside (28)

[0475] 27 (0.50 g, 0.57 mmol) was dissolved in anhydrous benzene (15 mL), then tributyltin hydride (0.83 g, 2.87 mmol) and a catalytic amount of AIBN were added and the reaction mixture was refluxed under an atmosphere of argon. After 7 h, hexane (60 mL) was added and the reaction mixture was extracted with acetonitrile (80 mL). The acetonitrile layers were washed with two additional portions of hexane (60 mL) before the solvent was evaporated under reduced pressure. Chromatography over silica gel (PE:EtOAc, 2:1 to 3:2) yielded 28 (0.36 g, 84%) as a colourless gum. 1H NMR (CDCl3, 400 MHz): δ 7.15-7.35 (m, 7 H, Ar), 6.84-6.89 (m, 2 H, Ar), 5.11 (dd, 1 H, J3,2 9.4, J3,4 9.2 Hz, H-3), 4.94 (dd, 1 H, J2,3 9.4, J2,1 7.9 Hz, H-2), 4.89 (ddd, 1 H, J3′,4′ax 11.5, J3′,2′ 9.7, J3′,4′eq 5.4 Hz, H-3′), 4.82 (d, 1 H, J 12.3 Hz, PhCH), 4.76 (dd, 1 H, J2′,3′ 9.7, J2′,1′ 7.8 Hz, H-2′), 4.55 (d, 1 H, J 12.3 Hz, PhCH), 4.49 (dd, 1 H, J6a,6b 12.0, J6a,5 2.0 Hz, H-6a), 4.47 (d, 1 H, J1,2 7.9 Hz, H-1), 4.41 (s, 2 H, MeOPhCH2), 4.35 (d, 1 H, J1′,2′ 7.8 Hz, H-1′), 4.10 (dd, 1 H, J6b,6a 12.0, J6b,5 4.9 Hz, H-6b), 3.73-3.80 (m, 4 H, H-4, OCH3), 3.51-3.64 (m, 2 H, H-5, H-5′), 3.51 (dd, 1 H, J6a′,6b′ 9.8, J6a′,5′ 5.1 Hz, H-6a′), 3.40 (dd, 1 H, J6b′,6a′ 9.8, J6b′,5′ 5.0 Hz, H-6b′), 2.09,2.01, 1.97, 1.95 (s, 15 H, 5×OAc), 1.47-1.63 (m, 2 H, H-4′ax, H-4′eq).

[0476] Benzyl 2,2′,3,3′,6-penta-O-acetyl-4′-deoxy-β-lactoside (29)

[0477] Ceric ammonium nitrate (0.55 g, 1.00 mmol) was added to a solution of 28 (0.34 g, 0.46 mmol) in 9:1 acetonitrile/water (4 mL) and the reaction mixture was stirred at room temperature for 6 h before being added to aq. NaHCO3 (15 mL) and extracted with CH2Cl2 (3×15 mL). The combined organic extracts were washed with aq. NaHCO3 (15 mL), water (15 mL) and brine (15 mL), dried over MgSO4 and the solvent was evaporated under reduced pressure. The resulting residue was crystallized from EtOAc/Hex to yield 29 (232 mg, 81%) as a white needle-like solid. 1H NMR (CDCl3, 400 MHz): δ 7.20-7.35 (m, 5 H, Ar), 5.14 (dd, 1 H, J3,2 92, J3,4 9.1 Hz, H-3), 4.94 (dd, 1H, J2,3 9.2, J2,1 7.8 Hz, H-2), 4.88-4.96 (m, 1 H, H-3′), 4.83 (d, 1 H, J 12.3 Hz, PhCH), 4.78 (dd, 1 H, J2′,3′ 9.4, J2′,1′ 7.7 Hz, H-2′), 4.57 (d, 1 H, J 12.3 Hz, PhCH), 4.51 (dd, 1 H, J6a,6b 11.8, J6a,5 2.1 Hz, H-6a), 4.49 (d, 1 H, J1,2 7.8 Hz, H -1), 4.46 (d, 1 H, J1′,2′ 7.7 Hz, H-1′), 4.08 (dd, 1 H, J6b,6a 11.8, J6b,5 5.3 Hz, H-6b), 3.82 (dd, 1 H, J4,5 9.5, J4,3 9.1 Hz, H-4), 3.51-3.64 (m, 4 H, H-5, H-5′, H-6a′, H-6b′), 2.11, 2.04, 2.03, 1.98, 1.97 (s, 15 H, 5×OAc), 1.46-1.60 (m, 2 H, H-4′ax, H-4′eq).

[0478] Anal. Calcd. for C29H38O15: C, 55.59; H, 6.11. Found: C, 55.91; H, 6.16.

[0479] Benzyl 4′-deoxy-β-lactoside (30)

[0480] A solution of 29 (0.21 g, 0.33 mmol) in anhydrous MeOH (10 mL) under argon was made basic through the addition of a catalytic amount of sodium methoxide. The reaction mixture was stirred at room temperature overnight before it was neutralized with acidic Amberlyte® resin. Removal of the resin by filtration followed by evaporation of the solvent in vacuo gave a quantitative yield of 30 (147 mg) as a white solid. m.p 169-171° C. 1H NMR (CD3OD, 400 MHz) selected data only: δ 7.22-7.45 (m, 5 H, Ar), 4.91 (d, 1H, J 11.8 Hz, PhCH), 4.66 (d, 1 H, J 11.8 Hz, PhCH), 4.39 (d, 1 H, J1,2 7.8 Hz, H-1), 4.34 (d, 1 H, J1′,2′ 7.8 Hz, H-1′), 3.93 (dd, 1 H, J6a,6b 12.1, J6a,5 2.4 Hz, H-6a), 3.86 (dd, 1 H, J6b,6a 12.1, J6b,5 4.2 Hz, H-6b), 3.13 (dd, 1 H, J4,5 8.7, J4,3 8.1 Hz, H4), 1.89 (dd, 1 H, J4′eq,4′ax 12.7, J4′eq,3′ 5.0 Hz, H-4′eq), 1.41 (ddd, 1 H, J4′ax,4′eq 12.7, J4′ax,3′ 11.9, J4′ax,5′ 11.9 Hz, H-4′ax).

[0481] Anal. Calcd. for C19H28O10: C, 54.80; H, 6.78. Found: C, 54.50; H, 6.72.

[0482] Synthesis of 18O-UDPGal:

[0483] Diphenyl (2,3,4,6-tetra-O-acetyl)-[1-18O]-α-D-galactopyranosyl Phosphate (31)

[0484] To a solution of 2,3,4,6-tetra-O-acetyl-D-galactose (0.49 g, 1.41 mmol) in anhydrous acetonitrile (2 mL) in a thick walled bomb was added 97% 18O-enriched water (0.5 mL). A few beads of Amberlyte® IR-120 acidic resin were added and the chamber was flooded with argon and sealed. The reaction mixture was then heated to 105° C. for 24 h. After this time, the solvent was removed in vacuo and the residue was chromatographed over silica gel (PE:EtOAc, 3:2 to 1:1). This 1-18O-labeled 2,3,4,6-tetra-O-acetyl-D-galactopyranose along with DMAP (025 g, 2.03 mmol) were then dissolved in anhydrous CH2Cl2 and stirred at room temperature for 20 min under an atmosphere of argon. Diphenyl chlorophosphate (0.54 g, 2.03 mmol) was then added to the reaction mixture and stirring was continued for 3 h, when it was then added to a 10% v/v solution of HCl (40 mL) and extracted with CH2Cl2 (3×40 mL). The combined organic extracts were washed with aq. NaHCO3 (35 mL) and water (3×35 mL), dried over MgSO4 and the solvent was evaporated under reduced pressure. Chromatography over silica gel (PE:EtOAc, 12:7 to 3:2) yielded 31 (316.1 mg, 39%) as a colourless gum. 1HNMR(CDCl3, 400 MHz): δ 7.15-7.45 (m, 10 H, Ar), 6.10 (dd, 1 H, J1,F 6.4, J1,2 3.3 Hz, H-1), 5.47 (dd, 1 H, J4,3 3.1, J4,5 1.1 Hz, H-4), 5.37 (dd, 1 H, J3,2 10.9, J3,4 3.1 Hz, H-3), 5.23 (ddd, 1 H J2,3 10.9, J2,1 3.3, J2,P 3.0 Hz, H-2), 4.32 (ddd, 1 H, J5,6a 6.6, J5,6b 6.5, J5,4 1.1 Hz, H-5), 4.06 (dd, 1 H, J6a,6b 11.3, J6a,5 6.6 Hz, H-6a), 3.91 (dd, 1 H, J6b,6a 11.3, J6b,5 6.5 Hz, H-6b), 2.12, 1.97, 1.90, 1.83 (s, 12 H, 4×OAc). 31P NMR (CDCl3, 81 MHz, proton decoupled): δ-13.70. LR-LSIMS: calcd. for C26H29O13P: 581. Found: 581 (C26H2916O13P), 583 (C26H2916O1218OP), 16O /18O=20/80.

[0485] α-D-Galactopyranosyl-[1-18O]-phosphate Monopyridinium Salt (32)

[0486] 31 (0.31 g, 0.54 mmol) was dissolved in 1:1 EtOAc:MeOH (6 mL) when PtO2 (0.10 g) was added and the reaction mixture was hydrogenated at 6 atm. After 2 d, this mixture was filtered through Celite® and chromatographed over silica gel (EtOAc to EtOAc:MeOH:H2O, 27:2:1 to 7:2:1). The desired fractions were pooled, concentrated and redissolved in THF (1 mL). To this was then added 2 M LiOH (2 mL) and the reaction mixture was allowed to stir at room temperature overnight. The reaction volume was then reduced and eluted through a Bio-Rad® AG 50W-X2, 200-400 mesh sulfonic acid cation exchange column (pyridinium form). The desired fractions were pooled and lyophilized to yield 32 (126 mg, 69%) as a white fluffy solid 1H NMR (D2O, 300 MHz): δ 7.90-8.70 (m, 5 H, pyridine), 5.40 (dd, 1 H, J1,P 7.0, J3,2 3.5 Hz, H-1), 4.00 (dd, 1 H, J5,6a 6.3, J5,6b 6.3 Hz, H-5), 3.88 (d, 1 H, J4,3 2.9 Hz, H-4), 3.77 (dd, 1 H, J3,2 10.3, J3,4 2.9 Hz, H-3), 3.68 (ddd, 1 H, J2,3 10.3, J2,1 3.5, J2,P 3.0 Hz, H-2), 3.53-3.63 (m, 2 H, H-6a, H-6b). 31P NMR (D2O, 121 MHz, proton decoupled): δ 0.09. LR-LSIMS: calcd for C6H12O9P-: 259. Found: 259 (C6H1216O9P−), 261 (C6H1216O818OP−), 16O/18O=17/83.

[0487] Uridine 5′-diphospho-[1″-18O-α-D-galactopyranose, Diammonium Salt (33)

[0488] To a solution of 32 (0.08 g, 0.24 mmol) in water (1.5 mL) was added tri-n-octylamine (0.10 mL, 0.24 mmol) and the mixture was lyophilized. The resulting residue along with UMP-morpholidate (0.18 g, 0.26 mmol) was dried over P2O5 overnight. The two reagents were then dissolved in anhydrous pyridine (2.5 mL) and the reaction mixture was stirred at room temperature in the presence of 4 Å molecular sieves under an argon atmosphere. An aliquot of the reaction mixture was transferred into an NMR tube containing a capillary of DMSO-d6 so that the reaction progress can be monitored by 31P NMR. After 11 d, the mixture was filtered and the filtrate was added to 50 mM NH4HCO3. The tri-n-octylamine was extracted with Et2O (3×15 mL) and the aqueous phase was lyophilized to yield the crude product. Purification was afforded by anion exchange chromatography on a DEAE Sephacel column (26 mm×12.5 cm, 50-500 mM NH4HCO3, 1.5 mL/min) followed by size exclusion chromatography on a Bio-Gel P2, extra fine column (16 mm×55 cm, 50 mM NH4HCO3, 0.15 mL/min) using a Beckman Biosepra ProSys Workstation. The desired fractions were pooled and lyophilized to yield 33 (25 mg, 18%) as a white powder. 1H NMR (D2O, 300 MHz): δ 7.83 (d, 1 H, J6,5 8.2 Hz, H-6), 5.30-5.40 (m, 2 H, H-5, H-1′), 5.53 (dd, 1 H, J1″,P 7.2, J1″,2″ 3.6 Hz, H-1″), 4.23-4.28 (m, 2 H, H-2′, H-3′), 4.07-4.20 (m, 3 H, H4′, H-5a′, H-5b′), 4.06 (dd, 1 H, J5″,6a″ 6.2, J5″, 6b″ 6.2 Hz, H-5″), 3.92 (d, 1 H, J4″,3″ 3.0 Hz, H-4″), 3.80 (dd, 1 H, J3″,2″ 10.2, J3″,4″ 3.0 Hz, H-3″), 3.68 (ddd, 1 H, J2″,3″ 10.2, J2″,1″ 3.6, J2″,P 3.0 Hz, H-2″), 3.55-3.65 (m, 2 H, H-6a″, H-6b″). 31P NMR (D2O, 121 MHz, proton decoupled): δ-9.95 (d, 1P, JPβ,Pα 20.1 Hz, Pβ), -11.51 (d, 1P, JPα,Pβ 20.7 Hz, Pα). HR-LSIMS: calcd. for C15H23N216O1618OP2−: 567.0513. Found 567.0515. LR-LSIMS: 16O/18O=15/85.

[0489] Anal. Calcd. for C15H22N216O1618OP22−.2NH4+: C, 29.86; H, 5.18; N, 9.29. Found: C, 30.21; H, 5.16; N, 8.97.

[0490] All publications mentioned in the above specification are herein incorporated by reference. Various modifications and variations of the described methods and system of the invention will be apparent to those skilled in the art without departing from the scope and spirit of the invention. Although the invention has been described in connection with specific preferred embodiments, it should be understood that the invention as claimed should not be unduly limited to such specific embodiments. Indeed, various modifications of the described modes for carrying out the invention which are obvious to those skilled in chemistry, biology or related fields are intended to be within the scope of the following claims.

2TABLE 1Kinetic parameters of wild-type LgtC and itsvarious mutants for its substrates UDP-Gal and lactose.UDP-Gal2Lactose3kcatKmkcatKmkcat/KmLgtC1(s)−1(μM)kcat/Km (μM−1s−1)(s)−1(mM)(mM−1s−1)WT14.2180.8124.0201.20C128/174S11.4120.9719.2131.48D103E0.0042180.000020.003340.00009D103N0.0061870.000030.006580.00010Y186F25.6151.6731.6161.92Q189A0.4250.0171.01360.00741All constructs in this table have the C-terminal 25 residues deleted. 2kinetic parameters were determined at a constant lactose concentration of 100 mM 3kinetic parameters were determined at a constant UDP-Gal concentration of 250 μM

[0491]

3

TABLE 2

Data collection and refinement statistics1

Data collection

4-deoxy-

Peak
Inflection
Remote1
Remote2
lactose

Resolution (Å)
20-2.0
20-2.0
20-2.0
20-2.0
20-2.0

Wavelength
0.97949
0.97996
0.92526
1.06883
1.5418

(Å)

Unique
18498
18492
18400
18516
18851

reflections

Completeness
99.0
99.0
98.9
97.2
98.3

(%)
(97.7)
(97.7)
(97.8)
(83.9)
(90.2)

I/I(σ)
19.8
19.9
19.1
19.7
20.7

(6.1)
(6.1)
(5.9)
(5.1)
(8.03)

Rmerge (%)
4.4
4.4
4.7
4.2
6.2

(11.4)
(11.4)
(12.3)
(9.2)
(15.2)

[0492]

4

Refinement statistics and model stereochemistry

LgtC/Mn/donor
LgtC/Mn/donor/acceptor

Resolution (Å)
20-2.0
20-2.0

Unique reflections
18038
18225

Rcryst/Rfree (%)
19.9/22.74
19.3/22.76

RMSD bonds (Å)
0.007
0.007

RMSD angles (°)
1.31
1.33

Average B-factor (Å2)

Protein
13.5
16.3

UDP 2-deoxy-2-fluoro-
11.6
15.4

galactose

4-deoxylactose

19.8

Mn
5.3
11.3

Water
21.1
23.6

Ramachandran plot

Residues in most favored
92.2
91.0

regions (%)

Additionally allowed
7.0
8.6

regions (%)

Generously allowed regions
0.4
0.4

(%)

Disallowed regions (%)
0.4
0

1
Statistics for the highest resolution shell (2.07-2.0) are given in brackets.

[0493]

5

TABLE 3

Atomic Interactions of a Retaining Glycosyltransferase with a

Sugar Nucleotide Donor and/or Acceptor Molecules

Atomic Contact on

Sugar Nucleotide

No. of Atomic
Donor or Acceptor

Binding Site

Interaction
Molecules
Atomic Contact on Enzyme
Property

1
Uracil O2
Main chain nitrogen of Asp 8
HB

2
Uracil N3
OD1 of Asp 8
HB

3
Uracil carbonyl 04
ND2 group of Asn 10
HB

4
Ribose ring 02
Carbonyl oxygen of Ala 6

5
Ribose O3
Main chain amide of Ile 104

6
Phosphate 02A
Lys 250 (NZ)
HB

7
Phosphate 02B
Gly 247 (N) and His 78 (NE2)
HB

8
Sugar donor ring O3
Asp 103 and Arg 86
HB

9
Sugar donor ring 04′
Carboxylate of Asp 188
HB

10
Sugar donor ring 06′
Carboxylate of Asp 188
HB

11
Mn2+
His 244, Asp 103,

Asp 105

12
Lactose 06
Asp 130 (OD2) and Gln 189 (NE2)
HB

13
Lactose 06
Side chain atoms of Val 76, His 78, Tyr
VdW

186, Cys 246, and Gly 247

14
Reducing end glucose
Phe 132
HP

moiety of lactose

15

Pro 211 and Pro 248
VdW

16
Reducing end glucose
Thr 212 hydroxyl, main chain nitrogen
HB

moiety of lactose 03′

17

Cys 246
HB

HB: hydrogen bond interaction

HP: hydrophobic

VdW van der Waals interaction

[0494]

6

REMARK
coordinates from minimization refinement

REMARK
refinement resolution: 20.0-2.0 A

REMARK
starting r = .2046 free_r = .2331

REMARK
final r = .2033 free_r = .2321

REMARK
rmsd bonds = .005248 rmsd angles = 1.22351

REMARK
wa = .890542

REMARK
target = mlf cycles = 1 steps = 100

REMARK
sg = P2 (1) 2 (1) 2 (1) a = 39.79 b = 76.05 c = 86.84 alpha = 90 beta = 90 gamma = 90

REMARK
parameter file 1: CNS_TOPPAR:protein_rep.param

REMARK
parameter file 2: ../rnd4/upg.par

REMARK
parameter file 3: CNS_TOPPAR:ion.param

REMARK
parameter file 4: CNS_TOPPAR:water_rep.param

REMARK
parameter file 5: ../rnd6/acy.par

REMARK
molecular structure file: generate7_2.mtf

REMARK
input coordinates: generate7_2.pdb

REMARK
reflection file = ../lgtC.cv

REMARK
ncs = none

REMARK
B-correction resolution: 6.0-2.0

REMARK
initial B-factor correction applied to fobs:

REMARK
B11 = 1.111 B22 = 2.062 B33 = −3.173

REMARK
B12 = .000 B13 = .000 B23 = .000

REMARK
B-factor correction applied to coordinate array B: .174

REMARK
bulk solvent: density level = .335425 e/A{circumflex over ( )}3, B-factor = 42.4467 A{circumflex over ( )}2

REMARK
reflections with |Fobs|/sigma_F < 0.0 rejected

REMARK
reflections with |Fobs| > 10000 * rms (Fobs) rejected

REMARK
theoretical total number of refl. in resol. range:
18411
(100.0%)

REMARK
number of unobserved reflections (no entry or |F|= 0):
373
(2.0%)

REMARK
number of reflections rejected:
0
(>.0%)

REMARK
total number of reflections used:
18038
(>98.0%)

REMARK
number of reflections in working set:
17161
(>93.2%)

REMARK
number of reflections in test set:
877
(>4.8%)

CRYST1
39.790 76.050 86.840 90.00 90.00 90.00 P 21 21 21

REMARK
FILENAME = “minimize7_3.pdb”

REMARK
DATE: 29-May-00 21:53:49 created by user: karina

REMARK
VERSION: 1.0

ATOM
1
CB
MSE
1
47.916
46.223
65.035
1.00
15.18
DIC

ATOM
2
CG
MSE
1
47.459
47.194
63.956
1.00
18.95
DIC

ATOM
3
SE
MSE
1
46.533
48.765
64.672
1.00
23.16
DIC

ATOM
4
CE
MSE
1
48.073
49.691
65.392
1.00
19.79
DIC

ATOM
5
C
MSE
1
47.671
44.106
63.711
1.00
10.02
DIC

ATOM
6
O
MSE
1
47.762
44.051
62.487
1.00
9.02
DIC

ATOM
7
N
MSE
1
49.817
45.335
63.713
1.00
9.31
DIC

ATOM
8
CA
MSE
1
48.632
44.961
64.526
1.00
10.07
DIC

ATOM
9
N
ASP
2
46.762
43.426
64.398
1.00
8.25
DIC

ATOM
10
CA
ASP
2
45.786
42.580
63.729
1.00
8.29
DIC

ATOM
11
CB
ASP
2
45.742
41.193
64.376
1.00
8.73
DIC

ATOM
12
CG
ASP
2
47.016
40.405
64.139
1.00
11.00
DIC

ATOM
13
OD1
ASP
2
47.966
40.549
64.934
1.00
9.98
DIC

ATOM
14
OD2
ASP
2
47.073
39.655
63.139
1.00
12.73
DIC

ATOM
15
C
ASP
2
44.413
43.224
63.763
1.00
6.99
DIC

ATOM
16
O
ASP
2
43.839
43.440
64.831
1.00
5.46
DIC

ATOM
17
N
ILE
3
43.906
43.535
62.573
1.00
7.26
DIC

ATOM
18
CA
ILE
3
42.604
44.172
62.399
1.00
5.51
DIC

ATOM
19
CB
ILE
3
42.680
45.315
61.356
1.00
6.61
DIC

ATOM
20
CG2
ILE
3
41.276
45.917
61.119
1.00
3.06
DIC

ATOM
21
CG1
ILE
3
43.692
46.372
61.806
1.00
4.70
DIC

ATOM
22
CD
ILE
3
43.312
47.108
63.082
1.00
7.67
DIC

ATOM
23
C
ILE
3
41.585
43.166
61.893
1.00
6.14
DIC

ATOM
24
O
ILE
3
41.881
42.379
60.990
1.00
6.52
DIC

ATOM
25
N
VAL
4
40.388
43.205
62.472
1.00
5.89
DIC

ATOM
26
CA
VAL
4
39.302
42.322
62.072
1.00
4.89
DIC

ATOM
27
CB
VAL
4
38.791
41.468
63.248
1.00
6.30
DIC

ATOM
28
CG1
VAL
4
37.584
40.638
62.795
1.00
8.75
DIC

ATOM
29
CG2
VAL
4
39.904
40.558
63.753
1.00
5.68
DIC

ATOM
30
C
VAL
4
38.115
43.110
61.519
1.00
5.54
DIC

ATOM
31
O
VAL
4
37.688
44.111
62.097
1.00
4.90
DIC

ATOM
32
N
PHE
5
37.603
42.655
60.382
1.00
5.50
DIC

ATOM
33
CA
PHE
5
36.449
43.260
59.728
1.00
5.20
DIC

ATOM
34
CB
PHE
5
36.832
43.859
58.364
1.00
5.40
DIC

ATOM
35
CG
PHE
5
37.439
45.234
58.430
1.00
4.45
DIC

ATOM
36
CD1
PHE
5
36.693
46.323
58.876
1.00
4.41
DIC

ATOM
37
CD2
PHE
5
38.732
45.453
57.969
1.00
5.91
DIC

ATOM
38
CE1
PHE
5
37.228
47.619
58.851
1.00
6.66
DIC

ATOM
39
CE2
PHE
5
39.276
46.743
57.940
1.00
7.08
DIC

ATOM
40
CZ
PHE
5
38.516
47.828
58.381
1.00
6.75
DIC

ATOM
41
C
PHE
5
35.501
42.090
59.479
1.00
6.22
DIC

ATOM
42
O
PHE
5
35.929
40.934
59.475
1.00
6.65
DIC

ATOM
43
N
ALA
6
34.222
42.390
59.282
1.00
4.81
DIC

ATOM
44
CA
ALA
6
33.221
41.372
58.988
1.00
4.67
DIC

ATOM
45
CB
ALA
6
32.352
41.084
60.213
1.00
2.66
DIC

ATOM
46
C
ALA
6
32.366
41.944
57.872
1.00
5.29
DIC

ATOM
47
O
ALA
6
31.920
43.090
57.952
1.00
4.39
DIC

ATOM
48
N
ALA
7
32.132
41.164
56.826
1.00
5.20
DIC

ATOM
49
CA
ALA
7
31.314
41.669
55.736
1.00
6.73
DIC

ATOM
50
CB
ALA
7
32.120
42.659
54.901
1.00
8.23
DIC

ATOM
51
C
ALA
7
30.755
40.590
54.834
1.00
8.12
DIC

ATOM
52
O
ALA
7
31.340
39.515
54.695
1.00
7.34
DIC

ATOM
53
N
ASP
8
29.598
40.885
54.247
1.00
8.39
DIC

ATOM
54
CA
ASP
8
28.967
39.987
53.295
1.00
8.38
DIC

ATOM
55
CB
ASP
8
27.449
39.915
53.502
1.00
9.33
DIC

ATOM
56
CG
ASP
8
26.832
41.261
53.816
1.00
9.71
DIC

ATOM
57
OD1
ASP
8
27.334
42.290
53.312
1.00
8.87
DIC

ATOM
58
OD2
ASP
8
25.828
41.285
54.561
1.00
9.54
DIC

ATOM
59
C
ASP
8
29.294
40.608
51.941
1.00
9.19
DIC

ATOM
60
O
ASP
8
29.926
41.664
51.878
1.00
7.12
DIC

ATOM
61
N
ASP
9
28.873
39.969
50.859
1.00
9.74
DIC

ATOM
62
CA
ASP
9
29.180
40.485
49.532
1.00
10.05
DIC

ATOM
63
CB
ASP
9
28.551
39.582
48.471
1.00
10.66
DIC

ATOM
64
CG
ASP
9
29.132
39.817
47.098
1.00
10.96
DIC

ATOM
65
OD1
ASP
9
30.353
39.613
46.927
1.00
9.95
DIC

ATOM
66
OD2
ASP
9
28.370
40.210
46.192
1.00
15.56
DIC

ATOM
67
C
ASP
9
28.731
41.935
49.328
1.00
11.33
DIC

ATOM
68
O
ASP
9
29.427
42.729
48.689
1.00
11.67
DIC

ATOM
69
N
ASN
10
27.578
42.282
49.889
1.00
11.40
DIC

ATOM
70
CA
ASN
10
27.033
43.626
49.760
1.00
12.66
DIC

ATOM
71
CB
ASN
10
25.707
43.721
50.518
1.00
14.73
DIC

ATOM
72
CG
ASN
10
25.079
45.098
50.424
1.00
16.23
DIC

ATOM
73
OD1
ASN
10
24.924
45.644
49.335
1.00
16.14
DIC

ATOM
74
ND2
ASN
10
24.706
45.662
51.569
1.00
15.48
DIC

ATOM
75
C
ASN
10
27.972
44.730
50.244
1.00
12.57
DIC

ATOM
76
O
ASN
10
27.962
45.839
49.705
1.00
12.93
DIC

ATOM
77
N
TYR
11
28.782
44.432
51.254
1.00
10.65
DIC

ATOM
78
CA
TYR
11
29.702
45.425
51.805
1.00
10.78
DIC

ATOM
79
CB
TYR
11
29.632
45.399
53.336
1.00
10.58
DIC

ATOM
80
CG
TYR
11
28.703
46.427
53.944
1.00
11.86
DIC

ATOM
81
CD1
TYR
11
27.599
46.915
53.239
1.00
11.68
DIC

ATOM
82
CE1
TYR
11
26.737
47.853
53.811
1.00
12.47
DIC

ATOM
83
CD2
TYR
11
28.918
46.900
55.239
1.00
11.28
DIC

ATOM
84
CE2
TYR
11
28.063
47.829
55.818
1.00
13.50
DIC

ATOM
85
CZ
TYR
11
26.978
48.301
55.101
1.00
12.90
DIC

ATOM
86
OH
TYR
11
26.144
49.225
55.681
1.00
15.54
DIC

ATOM
87
C
TYR
11
31.155
45.267
51.369
1.00
11.16
DIC

ATOM
88
O
TYR
11
32.043
45.919
51.925
1.00
11.02
DIC

ATOM
89
N
ALA
12
31.400
44.421
50.371
1.00
10.59
DIC

ATOM
90
CA
ALA
12
32.760
44.183
49.892
1.00
10.32
DIC

ATOM
91
CB
ALA
12
32.744
43.157
48.754
1.00
11.38
DIC

ATOM
92
C
ALA
12
33.489
45.450
49.441
1.00
9.91
DIC

ATOM
93
O
ALA
12
34.660
45.647
49.766
1.00
9.42
DIC

ATOM
94
N
ALA
13
32.804
46.306
48.688
1.00
9.60
DIC

ATOM
95
CA
ALA
13
33.414
47.540
48.205
1.00
9.28
DIC

ATOM
96
CB
ALA
13
32.481
48.229
47.204
1.00
9.14
DIC

ATOM
97
C
ALA
13
33.756
48.491
49.355
1.00
8.84
DIC

ATOM
98
O
ALA
13
34.815
49.125
49.357
1.00
8.22
DIC

ATOM
99
N
TYR
14
32.865
48.582
50.336
1.00
8.07
DIC

ATOM
100
CA
TYR
14
33.090
49.462
51.478
1.00
8.03
DIC

ATOM
101
CB
TYR
14
31.803
49.606
52.291
1.00
8.61
DIC

ATOM
102
CG
TYR
14
30.600
49.939
51.438
1.00
10.64
DIC

ATOM
103
CD1
TYR
14
30.700
50.855
50.394
1.00
11.14
DIC

ATOM
104
CE1
TYR
14
29.602
51.168
49.602
1.00
13.63
DIC

ATOM
105
CD2
TYR
14
29.363
49.340
51.676
1.00
11.59
DIC

ATOM
106
CE2
TYR
14
28.252
49.647
50.891
1.00
14.49
DIC

ATOM
107
CZ
TYR
14
28.384
50.563
49.854
1.00
14.26
DIC

ATOM
108
OH
TYR
14
27.302
50.879
49.068
1.00
17.66
DIC

ATOM
109
C
TYR
14
34.222
48.934
52.356
1.00
7.50
DIC

ATOM
110
O
TYR
14
34.995
49.710
52.914
1.00
8.49
DIC

ATOM
111
N
LEU
15
34.310
47.612
52.469
1.00
7.68
DIC

ATOM
112
CA
LEU
15
35.363
46.965
53.247
1.00
7.83
DIC

ATOM
113
CB
LEU
15
35.267
45.440
53.105
1.00
7.70
DIC

ATOM
114
CG
LEU
15
36.519
44.619
53.441
1.00
8.87
DIC

ATOM
115
CD1
LEU
15
36.881
44.790
54.913
1.00
7.99
DIC

ATOM
116
CD2
LEU
15
36.265
43.146
53.117
1.00
8.32
DIC

ATOM
117
C
LEU
15
36.719
47.428
52.729
1.00
6.26
DIC

ATOM
118
O
LEU
15
37.605
47.790
53.503
1.00
5.67
DIC

ATOM
119
N
CYS
16
36.868
47.407
51.407
1.00
6.41
DIC

ATOM
120
CA
CYS
16
38.109
47.814
50.761
1.00
6.53
DIC

ATOM
121
CB
CYS
16
37.972
47.683
49.241
1.00
7.09
DIC

ATOM
122
SG
CYS
16
39.490
48.066
48.352
1.00
10.90
DIC

ATOM
123
C
CYS
16
38.509
49.245
51.122
1.00
6.22
DIC

ATOM
124
O
CYS
16
39.673
49.521
51.415
1.00
6.80
DIC

ATOM
125
N
VAL
17
37.545
50.156
51.101
1.00
6.94
DIC

ATOM
126
CA
VAL
17
37.823
51.548
51.436
1.00
7.93
DIC

ATOM
127
CB
VAL
17
36.583
52.436
51.173
1.00
8.98
DIC

ATOM
128
CG1
VAL
17
36.840
53.854
51.651
1.00
8.40
DIC

ATOM
129
CG2
VAL
17
36.260
52.436
49.679
1.00
9.77
DIC

ATOM
130
C
VAL
17
38.240
51.670
52.900
1.00
7.79
DIC

ATOM
131
O
VAL
17
39.233
52.316
53.217
1.00
7.46
DIC

ATOM
132
N
ALA
18
37.481
51.041
53.790
1.00
7.51
DIC

ATOM
133
CA
ALA
18
37.789
51.091
55.213
1.00
7.78
DIC

ATOM
134
CB
ALA
18
36.750
50.295
56.005
1.00
7.26
DIC

ATOM
135
C
ALA
18
39.188
50.530
55.471
1.00
7.32
DIC

ATOM
136
O
ALA
18
39.978
51.125
56.201
1.00
8.92
DIC

ATOM
137
N
ALA
19
39.491
49.387
54.864
1.00
6.80
DIC

ATOM
138
CA
ALA
19
40.796
48.761
55.046
1.00
6.34
DIC

ATOM
139
CB
ALA
19
40.866
47.448
54.275
1.00
7.20
DIC

ATOM
140
C
ALA
19
41.904
49.698
54.585
1.00
9.12
DIC

ATOM
141
O
ALA
19
42.917
49.854
55.267
1.00
7.42
DIC

ATOM
142
N
LYS
20
41.714
50.333
53.431
1.00
9.41
DIC

ATOM
143
CA
LYS
20
42.736
51.243
52.937
1.00
10.30
DIC

ATOM
144
CB
LYS
20
42.404
51.725
51.523
1.00
11.46
DIC

ATOM
145
CG
LYS
20
43.560
52.483
50.883
1.00
17.23
DIC

ATOM
146
CD
LYS
20
43.346
52.750
49.404
1.00
19.42
DIC

ATOM
147
CE
LYS
20
44.561
53.444
48.812
1.00
21.28
DIC

ATOM
148
NZ
LYS
20
44.387
53.756
47.368
1.00
22.28
DIC

ATOM
149
C
LYS
20
42.912
52.435
53.881
1.00
10.50
DIC

ATOM
150
O
LYS
20
44.017
52.950
54.027
1.00
8.75
DIC

ATOM
151
N
SER
21
41.836
52.872
54.533
1.00
9.94
DIC

ATOM
152
CA
SER
21
41.959
53.997
55.459
1.00
9.54
DIC

ATOM
153
CB
SER
21
40.586
54.438
55.988
1.00
10.25
DIC

ATOM
154
OG
SER
21
40.096
53.556
56.983
1.00
11.69
DIC

ATOM
155
C
SER
21
42.859
53.588
56.626
1.00
7.93
DIC

ATOM
156
O
SER
21
43.587
54.411
57.172
1.00
8.07
DIC

ATOM
157
N
VAL
22
42.807
52.314
57.006
1.00
8.61
DIC

ATOM
158
CA
VAL
22
43.639
51.817
58.102
1.00
7.31
DIC

ATOM
159
CB
VAL
22
43.225
50.397
58.540
1.00
7.87
DIC

ATOM
160
CG1
VAL
22
44.163
49.901
59.630
1.00
7.62
DIC

ATOM
161
CG2
VAL
22
41.792
50.404
59.043
1.00
7.19
DIC

ATOM
162
C
VAL
22
45.107
51.785
57.684
1.00
8.07
DIC

ATOM
163
O
VAL
22
45.992
52.151
58.460
1.00
8.06
DIC

ATOM
164
N
GLU
23
45.371
51.340
56.460
1.00
7.76
DIC

ATOM
165
CA
GLU
23
46.749
51.296
55.977
1.00
9.02
DIC

ATOM
166
CB
GLU
23
46.832
50.605
54.609
1.00
9.88
DIC

ATOM
167
CG
GLU
23
46.444
49.125
54.602
1.00
11.02
DIC

ATOM
168
CD
GLU
23
46.763
48.450
53.276
1.00
13.23
DIC

ATOM
169
OE1
GLU
23
46.541
49.086
52.228
1.00
15.00
DIC

ATOM
170
OE2
GLU
23
47.221
47.285
53.279
1.00
12.64
DIC

ATOM
171
C
GLU
23
47.309
52.714
55.858
1.00
8.76
DIC

ATOM
172
O
GLU
23
48.447
52.976
56.246
1.00
8.97
DIC

ATOM
173
N
ALA
24
46.503
53.630
55.328
1.00
7.51
DIC

ATOM
174
CA
ALA
24
46.939
55.011
55.152
1.00
7.86
DIC

ATOM
175
CB
ALA
24
45.825
55.834
54.493
1.00
8.90
DIC

ATOM
176
C
ALA
24
47.367
55.664
56.465
1.00
8.07
DIC

ATOM
177
O
ALA
24
48.332
56.436
56.499
1.00
6.11
DIC

ATOM
178
N
ALA
25
46.654
55.353
57.543
1.00
7.25
DIC

ATOM
179
CA
ALA
25
46.961
55.923
58.853
1.00
7.99
DIC

ATOM
180
CB
ALA
25
45.705
55.908
59.736
1.00
6.76
DIC

ATOM
181
C
ALA
25
48.112
55.212
59.569
1.00
8.57
DIC

ATOM
182
O
ALA
25
48.504
55.611
60.663
1.00
7.27
DIC

ATOM
183
N
HIS
26
48.646
54.157
58.960
1.00
8.84
DIC

ATOM
184
CA
HIS
26
49.758
53.424
59.563
1.00
9.94
DIC

ATOM
185
CB
HIS
26
49.258
52.138
60.227
1.00
10.38
DIC

ATOM
186
CG
HIS
26
48.185
52.363
61.246
1.00
12.18
DIC

ATOM
187
CD2
HIS
26
48.251
52.548
62.587
1.00
12.40
DIC

ATOM
188
ND1
HIS
26
46.848
52.431
60.917
1.00
12.47
DIC

ATOM
189
CE1
HIS
26
46.137
52.644
62.010
1.00
13.32
DIC

ATOM
190
NE2
HIS
26
46.965
52.719
63.037
1.00
11.84
DIC

ATOM
191
C
HIS
26
50.804
53.090
58.502
1.00
8.30
DIC

ATOM
192
O
HIS
26
51.035
51.923
58.179
1.00
7.59
DIC

ATOM
193
N
PRO
27
51.465
54.124
57.959
1.00
8.95
DIC

ATOM
194
CD
PRO
27
51.399
55.521
58.424
1.00
9.38
DIC

ATOM
195
CA
PRO
27
52.490
53.970
56.927
1.00
9.59
DIC

ATOM
196
CB
PRO
27
52.940
55.408
56.672
1.00
10.14
DIC

ATOM
197
CG
PRO
27
52.738
56.064
57.999
1.00
11.05
DIC

ATOM
198
C
PRO
27
53.652
53.045
57.278
1.00
10.29
DIC

ATOM
199
O
PRO
27
54.227
52.414
56.389
1.00
12.94
DIC

ATOM
200
N
ASP
28
54.000
52.949
58.557
1.00
10.20
DIC

ATOM
201
CA
ASP
28
55.119
52.088
58.935
1.00
9.90
DIC

ATOM
202
CB
ASP
28
56.284
52.933
59.456
1.00
10.34
DIC

ATOM
203
CG
ASP
28
57.552
52.116
59.643
1.00
10.37
DIC

ATOM
204
OD1
ASP
28
57.857
51.288
58.758
1.00
11.78
DIC

ATOM
205
OD2
ASP
28
58.241
52.306
60.665
1.00
9.99
DIC

ATOM
206
C
ASP
28
54.765
51.009
59.951
1.00
11.28
DIC

ATOM
207
O
ASP
28
55.609
50.577
60.737
1.00
11.87
DIC

ATOM
208
N
THR
29
53.510
50.576
59.935
1.00
10.17
DIC

ATOM
209
CA
THR
29
53.062
49.523
60.836
1.00
11.26
DIC

ATOM
210
CB
THR
29
51.948
50.007
61.791
1.00
9.97
DIC

ATOM
211
OG1
THR
29
52.424
51.115
62.566
1.00
10.16
DIC

ATOM
212
CG2
THR
29
51.537
48.886
62.737
1.00
10.26
DIC

ATOM
213
C
THR
29
52.508
48.385
59.992
1.00
11.82
DIC

ATOM
214
O
THR
29
51.784
48.617
59.022
1.00
11.70
DIC

ATOM
215
N
GLU
30
52.868
47.159
60.349
1.00
11.89
DIC

ATOM
216
CA
GLU
30
52.382
45.987
59.632
1.00
14.04
DIC

ATOM
217
CB
GLU
30
53.142
44.743
60.097
1.00
17.64
DIC

ATOM
218
CG
GLU
30
53.297
43.655
59.051
1.00
25.15
DIC

ATOM
219
CD
GLU
30
54.060
44.126
57.822
1.00
27.98
DIC

ATOM
220
OE1
GLU
30
53.418
44.612
56.869
1.00
28.55
DIC

ATOM
221
OE2
GLU
30
55.306
44.026
57.816
1.00
31.94
DIC

ATOM
222
C
GLU
30
50.903
45.848
59.982
1.00
12.56
DIC

ATOM
223
O
GLU
30
50.545
45.798
61.158
1.00
13.85
DIC

ATOM
224
N
ILE
31
50.041
45.810
58.972
1.00
10.51
DIC

ATOM
225
CA
ILE
31
48.610
45.666
59.222
1.00
11.18
DIC

ATOM
226
CB
ILE
31
47.780
46.780
58.526
1.00
11.20
DIC

ATOM
227
CG2
ILE
31
46.287
46.575
58.809
1.00
9.63
DIC

ATOM
228
CG1
ILE
31
48.218
48.159
59.028
1.00
10.58
DIC

ATOM
229
CD
ILE
31
47.875
48.435
60.480
1.00
11.64
DIC

ATOM
230
C
ILE
31
48.142
44.317
58.696
1.00
10.56
DIC

ATOM
231
O
ILE
31
48.127
44.082
57.487
1.00
11.51
DIC

ATOM
232
N
ARG
32
47.770
43.430
59.609
1.00
9.50
DIC

ATOM
233
CA
ARG
32
47.296
42.108
59.227
1.00
9.26
DIC

ATOM
234
CB
ARG
32
47.919
41.042
60.137
1.00
12.86
DIC

ATOM
235
CG
ARG
32
49.451
41.101
60.168
1.00
15.87
DIC

ATOM
236
CD
ARG
32
50.090
39.888
60.831
1.00
19.22
DIC

ATOM
237
NE
ARG
32
49.697
39.723
62.228
1.00
23.57
DIC

ATOM
238
CZ
ARG
32
50.227
38.819
63.048
1.00
26.66
DIC

ATOM
239
NH1
ARG
32
51.177
38.002
62.608
1.00
27.60
DIC

ATOM
240
NH2
ARG
32
49.803
38.723
64.304
1.00
25.75
DIC

ATOM
241
C
ARG
32
45.774
42.083
59.328
1.00
8.78
DIC

ATOM
242
O
ARG
32
45.219
42.140
60.426
1.00
6.14
DIC

ATOM
243
N
PHE
33
45.111
42.021
58.174
1.00
7.42
DIC

ATOM
244
CA
PHE
33
43.653
41.993
58.107
1.00
6.88
DIC

ATOM
245
CB
PHE
33
43.159
42.646
56.809
1.00
6.79
DIC

ATOM
246
CG
PHE
33
43.424
44.126
56.715
1.00
6.63
DIC

ATOM
247
CD1
PHE
33
42.732
45.027
57.521
1.00
6.30
DIC

ATOM
248
CD2
PHE
33
44.333
44.622
55.784
1.00
6.14
DIC

ATOM
249
CE1
PHE
33
42.936
46.403
57.399
1.00
6.64
DIC

ATOM
250
CE2
PHE
33
44.548
45.995
55.651
1.00
7.13
DIC

ATOM
251
CZ
PHE
33
43.845
46.889
56.462
1.00
7.26
DIC

ATOM
252
C
PHE
33
43.083
40.575
58.175
1.00
7.51
DIC

ATOM
253
O
PHE
33
43.565
39.662
57.501
1.00
6.94
DIC

ATOM
254
N
HIS
34
42.048
40.413
58.992
1.00
6.28
DIC

ATOM
255
CA
HIS
34
41.345
39.141
59.159
1.00
7.93
DIC

ATOM
256
CB
HIS
34
41.450
38.652
60.604
1.00
8.52
DIC

ATOM
257
CG
HIS
34
42.855
38.517
61.100
1.00
10.09
DIC

ATOM
258
CD2
HIS
34
43.703
39.428
61.632
1.00
11.33
DIC

ATOM
259
ND1
HIS
34
43.541
37.322
61.079
1.00
11.33
DIC

ATOM
260
CE1
HIS
34
44.751
37.502
61.578
1.00
12.87
DIC

ATOM
261
NE2
HIS
34
44.874
38.772
61.921
1.00
11.31
DIC

ATOM
262
C
HIS
34
39.891
39.483
58.847
1.00
7.56
DIC

ATOM
263
O
HIS
34
39.260
40.244
59.579
1.00
6.31
DIC

ATOM
264
N
VAL
35
39.358
38.928
57.766
1.00
6.19
DIC

ATOM
265
CA
VAL
35
37.990
39.232
57.384
1.00
7.23
DIC

ATOM
266
CB
VAL
35
37.924
39.665
55.900
1.00
6.63
DIC

ATOM
267
CG1
VAL
35
36.498
40.013
55.515
1.00
8.73
DIC

ATOM
268
CG2
VAL
35
38.840
40.851
55.669
1.00
8.74
DIC

ATOM
269
C
VAL
35
37.013
38.081
57.596
1.00
8.74
DIC

ATOM
270
O
VAL
35
37.174
37.000
57.023
1.00
6.03
DIC

ATOM
271
N
LEU
36
36.010
38.314
58.438
1.00
7.38
DIC

ATOM
272
CA
LEU
36
34.984
37.307
58.683
1.00
8.45
DIC

ATOM
273
CB
LEU
36
34.190
37.639
59.954
1.00
7.92
DIC

ATOM
274
CG
LEU
36
34.993
37.773
61.259
1.00
8.01
DIC

ATOM
275
CD1
LEU
36
34.031
37.960
62.427
1.00
7.60
DIC

ATOM
276
CD2
LEU
36
35.847
36.535
61.492
1.00
7.27
DIC

ATOM
277
C
LEU
36
34.112
37.432
57.432
1.00
9.33
DIC

ATOM
278
O
LEU
36
33.319
38.365
57.299
1.00
8.93
DIC

ATOM
279
N
ASP
37
34.304
36.495
56.511
1.00
9.60
DIC

ATOM
280
CA
ASP
37
33.624
36.471
55.218
1.00
10.03
DIC

ATOM
281
CB
ASP
37
34.582
35.844
54.199
1.00
11.29
DIC

ATOM
282
CG
ASP
37
33.980
35.713
52.820
1.00
10.76
DIC

ATOM
283
OD1
ASP
37
32.772
35.965
52.659
1.00
10.09
DIC

ATOM
284
OD2
ASP
37
34.728
35.344
51.894
1.00
13.51
DIC

ATOM
285
C
ASP
37
32.287
35.728
55.223
1.00
11.39
DIC

ATOM
286
O
ASP
37
32.247
34.496
55.212
1.00
9.17
DIC

ATOM
287
N
ALA
38
31.196
36.489
55.209
1.00
11.46
DIC

ATOM
288
CA
ALA
38
29.853
35.917
55.230
1.00
13.65
DIC

ATOM
289
CB
ALA
38
28.914
36.832
56.015
1.00
14.69
DIC

ATOM
290
C
ALA
38
29.262
35.632
53.851
1.00
14.91
DIC

ATOM
291
O
ALA
38
28.045
35.490
53.714
1.00
17.68
DIC

ATOM
292
N
GLY
39
30.111
35.543
52.834
1.00
14.37
DIC

ATOM
293
CA
GLY
39
29.608
35.255
51.502
1.00
13.29
DIC

ATOM
294
C
GLY
39
30.109
36.181
50.410
1.00
12.56
DIC

ATOM
295
O
GLY
39
29.416
36.405
49.421
1.00
13.32
DIC

ATOM
296
N
ILE
40
31.308
36.724
50.588
1.00
10.63
DIC

ATOM
297
CA
ILE
40
31.906
37.616
49.597
1.00
9.24
DIC

ATOM
298
CB
ILE
40
33.142
38.337
50.192
1.00
8.46
DIC

ATOM
299
CG2
ILE
40
33.741
39.293
49.168
1.00
7.79
DIC

ATOM
300
CG1
ILE
40
32.729
39.099
51.456
1.00
6.53
DIC

ATOM
301
CD
ILE
40
33.894
39.641
52.273
1.00
9.79
DIC

ATOM
302
C
ILE
40
32.324
36.806
48.363
1.00
9.40
DIC

ATOM
303
O
ILE
40
32.951
35.753
48.482
1.00
8.50
DIC

ATOM
304
N
SER
41
31.972
37.294
47.179
1.00
10.73
DIC

ATOM
305
CA
SER
41
32.307
36.591
45.942
1.00
11.14
DIC

ATOM
306
CB
SER
41
31.669
37.295
44.742
1.00
11.01
DIC

ATOM
307
OG
SER
41
32.317
38.526
44.477
1.00
12.46
DIC

ATOM
308
C
SER
41
33.816
36.512
45.736
1.00
11.15
DIC

ATOM
309
O
SER
41
34.569
37.313
46.290
1.00
11.69
DIC

ATOM
310
N
GLU
42
34.253
35.541
44.940
1.00
12.21
DIC

ATOM
311
CA
GLU
42
35.673
35.371
44.659
1.00
11.82
DIC

ATOM
312
CB
GLU
42
35.906
34.153
43.755
1.00
15.43
DIC

ATOM
313
CG
GLU
42
37.376
33.842
43.483
1.00
19.50
DIC

ATOM
314
CD
GLU
42
37.989
34.710
42.392
1.00
24.05
DIC

ATOM
315
OE1
GLU
42
39.235
34.789
42.331
1.00
27.65
DIC

ATOM
316
OE2
GLU
42
37.235
35.302
41.589
1.00
24.25
DIC

ATOM
317
C
GLU
42
36.199
36.625
43.973
1.00
10.77
DIC

ATOM
318
O
GLU
42
37.309
37.070
44.248
1.00
9.02
DIC

ATOM
319
N
ALA
43
35.389
37.193
43.086
1.00
10.24
DIC

ATOM
320
CA
ALA
43
35.776
38.395
42.359
1.00
11.39
DIC

ATOM
321
CB
ALA
43
34.720
38.744
41.307
1.00
10.87
DIC

ATOM
322
C
ALA
43
35.963
39.564
43.317
1.00
10.68
DIC

ATOM
323
O
ALA
43
36.906
40.343
43.181
1.00
9.26
DIC

ATOM
324
N
ASN
44
35.070
39.681
44.294
1.00
11.27
DIC

ATOM
325
CA
ASN
44
35.169
40.774
45.253
1.00
11.66
DIC

ATOM
326
CB
ASN
44
33.839
40.954
45.997
1.00
10.82
DIC

ATOM
327
CG
ASN
44
32.789
41.645
45.141
1.00
13.91
DIC

ATOM
328
OD1
ASN
44
33.094
42.603
44.429
1.00
14.16
DIC

ATOM
329
ND2
ASN
44
31.547
41.171
45.213
1.00
13.53
DIC

ATOM
330
C
ASN
44
36.326
40.602
46.235
1.00
12.23
DIC

ATOM
331
O
ASN
44
36.912
41.585
46.686
1.00
12.30
DIC

ATOM
332
N
ARG
45
36.662
39.358
46.566
1.00
12.83
DIC

ATOM
333
CA
ARG
45
37.775
39.117
47.477
1.00
13.27
DIC

ATOM
334
CB
ARG
45
37.838
37.640
47.888
1.00
14.62
DIC

ATOM
335
CG
ARG
45
36.519
37.103
48.420
1.00
19.99
DIC

ATOM
336
CD
ARG
45
36.679
36.267
49.680
1.00
23.85
DIC

ATOM
337
NE
ARG
45
37.610
35.153
49.520
1.00
27.49
DIC

ATOM
338
CZ
ARG
45
37.746
34.167
50.404
1.00
30.19
DIC

ATOM
339
NH1
ARG
45
37.007
34.152
51.506
1.00
31.72
DIC

ATOM
340
NH2
ARG
45
38.634
33.202
50.199
1.00
29.60
DIC

ATOM
341
C
ARG
45
39.063
39.516
46.760
1.00
11.59
DIC

ATOM
342
O
ARG
45
39.936
40.159
47.337
1.00
8.60
DIC

ATOM
343
N
ALA
46
39.167
39.141
45.490
1.00
10.34
DIC

ATOM
344
CA
ALA
46
40.347
39.475
44.704
1.00
10.59
DIC

ATOM
345
CB
ALA
46
40.257
38.830
43.321
1.00
11.03
DIC

ATOM
346
C
ALA
46
40.480
40.987
44.567
1.00
10.58
DIC

ATOM
347
O
ALA
46
41.576
41.535
44.686
1.00
11.52
DIC

ATOM
348
N
AL A
47
39.360
41.661
44.318
1.00
10.04
DIC

ATOM
349
CA
ALA
47
39.363
43.112
44.155
1.00
9.25
DIC

ATOM
350
CB
ALA
47
37.997
43.587
43.672
1.00
11.48
DIC

ATOM
351
C
ALA
47
39.752
43.844
45.443
1.00
9.33
DIC

ATOM
352
O
ALA
47
40.459
44.849
45.399
1.00
8.11
DIC

ATOM
353
N
VAL
48
39.284
43.353
46.587
1.00
9.19
DIC

ATOM
354
CA
VAL
48
39.624
43.982
47.858
1.00
9.94
DIC

ATOM
355
CB
VAL
48
38.902
43.302
49.049
1.00
9.44
DIC

ATOM
356
CG1
VAL
48
39.431
43.863
50.367
1.00
7.91
DIC

ATOM
357
CG2
VAL
48
37.403
43.535
48.955
1.00
6.88
DIC

ATOM
358
C
VAL
48
41.133
43.867
48.067
1.00
10.57
DIC

ATOM
359
O
VAL
48
41.808
44.851
48.359
1.00
10.43
DIC

ATOM
360
N
ALA
49
41.655
42.657
47.898
1.00
11.00
DIC

ATOM
361
CA
ALA
49
43.079
42.401
48.075
1.00
12.61
DIC

ATOM
362
CB
ALA
49
43.352
40.903
47.955
1.00
11.98
DIC

ATOM
363
C
ALA
49
43.951
43.170
47.085
1.00
13.08
DIC

ATOM
364
O
ALA
49
45.011
43.683
47.446
1.00
13.68
DIC

ATOM
365
N
ALA
50
43.502
43.251
45.838
1.00
14.66
DIC

ATOM
366
CA
ALA
50
44.256
43.948
44.801
1.00
14.50
DIC

ATOM
367
CB
ALA
50
43.530
43.828
43.463
1.00
15.47
DIC

ATOM
368
C
ALA
50
44.497
45.421
45.132
1.00
15.39
DIC

ATOM
369
O
ALA
50
45.490
46.004
44.698
1.00
16.30
DIC

ATOM
370
N
ASN
51
43.590
46.020
45.899
1.00
14.62
DIC

ATOM
371
CA
ASN
51
43.708
47.429
46.269
1.00
14.05
DIC

ATOM
372
CB
ASN
51
42.317
48.048
46.439
1.00
12.38
DIC

ATOM
373
CG
ASN
51
41.634
48.316
45.116
1.00
12.84
DIC

ATOM
374
OD1
ASN
51
42.110
49.114
44.314
1.00
13.23
DIC

ATOM
375
ND2
ASN
51
40.511
47.651
44.881
1.00
11.33
DIC

ATOM
376
C
ASN
51
44.512
47.668
47.542
1.00
15.83
DIC

ATOM
377
O
ASN
51
44.891
48.804
47.841
1.00
17.23
DIC

ATOM
378
N
LEU
52
44.773
46.607
48.295
1.00
15.52
DIC

ATOM
379
CA
LEU
52
45.520
46.754
49.535
1.00
17.67
DIC

ATOM
380
CB
LEU
52
45.106
45.669
50.530
1.00
15.40
DIC

ATOM
381
CG
LEU
52
43.604
45.719
50.825
1.00
16.03
DIC

ATOM
382
CD1
LEU
52
43.233
44.666
51.852
1.00
16.15
DIC

ATOM
383
CD2
LEU
52
43.232
47.106
51.322
1.00
15.81
DIC

ATOM
384
C
LEU
52
47.021
46.730
49.305
1.00
19.77
DIC

ATOM
385
O
LEU
52
47.497
46.237
48.277
1.00
18.50
DIC

ATOM
386
N
ARG
53
47.754
47.275
50.271
1.00
21.96
DIC

ATOM
387
CA
ARG
53
49.207
47.361
50.210
1.00
25.17
DIC

ATOM
388
CB
ARG
53
49.773
47.572
51.619
1.00
24.25
DIC

ATOM
389
CG
ARG
53
50.746
48.726
51.703
1.00
23.54
DIC

ATOM
390
CD
ARG
53
50.512
49.603
52.931
1.00
20.57
DIC

ATOM
391
NE
ARG
53
50.702
48.882
54.184
1.00
16.68
DIC

ATOM
392
CZ
ARG
53
50.784
49.472
55.373
1.00
17.69
DIC

ATOM
393
NH1
ARG
53
50.694
50.794
55.469
1.00
14.96
DIC

ATOM
394
NH2
ARG
53
50.957
48.744
56.467
1.00
16.12
DIC

ATOM
395
C
ARG
53
49.811
46.124
49.565
1.00
26.76
DIC

ATOM
396
O
ARG
53
50.790
46.214
48.825
1.00
28.81
DIC

ATOM
397
N
GLY
55
49.212
44.969
49.834
1.00
28.95
DIC

ATOM
398
CA
GLY
55
49.702
43.742
49.245
1.00
30.90
DIC

ATOM
399
C
GLY
55
48.600
42.749
48.919
1.00
32.46
DIC

ATOM
400
O
GLY
55
48.361
42.412
47.756
1.00
33.41
DIC

ATOM
401
N
GLY
56
47.909
42.297
49.958
1.00
33.24
DIC

ATOM
402
CA
GLY
56
46.866
41.306
49.792
1.00
31.87
DIC

ATOM
403
C
GLY
56
47.421
40.103
50.521
1.00
31.64
DIC

ATOM
404
O
GLY
56
46.693
39.202
50.943
1.00
32.69
DIC

ATOM
405
N
GLY
57
48.743
40.105
50.666
1.00
29.97
DIC

ATOM
406
CA
GLY
57
49.415
39.035
51.373
1.00
28.09
DIC

ATOM
407
C
GLY
57
49.162
39.249
52.849
1.00
26.72
DIC

ATOM
408
O
GLY
57
49.474
38.394
53.677
1.00
28.17
DIC

ATOM
409
N
ASN
58
48.592
40.409
53.171
1.00
24.96
DIC

ATOM
410
CA
ASN
58
48.272
40.755
54.550
1.00
22.29
DIC

ATOM
411
CB
ASN
58
48.850
42.121
54.919
1.00
24.14
DIC

ATOM
412
CG
ASN
58
50.242
42.023
55.510
1.00
27.73
DIC

ATOM
413
OD1
ASN
58
50.457
41.332
56.509
1.00
27.14
DIC

ATOM
414
ND2
ASN
58
51.198
42.717
54.898
1.00
28.37
DIC

ATOM
415
C
ASN
58
46.777
40.748
54.832
1.00
19.33
DIC

ATOM
416
O
ASN
58
46.315
41.409
55.761
1.00
17.00
DIC

ATOM
417
N
ILE
59
46.016
40.020
54.021
1.00
16.23
DIC

ATOM
418
CA
ILE
59
44.584
39.920
54.254
1.00
14.14
DIC

ATOM
419
CB
ILE
59
43.766
40.863
53.329
1.00
15.68
DIC

ATOM
420
CG2
ILE
59
43.980
40.502
51.862
1.00
14.29
DIC

ATOM
421
CG1
ILE
59
42.283
40.774
53.699
1.00
14.17
DIC

ATOM
422
CD
ILE
59
41.413
41.795
52.996
1.00
16.56
DIC

ATOM
423
C
ILE
59
44.133
38.477
54.071
1.00
13.72
DIC

ATOM
424
O
ILE
59
44.418
37.839
53.056
1.00
12.08
DIC

ATOM
425
N
ARG
60
43.456
37.953
55.084
1.00
13.05
DIC

ATOM
426
CA
ARG
60
42.968
36.586
55.031
1.00
12.60
DIC

ATOM
427
CB
ARG
60
43.685
35.730
56.082
1.00
15.76
DIC

ATOM
428
CG
ARG
60
43.217
34.284
56.154
1.00
20.30
DIC

ATOM
429
CD
ARG
60
44.272
33.351
56.769
1.00
24.60
DIC

ATOM
430
NE
ARG
60
44.682
33.733
58.118
1.00
29.24
DIC

ATOM
431
CZ
ARG
60
45.606
34.650
58.398
1.00
31.92
DIC

ATOM
432
NH1
ARG
60
46.232
35.291
57.419
1.00
34.11
DIC

ATOM
433
NH2
ARG
60
45.908
34.926
59.660
1.00
32.11
DIC

ATOM
434
C
ARG
60
41.469
36.596
55.274
1.00
13.28
DIC

ATOM
435
O
ARG
60
40.986
37.219
56.225
1.00
12.52
DIC

ATOM
436
N
PHE
61
40.728
35.932
54.393
1.00
9.98
DIC

ATOM
437
CA
PHE
61
39.283
35.868
54.543
1.00
11.03
DIC

ATOM
438
CB
PHE
61
38.593
35.909
53.180
1.00
10.11
DIC

ATOM
439
CG
PHE
61
38.864
37.165
52.404
1.00
8.69
DIC

ATOM
440
CD1
PHE
61
40.001
37.279
51.611
1.00
10.62
DIC

ATOM
441
CD2
PHE
61
37.984
38.239
52.470
1.00
8.62
DIC

ATOM
442
CE1
PHE
61
40.255
38.444
50.896
1.00
10.15
DIC

ATOM
443
CE2
PHE
61
38.231
39.411
51.757
1.00
10.17
DIC

ATOM
444
CZ
PHE
61
39.368
39.511
50.969
1.00
8.33
DIC

ATOM
445
C
PHE
61
38.949
34.578
55.265
1.00
10.30
DIC

ATOM
446
O
PHE
61
39.474
33.520
54.934
1.00
10.02
DIC

ATOM
447
N
ILE
62
38.080
34.678
56.262
1.00
10.75
DIC

ATOM
448
CA
ILE
62
37.682
33.525
57.053
1.00
10.78
DIC

ATOM
449
CB
ILE
62
37.949
33.791
58.550
1.00
11.91
DIC

ATOM
450
CG2
ILE
62
37.750
32.516
59.358
1.00
9.27
DIC

ATOM
451
CG1
ILE
62
39.380
34.301
58.728
1.00
11.15
DIC

ATOM
452
CD
ILE
62
39.672
34.864
60.108
1.00
13.99
DIC

ATOM
453
C
ILE
62
36.199
33.259
56.829
1.00
11.22
DIC

ATOM
454
O
ILE
62
35.352
34.083
57.172
1.00
8.84
DIC

ATOM
455
N
ASP
63
35.891
32.102
56.249
1.00
12.77
DIC

ATOM
456
CA
ASP
63
34.509
31.743
55.963
1.00
15.03
DIC

ATOM
457
CB
ASP
63
34.450
30.425
55.186
1.00
19.05
DIC

ATOM
458
CG
ASP
63
35.078
30.533
53.815
1.00
22.78
DIC

ATOM
459
OD1
ASP
63
34.633
31.392
53.027
1.00
24.85
DIC

ATOM
460
OD2
ASP
63
36.017
29.762
53.526
1.00
26.44
DIC

ATOM
461
C
ASP
63
33.638
31.624
57.201
1.00
15.28
DIC

ATOM
462
O
ASP
63
33.989
30.943
58.164
1.00
13.87
DIC

ATOM
463
N
VAL
64
32.499
32.301
57.170
1.00
14.42
DIC

ATOM
464
CA
VAL
64
31.558
32.237
58.274
1.00
14.74
DIC

ATOM
465
CB
VAL
64
31.449
33.587
59.025
1.00
15.80
DIC

ATOM
466
CG1
VAL
64
32.778
33.930
59.669
1.00
16.58
DIC

ATOM
467
CG2
VAL
64
31.025
34.684
58.073
1.00
16.06
DIC

ATOM
468
C
VAL
64
30.196
31.865
57.706
1.00
14.22
DIC

ATOM
469
O
VAL
64
29.826
32.308
56.617
1.00
14.84
DIC

ATOM
470
N
ASN
65
29.463
31.033
58.435
1.00
12.47
DIC

ATOM
471
CA
ASN
65
28.137
30.614
58.010
1.00
13.60
DIC

ATOM
472
CB
ASN
65
27.857
29.182
58.476
1.00
14.16
DIC

ATOM
473
CG
ASN
65
26.564
28.624
57.906
1.00
16.61
DIC

ATOM
474
OD1
ASN
65
25.625
29.367
57.620
1.00
16.00
DIC

ATOM
475
ND2
ASN
65
26.505
27.305
57.752
1.00
14.91
DIC

ATOM
476
C
ASN
65
27.123
31.560
58.647
1.00
14.85
DIC

ATOM
477
O
ASN
65
26.895
31.510
59.856
1.00
15.54
DIC

ATOM
478
N
PRO
66
26.509
32.443
57.846
1.00
15.26
DIC

ATOM
479
CD
PRO
66
26.691
32.671
56.401
1.00
15.57
DIC

ATOM
480
CA
PRO
66
25.526
33.376
58.404
1.00
15.89
DIC

ATOM
481
CB
PRO
66
25.166
34.256
57.208
1.00
17.28
DIC

ATOM
482
CG
PRO
66
25.406
33.358
56.029
1.00
16.80
DIC

ATOM
483
C
PRO
66
24.311
32.678
59.019
1.00
15.69
DIC

ATOM
484
O
PRO
66
23.646
33.231
59.893
1.00
16.02
DIC

ATOM
485
N
ALA
67
24.028
31.461
58.568
1.00
14.83
DIC

ATOM
486
CA
ALA
67
22.896
30.713
59.101
1.00
15.30
DIC

ATOM
487
CB
ALA
67
22.749
29.382
58.366
1.00
16.72
DIC

ATOM
488
C
ALA
67
23.082
30.466
60.597
1.00
15.63
DIC

ATOM
489
O
ALA
67
22.112
30.252
61.322
1.00
15.80
DIC

ATOM
490
N
ASP
68
24.330
30.505
61.056
1.00
14.70
DIC

ATOM
491
CA
ASP
68
24.634
30.282
62.466
1.00
15.13
DIC

ATOM
492
CB
ASP
68
26.133
30.478
62.736
1.00
15.76
DIC

ATOM
493
CG
ASP
68
26.987
29.337
62.201
1.00
17.55
DIC

ATOM
494
OD1
ASP
68
28.216
29.367
62.418
1.00
17.24
DIC

ATOM
495
OD2
ASP
68
26.439
28.415
61.570
1.00
18.46
DIC

ATOM
496
C
ASP
68
23.854
31.213
63.391
1.00
14.63
DIC

ATOM
497
O
ASP
68
23.503
30.838
64.507
1.00
15.13
DIC

ATOM
498
N
PHE
69
23.580
32.424
62.923
1.00
13.83
DIC

ATOM
499
CA
PHE
69
22.880
33.406
63.740
1.00
14.98
DIC

ATOM
500
CB
PHE
69
23.691
34.708
63.745
1.00
13.87
DIC

ATOM
501
CG
PHE
69
25.180
34.484
63.681
1.00
14.17
DIC

ATOM
502
CD1
PHE
69
25.823
34.341
62.452
1.00
12.43
DIC

ATOM
503
CD2
PHE
69
25.929
34.355
64.847
1.00
12.05
DIC

ATOM
504
CE1
PHE
69
27.192
34.071
62.385
1.00
13.43
DIC

ATOM
505
CE2
PHE
69
27.297
34.084
64.794
1.00
12.77
DIC

ATOM
506
CZ
PHE
69
27.932
33.941
63.561
1.00
11.69
DIC

ATOM
507
C
PHE
69
21.447
33.672
63.285
1.00
15.85
DIC

ATOM
508
O
PHE
69
20.877
34.719
63.587
1.00
14.86
DIC

ATOM
509
N
ALA
70
20.863
32.708
62.585
1.00
16.36
DIC

ATOM
510
CA
ALA
70
19.502
32.840
62.074
1.00
19.02
DIC

ATOM
511
CB
ALA
70
19.135
31.594
61.269
1.00
20.70
DIC

ATOM
512
C
ALA
70
18.437
33.095
63.143
1.00
19.98
DIC

ATOM
513
O
ALA
70
17.366
33.616
62.840
1.00
22.15
DIC

ATOM
514
N
GLY
71
18.723
32.734
64.388
1.00
18.98
DIC

ATOM
515
CA
GLY
71
17.740
32.935
65.437
1.00
19.23
DIC

ATOM
516
C
GLY
71
17.753
34.294
66.114
1.00
19.37
DIC

ATOM
517
O
GLY
71
16.795
34.653
66.806
1.00
18.55
DIC

ATOM
518
N
PHE
72
18.824
35.056
65.910
1.00
17.12
DIC

ATOM
519
CA
PHE
72
18.959
36.370
66.528
1.00
16.52
DIC

ATOM
520
CB
PHE
72
20.444
36.736
66.627
1.00
17.36
DIC

ATOM
521
CG
PHE
72
21.244
35.800
67.502
1.00
20.69
DIC

ATOM
522
CD1
PHE
72
22.622
35.942
67.615
1.00
20.90
DIC

ATOM
523
CD2
PHE
72
20.616
34.781
68.220
1.00
20.65
DIC

ATOM
524
CE1
PHE
72
23.365
35.084
68.429
1.00
22.32
DIC

ATOM
525
CE2
PHE
72
21.350
33.918
69.036
1.00
21.81
DIC

ATOM
526
CZ
PHE
72
22.728
34.071
69.139
1.00
22.14
DIC

ATOM
527
C
PHE
72
18.182
37.476
65.809
1.00
15.69
DIC

ATOM
528
O
PHE
72
18.062
37.475
64.582
1.00
16.74
DIC

ATOM
529
N
PRO
73
17.644
38.438
66.576
1.00
14.19
DIC

ATOM
530
CD
PRO
73
17.784
38.566
68.037
1.00
14.66
DIC

ATOM
531
CA
PRO
73
16.870
39.558
66.033
1.00
13.58
DIC

ATOM
532
CB
PRO
73
16.430
40.313
67.287
1.00
14.13
DIC

ATOM
533
CG
PRO
73
17.522
40.037
68.251
1.00
14.64
DIC

ATOM
534
C
PRO
73
17.632
40.441
65.053
1.00
13.06
DIC

ATOM
535
O
PRO
73
18.839
40.647
65.183
1.00
11.47
DIC

ATOM
536
N
LEU
74
16.912
40.951
64.061
1.00
12.77
DIC

ATOM
537
CA
LEU
74
17.498
41.819
63.049
1.00
14.73
DIC

ATOM
538
CB
LEU
74
17.807
40.997
61.793
1.00
16.34
DIC

ATOM
539
CG
LEU
74
18.987
41.439
60.926
1.00
18.53
DIC

ATOM
540
CD1
LEU
74
20.262
41.429
61.767
1.00
15.81
DIC

ATOM
541
CD2
LEU
74
19.127
40.503
59.727
1.00
17.94
DIC

ATOM
542
C
LEU
74
16.493
42.935
62.731
1.00
14.70
DIC

ATOM
543
O
LEU
74
16.013
43.048
61.603
1.00
17.35
DIC

ATOM
544
N
ASN
75
16.186
43.758
63.732
1.00
12.80
DIC

ATOM
545
CA
ASN
75
15.222
44.848
63.573
1.00
11.77
DIC

ATOM
546
CB
ASN
75
14.595
45.205
64.934
1.00
13.05
DIC

ATOM
547
CG
ASN
75
15.634
45.441
66.031
1.00
15.54
DIC

ATOM
548
OD1
ASN
75
16.359
44.524
66.427
1.00
14.39
DIC

ATOM
549
ND2
ASN
75
15.699
46.673
66.533
1.00
13.85
DIC

ATOM
550
C
ASN
75
15.741
46.122
62.900
1.00
11.45
DIC

ATOM
551
O
ASN
75
14.947
46.933
62.421
1.00
10.31
DIC

ATOM
552
N
ILE
76
17.059
46.302
62.865
1.00
9.67
DIC

ATOM
553
CA
ILE
76
17.649
47.486
62.242
1.00
8.64
DIC

ATOM
554
CB
ILE
76
18.989
47.859
62.920
1.00
10.45
DIC

ATOM
555
CG2
ILE
76
19.526
49.164
62.336
1.00
10.96
DIC

ATOM
556
CG1
ILE
76
18.771
48.010
64.433
1.00
11.13
DIC

ATOM
557
CD
ILE
76
20.026
48.383
65.224
1.00
10.33
DIC

ATOM
558
C
ILE
76
17.858
47.180
60.761
1.00
6.66
DIC

ATOM
559
O
ILE
76
18.744
46.417
60.386
1.00
6.82
DIC

ATOM
560
N
ARG
77
17.022
47.791
59.929
1.00
6.55
DIC

ATOM
561
CA
ARG
77
17.020
47.565
58.487
1.00
4.60
DIC

ATOM
562
CB
ARG
77
16.009
48.506
57.830
1.00
6.27
DIC

ATOM
563
CG
ARG
77
15.689
48.175
56.373
1.00
7.44
DIC

ATOM
564
CD
ARG
77
14.783
49.243
55.776
1.00
13.42
DIC

ATOM
565
NE
ARG
77
14.442
48.985
54.379
1.00
15.86
DIC

ATOM
566
CZ
ARG
77
14.048
49.925
53.525
1.00
17.42
DIC

ATOM
567
NH1
ARG
77
13.948
51.184
53.927
1.00
18.20
DIC

ATOM
568
NH2
ARG
77
13.755
49.611
52.270
1.00
19.12
DIC

ATOM
569
C
ARG
77
18.341
47.637
57.727
1.00
5.81
DIC

ATOM
570
O
ARG
77
18.598
46.795
56.870
1.00
5.17
DIC

ATOM
571
N
HIS
78
19.182
48.623
58.022
1.00
6.00
DIC

ATOM
572
CA
HIS
78
20.440
48.744
57.287
1.00
9.02
DIC

ATOM
573
CB
HIS
78
20.979
50.175
57.389
1.00
10.15
DIC

ATOM
574
CG
HIS
78
21.474
50.544
58.751
1.00
9.33
DIC

ATOM
575
CD2
HIS
78
20.848
51.131
59.797
1.00
6.75
DIC

ATOM
576
ND1
HIS
78
22.765
50.293
59.168
1.00
11.81
DIC

ATOM
577
CE1
HIS
78
22.911
50.712
60.412
1.00
8.70
DIC

ATOM
578
NE2
HIS
78
21.762
51.224
60.817
1.00
11.84
DIC

ATOM
579
C
HIS
78
21.509
47.751
57.734
1.00
8.20
DIC

ATOM
580
O
HIS
78
22.624
47.761
57.219
1.00
7.53
DIC

ATOM
581
N
ILE
79
21.162
46.872
58.669
1.00
7.37
DIC

ATOM
582
CA
ILE
79
22.129
45.895
59.158
1.00
7.68
DIC

ATOM
583
CB
ILE
79
22.262
45.979
60.687
1.00
5.65
DIC

ATOM
584
CG2
ILE
79
23.256
44.932
61.180
1.00
4.12
DIC

ATOM
585
CG1
ILE
79
22.715
47.384
61.083
1.00
4.91
DIC

ATOM
586
CD
ILE
79
22.696
47.634
62.575
1.00
5.56
DIC

ATOM
587
C
ILE
79
21.794
44.460
58.783
1.00
8.61
DIC

ATOM
588
O
ILE
79
20.693
43.983
59.046
1.00
9.77
DIC

ATOM
589
N
SER
80
22.752
43.773
58.169
1.00
9.76
DIC

ATOM
590
CA
SER
80
22.561
42.379
57.774
1.00
8.74
DIC

ATOM
591
CB
SER
80
23.402
42.050
56.541
1.00
8.44
DIC

ATOM
592
OG
SER
80
24.781
42.091
56.852
1.00
8.55
DIC

ATOM
593
C
SER
80
22.973
41.462
58.927
1.00
9.00
DIC

ATOM
594
O
SER
80
23.580
41.913
59.903
1.00
8.52
DIC

ATOM
595
N
ILE
81
22.637
40.181
58.800
1.00
8.69
DIC

ATOM
596
CA
ILE
81
22.932
39.167
59.814
1.00
9.32
DIC

ATOM
597
CB
ILE
81
22.342
37.793
59.391
1.00
11.01
DIC

ATOM
598
CG2
ILE
81
23.127
37.231
58.211
1.00
12.45
DIC

ATOM
599
CG1
ILE
81
22.387
36.802
60.557
1.00
13.43
DIC

ATOM
600
CD
ILE
81
21.500
37.182
61.726
1.00
16.17
DIC

ATOM
601
C
ILE
81
24.433
39.007
60.082
1.00
8.61
DIC

ATOM
602
O
ILE
81
24.831
38.496
61.123
1.00
9.44
DIC

ATOM
603
N
THR
82
25.259
39.450
59.144
1.00
8.29
DIC

ATOM
604
CA
THR
82
26.711
39.346
59.290
1.00
9.90
DIC

ATOM
605
CB
THR
82
27.416
39.899
58.032
1.00
9.68
DIC

ATOM
606
OG1
THR
82
27.081
39.078
56.908
1.00
11.57
DIC

ATOM
607
CG2
THR
82
28.924
39.902
58.208
1.00
11.14
DIC

ATOM
608
C
THR
82
27.226
40.083
60.532
1.00
9.31
DIC

ATOM
609
O
THR
82
28.308
39.784
61.044
1.00
11.54
DIC

ATOM
610
N
THR
83
26.442
41.044
61.007
1.00
7.10
DIC

ATOM
611
CA
THR
83
26.793
41.843
62.178
1.00
6.02
DIC

ATOM
612
CB
THR
83
25.681
42.891
62.460
1.00
4.53
DIC

ATOM
613
OG1
THR
83
26.153
43.855
63.407
1.00
3.63
DIC

ATOM
614
CG2
THR
83
24.428
42.217
63.004
1.00
2.50
DIC

ATOM
615
C
THR
83
27.028
40.992
63.439
1.00
5.43
DIC

ATOM
616
O
THR
83
27.686
41.435
64.389
1.00
2.82
DIC

ATOM
617
N
TYR
84
26.490
39.775
63.442
1.00
4.36
DIC

ATOM
618
CA
TYR
84
26.636
38.865
64.579
1.00
4.81
DIC

ATOM
619
CB
TYR
84
25.399
37.962
64.707
1.00
5.98
DIC

ATOM
620
CG
TYR
84
24.158
38.632
65.252
1.00
5.88
DIC

ATOM
621
CD1
TYR
84
23.083
38.948
64.415
1.00
7.00
DIC

ATOM
622
CE1
TYR
84
21.922
39.534
64.921
1.00
7.41
DIC

ATOM
623
CD2
TYR
84
24.040
38.920
66.611
1.00
6.51
DIC

ATOM
624
CE2
TYR
84
22.882
39.503
67.129
1.00
6.56
DIC

ATOM
625
CZ
TYR
84
21.829
39.805
66.277
1.00
7.16
DIC

ATOM
626
OH
TYR
84
20.682
40.370
66.782
1.00
7.35
DIC

ATOM
627
C
TYR
84
27.872
37.966
64.507
1.00
5.01
DIC

ATOM
628
O
TYR
84
28.228
37.317
65.497
1.00
6.35
DIC

ATOM
629
N
ALA
85
28.524
37.923
63.350
1.00
4.75
DIC

ATOM
630
CA
ALA
85
29.697
37.068
63.174
1.00
5.04
DIC

ATOM
631
CB
ALA
85
30.266
37.240
61.765
1.00
5.81
DIC

ATOM
632
C
ALA
85
30.788
37.323
64.211
1.00
4.45
DIC

ATOM
633
O
ALA
85
31.506
36.409
64.601
1.00
3.97
DIC

ATOM
634
N
ARG
86
30.899
38.566
64.663
1.00
5.28
DIC

ATOM
635
CA
ARG
86
31.918
38.932
65.636
1.00
6.46
DIC

ATOM
636
CB
ARG
86
31.830
40.436
65.927
1.00
6.54
DIC

ATOM
637
CG
ARG
86
30.578
40.885
66.662
1.00
7.60
DIC

ATOM
638
CD
ARG
86
30.479
42.411
66.665
1.00
6.22
DIC

ATOM
639
NE
ARG
86
29.753
42.918
65.502
1.00
7.60
DIC

ATOM
640
CZ
ARG
86
29.592
44.209
65.223
1.00
8.07
DIC

ATOM
641
NH1
ARG
86
30.121
45.135
66.016
1.00
6.32
DIC

ATOM
642
NH2
ARG
86
28.866
44.578
64.173
1.00
6.28
DIC

ATOM
643
C
ARG
86
31.834
38.123
66.933
1.00
6.26
DIC

ATOM
644
O
ARG
86
32.825
37.970
67.642
1.00
5.75
DIC

ATOM
645
N
LEU
87
30.654
37.594
67.231
1.00
6.67
DIC

ATOM
646
CA
LEU
87
30.453
36.800
68.444
1.00
9.15
DIC

ATOM
647
CB
LEU
87
28.978
36.423
68.579
1.00
9.79
DIC

ATOM
648
CG
LEU
87
27.968
37.573
68.662
1.00
10.81
DIC

ATOM
649
CD1
LEU
87
26.565
36.998
68.625
1.00
10.16
DIC

ATOM
650
CD2
LEU
87
28.186
38.385
69.928
1.00
9.69
DIC

ATOM
651
C
LEU
87
31.309
35.531
68.500
1.00
8.69
DIC

ATOM
652
O
LEU
87
31.663
35.069
69.583
1.00
8.91
DIC

ATOM
653
N
LYS
88
31.633
34.964
67.337
1.00
9.25
DIC

ATOM
654
CA
LYS
88
32.453
33.749
67.269
1.00
7.47
DIC

ATOM
655
CB
LYS
88
31.882
32.787
66.215
1.00
8.55
DIC

ATOM
656
CG
LYS
88
30.591
32.084
66.618
1.00
5.05
DIC

ATOM
657
CD
LYS
88
30.239
31.000
65.605
1.00
9.57
DIC

ATOM
658
CE
LYS
88
29.127
30.091
66.111
1.00
11.92
DIC

ATOM
659
NZ
LYS
88
28.966
28.889
65.234
1.00
9.27
DIC

ATOM
660
C
LYS
88
33.921
34.034
66.932
1.00
8.56
DIC

ATOM
661
O
LYS
88
34.635
33.166
66.426
1.00
7.98
DIC

ATOM
662
N
LEU
89
34.374
35.247
67.221
1.00
8.21
DIC

ATOM
663
CA
LEU
89
35.746
35.638
66.924
1.00
9.63
DIC

ATOM
664
CB
LEU
89
35.968
37.079
67.392
1.00
11.64
DIC

ATOM
665
CG
LEU
89
36.996
37.961
66.683
1.00
15.58
DIC

ATOM
666
CD1
LEU
89
36.916
37.802
65.176
1.00
14.23
DIC

ATOM
667
CD2
LEU
89
36.731
39.405
67.074
1.00
15.43
DIC

ATOM
668
C
LEU
89
36.760
34.688
67.564
1.00
10.10
DIC

ATOM
669
O
LEU
89
37.825
34.423
66.998
1.00
10.90
DIC

ATOM
670
N
GLY
90
36.420
34.165
68.738
1.00
8.62
DIC

ATOM
671
CA
GLY
90
37.306
33.238
69.422
1.00
9.71
DIC

ATOM
672
C
GLY
90
37.439
31.920
68.679
1.00
10.61
DIC

ATOM
673
O
GLY
90
38.417
31.195
68.858
1.00
9.41
DIC

ATOM
674
N
GLU
91
36.447
31.607
67.848
1.00
9.92
DIC

ATOM
675
CA
GLU
91
36.453
30.379
67.058
1.00
11.25
DIC

ATOM
676
CB
GLU
91
35.022
29.875
66.839
1.00
14.13
DIC

ATOM
677
CG
GLU
91
34.281
29.413
68.084
1.00
17.36
DIC

ATOM
678
CD
GLU
91
32.897
28.871
67.750
1.00
20.17
DIC

ATOM
679
OE1
GLU
91
32.791
28.072
66.794
1.00
19.66
DIC

ATOM
680
OE2
GLU
91
31.921
29.234
68.441
1.00
19.51
DIC

ATOM
681
C
GLU
91
37.093
30.594
65.683
1.00
11.62
DIC

ATOM
682
O
GLU
91
37.663
29.664
65.100
1.00
11.92
DIC

ATOM
683
N
TYR
92
36.989
31.819
65.173
1.00
10.48
DIC

ATOM
684
CA
TYR
92
37.516
32.165
63.854
1.00
10.15
DIC

ATOM
685
CB
TYR
92
36.725
33.331
63.253
1.00
9.65
DIC

ATOM
686
CG
TYR
92
35.244
33.078
63.086
1.00
11.40
DIC

ATOM
687
CD1
TYR
92
34.774
31.872
62.568
1.00
10.51
DIC

ATOM
688
CE1
TYR
92
33.411
31.655
62.371
1.00
13.36
DIC

ATOM
689
CD2
TYR
92
34.312
34.066
63.406
1.00
11.86
DIC

ATOM
690
CE2
TYR
92
32.948
33.861
63.211
1.00
13.22
DIC

ATOM
691
CZ
TYR
92
32.505
32.654
62.695
1.00
14.23
DIC

ATOM
692
OH
TYR
92
31.159
32.447
62.507
1.00
12.62
DIC

ATOM
693
C
TYR
92
38.992
32.518
63.776
1.00
10.04
DIC

ATOM
694
O
TYR
92
39.601
32.361
62.723
1.00
9.17
DIC

ATOM
695
N
ILE
93
39.563
33.014
64.870
1.00
11.91
DIC

ATOM
696
CA
ILE
93
40.971
33.405
64.886
1.00
13.98
DIC

ATOM
697
CB
ILE
93
41.122
34.938
65.044
1.00
15.92
DIC

ATOM
698
CG2
ILE
93
42.597
35.318
65.098
1.00
14.58
DIC

ATOM
699
CG1
ILE
93
40.441
35.650
63.872
1.00
16.29
DIC

ATOM
700
CD
ILE
93
40.462
37.154
63.985
1.00
14.93
DIC

ATOM
701
C
ILE
93
41.728
32.721
66.018
1.00
15.16
DIC

ATOM
702
O
ILE
93
41.350
32.830
67.185
1.00
14.37
DIC

ATOM
703
N
ALA
94
42.804
32.028
65.663
1.00
14.83
DIC

ATOM
704
CA
ALA
94
43.608
31.305
66.639
1.00
19.11
DIC

ATOM
705
CB
ALA
94
43.703
29.845
66.231
1.00
19.20
DIC

ATOM
706
C
ALA
94
45.013
31.871
66.836
1.00
19.59
DIC

ATOM
707
O
ALA
94
45.592
31.747
67.915
1.00
20.84
DIC

ATOM
708
N
ASP
95
45.552
32.493
65.794
1.00
21.87
DIC

ATOM
709
CA
ASP
95
46.905
33.044
65.831
1.00
23.46
DIC

ATOM
710
CB
ASP
95
47.409
33.251
64.397
1.00
26.41
DIC

ATOM
711
CG
ASP
95
46.424
34.024
63.537
1.00
29.30
DIC

ATOM
712
OD1
ASP
95
46.717
34.258
62.344
1.00
32.19
DIC

ATOM
713
OD2
ASP
95
45.351
34.398
64.050
1.00
33.42
DIC

ATOM
714
C
ASP
95
47.115
34.332
66.626
1.00
22.72
DIC

ATOM
715
O
ASP
95
48.257
34.737
66.851
1.00
24.34
DIC

ATOM
716
N
CYS
96
46.036
34.968
67.069
1.00
21.07
DIC

ATOM
717
CA
CYS
96
46.168
36.221
67.811
1.00
19.00
DIC

ATOM
718
CB
CYS
96
45.485
37.356
67.043
1.00
17.51
DIC

ATOM
719
SG
CYS
96
46.000
37.495
65.337
1.00
17.81
DIC

ATOM
720
C
CYS
96
45.603
36.192
69.223
1.00
17.30
DIC

ATOM
721
O
CYS
96
44.532
35.636
69.459
1.00
18.98
DIC

ATOM
722
N
ASP
97
46.326
36.804
70.155
1.00
15.20
DIC

ATOM
723
CA
ASP
97
45.879
36.886
71.540
1.00
15.33
DIC

ATOM
724
CB
ASP
97
47.070
36.957
72.495
1.00
16.39
DIC

ATOM
725
CG
ASP
97
47.696
35.605
72.741
1.00
17.76
DIC

ATOM
726
OD1
ASP
97
48.786
35.559
73.347
1.00
22.14
DIC

ATOM
727
OD2
ASP
97
47.091
34.590
72.335
1.00
18.91
DIC

ATOM
728
C
ASP
97
45.041
38.146
71.689
1.00
14.04
DIC

ATOM
729
O
ASP
97
44.289
38.297
72.652
1.00
13.55
DIC

ATOM
730
N
ALA
98
45.192
39.051
70.728
1.00
12.61
DIC

ATOM
731
CA
ALA
98
44.457
40.309
70.727
1.00
12.75
DIC

ATOM
732
CB
ALA
98
45.220
41.362
71.513
1.00
14.90
DIC

ATOM
733
C
ALA
98
44.243
40.786
69.299
1.00
10.95
DIC

ATOM
734
O
ALA
98
45.130
40.664
68.456
1.00
10.19
DIC

ATOM
735
N
VAL
99
43.055
41.317
69.032
1.00
9.01
DIC

ATOM
736
CA
VAL
99
42.726
41.827
67.710
1.00
8.36
DIC

ATOM
737
CB
VAL
99
41.911
40.801
66.883
1.00
7.71
DIC

ATOM
738
CG1
VAL
99
42.761
39.579
66.590
1.00
4.15
DIC

ATOM
739
CG2
VAL
99
40.639
40.407
67.637
1.00
5.20
DIC

ATOM
740
C
VAL
99
41.902
43.090
67.862
1.00
8.06
DIC

ATOM
741
O
VAL
99
41.233
43.282
68.877
1.00
8.30
DIC

ATOM
742
N
LEU
100
41.965
43.961
66.864
1.00
6.36
DIC

ATOM
743
CA
LEU
100
41.193
45.193
66.905
1.00
5.80
DIC

ATOM
744
CB
LEU
100
42.084
46.407
66.611
1.00
5.45
DIC

ATOM
745
CG
LEU
100
41.418
47.790
66.524
1.00
8.26
DIC

ATOM
746
CD1
LEU
100
40.403
47.975
67.641
1.00
6.61
DIC

ATOM
747
CD2
LEU
100
42.492
48.867
66.602
1.00
8.45
DIC

ATOM
748
C
LEU
100
40.092
45.086
65.867
1.00
5.59
DIC

ATOM
749
O
LEU
100
40.352
45.145
64.663
1.00
5.35
DIC

ATOM
750
N
TYR
101
38.864
44.910
66.343
1.00
4.71
DIC

ATOM
751
CA
TYR
101
37.720
44.795
65.462
1.00
5.45
DIC

ATOM
752
CB
TYR
101
36.624
43.930
66.105
1.00
7.22
DIC

ATOM
753
CG
TYR
101
35.306
44.030
65.366
1.00
6.26
DIC

ATOM
754
CD1
TYR
101
34.459
45.119
65.565
1.00
10.55
DIC

ATOM
755
CE1
TYR
101
33.308
45.290
64.805
1.00
11.37
DIC

ATOM
756
CD2
TYR
101
34.957
43.099
64.390
1.00
9.90
DIC

ATOM
757
CE2
TYR
101
33.799
43.261
63.622
1.00
10.47
DIC

ATOM
758
CZ
TYR
101
32.987
44.361
63.834
1.00
10.64
DIC

ATOM
759
OH
TYR
101
31.868
44.565
63.051
1.00
16.19
DIC

ATOM
760
C
TYR
101
37.142
46.160
65.101
1.00
5.61
DIC

ATOM
761
O
TYR
101
36.947
47.020
65.968
1.00
4.16
DIC

ATOM
762
N
LEU
102
36.857
46.339
63.816
1.00
4.05
DIC

ATOM
763
CA
LEU
102
36.279
47.580
63.314
1.00
4.38
DIC

ATOM
764
CB
LEU
102
37.295
48.338
62.462
1.00
4.30
DIC

ATOM
765
CG
LEU
102
38.591
48.754
63.147
1.00
7.19
DIC

ATOM
766
CD1
LEU
102
39.510
49.400
62.128
1.00
6.72
DIC

ATOM
767
CD2
LEU
102
38.276
49.714
64.293
1.00
3.87
DIC

ATOM
768
C
LEU
102
35.061
47.286
62.451
1.00
4.47
DIC

ATOM
769
O
LEU
102
35.034
46.284
61.733
1.00
4.61
DIC

ATOM
770
N
ASP
103
34.054
48.153
62.534
1.00
3.95
DIC

ATOM
771
CA
ASP
103
32.860
48.016
61.715
1.00
4.24
DIC

ATOM
772
CB
ASP
103
31.761
48.979
62.177
1.00
2.65
DIC

ATOM
773
CG
ASP
103
30.737
48.327
63.095
1.00
2.68
DIC

ATOM
774
OD1
ASP
103
29.754
49.012
63.436
1.00
4.76
DIC

ATOM
775
OD2
ASP
103
30.897
47.152
63.482
1.00
3.70
DIC

ATOM
776
C
ASP
103
33.328
48.428
60.320
1.00
5.01
DIC

ATOM
777
O
ASP
103
34.417
48.975
60.169
1.00
3.63
DIC

ATOM
778
N
ILE
104
32.507
48.184
59.310
1.00
6.60
DIC

ATOM
779
CA
ILE
104
32.867
48.531
57.935
1.00
5.92
DIC

ATOM
780
CB
ILE
104
32.014
47.723
56.933
1.00
6.60
DIC

ATOM
781
CG2
ILE
104
32.269
48.202
55.505
1.00
5.47
DIC

ATOM
782
CG1
ILE
104
32.308
46.229
57.092
1.00
6.21
DIC

ATOM
783
CD
ILE
104
33.753
45.837
56.829
1.00
6.76
DIC

ATOM
784
C
ILE
104
32.675
50.018
57.655
1.00
6.14
DIC

ATOM
785
O
ILE
104
33.386
50.610
56.838
1.00
6.24
DIC

ATOM
786
N
ASP
105
31.712
50.618
58.344
1.00
4.96
DIC

ATOM
787
CA
ASP
105
31.399
52.028
58.167
1.00
5.98
DIC

ATOM
788
CB
ASP
105
29.930
52.274
58.513
1.00
4.82
DIC

ATOM
789
CG
ASP
105
29.609
51.925
59.956
1.00
3.16
DIC

ATOM
790
OD1
ASP
105
30.337
51.092
60.532
1.00
2.79
DIC

ATOM
791
OD2
ASP
105
28.627
52.466
60.507
1.00
5.38
DIC

ATOM
792
C
ASP
105
32.286
52.943
59.009
1.00
6.62
DIC

ATOM
793
O
ASP
105
31.790
53.838
59.693
1.00
6.81
DIC

ATOM
794
N
VAL
106
33.594
52.710
58.966
1.00
7.03
DIC

ATOM
795
CA
VAL
106
34.536
53.540
59.706
1.00
7.28
DIC

ATOM
796
CB
VAL
106
35.300
52.752
60.801
1.00
8.49
DIC

ATOM
797
CG1
VAL
106
34.321
52.057
61.732
1.00
7.70
DIC

ATOM
798
CG2
VAL
106
36.257
51.754
60.156
1.00
8.17
DIC

ATOM
799
C
VAL
106
35.575
54.126
58.761
1.00
6.79
DIC

ATOM
800
O
VAL
106
35.848
53.586
57.684
1.00
5.38
DIC

ATOM
801
N
LEU
107
36.151
55.243
59.180
1.00
7.44
DIC

ATOM
802
CA
LEU
107
37.179
55.916
58.410
1.00
9.27
DIC

ATOM
803
CB
LEU
107
36.598
57.173
57.756
1.00
11.52
DIC

ATOM
804
CG
LEU
107
36.654
57.330
56.232
1.00
15.69
DIC

ATOM
805
CD1
LEU
107
36.132
56.088
55.542
1.00
17.09
DIC

ATOM
806
CD2
LEU
107
35.829
58.543
55.834
1.00
16.31
DIC

ATOM
807
C
LEU
107
38.239
56.284
59.441
1.00
8.22
DIC

ATOM
808
O
LEU
107
38.038
57.190
60.241
1.00
8.43
DIC

ATOM
809
N
VAL
108
39.346
55.548
59.447
1.00
9.38
DIC

ATOM
810
CA
VAL
108
40.429
55.812
60.390
1.00
9.80
DIC

ATOM
811
CB
VAL
108
41.415
54.627
60.456
1.00
8.32
DIC

ATOM
812
CG1
VAL
108
42.534
54.927
61.462
1.00
7.62
DIC

ATOM
813
CG2
VAL
108
40.667
53.368
60.857
1.00
8.96
DIC

ATOM
814
C
VAL
108
41.165
57.056
59.926
1.00
11.09
DIC

ATOM
815
O
VAL
108
41.661
57.100
58.801
1.00
11.19
DIC

ATOM
816
N
ARG
109
41.234
58.061
60.794
1.00
11.01
DIC

ATOM
817
CA
ARG
109
41.879
59.327
60.453
1.00
12.38
DIC

ATOM
818
CB
ARG
109
40.927
60.487
60.743
1.00
14.98
DIC

ATOM
819
CG
ARG
109
39.453
60.116
60.700
1.00
19.75
DIC

ATOM
820
CD
ARG
109
38.650
61.137
59.922
1.00
23.34
DIC

ATOM
821
NE
ARG
109
39.023
62.512
60.241
1.00
26.83
DIC

ATOM
822
CZ
ARG
109
38.634
63.568
59.529
1.00
28.43
DIC

ATOM
823
NH1
ARG
109
39.017
64.789
59.879
1.00
28.45
DIC

ATOM
824
NH2
ARG
109
37.862
63.400
58.462
1.00
27.61
DIC

ATOM
825
C
ARG
109
43.197
59.582
61.181
1.00
12.26
DIC

ATOM
826
O
ARG
109
43.930
60.511
60.836
1.00
12.24
DIC

ATOM
827
N
ASP
110
43.484
58.780
62.201
1.00
10.65
DIC

ATOM
828
CA
ASP
110
44.723
58.934
62.954
1.00
10.25
DIC

ATOM
829
CB
ASP
110
44.519
59.891
64.140
1.00
11.53
DIC

ATOM
830
CG
ASP
110
45.831
60.491
64.648
1.00
16.88
DIC

ATOM
831
OD1
ASP
110
46.727
60.759
63.819
1.00
17.49
DIC

ATOM
832
OD2
ASP
110
45.962
60.717
65.873
1.00
16.60
DIC

ATOM
833
C
ASP
110
45.160
57.560
63.436
1.00
10.59
DIC

ATOM
834
O
ASP
110
44.371
56.613
63.457
1.00
9.32
DIC

ATOM
835
N
ARG
111
46.426
57.455
63.817
1.00
10.81
DIC

ATOM
836
CA
ARG
111
46.983
56.199
64.279
1.00
9.88
DIC

ATOM
837
CB
ARG
111
48.427
56.420
64.706
1.00
13.67
DIC

ATOM
838
CG
ARG
111
49.043
55.233
65.361
1.00
12.82
DIC

ATOM
839
CD
ARG
111
49.542
55.638
66.719
1.00
24.99
DIC

ATOM
840
NE
ARG
111
50.595
56.646
66.660
1.00
28.05
DIC

ATOM
841
CZ
ARG
111
51.187
57.155
67.733
1.00
29.20
DIC

ATOM
842
NH1
ARG
111
50.825
56.747
68.943
1.00
29.64
DIC

ATOM
843
NH2
ARG
111
52.141
58.069
67.597
1.00
32.61
DIC

ATOM
844
C
ARG
111
46.201
55.533
65.410
1.00
9.74
DIC

ATOM
845
O
ARG
111
45.718
56.189
66.330
1.00
6.00
DIC

ATOM
846
N
LEU
112
46.097
54.211
65.330
1.00
7.64
DIC

ATOM
847
CA
LEU
112
45.381
53.419
66.322
1.00
7.15
DIC

ATOM
848
CB
LEU
112
44.572
52.328
65.613
1.00
7.72
DIC

ATOM
849
CG
LEU
112
43.132
52.585
65.149
1.00
11.87
DIC

ATOM
850
CD1
LEU
112
42.820
54.067
65.067
1.00
11.31
DIC

ATOM
851
CD2
LEU
112
42.934
51.891
63.815
1.00
12.19
DIC

ATOM
852
C
LEU
112
46.294
52.759
67.358
1.00
6.68
DIC

ATOM
853
O
LEU
112
45.812
52.069
68.256
1.00
5.47
DIC

ATOM
854
N
THR
113
47.601
52.968
67.262
1.00
6.84
DIC

ATOM
855
CA
THR
113
48.491
52.305
68.211
1.00
9.74
DIC

ATOM
856
CB
THR
113
49.982
52.542
67.867
1.00
13.43
DIC

ATOM
857
OG1
THR
113
50.395
53.834
68.316
1.00
20.21
DIC

ATOM
858
CG2
THR
113
50.191
52.430
66.366
1.00
9.16
DIC

ATOM
859
C
THR
113
48.233
52.627
69.686
1.00
9.89
DIC

ATOM
860
O
THR
113
48.456
51.780
70.549
1.00
10.39
DIC

ATOM
861
N
PRO
114
47.763
53.847
70.005
1.00
10.53
DIC

ATOM
862
CD
PRO
114
47.662
55.093
69.228
1.00
10.25
DIC

ATOM
863
CA
PRO
114
47.521
54.104
71.428
1.00
9.66
DIC

ATOM
864
CB
PRO
114
47.058
55.558
71.440
1.00
10.92
DIC

ATOM
865
CG
PRO
114
47.832
56.151
70.300
1.00
12.85
DIC

ATOM
866
C
PRO
114
46.445
53.146
71.932
1.00
8.05
DIC

ATOM
867
O
PRO
114
46.529
52.620
73.039
1.00
6.80
DIC

ATOM
868
N
LEU
115
45.432
52.918
71.103
1.00
7.04
DIC

ATOM
869
CA
LEU
115
44.353
52.008
71.467
1.00
8.26
DIC

ATOM
870
CB
LEU
115
43.193
52.130
70.472
1.00
6.84
DIC

ATOM
871
CG
LEU
115
42.014
51.170
70.661
1.00
8.47
DIC

ATOM
872
CD1
LEU
115
41.399
51.358
72.036
1.00
8.73
DIC

ATOM
873
CD2
LEU
115
40.980
51.430
69.568
1.00
11.14
DIC

ATOM
874
C
LEU
115
44.897
50.582
71.471
1.00
5.85
DIC

ATOM
875
O
LEU
115
44.663
49.821
72.407
1.00
10.05
DIC

ATOM
876
N
TRP
116
45.634
50.238
70.422
1.00
6.30
DIC

ATOM
877
CA
TRP
116
46.233
48.914
70.284
1.00
7.03
DIC

ATOM
878
CB
TRP
116
47.005
48.836
68.962
1.00
5.84
DIC

ATOM
879
CG
TRP
116
47.720
47.527
68.737
1.00
8.60
DIC

ATOM
880
CD2
TRP
116
47.120
46.266
68.423
1.00
7.22
DIC

ATOM
881
CE2
TRP
116
48.165
45.319
68.322
1.00
8.24
DIC

ATOM
882
CE3
TRP
116
45.797
45.841
68.221
1.00
7.76
DIC

ATOM
883
CD1
TRP
116
49.067
47.303
68.810
1.00
8.45
DIC

ATOM
884
NE1
TRP
116
49.342
45.980
68.562
1.00
8.62
DIC

ATOM
885
CZ2
TRP
116
47.933
43.973
68.024
1.00
7.56
DIC

ATOM
886
CZ3
TRP
116
45.565
44.501
67.923
1.00
9.68
DIC

ATOM
887
CH2
TRP
116
46.632
43.581
67.829
1.00
9.41
DIC

ATOM
888
C
TRP
116
47.165
48.584
71.455
1.00
8.65
DIC

ATOM
889
O
TRP
116
47.199
47.448
71.926
1.00
8.41
DIC

ATOM
890
N
ASP
117
47.907
49.582
71.932
1.00
10.05
DIC

ATOM
891
CA
ASP
117
48.841
49.373
73.038
1.00
10.53
DIC

ATOM
892
CB
ASP
117
49.912
50.474
73.063
1.00
9.66
DIC

ATOM
893
CG
ASP
117
50.846
50.423
71.863
1.00
12.25
DIC

ATOM
894
OD1
ASP
117
51.014
49.337
71.266
1.00
8.12
DIC

ATOM
895
OD2
ASP
117
51.434
51.476
71.529
1.00
10.94
DIC

ATOM
896
C
ASP
117
48.168
49.313
74.409
1.00
12.03
DIC

ATOM
897
O
ASP
117
48.827
49.044
75.415
1.00
11.16
DIC

ATOM
898
N
THR
118
46.862
49.564
74.457
1.00
12.84
DIC

ATOM
899
CA
THR
118
46.141
49.536
75.727
1.00
13.69
DIC

ATOM
900
CB
THR
118
44.652
49.929
75.542
1.00
13.94
DIC

ATOM
901
OG1
THR
118
44.568
51.266
75.027
1.00
13.81
DIC

ATOM
902
CG2
THR
118
43.913
49.864
76.871
1.00
13.09
DIC

ATOM
903
C
THR
118
46.212
48.148
76.359
1.00
15.13
DIC

ATOM
904
O
THR
118
46.004
47.137
75.683
1.00
13.70
DIC

ATOM
905
N
ASP
119
46.523
48.102
77.652
1.00
16.15
DIC

ATOM
906
CA
ASP
119
46.608
46.831
78.368
1.00
18.15
DIC

ATOM
907
CB
ASP
119
47.565
46.945
79.557
1.00
22.51
DIC

ATOM
908
CG
ASP
119
47.891
45.597
80.177
1.00
26.80
DIC

ATOM
909
OD1
ASP
119
46.976
44.757
80.303
1.00
29.43
DIC

ATOM
910
OD2
ASP
119
49.064
45.378
80.549
1.00
32.86
DIC

ATOM
911
C
ASP
119
45.208
46.483
78.869
1.00
17.06
DIC

ATOM
912
O
ASP
119
44.670
47.164
79.740
1.00
16.61
DIC

ATOM
913
N
LEU
120
44.628
45.424
78.314
1.00
15.39
DIC

ATOM
914
CA
LEU
120
43.281
44.997
78.681
1.00
15.18
DIC

ATOM
915
CB
LEU
120
42.688
44.134
77.562
1.00
14.33
DIC

ATOM
916
CG
LEU
120
42.345
44.801
76.223
1.00
13.88
DIC

ATOM
917
CD1
LEU
120
43.564
45.510
75.668
1.00
17.27
DIC

ATOM
918
CD2
LEU
120
41.852
43.749
75.243
1.00
12.16
DIC

ATOM
919
C
LEU
120
43.205
44.227
79.998
1.00
15.94
DIC

ATOM
920
O
LEU
120
42.117
44.031
80.541
1.00
16.09
DIC

ATOM
921
N
GLY
121
44.349
43.789
80.513
1.00
15.28
DIC

ATOM
922
CA
GLY
121
44.329
43.033
81.752
1.00
16.86
DIC

ATOM
923
C
GLY
121
43.407
41.838
81.581
1.00
17.04
DIC

ATOM
924
O
GLY
121
43.440
41.174
80.542
1.00
16.37
DIC

ATOM
925
N
ASN
122
42.575
41.563
82.578
1.00
16.91
DIC

ATOM
926
CA
ASN
122
41.659
40.433
82.486
1.00
17.19
DIC

ATOM
927
CB
ASN
122
41.549
39.714
83.835
1.00
20.20
DIC

ATOM
928
CG
ASN
122
40.814
38.386
83.729
1.00
23.09
DIC

ATOM
929
OD1
ASN
122
41.147
37.543
82.892
1.00
25.09
DIC

ATOM
930
ND2
ASN
122
39.813
38.193
84.582
1.00
25.01
DIC

ATOM
931
C
ASN
122
40.275
40.868
82.014
1.00
15.72
DIC

ATOM
932
O
ASN
122
39.290
40.151
82.204
1.00
14.86
DIC

ATOM
933
N
ASN
123
40.201
42.053
81.415
1.00
13.48
DIC

ATOM
934
CA
ASN
123
38.937
42.556
80.891
1.00
12.64
DIC

ATOM
935
CB
ASN
123
39.026
44.057
80.579
1.00
12.19
DIC

ATOM
936
CG
ASN
123
39.078
44.921
81.831
1.00
15.92
DIC

ATOM
937
OD1
ASN
123
40.093
45.563
82.122
1.00
15.70
DIC

ATOM
938
ND2
ASN
123
37.983
44.940
82.576
1.00
13.08
DIC

ATOM
939
C
ASN
123
38.657
41.791
79.600
1.00
11.07
DIC

ATOM
940
O
ASN
123
39.582
41.276
78.971
1.00
10.73
DIC

ATOM
941
N
TRP
124
37.386
41.721
79.212
1.00
11.13
DIC

ATOM
942
CA
TRP
124
36.988
41.025
77.991
1.00
8.79
DIC

ATOM
943
CB
TRP
124
35.477
40.814
77.965
1.00
9.02
DIC

ATOM
944
CG
TRP
124
34.945
39.904
79.021
1.00
9.43
DIC

ATOM
945
CD2
TRP
124
34.870
38.478
78.954
1.00
9.01
DIC

ATOM
946
CE2
TRP
124
34.238
38.035
80.140
1.00
9.81
DIC

ATOM
947
CE3
TRP
124
35.274
37.527
78.005
1.00
8.70
DIC

ATOM
948
CD1
TRP
124
34.378
40.264
80.213
1.00
9.23
DIC

ATOM
949
NE1
TRP
124
33.947
39.145
80.890
1.00
9.23
DIC

ATOM
950
CZ2
TRP
124
33.997
36.681
80.401
1.00
9.69
DIC

ATOM
951
CZ3
TRP
124
35.033
36.179
78.266
1.00
9.36
DIC

ATOM
952
CH2
TRP
124
34.400
35.772
79.456
1.00
9.63
DIC

ATOM
953
C
TRP
124
37.381
41.804
76.735
1.00
8.82
DIC

ATOM
954
O
TRP
124
37.742
41.218
75.712
1.00
7.06
DIC

ATOM
955
N
LEU
125
37.294
43.125
76.812
1.00
7.98
DIC

ATOM
956
CA
LEU
125
37.630
43.966
75.669
1.00
9.33
DIC

ATOM
957
CB
LEU
125
36.580
43.793
74.563
1.00
7.77
DIC

ATOM
958
CG
LEU
125
35.173
44.370
74.791
1.00
11.95
DIC

ATOM
959
CD1
LEU
125
34.233
43.857
73.703
1.00
11.77
DIC

ATOM
960
CD2
LEU
125
34.641
43.968
76.154
1.00
15.27
DIC

ATOM
961
C
LEU
125
37.701
45.437
76.055
1.00
9.18
DIC

ATOM
962
O
LEU
125
37.325
45.826
77.160
1.00
9.87
DIC

ATOM
963
N
GLY
126
38.202
46.240
75.127
1.00
8.36
DIC

ATOM
964
CA
GLY
126
38.291
47.667
75.333
1.00
9.63
DIC

ATOM
965
C
GLY
126
37.379
48.269
74.284
1.00
9.92
DIC

ATOM
966
O
GLY
126
37.397
47.838
73.128
1.00
8.79
DIC

ATOM
967
N
ALA
127
36.566
49.243
74.674
1.00
8.77
DIC

ATOM
968
CA
ALA
127
35.650
49.870
73.726
1.00
7.45
DIC

ATOM
969
CB
ALA
127
34.386
49.022
73.594
1.00
7.33
DIC

ATOM
970
C
ALA
127
35.284
51.290
74.145
1.00
8.08
DIC

ATOM
971
O
ALA
127
35.462
51.675
75.305
1.00
5.69
DIC

ATOM
972
N
SER
128
34.787
52.069
73.189
1.00
6.63
DIC

ATOM
973
CA
SER
128
34.383
53.441
73.461
1.00
7.92
DIC

ATOM
974
CB
SER
128
34.631
54.327
72.233
1.00
8.31
DIC

ATOM
975
OG
SER
128
36.021
54.413
71.932
1.00
7.53
DIC

ATOM
976
C
SER
128
32.905
53.452
73.843
1.00
7.98
DIC

ATOM
977
O
SER
128
32.129
52.605
73.390
1.00
6.12
DIC

ATOM
978
N
ILE
129
32.529
54.411
74.683
1.00
8.45
DIC

ATOM
979
CA
ILE
129
31.157
54.547
75.165
1.00
7.19
DIC

ATOM
980
CB
ILE
129
31.110
55.479
76.406
1.00
8.54
DIC

ATOM
981
CG2
ILE
129
29.667
55.842
76.752
1.00
9.06
DIC

ATOM
982
CG1
ILE
129
31.815
54.799
77.586
1.00
8.78
DIC

ATOM
983
CD
ILE
129
31.972
55.685
78.804
1.00
8.26
DIC

ATOM
984
C
ILE
129
30.205
55.092
74.104
1.00
8.79
DIC

ATOM
985
O
ILE
129
30.572
55.954
73.305
1.00
6.50
DIC

ATOM
986
N
ASP
130
28.980
54.577
74.100
1.00
7.31
DIC

ATOM
987
CA
ASP
130
27.978
55.037
73.152
1.00
8.69
DIC

ATOM
988
CB
ASP
130
27.102
53.873
72.692
1.00
6.90
DIC

ATOM
989
CG
ASP
130
26.237
54.238
71.510
1.00
7.79
DIC

ATOM
990
OD1
ASP
130
25.535
55.274
71.578
1.00
7.38
DIC

ATOM
991
OD2
ASP
130
26.258
53.493
70.511
1.00
8.54
DIC

ATOM
992
C
ASP
130
27.125
56.078
73.871
1.00
8.24
DIC

ATOM
993
O
ASP
130
26.249
55.729
74.660
1.00
9.03
DIC

ATOM
994
N
LEU
131
27.398
57.353
73.608
1.00
10.56
DIC

ATOM
995
CA
LEU
131
26.668
58.456
74.242
1.00
11.56
DIC

ATOM
996
CB
LEU
131
27.234
59.808
73.785
1.00
11.69
DIC

ATOM
997
CG
LEU
131
28.607
60.232
74.318
1.00
15.03
DIC

ATOM
998
CD1
LEU
131
29.662
59.190
73.969
1.00
17.38
DIC

ATOM
999
CD2
LEU
131
28.981
61.583
73.722
1.00
15.49
DIC

ATOM
1000
C
LEU
131
25.168
58.428
73.974
1.00
11.77
DIC

ATOM
1001
O
LEU
131
24.367
58.755
74.853
1.00
10.73
DIC

ATOM
1002
N
PHE
132
24.789
58.045
72.760
1.00
11.04
DIC

ATOM
1003
CA
PHE
132
23.381
57.988
72.388
1.00
12.06
DIC

ATOM
1004
CB
PHE
132
23.244
57.642
70.903
1.00
14.10
DIC

ATOM
1005
CG
PHE
132
21.820
57.544
70.433
1.00
16.45
DIC

ATOM
1006
CD1
PHE
132
21.121
56.346
70.531
1.00
16.62
DIC

ATOM
1007
CD2
PHE
132
21.167
58.658
69.922
1.00
19.15
DIC

ATOM
1008
CE1
PHE
132
19.793
56.257
70.128
1.00
16.52
DIC

ATOM
1009
CE2
PHE
132
19.834
58.582
69.515
1.00
19.44
DIC

ATOM
1010
CZ
PHE
132
19.148
57.378
69.619
1.00
18.41
DIC

ATOM
1011
C
PHE
132
22.589
56.988
73.230
1.00
12.25
DIC

ATOM
1012
O
PHE
132
21.542
57.327
73.789
1.00
12.83
DIC

ATOM
1013
N
VAL
133
23.086
55.757
73.321
1.00
10.53
DIC

ATOM
1014
CA
VAL
133
22.404
54.722
74.093
1.00
10.89
DIC

ATOM
1015
CB
VAL
133
23.017
53.330
73.843
1.00
10.97
DIC

ATOM
1016
CG1
VAL
133
22.268
52.280
74.669
1.00
12.18
DIC

ATOM
1017
CG2
VAL
133
22.953
52.987
72.365
1.00
10.49
DIC

ATOM
1018
C
VAL
133
22.481
55.006
75.586
1.00
12.00
DIC

ATOM
1019
O
VAL
133
21.532
54.746
76.327
1.00
10.73
DIC

ATOM
1020
N
GLU
134
23.620
55.533
76.022
1.00
12.24
DIC

ATOM
1021
CA
GLU
134
23.822
55.843
77.431
1.00
14.14
DIC

ATOM
1022
CB
GLU
134
25.250
56.354
77.656
1.00
14.36
DIC

ATOM
1023
CG
GLU
134
25.592
56.614
79.114
1.00
16.20
DIC

ATOM
1024
CD
GLU
134
25.664
55.348
79.951
1.00
14.45
DIC

ATOM
1025
OE1
GLU
134
25.645
55.468
81.189
1.00
17.32
DIC

ATOM
1026
OE2
GLU
134
25.750
54.235
79.383
1.00
14.66
DIC

ATOM
1027
C
GLU
134
22.813
56.872
77.927
1.00
14.91
DIC

ATOM
1028
O
GLU
134
22.415
56.845
79.090
1.00
16.45
DIC

ATOM
1029
N
ARG
135
22.388
57.776
77.051
1.00
16.10
DIC

ATOM
1030
CA
ARG
135
21.428
58.792
77.454
1.00
16.53
DIC

ATOM
1031
CB
ARG
135
21.785
60.150
76.834
1.00
19.31
DIC

ATOM
1032
CG
ARG
135
21.548
60.279
75.341
1.00
22.07
DIC

ATOM
1033
CD
ARG
135
22.304
61.487
74.800
1.00
26.30
DIC

ATOM
1034
NE
ARG
135
21.972
62.716
75.516
1.00
29.13
DIC

ATOM
1035
CZ
ARG
135
20.851
63.410
75.339
1.00
32.01
DIC

ATOM
1036
NH1
ARG
135
20.635
64.516
76.041
1.00
31.51
DIC

ATOM
1037
NH2
ARG
135
19.950
63.007
74.450
1.00
32.01
DIC

ATOM
1038
C
ARG
135
19.992
58.405
77.110
1.00
17.25
DIC

ATOM
1039
O
ARG
135
19.078
59.217
77.232
1.00
17.38
DIC

ATOM
1040
N
GLN
136
19.800
57.164
76.674
1.00
15.73
DIC

ATOM
1041
CA
GLN
136
18.462
56.673
76.361
1.00
17.42
DIC

ATOM
1042
CB
GLN
136
18.538
55.479
75.413
1.00
16.78
DIC

ATOM
1043
CG
GLN
136
17.213
55.086
74.796
1.00
18.64
DIC

ATOM
1044
CD
GLN
136
17.355
53.916
73.845
1.00
21.61
DIC

ATOM
1045
OE1
GLN
136
18.327
53.833
73.097
1.00
23.71
DIC

ATOM
1046
NE2
GLN
136
16.383
53.012
73.861
1.00
21.40
DIC

ATOM
1047
C
GLN
136
17.905
56.236
77.713
1.00
18.33
DIC

ATOM
1048
O
GLN
136
18.123
55.106
78.149
1.00
16.98
DIC

ATOM
1049
N
GLU
137
17.199
57.146
78.375
1.00
20.02
DIC

ATOM
1050
CA
GLU
137
16.649
56.895
79.705
1.00
22.25
DIC

ATOM
1051
CB
GLU
137
15.653
58.004
80.072
1.00
26.10
DIC

ATOM
1052
CG
GLU
137
15.839
58.561
81.485
1.00
31.74
DIC

ATOM
1053
CD
GLU
137
15.083
57.774
82.544
1.00
35.77
DIC

ATOM
1054
OE1
GLU
137
13.842
57.916
82.611
1.00
38.12
DIC

ATOM
1055
OE2
GLU
137
15.723
57.016
83.308
1.00
36.14
DIC

ATOM
1056
C
GLU
137
16.008
55.529
79.927
1.00
20.26
DIC

ATOM
1057
O
GLU
137
15.064
55.145
79.234
1.00
21.74
DIC

ATOM
1058
N
GLY
138
16.547
54.798
80.898
1.00
19.39
DIC

ATOM
1059
CA
GLY
138
16.023
53.488
81.244
1.00
17.93
DIC

ATOM
1060
C
GLY
138
16.402
52.294
80.383
1.00
16.30
DIC

ATOM
1061
O
GLY
138
16.196
51.156
80.799
1.00
16.99
DIC

ATOM
1062
N
TYR
139
16.955
52.520
79.196
1.00
14.22
DIC

ATOM
1063
CA
TYR
139
17.303
51.392
78.340
1.00
12.95
DIC

ATOM
1064
CB
TYR
139
17.775
51.852
76.962
1.00
11.93
DIC

ATOM
1065
CG
TYR
139
18.077
50.670
76.066
1.00
9.65
DIC

ATOM
1066
CD1
TYR
139
17.051
49.841
75.618
1.00
9.55
DIC

ATOM
1067
CE1
TYR
139
17.318
48.699
74.870
1.00
6.57
DIC

ATOM
1068
CD2
TYR
139
19.390
50.327
75.735
1.00
8.27
DIC

ATOM
1069
CE2
TYR
139
19.668
49.180
74.983
1.00
6.71
DIC

ATOM
1070
CZ
TYR
139
18.622
48.372
74.558
1.00
6.55
DIC

ATOM
1071
OH
TYR
139
18.868
47.224
73.836
1.00
7.26
DIC

ATOM
1072
C
TYR
139
18.372
50.479
78.916
1.00
12.54
DIC

ATOM
1073
O
TYR
139
18.174
49.274
79.025
1.00
14.54
DIC

ATOM
1074
N
LYS
140
19.511
51.066
79.257
1.00
12.11
DIC

ATOM
1075
CA
LYS
140
20.643
50.335
79.801
1.00
12.14
DIC

ATOM
1076
CB
LYS
140
21.660
51.338
80.350
1.00
14.79
DIC

ATOM
1077
CG
LYS
140
22.981
50.743
80.761
1.00
17.75
DIC

ATOM
1078
CD
LYS
140
24.029
51.821
81.007
1.00
15.95
DIC

ATOM
1079
CE
LYS
140
23.711
52.669
82.224
1.00
17.64
DIC

ATOM
1080
NZ
LYS
140
24.887
53.502
82.602
1.00
16.20
DIC

ATOM
1081
C
LYS
140
20.229
49.344
80.884
1.00
13.45
DIC

ATOM
1082
O
LYS
140
20.690
48.201
80.903
1.00
13.33
DIC

ATOM
1083
N
GLN
141
19.348
49.776
81.778
1.00
11.99
DIC

ATOM
1084
CA
GLN
141
18.890
48.917
82.860
1.00
14.94
DIC

ATOM
1085
CB
GLN
141
18.150
49.752
83.914
1.00
15.97
DIC

ATOM
1086
CG
GLN
141
19.049
50.738
84.676
1.00
16.22
DIC

ATOM
1087
CD
GLN
141
19.452
51.962
83.859
1.00
19.15
DIC

ATOM
1088
OE1
GLN
141
19.056
52.118
82.702
1.00
20.43
DIC

ATOM
1089
NE2
GLN
141
20.240
52.843
84.469
1.00
16.02
DIC

ATOM
1090
C
GLN
141
18.008
47.766
82.369
1.00
14.90
DIC

ATOM
1091
O
GLN
141
17.990
46.686
82.968
1.00
15.34
DIC

ATOM
1092
N
LYS
142
17.284
47.992
81.278
1.00
14.30
DIC

ATOM
1093
CA
LYS
142
16.427
46.957
80.716
1.00
15.53
DIC

ATOM
1094
CB
LYS
142
15.698
47.475
79.470
1.00
17.58
DIC

ATOM
1095
CG
LYS
142
14.482
48.333
79.757
1.00
21.30
DIC

ATOM
1096
CD
LYS
142
13.895
48.879
78.459
1.00
25.10
DIC

ATOM
1097
CE
LYS
142
12.527
49.508
78.678
1.00
28.09
DIC

ATOM
1098
NZ
LYS
142
11.484
48.490
78.984
1.00
31.88
DIC

ATOM
1099
C
LYS
142
17.229
45.709
80.351
1.00
14.42
DIC

ATOM
1100
O
LYS
142
16.684
44.606
80.317
1.00
15.12
DIC

ATOM
1101
N
ILE
143
18.517
45.870
80.060
1.00
12.66
DIC

ATOM
1102
CA
ILE
143
19.319
44.699
79.724
1.00
11.78
DIC

ATOM
1103
CB
ILE
143
20.131
44.898
78.421
1.00
11.52
DIC

ATOM
1104
CG2
ILE
143
19.177
45.095
77.249
1.00
9.94
DIC

ATOM
1105
CG1
ILE
143
21.084
46.085
78.550
1.00
10.92
DIC

ATOM
1106
CD
ILE
143
22.037
46.202
77.376
1.00
9.97
DIC

ATOM
1107
C
ILE
143
20.246
44.268
80.863
1.00
11.61
DIC

ATOM
1108
O
ILE
143
21.264
43.612
80.639
1.00
11.97
DIC

ATOM
1109
N
GLY
144
19.873
44.649
82.085
1.00
11.10
DIC

ATOM
1110
CA
GLY
144
20.624
44.268
83.270
1.00
9.94
DIC

ATOM
1111
C
GLY
144
21.853
45.060
83.663
1.00
11.04
DIC

ATOM
1112
O
GLY
144
22.626
44.621
84.518
1.00
9.79
DIC

ATOM
1113
N
MSE
145
22.048
46.227
83.062
1.00
10.12
DIC

ATOM
1114
CA
MSE
145
23.212
47.031
83.390
1.00
11.90
DIC

ATOM
1115
CB
MSE
145
23.725
47.738
82.135
1.00
12.20
DIC

ATOM
1116
CG
MSE
145
24.329
46.789
81.111
1.00
13.32
DIC

ATOM
1117
SE
MSE
145
24.908
47.720
79.517
1.00
19.71
DIC

ATOM
1118
CE
MSE
145
26.468
48.596
80.243
1.00
14.79
DIC

ATOM
1119
C
MSE
145
22.931
48.048
84.487
1.00
12.83
DIC

ATOM
1120
O
MSE
145
21.821
48.576
84.594
1.00
11.70
DIC

ATOM
1121
N
ALA
146
23.948
48.314
85.301
1.00
14.28
DIC

ATOM
1122
CA
ALA
146
23.832
49.274
86.395
1.00
14.92
DIC

ATOM
1123
CB
ALA
146
24.793
48.903
87.517
1.00
14.61
DIC

ATOM
1124
C
ALA
146
24.140
50.677
85.891
1.00
15.53
DIC

ATOM
1125
O
ALA
146
24.776
50.843
84.852
1.00
14.24
DIC

ATOM
1126
N
ASP
147
23.688
51.683
86.634
1.00
16.07
DIC

ATOM
1127
CA
ASP
147
23.917
53.075
86.262
1.00
16.26
DIC

ATOM
1128
CB
ASP
147
23.370
54.011
87.346
1.00
20.59
DIC

ATOM
1129
CG
ASP
147
23.700
55.473
87.078
1.00
23.36
DIC

ATOM
1130
OD1
ASP
147
23.214
56.026
86.069
1.00
25.96
DIC

ATOM
1131
OD2
ASP
147
24.451
56.071
87.878
1.00
28.48
DIC

ATOM
1132
C
ASP
147
25.400
53.352
86.066
1.00
14.79
DIC

ATOM
1133
O
ASP
147
25.780
54.135
85.194
1.00
13.86
DIC

ATOM
1134
N
GLY
148
26.230
52.697
86.876
1.00
13.02
DIC

ATOM
1135
CA
GLY
148
27.668
52.894
86.806
1.00
11.35
DIC

ATOM
1136
C
GLY
148
28.396
52.094
85.744
1.00
10.20
DIC

ATOM
1137
O
GLY
148
29.606
52.246
85.574
1.00
11.09
DIC

ATOM
1138
N
GLU
149
27.676
51.225
85.043
1.00
9.04
DIC

ATOM
1139
CA
GLU
149
28.277
50.429
83.979
1.00
9.03
DIC

ATOM
1140
CB
GLU
149
27.733
49.001
84.003
1.00
8.78
DIC

ATOM
1141
CG
GLU
149
27.982
48.306
85.330
1.00
12.20
DIC

ATOM
1142
CD
GLU
149
27.390
46.916
85.382
1.00
11.83
DIC

ATOM
1143
OE1
GLU
149
26.235
46.747
84.947
1.00
12.11
DIC

ATOM
1144
OE2
GLU
149
28.073
45.994
85.871
1.00
16.06
DIC

ATOM
1145
C
GLU
149
27.884
51.142
82.697
1.00
8.47
DIC

ATOM
1146
O
GLU
149
26.701
51.294
82.393
1.00
9.02
DIC

ATOM
1147
N
TYR
150
28.886
51.591
81.956
1.00
8.23
DIC

ATOM
1148
CA
TYR
150
28.645
52.343
80.738
1.00
9.12
DIC

ATOM
1149
CB
TYR
150
29.760
53.383
80.590
1.00
8.51
DIC

ATOM
1150
CG
TYR
150
29.912
54.216
81.854
1.00
9.43
DIC

ATOM
1151
CD1
TYR
150
31.155
54.388
82.461
1.00
10.16
DIC

ATOM
1152
CE1
TYR
150
31.283
55.106
83.654
1.00
10.95
DIC

ATOM
1153
CD2
TYR
150
28.796
54.790
82.469
1.00
12.27
DIC

ATOM
1154
CE2
TYR
150
28.913
55.511
83.662
1.00
10.90
DIC

ATOM
1155
CZ
TYR
150
30.160
55.661
84.248
1.00
13.06
DIC

ATOM
1156
OH
TYR
150
30.279
56.354
85.433
1.00
12.48
DIC

ATOM
1157
C
TYR
150
28.488
51.494
79.487
1.00
7.57
DIC

ATOM
1158
O
TYR
150
29.309
50.625
79.187
1.00
6.61
DIC

ATOM
1159
N
TYR
151
27.401
51.755
78.769
1.00
7.71
DIC

ATOM
1160
CA
TYR
151
27.069
51.035
77.547
1.00
7.79
DIC

ATOM
1161
CB
TYR
151
25.629
51.375
77.144
1.00
6.89
DIC

ATOM
1162
CG
TYR
151
25.057
50.553
76.009
1.00
7.54
DIC

ATOM
1163
CD1
TYR
151
25.432
50.789
74.685
1.00
5.74
DIC

ATOM
1164
CE1
TYR
151
24.889
50.039
73.635
1.00
4.54
DIC

ATOM
1165
CD2
TYR
151
24.125
49.546
76.260
1.00
7.45
DIC

ATOM
1166
CE2
TYR
151
23.579
48.792
75.222
1.00
6.69
DIC

ATOM
1167
CZ
TYR
151
23.964
49.042
73.913
1.00
6.52
DIC

ATOM
1168
OH
TYR
151
23.432
48.282
72.891
1.00
6.05
DIC

ATOM
1169
C
TYR
151
28.047
51.443
76.454
1.00
6.36
DIC

ATOM
1170
O
TYR
151
28.148
52.621
76.116
1.00
7.50
DIC

ATOM
1171
N
PHE
152
28.776
50.475
75.909
1.00
5.53
DIC

ATOM
1172
CA
PHE
152
29.745
50.779
74.870
1.00
4.94
DIC

ATOM
1173
CB
PHE
152
31.060
50.016
75.108
1.00
4.86
DIC

ATOM
1174
CG
PHE
152
30.919
48.513
75.089
1.00
6.40
DIC

ATOM
1175
CD1
PHE
152
30.724
47.802
76.271
1.00
6.43
DIC

ATOM
1176
CD2
PHE
152
30.984
47.808
73.888
1.00
4.17
DIC

ATOM
1177
CE1
PHE
152
30.594
46.408
76.259
1.00
5.71
DIC

ATOM
1178
CE2
PHE
152
30.854
46.416
73.865
1.00
5.71
DIC

ATOM
1179
CZ
PHE
152
30.659
45.717
75.055
1.00
5.50
DIC

ATOM
1180
C
PHE
152
29.229
50.481
73.470
1.00
5.82
DIC

ATOM
1181
O
PHE
152
28.301
49.695
73.290
1.00
5.93
DIC

ATOM
1182
N
ASN
153
29.828
51.133
72.481
1.00
5.20
DIC

ATOM
1183
CA
ASN
153
29.447
50.910
71.094
1.00
5.79
DIC

ATOM
1184
CB
ASN
153
29.685
52.176
70.260
1.00
6.58
DIC

ATOM
1185
CG
ASN
153
29.282
51.998
68.809
1.00
6.46
DIC

ATOM
1186
OD1
ASN
153
30.095
51.621
67.974
1.00
6.69
DIC

ATOM
1187
ND2
ASN
153
28.011
52.247
68.510
1.00
9.09
DIC

ATOM
1188
C
ASN
153
30.296
49.752
70.585
1.00
5.25
DIC

ATOM
1189
O
ASN
153
31.492
49.683
70.861
1.00
3.87
DIC

ATOM
1190
N
ALA
154
29.674
48.838
69.847
1.00
5.40
DIC

ATOM
1191
CA
ALA
154
30.373
47.661
69.336
1.00
7.13
DIC

ATOM
1192
CB
ALA
154
29.381
46.508
69.188
1.00
4.44
DIC

ATOM
1193
C
ALA
154
31.134
47.859
68.024
1.00
6.42
DIC

ATOM
1194
O
ALA
154
31.733
46.913
67.507
1.00
7.14
DIC

ATOM
1195
N
GLY
155
31.118
49.080
67.496
1.00
6.03
DIC

ATOM
1196
CA
GLY
155
31.792
49.359
66.239
1.00
4.30
DIC

ATOM
1197
C
GLY
155
33.312
49.368
66.250
1.00
6.06
DIC

ATOM
1198
O
GLY
155
33.939
49.273
65.192
1.00
4.92
DIC

ATOM
1199
N
VAL
156
33.907
49.496
67.433
1.00
4.75
DIC

ATOM
1200
CA
VAL
156
35.362
49.510
67.582
1.00
4.31
DIC

ATOM
1201
CB
VAL
156
35.901
50.954
67.701
1.00
5.59
DIC

ATOM
1202
CG1
VAL
156
37.398
50.931
67.984
1.00
5.38
DIC

ATOM
1203
CG2
VAL
156
35.617
51.727
66.405
1.00
2.76
DIC

ATOM
1204
C
VAL
156
35.686
48.741
68.855
1.00
5.47
DIC

ATOM
1205
O
VAL
156
35.396
49.203
69.959
1.00
5.04
DIC

ATOM
1206
N
LEU
157
36.300
47.573
68.703
1.00
4.91
DIC

ATOM
1207
CA
LEU
157
36.599
46.741
69.858
1.00
6.02
DIC

ATOM
1208
CB
LEU
157
35.606
45.580
69.908
1.00
5.28
DIC

ATOM
1209
CG
LEU
157
34.120
45.923
69.800
1.00
5.55
DIC

ATOM
1210
CD1
LEU
157
33.324
44.655
69.516
1.00
3.12
DIC

ATOM
1211
CD2
LEU
157
33.658
46.599
71.084
1.00
3.69
DIC

ATOM
1212
C
LEU
157
37.998
46.157
69.915
1.00
6.93
DIC

ATOM
1213
O
LEU
157
38.403
45.431
69.008
1.00
7.95
DIC

ATOM
1214
N
LEU
158
38.733
46.474
70.978
1.00
6.51
DIC

ATOM
1215
CA
LEU
158
40.059
45.897
71.174
1.00
6.78
DIC

ATOM
1216
CB
LEU
158
40.956
46.826
71.995
1.00
8.24
DIC

ATOM
1217
CG
LEU
158
42.416
46.378
72.110
1.00
8.34
DIC

ATOM
1218
CD1
LEU
158
43.062
46.337
70.728
1.00
8.63
DIC

ATOM
1219
CD2
LEU
158
43.164
47.331
73.018
1.00
9.77
DIC

ATOM
1220
C
LEU
158
39.693
44.652
71.978
1.00
7.75
DIC

ATOM
1221
O
LEU
158
39.304
44.740
73.146
1.00
5.84
DIC

ATOM
1222
N
ILE
159
39.803
43.493
71.343
1.00
7.13
DIC

ATOM
1223
CA
ILE
159
39.401
42.246
71.973
1.00
7.06
DIC

ATOM
1224
CB
ILE
159
38.582
41.418
70.951
1.00
8.06
DIC

ATOM
1225
CG2
ILE
159
38.329
40.009
71.467
1.00
5.92
DIC

ATOM
1226
CG1
ILE
159
37.274
42.160
70.652
1.00
7.50
DIC

ATOM
1227
CD
ILE
159
36.439
41.533
69.576
1.00
12.31
DIC

ATOM
1228
C
ILE
159
40.494
41.377
72.585
1.00
8.00
DIC

ATOM
1229
O
ILE
159
41.513
41.099
71.958
1.00
5.43
DIC

ATOM
1230
N
ASN
160
40.261
40.952
73.824
1.00
8.08
DIC

ATOM
1231
CA
ASN
160
41.198
40.079
74.530
1.00
8.60
DIC

ATOM
1232
CB
ASN
160
40.987
40.197
76.037
1.00
9.75
DIC

ATOM
1233
CG
ASN
160
41.948
39.334
76.838
1.00
8.59
DIC

ATOM
1234
OD1
ASN
160
42.542
38.393
76.317
1.00
6.73
DIC

ATOM
1235
ND2
ASN
160
42.092
39.648
78.119
1.00
8.57
DIC

ATOM
1236
C
ASN
160
40.857
38.665
74.066
1.00
9.81
DIC

ATOM
1237
O
ASN
160
40.217
37.898
74.793
1.00
9.36
DIC

ATOM
1238
N
LEU
161
41.276
38.331
72.849
1.00
11.11
DIC

ATOM
1239
CA
LEU
161
40.987
37.024
72.268
1.00
11.84
DIC

ATOM
1240
CB
LEU
161
41.603
36.905
70.871
1.00
13.69
DIC

ATOM
1241
CG
LEU
161
40.670
37.132
69.680
1.00
18.63
DIC

ATOM
1242
CD1
LEU
161
41.441
36.900
68.392
1.00
17.69
DIC

ATOM
1243
CD2
LEU
161
39.479
36.185
69.753
1.00
17.40
DIC

ATOM
1244
C
LEU
161
41.423
35.830
73.104
1.00
12.22
DIC

ATOM
1245
O
LEU
161
40.733
34.811
73.132
1.00
10.35
DIC

ATOM
1246
N
LYS
162
42.568
35.935
73.769
1.00
12.29
DIC

ATOM
1247
CA
LYS
162
43.031
34.823
74.591
1.00
13.27
DIC

ATOM
1248
CB
LYS
162
44.369
35.159
75.261
1.00
16.11
DIC

ATOM
1249
CG
LYS
162
44.829
34.102
76.258
1.00
20.91
DIC

ATOM
1250
CD
LYS
162
46.278
34.286
76.686
1.00
24.43
DIC

ATOM
1251
CE
LYS
162
47.247
33.739
75.643
1.00
27.26
DIC

ATOM
1252
NZ
LYS
162
48.647
33.711
76.161
1.00
27.23
DIC

ATOM
1253
C
LYS
162
41.975
34.491
75.643
1.00
12.71
DIC

ATOM
1254
O
LYS
162
41.677
33.325
75.878
1.00
13.95
DIC

ATOM
1255
N
LYS
163
41.400
35.516
76.268
1.00
12.30
DIC

ATOM
1256
CA
LYS
163
40.369
35.287
77.275
1.00
10.73
DIC

ATOM
1257
CB
LYS
163
40.006
36.594
77.987
1.00
9.94
DIC

ATOM
1258
CG
LYS
163
38.984
36.419
79.113
1.00
9.80
DIC

ATOM
1259
CD
LYS
163
38.667
37.744
79.792
1.00
12.02
DIC

ATOM
1260
CE
LYS
163
37.685
37.563
80.946
1.00
11.59
DIC

ATOM
1261
NZ
LYS
163
38.230
36.656
81.994
1.00
15.21
DIC

ATOM
1262
C
LYS
163
39.120
34.695
76.616
1.00
10.32
DIC

ATOM
1263
O
LYS
163
38.527
33.748
77.133
1.00
10.04
DIC

ATOM
1264
N
TRP
164
38.718
35.260
75.481
1.00
10.10
DIC

ATOM
1265
CA
TRP
164
37.545
34.768
74.762
1.00
10.66
DIC

ATOM
1266
CB
TRP
164
37.366
35.524
73.443
1.00
8.99
DIC

ATOM
1267
CG
TRP
164
36.729
36.883
73.567
1.00
7.04
DIC

ATOM
1268
CD2
TRP
164
35.780
37.469
72.665
1.00
6.04
DIC

ATOM
1269
CE2
TRP
164
35.516
38.777
73.127
1.00
5.54
DIC

ATOM
1270
CE3
TRP
164
35.131
37.015
71.508
1.00
5.98
DIC

ATOM
1271
CD1
TRP
164
36.989
37.829
74.514
1.00
7.19
DIC

ATOM
1272
NE1
TRP
164
36.265
38.970
74.257
1.00
6.74
DIC

ATOM
1273
CZ2
TRP
164
34.630
39.642
72.471
1.00
7.14
DIC

ATOM
1274
CZ3
TRP
164
34.249
37.873
70.856
1.00
6.29
DIC

ATOM
1275
CH2
TRP
164
34.008
39.174
71.342
1.00
6.21
DIC

ATOM
1276
C
TRP
164
37.657
33.271
74.464
1.00
11.95
DIC

ATOM
1277
O
TRP
164
36.695
32.519
74.642
1.00
9.24
DIC

ATOM
1278
N
ARG
165
38.829
32.841
74.005
1.00
11.53
DIC

ATOM
1279
CA
ARG
165
39.025
31.433
73.677
1.00
12.97
DIC

ATOM
1280
CB
ARG
165
40.392
31.220
73.011
1.00
13.33
DIC

ATOM
1281
CG
ARG
165
40.431
31.666
71.546
1.00
16.11
DIC

ATOM
1282
CD
ARG
165
41.607
31.041
70.792
1.00
16.25
DIC

ATOM
1283
NE
ARG
165
42.889
31.519
71.293
1.00
16.10
DIC

ATOM
1284
CZ
ARG
165
43.467
32.653
70.914
1.00
16.79
DIC

ATOM
1285
NH1
ARG
165
44.632
33.005
71.440
1.00
19.33
DIC

ATOM
1286
NH2
ARG
165
42.898
33.423
69.994
1.00
15.46
DIC

ATOM
1287
C
ARG
165
38.858
30.495
74.871
1.00
13.30
DIC

ATOM
1288
O
ARG
165
38.699
29.292
74.698
1.00
13.71
DIC

ATOM
1289
N
ARG
166
38.876
31.041
76.081
1.00
14.72
DIC

ATOM
1290
CA
ARG
166
38.699
30.218
77.277
1.00
14.91
DIC

ATOM
1291
CB
ARG
166
39.333
30.891
78.497
1.00
16.73
DIC

ATOM
1292
CG
ARG
166
40.852
30.924
78.497
1.00
18.26
DIC

ATOM
1293
CD
ARG
166
41.361
31.920
79.529
1.00
19.78
DIC

ATOM
1294
NE
ARG
166
42.817
32.015
79.525
1.00
23.68
DIC

ATOM
1295
CZ
ARG
166
43.494
33.142
79.725
1.00
22.99
DIC

ATOM
1296
NH1
ARG
166
42.847
34.279
79.943
1.00
23.36
DIC

ATOM
1297
NH2
ARG
166
44.820
33.133
79.697
1.00
25.53
DIC

ATOM
1298
C
ARG
166
37.213
29.999
77.558
1.00
14.47
DIC

ATOM
1299
O
ARG
166
36.854
29.254
78.463
1.00
14.64
DIC

ATOM
1300
N
HIS
167
36.352
30.640
76.776
1.00
13.19
DIC

ATOM
1301
CA
HIS
167
34.912
30.523
76.990
1.00
13.58
DIC

ATOM
1302
CB
HIS
167
34.380
31.815
77.624
1.00
14.56
DIC

ATOM
1303
CG
HIS
167
35.031
32.166
78.928
1.00
15.72
DIC

ATOM
1304
CD2
HIS
167
36.121
32.920
79.206
1.00
14.81
DIC

ATOM
1305
ND1
HIS
167
34.570
31.700
80.141
1.00
15.43
DIC

ATOM
1306
CE1
HIS
167
35.347
32.151
81.109
1.00
14.64
DIC

ATOM
1307
NE2
HIS
167
36.296
32.895
80.568
1.00
15.87
DIC

ATOM
1308
C
HIS
167
34.145
30.251
75.701
1.00
13.20
DIC

ATOM
1309
O
HIS
167
34.673
30.410
74.600
1.00
14.22
DIC

ATOM
1310
N
ASP
168
32.894
29.831
75.848
1.00
10.69
DIC

ATOM
1311
CA
ASP
168
32.045
29.572
74.699
1.00
10.18
DIC

ATOM
1312
CB
ASP
168
31.212
28.303
74.914
1.00
11.40
DIC

ATOM
1313
CG
ASP
168
30.499
27.860
73.654
1.00
11.10
DIC

ATOM
1314
OD1
ASP
168
30.114
26.676
73.566
1.00
13.98
DIC

ATOM
1315
OD2
ASP
168
30.317
28.698
72.748
1.00
13.04
DIC

ATOM
1316
C
ASP
168
31.150
30.801
74.568
1.00
9.57
DIC

ATOM
1317
O
ASP
168
30.019
30.830
75.056
1.00
6.68
DIC

ATOM
1318
N
ILE
169
31.690
31.818
73.904
1.00
8.34
DIC

ATOM
1319
CA
ILE
169
31.001
33.084
73.710
1.00
8.76
DIC

ATOM
1320
CB
ILE
169
31.918
34.092
72.985
1.00
8.29
DIC

ATOM
1321
CG2
ILE
169
31.221
35.441
72.863
1.00
8.00
DIC

ATOM
1322
CG1
ILE
169
33.230
34.244
73.759
1.00
10.02
DIC

ATOM
1323
CD
ILE
169
33.046
34.721
75.202
1.00
11.51
DIC

ATOM
1324
C
ILE
169
29.689
32.963
72.947
1.00
7.31
DIC

ATOM
1325
O
ILE
169
28.718
33.644
73.270
1.00
7.10
DIC

ATOM
1326
N
PHE
170
29.653
32.102
71.937
1.00
9.62
DIC

ATOM
1327
CA
PHE
170
28.428
31.936
71.162
1.00
9.67
DIC

ATOM
1328
CB
PHE
170
28.670
31.053
69.941
1.00
11.96
DIC

ATOM
1329
CG
PHE
170
27.451
30.875
69.082
1.00
12.14
DIC

ATOM
1330
CD1
PHE
170
26.782
29.657
69.043
1.00
15.39
DIC

ATOM
1331
CD2
PHE
170
26.950
31.939
68.339
1.00
13.78
DIC

ATOM
1332
CE1
PHE
170
25.628
29.500
68.276
1.00
16.66
DIC

ATOM
1333
CE2
PHE
170
25.800
31.793
67.569
1.00
16.17
DIC

ATOM
1334
CZ
PHE
170
25.136
30.569
67.539
1.00
15.75
DIC

ATOM
1335
C
PHE
170
27.314
31.336
72.012
1.00
10.61
DIC

ATOM
1336
O
PHE
170
26.163
31.765
71.933
1.00
10.59
DIC

ATOM
1337
N
LYS
171
27.652
30.345
72.830
1.00
10.05
DIC

ATOM
1338
CA
LYS
171
26.648
29.723
73.682
1.00
10.03
DIC

ATOM
1339
CB
LYS
171
27.239
28.505
74.399
1.00
13.97
DIC

ATOM
1340
CG
LYS
171
26.201
27.670
75.138
1.00
18.06
DIC

ATOM
1341
CD
LYS
171
26.735
26.285
75.464
1.00
22.03
DIC

ATOM
1342
CE
LYS
171
27.078
25.516
74.194
1.00
24.58
DIC

ATOM
1343
NZ
LYS
171
27.566
24.142
74.489
1.00
29.13
DIC

ATOM
1344
C
LYS
171
26.137
30.743
74.699
1.00
9.12
DIC

ATOM
1345
O
LYS
171
24.935
30.853
74.928
1.00
9.26
DIC

ATOM
1346
N
MSE
172
27.058
31.485
75.303
1.00
6.97
DIC

ATOM
1347
CA
MSE
172
26.708
32.512
76.278
1.00
9.01
DIC

ATOM
1348
CB
MSE
172
27.980
33.168
76.828
1.00
11.24
DIC

ATOM
1349
CG
MSE
172
28.846
32.238
77.665
1.00
13.80
DIC

ATOM
1350
SE
MSE
172
30.625
32.946
77.970
1.00
25.22
DIC

ATOM
1351
CE
MSE
172
30.177
34.354
79.221
1.00
18.63
DIC

ATOM
1352
C
MSE
172
25.836
33.562
75.593
1.00
9.14
DIC

ATOM
1353
O
MSE
172
24.924
34.123
76.202
1.00
10.30
DIC

ATOM
1354
N
SER
173
26.126
33.819
74.320
1.00
7.61
DIC

ATOM
1355
CA
SER
173
25.364
34.790
73.543
1.00
8.52
DIC

ATOM
1356
CB
SER
173
26.038
35.042
72.191
1.00
8.17
DIC

ATOM
1357
OG
SER
173
27.276
35.717
72.350
1.00
7.46
DIC

ATOM
1358
C
SER
173
23.945
34.278
73.316
1.00
9.07
DIC

ATOM
1359
O
SER
173
22.972
35.020
73.482
1.00
7.42
DIC

ATOM
1360
N
SER
174
23.837
33.008
72.935
1.00
7.76
DIC

ATOM
1361
CA
SER
174
22.539
32.397
72.682
1.00
9.45
DIC

ATOM
1362
CB
SER
174
22.718
30.952
72.210
1.00
9.22
DIC

ATOM
1363
OG
SER
174
23.382
30.917
70.961
1.00
8.11
DIC

ATOM
1364
C
SER
174
21.651
32.428
73.916
1.00
9.49
DIC

ATOM
1365
O
SER
174
20.460
32.725
73.824
1.00
9.51
DIC

ATOM
1366
N
GLU
175
22.234
32.123
75.071
1.00
10.06
DIC

ATOM
1367
CA
GLU
175
21.486
32.118
76.321
1.00
11.19
DIC

ATOM
1368
CB
GLU
175
22.336
31.537
77.452
1.00
14.11
DIC

ATOM
1369
CG
GLU
175
22.905
30.162
77.158
1.00
18.91
DIC

ATOM
1370
CD
GLU
175
23.568
29.540
78.372
1.00
21.75
DIC

ATOM
1371
OE1
GLU
175
24.311
30.255
79.079
1.00
21.00
DIC

ATOM
1372
OE2
GLU
175
23.350
28.333
78.615
1.00
24.48
DIC

ATOM
1373
C
GLU
175
21.046
33.525
76.697
1.00
10.40
DIC

ATOM
1374
O
GLU
175
19.942
33.725
77.202
1.00
10.43
DIC

ATOM
1375
N
TRP
176
21.912
34.502
76.453
1.00
11.21
DIC

ATOM
1376
CA
TRP
176
21.588
35.886
76.778
1.00
10.92
DIC

ATOM
1377
CB
TRP
176
22.804
36.788
76.550
1.00
11.86
DIC

ATOM
1378
CG
TRP
176
22.661
38.151
77.172
1.00
10.34
DIC

ATOM
1379
CD2
TRP
176
22.094
39.317
76.564
1.00
10.13
DIC

ATOM
1380
CE2
TRP
176
22.131
40.350
77.525
1.00
10.66
DIC

ATOM
1381
CE3
TRP
176
21.555
39.588
75.299
1.00
11.84
DIC

ATOM
1382
CD1
TRP
176
23.009
38.513
78.440
1.00
10.51
DIC

ATOM
1383
NE1
TRP
176
22.695
39.832
78.662
1.00
11.39
DIC

ATOM
1384
CZ2
TRP
176
21.649
41.636
77.263
1.00
10.57
DIC

ATOM
1385
CZ3
TRP
176
21.073
40.869
75.037
1.00
9.09
DIC

ATOM
1386
CH2
TRP
176
21.124
41.876
76.016
1.00
10.83
DIC

ATOM
1387
C
TRP
176
20.422
36.351
75.903
1.00
10.57
DIC

ATOM
1388
O
TRP
176
19.496
37.008
76.386
1.00
10.92
DIC

ATOM
1389
N
VAL
177
20.474
36.008
74.617
1.00
9.67
DIC

ATOM
1390
CA
VAL
177
19.415
36.382
73.681
1.00
8.71
DIC

ATOM
1391
CB
VAL
177
19.737
35.905
72.245
1.00
10.47
DIC

ATOM
1392
CG1
VAL
177
18.483
35.975
71.369
1.00
9.48
DIC

ATOM
1393
CG2
VAL
177
20.836
36.771
71.642
1.00
5.59
DIC

ATOM
1394
C
VAL
177
18.091
35.758
74.118
1.00
10.57
DIC

ATOM
1395
O
VAL
177
17.027
36.376
74.019
1.00
9.35
DIC

ATOM
1396
N
GLU
178
18.160
34.524
74.597
1.00
11.52
DIC

ATOM
1397
CA
GLU
178
16.961
33.833
75.038
1.00
15.37
DIC

ATOM
1398
CB
GLU
178
17.310
32.407
75.471
1.00
16.80
DIC

ATOM
1399
CG
GLU
178
16.111
31.557
75.857
1.00
22.43
DIC

ATOM
1400
CD
GLU
178
15.023
31.554
74.797
1.00
25.01
DIC

ATOM
1401
OE1
GLU
178
15.345
31.366
73.603
1.00
27.14
DIC

ATOM
1402
OE2
GLU
178
13.841
31.735
75.161
1.00
29.11
DIC

ATOM
1403
C
GLU
178
16.355
34.603
76.204
1.00
15.38
DIC

ATOM
1404
O
GLU
178
15.139
34.679
76.352
1.00
15.87
DIC

ATOM
1405
N
GLN
179
17.223
35.198
77.012
1.00
15.89
DIC

ATOM
1406
CA
GLN
179
16.803
35.954
78.180
1.00
17.35
DIC

ATOM
1407
CB
GLN
179
17.962
35.998
79.182
1.00
19.05
DIC

ATOM
1408
CG
GLN
179
17.658
36.694
80.493
1.00
24.86
DIC

ATOM
1409
CD
GLN
179
18.839
36.659
81.454
1.00
27.98
DIC

ATOM
1410
OE1
GLN
179
18.761
37.170
82.573
1.00
31.11
DIC

ATOM
1411
NE2
GLN
179
19.939
36.053
81.019
1.00
29.53
DIC

ATOM
1412
C
GLN
179
16.313
37.375
77.884
1.00
16.67
DIC

ATOM
1413
O
GLN
179
15.381
37.850
78.528
1.00
17.16
DIC

ATOM
1414
N
TYR
180
16.918
38.045
76.904
1.00
15.88
DIC

ATOM
1415
CA
TYR
180
16.543
39.423
76.585
1.00
14.53
DIC

ATOM
1416
CB
TYR
180
17.736
40.347
76.831
1.00
15.01
DIC

ATOM
1417
CG
TYR
180
18.196
40.402
78.264
1.00
12.97
DIC

ATOM
1418
CD1
TYR
180
19.108
39.476
78.765
1.00
13.79
DIC

ATOM
1419
CE1
TYR
180
19.545
39.543
80.085
1.00
15.48
DIC

ATOM
1420
CD2
TYR
180
17.725
41.393
79.121
1.00
14.79
DIC

ATOM
1421
CE2
TYR
180
18.152
41.466
80.439
1.00
15.22
DIC

ATOM
1422
CZ
TYR
180
19.062
40.542
80.915
1.00
14.58
DIC

ATOM
1423
OH
TYR
180
19.489
40.624
82.222
1.00
18.45
DIC

ATOM
1424
C
TYR
180
16.011
39.696
75.177
1.00
15.69
DIC

ATOM
1425
O
TYR
180
15.974
40.846
74.741
1.00
14.37
DIC

ATOM
1426
N
LYS
181
15.597
38.650
74.474
1.00
15.60
DIC

ATOM
1427
CA
LYS
181
15.082
38.788
73.116
1.00
18.04
DIC

ATOM
1428
CB
LYS
181
14.660
37.415
72.585
1.00
19.59
DIC

ATOM
1429
CG
LYS
181
13.984
37.447
71.226
1.00
24.70
DIC

ATOM
1430
CD
LYS
181
14.910
37.984
70.145
1.00
27.36
DIC

ATOM
1431
CE
LYS
181
14.215
37.989
68.789
1.00
27.65
DIC

ATOM
1432
NZ
LYS
181
13.752
36.628
68.397
1.00
29.00
DIC

ATOM
1433
C
LYS
181
13.910
39.762
72.973
1.00
16.82
DIC

ATOM
1434
O
LYS
181
13.759
40.414
71.939
1.00
16.53
DIC

ATOM
1435
N
ASP
182
13.083
39.860
74.006
1.00
16.61
DIC

ATOM
1436
CA
ASP
182
11.915
40.738
73.964
1.00
18.34
DIC

ATOM
1437
CB
ASP
182
10.842
40.220
74.920
1.00
19.12
DIC

ATOM
1438
CG
ASP
182
10.268
38.885
74.492
1.00
20.80
DIC

ATOM
1439
OD1
ASP
182
9.625
38.232
75.336
1.00
23.00
DIC

ATOM
1440
OD2
ASP
182
10.447
38.491
73.317
1.00
23.17
DIC

ATOM
1441
C
ASP
182
12.197
42.199
74.301
1.00
17.72
DIC

ATOM
1442
O
ASP
182
11.312
43.042
74.178
1.00
19.56
DIC

ATOM
1443
N
VAL
183
13.416
42.507
74.724
1.00
16.43
DIC

ATOM
1444
CA
VAL
183
13.737
43.880
75.092
1.00
15.35
DIC

ATOM
1445
CB
VAL
183
14.003
43.979
76.619
1.00
17.44
DIC

ATOM
1446
CG1
VAL
183
15.207
43.133
76.998
1.00
17.05
DIC

ATOM
1447
CG2
VAL
183
14.215
45.422
77.022
1.00
21.13
DIC

ATOM
1448
C
VAL
183
14.914
44.489
74.334
1.00
14.50
DIC

ATOM
1449
O
VAL
183
14.957
45.703
74.122
1.00
13.37
DIC

ATOM
1450
N
MSE
184
15.863
43.659
73.914
1.00
13.04
DIC

ATOM
1451
CA
MSE
184
17.024
44.177
73.203
1.00
12.36
DIC

ATOM
1452
CB
MSE
184
18.002
43.038
72.852
1.00
15.98
DIC

ATOM
1453
CG
MSE
184
17.427
41.874
72.058
1.00
17.28
DIC

ATOM
1454
SE
MSE
184
18.615
40.314
72.140
1.00
23.65
DIC

ATOM
1455
CE
MSE
184
19.958
40.898
70.874
1.00
16.42
DIC

ATOM
1456
C
MSE
184
16.641
44.976
71.960
1.00
11.92
DIC

ATOM
1457
O
MSE
184
15.749
44.594
71.198
1.00
11.41
DIC

ATOM
1458
N
GLN
185
17.324
46.098
71.772
1.00
10.32
DIC

ATOM
1459
CA
GLN
185
17.066
46.983
70.647
1.00
10.61
DIC

ATOM
1460
CB
GLN
185
16.644
48.362
71.164
1.00
13.31
DIC

ATOM
1461
CG
GLN
185
15.271
48.406
71.823
1.00
13.72
DIC

ATOM
1462
CD
GLN
185
14.959
49.766
72.438
1.00
16.61
DIC

ATOM
1463
OE1
GLN
185
15.407
50.805
71.944
1.00
14.88
DIC

ATOM
1464
NE2
GLN
185
14.174
49.764
73.513
1.00
14.58
DIC

ATOM
1465
C
GLN
185
18.287
47.141
69.748
1.00
9.38
DIC

ATOM
1466
O
GLN
185
18.167
47.581
68.602
1.00
7.58
DIC

ATOM
1467
N
TYR
186
19.460
46.772
70.254
1.00
7.31
DIC

ATOM
1468
CA
TYR
186
20.670
46.938
69.465
1.00
8.32
DIC

ATOM
1469
CB
TYR
186
21.601
47.929
70.169
1.00
8.66
DIC

ATOM
1470
CG
TYR
186
20.939
49.274
70.383
1.00
12.08
DIC

ATOM
1471
CD1
TYR
186
20.325
49.589
71.594
1.00
11.99
DIC

ATOM
1472
CE1
TYR
186
19.659
50.805
71.774
1.00
11.92
DIC

ATOM
1473
CD2
TYR
186
20.873
50.213
69.348
1.00
14.31
DIC

ATOM
1474
CE2
TYR
186
20.210
51.428
69.516
1.00
13.76
DIC

ATOM
1475
CZ
TYR
186
19.605
51.716
70.732
1.00
13.90
DIC

ATOM
1476
OH
TYR
186
18.947
52.915
70.901
1.00
12.39
DIC

ATOM
1477
C
TYR
186
21.422
45.672
69.065
1.00
6.28
DIC

ATOM
1478
O
TYR
186
22.640
45.679
68.913
1.00
5.43
DIC

ATOM
1479
N
GLN
187
20.676
44.587
68.907
1.00
5.24
DIC

ATOM
1480
CA
GLN
187
21.217
43.316
68.445
1.00
5.09
DIC

ATOM
1481
CB
GLN
187
21.306
43.393
66.913
1.00
6.13
DIC

ATOM
1482
CG
GLN
187
20.085
44.111
66.309
1.00
6.96
DIC

ATOM
1483
CD
GLN
187
20.155
44.327
64.800
1.00
9.84
DIC

ATOM
1484
OE1
GLN
187
21.221
44.577
64.235
1.00
11.83
DIC

ATOM
1485
NE2
GLN
187
19.005
44.262
64.150
1.00
8.23
DIC

ATOM
1486
C
GLN
187
22.550
42.857
69.065
1.00
4.73
DIC

ATOM
1487
O
GLN
187
22.659
42.726
70.285
1.00
5.09
DIC

ATOM
1488
N
ASP
188
23.561
42.608
68.235
1.00
4.04
DIC

ATOM
1489
CA
ASP
188
24.849
42.128
68.740
1.00
4.79
DIC

ATOM
1490
CB
ASP
188
25.832
41.901
67.589
1.00
5.88
DIC

ATOM
1491
CG
ASP
188
26.115
43.164
66.807
1.00
7.65
DIC

ATOM
1492
OD1
ASP
188
25.242
43.574
66.013
1.00
8.96
DIC

ATOM
1493
OD2
ASP
188
27.203
43.747
66.990
1.00
5.04
DIC

ATOM
1494
C
ASP
188
25.493
43.049
69.770
1.00
4.86
DIC

ATOM
1495
O
ASP
188
26.208
42.595
70.671
1.00
3.28
DIC

ATOM
1496
N
GLN
189
25.236
44.342
69.633
1.00
4.17
DIC

ATOM
1497
CA
GLN
189
25.789
45.334
70.547
1.00
5.49
DIC

ATOM
1498
CB
GLN
189
25.421
46.730
70.050
1.00
4.71
DIC

ATOM
1499
CG
GLN
189
26.008
47.868
70.848
1.00
5.10
DIC

ATOM
1500
CD
GLN
189
25.851
49.189
70.117
1.00
6.21
DIC

ATOM
1501
OE1
GLN
189
26.760
49.634
69.414
1.00
6.99
DIC

ATOM
1502
NE2
GLN
189
24.684
49.809
70.258
1.00
5.59
DIC

ATOM
1503
C
GLN
189
25.258
45.101
71.963
1.00
5.73
DIC

ATOM
1504
O
GLN
189
25.990
45.232
72.940
1.00
5.04
DIC

ATOM
1505
N
ASP
190
23.980
44.755
72.064
1.00
6.60
DIC

ATOM
1506
CA
ASP
190
23.371
44.480
73.361
1.00
6.99
DIC

ATOM
1507
CB
ASP
190
21.873
44.203
73.200
1.00
6.82
DIC

ATOM
1508
CG
ASP
190
21.061
45.466
72.999
1.00
7.01
DIC

ATOM
1509
OD1
ASP
190
19.957
45.369
72.422
1.00
5.87
DIC

ATOM
1510
OD2
ASP
190
21.515
46.547
73.428
1.00
5.97
DIC

ATOM
1511
C
ASP
190
24.040
43.256
73.976
1.00
6.81
DIC

ATOM
1512
O
ASP
190
24.454
43.277
75.135
1.00
8.46
DIC

ATOM
1513
N
ILE
191
24.135
42.188
73.187
1.00
6.27
DIC

ATOM
1514
CA
ILE
191
24.747
40.947
73.645
1.00
5.03
DIC

ATOM
1515
CB
ILE
191
24.896
39.932
72.487
1.00
3.31
DIC

ATOM
1516
CG2
ILE
191
25.566
38.655
72.999
1.00
1.40
DIC

ATOM
1517
CG1
ILE
191
23.518
39.598
71.909
1.00
4.10
DIC

ATOM
1518
CD
ILE
191
23.555
38.693
70.687
1.00
1.67
DIC

ATOM
1519
C
ILE
191
26.118
41.188
74.259
1.00
5.12
DIC

ATOM
1520
O
ILE
191
26.389
40.751
75.376
1.00
6.29
DIC

ATOM
1521
N
LEU
192
26.979
41.890
73.529
1.00
4.92
DIC

ATOM
1522
CA
LEU
192
28.326
42.168
74.009
1.00
5.86
DIC

ATOM
1523
CB
LEU
192
29.107
42.956
72.955
1.00
6.75
DIC

ATOM
1524
CG
LEU
192
29.278
42.257
71.601
1.00
6.62
DIC

ATOM
1525
CD1
LEU
192
29.967
43.202
70.626
1.00
6.82
DIC

ATOM
1526
CD2
LEU
192
30.086
40.988
71.771
1.00
8.14
DIC

ATOM
1527
C
LEU
192
28.306
42.930
75.332
1.00
6.87
DIC

ATOM
1528
O
LEU
192
29.053
42.603
76.253
1.00
6.68
DIC

ATOM
1529
N
ASN
193
27.449
43.943
75.424
1.00
6.22
DIC

ATOM
1530
CA
ASN
193
27.339
44.732
76.650
1.00
8.19
DIC

ATOM
1531
CB
ASN
193
26.403
45.921
76.434
1.00
8.71
DIC

ATOM
1532
CG
ASN
193
27.139
47.159
75.972
1.00
9.44
DIC

ATOM
1533
OD1
ASN
193
27.826
47.814
76.760
1.00
7.46
DIC

ATOM
1534
ND2
ASN
193
27.007
47.487
74.690
1.00
6.34
DIC

ATOM
1535
C
ASN
193
26.827
43.897
77.815
1.00
7.45
DIC

ATOM
1536
O
ASN
193
27.355
43.977
78.926
1.00
9.83
DIC

ATOM
1537
N
GLY
194
25.798
43.099
77.556
1.00
7.11
DIC

ATOM
1538
CA
GLY
194
25.227
42.268
78.599
1.00
7.61
DIC

ATOM
1539
C
GLY
194
26.196
41.240
79.139
1.00
8.02
DIC

ATOM
1540
O
GLY
194
26.318
41.064
80.351
1.00
8.13
DIC

ATOM
1541
N
LEU
195
26.893
40.559
78.237
1.00
6.93
DIC

ATOM
1542
CA
LEU
195
27.851
39.539
78.632
1.00
8.13
DIC

ATOM
1543
CB
LEU
195
28.330
38.746
77.407
1.00
5.03
DIC

ATOM
1544
CG
LEU
195
27.361
37.849
76.641
1.00
6.16
DIC

ATOM
1545
CD1
LEU
195
28.134
37.104
75.553
1.00
5.85
DIC

ATOM
1546
CD2
LEU
195
26.693
36.861
77.591
1.00
6.84
DIC

ATOM
1547
C
LEU
195
29.086
40.077
79.349
1.00
7.32
DIC

ATOM
1548
O
LEU
195
29.555
39.478
80.314
1.00
6.97
DIC

ATOM
1549
N
PHE
196
29.609
41.205
78.882
1.00
8.32
DIC

ATOM
1550
CA
PHE
196
30.842
41.739
79.448
1.00
6.43
DIC

ATOM
1551
CB
PHE
196
31.788
42.122
78.302
1.00
7.48
DIC

ATOM
1552
CG
PHE
196
31.994
41.021
77.293
1.00
7.64
DIC

ATOM
1553
CD1
PHE
196
32.079
39.694
77.702
1.00
7.32
DIC

ATOM
1554
CD2
PHE
196
32.138
41.315
75.939
1.00
8.39
DIC

ATOM
1555
CE1
PHE
196
32.309
38.669
76.783
1.00
9.53
DIC

ATOM
1556
CE2
PHE
196
32.370
40.300
75.008
1.00
8.57
DIC

ATOM
1557
CZ
PHE
196
32.456
38.974
75.431
1.00
9.27
DIC

ATOM
1558
C
PHE
196
30.773
42.883
80.453
1.00
7.23
DIC

ATOM
1559
O
PHE
196
31.813
43.342
80.931
1.00
6.97
DIC

ATOM
1560
N
LYS
197
29.571
43.340
80.787
1.00
7.17
DIC

ATOM
1561
CA
LYS
197
29.430
44.428
81.745
1.00
7.37
DIC

ATOM
1562
CB
LYS
197
27.950
44.632
82.106
1.00
8.11
DIC

ATOM
1563
CG
LYS
197
27.239
43.431
82.719
1.00
9.34
DIC

ATOM
1564
CD
LYS
197
25.752
43.730
82.867
1.00
7.17
DIC

ATOM
1565
CE
LYS
197
24.991
42.602
83.562
1.00
9.65
DIC

ATOM
1566
NZ
LYS
197
25.011
41.324
82.791
1.00
9.78
DIC

ATOM
1567
C
LYS
197
30.260
44.164
83.001
1.00
8.15
DIC

ATOM
1568
O
LYS
197
30.289
43.049
83.517
1.00
6.36
DIC

ATOM
1569
N
GLY
198
30.951
45.194
83.478
1.00
8.63
DIC

ATOM
1570
CA
GLY
198
31.781
45.043
84.660
1.00
9.48
DIC

ATOM
1571
C
GLY
198
33.170
44.550
84.307
1.00
11.16
DIC

ATOM
1572
O
GLY
198
34.065
44.534
85.151
1.00
11.56
DIC

ATOM
1573
N
GLY
199
33.353
44.147
83.052
1.00
9.98
DIC

ATOM
1574
CA
GLY
199
34.649
43.656
82.617
1.00
10.95
DIC

ATOM
1575
C
GLY
199
35.067
44.312
81.315
1.00
11.00
DIC

ATOM
1576
O
GLY
199
35.598
43.659
80.420
1.00
10.44
DIC

ATOM
1577
N
VAL
200
34.823
45.614
81.217
1.00
9.87
DIC

ATOM
1578
CA
VAL
200
35.159
46.377
80.022
1.00
10.31
DIC

ATOM
1579
CB
VAL
200
33.890
47.027
79.405
1.00
9.97
DIC

ATOM
1580
CG1
VAL
200
34.265
47.857
78.186
1.00
13.00
DIC

ATOM
1581
CG2
VAL
200
32.884
45.955
79.018
1.00
9.98
DIC

ATOM
1582
C
VAL
200
36.157
47.492
80.315
1.00
9.00
DIC

ATOM
1583
O
VAL
200
36.037
48.197
81.316
1.00
9.62
DIC

ATOM
1584
N
CYS
201
37.149
47.633
79.443
1.00
10.08
DIC

ATOM
1585
CA
CYS
201
38.137
48.696
79.561
1.00
11.93
DIC

ATOM
1586
CB
CYS
201
39.508
48.204
79.102
1.00
16.16
DIC

ATOM
1587
SG
CYS
201
40.754
49.497
78.999
1.00
22.80
DIC

ATOM
1588
C
CYS
201
37.624
49.778
78.615
1.00
12.32
DIC

ATOM
1589
O
CYS
201
37.383
49.504
77.438
1.00
11.10
DIC

ATOM
1590
N
TYR
202
37.434
50.998
79.110
1.00
11.44
DIC

ATOM
1591
CA
TYR
202
36.914
52.051
78.245
1.00
11.56
DIC

ATOM
1592
CB
TYR
202
36.008
53.001
79.034
1.00
13.47
DIC

ATOM
1593
CG
TYR
202
34.888
52.317
79.784
1.00
12.77
DIC

ATOM
1594
CD1
TYR
202
34.977
52.112
81.159
1.00
14.55
DIC

ATOM
1595
CE1
TYR
202
33.950
51.501
81.865
1.00
15.50
DIC

ATOM
1596
CD2
TYR
202
33.734
51.884
79.124
1.00
13.35
DIC

ATOM
1597
CE2
TYR
202
32.695
51.263
79.824
1.00
13.55
DIC

ATOM
1598
CZ
TYR
202
32.815
51.080
81.197
1.00
14.96
DIC

ATOM
1599
OH
TYR
202
31.801
50.494
81.912
1.00
15.14
DIC

ATOM
1600
C
TYR
202
37.998
52.860
77.543
1.00
12.95
DIC

ATOM
1601
O
TYR
202
38.970
53.291
78.160
1.00
12.67
DIC

ATOM
1602
N
ALA
203
37.818
53.060
76.243
1.00
12.15
DIC

ATOM
1603
CA
ALA
203
38.762
53.829
75.443
1.00
12.67
DIC

ATOM
1604
CB
ALA
203
39.001
53.134
74.107
1.00
11.34
DIC

ATOM
1605
C
ALA
203
38.181
55.220
75.212
1.00
11.62
DIC

ATOM
1606
O
ALA
203
36.968
55.412
75.300
1.00
10.59
DIC

ATOM
1607
N
ASN
204
39.041
56.188
74.916
1.00
10.55
DIC

ATOM
1608
CA
ASN
204
38.575
57.550
74.669
1.00
9.36
DIC

ATOM
1609
CB
ASN
204
39.758
58.498
74.487
1.00
7.28
DIC

ATOM
1610
CG
ASN
204
39.333
59.943
74.432
1.00
9.32
DIC

ATOM
1611
OD1
ASN
204
39.037
60.559
75.463
1.00
9.40
DIC

ATOM
1612
ND2
ASN
204
39.281
60.494
73.226
1.00
5.22
DIC

ATOM
1613
C
ASN
204
37.711
57.566
73.411
1.00
8.45
DIC

ATOM
1614
O
ASN
204
37.921
56.771
72.493
1.00
8.52
DIC

ATOM
1615
N
SER
205
36.743
58.474
73.370
1.00
6.68
DIC

ATOM
1616
CA
SER
205
35.845
58.573
72.227
1.00
8.43
DIC

ATOM
1617
CB
SER
205
34.708
59.552
72.539
1.00
6.55
DIC

ATOM
1618
OG
SER
205
33.769
58.945
73.415
1.00
5.21
DIC

ATOM
1619
C
SER
205
36.520
58.947
70.908
1.00
8.25
DIC

ATOM
1620
O
SER
205
35.890
58.884
69.846
1.00
7.41
DIC

ATOM
1621
N
ARG
206
37.796
59.324
70.959
1.00
6.24
DIC

ATOM
1622
CA
ARG
206
38.503
59.664
69.727
1.00
5.53
DIC

ATOM
1623
CB
ARG
206
39.901
60.235
70.031
1.00
5.02
DIC

ATOM
1624
CG
ARG
206
40.916
59.262
70.645
1.00
3.89
DIC

ATOM
1625
CD
ARG
206
42.220
60.002
71.003
1.00
6.14
DIC

ATOM
1626
NE
ARG
206
42.757
60.730
69.852
1.00
5.51
DIC

ATOM
1627
CZ
ARG
206
43.820
60.352
69.145
1.00
6.07
DIC

ATOM
1628
NH1
ARG
206
44.486
59.252
69.471
1.00
5.54
DIC

ATOM
1629
NH2
ARG
206
44.196
61.056
68.086
1.00
3.75
DIC

ATOM
1630
C
ARG
206
38.625
58.421
68.844
1.00
4.90
DIC

ATOM
1631
O
ARG
206
38.815
58.525
67.632
1.00
5.35
DIC

ATOM
1632
N
PHE
207
38.501
57.246
69.455
1.00
4.24
DIC

ATOM
1633
CA
PHE
207
38.612
55.988
68.722
1.00
4.90
DIC

ATOM
1634
CB
PHE
207
39.326
54.945
69.588
1.00
4.86
DIC

ATOM
1635
CG
PHE
207
40.764
55.288
69.875
1.00
5.99
DIC

ATOM
1636
CD1
PHE
207
41.176
55.620
71.162
1.00
5.64
DIC

ATOM
1637
CD2
PHE
207
41.700
55.322
68.842
1.00
4.91
DIC

ATOM
1638
CE1
PHE
207
42.497
55.983
71.417
1.00
7.00
DIC

ATOM
1639
CE2
PHE
207
43.024
55.684
69.085
1.00
7.26
DIC

ATOM
1640
CZ
PHE
207
43.424
56.016
70.375
1.00
6.13
DIC

ATOM
1641
C
PHE
207
37.276
55.439
68.224
1.00
5.37
DIC

ATOM
1642
O
PHE
207
37.208
54.338
67.682
1.00
6.61
DIC

ATOM
1643
N
ASN
208
36.215
56.214
68.414
1.00
5.44
DIC

ATOM
1644
CA
ASN
208
34.882
55.831
67.963
1.00
7.19
DIC

ATOM
1645
CB
ASN
208
34.279
54.752
68.863
1.00
4.53
DIC

ATOM
1646
CG
ASN
208
33.112
54.038
68.201
1.00
4.94
DIC

ATOM
1647
OD1
ASN
208
32.464
54.587
67.304
1.00
3.79
DIC

ATOM
1648
ND2
ASN
208
32.832
52.814
68.645
1.00
3.51
DIC

ATOM
1649
C
ASN
208
34.037
57.094
68.026
1.00
7.68
DIC

ATOM
1650
O
ASN
208
33.170
57.241
68.888
1.00
7.11
DIC

ATOM
1651
N
PHE
209
34.315
57.998
67.093
1.00
6.81
DIC

ATOM
1652
CA
PHE
209
33.647
59.288
67.004
1.00
8.34
DIC

ATOM
1653
CB
PHE
209
34.636
60.315
66.439
1.00
8.19
DIC

ATOM
1654
CG
PHE
209
34.226
61.740
66.648
1.00
7.78
DIC

ATOM
1655
CD1
PHE
209
34.260
62.308
67.918
1.00
8.92
DIC

ATOM
1656
CD2
PHE
209
33.830
62.525
65.569
1.00
9.53
DIC

ATOM
1657
CE1
PHE
209
33.907
63.644
68.112
1.00
11.27
DIC

ATOM
1658
CE2
PHE
209
33.476
63.858
65.751
1.00
8.49
DIC

ATOM
1659
CZ
PHE
209
33.515
64.419
67.025
1.00
9.96
DIC

ATOM
1660
C
PHE
209
32.431
59.166
66.094
1.00
8.23
DIC

ATOM
1661
O
PHE
209
32.569
59.073
64.877
1.00
8.27
DIC

ATOM
1662
N
MSE
210
31.244
59.179
66.692
1.00
7.38
DIC

ATOM
1663
CA
MSE
210
29.999
59.037
65.941
1.00
9.26
DIC

ATOM
1664
CB
MSE
210
29.159
57.918
66.581
1.00
9.05
DIC

ATOM
1665
CG
MSE
210
29.866
56.564
66.584
1.00
10.93
DIC

ATOM
1666
SE
MSE
210
29.082
55.239
67.779
1.00
18.26
DIC

ATOM
1667
CE
MSE
210
30.053
55.690
69.381
1.00
8.17
DIC

ATOM
1668
C
MSE
210
29.195
60.338
65.870
1.00
8.65
DIC

ATOM
1669
O
MSE
210
29.562
61.340
66.486
1.00
6.86
DIC

ATOM
1670
N
PRO
211
28.086
60.343
65.105
1.00
9.68
DIC

ATOM
1671
CD
PRO
211
27.573
59.289
64.211
1.00
9.09
DIC

ATOM
1672
CA
PRO
211
27.266
61.554
64.990
1.00
9.29
DIC

ATOM
1673
CB
PRO
211
26.037
61.058
64.240
1.00
9.60
DIC

ATOM
1674
CG
PRO
211
26.637
60.064
63.296
1.00
10.03
DIC

ATOM
1675
C
PRO
211
26.918
62.189
66.335
1.00
10.27
DIC

ATOM
1676
O
PRO
211
26.973
63.413
66.482
1.00
10.62
DIC

ATOM
1677
N
THR
212
26.572
61.367
67.322
1.00
7.87
DIC

ATOM
1678
CA
THR
212
26.222
61.906
68.629
1.00
8.03
DIC

ATOM
1679
CB
THR
212
25.663
60.807
69.561
1.00
8.27
DIC

ATOM
1680
OG1
THR
212
24.528
60.191
68.939
1.00
9.40
DIC

ATOM
1681
CG2
THR
212
25.216
61.410
70.886
1.00
9.47
DIC

ATOM
1682
C
THR
212
27.422
62.594
69.285
1.00
8.51
DIC

ATOM
1683
O
THR
212
27.266
63.607
69.975
1.00
8.07
DIC

ATOM
1684
N
ASN
213
28.616
62.046
69.074
1.00
6.60
DIC

ATOM
1685
CA
ASN
213
29.827
62.641
69.628
1.00
7.57
DIC

ATOM
1686
CB
ASN
213
31.047
61.768
69.315
1.00
7.05
DIC

ATOM
1687
CG
ASN
213
30.968
60.395
69.967
1.00
5.69
DIC

ATOM
1688
OD1
ASN
213
31.421
60.198
71.098
1.00
5.17
DIC

ATOM
1689
ND2
ASN
213
30.379
59.443
69.259
1.00
2.99
DIC

ATOM
1690
C
ASN
213
30.007
64.017
68.990
1.00
9.85
DIC

ATOM
1691
O
ASN
213
30.326
64.991
69.666
1.00
11.63
DIC

ATOM
1692
N
TYR
214
29.801
64.082
67.679
1.00
10.25
DIC

ATOM
1693
CA
TYR
214
29.926
65.333
66.945
1.00
12.74
DIC

ATOM
1694
CB
TYR
214
29.671
65.103
65.451
1.00
15.29
DIC

ATOM
1695
CG
TYR
214
29.730
66.365
64.619
1.00
17.71
DIC

ATOM
1696
CD1
TYR
214
30.950
66.894
64.203
1.00
19.79
DIC

ATOM
1697
CE1
TYR
214
31.011
68.072
63.461
1.00
21.10
DIC

ATOM
1698
CD2
TYR
214
28.564
67.049
64.271
1.00
19.74
DIC

ATOM
1699
CE2
TYR
214
28.612
68.230
63.530
1.00
22.09
DIC

ATOM
1700
CZ
TYR
214
29.838
68.735
63.128
1.00
22.87
DIC

ATOM
1701
OH
TYR
214
29.892
69.901
62.393
1.00
24.30
DIC

ATOM
1702
C
TYR
214
28.922
66.347
67.481
1.00
13.83
DIC

ATOM
1703
O
TYR
214
29.276
67.490
67.761
1.00
12.55
DIC

ATOM
1704
N
ALA
215
27.669
65.923
67.625
1.00
15.46
DIC

ATOM
1705
CA
ALA
215
26.615
66.803
68.124
1.00
17.53
DIC

ATOM
1706
CB
ALA
215
25.271
66.081
68.099
1.00
15.12
DIC

ATOM
1707
C
ALA
215
26.919
67.288
69.539
1.00
19.46
DIC

ATOM
1708
O
ALA
215
26.509
68.381
69.931
1.00
19.21
DIC

ATOM
1709
N
ALA
216
27.639
66.471
70.300
1.00
21.21
DIC

ATOM
1710
CA
ALA
216
27.991
66.821
71.669
1.00
24.59
DIC

ATOM
1711
CB
ALA
216
28.459
65.580
72.421
1.00
23.56
DIC

ATOM
1712
C
ALA
216
29.069
67.905
71.713
1.00
27.77
DIC

ATOM
1713
O
ALA
216
29.317
68.497
72.762
1.00
27.20
DIC

ATOM
1714
N
MSE
217
29.703
68.166
70.573
1.00
31.06
DIC

ATOM
1715
CA
MSE
217
30.743
69.189
70.498
1.00
34.21
DIC

ATOM
1716
CB
MSE
217
31.385
69.208
69.107
1.00
35.99
DIC

ATOM
1717
CG
MSE
217
32.193
67.966
68.760
1.00
39.28
DIC

ATOM
1718
SE
MSE
217
33.550
67.557
70.080
1.00
45.10
DIC

ATOM
1719
CE
MSE
217
34.867
68.888
69.607
1.00
42.38
DIC

ATOM
1720
C
MSE
217
30.175
70.570
70.809
1.00
35.31
DIC

ATOM
1721
O
MSE
217
29.016
70.860
70.503
1.00
36.62
DIC

ATOM
1722
N
ALA
222
25.134
68.364
77.425
1.00
31.46
DIC

ATOM
1723
CA
ALA
222
24.583
68.352
78.775
1.00
31.66
DIC

ATOM
1724
CB
ALA
222
23.312
67.513
78.813
1.00
32.95
DIC

ATOM
1725
C
ALA
222
25.604
67.803
79.765
1.00
31.68
DIC

ATOM
1726
O
ALA
222
26.479
68.538
80.229
1.00
32.14
DIC

ATOM
1727
N
ALA
223
25.483
66.511
80.071
1.00
31.10
DIC

ATOM
1728
CA
ALA
223
26.370
65.807
81.003
1.00
30.32
DIC

ATOM
1729
CB
ALA
223
26.806
66.741
82.137
1.00
30.79
DIC

ATOM
1730
C
ALA
223
25.626
64.605
81.581
1.00
28.04
DIC

ATOM
1731
O
ALA
223
24.856
64.749
82.528
1.00
29.66
DIC

ATOM
1732
N
ALA
224
25.856
63.422
81.018
1.00
27.00
DIC

ATOM
1733
CA
ALA
224
25.171
62.219
81.490
1.00
25.23
DIC

ATOM
1734
CB
ALA
224
25.440
61.057
80.543
1.00
25.60
DIC

ATOM
1735
C
ALA
224
25.530
61.817
82.918
1.00
24.60
DIC

ATOM
1736
O
ALA
224
24.642
61.593
83.742
1.00
24.76
DIC

ATOM
1737
N
HIS
225
26.825
61.716
83.206
1.00
23.10
DIC

ATOM
1738
CA
HIS
225
27.297
61.330
84.534
1.00
21.99
DIC

ATOM
1739
CB
HIS
225
27.907
59.926
84.490
1.00
22.53
DIC

ATOM
1740
CG
HIS
225
26.949
58.857
84.064
1.00
22.70
DIC

ATOM
1741
CD2
HIS
225
26.829
58.183
82.896
1.00
21.83
DIC

ATOM
1742
ND1
HIS
225
25.966
58.364
84.894
1.00
21.91
DIC

ATOM
1743
CE1
HIS
225
25.282
57.430
84.256
1.00
22.15
DIC

ATOM
1744
NE2
HIS
225
25.786
57.301
83.041
1.00
21.79
DIC

ATOM
1745
C
HIS
225
28.357
62.307
85.039
1.00
21.96
DIC

ATOM
1746
O
HIS
225
29.052
62.940
84.243
1.00
21.13
DIC

ATOM
1747
N
THR
226
28.480
62.422
86.360
1.00
21.29
DIC

ATOM
1748
CA
THR
226
29.474
63.313
86.956
1.00
20.93
DIC

ATOM
1749
CB
THR
226
29.032
63.827
88.347
1.00
20.27
DIC

ATOM
1750
OG1
THR
226
28.812
62.715
89.225
1.00
23.22
DIC

ATOM
1751
CG2
THR
226
27.756
64.637
88.233
1.00
21.25
DIC

ATOM
1752
C
THR
226
30.790
62.562
87.108
1.00
19.54
DIC

ATOM
1753
O
THR
226
31.854
63.168
87.205
1.00
19.24
DIC

ATOM
1754
N
ASP
227
30.702
61.236
87.133
1.00
18.16
DIC

ATOM
1755
CA
ASP
227
31.875
60.379
87.256
1.00
17.84
DIC

ATOM
1756
CB
ASP
227
31.512
58.958
86.827
1.00
19.84
DIC

ATOM
1757
CG
ASP
227
32.706
58.030
86.808
1.00
20.03
DIC

ATOM
1758
OD1
ASP
227
32.607
56.955
86.185
1.00
21.19
DIC

ATOM
1759
OD2
ASP
227
33.740
58.369
87.420
1.00
22.49
DIC

ATOM
1760
C
ASP
227
33.028
60.889
86.386
1.00
18.14
DIC

ATOM
1761
O
ASP
227
32.904
60.971
85.165
1.00
16.47
DIC

ATOM
1762
N
PRO
228
34.167
61.233
87.006
1.00
17.73
DIC

ATOM
1763
CD
PRO
228
34.480
61.151
88.443
1.00
18.17
DIC

ATOM
1764
CA
PRO
228
35.321
61.731
86.250
1.00
17.33
DIC

ATOM
1765
CB
PRO
228
36.363
61.995
87.339
1.00
18.94
DIC

ATOM
1766
CG
PRO
228
35.980
61.034
88.425
1.00
20.23
DIC

ATOM
1767
C
PRO
228
35.827
60.772
85.172
1.00
16.87
DIC

ATOM
1768
O
PRO
228
36.297
61.209
84.122
1.00
15.06
DIC

ATOM
1769
N
LEU
229
35.737
59.470
85.428
1.00
15.80
DIC

ATOM
1770
CA
LEU
229
36.188
58.496
84.446
1.00
15.66
DIC

ATOM
1771
CB
LEU
229
36.155
57.079
85.033
1.00
16.65
DIC

ATOM
1772
CG
LEU
229
36.728
55.969
84.147
1.00
17.28
DIC

ATOM
1773
CD1
LEU
229
37.236
54.824
85.008
1.00
18.64
DIC

ATOM
1774
CD2
LEU
229
35.661
55.487
83.172
1.00
15.76
DIC

ATOM
1775
C
LEU
229
35.281
58.596
83.224
1.00
14.21
DIC

ATOM
1776
O
LEU
229
35.759
58.658
82.092
1.00
15.12
DIC

ATOM
1777
N
TYR
230
33.972
58.628
83.457
1.00
14.01
DIC

ATOM
1778
CA
TYR
230
33.017
58.739
82.363
1.00
11.87
DIC

ATOM
1779
CB
TYR
230
31.585
58.846
82.895
1.00
14.20
DIC

ATOM
1780
CG
TYR
230
30.544
58.919
81.794
1.00
11.26
DIC

ATOM
1781
CD1
TYR
230
30.146
57.774
81.105
1.00
13.91
DIC

ATOM
1782
CE1
TYR
230
29.222
57.840
80.061
1.00
10.82
DIC

ATOM
1783
CD2
TYR
230
29.991
60.139
81.414
1.00
12.75
DIC

ATOM
1784
CE2
TYR
230
29.066
60.218
80.371
1.00
12.59
DIC

ATOM
1785
CZ
TYR
230
28.688
59.062
79.700
1.00
12.84
DIC

ATOM
1786
OH
TYR
230
27.779
59.132
78.665
1.00
11.30
DIC

ATOM
1787
C
TYR
230
33.332
59.983
81.538
1.00
11.96
DIC

ATOM
1788
O
TYR
230
33.441
59.913
80.317
1.00
9.30
DIC

ATOM
1789
N
ARG
231
33.472
61.119
82.218
1.00
11.98
DIC

ATOM
1790
CA
ARG
231
33.770
62.390
81.558
1.00
13.86
DIC

ATOM
1791
CB
ARG
231
33.823
63.515
82.598
1.00
16.38
DIC

ATOM
1792
CG
ARG
231
32.472
63.840
83.225
1.00
19.41
DIC

ATOM
1793
CD
ARG
231
32.635
64.503
84.588
1.00
24.54
DIC

ATOM
1794
NE
ARG
231
33.603
65.598
84.574
1.00
30.72
DIC

ATOM
1795
CZ
ARG
231
33.449
66.731
83.895
1.00
31.79
DIC

ATOM
1796
NH1
ARG
231
34.390
67.667
83.945
1.00
33.17
DIC

ATOM
1797
NH2
ARG
231
32.357
66.934
83.172
1.00
34.16
DIC

ATOM
1798
C
ARG
231
35.082
62.340
80.779
1.00
13.10
DIC

ATOM
1799
O
ARG
231
35.179
62.861
79.666
1.00
12.39
DIC

ATOM
1800
N
ASP
232
36.097
61.724
81.372
1.00
12.75
DIC

ATOM
1801
CA
ASP
232
37.393
61.609
80.716
1.00
12.99
DIC

ATOM
1802
CB
ASP
232
38.396
60.936
81.656
1.00
14.85
DIC

ATOM
1803
CG
ASP
232
39.709
60.610
80.973
1.00
16.86
DIC

ATOM
1804
OD1
ASP
232
39.794
59.558
80.306
1.00
18.36
DIC

ATOM
1805
OD2
ASP
232
40.656
61.412
81.094
1.00
16.54
DIC

ATOM
1806
C
ASP
232
37.302
60.819
79.406
1.00
12.82
DIC

ATOM
1807
O
ASP
232
37.864
61.224
78.387
1.00
10.29
DIC

ATOM
1808
N
ARG
233
36.584
59.699
79.435
1.00
10.29
DIC

ATOM
1809
CA
ARG
233
36.452
58.853
78.256
1.00
10.00
DIC

ATOM
1810
CB
ARG
233
35.932
57.470
78.661
1.00
9.23
DIC

ATOM
1811
CG
ARG
233
36.782
56.750
79.704
1.00
9.41
DIC

ATOM
1812
CD
ARG
233
38.153
56.364
79.163
1.00
8.38
DIC

ATOM
1813
NE
ARG
233
38.825
55.417
80.047
1.00
11.90
DIC

ATOM
1814
CZ
ARG
233
39.366
55.731
81.221
1.00
15.57
DIC

ATOM
1815
NH1
ARG
233
39.332
56.983
81.666
1.00
14.61
DIC

ATOM
1816
NH2
ARG
233
39.920
54.782
81.966
1.00
13.98
DIC

ATOM
1817
C
ARG
233
35.549
59.431
77.165
1.00
10.24
DIC

ATOM
1818
O
ARG
233
35.814
59.244
75.975
1.00
9.03
DIC

ATOM
1819
N
THR
234
34.490
60.132
77.564
1.00
8.98
DIC

ATOM
1820
CA
THR
234
33.559
60.693
76.592
1.00
10.49
DIC

ATOM
1821
CB
THR
234
32.141
60.811
77.183
1.00
10.70
DIC

ATOM
1822
OG1
THR
234
32.181
61.585
78.387
1.00
9.78
DIC

ATOM
1823
CG2
THR
234
31.587
59.416
77.488
1.00
8.75
DIC

ATOM
1824
C
THR
234
33.993
62.035
76.016
1.00
11.41
DIC

ATOM
1825
O
THR
234
33.481
62.459
74.982
1.00
11.24
DIC

ATOM
1826
N
ASN
235
34.924
62.710
76.681
1.00
9.83
DIC

ATOM
1827
CA
ASN
235
35.418
63.968
76.148
1.00
12.54
DIC

ATOM
1828
CB
ASN
235
36.045
64.845
77.232
1.00
15.96
DIC

ATOM
1829
CG
ASN
235
36.643
66.120
76.663
1.00
20.34
DIC

ATOM
1830
OD1
ASN
235
35.940
66.934
76.063
1.00
25.44
DIC

ATOM
1831
ND2
ASN
235
37.948
66.295
76.838
1.00
22.52
DIC

ATOM
1832
C
ASN
235
36.488
63.561
75.151
1.00
11.14
DIC

ATOM
1833
O
ASN
235
37.586
63.169
75.536
1.00
11.10
DIC

ATOM
1834
N
THR
236
36.154
63.638
73.870
1.00
11.67
DIC

ATOM
1835
CA
THR
236
37.081
63.260
72.813
1.00
11.17
DIC

ATOM
1836
CB
THR
236
36.413
63.396
71.433
1.00
11.34
DIC

ATOM
1837
OG1
THR
236
35.373
62.417
71.318
1.00
10.79
DIC

ATOM
1838
CG2
THR
236
37.431
63.197
70.315
1.00
9.33
DIC

ATOM
1839
C
THR
236
38.355
64.090
72.827
1.00
11.07
DIC

ATOM
1840
O
THR
236
38.307
65.320
72.919
1.00
11.47
DIC

ATOM
1841
N
VAL
237
39.494
63.409
72.754
1.00
10.07
DIC

ATOM
1842
CA
VAL
237
40.785
64.086
72.729
1.00
12.15
DIC

ATOM
1843
CB
VAL
237
41.865
63.310
73.523
1.00
12.90
DIC

ATOM
1844
CG1
VAL
237
43.208
64.035
73.423
1.00
13.23
DIC

ATOM
1845
CG2
VAL
237
41.448
63.183
74.980
1.00
13.18
DIC

ATOM
1846
C
VAL
237
41.210
64.177
71.268
1.00
12.16
DIC

ATOM
1847
O
VAL
237
41.583
63.175
70.654
1.00
12.69
DIC

ATOM
1848
N
MSE
238
41.133
65.381
70.714
1.00
12.20
DIC

ATOM
1849
CA
MSE
238
41.495
65.611
69.320
1.00
12.91
DIC

ATOM
1850
CB
MSE
238
41.283
67.081
68.960
1.00
15.07
DIC

ATOM
1851
CG
MSE
238
39.831
67.539
69.018
1.00
19.98
DIC

ATOM
1852
SE
MSE
238
38.678
66.551
67.809
1.00
27.67
DIC

ATOM
1853
CE
MSE
238
37.206
66.207
69.005
1.00
27.27
DIC

ATOM
1854
C
MSE
238
42.942
65.221
69.044
1.00
12.33
DIC

ATOM
1855
O
MSE
238
43.784
65.268
69.938
1.00
12.98
DIC

ATOM
1856
N
PRO
239
43.248
64.827
67.795
1.00
11.27
DIC

ATOM
1857
CD
PRO
239
44.633
64.625
67.335
1.00
13.15
DIC

ATOM
1858
CA
PRO
239
42.314
64.730
66.667
1.00
11.13
DIC

ATOM
1859
CB
PRO
239
43.239
64.787
65.455
1.00
12.20
DIC

ATOM
1860
CG
PRO
239
44.434
64.051
65.942
1.00
12.26
DIC

ATOM
1861
C
PRO
239
41.507
63.437
66.693
1.00
11.12
DIC

ATOM
1862
O
PRO
239
41.875
62.481
67.381
1.00
11.27
DIC

ATOM
1863
N
VAL
240
40.406
63.411
65.947
1.00
10.78
DIC

ATOM
1864
CA
VAL
240
39.582
62.212
65.873
1.00
8.88
DIC

ATOM
1865
CB
VAL
240
38.332
62.435
64.987
1.00
10.97
DIC

ATOM
1866
CG1
VAL
240
37.571
61.120
64.817
1.00
11.55
DIC

ATOM
1867
CG2
VAL
240
37.428
63.490
65.617
1.00
10.39
DIC

ATOM
1868
C
VAL
240
40.464
61.143
65.239
1.00
8.25
DIC

ATOM
1869
O
VAL
240
41.174
61.419
64.273
1.00
8.08
DIC

ATOM
1870
N
ALA
241
40.448
59.939
65.802
1.00
5.68
DIC

ATOM
1871
CA
ALA
241
41.255
58.844
65.277
1.00
5.69
DIC

ATOM
1872
CB
ALA
241
41.887
58.055
66.424
1.00
5.65
DIC

ATOM
1873
C
ALA
241
40.389
57.929
64.424
1.00
6.50
DIC

ATOM
1874
O
ALA
241
40.853
57.370
63.431
1.00
4.72
DIC

ATOM
1875
N
VAL
242
39.124
57.786
64.809
1.00
6.23
DIC

ATOM
1876
CA
VAL
242
38.204
56.940
64.058
1.00
5.56
DIC

ATOM
1877
CB
VAL
242
37.989
55.571
64.759
1.00
5.40
DIC

ATOM
1878
CG1
VAL
242
37.029
54.707
63.939
1.00
5.43
DIC

ATOM
1879
CG2
VAL
242
39.325
54.859
64.941
1.00
6.26
DIC

ATOM
1880
C
VAL
242
36.838
57.583
63.879
1.00
6.91
DIC

ATOM
1881
O
VAL
242
36.149
57.868
64.860
1.00
6.73
DIC

ATOM
1882
N
SER
243
36.462
57.823
62.623
1.00
6.89
DIC

ATOM
1883
CA
SER
243
35.148
58.370
62.300
1.00
7.37
DIC

ATOM
1884
CB
SER
243
35.177
59.164
60.985
1.00
9.26
DIC

ATOM
1885
OG
SER
243
35.627
60.492
61.187
1.00
12.73
DIC

ATOM
1886
C
SER
243
34.248
57.153
62.120
1.00
7.64
DIC

ATOM
1887
O
SER
243
34.542
56.279
61.309
1.00
7.80
DIC

ATOM
1888
N
HIS
244
33.164
57.082
62.882
1.00
6.24
DIC

ATOM
1889
CA
HIS
244
32.247
55.952
62.779
1.00
7.04
DIC

ATOM
1890
CB
HIS
244
32.209
55.183
64.103
1.00
5.69
DIC

ATOM
1891
CG
HIS
244
31.327
53.973
64.075
1.00
5.79
DIC

ATOM
1892
CD2
HIS
244
30.668
53.373
63.055
1.00
5.25
DIC

ATOM
1893
ND1
HIS
244
31.040
53.235
65.204
1.00
5.99
DIC

ATOM
1894
CE1
HIS
244
30.242
52.233
64.880
1.00
8.18
DIC

ATOM
1895
NE2
HIS
244
30.001
52.294
63.583
1.00
4.85
DIC

ATOM
1896
C
HIS
244
30.853
56.464
62.424
1.00
6.27
DIC

ATOM
1897
O
HIS
244
30.195
57.118
63.230
1.00
7.86
DIC

ATOM
1898
N
TYR
245
30.410
56.148
61.213
1.00
6.95
DIC

ATOM
1899
CA
TYR
245
29.112
56.585
60.719
1.00
8.61
DIC

ATOM
1900
CB
TYR
245
29.187
56.715
59.198
1.00
9.86
DIC

ATOM
1901
CG
TYR
245
30.263
57.699
58.815
1.00
10.60
DIC

ATOM
1902
CD1
TYR
245
30.062
59.070
58.974
1.00
12.04
DIC

ATOM
1903
CE1
TYR
245
31.090
59.983
58.752
1.00
12.10
DIC

ATOM
1904
CD2
TYR
245
31.524
57.262
58.411
1.00
12.41
DIC

ATOM
1905
CE2
TYR
245
32.564
58.169
58.187
1.00
12.40
DIC

ATOM
1906
CZ
TYR
245
32.339
59.527
58.364
1.00
12.62
DIC

ATOM
1907
OH
TYR
245
33.364
60.428
58.185
1.00
13.88
DIC

ATOM
1908
C
TYR
245
27.988
55.658
61.147
1.00
9.69
DIC

ATOM
1909
O
TYR
245
27.229
55.142
60.319
1.00
9.49
DIC

ATOM
1910
N
CYS
246
27.895
55.471
62.461
1.00
9.14
DIC

ATOM
1911
CA
CYS
246
26.888
54.618
63.071
1.00
11.69
DIC

ATOM
1912
CB
CYS
246
27.054
54.634
64.595
1.00
11.19
DIC

ATOM
1913
SG
CYS
246
26.047
53.422
65.477
1.00
17.18
DIC

ATOM
1914
C
CYS
246
25.511
55.147
62.689
1.00
12.03
DIC

ATOM
1915
O
CYS
246
25.273
56.351
62.722
1.00
11.82
DIC

ATOM
1916
N
GLY
247
24.607
54.246
62.323
1.00
12.35
DIC

ATOM
1917
CA
GLY
247
23.275
54.674
61.940
1.00
12.18
DIC

ATOM
1918
C
GLY
247
23.036
54.572
60.443
1.00
13.09
DIC

ATOM
1919
O
GLY
247
23.949
54.244
59.685
1.00
12.04
DIC

ATOM
1920
N
PRO
248
21.811
54.874
59.985
1.00
14.33
DIC

ATOM
1921
CD
PRO
248
20.738
55.471
60.803
1.00
14.23
DIC

ATOM
1922
CA
PRO
248
21.412
54.819
58.575
1.00
15.43
DIC

ATOM
1923
CB
PRO
248
19.940
55.227
58.625
1.00
17.10
DIC

ATOM
1924
CG
PRO
248
19.912
56.199
59.769
1.00
16.43
DIC

ATOM
1925
C
PRO
248
22.214
55.678
57.594
1.00
14.95
DIC

ATOM
1926
O
PRO
248
22.395
55.294
56.441
1.00
15.51
DIC

ATOM
1927
N
ALA
249
22.692
56.832
58.044
1.00
15.80
DIC

ATOM
1928
CA
ALA
249
23.442
57.737
57.175
1.00
16.01
DIC

ATOM
1929
CB
ALA
249
23.403
59.152
57.748
1.00
17.18
DIC

ATOM
1930
C
ALA
249
24.889
57.294
56.964
1.00
16.42
DIC

ATOM
1931
O
ALA
249
25.748
57.533
57.811
1.00
16.26
DIC

ATOM
1932
N
LYS
250
25.152
56.658
55.825
1.00
14.75
DIC

ATOM
1933
CA
LYS
250
26.490
56.169
55.506
1.00
14.92
DIC

ATOM
1934
CB
LYS
250
26.407
54.766
54.901
1.00
11.81
DIC

ATOM
1935
CG
LYS
250
25.716
53.736
55.783
1.00
11.87
DIC

ATOM
1936
CD
LYS
250
26.383
53.603
57.153
1.00
10.01
DIC

ATOM
1937
CE
LYS
250
25.710
52.507
57.983
1.00
10.47
DIC

ATOM
1938
NZ
LYS
250
26.130
52.549
59.415
1.00
8.71
DIC

ATOM
1939
C
LYS
250
27.225
57.093
54.542
1.00
15.74
DIC

ATOM
1940
O
LYS
250
26.609
57.737
53.695
1.00
16.86
DIC

ATOM
1941
N
PRO
251
28.563
57.152
54.646
1.00
16.85
DIC

ATOM
1942
CD
PRO
251
29.427
56.337
55.520
1.00
16.47
DIC

ATOM
1943
CA
PRO
251
29.369
58.010
53.771
1.00
17.98
DIC

ATOM
1944
CB
PRO
251
30.782
57.836
54.326
1.00
16.79
DIC

ATOM
1945
CG
PRO
251
30.769
56.421
54.821
1.00
18.00
DIC

ATOM
1946
C
PRO
251
29.270
57.654
52.289
1.00
19.21
DIC

ATOM
1947
O
PRO
251
29.493
58.504
51.425
1.00
20.56
DIC

ATOM
1948
N
TRP
252
28.936
56.401
51.993
1.00
20.23
DIC

ATOM
1949
CA
TRP
252
28.807
55.966
50.604
1.00
20.95
DIC

ATOM
1950
CB
TRP
252
29.134
54.476
50.483
1.00
18.75
DIC

ATOM
1951
CG
TRP
252
28.377
53.604
51.431
1.00
15.29
DIC

ATOM
1952
CD2
TRP
252
28.895
52.971
52.607
1.00
13.13
DIC

ATOM
1953
CE2
TRP
252
27.839
52.236
53.185
1.00
11.47
DIC

ATOM
1954
CE3
TRP
252
30.151
52.952
53.227
1.00
11.22
DIC

ATOM
1955
CD1
TRP
252
27.065
53.243
51.347
1.00
14.01
DIC

ATOM
1956
NE1
TRP
252
26.733
52.420
52.397
1.00
12.89
DIC

ATOM
1957
CZ2
TRP
252
27.998
51.488
54.357
1.00
11.76
DIC

ATOM
1958
CZ3
TRP
252
30.311
52.207
54.395
1.00
10.17
DIC

ATOM
1959
CH2
TRP
252
29.239
51.486
54.945
1.00
9.82
DIC

ATOM
1960
C
TRP
252
27.415
56.249
50.046
1.00
23.17
DIC

ATOM
1961
O
TRP
252
27.069
55.808
48.948
1.00
24.13
DIC

ATOM
1962
N
HIS
253
26.620
56.990
50.809
1.00
24.69
DIC

ATOM
1963
CA
HIS
253
25.273
57.351
50.388
1.00
27.61
DIC

ATOM
1964
CB
HIS
253
24.364
57.523
51.605
1.00
26.78
DIC

ATOM
1965
CG
HIS
253
23.843
56.233
52.156
1.00
27.30
DIC

ATOM
1966
CD2
HIS
253
23.890
54.972
51.666
1.00
26.61
DIC

ATOM
1967
ND1
HIS
253
23.147
56.159
53.343
1.00
27.44
DIC

ATOM
1968
CE1
HIS
253
22.786
54.907
53.561
1.00
27.37
DIC

ATOM
1969
NE2
HIS
253
23.224
54.167
52.559
1.00
27.99
DIC

ATOM
1970
C
HIS
253
25.293
58.645
49.582
1.00
29.67
DIC

ATOM
1971
O
HIS
253
24.324
58.968
48.892
1.00
14.02
DIC

ATOM
1972
N
ALA
258
27.264
63.867
56.914
1.00
29.28
DIC

ATOM
1973
CA
ALA
258
27.941
63.637
58.185
1.00
27.86
DIC

ATOM
1974
CB
ALA
258
27.889
62.162
58.545
1.00
26.95
DIC

ATOM
1975
C
ALA
258
29.388
64.107
58.096
1.00
26.15
DIC

ATOM
1976
O
ALA
258
29.995
64.081
57.026
1.00
26.60
DIC

ATOM
1977
N
TRP
259
29.933
64.540
59.228
1.00
25.33
DIC

ATOM
1978
CA
TRP
259
31.305
65.026
59.282
1.00
24.17
DIC

ATOM
1979
CB
TRP
259
31.678
65.406
60.716
1.00
24.67
DIC

ATOM
1980
CG
TRP
259
33.088
65.907
60.841
1.00
24.17
DIC

ATOM
1981
CD2
TRP
259
34.222
65.166
61.307
1.00
23.57
DIC

ATOM
1982
CE2
TRP
259
35.347
66.012
61.199
1.00
24.08
DIC

ATOM
1983
CE3
TRP
259
34.398
63.867
61.803
1.00
23.76
DIC

ATOM
1984
CD1
TRP
259
33.556
67.137
60.482
1.00
24.26
DIC

ATOM
1985
NE1
TRP
259
34.913
67.209
60.693
1.00
24.21
DIC

ATOM
1986
CZ2
TRP
259
36.633
65.602
61.571
1.00
24.47
DIC

ATOM
1987
CZ3
TRP
259
35.678
63.459
62.172
1.00
21.73
DIC

ATOM
1988
CH2
TRP
259
36.776
64.324
62.054
1.00
23.77
DIC

ATOM
1989
C
TRP
259
32.319
64.006
58.770
1.00
24.50
DIC

ATOM
1990
O
TRP
259
32.183
62.804
59.006
1.00
24.08
DIC

ATOM
1991
N
GLY
260
33.333
64.503
58.065
1.00
22.84
DIC

ATOM
1992
CA
GLY
260
34.389
63.651
57.545
1.00
22.82
DIC

ATOM
1993
C
GLY
260
34.026
62.699
56.421
1.00
22.52
DIC

ATOM
1994
O
GLY
260
34.883
61.959
55.944
1.00
22.25
DIC

ATOM
1995
N
ALA
261
32.769
62.713
55.992
1.00
23.04
DIC

ATOM
1996
CA
ALA
261
32.324
61.830
54.923
1.00
22.66
DIC

ATOM
1997
CB
ALA
261
30.849
62.081
54.623
1.00
24.10
DIC

ATOM
1998
C
ALA
261
33.156
61.989
53.648
1.00
23.16
DIC

ATOM
1999
O
ALA
261
33.369
61.023
52.915
1.00
24.06
DIC

ATOM
2000
N
ALA
262
33.628
63.205
53.388
1.00
22.44
DIC

ATOM
2001
CA
ALA
262
34.423
63.489
52.194
1.00
21.08
DIC

ATOM
2002
CB
ALA
262
34.829
64.960
52.174
1.00
22.66
DIC

ATOM
2003
C
ALA
262
35.663
62.616
52.058
1.00
20.72
DIC

ATOM
2004
O
ALA
262
36.129
62.368
50.943
1.00
18.77
DIC

ATOM
2005
N
ARG
263
36.208
62.163
53.184
1.00
18.78
DIC

ATOM
2006
CA
ARG
263
37.397
61.318
53.153
1.00
18.76
DIC

ATOM
2007
CB
ARG
263
37.924
61.067
54.570
1.00
21.15
DIC

ATOM
2008
CG
ARG
263
39.094
60.079
54.635
1.00
25.36
DIC

ATOM
2009
CD
ARG
263
39.670
59.996
56.051
1.00
30.63
DIC

ATOM
2010
NE
ARG
263
40.709
58.973
56.199
1.00
32.82
DIC

ATOM
2011
CZ
ARG
263
41.814
58.901
55.460
1.00
34.60
DIC

ATOM
2012
NH1
ARG
263
42.696
57.933
55.681
1.00
34.80
DIC

ATOM
2013
NH2
ARG
263
42.037
59.785
54.495
1.00
34.28
DIC

ATOM
2014
C
ARG
263
37.089
59.991
52.478
1.00
17.13
DIC

ATOM
2015
O
ARG
263
37.963
59.384
51.862
1.00
16.27
DIC

ATOM
2016
N
PHE
264
35.844
59.540
52.599
1.00
15.52
DIC

ATOM
2017
CA
PHE
264
35.437
58.284
51.983
1.00
15.68
DIC

ATOM
2018
CB
PHE
264
33.970
57.978
52.293
1.00
15.52
DIC

ATOM
2019
CG
PHE
264
33.495
56.678
51.716
1.00
14.73
DIC

ATOM
2020
CD1
PHE
264
33.570
55.504
52.459
1.00
15.37
DIC

ATOM
2021
CD2
PHE
264
33.009
56.617
50.412
1.00
14.26
DIC

ATOM
2022
CE1
PHE
264
33.170
54.289
51.915
1.00
14.89
DIC

ATOM
2023
CE2
PHE
264
32.606
55.405
49.856
1.00
13.60
DIC

ATOM
2024
CZ
PHE
264
32.687
54.239
50.609
1.00
14.32
DIC

ATOM
2025
C
PHE
264
35.611
58.372
50.469
1.00
16.23
DIC

ATOM
2026
O
PHE
264
36.271
57.529
49.858
1.00
16.76
DIC

ATOM
2027
N
THR
265
35.014
59.398
49.870
1.00
17.19
DIC

ATOM
2028
CA
THR
265
35.092
59.587
48.426
1.00
19.52
DIC

ATOM
2029
CB
THR
265
34.227
60.789
47.970
1.00
21.53
DIC

ATOM
2030
OG1
THR
265
34.141
60.802
46.538
1.00
24.56
DIC

ATOM
2031
CG2
THR
265
34.832
62.095
48.437
1.00
22.63
DIC

ATOM
2032
C
THR
265
36.539
59.788
47.971
1.00
19.59
DIC

ATOM
2033
O
THR
265
36.938
59.308
46.910
1.00
18.82
DIC

ATOM
2034
N
GLU
266
37.331
60.485
48.780
1.00
18.91
DIC

ATOM
2035
CA
GLU
266
38.729
60.710
48.435
1.00
19.77
DIC

ATOM
2036
CB
GLU
266
39.394
61.635
49.450
1.00
22.93
DIC

ATOM
2037
CG
GLU
266
40.890
61.785
49.227
1.00
29.46
DIC

ATOM
2038
CD
GLU
266
41.516
62.808
50.146
1.00
32.08
DIC

ATOM
2039
OE1
GLU
266
41.433
62.632
51.380
1.00
34.07
DIC

ATOM
2040
OE2
GLU
266
42.091
63.790
49.631
1.00
35.23
DIC

ATOM
2041
C
GLU
266
39.488
59.386
48.384
1.00
18.19
DIC

ATOM
2042
O
GLU
266
40.345
59.185
47.525
1.00
16.67
DIC

ATOM
2043
N
LEU
267
39.177
58.488
49.315
1.00
16.93
DIC

ATOM
2044
CA
LEU
267
39.823
57.181
49.362
1.00
15.79
DIC

ATOM
2045
CB
LEU
267
39.571
56.509
50.715
1.00
17.37
DIC

ATOM
2046
CG
LEU
267
40.497
56.943
51.851
1.00
16.52
DIC

ATOM
2047
CD1
LEU
267
40.007
56.374
53.165
1.00
17.75
DIC

ATOM
2048
CD2
LEU
267
41.911
56.466
51.549
1.00
16.20
DIC

ATOM
2049
C
LEU
267
39.320
56.279
48.243
1.00
15.71
DIC

ATOM
2050
O
LEU
267
40.096
55.550
47.623
1.00
14.15
DIC

ATOM
2051
N
ALA
268
38.018
56.330
47.984
1.00
16.10
DIC

ATOM
2052
CA
ALA
268
37.430
55.511
46.932
1.00
18.09
DIC

ATOM
2053
CB
ALA
268
35.919
55.683
46.915
1.00
18.61
DIC

ATOM
2054
C
ALA
268
38.019
55.901
45.581
1.00
19.91
DIC

ATOM
2055
O
ALA
268
38.128
55.072
44.680
1.00
20.47
DIC

ATOM
2056
N
GLY
269
38.404
57.165
45.447
1.00
20.77
DIC

ATOM
2057
CA
GLY
269
38.974
57.627
44.196
1.00
22.67
DIC

ATOM
2058
C
GLY
269
40.431
57.241
44.014
1.00
23.70
DIC

ATOM
2059
O
GLY
269
40.946
57.266
42.898
1.00
24.52
DIC

ATOM
2060
N
SER
270
41.096
56.879
45.107
1.00
24.12
DIC

ATOM
2061
CA
SER
270
42.505
56.498
45.054
1.00
24.97
DIC

ATOM
2062
CB
SER
270
43.210
56.903
46.350
1.00
25.49
DIC

ATOM
2063
OG
SER
270
42.733
56.143
47.448
1.00
27.01
DIC

ATOM
2064
C
SER
270
42.687
55.001
44.842
1.00
25.34
DIC

ATOM
2065
O
SER
270
43.813
54.511
44.769
1.00
25.69
DIC

ATOM
2066
N
LEU
271
41.578
54.276
44.742
1.00
25.34
DIC

ATOM
2067
CA
LEU
271
41.633
52.834
44.558
1.00
25.82
DIC

ATOM
2068
CB
LEU
271
40.218
52.247
44.564
1.00
24.31
DIC

ATOM
2069
CG
LEU
271
39.497
52.396
45.907
1.00
23.12
DIC

ATOM
2070
CD1
LEU
271
38.112
51.772
45.833
1.00
23.63
DIC

ATOM
2071
CD2
LEU
271
40.328
51.732
46.999
1.00
21.99
DIC

ATOM
2072
C
LEU
271
42.370
52.410
43.295
1.00
26.79
DIC

ATOM
2073
O
LEU
271
42.110
52.916
42.205
1.00
26.57
DIC

ATOM
2074
N
THR
272
43.297
51.474
43.469
1.00
27.68
DIC

ATOM
2075
CA
THR
272
44.099
50.940
42.378
1.00
28.62
DIC

ATOM
2076
CB
THR
272
45.090
49.884
42.902
1.00
28.86
DIC

ATOM
2077
OG1
THR
272
45.988
50.496
43.835
1.00
31.54
DIC

ATOM
2078
CG2
THR
272
45.882
49.278
41.757
1.00
29.83
DIC

ATOM
2079
C
THR
272
43.219
50.290
41.320
1.00
28.48
DIC

ATOM
2080
O
THR
272
43.315
50.615
40.136
1.00
27.52
DIC

ATOM
2081
N
THR
273
42.368
49.366
41.759
1.00
28.31
DIC

ATOM
2082
CA
THR
273
41.463
48.649
40.867
1.00
27.75
DIC

ATOM
2083
CB
THR
273
41.776
47.136
40.851
1.00
29.35
DIC

ATOM
2084
OG1
THR
273
43.155
46.931
40.515
1.00
31.31
DIC

ATOM
2085
CG2
THR
273
40.900
46.426
39.828
1.00
31.25
DIC

ATOM
2086
C
THR
273
40.018
48.824
41.324
1.00
25.84
DIC

ATOM
2087
O
THR
273
39.695
48.590
42.489
1.00
24.34
DIC

ATOM
2088
N
VAL
274
39.151
49.230
40.402
1.00
22.69
DIC

ATOM
2089
CA
VAL
274
37.745
49.425
40.725
1.00
20.88
DIC

ATOM
2090
CB
VAL
274
37.378
50.932
40.744
1.00
19.63
DIC

ATOM
2091
CG1
VAL
274
37.700
51.569
39.405
1.00
21.82
DIC

ATOM
2092
CG2
VAL
274
35.906
51.106
41.077
1.00
20.86
DIC

ATOM
2093
C
VAL
274
36.851
48.684
39.735
1.00
19.45
DIC

ATOM
2094
O
VAL
274
36.644
49.129
38.604
1.00
19.49
DIC

ATOM
2095
N
PRO
275
36.317
47.524
40.151
1.00
18.18
DIC

ATOM
2096
CD
PRO
275
36.580
46.851
41.433
1.00
16.49
DIC

ATOM
2097
CA
PRO
275
35.441
46.705
39.311
1.00
17.39
DIC

ATOM
2098
CB
PRO
275
35.079
45.540
40.230
1.00
17.76
DIC

ATOM
2099
CG
PRO
275
36.283
45.416
41.097
1.00
17.23
DIC

ATOM
2100
C
PRO
275
34.208
47.476
38.858
1.00
16.95
DIC

ATOM
2101
O
PRO
275
33.642
48.257
39.619
1.00
14.46
DIC

ATOM
2102
N
GLU
276
33.799
47.257
37.613
1.00
18.62
DIC

ATOM
2103
CA
GLU
276
32.620
47.924
37.070
1.00
19.68
DIC

ATOM
2104
CB
GLU
276
32.250
47.292
35.720
1.00
20.05
DIC

ATOM
2105
CG
GLU
276
30.884
47.680
35.146
1.00
23.31
DIC

ATOM
2106
CD
GLU
276
30.747
49.162
34.846
1.00
24.44
DIC

ATOM
2107
OE1
GLU
276
31.776
49.825
34.606
1.00
25.94
DIC

ATOM
2108
OE2
GLU
276
29.601
49.662
34.834
1.00
26.03
DIC

ATOM
2109
C
GLU
276
31.453
47.812
38.056
1.00
19.58
DIC

ATOM
2110
O
GLU
276
30.705
48.765
38.255
1.00
19.51
DIC

ATOM
2111
N
GLU
277
31.325
46.651
38.693
1.00
19.98
DIC

ATOM
2112
CA
GLU
277
30.246
46.413
39.647
1.00
21.58
DIC

ATOM
2113
CB
GLU
277
30.155
44.916
39.962
1.00
25.97
DIC

ATOM
2114
CG
GLU
277
28.727
44.372
40.027
1.00
31.33
DIC

ATOM
2115
CD
GLU
277
28.073
44.244
38.653
1.00
33.58
DIC

ATOM
2116
OE1
GLU
277
27.923
45.267
37.948
1.00
34.50
DIC

ATOM
2117
OE2
GLU
277
27.706
43.111
38.279
1.00
36.07
DIC

ATOM
2118
C
GLU
277
30.383
47.210
40.953
1.00
21.12
DIC

ATOM
2119
O
GLU
277
29.507
47.148
41.816
1.00
21.31
DIC

ATOM
2120
N
TRP
278
31.481
47.949
41.097
1.00
19.40
DIC

ATOM
2121
CA
TRP
278
31.719
48.772
42.286
1.00
18.57
DIC

ATOM
2122
CB
TRP
279
33.174
48.652
42.744
1.00
16.02
DIC

ATOM
2123
CG
TRP
278
33.510
47.418
43.518
1.00
13.84
DIC

ATOM
2124
CD2
TRP
278
34.666
47.224
44.339
1.00
13.65
DIC

ATOM
2125
CE2
TRP
278
34.617
45.899
44.823
1.00
12.87
DIC

ATOM
2126
CE3
TRP
278
35.742
48.042
44.711
1.00
11.77
DIC

ATOM
2127
CD1
TRP
278
32.822
46.240
43.539
1.00
13.38
DIC

ATOM
2128
NE1
TRP
278
33.481
45.321
44.321
1.00
14.26
DIC

ATOM
2129
CZ2
TRP
278
35.604
45.371
45.661
1.00
11.66
DIC

ATOM
2130
CZ3
TRP
278
36.724
47.516
45.546
1.00
12.57
DIC

ATOM
2131
CH2
TRP
278
36.646
46.192
46.010
1.00
11.95
DIC

ATOM
2132
C
TRP
278
31.443
50.240
41.977
1.00
19.09
DIC

ATOM
2133
O
TRP
278
31.266
51.051
42.885
1.00
17.92
DIC

ATOM
2134
N
ALA
279
31.422
50.572
40.690
1.00
21.02
DIC.

ATOM
2135
CA
ALA
279
31.200
51.943
40.235
1.00
23.01
DIC

ATOM
2136
CB
ALA
279
31.061
51.969
38.717
1.00
24.70
DIC

ATOM
2137
C
ALA
279
29.997
52.619
40.875
1.00
23.44
DIC

ATOM
2138
O
ALA
279
30.088
53.764
41.317
1.00
25.20
DIC

ATOM
2139
N
ALA
280
28.871
51.917
40.918
1.00
24.09
DIC

ATOM
2140
CA
ALA
280
27.656
52.470
41.504
1.00
24.89
DIC

ATOM
2141
CB
ALA
280
26.460
51.598
41.140
1.00
25.25
DIC

ATOM
2142
C
ALA
280
27.765
52.604
43.024
1.00
25.44
DIC

ATOM
2143
O
ALA
280
27.449
53.655
43.586
1.00
26.12
DIC

ATOM
2144
N
ALA
281
28.214
51.538
43.680
1.00
24.53
DIC

ATOM
2145
CA
ALA
281
28.363
51.529
45.132
1.00
24.14
DIC

ATOM
2146
CB
ALA
281
28.895
50.176
45.592
1.00
22.30
DIC

ATOM
2147
C
ALA
281
29.301
52.637
45.590
1.00
24.69
DIC

ATOM
2148
O
ALA
281
29.097
53.231
46.649
1.00
24.21
DIC

ATOM
2149
N
ALA
282
30.326
52.890
44.775
1.00
25.23
DIC

ATOM
2150
CA
ALA
282
31.354
53.907
45.008
1.00
28.24
DIC

ATOM
2151
CB
ALA
282
30.889
54.936
46.040
1.00
29.57
DIC

ATOM
2152
C
ALA
282
32.672
53.285
45.456
1.00
29.28
DIC

ATOM
2153
OT1
ALA
282
32.749
52.040
45.554
1.00
30.11
DIC

ATOM
2154
OT2
ALA
282
33.619
54.061
45.703
1.00
31.66
DIC

ATOM
2155
N1
UPG
341
27.143
44.459
57.507
1.00
10.01

ATOM
2156
C2
UPG
341
27.525
43.800
56.322
1.00
9.52

ATOM
2157
N3
UPG
341
26.652
44.070
55.245
1.00
8.67

ATOM
2158
C4
UPG
341
25.480
44.911
55.273
1.00
8.79

ATOM
2159
C5
UPG
341
25.173
45.541
56.522
1.00
8.07

ATOM
2160
C6
UPG
341
25.965
45.316
57.564
1.00
8.80

ATOM
2161
O2
UPG
341
28.508
43.077
56.249
1.00
9.10

ATOM
2162
O4
UPG
341
24.821
45.047
54.262
1.00
10.92

ATOM
2163
C4*
UPG
341
28.064
45.814
60.802
1.00
9.49

ATOM
2164
O4*
UPG
341
27.241
44.769
60.117
1.00
9.77

ATOM
2165
C3*
UPG
341
28.852
46.439
59.647
1.00
8.11

ATOM
2166
O3*
UPG
341
29.963
47.181
60.117
1.00
10.37

ATOM
2167
C2*
UPG
341
29.109
45.217
58.781
1.00
9.07

ATOM
2168
O2*
UPG
341
30.227
44.448
59.212
1.00
9.05

ATOM
2169
C1*
UPG
341
27.829
44.408
58.886
1.00
10.20

ATOM
2170
C5*
UPG
341
26.745
46.233
61.382
1.00
8.16

ATOM
2171
O5*
UPG
341
26.201
47.589
61.086
1.00
14.00

ATOM
2172
PA
UPG
341
26.684
49.097
60.762
1.00
11.18

ATOM
2173
O1A
UPG
341
28.145
49.287
60.708
1.00
12.79

ATOM
2174
O2A
UPG
341
25.988
49.605
59.534
1.00
13.97

ATOM
2175
O3A
UPG
341
25.956
49.273
62.186
1.00
12.14

ATOM
2176
PB
UPG
341
25.671
50.458
63.209
1.00
14.34

ATOM
2177
O1B
UPG
341
26.996
51.096
63.328
1.00
11.37

ATOM
2178
O2B
UPG
341
24.689
51.364
62.606
1.00
15.46

ATOM
2179
O3B
UPG
341
25.195
49.937
64.603
1.00
15.30

ATOM
2180
C1′
UPG
341
25.560
49.791
66.150
1.00
20.50

ATOM
2181
C2′
UPG
341
27.035
49.261
66.121
1.00
19.24

ATOM
2182
C3′
UPG
341
27.359
48.017
65.147
1.00
20.09

ATOM
2183
C4′
UPG
341
26.330
46.877
65.447
1.00
19.60

ATOM
2184
C5′
UPG
341
24.895
47.560
65.400
1.00
19.91

ATOM
2185
C6′
UPG
341
23.873
46.533
65.880
1.00
21.17

ATOM
2186
F2′
UPG
341
27.959
50.293
65.853
1.00
22.12

ATOM
2187
O3′
UPG
341
28.644
47.531
65.431
1.00
18.85

ATOM
2188
O4′
UPG
341
26.604
46.316
66.765
1.00
17.85

ATOM
2189
O5′
UPG
341
24.675
48.684
66.396
1.00
19.90

ATOM
2190
O6′
UPG
341
23.634
45.281
65.305
1.00
20.17

ATOM
2191
MN
MN
400
28.972
50.701
62.315
1.00
5.95
MN

ATOM
2192
O
HOH
500
33.706
51.230
70.721
1.00
5.79

ATOM
2193
O
HOH
501
34.343
56.571
75.304
1.00
6.75

ATOM
2194
O
HOH
502
17.802
43.967
68.994
1.00
10.59

ATOM
2195
O
HOH
503
30.228
40.611
62.764
1.00
5.01

ATOM
2196
O
HOH
504
39.307
27.582
66.202
1.00
10.52

ATOM
2197
O
HOH
505
28.063
58.310
70.871
1.00
11.73

ATOM
2198
O
HOH
506
28.710
46.590
79.022
1.00
6.65

ATOM
2199
O
HOH
507
52.557
49.070
68.969
1.00
12.93

ATOM
2200
O
HOH
508
45.198
58.379
72.300
1.00
14.17

ATOM
2201
O
HOH
509
34.051
65.873
73.044
1.00
11.35

ATOM
2202
O
HOH
510
41.782
55.536
74.876
1.00
9.63

ATOM
2203
O
HOH
511
34.074
33.978
70.193
1.00
11.60

ATOM
2204
O
HOH
512
26.575
37.907
50.900
1.00
12.73

ATOM
2205
O
HOH
513
20.508
53.715
78.759
1.00
13.23

ATOM
2206
O
HOH
514
51.349
46.691
65.666
1.00
17.16

ATOM
2207
O
HOH
515
46.546
58.564
67.349
1.00
8.65

ATOM
2208
O
HOH
516
52.691
53.505
61.177
1.00
12.18

ATOM
2209
O
HOH
517
32.821
62.545
72.466
1.00
11.60

ATOM
2210
O
HOH
518
25.540
58.412
67.321
1.00
14.19

ATOM
2211
O
HOH
519
43.067
31.129
75.720
1.00
15.28

ATOM
2212
O
HOH
520
42.729
59.876
74.613
1.00
15.64

ATOM
2213
O
HOH
521
22.179
51.497
64.101
1.00
18.51

ATOM
2214
O
HOH
522
34.014
47.551
83.195
1.00
9.04

ATOM
2215
O
HOH
523
31.143
47.689
82.928
1.00
12.50

ATOM
2216
O
HOH
524
32.337
57.530
71.624
1.00
8.71

ATOM
2217
O
HOH
525
32.452
44.011
37.817
1.00
14.80

ATOM
2218
O
HOH
526
24.863
45.001
86.150
1.00
15.13

ATOM
2219
O
HOH
527
30.407
45.125
46.996
1.00
21.84

ATOM
2220
O
HOH
528
20.754
39.640
56.706
1.00
9.45

ATOM
2221
O
HOH
529
38.854
52.122
81.581
1.00
10.97

ATOM
2222
O
HOH
530
40.378
59.034
77.824
1.00
17.34

ATOM
2223
O
HOH
531
45.109
40.792
78.558
1.00
18.88

ATOM
2224
O
HOH
532
48.994
58.795
68.032
1.00
18.00

ATOM
2225
O
HOH
533
40.483
67.706
72.634
1.00
23.92

ATOM
2226
O
HOH
534
41.280
60.433
45.444
1.00
22.17

ATOM
2227
O
HOH
535
26.497
64.111
54.278
1.00
24.53

ATOM
2228
O
HOH
536
45.960
43.860
76.459
1.00
17.37

ATOM
2229
O
HOH
537
14.734
48.868
65.365
1.00
18.59

ATOM
2230
O
HOH
538
46.131
38.545
57.874
1.00
24.34

ATOM
2231
O
HOH
539
28.264
60.048
87.951
1.00
24.52

ATOM
2232
O
HOH
540
46.748
45.401
73.816
1.00
16.95

ATOM
2233
O
HOH
541
37.416
49.298
83.116
1.00
21.65

ATOM
2234
O
HOH
542
27.237
60.848
55.024
1.00
18.79

ATOM
2235
O
HOH
543
19.040
32.149
71.513
1.00
19.39

ATOM
2236
O
HOH
544
24.859
59.199
87.172
1.00
21.96

ATOM
2237
O
HOH
545
31.727
30.205
70.890
1.00
15.96

ATOM
2238
O
HOH
546
50.448
55.331
62.596
1.00
19.00

ATOM
2239
O
HOH
547
44.684
61.061
73.050
1.00
18.55

ATOM
2240
O
HOH
548
23.917
28.286
65.355
1.00
22.75

ATOM
2241
O
HOH
549
48.030
45.080
55.012
1.00
18.04

ATOM
2242
O
HOH
550
31.863
50.861
84.807
1.00
12.35

ATOM
2243
O
HOH
551
47.230
50.648
79.238
1.00
20.70

ATOM
2244
O
HOH
552
45.574
59.143
57.227
1.00
26.33

ATOM
2245
O
HOH
553
30.141
30.242
60.911
1.00
18.49

ATOM
2246
O
HOH
554
39.361
63.494
77.807
1.00
19.60

ATOM
2247
O
HOH
555
47.878
40.139
68.058
1.00
19.90

ATOM
2248
O
HOH
556
33.763
51.759
54.205
1.00
21.40

ATOM
2249
O
HOH
557
26.346
51.553
89.495
1.00
25.04

ATOM
2250
O
HOH
558
43.622
40.021
44.147
1.00
18.14

ATOM
2251
O
HOH
559
22.590
60.674
51.245
1.00
20.28

ATOM
2252
O
HOH
560
46.899
45.705
42.406
1.00
23.24

ATOM
2253
O
HOH
561
22.785
41.493
81.141
1.00
16.19

ATOM
2254
O
HOH
562
24.738
38.970
55.796
1.00
22.33

ATOM
2255
O
HOH
563
44.428
51.002
46.157
1.00
14.80

ATOM
2256
O
HOH
564
24.412
40.573
48.290
1.00
23.85

ATOM
2257
O
HOH
565
28.192
56.913
87.234
1.00
17.82

ATOM
2258
O
HOH
566
49.326
45.339
71.775
1.00
22.08

ATOM
2259
O
HOH
567
13.438
46.500
69.972
1.00
21.87

ATOM
2260
O
HOH
568
36.472
30.850
71.825
1.00
24.81

ATOM
2261
O
HOH
569
48.009
36.876
62.329
1.00
23.86

ATOM
2262
O
HOH
570
24.860
62.779
55.872
1.00
26.97

ATOM
2263
O
HOH
571
33.245
67.145
56.945
1.00
20.42

ATOM
2264
O
HOH
572
42.157
34.486
52.245
1.00
16.87

ATOM
2265
O
HOH
573
50.717
47.209
75.899
1.00
22.49

ATOM
2266
O
HOH
574
29.865
33.602
47.244
1.00
32.56

ATOM
2267
O
HOH
575
22.722
37.430
81.986
1.00
23.93

ATOM
2268
O
HOH
576
50.100
42.319
65.178
1.00
22.32

ATOM
2269
O
HOH
577
57.571
51.761
56.046
1.00
21.27

ATOM
2270
O
HOH
578
47.296
51.529
51.324
1.00
20.20

ATOM
2271
O
HOH
579
29.733
32.008
53.762
1.00
26.39

ATOM
2272
O
HOH
580
26.968
35.843
81.316
1.00
22.87

ATOM
2273
O
HOH
581
14.080
40.066
63.324
1.00
21.92

ATOM
2274
O
HOH
582
28.224
49.947
38.771
1.00
25.67

ATOM
2275
O
HOH
583
31.203
53.364
87.667
1.00
15.87

ATOM
2276
O
HOH
584
42.912
37.536
80.236
1.00
23.43

ATOM
2277
O
HOH
585
22.186
39.308
53.880
1.00
20.38

ATOM
2278
O
HOH
586
48.511
56.150
75.023
1.00
32.95

ATOM
2279
O
HOH
587
24.730
34.535
78.912
1.00
18.02

ATOM
2280
O
HOH
588
32.604
39.346
83.395
1.00
22.21

ATOM
2281
O
HOH
589
41.240
63.564
62.618
1.00
10.36

ATOM
2282
O
HOH
590
26.537
56.699
69.106
1.00
8.22

ATOM
2283
O
HOH
591
52.797
47.471
74.334
1.00
9.21

ATOM
2284
O
HOH
592
41.777
32.558
61.182
1.00
10.73

ATOM
2285
O
HOH
593
33.437
44.877
60.209
1.00
7.34

ATOM
2286
O
HOH
594
33.888
31.650
71.550
1.00
14.92

ATOM
2287
O
HOH
595
25.462
40.367
50.723
1.00
11.84

ATOM
2288
O
HOH
596
43.591
57.443
74.474
1.00
17.30

ATOM
2289
O
HOH
597
33.115
35.658
41.851
1.00
14.12

ATOM
2290
O
HOH
598
44.433
41.685
76.122
1.00
16.31

ATOM
2291
O
HOH
599
29.834
27.545
68.444
1.00
22.39

ATOM
2292
O
HOH
600
37.953
40.975
40.829
1.00
14.27

ATOM
2293
O
HOH
601
12.155
45.294
67.909
1.00
17.65

ATOM
2294
O
HOH
602
22.482
36.971
50.284
1.00
24.49

ATOM
2295
O
HOH
603
23.544
68.425
75.283
1.00
28.58

ATOM
2296
O
HOH
604
45.872
62.745
70.934
1.00
20.85

ATOM
2297
O
HOH
605
27.938
49.214
42.120
1.00
30.40

ATOM
2298
O
HOH
606
27.096
61.728
78.244
1.00
24.23

ATOM
2299
O
HOH
607
31.086
37.382
40.546
1.00
19.00

ATOM
2300
O
HOH
608
41.624
62.545
78.909
1.00
18.97

ATOM
2301
O
HOH
609
41.687
56.553
77.779
1.00
20.00

ATOM
2302
O
HOH
610
24.401
57.605
65.060
1.00
18.11

ATOM
2303
O
HOH
611
22.321
34.679
80.031
1.00
20.17

ATOM
2304
O
HOH
612
50.721
43.533
70.330
1.00
19.94

ATOM
2305
O
HOH
613
13.420
52.527
51.343
1.00
25.95

ATOM
2306
O
HOH
614
24.279
27.169
60.916
1.00
21.76

ATOM
2307
O
HOH
615
34.037
52.439
85.454
1.00
17.26

ATOM
2308
O
HOH
616
39.054
65.244
80.148
1.00
24.89

ATOM
2309
O
HOH
617
39.054
64.302
51.723
1.00
29.39

ATOM
2310
O
HOH
618
43.601
62.259
58.842
1.00
27.04

ATOM
2311
O
HOH
619
22.409
56.766
90.280
1.00
33.32

ATOM
2312
O
HOH
620
20.846
28.993
74.299
1.00
20.46

ATOM
2313
O
HOH
621
17.253
46.648
86.012
1.00
32.49

ATOM
2314
O
HOH
622
21.298
51.633
88.129
1.00
31.62

ATOM
2315
O
HOH
623
28.632
26.574
61.870
1.00
27.33

ATOM
2316
O
HOH
624
48.345
58.417
61.097
1.00
25.77

ATOM
2317
O
HOH
625
36.305
67.237
72.635
1.00
20.04

ATOM
2318
O
HOH
626
42.598
53.012
75.632
1.00
19.40

ATOM
2319
O
HOH
627
20.218
47.782
86.726
1.00
22.94

ATOM
2320
O
HOH
628
32.159
63.722
48.806
1.00
23.31

ATOM
2321
O
HOH
629
23.413
63.225
51.020
1.00
26.53

ATOM
2322
O
HOH
630
29.942
43.073
43.112
1.00
28.69

ATOM
2323
O
HOH
631
26.522
26.069
67.811
1.00
29.08

ATOM
2324
O
HOH
632
22.688
56.444
82.013
1.00
24.60

ATOM
2325
O
HOH
633
52.189
43.104
63.856
1.00
22.68

ATOM
2326
O
HOH
634
25.706
64.912
64.257
1.00
22.84

ATOM
2327
O
HOH
635
36.511
40.834
83.556
1.00
23.63

ATOM
2328
O
HOH
636
31.226
27.212
64.879
1.00
21.79

ATOM
2329
O
HOH
637
40.945
34.644
81.702
1.00
23.90

ATOM
2330
O
HOH
638
21.448
59.284
81.673
1.00
34.56

ATOM
2331
O
HOH
639
49.130
60.035
70.370
1.00
30.49

ATOM
2332
O
HOH
640
45.879
54.032
77.176
1.00
28.11

ATOM
2333
O
HOH
641
41.217
55.181
84.434
1.00
27.45

ATOM
2334
O
HOH
642
15.917
59.351
77.084
1.00
22.78

ATOM
2335
O
HOH
643
26.422
58.999
59.868
1.00
26.25

ATOM
2336
O
HOH
644
23.973
36.865
54.522
1.00
23.25

ATOM
2337
O
HOH
645
23.524
48.998
51.566
1.00
30.36

ATOM
2338
O
HOH
646
46.194
61.930
74.996
1.00
35.99

ATOM
2339
O
HOH
647
9.547
44.920
75.322
1.00
30.40

ATOM
2340
O
HOH
648
40.501
29.426
67.866
1.00
27.54

ATOM
2341
O
HOH
649
42.953
47.204
81.751
1.00
28.53

ATOM
2342
O
HOH
650
26.628
46.271
47.232
1.00
28.74

ATOM
2343
O
HOH
651
41.609
36.542
46.766
1.00
26.30

ATOM
2344
O
HOH
652
47.789
62.434
66.963
1.00
22.24

ATOM
2345
O
HOH
653
49.409
58.883
57.890
1.00
32.71

ATOM
2346
O
HOH
654
17.321
49.855
67.521
1.00
17.23

ATOM
2347
O
HOH
655
51.495
46.932
72.085
1.00
20.28

ATOM
2348
O
HOH
656
34.466
27.259
73.207
1.00
21.37

ATOM
2349
O
HOH
657
38.002
69.000
71.442
1.00
14.96

ATOM
2350
O
HOH
658
20.746
31.132
65.541
1.00
23.69

ATOM
2351
O
HOH
659
58.157
43.951
58.062
1.00
20.32

ATOM
2352
O
HOH
660
38.437
33.849
81.870
1.00
20.83

ATOM
2353
O
HOH
661
43.258
34.683
60.615
1.00
17.70

ATOM
2354
O
HOH
662
36.377
51.103
84.600
1.00
27.30

ATOM
2355
O
HOH
663
25.933
38.583
81.765
1.00
24.70

ATOM
2356
O
HOH
664
29.974
47.696
49.284
1.00
24.16

ATOM
2357
O
HOH
665
49.678
57.581
72.793
1.00
26.38

ATOM
2358
O
HOH
666
50.099
56.413
54.533
1.00
21.01

ATOM
2359
O
HOH
667
52.662
42.022
61.588
1.00
28.15

ATOM
2360
O
HOH
668
20.130
54.995
81.261
1.00
24.64

ATOM
2361
O
HOH
669
46.100
40.982
44.473
1.00
25.43

ATOM
2362
O
HOH
670
47.498
47.532
45.696
1.00
27.31

ATOM
2363
O
HOH
671
32.535
33.305
43.257
1.00
27.22

ATOM
2364
O
HOH
672
43.715
31.852
63.188
1.00
19.52

ATOM
2365
O
HOH
673
24.492
65.745
55.161
1.00
28.73

ATOM
2366
O
HOH
674
27.731
64.219
61.902
1.00
29.97

ATOM
2367
O
HOH
675
44.865
49.755
80.491
1.00
26.39

ATOM
2368
O
HOH
676
37.157
68.382
83.515
1.00
28.68

ATOM
2369
O
HOH
677
30.154
55.040
89.681
1.00
29.35

ATOM
2370
O
HOH
678
30.684
39.377
42.310
1.00
17.22

ATOM
2371
O
HOH
679
18.954
28.710
77.300
1.00
34.29

ATOM
2372
O
HOH
680
36.128
60.169
43.709
1.00
32.96

ATOM
2373
O
HOH
681
41.469
52.484
78.099
1.00
23.04

ATOM
2374
O
HOH
682
26.597
36.390
48.638
1.00
26.34

ATOM
2375
O
HOH
683
50.624
46.042
56.343
1.00
27.15

ATOM
2376
O
HOH
684
32.352
60.908
62.085
1.00
29.37

ATOM
2377
O
HOH
685
36.543
42.286
39.079
1.00
36.28

ATOM
2378
O
HOH
686
13.775
50.845
82.171
1.00
28.05

ATOM
2379
O
HOH
687
47.886
43.395
52.513
1.00
28.22

ATOM
2380
O
HOH
688
50.808
53.317
53.903
1.00
33.82

ATOM
2381
O
HOH
689
33.470
54.665
86.847
1.00
17.58

ATOM
2382
O
HOH
690
19.330
58.463
73.532
1.00
17.09

ATOM
2383
O
HOH
691
51.990
49.111
66.439
1.00
25.06

ATOM
2384
O
HOH
692
55.576
56.592
60.334
1.00
24.70

ATOM
2385
O
HOH
693
50.867
41.843
47.444
1.00
32.36

ATOM
2386
O
HOH
694
28.359
36.216
43.792
1.00
27.71

ATOM
2387
O
HOH
695
30.229
40.375
82.671
1.00
15.17

ATOM
2388
O
HOH
696
34.080
42.336
41.876
1.00
15.17

ATOM
2389
C
ACY
244
23.704
53.254
68.309
1.00
20.17

ATOM
2390
O
ACY
244
24.283
54.249
68.921
1.00
20.17

ATOM
2391
OXT
ACY
244
23.988
52.013
68.413
1.00
20.17

ATOM
2392
CH3
ACY
244
22.577
53.681
67.378
1.00
20.17

[0495]

7

TABLE 5

REMARK coordinates from minimization refinement

REMARK refinement resolution: 20.0-2.0 A

REMARK starting r = .2565 free_r = .2833

REMARK final r = .2545 free_r = .2823

REMARK rmsd bonds = .006693 rmsd angles = 1.31286

REMARK wa = 1.49748

REMARK target = mlf cycles = 1 steps = 25

REMARK sg = P2 (1) 2 (1) 2 (1) a = 39.975 b = 76.158 c = 87.228

alpha = 90 beta = 90 gamma = 90

REMARK parameter file 1: CNS_TOPPAR: protein_rep.param

REMARK parameter file 2: ../upg.par

REMARK parameter file 3: CNS_TOPPAR: ion.param

REMARK parameter file 4: CNS_TOPPAR: water_rep.param

REMARK parameter file 5: ../lat.par

REMARK molecular structure file: generate3.mtf

REMARK input coordinates: generate3.pdb

REMARK reflection file = ../../deoxyse.cv

REMARK ncs = none

REMARK B-correction resolution: 6.0-2.0

REMARK initial B-factor correction applied to fobs:

REMARK B11 = 1.331 B22 = 2.292 B33 = −3.623

REMARK B12 = .000 B13 = .000 B23 = .000

REMARK B-factor correction applied to coordinate array B: −.107

REMARK bulk solvent: density level = .364834 e/A{circumflex over ( )}3, B-factor = 28.3776 A{circumflex over ( )}2

REMARK reflections with |Fobs|/sigma_F < 0.0 rejected

REMARK reflections with |Fobs| > 10000 * rms (Fobs) rejected

REMARK theoretical total number of refl. in resol. range:
18599 (>100.0%)

REMARK number of unobserved reflections (no entry or |F| = 0):
374 (>2.0%)

REMARK number of reflections rejected:
0 (.0%)

REMARK total number of reflections used:
18225 (>98.0%)

REMARK number of reflections in working set:
17339 (93.2%)

REMARK number of reflections in test set:
886 (>4.8%)

CRYST1 39.975 76.158 87.228 90.00 90.00 90.00 P 21 21 21

REMARK FILENAME = “minimize3.pdb”

REMARK DATE: 7-Jun-00 00:41:57 created by user: karina

REMARK VERSION: 1.0

ATOM
1
CB
MSE
1
48.137
46.257
65.175
1.00
15.20
DIC

ATOM
2
CG
MSE
1
47.648
47.190
64.082
1.00
16.41
DIC

ATOM
3
SE
MSE
1
46.777
48.813
64.794
1.00
17.84
DIC

ATOM
4
CE
MSE
1
48.349
49.605
65.593
1.00
17.32
DIC

ATOM
5
C
MSE
1
47.761
44.130
63.891
1.00
12.29
DIC

ATOM
6
O
MSE
1
47.811
44.149
62.665
1.00
12.03
DIC

ATOM
7
N
MSE
1
50.002
45.161
63.937
1.00
12.69
DIC

ATOM
8
CA
MSE
1
48.762
44.924
64.719
1.00
12.79
DIC

ATOM
9
N
ASP
2
46.865
43.424
64.570
1.00
11.18
DIC

ATOM
10
CA
ASP
2
45.852
42.621
63.902
1.00
11.07
DIC

ATOM
11
CB
ASP
2
45.779
41.223
64.516
1.00
11.12
DIC

ATOM
12
CG
ASP
2
47.054
40.435
64.305
1.00
12.17
DIC

ATOM
13
OD1
ASP
2
47.948
40.480
65.180
1.00
11.27
DIC

ATOM
14
OD2
ASP
2
47.164
39.783
63.247
1.00
12.68
DIC

ATOM
15
C
ASP
2
44.494
43.289
63.985
1.00
10.71
DIC

ATOM
16
O
ASP
2
43.971
43.534
65.072
1.00
10.39
DIC

ATOM
17
N
ILE
3
43.946
43.590
62.813
1.00
9.90
DIC

ATOM
18
CA
ILE
3
42.650
44.245
62.675
1.00
9.22
DIC

ATOM
19
CB
ILE
3
42.716
45.381
61.627
1.00
9.23
DIC

ATOM
20
CG2
ILE
3
41.353
46.043
61.480
1.00
6.69
DIC

ATOM
21
CG1
ILE
3
43.799
46.392
62.019
1.00
8.74
DIC

ATOM
22
CD
ILE
3
43.544
47.108
63.340
1.00
10.46
DIC

ATOM
23
C
ILE
3
41.649
43.216
62.186
1.00
9.22
DIC

ATOM
24
O
ILE
3
41.974
42.392
61.330
1.00
8.87
DIC

ATOM
25
N
VAL
4
40.443
43.262
62.738
1.00
9.68
DIC

ATOM
26
CA
VAL
4
39.383
42.346
62.343
1.00
9.18
DIC

ATOM
27
CB
VAL
4
38.861
41.512
63.519
1.00
9.44
DIC

ATOM
28
CG1
VAL
4
37.758
40.566
63.024
1.00
9.88
DIC

ATOM
29
CG2
VAL
4
39.994
40.741
64.157
1.00
9.29
DIC

ATOM
30
C
VAL
4
38.198
43.127
61.807
1.00
9.80
DIC

ATOM
31
O
VAL
4
37.805
44.137
62.381
1.00
8.97
DIC

ATOM
32
N
PHE
5
37.653
42.651
60.693
1.00
9.50
DIC

ATOM
33
CA
PHE
5
36.477
43.241
60.060
1.00
9.57
DIC

ATOM
34
CB
PHE
5
36.823
43.854
58.694
1.00
9.78
DIC

ATOM
35
CG
PHE
5
37.479
45.205
58.763
1.00
8.54
DIC

ATOM
36
CD1
PHE
5
36.784
46.308
59.248
1.00
7.97
DIC

ATOM
37
CD2
PHE
5
38.772
45.385
58.283
1.00
9.19
DIC

ATOM
38
CE1
PHE
5
37.368
47.577
59.246
1.00
8.53
DIC

ATOM
39
CE2
PHE
5
39.366
46.645
58.275
1.00
9.07
DIC

ATOM
40
CZ
PHE
5
38.661
47.744
58.757
1.00
9.04
DIC

ATOM
41
C
PHE
5
35.544
42.052
59.818
1.00
9.75
DIC

ATOM
42
O
PHE
5
35.985
40.896
59.803
1.00
8.48
DIC

ATOM
43
N
ALA
6
34.265
42.338
59.638
1.00
8.31
DIC

ATOM
44
CA
ALA
6
33.273
41.316
59.345
1.00
9.26
DIC

ATOM
45
CB
ALA
6
32.416
41.019
60.572
1.00
9.18
DIC

ATOM
46
C
ALA
6
32.424
41.941
58.252
1.00
9.59
DIC

ATOM
47
O
ALA
6
31.983
43.077
58.388
1.00
9.30
DIC

ATOM
48
N
ALA
7
32.195
41.218
57.165
1.00
9.68
DIC

ATOM
49
CA
ALA
7
31.385
41.777
56.088
1.00
9.55
DIC

ATOM
50
CB
ALA
7
32.242
42.714
55.237
1.00
10.43
DIC

ATOM
51
C
ALA
7
30.784
40.703
55.205
1.00
10.26
DIC

ATOM
52
O
ALA
7
31.358
39.628
55.069
1.00
9.81
DIC

ATOM
53
N
ASP
8
29.614
40.982
54.630
1.00
10.79
DIC

ATOM
54
CA
ASP
8
29.008
40.048
53.693
1.00
10.98
DIC

ATOM
55
CB
ASP
8
27.481
39.986
53.822
1.00
11.13
DIC

ATOM
56
CG
ASP
8
26.852
41.337
54.092
1.00
10.25
DIC

ATOM
57
OD1
ASP
8
27.419
42.365
53.676
1.00
8.93
DIC

ATOM
58
OD2
ASP
8
25.768
41.361
54.719
1.00
11.96
DIC

ATOM
59
C
ASP
8
29.399
40.620
52.340
1.00
12.11
DIC

ATOM
60
O
ASP
8
30.143
41.596
52.281
1.00
11.30
DIC

ATOM
61
N
ASP
9
28.903
40.042
51.255
1.00
12.32
DIC

ATOM
62
CA
ASP
9
29.269
40.534
49.931
1.00
13.23
DIC

ATOM
63
CB
ASP
9
28.701
39.607
48.852
1.00
14.44
DIC

ATOM
64
CG
ASP
9
29.286
39.890
47.486
1.00
14.65
DIC

ATOM
65
OD1
ASP
9
30.516
39.787
47.335
1.00
13.72
DIC

ATOM
66
OD2
ASP
9
28.520
40.222
46.567
1.00
17.00
DIC

ATOM
67
C
ASP
9
28.817
41.977
49.674
1.00
13.55
DIC

ATOM
68
O
ASP
9
29.500
42.737
48.984
1.00
12.70
DIC

ATOM
69
N
ASN
10
27.671
42.349
50.237
1.00
13.42
DIC

ATOM
70
CA
ASN
10
27.122
43.689
50.068
1.00
13.87
DIC

ATOM
71
CB
ASN
10
25.804
43.814
50.836
1.00
14.04
DIC

ATOM
72
CG
ASN
10
25.148
45.171
50.650
1.00
15.16
DIC

ATOM
73
OD1
ASN
10
24.977
45.634
49.523
1.00
14.38
DIC

ATOM
74
ND2
ASN
10
24.767
45.810
51.754
1.00
13.92
DIC

ATOM
75
C
ASN
10
28.074
44.794
50.527
1.00
13.56
DIC

ATOM
76
O
ASN
10
28.076
45.900
49.965
1.00
13.16
DIC

ATOM
77
N
TYR
11
28.879
44.492
51.541
1.00
12.92
DIC

ATOM
78
CA
TYR
11
29.821
45.460
52.091
1.00
13.06
DIC

ATOM
79
CB
TYR
11
29.733
45.440
53.616
1.00
13.83
DIC

ATOM
80
CG
TYR
11
28.756
46.430
54.192
1.00
14.83
DIC

ATOM
81
CD1
TYR
11
27.652
46.865
53.459
1.00
14.49
DIC

ATOM
82
CE1
TYR
11
26.758
47.782
53.995
1.00
15.54
DIC

ATOM
83
CD2
TYR
11
28.934
46.935
55.480
1.00
15.47
DIC

ATOM
84
CE2
TYR
11
28.044
47.849
56.021
1.00
16.13
DIC

ATOM
85
CZ
TYR
11
26.962
48.268
55.277
1.00
15.85
DIC

ATOM
86
OH
TYR
11
26.082
49.171
55.822
1.00
17.10
DIC

ATOM
87
C
TYR
11
31.278
45.291
51.677
1.00
13.35
DIC

ATOM
88
O
TYR
11
32.156
45.945
52.246
1.00
12.67
DIC

ATOM
89
N
ALA
12
31.540
44.436
50.689
1.00
12.77
DIC

ATOM
90
CA
ALA
12
32.905
44.196
50.226
1.00
11.93
DIC

ATOM
91
CB
ALA
12
32.898
43.176
49.085
1.00
12.43
DIC

ATOM
92
C
ALA
12
33.646
45.465
49.786
1.00
12.10
DIC

ATOM
93
O
ALA
12
34.812
45.659
50.131
1.00
9.34
DIC

ATOM
94
N
ALA
13
32.981
46.321
49.014
1.00
11.40
DIC

ATOM
95
CA
ALA
13
33.614
47.552
48.548
1.00
11.49
DIC

ATOM
96
CB
ALA
13
32.711
48.259
47.525
1.00
12.59
DIC

ATOM
97
C
ALA
13
33.935
48.486
49.719
1.00
11.12
DIC

ATOM
98
O
ALA
13
35.028
49.062
49.786
1.00
10.82
DIC

ATOM
99
N
TYR
14
32.988
48.624
50.643
1.00
10.01
DIC

ATOM
100
CA
TYR
14
33.169
49.479
51.812
1.00
10.22
DIC

ATOM
101
CB
TYR
14
31.869
49.535
52.623
1.00
10.13
DIC

ATOM
102
CG
TYR
14
30.670
49.883
51.775
1.00
11.37
DIC

ATOM
103
CD1
TYR
14
30.798
50.752
50.692
1.00
11.46
DIC

ATOM
104
CE1
TYR
14
29.709
51.098
49.913
1.00
12.49
DIC

ATOM
105
CD2
TYR
14
29.406
49.363
52.061
1.00
11.77
DIC

ATOM
106
CE2
TYR
14
28.301
49.708
51.288
1.00
12.94
DIC

ATOM
107
CZ
TYR
14
28.464
50.581
50.211
1.00
13.37
DIC

ATOM
108
OH
TYR
14
27.387
50.969
49.445
1.00
13.68
DIC

ATOM
109
C
TYR
14
34.320
48.993
52.692
1.00
10.01
DIC

ATOM
110
O
TYR
14
35.101
49.796
53.209
1.00
10.44
DIC

ATOM
111
N
LEU
15
34.402
47.677
52.864
1.00
9.93
DIC

ATOM
112
CA
LEU
15
35.454
47.043
53.649
1.00
10.44
DIC

ATOM
113
CB
LEU
15
35.311
45.523
53.558
1.00
10.41
DIC

ATOM
114
CG
LEU
15
36.559
44.670
53.803
1.00
11.91
DIC

ATOM
115
CD1
LEU
15
36.951
44.732
55.262
1.00
12.15
DIC

ATOM
116
CD2
LEU
15
36.282
43.228
53.380
1.00
10.34
DIC

ATOM
117
C
LEU
15
36.822
47.451
53.097
1.00
9.78
DIC

ATOM
118
O
LEU
15
37.767
47.689
53.852
1.00
10.03
DIC

ATOM
119
N
CYS
16
36.917
47.505
51.771
1.00
9.90
DIC

ATOM
120
CA
CYS
16
38.160
47.878
51.111
1.00
9.59
DIC

ATOM
121
CB
CYS
16
38.005
47.761
49.590
1.00
9.35
DIC

ATOM
122
SG
CYS
16
39.528
48.155
48.711
1.00
10.55
DIC

ATOM
123
C
CYS
16
38.574
49.301
51.483
1.00
9.71
DIC

ATOM
124
O
CYS
16
39.737
49.564
51.793
1.00
10.85
DIC

ATOM
125
N
VAL
17
37.618
50.219
51.452
1.00
9.93
DIC

ATOM
126
CA
VAL
17
37.891
51.611
51.805
1.00
10.54
DIC

ATOM
127
CB
VAL
17
36.663
52.502
51.509
1.00
9.19
DIC

ATOM
128
CG1
VAL
17
36.853
53.889
52.088
1.00
9.35
DIC

ATOM
129
CG2
VAL
17
36.459
52.596
49.993
1.00
10.21
DIC

ATOM
130
C
VAL
17
38.277
51.730
53.281
1.00
11.16
DIC

ATOM
131
O
VAL
17
39.214
52.445
53.625
1.00
12.58
DIC

ATOM
132
N
ALA
18
37.562
51.031
54.154
1.00
11.08
DIC

ATOM
133
CA
ALA
18
37.877
51.094
55.580
1.00
10.23
DIC

ATOM
134
CB
ALA
18
36.838
50.319
56.390
1.00
9.79
DIC

ATOM
135
C
ALA
18
39.267
50.515
55.830
1.00
10.26
DIC

ATOM
136
O
ALA
18
40.059
51.075
56.598
1.00
9.16
DIC

ATOM
137
N
ALA
19
39.554
49.387
55.187
1.00
10.33
DIC

ATOM
138
CA
ALA
19
40.843
48.729
55.343
1.00
11.10
DIC

ATOM
139
CB
ALA
19
40.883
47.450
54.519
1.00
12.50
DIC

ATOM
140
C
ALA
19
41.955
49.672
54.910
1.00
12.35
DIC

ATOM
141
O
ALA
19
42.945
49.839
55.620
1.00
11.18
DIC

ATOM
142
N
LYS
20
41.786
50.307
53.755
1.00
12.66
DIC

ATOM
143
CA
LYS
20
42.812
51.227
53.277
1.00
13.17
DIC

ATOM
144
CB
LYS
20
42.485
51.723
51.872
1.00
14.36
DIC

ATOM
145
CG
LYS
20
43.592
52.576
51.284
1.00
18.06
DIC

ATOM
146
CD
LYS
20
43.350
52.878
49.815
1.00
21.04
DIC

ATOM
147
CE
LYS
20
44.518
53.666
49.229
1.00
22.73
DIC

ATOM
148
NZ
LYS
20
44.283
54.010
47.797
1.00
23.84
DIC

ATOM
149
C
LYS
20
42.994
52.410
54.227
1.00
12.86
DIC

ATOM
150
O
LYS
20
44.114
52.877
54.426
1.00
11.70
DIC

ATOM
151
N
SER
21
41.909
52.893
54.830
1.00
12.92
DIC

ATOM
152
CA
SER
21
42.049
54.014
55.759
1.00
13.27
DIC

ATOM
153
CB
SER
21
40.684
54.476
56.298
1.00
13.74
DIC

ATOM
154
OG
SER
21
40.217
53.672
57.370
1.00
13.06
DIC

ATOM
155
C
SER
21
42.964
53.580
56.904
1.00
12.88
DIC

ATOM
156
O
SER
21
43.782
54.360
57.383
1.00
13.01
DIC

ATOM
157
N
VAL
22
42.845
52.327
57.332
1.00
13.22
DIC

ATOM
158
CA
VAL
22
43.698
51.825
58.410
1.00
12.36
DIC

ATOM
159
CB
VAL
22
43.308
50.398
58.836
1.00
12.30
DIC

ATOM
160
CG1
VAL
22
44.288
49.892
59.872
1.00
11.72
DIC

ATOM
161
CG2
VAL
22
41.887
50.383
59.389
1.00
11.48
DIC

ATOM
162
C
VAL
22
45.164
51.799
57.979
1.00
12.37
DIC

ATOM
163
O
VAL
22
46.059
52.159
58.749
1.00
11.98
DIC

ATOM
164
N
GLU
23
45.420
51.364
56.751
1.00
12.92
DIC

ATOM
165
CA
GLU
23
46.800
51.317
56.276
1.00
13.21
DIC

ATOM
166
CB
GLU
23
46.890
50.655
54.897
1.00
13.48
DIC

ATOM
167
CG
GLU
23
46.489
49.186
54.863
1.00
14.09
DIC

ATOM
168
CD
GLU
23
46.831
48.546
53.536
1.00
14.75
DIC

ATOM
169
OE1
GLU
23
46.676
49.224
52.503
1.00
14.77
DIC

ATOM
170
OE2
GLU
23
47.247
47.369
53.519
1.00
14.64
DIC

ATOM
171
C
GLU
23
47.376
52.724
56.193
1.00
13.14
DIC

ATOM
172
O
GLU
23
48.504
52.961
56.615
1.00
13.52
DIC

ATOM
173
N
ALA
24
46.591
53.653
55.649
1.00
11.95
DIC

ATOM
174
CA
ALA
24
47.030
55.032
55.501
1.00
12.18
DIC

ATOM
175
CB
ALA
24
45.916
55.881
54.857
1.00
13.20
DIC

ATOM
176
C
ALA
24
47.433
55.636
56.833
1.00
11.58
DIC

ATOM
177
O
ALA
24
48.382
56.422
56.905
1.00
10.67
DIC

ATOM
178
N
ALA
25
46.722
55.259
57.891
1.00
11.32
DIC

ATOM
179
CA
ALA
25
46.994
55.784
59.225
1.00
11.21
DIC

ATOM
180
CB
ALA
25
45.745
55.648
60.096
1.00
10.62
DIC

ATOM
181
C
ALA
25
48.199
55.160
59.939
1.00
11.67
DIC

ATOM
182
O
ALA
25
48.613
55.651
60.985
1.00
11.24
DIC

ATOM
183
N
HIS
26
48.763
54.088
59.393
1.00
11.30
DIC

ATOM
184
CA
HIS
26
49.926
53.459
60.027
1.00
12.66
DIC

ATOM
185
CB
HIS
26
49.529
52.171
60.761
1.00
12.73
DIC

ATOM
186
CG
HIS
26
48.360
52.331
61.682
1.00
14.25
DIC

ATOM
187
CD2
HIS
26
48.296
52.451
63.030
1.00
13.73
DIC

ATOM
188
ND1
HIS
26
47.058
52.385
61.229
1.00
13.15
DIC

ATOM
189
CE1
HIS
26
46.244
52.529
62.258
1.00
13.73
DIC

ATOM
190
NE2
HIS
26
46.970
52.571
63.362
1.00
14.21
DIC

ATOM
191
C
HIS
26
50.968
53.126
58.965
1.00
12.72
DIC

ATOM
192
O
HIS
26
51.201
51.956
58.654
1.00
12.84
DIC

ATOM
193
N
PRO
27
51.616
54.155
58.402
1.00
13.48
DIC

ATOM
194
CD
PRO
27
51.482
55.586
58.732
1.00
14.47
DIC

ATOM
195
CA
PRO
27
52.628
53.949
57.369
1.00
14.03
DIC

ATOM
196
CB
PRO
27
53.064
55.377
57.015
1.00
14.64
DIC

ATOM
197
CG
PRO
27
52.802
56.148
58.271
1.00
15.02
DIC

ATOM
198
C
PRO
27
53.800
53.040
57.730
1.00
13.73
DIC

ATOM
199
O
PRO
27
54.418
52.447
56.842
1.00
14.16
DIC

ATOM
200
N
ASP
28
54.119
52.912
59.013
1.00
13.19
DIC

ATOM
201
CA
ASP
28
55.240
52.044
59.368
1.00
13.54
DIC

ATOM
202
CB
ASP
28
56.407
52.855
59.934
1.00
14.01
DIC

ATOM
203
CG
ASP
28
57.687
52.033
60.027
1.00
12.49
DIC

ATOM
204
OD1
ASP
28
57.987
51.294
59.066
1.00
13.79
DIC

ATOM
205
OD2
ASP
28
58.390
52.123
61.047
1.00
11.67
DIC

ATOM
206
C
ASP
28
54.883
50.930
60.335
1.00
14.24
DIC

ATOM
207
O
ASP
28
55.706
50.504
61.146
1.00
13.51
DIC

ATOM
208
N
THR
29
53.651
50.450
60.242
1.00
14.30
DIC

ATOM
209
CA
THR
29
53.219
49.367
61.102
1.00
15.03
DIC

ATOM
210
CB
THR
29
52.156
49.818
62.104
1.00
13.26
DIC

ATOM
211
OG1
THR
29
52.632
50.956
62.828
1.00
12.77
DIC

ATOM
212
CG2
THR
29
51.865
48.694
63.090
1.00
13.03
DIC

ATOM
213
C
THR
29
52.636
48.266
60.243
1.00
15.57
DIC

ATOM
214
O
THR
29
51.882
48.528
59.305
1.00
14.98
DIC

ATOM
215
N
GLU
30
53.012
47.034
60.554
1.00
16.16
DIC

ATOM
216
CA
GLU
30
52.520
45.874
59.825
1.00
17.32
DIC

ATOM
217
CB
GLU
30
53.287
44.630
60.281
1.00
19.02
DIC

ATOM
218
CG
GLU
30
53.694
43.659
59.178
1.00
23.03
DIC

ATOM
219
CD
GLU
30
54.316
44.344
57.969
1.00
23.93
DIC

ATOM
220
OE1
GLU
30
53.564
44.698
57.039
1.00
24.55
DIC

ATOM
221
OE2
GLU
30
55.549
44.537
57.947
1.00
24.76
DIC

ATOM
222
C
GLU
30
51.046
45.750
60.185
1.00
16.48
DIC

ATOM
223
O
GLU
30
50.701
45.675
61.368
1.00
16.29
DIC

ATOM
224
N
ILE
31
50.174
45.760
59.181
1.00
15.30
DIC

ATOM
225
CA
ILE
31
48.743
45.628
59.436
1.00
15.17
DIC

ATOM
226
CB
ILE
31
47.905
46.770
58.778
1.00
14.27
DIC

ATOM
227
CG2
ILE
31
46.420
46.573
59.106
1.00
14.26
DIC

ATOM
228
CG1
ILE
31
48.368
48.140
59.277
1.00
13.70
DIC

ATOM
229
CD
ILE
31
48.085
48.397
60.740
1.00
12.11
DIC

ATOM
230
C
ILE
31
48.245
44.305
58.868
1.00
14.65
DIC

ATOM
231
O
ILE
31
48.185
44.127
57.650
1.00
14.91
DIC

ATOM
232
N
ARG
32
47.891
43.384
59.757
1.00
13.99
DIC

ATOM
233
CA
ARG
32
47.384
42.087
59.349
1.00
13.79
DIC

ATOM
234
CB
ARG
32
47.983
40.982
60.225
1.00
15.26
DIC

ATOM
235
CG
ARG
32
49.510
40.934
60.177
1.00
18.70
DIC

ATOM
236
CD
ARG
32
50.067
39.639
60.752
1.00
21.47
DIC

ATOM
237
NE
ARG
32
49.766
39.471
62.173
1.00
24.86
DIC

ATOM
238
CZ
ARG
32
50.180
38.439
62.905
1.00
27.54
DIC

ATOM
239
NH1
ARG
32
50.916
37.483
62.346
1.00
28.88
DIC

ATOM
240
NH2
ARG
32
49.861
38.360
64.196
1.00
27.69
DIC

ATOM
241
C
ARG
32
45.867
42.107
59.478
1.00
13.24
DIC

ATOM
242
O
ARG
32
45.330
42.234
60.578
1.00
11.50
DIC

ATOM
243
N
PHE
33
45.185
41.997
58.341
1.00
12.52
DIC

ATOM
244
CA
PHE
33
43.730
42.009
58.301
1.00
11.78
DIC

ATOM
245
CB
PHE
33
43.246
42.686
57.010
1.00
10.75
DIC

ATOM
246
CG
PHE
33
43.502
44.171
56.950
1.00
9.65
DIC

ATOM
247
CD1
PHE
33
42.777
45.054
57.748
1.00
9.25
DIC

ATOM
248
CD2
PHE
33
44.414
44.693
56.038
1.00
10.53
DIC

ATOM
249
CE1
PHE
33
42.953
46.436
57.627
1.00
9.15
DIC

ATOM
250
CE2
PHE
33
44.600
46.077
55.908
1.00
9.49
DIC

ATOM
251
CZ
PHE
33
43.864
46.944
56.703
1.00
9.68
DIC

ATOM
252
C
PHE
33
43.134
40.597
58.365
1.00
11.96
DIC

ATOM
253
O
PHE
33
43.565
39.697
57.639
1.00
12.74
DIC

ATOM
254
N
HIS
34
42.145
40.420
59.238
1.00
11.46
DIC

ATOM
255
CA
HIS
34
41.431
39.149
59.403
1.00
11.17
DIC

ATOM
256
CB
HIS
34
41.523
38.659
60.850
1.00
11.57
DIC

ATOM
257
CG
HIS
34
42.919
38.593
61.384
1.00
12.66
DIC

ATOM
258
CD2
HIS
34
43.704
39.544
61.942
1.00
13.37
DIC

ATOM
259
ND1
HIS
34
43.667
37.437
61.370
1.00
13.22
DIC

ATOM
260
CE1
HIS
34
44.854
37.677
61.899
1.00
13.27
DIC

ATOM
261
NE2
HIS
34
44.903
38.947
62.255
1.00
14.11
DIC

ATOM
262
C
HIS
34
39.971
39.480
59.091
1.00
11.20
DIC

ATOM
263
O
HIS
34
39.336
40.217
59.830
1.00
9.79
DIC

ATOM
264
N
VAL
35
39.428
38.944
58.010
1.00
10.16
DIC

ATOM
265
CA
VAL
35
38.050
39.266
57.679
1.00
10.38
DIC

ATOM
266
CB
VAL
35
37.945
39.733
56.208
1.00
11.51
DIC

ATOM
267
CG1
VAL
35
36.512
40.077
55.867
1.00
11.42
DIC

ATOM
268
CG2
VAL
35
38.847
40.945
55.985
1.00
12.17
DIC

ATOM
269
C
VAL
35
37.072
38.126
57.929
1.00
10.51
DIC

ATOM
270
O
VAL
35
37.240
37.017
57.408
1.00
9.02
DIC

ATOM
271
N
LEU
36
36.060
38.397
58.754
1.00
10.05
DIC

ATOM
272
CA
LEU
36
35.027
37.412
59.044
1.00
10.98
DIC

ATOM
273
CB
LEU
36
34.282
37.766
60.341
1.00
11.52
DIC

ATOM
274
CG
LEU
36
35.176
37.835
61.592
1.00
12.34
DIC

ATOM
275
CD1
LEU
36
34.319
37.965
62.858
1.00
13.53
DIC

ATOM
276
CD2
LEU
36
36.035
36.574
61.679
1.00
13.20
DIC

ATOM
277
C
LEU
36
34.123
37.527
57.821
1.00
11.61
DIC

ATOM
278
O
LEU
36
33.275
38.409
57.728
1.00
10.93
DIC

ATOM
279
N
ASP
37
34.352
36.620
56.881
1.00
12.50
DIC

ATOM
280
CA
ASP
37
33.678
36.580
55.591
1.00
13.19
DIC

ATOM
281
CB
ASP
37
34.660
35.981
54.580
1.00
13.28
DIC

ATOM
282
CG
ASP
37
34.090
35.878
53.189
1.00
13.48
DIC

ATOM
283
OD1
ASP
37
32.903
36.212
52.997
1.00
14.14
DIC

ATOM
284
OD2
ASP
37
34.843
35.456
52.290
1.00
13.50
DIC

ATOM
285
C
ASP
37
32.369
35.803
55.588
1.00
14.68
DIC

ATOM
286
O
ASP
37
32.363
34.569
55.634
1.00
14.18
DIC

ATOM
287
N
ALA
38
31.258
36.526
55.511
1.00
14.79
DIC

ATOM
288
CA
ALA
38
29.954
35.884
55.521
1.00
15.72
DIC

ATOM
289
CB
ALA
38
28.983
36.689
56.390
1.00
16.90
DIC

ATOM
290
C
ALA
38
29.362
35.669
54.132
1.00
15.90
DIC

ATOM
291
O
ALA
38
28.143
35.600
53.978
1.00
17.34
DIC

ATOM
292
N
GLY
39
30.213
35.557
53.120
1.00
15.36
DIC

ATOM
293
CA
GLY
39
29.698
35.321
51.786
1.00
13.98
DIC

ATOM
294
C
GLY
39
30.208
36.249
50.706
1.00
12.66
DIC

ATOM
295
O
GLY
39
29.534
36.454
49.701
1.00
13.26
DIC

ATOM
296
N
ILE
40
31.395
36.805
50.901
1.00
11.81
DIC

ATOM
297
CA
ILE
40
31.985
37.695
49.909
1.00
12.00
DIC

ATOM
298
CB
ILE
40
33.220
38.417
50.493
1.00
11.76
DIC

ATOM
299
CG2
ILE
40
33.764
39.419
49.488
1.00
12.77
DIC

ATOM
300
CG1
ILE
40
32.815
39.178
51.761
1.00
10.15
DIC

ATOM
301
CD
ILE
40
33.981
39.741
52.549
1.00
10.52
DIC

ATOM
302
C
ILE
40
32.389
36.857
48.688
1.00
12.84
DIC

ATOM
303
O
ILE
40
32.958
35.772
48.828
1.00
12.10
DIC

ATOM
304
N
SER
41
32.078
37.350
47.491
1.00
13.34
DIC

ATOM
305
CA
SER
41
32.410
36.629
46.265
1.00
13.44
DIC

ATOM
306
CB
SER
41
31.778
37.311
45.043
1.00
12.76
DIC

ATOM
307
OG
SER
41
32.427
38.536
44.747
1.00
12.89
DIC

ATOM
308
C
SER
41
33.909
36.552
46.055
1.00
14.12
DIC

ATOM
309
O
SER
41
34.662
37.369
46.583
1.00
14.41
DIC

ATOM
310
N
GLU
42
34.336
35.570
45.267
1.00
15.57
DIC

ATOM
311
CA
GLU
42
35.749
35.401
44.968
1.00
16.08
DIC

ATOM
312
CB
GLU
42
35.967
34.183
44.060
1.00
17.55
DIC

ATOM
313
CG
GLU
42
37.424
33.922
43.704
1.00
19.96
DIC

ATOM
314
CD
GLU
42
37.961
34.853
42.631
1.00
21.69
DIC

ATOM
315
OE1
GLU
42
39.199
35.047
42.572
1.00
23.34
DIC

ATOM
316
OE2
GLU
42
37.153
35.382
41.835
1.00
22.79
DIC

ATOM
317
C
GLU
42
36.229
36.660
44.265
1.00
15.85
DIC

ATOM
318
O
GLU
42
37.332
37.137
44.511
1.00
15.67
DIC

ATOM
319
N
ALA
43
35.385
37.198
43.393
1.00
14.84
DIC

ATOM
320
CA
ALA
43
35.725
38.399
42.654
1.00
15.14
DIC

ATOM
321
CB
ALA
43
34.635
38.710
41.622
1.00
15.42
DIC

ATOM
322
C
ALA
43
35.907
39.579
43.600
1.00
14.89
DIC

ATOM
323
O
ALA
43
36.821
40.381
43.430
1.00
14.31
DIC

ATOM
324
N
ASN
44
35.048
39.683
44.610
1.00
15.08
DIC

ATOM
325
CA
ASN
44
35.163
40.794
45.550
1.00
14.76
DIC

ATOM
326
CB
ASN
44
33.847
41.008
46.304
1.00
14.30
DIC

ATOM
327
CG
ASN
44
32.817
41.746
45.464
1.00
15.33
DIC

ATOM
328
OD1
ASN
44
33.167
42.625
44.674
1.00
14.17
DIC

ATOM
329
ND2
ASN
44
31.543
41.406
45.637
1.00
15.84
DIC

ATOM
330
C
ASN
44
36.324
40.661
46.529
1.00
14.57
DIC

ATOM
331
O
ASN
44
36.852
41.666
47.005
1.00
14.31
DIC

ATOM
332
N
ARG
45
36.732
39.431
46.828
1.00
14.77
DIC

ATOM
333
CA
ARG
45
37.853
39.229
47.739
1.00
15.32
DIC

ATOM
334
CB
ARG
45
37.926
37.771
48.205
1.00
16.87
DIC

ATOM
335
CG
ARG
45
36.589
37.242
48.689
1.00
20.54
DIC

ATOM
336
CD
ARG
45
36.710
36.377
49.924
1.00
24.39
DIC

ATOM
337
NE
ARG
45
37.571
35.215
49.725
1.00
27.75
DIC

ATOM
338
CZ
ARG
45
37.704
34.225
50.608
1.00
29.60
DIC

ATOM
339
NH1
ARG
45
37.028
34.247
51.752
1.00
30.56
DIC

ATOM
340
NH2
ARG
45
38.526
33.216
50.353
1.00
30.76
DIC

ATOM
341
C
ARG
45
39.141
39.608
47.020
1.00
15.22
DIC

ATOM
342
O
ARG
45
40.002
40.277
47.590
1.00
14.16
DIC

ATOM
343
N
ALA
46
39.265
39.194
45.761
1.00
14.15
DIC

ATOM
344
CA
ALA
46
40.458
39.515
44.983
1.00
14.85
DIC

ATOM
345
CB
ALA
46
40.395
38.840
43.610
1.00
15.30
DIC

ATOM
346
C
ALA
46
40.545
41.029
44.823
1.00
14.64
DIC

ATOM
347
O
ALA
46
41.623
41.616
44.910
1.00
15.26
DIC

ATOM
348
N
ALA
47
39.397
41.662
44.600
1.00
14.80
DIC

ATOM
349
CA
ALA
47
39.348
43.112
44.430
1.00
14.02
DIC

ATOM
350
CB
ALA
47
37.938
43.536
44.039
1.00
15.12
DIC

ATOM
351
C
ALA
47
39.795
43.857
45.693
1.00
13.42
DIC

ATOM
352
O
ALA
47
40.562
44.823
45.618
1.00
12.41
DIC

ATOM
353
N
VAL
48
39.316
43.415
46.853
1.00
13.25
DIC

ATOM
354
CA
VAL
48
39.694
44.052
48.111
1.00
12.62
DIC

ATOM
355
CB
VAL
48
38.922
43.445
49.305
1.00
11.98
DIC

ATOM
356
CG1
VAL
48
39.458
43.992
50.609
1.00
10.86
DIC

ATOM
357
CG2
VAL
48
37.460
43.786
49.193
1.00
11.68
DIC

ATOM
358
C
VAL
48
41.192
43.891
48.350
1.00
12.98
DIC

ATOM
359
O
VAL
48
41.884
44.855
48.682
1.00
12.57
DIC

ATOM
360
N
ALA
49
41.692
42.672
48.168
1.00
13.13
DIC

ATOM
361
CA
ALA
49
43.102
42.386
48.374
1.00
14.18
DIC

ATOM
362
CB
ALA
49
43.355
40.892
48.245
1.00
13.51
DIC

ATOM
363
C
ALA
49
43.983
43.145
47.397
1.00
14.36
DIC

ATOM
364
O
ALA
49
45.072
43.601
47.752
1.00
15.03
DIC

ATOM
365
N
ALA
50
43.519
43.274
46.162
1.00
15.04
DIC

ATOM
366
CA
ALA
50
44.290
43.979
45.142
1.00
15.89
DIC

ATOM
367
CB
ALA
50
43.582
43.882
43.792
1.00
16.15
DIC

ATOM
368
C
ALA
50
44.530
45.443
45.492
1.00
16.46
DIC

ATOM
369
O
ALA
50
45.515
46.039
45.052
1.00
17.84
DIC

ATOM
370
N
ASN
51
43.631
46.029
46.277
1.00
16.90
DIC

ATOM
371
CA
ASN
51
43.758
47.432
46.661
1.00
17.24
DIC

ATOM
372
CB
ASN
51
42.379
48.060
46.826
1.00
17.14
DIC

ATOM
373
CG
ASN
51
41.709
48.355
45.507
1.00
16.69
DIC

ATOM
374
OD1
ASN
51
42.190
49.172
44.729
1.00
18.27
DIC

ATOM
375
ND2
ASN
51
40.584
47.700
45.253
1.00
16.79
DIC

ATOM
376
C
ASN
51
44.545
47.667
47.942
1.00
18.59
DIC

ATOM
377
O
ASN
51
44.784
48.815
48.324
1.00
17.91
DIC

ATOM
378
N
LEU
52
44.946
46.595
48.613
1.00
19.74
DIC

ATOM
379
CA
LEU
52
45.689
46.750
49.860
1.00
21.37
DIC

ATOM
380
CB
LEU
52
45.316
45.636
50.834
1.00
20.31
DIC

ATOM
381
CG
LEU
52
43.808
45.589
51.097
1.00
19.14
DIC

ATOM
382
CD1
LEU
52
43.488
44.439
52.019
1.00
19.58
DIC

ATOM
383
CD2
LEU
52
43.344
46.896
51.694
1.00
19.21
DIC

ATOM
384
C
LEU
52
47.195
46.798
49.645
1.00
23.35
DIC

ATOM
385
O
LEU
52
47.703
46.358
48.611
1.00
23.99
DIC

ATOM
386
N
ARG
53
47.896
47.337
50.639
1.00
25.01
DIC

ATOM
387
CA
ARG
53
49.346
47.509
50.589
1.00
27.42
DIC

ATOM
388
CB
ARG
53
49.894
47.695
52.012
1.00
26.42
DIC

ATOM
389
CG
ARG
53
50.983
48.739
52.099
1.00
25.31
DIC

ATOM
390
CD
ARG
53
50.808
49.649
53.310
1.00
24.31
DIC

ATOM
391
NE
ARG
53
50.903
48.918
54.567
1.00
22.35
DIC

ATOM
392
CZ
ARG
53
50.893
49.492
55.766
1.00
21.59
DIC

ATOM
393
NH1
ARG
53
50.791
50.811
55.878
1.00
20.50
DIC

ATOM
394
NH2
ARG
53
50.987
48.741
56.854
1.00
20.22
DIC

ATOM
395
C
ARG
53
50.089
46.390
49.875
1.00
28.67
DIC

ATOM
396
O
ARG
53
50.483
46.536
48.717
1.00
29.49
DIC

ATOM
397
N
GLY
55
50.292
45.278
50.563
1.00
30.50
DIC

ATOM
398
CA
GLY
55
50.987
44.173
49.937
1.00
32.29
DIC

ATOM
399
C
GLY
55
49.974
43.171
49.431
1.00
33.53
DIC

ATOM
400
O
GLY
55
50.312
42.264
48.663
1.00
34.18
DIC

ATOM
401
N
GLY
56
48.724
43.351
49.857
1.00
33.60
DIC

ATOM
402
CA
GLY
56
47.659
42.445
49.462
1.00
33.15
DIC

ATOM
403
C
GLY
56
47.872
41.107
50.146
1.00
33.10
DIC

ATOM
404
O
GLY
56
46.962
40.273
50.215
1.00
33.20
DIC

ATOM
405
N
GLY
57
49.088
40.914
50.656
1.00
32.04
DIC

ATOM
406
CA
GLY
57
49.447
39.682
51.333
1.00
30.83
DIC

ATOM
407
C
GLY
57
49.086
39.682
52.804
1.00
29.47
DIC

ATOM
408
O
GLY
57
49.138
38.640
53.457
1.00
30.37
DIC

ATOM
409
N
ASN
58
48.726
40.843
53.341
1.00
28.08
DIC

ATOM
410
CA
ASN
58
48.353
40.905
54.747
1.00
26.03
DIC

ATOM
411
CB
ASN
58
48.987
42.120
55.427
1.00
27.85
DIC

ATOM
412
CG
ASN
58
50.322
41.789
56.080
1.00
29.56
DIC

ATOM
413
OD1
ASN
58
50.447
40.787
56.791
1.00
30.26
DIC

ATOM
414
ND2
ASN
58
51.325
42.635
55.852
1.00
30.45
DIC

ATOM
415
C
ASN
58
46.845
40.893
54.995
1.00
24.13
DIC

ATOM
416
O
ASN
58
46.347
41.597
55.872
1.00
23.13
DIC

ATOM
417
N
ILE
59
46.114
40.099
54.217
1.00
20.72
DIC

ATOM
418
CA
ILE
59
44.678
39.992
54.423
1.00
19.23
DIC

ATOM
419
CB
ILE
59
43.873
40.915
53.471
1.00
19.07
DIC

ATOM
420
CG2
ILE
59
44.100
40.511
52.016
1.00
18.83
DIC

ATOM
421
CG1
ILE
59
42.387
40.848
53.838
1.00
18.98
DIC

ATOM
422
CD
ILE
59
41.510
41.865
53.110
1.00
19.26
DIC

ATOM
423
C
ILE
59
44.213
38.551
54.259
1.00
18.23
DIC

ATOM
424
O
ILE
59
44.446
37.916
53.233
1.00
17.66
DIC

ATOM
425
N
ARG
60
43.561
38.035
55.289
1.00
17.86
DIC

ATOM
426
CA
ARG
60
43.065
36.667
55.267
1.00
17.16
DIC

ATOM
427
CB
ARG
60
43.768
35.845
56.355
1.00
18.42
DIC

ATOM
428
CG
ARG
60
43.308
34.401
56.461
1.00
21.63
DIC

ATOM
429
CD
ARG
60
44.434
33.455
56.908
1.00
25.56
DIC

ATOM
430
NE
ARG
60
44.956
33.771
58.234
1.00
29.10
DIC

ATOM
431
CZ
ARG
60
45.878
34.698
58.483
1.00
31.08
DIC

ATOM
432
NH1
ARG
60
46.397
35.411
57.489
1.00
32.55
DIC

ATOM
433
NH2
ARG
60
46.277
34.922
59.730
1.00
31.29
DIC

ATOM
434
C
ARG
60
41.564
36.668
55.491
1.00
16.93
DIC

ATOM
435
O
ARG
60
41.067
37.309
56.422
1.00
16.37
DIC

ATOM
436
N
PHE
61
40.834
35.967
54.629
1.00
14.83
DIC

ATOM
437
CA
PHE
61
39.391
35.895
54.777
1.00
15.90
DIC

ATOM
438
CB
PHE
61
38.705
35.931
53.413
1.00
14.84
DIC

ATOM
439
CG
PHE
61
38.919
37.215
52.670
1.00
13.10
DIC

ATOM
440
CD1
PHE
61
40.034
37.389
51.862
1.00
14.08
DIC

ATOM
441
CD2
PHE
61
38.010
38.258
52.793
1.00
12.89
DIC

ATOM
442
CE1
PHE
61
40.241
38.585
51.185
1.00
13.50
DIC

ATOM
443
CE2
PHE
61
38.206
39.457
52.121
1.00
12.60
DIC

ATOM
444
CZ
PHE
61
39.322
39.623
51.316
1.00
13.60
DIC

ATOM
445
C
PHE
61
39.022
34.624
55.520
1.00
15.95
DIC

ATOM
446
O
PHE
61
39.541
33.555
55.221
1.00
15.87
DIC

ATOM
447
N
ILE
62
38.131
34.750
56.498
1.00
16.48
DIC

ATOM
448
CA
ILE
62
37.709
33.611
57.304
1.00
16.08
DIC

ATOM
449
CB
ILE
62
37.979
33.864
58.801
1.00
15.26
DIC

ATOM
450
CG2
ILE
62
37.698
32.604
59.611
1.00
13.49
DIC

ATOM
451
CG1
ILE
62
39.428
34.292
59.002
1.00
14.70
DIC

ATOM
452
CD
ILE
62
39.692
34.939
60.347
1.00
14.47
DIC

ATOM
453
C
ILE
62
36.220
33.360
57.123
1.00
17.10
DIC

ATOM
454
O
ILE
62
35.385
34.154
57.558
1.00
16.19
DIC

ATOM
455
N
ASP
63
35.895
32.242
56.489
1.00
18.05
DIC

ATOM
456
CA
ASP
63
34.511
31.883
56.245
1.00
18.87
DIC

ATOM
457
CB
ASP
63
34.451
30.589
55.420
1.00
21.18
DIC

ATOM
458
CG
ASP
63
34.653
30.834
53.932
1.00
22.82
DIC

ATOM
459
OD1
ASP
63
35.479
31.697
53.565
1.00
23.93
DIC

ATOM
460
OD2
ASP
63
33.986
30.157
53.127
1.00
23.20
DIC

ATOM
461
C
ASP
63
33.712
31.708
57.530
1.00
18.75
DIC

ATOM
462
O
ASP
63
34.127
31.004
58.448
1.00
18.31
DIC

ATOM
463
N
VAL
64
32.570
32.377
57.595
1.00
18.18
DIC

ATOM
464
CA
VAL
64
31.681
32.258
58.739
1.00
17.99
DIC

ATOM
465
CB
VAL
64
31.571
33.582
59.544
1.00
17.92
DIC

ATOM
466
CG1
VAL
64
32.939
33.989
60.053
1.00
17.77
DIC

ATOM
467
CG2
VAL
64
30.960
34.681
58.694
1.00
16.70
DIC

ATOM
468
C
VAL
64
30.325
31.889
58.161
1.00
17.88
DIC

ATOM
469
O
VAL
64
29.990
32.298
57.049
1.00
18.31
DIC

ATOM
470
N
ASN
65
29.562
31.085
58.891
1.00
17.42
DIC

ATOM
471
CA
ASN
65
28.241
30.685
58.430
1.00
17.62
DIC

ATOM
472
CB
ASN
65
27.924
29.261
58.885
1.00
18.50
DIC

ATOM
473
CG
ASN
65
26.616
28.743
58.306
1.00
20.54
DIC

ATOM
474
OD1
ASN
65
25.714
29.521
57.968
1.00
20.86
DIC

ATOM
475
ND2
ASN
65
26.499
27.420
58.200
1.00
19.60
DIC

ATOM
476
C
ASN
65
27.227
31.652
59.035
1.00
17.64
DIC

ATOM
477
O
ASN
65
26.932
31.585
60.230
1.00
16.65
DIC

ATOM
478
N
PRO
66
26.675
32.565
58.219
1.00
17.39
DIC

ATOM
479
CD
PRO
66
26.861
32.781
56.774
1.00
17.24
DIC

ATOM
480
CA
PRO
66
25.703
33.510
58.769
1.00
18.54
DIC

ATOM
481
CB
PRO
66
25.296
34.347
57.551
1.00
18.56
DIC

ATOM
482
CG
PRO
66
25.566
33.444
56.388
1.00
17.52
DIC

ATOM
483
C
PRO
66
24.516
32.866
59.480
1.00
19.19
DIC

ATOM
484
O
PRO
66
24.040
33.396
60.479
1.00
19.74
DIC

ATOM
485
N
ALA
67
24.058
31.717
58.984
1.00
19.24
DIC

ATOM
486
CA
ALA
67
22.913
31.029
59.583
1.00
18.98
DIC

ATOM
487
CB
ALA
67
22.603
29.740
58.805
1.00
19.76
DIC

ATOM
488
C
ALA
67
23.117
30.710
61.062
1.00
18.67
DIC

ATOM
489
O
ALA
67
22.154
30.496
61.797
1.00
18.27
DIC

ATOM
490
N
ASP
68
24.370
30.678
61.497
1.00
18.15
DIC

ATOM
491
CA
ASP
68
24.672
30.382
62.892
1.00
17.77
DIC

ATOM
492
CB
ASP
68
26.176
30.488
63.148
1.00
18.64
DIC

ATOM
493
CG
ASP
68
26.963
29.362
62.507
1.00
19.18
DIC

ATOM
494
OD1
ASP
68
28.206
29.374
62.630
1.00
19.68
DIC

ATOM
495
OD2
ASP
68
26.349
28.466
61.889
1.00
19.92
DIC

ATOM
496
C
ASP
68
23.948
31.307
63.868
1.00
17.23
DIC

ATOM
497
O
ASP
68
23.621
30.908
64.986
1.00
14.77
DIC

ATOM
498
N
PHE
69
23.705
32.544
63.452
1.00
17.46
DIC

ATOM
499
CA
PHE
69
23.061
33.513
64.332
1.00
18.56
DIC

ATOM
500
CB
PHE
69
23.895
34.801
64.374
1.00
19.00
DIC

ATOM
501
CG
PHE
69
25.382
34.558
64.338
1.00
18.44
DIC

ATOM
502
CD1
PHE
69
26.069
34.550
63.126
1.00
18.34
DIC

ATOM
503
CD2
PHE
69
26.080
34.274
65.506
1.00
17.81
DIC

ATOM
504
CE1
PHE
69
27.435
34.256
63.081
1.00
17.68
DIC

ATOM
505
CE2
PHE
69
27.441
33.980
65.477
1.00
17.08
DIC

ATOM
506
CZ
PHE
69
28.122
33.968
64.264
1.00
17.08
DIC

ATOM
507
C
PHE
69
21.642
33.825
63.889
1.00
19.64
DIC

ATOM
508
O
PHE
69
21.075
34.854
64.259
1.00
18.70
DIC

ATOM
509
N
ALA
70
21.067
32.919
63.109
1.00
20.08
DIC

ATOM
510
CA
ALA
70
19.718
33.094
62.593
1.00
21.26
DIC

ATOM
511
CB
ALA
70
19.302
31.846
61.818
1.00
22.16
DIC

ATOM
512
C
ALA
70
18.664
33.419
63.654
1.00
21.75
DIC

ATOM
513
O
ALA
70
17.783
34.246
63.421
1.00
22.84
DIC

ATOM
514
N
GLY
71
18.753
32.775
64.813
1.00
20.77
DIC

ATOM
515
CA
GLY
71
17.773
33.010
65.861
1.00
20.62
DIC

ATOM
516
C
GLY
71
17.817
34.344
66.599
1.00
20.26
DIC

ATOM
517
O
GLY
71
16.882
34.670
67.342
1.00
19.68
DIC

ATOM
518
N
PHE
72
18.878
35.120
66.392
1.00
18.49
DIC

ATOM
519
CA
PHE
72
19.042
36.412
67.063
1.00
17.73
DIC

ATOM
520
CB
PHE
72
20.536
36.763
67.145
1.00
18.72
DIC

ATOM
521
CG
PHE
72
21.348
35.802
67.980
1.00
20.16
DIC

ATOM
522
CD1
PHE
72
22.724
35.960
68.097
1.00
20.37
DIC

ATOM
523
CD2
PHE
72
20.737
34.760
68.668
1.00
20.44
DIC

ATOM
524
CE1
PHE
72
23.477
35.100
68.888
1.00
21.46
DIC

ATOM
525
CE2
PHE
72
21.484
33.892
69.462
1.00
21.52
DIC

ATOM
526
CZ
PHE
72
22.858
34.065
69.572
1.00
20.60
DIC

ATOM
527
C
PHE
72
18.274
37.551
66.386
1.00
16.90
DIC

ATOM
528
O
PHE
72
18.171
37.603
65.163
1.00
16.76
DIC

ATOM
529
N
PRO
73
17.738
38.492
67.176
1.00
16.37
DIC

ATOM
530
CD
PRO
73
17.908
38.675
68.626
1.00
16.89
DIC

ATOM
531
CA
PRO
73
16.984
39.609
66.600
1.00
16.59
DIC

ATOM
532
CB
PRO
73
16.616
40.447
67.825
1.00
16.80
DIC

ATOM
533
CG
PRO
73
17.705
40.164
68.773
1.00
17.34
DIC

ATOM
534
C
PRO
73
17.720
40.419
65.537
1.00
16.70
DIC

ATOM
535
O
PRO
73
18.924
40.645
65.629
1.00
15.30
DIC

ATOM
536
N
LEU
74
16.980
40.839
64.517
1.00
16.98
DIC

ATOM
537
CA
LEU
74
17.548
41.634
63.434
1.00
17.87
DIC

ATOM
538
CB
LEU
74
17.843
40.730
62.234
1.00
17.95
DIC

ATOM
539
CG
LEU
74
18.954
41.199
61.293
1.00
17.88
DIC

ATOM
540
CD1
LEU
74
20.295
41.203
62.038
1.00
18.31
DIC

ATOM
541
CD2
LEU
74
19.023
40.272
60.092
1.00
19.47
DIC

ATOM
542
C
LEU
74
16.520
42.713
63.068
1.00
18.09
DIC

ATOM
543
O
LEU
74
15.955
42.709
61.972
1.00
19.62
DIC

ATOM
544
N
ASN
75
16.290
43.630
64.005
1.00
17.72
DIC

ATOM
545
CA
ASN
75
15.322
44.715
63.846
1.00
17.11
DIC

ATOM
546
CB
ASN
75
14.735
45.110
65.229
1.00
17.62
DIC

ATOM
547
CG
ASN
75
15.817
45.329
66.338
1.00
20.20
DIC

ATOM
548
OD1
ASN
75
16.525
44.396
66.744
1.00
19.66
DIC

ATOM
549
ND2
ASN
75
15.911
46.566
66.844
1.00
20.31
DIC

ATOM
550
C
ASN
75
15.830
45.971
63.124
1.00
16.07
DIC

ATOM
551
O
ASN
75
15.053
46.683
62.477
1.00
15.53
DIC

ATOM
552
N
ILE
76
17.123
46.244
63.238
1.00
13.71
DIC

ATOM
553
CA
ILE
76
17.706
47.421
62.606
1.00
11.78
DIC

ATOM
554
CB
ILE
76
19.043
47.771
63.295
1.00
10.80
DIC

ATOM
555
CG2
ILE
76
19.621
49.050
62.717
1.00
10.89
DIC

ATOM
556
CG1
ILE
76
18.784
47.965
64.795
1.00
11.97
DIC

ATOM
557
CD
ILE
76
20.028
48.230
65.615
1.00
11.60
DIC

ATOM
558
C
ILE
76
17.880
47.165
61.112
1.00
10.59
DIC

ATOM
559
O
ILE
76
18.735
46.393
60.692
1.00
9.86
DIC

ATOM
560
N
ARG
77
17.047
47.823
60.312
1.00
10.58
DIC

ATOM
561
CA
ARG
77
17.046
47.629
58.865
1.00
9.71
DIC

ATOM
562
CB
ARG
77
16.017
48.560
58.224
1.00
10.51
DIC

ATOM
563
CG
ARG
77
15.694
48.227
56.770
1.00
12.15
DIC

ATOM
564
CD
ARG
77
14.702
49.229
56.194
1.00
14.05
DIC

ATOM
565
NE
ARG
77
14.405
48.956
54.792
1.00
15.41
DIC

ATOM
566
CZ
ARG
77
14.025
49.879
53.915
1.00
15.57
DIC

ATOM
567
NH1
ARG
77
13.894
51.145
54.291
1.00
16.47
DIC

ATOM
568
NH2
ARG
77
13.783
49.537
52.660
1.00
16.39
DIC

ATOM
569
C
ARG
77
18.370
47.769
58.125
1.00
9.25
DIC

ATOM
570
O
ARG
77
18.662
46.979
57.228
1.00
8.24
DIC

ATOM
571
N
HIS
78
19.175
48.765
58.475
1.00
9.54
DIC

ATOM
572
CA
HIS
78
20.435
48.953
57.763
1.00
9.73
DIC

ATOM
573
CB
HIS
78
20.945
50.392
57.948
1.00
9.99
DIC

ATOM
574
CG
HIS
78
21.495
50.677
59.313
1.00
9.83
DIC

ATOM
575
CD2
HIS
78
20.910
51.193
60.417
1.00
9.26
DIC

ATOM
576
ND1
HIS
78
22.801
50.399
59.664
1.00
12.11
DIC

ATOM
577
CE1
HIS
78
22.992
50.731
60.927
1.00
10.27
DIC

ATOM
578
NE2
HIS
78
21.860
51.213
61.407
1.00
10.71
DIC

ATOM
579
C
HIS
78
21.518
47.956
58.160
1.00
9.77
DIC

ATOM
580
O
HIS
78
22.634
48.014
57.643
1.00
9.16
DIC

ATOM
581
N
ILE
79
21.186
47.018
59.046
1.00
8.59
DIC

ATOM
582
CA
ILE
79
22.176
46.041
59.499
1.00
9.47
DIC

ATOM
583
CB
ILE
79
22.352
46.115
61.036
1.00
8.92
DIC

ATOM
584
CG2
ILE
79
23.362
45.071
61.497
1.00
9.10
DIC

ATOM
585
CG1
ILE
79
22.817
47.519
61.444
1.00
8.56
DIC

ATOM
586
CD
ILE
79
22.873
47.729
62.947
1.00
7.54
DIC

ATOM
587
C
ILE
79
21.855
44.597
59.129
1.00
9.95
DIC

ATOM
588
O
ILE
79
20.745
44.118
59.370
1.00
9.89
DIC

ATOM
589
N
SER
80
22.834
43.897
58.558
1.00
10.77
DIC

ATOM
590
CA
SER
80
22.644
42.489
58.185
1.00
10.59
DIC

ATOM
591
CB
SER
80
23.405
42.148
56.896
1.00
11.09
DIC

ATOM
592
OG
SER
80
24.799
42.152
57.115
1.00
11.31
DIC

ATOM
593
C
SER
80
23.102
41.551
59.304
1.00
10.27
DIC

ATOM
594
O
SER
80
23.784
41.967
60.250
1.00
9.68
DIC

ATOM
595
N
ILE
81
22.719
40.282
59.181
1.00
9.94
DIC

ATOM
596
CA
ILE
81
23.035
39.260
60.167
1.00
10.92
DIC

ATOM
597
CB
ILE
81
22.450
37.880
59.731
1.00
10.93
DIC

ATOM
598
CG2
ILE
81
23.161
37.384
58.480
1.00
10.14
DIC

ATOM
599
CG1
ILE
81
22.602
36.851
60.856
1.00
11.94
DIC

ATOM
600
CD
ILE
81
21.957
37.263
62.171
1.00
14.84
DIC

ATOM
601
C
ILE
81
24.530
39.131
60.452
1.00
10.21
DIC

ATOM
602
O
ILE
81
24.914
38.697
61.527
1.00
10.54
DIC

ATOM
603
N
THR
82
25.370
39.530
59.504
1.00
10.02
DIC

ATOM
604
CA
THR
82
26.814
39.440
59.690
1.00
11.39
DIC

ATOM
605
CB
THR
82
27.562
39.940
58.441
1.00
11.65
DIC

ATOM
606
OG1
THR
82
27.204
39.125
57.325
1.00
14.61
DIC

ATOM
607
CG2
THR
82
29.065
39.859
58.646
1.00
12.44
DIC

ATOM
608
C
THR
82
27.294
40.228
60.909
1.00
10.13
DIC

ATOM
609
O
THR
82
28.376
39.972
61.438
1.00
11.18
DIC

ATOM
610
N
THR
83
26.490
41.184
61.352
1.00
9.24
DIC

ATOM
611
CA
THR
83
26.839
41.991
62.518
1.00
8.73
DIC

ATOM
612
CB
THR
83
25.721
43.017
62.837
1.00
8.11
DIC

ATOM
613
OG1
THR
83
26.189
43.930
63.833
1.00
6.94
DIC

ATOM
614
CG2
THR
83
24.463
42.316
63.354
1.00
5.65
DIC

ATOM
615
C
THR
83
27.095
41.143
63.774
1.00
8.48
DIC

ATOM
616
O
THR
83
27.764
41.597
64.714
1.00
7.40
DIC

ATOM
617
N
TYR
84
26.571
39.917
63.796
1.00
7.85
DIC

ATOM
618
CA
TYR
84
26.750
39.036
64.961
1.00
7.48
DIC

ATOM
619
CB
TYR
84
25.541
38.118
65.149
1.00
8.12
DIC

ATOM
620
CG
TYR
84
24.309
38.765
65.730
1.00
8.79
DIC

ATOM
621
CD1
TYR
84
23.223
39.089
64.920
1.00
8.55
DIC

ATOM
622
CE1
TYR
84
22.061
39.639
65.456
1.00
8.25
DIC

ATOM
623
CD2
TYR
84
24.208
39.014
67.100
1.00
9.35
DIC

ATOM
624
CE2
TYR
84
23.047
39.569
67.647
1.00
8.56
DIC

ATOM
625
CZ
TYR
84
21.977
39.873
66.813
1.00
8.60
DIC

ATOM
626
OH
TYR
84
20.811
40.386
67.340
1.00
10.62
DIC

ATOM
627
C
TYR
84
27.988
38.142
64.917
1.00
7.79
DIC

ATOM
628
O
TYR
84
28.356
37.544
65.934
1.00
7.52
DIC

ATOM
629
N
ALA
85
28.631
38.046
63.756
1.00
7.28
DIC

ATOM
630
CA
ALA
85
29.802
37.172
63.608
1.00
8.87
DIC

ATOM
631
CB
ALA
85
30.381
37.297
62.200
1.00
8.53
DIC

ATOM
632
C
ALA
85
30.905
37.410
64.627
1.00
9.13
DIC

ATOM
633
O
ALA
85
31.639
36.483
64.993
1.00
8.63
DIC

ATOM
634
N
ARG
86
31.024
38.649
65.082
1.00
9.00
DIC

ATOM
635
CA
ARG
86
32.065
38.996
66.026
1.00
9.80
DIC

ATOM
636
CB
ARG
86
32.022
40.502
66.310
1.00
9.41
DIC

ATOM
637
CG
ARG
86
30.870
40.984
67.172
1.00
9.46
DIC

ATOM
638
CD
ARG
86
30.719
42.501
67.076
1.00
8.59
DIC

ATOM
639
NE
ARG
86
29.920
42.881
65.919
1.00
7.42
DIC

ATOM
640
CZ
ARG
86
29.754
44.128
65.491
1.00
8.59
DIC

ATOM
641
NH1
ARG
86
30.342
45.144
66.115
1.00
7.18
DIC

ATOM
642
NH2
ARG
86
28.974
44.361
64.449
1.00
9.43
DIC

ATOM
643
C
ARG
86
31.979
38.185
67.313
1.00
9.79
DIC

ATOM
644
O
ARG
86
32.978
38.004
68.000
1.00
10.73
DIC

ATOM
645
N
LEU
87
30.788
37.680
67.624
1.00
10.39
DIC

ATOM
646
CA
LEU
87
30.584
36.880
68.836
1.00
10.81
DIC

ATOM
647
CB
LEU
87
29.092
36.574
69.016
1.00
10.20
DIC

ATOM
648
CG
LEU
87
28.168
37.787
69.233
1.00
10.48
DIC

ATOM
649
CD1
LEU
87
26.731
37.315
69.344
1.00
9.48
DIC

ATOM
650
CD2
LEU
87
28.579
38.549
70.491
1.00
9.82
DIC

ATOM
651
C
LEU
87
31.394
35.574
68.884
1.00
10.74
DIC

ATOM
652
O
LEU
87
31.635
35.036
69.957
1.00
9.80
DIC

ATOM
653
N
LYS
88
31.811
35.067
67.725
1.00
11.78
DIC

ATOM
654
CA
LYS
88
32.599
33.831
67.665
1.00
11.01
DIC

ATOM
655
CB
LYS
88
32.009
32.882
66.612
1.00
11.35
DIC

ATOM
656
CG
LYS
88
30.771
32.128
67.071
1.00
9.90
DIC

ATOM
657
CD
LYS
88
30.341
31.114
66.016
1.00
11.02
DIC

ATOM
658
CE
LYS
88
29.384
30.086
66.593
1.00
10.58
DIC

ATOM
659
NZ
LYS
88
29.046
29.040
65.576
1.00
11.61
DIC

ATOM
660
C
LYS
88
34.071
34.097
67.332
1.00
11.82
DIC

ATOM
661
O
LYS
88
34.782
33.215
66.852
1.00
12.29
DIC

ATOM
662
N
LEU
89
34.531
35.307
67.611
1.00
12.36
DIC

ATOM
663
CA
LEU
89
35.902
35.686
67.303
1.00
13.57
DIC

ATOM
664
CB
LEU
89
36.144
37.121
67.772
1.00
15.15
DIC

ATOM
665
CG
LEU
89
36.980
38.051
66.888
1.00
16.39
DIC

ATOM
666
CD1
LEU
89
36.680
37.846
65.418
1.00
16.80
DIC

ATOM
667
CD2
LEU
89
36.684
39.481
67.294
1.00
17.50
DIC

ATOM
668
C
LEU
89
36.919
34.725
67.918
1.00
13.79
DIC

ATOM
669
O
LEU
89
37.951
34.420
67.310
1.00
12.41
DIC

ATOM
670
N
GLY
90
36.615
34.241
69.116
1.00
12.82
DIC

ATOM
671
CA
GLY
90
37.496
33.303
69.785
1.00
13.31
DIC

ATOM
672
C
GLY
90
37.608
31.968
69.057
1.00
13.77
DIC

ATOM
673
O
GLY
90
38.568
31.225
69.270
1.00
12.09
DIC

ATOM
674
N
GLU
91
36.625
31.662
68.210
1.00
13.93
DIC

ATOM
675
CA
GLU
91
36.608
30.423
67.431
1.00
14.80
DIC

ATOM
676
CB
GLU
91
35.172
29.930
67.221
1.00
15.97
DIC

ATOM
677
CG
GLU
91
34.422
29.493
68.475
1.00
18.54
DIC

ATOM
678
CD
GLU
91
33.035
28.944
68.145
1.00
20.57
DIC

ATOM
679
OE1
GLU
91
32.929
28.123
67.211
1.00
21.70
DIC

ATOM
680
OE2
GLU
91
32.057
29.326
68.816
1.00
20.80
DIC

ATOM
681
C
GLU
91
37.232
30.632
66.050
1.00
14.18
DIC

ATOM
682
O
GLU
91
37.833
29.717
65.478
1.00
13.91
DIC

ATOM
683
N
TYR
92
37.076
31.838
65.518
1.00
14.10
DIC

ATOM
684
CA
TYR
92
37.591
32.171
64.193
1.00
14.43
DIC

ATOM
685
CB
TYR
92
36.791
33.330
63.595
1.00
13.92
DIC

ATOM
686
CG
TYR
92
35.306
33.081
63.464
1.00
14.30
DIC

ATOM
687
CD1
TYR
92
34.816
31.844
63.032
1.00
14.28
DIC

ATOM
688
CE1
TYR
92
33.448
31.630
62.854
1.00
14.75
DIC

ATOM
689
CD2
TYR
92
34.392
34.099
63.717
1.00
13.77
DIC

ATOM
690
CE2
TYR
92
33.027
33.900
63.539
1.00
15.62
DIC

ATOM
691
CZ
TYR
92
32.560
32.663
63.105
1.00
14.94
DIC

ATOM
692
OH
TYR
92
31.213
32.477
62.906
1.00
15.54
DIC

ATOM
693
C
TYR
92
39.073
32.531
64.108
1.00
14.98
DIC

ATOM
694
O
TYR
92
39.701
32.328
63.072
1.00
14.45
DIC

ATOM
695
N
ILE
93
39.629
33.078
65.181
1.00
16.91
DIC

ATOM
696
CA
ILE
93
41.028
33.486
65.177
1.00
17.72
DIC

ATOM
697
CB
ILE
93
41.133
35.016
65.393
1.00
18.50
DIC

ATOM
698
CG2
ILE
93
42.591
35.432
65.555
1.00
17.36
DIC

ATOM
699
CG1
ILE
93
40.487
35.734
64.201
1.00
18.54
DIC

ATOM
700
CD
ILE
93
40.412
37.226
64.340
1.00
19.24
DIC

ATOM
701
C
ILE
93
41.858
32.751
66.220
1.00
18.60
DIC

ATOM
702
O
ILE
93
41.575
32.824
67.419
1.00
19.10
DIC

ATOM
703
N
ALA
94
42.885
32.043
65.758
1.00
18.48
DIC

ATOM
704
CA
ALA
94
43.748
31.279
66.651
1.00
20.07
DIC

ATOM
705
CB
ALA
94
43.905
29.870
66.122
1.00
19.66
DIC

ATOM
706
C
ALA
94
45.123
31.896
66.856
1.00
20.84
DIC

ATOM
707
O
ALA
94
45.715
31.768
67.931
1.00
20.49
DIC

ATOM
708
N
ASP
95
45.625
32.568
65.825
1.00
22.76
DIC

ATOM
709
CA
ASP
95
46.953
33.177
65.862
1.00
25.64
DIC

ATOM
710
CB
ASP
95
47.476
33.365
64.430
1.00
27.52
DIC

ATOM
711
CG
ASP
95
46.420
33.918
63.484
1.00
29.58
DIC

ATOM
712
OD1
ASP
95
46.777
34.365
62.374
1.00
31.56
DIC

ATOM
713
OD2
ASP
95
45.226
33.898
63.838
1.00
31.61
DIC

ATOM
714
C
ASP
95
47.129
34.494
66.625
1.00
25.59
DIC

ATOM
715
O
ASP
95
48.215
35.072
66.591
1.00
27.43
DIC

ATOM
716
N
CYS
96
46.102
34.967
67.325
1.00
24.71
DIC

ATOM
717
CA
CYS
96
46.232
36.235
68.043
1.00
23.67
DIC

ATOM
718
CB
CYS
96
45.513
37.347
67.274
1.00
23.87
DIC

ATOM
719
SG
CYS
96
46.038
37.496
65.578
1.00
26.37
DIC

ATOM
720
C
CYS
96
45.728
36.252
69.478
1.00
22.46
DIC

ATOM
721
O
CYS
96
44.646
35.741
69.776
1.00
22.34
DIC

ATOM
722
N
ASP
97
46.515
36.858
70.364
1.00
20.39
DIC

ATOM
723
CA
ASP
97
46.124
36.987
71.762
1.00
20.32
DIC

ATOM
724
CB
ASP
97
47.354
37.031
72.667
1.00
20.67
DIC

ATOM
725
CG
ASP
97
47.976
35.667
72.871
1.00
21.98
DIC

ATOM
726
OD1
ASP
97
49.035
35.593
73.525
1.00
23.35
DIC

ATOM
727
OD2
ASP
97
47.405
34.666
72.386
1.00
23.09
DIC

ATOM
728
C
ASP
97
45.323
38.279
71.925
1.00
18.84
DIC

ATOM
729
O
ASP
97
44.574
38.438
72.887
1.00
19.35
DIC

ATOM
730
N
LYS
98
45.503
39.198
70.978
1.00
16.98
DIC

ATOM
731
CA
LYS
98
44.814
40.488
70.975
1.00
15.16
DIC

ATOM
732
CB
LYS
98
45.704
41.580
71.585
1.00
15.88
DIC

ATOM
733
CG
LYS
98
45.142
42.998
71.424
1.00
16.96
DIC

ATOM
734
CD
LYS
98
46.102
44.099
71.908
1.00
16.73
DIC

ATOM
735
CE
LYS
98
46.335
44.046
73.413
1.00
16.78
DIC

ATOM
736
NZ
LYS
98
47.070
45.241
73.933
1.00
13.95
DIC

ATOM
737
C
LYS
98
44.479
40.890
69.540
1.00
14.03
DIC

ATOM
738
O
LYS
98
45.287
40.695
68.637
1.00
13.30
DIC

ATOM
739
N
VAL
99
43.281
41.431
69.332
1.00
11.95
DIC

ATOM
740
CA
VAL
99
42.868
41.900
68.012
1.00
11.37
DIC

ATOM
741
CB
VAL
99
42.024
40.852
67.236
1.00
11.54
DIC

ATOM
742
CG1
VAL
99
42.877
39.639
66.882
1.00
11.02
DIC

ATOM
743
CG2
VAL
99
40.794
40.453
68.058
1.00
10.46
DIC

ATOM
744
C
VAL
99
42.021
43.156
68.171
1.00
11.18
DIC

ATOM
745
O
VAL
99
41.327
43.322
69.171
1.00
10.93
DIC

ATOM
746
N
LEU
100
42.095
44.044
67.187
1.00
10.87
DIC

ATOM
747
CA
LEU
100
41.314
45.271
67.212
1.00
10.79
DIC

ATOM
748
CB
LEU
100
42.197
46.484
66.880
1.00
10.94
DIC

ATOM
749
CG
LEU
100
41.529
47.869
66.831
1.00
12.58
DIC

ATOM
750
CD1
LEU
100
40.633
48.068
68.043
1.00
11.52
DIC

ATOM
751
CD2
LEU
100
42.601
48.949
66.788
1.00
13.16
DIC

ATOM
752
C
LEU
100
40.219
45.108
66.169
1.00
10.87
DIC

ATOM
753
O
LEU
100
40.499
45.034
64.964
1.00
10.41
DIC

ATOM
754
N
TYR
101
38.981
45.026
66.651
1.00
10.75
DIC

ATOM
755
CA
TYR
101
37.811
44.861
65.806
1.00
10.15
DIC

ATOM
756
CB
TYR
101
36.714
44.096
66.553
1.00
11.92
DIC

ATOM
757
CG
TYR
101
35.519
43.787
65.679
1.00
12.22
DIC

ATOM
758
CD1
TYR
101
35.489
42.629
64.912
1.00
13.77
DIC

ATOM
759
CE1
TYR
101
34.442
42.355
64.055
1.00
14.00
DIC

ATOM
760
CD2
TYR
101
34.452
44.677
65.566
1.00
13.42
DIC

ATOM
761
CE2
TYR
101
33.377
44.409
64.690
1.00
13.71
DIC

ATOM
762
CZ
TYR
101
33.390
43.240
63.944
1.00
14.55
DIC

ATOM
763
OH
TYR
101
32.356
42.920
63.085
1.00
16.39
DIC

ATOM
764
C
TYR
101
37.251
46.216
65.411
1.00
10.17
DIC

ATOM
765
O
TYR
101
37.062
47.088
66.267
1.00
8.43
DIC

ATOM
766
N
LEU
102
36.972
46.385
64.121
1.00
8.96
DIC

ATOM
767
CA
LEU
102
36.409
47.629
63.617
1.00
9.15
DIC

ATOM
768
CB
LEU
102
37.429
48.370
62.757
1.00
9.36
DIC

ATOM
769
CG
LEU
102
38.760
48.796
63.379
1.00
10.19
DIC

ATOM
770
CD1
LEU
102
39.640
49.399
62.292
1.00
9.39
DIC

ATOM
771
CD2
LEU
102
38.507
49.791
64.514
1.00
9.64
DIC

ATOM
772
C
LEU
102
35.182
47.341
62.757
1.00
9.25
DIC

ATOM
773
O
LEU
102
35.178
46.379
61.988
1.00
9.46
DIC

ATOM
774
N
ASP
103
34.141
48.160
62.902
1.00
7.67
DIC

ATOM
775
CA
ASP
103
32.942
48.022
62.074
1.00
6.79
DIC

ATOM
776
CB
ASP
103
31.854
49.000
62.505
1.00
6.14
DIC

ATOM
777
CG
ASP
103
30.853
48.392
63.452
1.00
6.30
DIC

ATOM
778
OD1
ASP
103
29.900
49.112
63.821
1.00
6.96
DIC

ATOM
779
OD2
ASP
103
31.013
47.212
63.831
1.00
6.76
DIC

ATOM
780
C
ASP
103
33.407
48.438
60.689
1.00
6.85
DIC

ATOM
781
O
ASP
103
34.500
48.972
60.536
1.00
6.31
DIC

ATOM
782
N
ILE
104
32.564
48.234
59.690
1.00
8.06
DIC

ATOM
783
CA
ILE
104
32.914
48.593
58.318
1.00
7.88
DIC

ATOM
784
CB
ILE
104
32.057
47.796
57.315
1.00
9.07
DIC

ATOM
785
CG2
ILE
104
32.357
48.246
55.891
1.00
9.25
DIC

ATOM
786
CG1
ILE
104
32.297
46.290
57.504
1.00
8.98
DIC

ATOM
787
CD
ILE
104
33.728
45.819
57.279
1.00
9.78
DIC

ATOM
788
C
ILE
104
32.697
50.077
58.058
1.00
8.07
DIC

ATOM
789
O
ILE
104
33.375
50.675
57.223
1.00
7.27
DIC

ATOM
790
N
ASP
105
31.747
50.663
58.778
1.00
7.66
DIC

ATOM
791
CA
ASP
105
31.412
52.075
58.630
1.00
8.00
DIC

ATOM
792
CB
ASP
105
29.941
52.304
59.001
1.00
6.68
DIC

ATOM
793
CG
ASP
105
29.618
51.884
60.426
1.00
5.32
DIC

ATOM
794
OD1
ASP
105
30.399
51.116
61.034
1.00
5.29
DIC

ATOM
795
OD2
ASP
105
28.555
52.303
60.942
1.00
5.88
DIC

ATOM
796
C
ASP
105
32.303
52.991
59.469
1.00
8.38
DIC

ATOM
797
O
ASP
105
31.811
53.904
60.140
1.00
8.29
DIC

ATOM
798
N
VAL
106
33.609
52.733
59.437
1.00
9.42
DIC

ATOM
799
CA
VAL
106
34.565
53.552
60.170
1.00
10.80
DIC

ATOM
800
CB
VAL
106
35.344
52.758
61.252
1.00
11.19
DIC

ATOM
801
CG1
VAL
106
34.380
52.108
62.219
1.00
10.51
DIC

ATOM
802
CG2
VAL
106
36.258
51.732
60.595
1.00
11.56
DIC

ATOM
803
C
VAL
106
35.585
54.115
59.201
1.00
11.38
DIC

ATOM
804
O
VAL
106
35.790
53.579
58.112
1.00
10.35
DIC

ATOM
805
N
LEU
107
36.227
55.194
59.623
1.00
12.57
DIC

ATOM
806
CA
LEU
107
37.249
55.860
58.833
1.00
13.47
DIC

ATOM
807
CB
LEU
107
36.648
57.092
58.159
1.00
13.56
DIC

ATOM
808
CG
LEU
107
36.761
57.246
56.639
1.00
15.06
DIC

ATOM
809
CD1
LEU
107
36.504
55.925
55.932
1.00
14.78
DIC

ATOM
810
CD2
LEU
107
35.761
58.311
56.183
1.00
15.25
DIC

ATOM
811
C
LEU
107
38.346
56.262
59.820
1.00
13.50
DIC

ATOM
812
O
LEU
107
38.173
57.193
60.602
1.00
13.59
DIC

ATOM
813
N
VAL
108
39.457
55.532
59.798
1.00
13.84
DIC

ATOM
814
CA
VAL
108
40.581
55.799
60.689
1.00
14.29
DIC

ATOM
815
CB
VAL
108
41.566
54.613
60.695
1.00
13.17
DIC

ATOM
816
CG1
VAL
108
42.776
54.931
61.572
1.00
11.37
DIC

ATOM
817
CG2
VAL
108
40.866
53.378
61.199
1.00
11.78
DIC

ATOM
818
C
VAL
108
41.303
57.050
60.223
1.00
15.14
DIC

ATOM
819
O
VAL
108
41.829
57.080
59.111
1.00
15.87
DIC

ATOM
820
N
ARG
109
41.336
58.077
61.072
1.00
16.17
DIC

ATOM
821
CA
ARG
109
41.975
59.341
60.711
1.00
16.20
DIC

ATOM
822
CB
ARG
109
41.024
60.505
60.978
1.00
18.37
DIC

ATOM
823
CG
ARG
109
39.558
60.117
61.037
1.00
21.36
DIC

ATOM
824
CD
ARG
109
38.713
61.006
60.157
1.00
23.86
DIC

ATOM
825
NE
ARG
109
39.024
62.420
60.326
1.00
26.81
DIC

ATOM
826
CZ
ARG
109
38.490
63.389
59.584
1.00
27.63
DIC

ATOM
827
NH1
ARG
109
38.828
64.653
59.792
1.00
28.71
DIC

ATOM
828
NH2
ARG
109
37.614
63.089
58.635
1.00
27.97
DIC

ATOM
829
C
ARG
109
43.284
59.610
61.444
1.00
15.84
DIC

ATOM
830
O
ARG
109
43.962
60.596
61.159
1.00
15.77
DIC

ATOM
831
N
ASP
110
43.623
58.758
62.401
1.00
14.29
DIC

ATOM
832
CA
ASP
110
44.854
58.930
63.156
1.00
14.80
DIC

ATOM
833
CB
ASP
110
44.643
59.920
64.309
1.00
15.65
DIC

ATOM
834
CG
ASP
110
45.953
60.434
64.894
1.00
17.51
DIC

ATOM
835
OD1
ASP
110
46.918
60.646
64.127
1.00
18.17
DIC

ATOM
836
OD2
ASP
110
46.019
60.651
66.121
1.00
17.67
DIC

ATOM
837
C
ASP
110
45.302
57.577
63.683
1.00
15.01
DIC

ATOM
838
O
ASP
110
44.514
56.635
63.761
1.00
13.14
DIC

ATOM
839
N
ARG
111
46.580
57.493
64.026
1.00
15.41
DIC

ATOM
840
CA
ARG
111
47.185
56.274
64.532
1.00
15.96
DIC

ATOM
841
CB
ARG
111
48.589
56.587
65.040
1.00
18.93
DIC

ATOM
842
CG
ARG
111
49.292
55.406
65.638
1.00
21.10
DIC

ATOM
843
CD
ARG
111
49.885
55.785
66.979
1.00
26.48
DIC

ATOM
844
NE
ARG
111
50.917
56.811
66.896
1.00
29.16
DIC

ATOM
845
CZ
ARG
111
51.589
57.267
67.946
1.00
29.73
DIC

ATOM
846
NH1
ARG
111
51.332
56.778
69.155
1.00
30.77
DIC

ATOM
847
NH2
ARG
111
52.514
58.211
67.789
1.00
30.14
DIC

ATOM
848
C
ARG
111
46.381
55.601
65.643
1.00
15.25
DIC

ATOM
849
O
ARG
111
45.870
56.266
66.543
1.00
13.85
DIC

ATOM
850
N
LEU
112
46.294
54.275
65.572
1.00
13.25
DIC

ATOM
851
CA
LEU
112
45.569
53.467
66.555
1.00
13.07
DIC

ATOM
852
CB
LEU
112
44.820
52.336
65.845
1.00
12.62
DIC

ATOM
853
CG
LEU
112
43.346
52.448
65.422
1.00
13.47
DIC

ATOM
854
CD1
LEU
112
42.780
53.836
65.654
1.00
11.94
DIC

ATOM
855
CD2
LEU
112
43.243
52.037
63.970
1.00
13.50
DIC

ATOM
856
C
LEU
112
46.508
52.850
67.593
1.00
12.50
DIC

ATOM
857
O
LEU
112
46.067
52.151
68.497
1.00
11.71
DIC

ATOM
858
N
THR
113
47.802
53.107
67.462
1.00
11.56
DIC

ATOM
859
CA
THR
113
48.783
52.539
68.380
1.00
12.01
DIC

ATOM
860
CB
THR
113
50.184
53.060
68.041
1.00
11.89
DIC

ATOM
861
OG1
THR
113
50.408
52.885
66.634
1.00
11.98
DIC

ATOM
862
CG2
THR
113
51.261
52.293
68.820
1.00
13.32
DIC

ATOM
863
C
THR
113
48.475
52.770
69.864
1.00
12.09
DIC

ATOM
864
O
THR
113
48.600
51.851
70.672
1.00
13.00
DIC

ATOM
865
N
PRO
114
48.071
53.997
70.246
1.00
11.73
DIC

ATOM
866
CD
PRO
114
48.006
55.257
69.488
1.00
11.33
DIC

ATOM
867
CA
PRO
114
47.764
54.227
71.662
1.00
12.05
DIC

ATOM
868
CB
PRO
114
47.313
55.685
71.685
1.00
11.93
DIC

ATOM
869
CG
PRO
114
48.143
56.295
70.585
1.00
12.09
DIC

ATOM
870
C
PRO
114
46.674
53.271
72.150
1.00
11.56
DIC

ATOM
871
O
PRO
114
46.743
52.757
73.266
1.00
11.37
DIC

ATOM
872
N
LEU
115
45.664
53.037
71.314
1.00
10.81
DIC

ATOM
873
CA
LEU
115
44.590
52.120
71.683
1.00
10.71
DIC

ATOM
874
CB
LEU
115
43.423
52.211
70.689
1.00
10.70
DIC

ATOM
875
CG
LEU
115
42.277
51.209
70.886
1.00
10.89
DIC

ATOM
876
CD1
LEU
115
41.718
51.306
72.293
1.00
11.32
DIC

ATOM
877
CD2
LEU
115
41.184
51.495
69.857
1.00
10.96
DIC

ATOM
878
C
LEU
115
45.150
50.703
71.693
1.00
9.83
DIC

ATOM
879
O
LEU
115
44.966
49.967
72.648
1.00
11.08
DIC

ATOM
880
N
TRP
116
45.850
50.338
70.628
1.00
9.48
DIC

ATOM
881
CA
TRP
116
46.436
49.007
70.511
1.00
10.20
DIC

ATOM
882
CB
TRP
116
47.167
48.873
69.164
1.00
9.44
DIC

ATOM
883
CG
TRP
116
47.899
47.551
68.983
1.00
10.50
DIC

ATOM
884
CD2
TRP
116
47.327
46.288
68.606
1.00
10.45
DIC

ATOM
885
CE2
TRP
116
48.374
45.337
68.603
1.00
11.26
DIC

ATOM
886
CE3
TRP
116
46.033
45.869
68.276
1.00
11.37
DIC

ATOM
887
CD1
TRP
116
49.228
47.320
69.185
1.00
10.48
DIC

ATOM
888
NE1
TRP
116
49.522
45.992
68.956
1.00
11.48
DIC

ATOM
889
CZ2
TRP
116
48.166
43.988
68.276
1.00
10.98
DIC

ATOM
890
CZ3
TRP
116
45.827
44.529
67.951
1.00
10.53
DIC

ATOM
891
CH2
TRP
116
46.892
43.605
67.954
1.00
9.77
DIC

ATOM
892
C
TRP
116
47.388
48.674
71.662
1.00
11.01
DIC

ATOM
893
O
TRP
116
47.439
47.533
72.117
1.00
11.69
DIC

ATOM
894
N
ASP
117
48.133
49.667
72.138
1.00
11.59
DIC

ATOM
895
CA
ASP
117
49.084
49.442
73.223
1.00
12.22
DIC

ATOM
896
CB
ASP
117
50.162
50.534
73.238
1.00
12.26
DIC

ATOM
897
CG
ASP
117
51.120
50.425
72.077
1.00
13.59
DIC

ATOM
898
OD1
ASP
117
51.257
49.321
71.515
1.00
12.25
DIC

ATOM
899
OD2
ASP
117
51.752
51.449
71.745
1.00
14.88
DIC

ATOM
900
C
ASP
117
48.438
49.390
74.599
1.00
13.46
DIC

ATOM
901
O
ASP
117
49.125
49.168
75.598
1.00
13.16
DIC

ATOM
902
N
THR
118
47.127
49.606
74.660
1.00
14.71
DIC

ATOM
903
CA
THR
118
46.425
49.575
75.939
1.00
16.37
DIC

ATOM
904
CB
THR
118
44.938
49.978
75.779
1.00
16.43
DIC

ATOM
905
OG1
THR
118
44.862
51.305
75.244
1.00
16.77
DIC

ATOM
906
CG2
THR
118
44.220
49.948
77.129
1.00
17.74
DIC

ATOM
907
C
THR
118
46.494
48.183
76.555
1.00
17.33
DIC

ATOM
908
O
THR
118
46.284
47.184
75.871
1.00
16.96
DIC

ATOM
909
N
ASP
119
46.792
48.123
77.849
1.00
18.74
DIC

ATOM
910
CA
ASP
119
46.871
46.843
78.552
1.00
20.28
DIC

ATOM
911
CB
ASP
119
47.930
46.919
79.656
1.00
22.23
DIC

ATOM
912
CG
ASP
119
47.948
45.685
80.536
1.00
24.82
DIC

ATOM
913
OD1
ASP
119
47.718
44.570
80.020
1.00
25.22
DIC

ATOM
914
OD2
ASP
119
48.211
45.832
81.750
1.00
27.28
DIC

ATOM
915
C
ASP
119
45.496
46.519
79.137
1.00
20.16
DIC

ATOM
916
O
ASP
119
45.038
47.173
80.076
1.00
19.67
DIC

ATOM
917
N
LEU
120
44.844
45.511
78.565
1.00
19.65
DIC

ATOM
918
CA
LEU
120
43.505
45.102
78.985
1.00
19.29
DIC

ATOM
919
CB
LEU
120
42.851
44.242
77.892
1.00
18.66
DIC

ATOM
920
CG
LEU
120
42.554
44.848
76.517
1.00
18.25
DIC

ATOM
921
CD1
LEU
120
43.830
45.349
75.890
1.00
19.33
DIC

ATOM
922
CD2
LEU
120
41.924
43.796
75.627
1.00
17.41
DIC

ATOM
923
C
LEU
120
43.457
44.333
80.303
1.00
19.39
DIC

ATOM
924
O
LEU
120
42.377
44.121
80.857
1.00
19.64
DIC

ATOM
925
N
GLY
121
44.611
43.908
80.804
1.00
19.06
DIC

ATOM
926
CA
GLY
121
44.618
43.151
82.044
1.00
19.45
DIC

ATOM
927
C
GLY
121
43.724
41.933
81.890
1.00
19.65
DIC

ATOM
928
O
GLY
121
43.805
41.225
80.884
1.00
19.83
DIC

ATOM
929
N
ASN
122
42.863
41.672
82.866
1.00
19.86
DIC

ATOM
930
CA
ASN
122
41.982
40.518
82.747
1.00
20.32
DIC

ATOM
931
CB
ASN
122
41.870
39.765
84.079
1.00
22.30
DIC

ATOM
932
CG
ASN
122
41.270
38.374
83.910
1.00
23.86
DIC

ATOM
933
OD1
ASN
122
41.773
37.559
83.132
1.00
24.87
DIC

ATOM
934
ND2
ASN
122
40.193
38.099
84.637
1.00
24.89
DIC

ATOM
935
C
ASN
122
40.597
40.944
82.271
1.00
19.00
DIC

ATOM
936
O
ASN
122
39.629
40.201
82.424
1.00
18.30
DIC

ATOM
937
N
ASN
123
40.507
42.149
81.707
1.00
17.37
DIC

ATOM
938
CA
ASN
123
39.238
42.651
81.186
1.00
16.29
DIC

ATOM
939
CB
ASN
123
39.313
44.147
80.858
1.00
15.93
DIC

ATOM
940
CG
ASN
123
39.347
45.014
82.090
1.00
16.95
DIC

ATOM
941
OD1
ASN
123
40.344
45.684
82.366
1.00
17.08
DIC

ATOM
942
ND2
ASN
123
38.257
45.013
82.839
1.00
16.13
DIC

ATOM
943
C
ASN
123
38.935
41.895
79.908
1.00
15.30
DIC

ATOM
944
O
ASN
123
39.842
41.387
79.253
1.00
15.35
DIC

ATOM
945
N
TRP
124
37.656
41.834
79.551
1.00
14.51
DIC

ATOM
946
CA
TRP
124
37.238
41.137
78.350
1.00
12.04
DIC

ATOM
947
CB
TRP
124
35.727
40.935
78.354
1.00
12.24
DIC

ATOM
948
CG
TRP
124
35.220
39.973
79.384
1.00
12.53
DIC

ATOM
949
CD2
TRP
124
35.162
38.547
79.264
1.00
12.85
DIC

ATOM
950
CE2
TRP
124
34.518
38.054
80.422
1.00
12.47
DIC

ATOM
951
CE3
TRP
124
35.587
37.635
78.285
1.00
12.98
DIC

ATOM
952
CD1
TRP
124
34.635
40.282
80.583
1.00
11.72
DIC

ATOM
953
NE1
TRP
124
34.206
39.131
81.210
1.00
12.73
DIC

ATOM
954
CZ2
TRP
124
34.285
36.689
80.627
1.00
13.82
DIC

ATOM
955
CZ3
TRP
124
35.354
36.277
78.491
1.00
14.04
DIC

ATOM
956
CH2
TRP
124
34.709
35.821
79.652
1.00
13.35
DIC

ATOM
957
C
TRP
124
37.628
41.904
77.094
1.00
11.46
DIC

ATOM
958
O
TRP
124
37.992
41.308
76.088
1.00
10.17
DIC

ATOM
959
N
LEU
125
37.558
43.227
77.158
1.00
10.45
DIC

ATOM
960
CA
LEU
125
37.898
44.035
76.000
1.00
11.28
DIC

ATOM
961
CB
LEU
125
36.841
43.844
74.903
1.00
11.69
DIC

ATOM
962
CG
LEU
125
35.439
44.448
75.080
1.00
12.44
DIC

ATOM
963
CD1
LEU
125
34.499
43.821
74.070
1.00
12.81
DIC

ATOM
964
CD2
LEU
125
34.910
44.193
76.465
1.00
13.63
DIC

ATOM
965
C
LEU
125
37.995
45.505
76.366
1.00
11.38
DIC

ATOM
966
O
LEU
125
37.713
45.897
77.500
1.00
11.51
DIC

ATOM
967
N
GLY
126
38.415
46.305
75.397
1.00
10.75
DIC

ATOM
968
CA
GLY
126
38.526
47.735
75.592
1.00
11.81
DIC

ATOM
969
C
GLY
126
37.590
48.359
74.577
1.00
11.37
DIC

ATOM
970
O
GLY
126
37.579
47.939
73.418
1.00
11.54
DIC

ATOM
971
N
ALA
127
36.804
49.345
74.998
1.00
10.41
DIC

ATOM
972
CA
ALA
127
35.860
50.006
74.095
1.00
8.96
DIC

ATOM
973
CB
ALA
127
34.577
49.190
74.008
1.00
8.65
DIC

ATOM
974
C
ALA
127
35.536
51.431
74.535
1.00
9.67
DIC

ATOM
975
O
ALA
127
35.735
51.795
75.701
1.00
7.21
DIC

ATOM
976
N
SER
128
35.039
52.240
73.599
1.00
9.58
DIC

ATOM
977
CA
SER
128
34.675
53.617
73.916
1.00
10.71
DIC

ATOM
978
CB
SER
128
34.895
54.538
72.711
1.00
10.39
DIC

ATOM
979
OG
SER
128
36.250
54.510
72.286
1.00
10.31
DIC

ATOM
980
C
SER
128
33.206
53.644
74.321
1.00
11.60
DIC

ATOM
981
O
SER
128
32.408
52.818
73.857
1.00
10.65
DIC

ATOM
982
N
ILE
129
32.859
54.597
75.179
1.00
11.17
DIC

ATOM
983
CA
ILE
129
31.496
54.744
75.675
1.00
11.89
DIC

ATOM
984
CB
ILE
129
31.484
55.693
76.909
1.00
12.55
DIC

ATOM
985
CG2
ILE
129
30.059
55.997
77.348
1.00
11.82
DIC

ATOM
986
CG1
ILE
129
32.269
55.040
78.049
1.00
13.27
DIC

ATOM
987
CD
ILE
129
32.567
55.968
79.199
1.00
14.30
DIC

ATOM
988
C
ILE
129
30.538
55.257
74.600
1.00
13.23
DIC

ATOM
989
O
ILE
129
30.913
56.068
73.746
1.00
13.13
DIC

ATOM
990
N
ASP
130
29.300
54.771
74.647
1.00
12.89
DIC

ATOM
991
CA
ASP
130
28.280
55.167
73.693
1.00
13.14
DIC

ATOM
992
CB
ASP
130
27.447
53.944
73.284
1.00
12.35
DIC

ATOM
993
CG
ASP
130
26.610
54.195
72.039
1.00
12.78
DIC

ATOM
994
OD1
ASP
130
25.776
55.130
72.033
1.00
14.26
DIC

ATOM
995
OD2
ASP
130
26.784
53.454
71.060
1.00
13.48
DIC

ATOM
996
C
ASP
130
27.379
56.215
74.340
1.00
13.29
DIC

ATOM
997
O
ASP
130
26.483
55.878
75.112
1.00
13.88
DIC

ATOM
998
N
LEU
131
27.626
57.483
74.027
1.00
14.55
DIC

ATOM
999
CA
LEU
131
26.843
58.597
74.574
1.00
14.53
DIC

ATOM
1000
CB
LEU
131
27.401
59.933
74.071
1.00
15.55
DIC

ATOM
1001
CG
LEU
131
28.630
60.539
74.752
1.00
16.42
DIC

ATOM
1002
CD1
LEU
131
29.698
59.495
75.006
1.00
17.97
DIC

ATOM
1003
CD2
LEU
131
29.161
61.654
73.872
1.00
16.87
DIC

ATOM
1004
C
LEU
131
25.364
58.516
74.215
1.00
14.67
DIC

ATOM
1005
O
LEU
131
24.496
58.874
75.016
1.00
14.54
DIC

ATOM
1006
N
PHE
132
25.083
58.059
73.002
1.00
13.83
DIC

ATOM
1007
CA
PHE
132
23.714
57.935
72.528
1.00
14.23
DIC

ATOM
1008
CB
PHE
132
23.722
57.462
71.070
1.00
14.97
DIC

ATOM
1009
CG
PHE
132
22.354
57.288
70.481
1.00
16.38
DIC

ATOM
1010
CD1
PHE
132
21.728
56.044
70.494
1.00
17.39
DIC

ATOM
1011
CD2
PHE
132
21.685
58.368
69.924
1.00
17.06
DIC

ATOM
1012
CE1
PHE
132
20.456
55.877
69.961
1.00
17.85
DIC

ATOM
1013
CE2
PHE
132
20.405
58.215
69.385
1.00
19.05
DIC

ATOM
1014
CZ
PHE
132
19.790
56.962
69.404
1.00
19.20
DIC

ATOM
1015
C
PHE
132
22.896
56.974
73.398
1.00
14.47
DIC

ATOM
1016
O
PHE
132
21.769
57.290
73.793
1.00
14.19
DIC

ATOM
1017
N
VAL
133
23.464
55.807
73.703
1.00
12.67
DIC

ATOM
1018
CA
VAL
133
22.757
54.829
74.523
1.00
13.81
DIC

ATOM
1019
CB
VAL
133
23.396
53.433
74.433
1.00
12.45
DIC

ATOM
1020
CG1
VAL
133
22.658
52.469
75.359
1.00
13.71
DIC

ATOM
1021
CG2
VAL
133
23.330
52.924
73.002
1.00
12.09
DIC

ATOM
1022
C
VAL
133
22.734
55.248
75.983
1.00
14.81
DIC

ATOM
1023
O
VAL
133
21.710
55.125
76.659
1.00
15.65
DIC

ATOM
1024
N
GLU
134
23.864
55.753
76.462
1.00
16.17
DIC

ATOM
1025
CA
GLU
134
23.987
56.184
77.845
1.00
17.03
DIC

ATOM
1026
CB
GLU
134
25.408
56.700
78.089
1.00
17.49
DIC

ATOM
1027
CG
GLU
134
25.763
56.880
79.553
1.00
20.47
DIC

ATOM
1028
CD
GLU
134
25.781
55.575
80.329
1.00
18.73
DIC

ATOM
1029
OE1
GLU
134
25.626
55.635
81.556
1.00
20.44
DIC

ATOM
1030
OE2
GLU
134
25.959
54.496
79.729
1.00
20.43
DIC

ATOM
1031
C
GLU
134
22.955
57.252
78.230
1.00
18.44
DIC

ATOM
1032
O
GLU
134
22.529
57.321
79.378
1.00
18.74
DIC

ATOM
1033
N
ARG
135
22.540
58.082
77.281
1.00
18.60
DIC

ATOM
1034
CA
ARG
135
21.560
59.115
77.594
1.00
20.63
DIC

ATOM
1035
CB
ARG
135
21.897
60.419
76.867
1.00
22.18
DIC

ATOM
1036
CG
ARG
135
21.810
60.353
75.362
1.00
25.33
DIC

ATOM
1037
CD
ARG
135
22.541
61.540
74.759
1.00
28.60
DIC

ATOM
1038
NE
ARG
135
21.996
62.820
75.204
1.00
30.75
DIC

ATOM
1039
CZ
ARG
135
20.972
63.444
74.626
1.00
31.82
DIC

ATOM
1040
NH1
ARG
135
20.547
64.606
75.110
1.00
32.80
DIC

ATOM
1041
NH2
ARG
135
20.379
62.917
73.560
1.00
32.31
DIC

ATOM
1042
C
ARG
135
20.140
58.682
77.261
1.00
20.30
DIC

ATOM
1043
O
ARG
135
19.215
59.488
77.293
1.00
20.01
DIC

ATOM
1044
N
GLN
136
19.975
57.408
76.928
1.00
20.15
DIC

ATOM
1045
CA
GLN
136
18.660
56.864
76.631
1.00
20.32
DIC

ATOM
1046
CB
GLN
136
18.789
55.671
75.688
1.00
20.65
DIC

ATOM
1047
CG
GLN
136
17.480
55.152
75.143
1.00
21.22
DIC

ATOM
1048
CD
GLN
136
17.681
53.987
74.193
1.00
22.55
DIC

ATOM
1049
OE1
GLN
136
18.653
53.953
73.436
1.00
22.60
DIC

ATOM
1050
NE2
GLN
136
16.757
53.031
74.218
1.00
22.18
DIC

ATOM
1051
C
GLN
136
18.143
56.411
77.993
1.00
21.14
DIC

ATOM
1052
O
GLN
136
18.358
55.271
78.397
1.00
19.68
DIC

ATOM
1053
N
GLU
137
17.480
57.326
78.698
1.00
22.64
DIC

ATOM
1054
CA
GLU
137
16.955
57.086
80.045
1.00
24.24
DIC

ATOM
1055
CB
GLU
137
15.856
58.113
80.369
1.00
27.33
DIC

ATOM
1056
CG
GLU
137
15.631
58.389
81.868
1.00
32.13
DIC

ATOM
1057
CD
GLU
137
15.115
57.184
82.658
1.00
34.75
DIC

ATOM
1058
OE1
GLU
137
14.132
56.543
82.217
1.00
36.51
DIC

ATOM
1059
OE2
GLU
137
15.684
56.884
83.735
1.00
35.95
DIC

ATOM
1060
C
GLU
137
16.428
55.688
80.342
1.00
22.27
DIC

ATOM
1061
O
GLU
137
15.508
55.194
79.687
1.00
23.05
DIC

ATOM
1062
N
GLY
138
17.029
55.058
81.346
1.00
21.87
DIC

ATOM
1063
CA
GLY
138
16.604
53.738
81.774
1.00
20.02
DIC

ATOM
1064
C
GLY
138
16.855
52.556
80.859
1.00
19.14
DIC

ATOM
1065
O
GLY
138
16.587
51.426
81.253
1.00
19.29
DIC

ATOM
1066
N
TYR
139
17.371
52.779
79.654
1.00
18.23
DIC

ATOM
1067
CA
TYR
139
17.605
51.643
78.762
1.00
17.46
DIC

ATOM
1068
CB
TYR
139
18.111
52.080
77.389
1.00
15.54
DIC

ATOM
1069
CG
TYR
139
18.398
50.877
76.513
1.00
14.37
DIC

ATOM
1070
CD1
TYR
139
17.358
50.087
76.029
1.00
14.45
DIC

ATOM
1071
CE1
TYR
139
17.604
48.932
75.298
1.00
14.12
DIC

ATOM
1072
CD2
TYR
139
19.708
50.480
76.237
1.00
14.19
DIC

ATOM
1073
CE2
TYR
139
19.969
49.313
75.503
1.00
13.62
DIC

ATOM
1074
CZ
TYR
139
18.910
48.547
75.039
1.00
13.67
DIC

ATOM
1075
OH
TYR
139
19.142
47.398
74.316
1.00
12.91
DIC

ATOM
1076
C
TYR
139
18.621
50.664
79.326
1.00
16.80
DIC

ATOM
1077
O
TYR
139
18.353
49.474
79.442
1.00
18.25
DIC

ATOM
1078
N
LYS
140
19.798
51.183
79.638
1.00
15.97
DIC

ATOM
1079
CA
LYS
140
20.905
50.398
80.166
1.00
16.47
DIC

ATOM
1080
CB
LYS
140
21.957
51.356
80.726
1.00
17.96
DIC

ATOM
1081
CG
LYS
140
23.344
50.799
80.841
1.00
18.12
DIC

ATOM
1082
CD
LYS
140
24.340
51.897
81.191
1.00
17.26
DIC

ATOM
1083
CE
LYS
140
24.014
52.584
82.505
1.00
18.38
DIC

ATOM
1084
NZ
LYS
140
25.094
53.524
82.900
1.00
18.19
DIC

ATOM
1085
C
LYS
140
20.443
49.427
81.244
1.00
17.24
DIC

ATOM
1086
O
LYS
140
20.853
48.264
81.264
1.00
16.57
DIC

ATOM
1087
N
GLN
141
19.579
49.907
82.134
1.00
16.44
DIC

ATOM
1088
CA
GLN
141
19.064
49.086
83.219
1.00
17.66
DIC

ATOM
1089
CB
GLN
141
18.298
49.958
84.220
1.00
17.58
DIC

ATOM
1090
CG
GLN
141
19.177
50.921
85.010
1.00
16.44
DIC

ATOM
1091
CD
GLN
141
19.667
52.100
84.183
1.00
18.00
DIC

ATOM
1092
OE1
GLN
141
19.272
52.274
83.033
1.00
17.29
DIC

ATOM
1093
NE2
GLN
141
20.525
52.920
84.772
1.00
17.45
DIC

ATOM
1094
C
GLN
141
18.176
47.941
82.730
1.00
17.85
DIC

ATOM
1095
O
GLN
141
18.076
46.902
83.384
1.00
18.70
DIC

ATOM
1096
N
LYS
142
17.534
48.130
81.582
1.00
18.33
DIC

ATOM
1097
CA
LYS
142
16.678
47.094
81.007
1.00
18.53
DIC

ATOM
1098
CB
LYS
142
15.989
47.600
79.736
1.00
20.13
DIC

ATOM
1099
CG
LYS
142
14.819
48.553
79.963
1.00
23.26
DIC

ATOM
1100
CD
LYS
142
14.382
49.182
78.639
1.00
24.62
DIC

ATOM
1101
CE
LYS
142
13.112
50.012
78.779
1.00
27.12
DIC

ATOM
1102
NZ
LYS
142
11.922
49.174
79.116
1.00
27.95
DIC

ATOM
1103
C
LYS
142
17.477
45.839
80.662
1.00
17.52
DIC

ATOM
1104
O
LYS
142
16.921
44.737
80.628
1.00
17.09
DIC

ATOM
1105
N
ILE
143
18.771
45.987
80.384
1.00
15.77
DIC

ATOM
1106
CA
ILE
143
19.561
44.802
80.054
1.00
13.94
DIC

ATOM
1107
CB
ILE
143
20.391
44.979
78.754
1.00
13.64
DIC

ATOM
1108
CG2
ILE
143
19.467
45.307
77.584
1.00
13.27
DIC

ATOM
1109
CG1
ILE
143
21.434
46.079
78.919
1.00
13.02
DIC

ATOM
1110
CD
ILE
143
22.390
46.147
77.731
1.00
13.03
DIC

ATOM
1111
C
ILE
143
20.472
44.349
81.193
1.00
13.33
DIC

ATOM
1112
O
ILE
143
21.480
43.679
80.974
1.00
12.63
DIC

ATOM
1113
N
GLY
144
20.099
44.722
82.415
1.00
13.50
DIC

ATOM
1114
CA
GLY
144
20.849
44.304
83.585
1.00
12.47
DIC

ATOM
1115
C
GLY
144
22.073
45.084
84.013
1.00
13.88
DIC

ATOM
1116
O
GLY
144
22.794
44.632
84.903
1.00
12.20
DIC

ATOM
1117
N
MSE
145
22.320
46.242
83.410
1.00
14.02
DIC

ATOM
1118
CA
MSE
145
23.487
47.028
83.789
1.00
15.34
DIC

ATOM
1119
CB
MSE
145
24.054
47.746
82.568
1.00
14.88
DIC

ATOM
1120
CG
MSE
145
24.544
46.810
81.471
1.00
14.27
DIC

ATOM
1121
SE
MSE
145
25.198
47.793
79.939
1.00
16.53
DIC

ATOM
1122
CE
MSE
145
26.784
48.563
80.704
1.00
12.51
DIC

ATOM
1123
C
MSE
145
23.166
48.045
84.882
1.00
16.35
DIC

ATOM
1124
O
MSE
145
22.033
48.516
84.996
1.00
16.93
DIC

ATOM
1125
N
ALA
146
24.168
48.379
85.687
1.00
17.18
DIC

ATOM
1126
CA
ALA
146
23.979
49.357
86.760
1.00
17.93
DIC

ATOM
1127
CB
ALA
146
24.876
49.016
87.947
1.00
19.51
DIC

ATOM
1128
C
ALA
146
24.304
50.753
86.235
1.00
18.51
DIC

ATOM
1129
O
ALA
146
24.880
50.892
85.156
1.00
16.64
DIC

ATOM
1130
N
ASP
147
23.929
51.782
86.995
1.00
18.52
DIC

ATOM
1131
CA
ASP
147
24.181
53.166
86.594
1.00
19.15
DIC

ATOM
1132
CB
ASP
147
23.589
54.143
87.622
1.00
22.16
DIC

ATOM
1133
CG
ASP
147
23.911
55.600
87.299
1.00
24.53
DIC

ATOM
1134
OD1
ASP
147
23.468
56.101
86.245
1.00
27.39
DIC

ATOM
1135
OD2
ASP
147
24.614
56.250
88.096
1.00
26.51
DIC

ATOM
1136
C
ASP
147
25.668
53.456
86.427
1.00
18.18
DIC

ATOM
1137
O
ASP
147
26.062
54.243
85.558
1.00
18.44
DIC

ATOM
1138
N
GLY
148
26.485
52.813
87.258
1.00
15.95
DIC

ATOM
1139
CA
GLY
148
27.920
53.015
87.207
1.00
14.91
DIC

ATOM
1140
C
GLY
148
28.645
52.201
86.152
1.00
14.80
DIC

ATOM
1141
O
GLY
148
29.858
52.324
85.996
1.00
14.63
DIC

ATOM
1142
N
GLU
149
27.912
51.360
85.430
1.00
13.75
DIC

ATOM
1143
CA
GLU
149
28.510
50.548
84.379
1.00
14.04
DIC

ATOM
1144
CB
GLU
149
27.953
49.121
84.424
1.00
13.92
DIC

ATOM
1145
CG
GLU
149
28.202
48.416
85.755
1.00
14.93
DIC

ATOM
1146
CD
GLU
149
27.689
46.989
85.769
1.00
14.83
DIC

ATOM
1147
OE1
GLU
149
26.585
46.749
85.238
1.00
15.36
DIC

ATOM
1148
OE2
GLU
149
28.383
46.109
86.320
1.00
14.29
DIC

ATOM
1149
C
GLU
149
28.150
51.237
83.067
1.00
13.46
DIC

ATOM
1150
O
GLU
149
26.980
51.361
82.716
1.00
13.23
DIC

ATOM
1151
N
TYR
150
29.165
51.695
82.349
1.00
12.32
DIC

ATOM
1152
CA
TYR
150
28.928
52.419
81.116
1.00
12.18
DIC

ATOM
1153
CB
TYR
150
30.023
53.470
80.961
1.00
12.48
DIC

ATOM
1154
CG
TYR
150
30.127
54.320
82.211
1.00
13.07
DIC

ATOM
1155
CD1
TYR
150
31.351
54.526
82.833
1.00
12.79
DIC

ATOM
1156
CE1
TYR
150
31.442
55.235
84.016
1.00
13.05
DIC

ATOM
1157
CD2
TYR
150
28.984
54.860
82.807
1.00
12.92
DIC

ATOM
1158
CE2
TYR
150
29.063
55.577
83.999
1.00
13.33
DIC

ATOM
1159
CZ
TYR
150
30.302
55.756
84.595
1.00
14.14
DIC

ATOM
1160
OH
TYR
150
30.417
56.439
85.775
1.00
13.21
DIC

ATOM
1161
C
TYR
150
28.786
51.562
79.870
1.00
10.46
DIC

ATOM
1162
O
TYR
150
29.604
50.681
79.603
1.00
9.61
DIC

ATOM
1163
N
TYR
151
27.720
51.839
79.126
1.00
9.17
DIC

ATOM
1164
CA
TYR
151
27.381
51.124
77.901
1.00
8.84
DIC

ATOM
1165
CB
TYR
151
25.949
51.469
77.502
1.00
8.39
DIC

ATOM
1166
CG
TYR
151
25.359
50.630
76.391
1.00
9.04
DIC

ATOM
1167
CD1
TYR
151
25.744
50.817
75.065
1.00
8.73
DIC

ATOM
1168
CE1
TYR
151
25.175
50.062
74.039
1.00
8.50
DIC

ATOM
1169
CD2
TYR
151
24.387
49.666
76.668
1.00
8.78
DIC

ATOM
1170
CE2
TYR
151
23.813
48.910
75.649
1.00
8.51
DIC

ATOM
1171
CZ
TYR
151
24.212
49.113
74.339
1.00
8.79
DIC

ATOM
1172
OH
TYR
151
23.650
48.364
73.331
1.00
6.56
DIC

ATOM
1173
C
TYR
151
28.346
51.519
76.797
1.00
7.98
DIC

ATOM
1174
O
TYR
151
28.461
52.697
76.456
1.00
8.75
DIC

ATOM
1175
N
PHE
152
29.048
50.538
76.239
1.00
7.59
DIC

ATOM
1176
CA
PHE
152
30.008
50.839
75.192
1.00
8.73
DIC

ATOM
1177
CB
PHE
152
31.315
50.076
75.426
1.00
9.12
DIC

ATOM
1178
CG
PHE
152
31.165
48.581
75.416
1.00
9.52
DIC

ATOM
1179
CD1
PHE
152
31.025
47.870
76.605
1.00
10.37
DIC

ATOM
1180
CD2
PHE
152
31.206
47.875
74.219
1.00
9.21
DIC

ATOM
1181
CE1
PHE
152
30.933
46.470
76.601
1.00
10.52
DIC

ATOM
1182
CE2
PHE
152
31.115
46.474
74.208
1.00
10.71
DIC

ATOM
1183
CZ
PHE
152
30.980
45.775
75.397
1.00
10.62
DIC

ATOM
1184
C
PHE
152
29.468
50.530
73.810
1.00
9.25
DIC

ATOM
1185
O
PHE
152
28.521
49.753
73.659
1.00
9.63
DIC

ATOM
1186
N
ASN
153
30.060
51.169
72.804
1.00
9.40
DIC

ATOM
1187
CA
ASN
153
29.661
50.955
71.422
1.00
8.94
DIC

ATOM
1188
CB
ASN
153
29.916
52.211
70.590
1.00
10.41
DIC

ATOM
1189
CG
ASN
153
29.541
52.025
69.136
1.00
10.47
DIC

ATOM
1190
OD1
ASN
153
30.337
51.537
68.334
1.00
11.66
DIC

ATOM
1191
ND2
ASN
153
28.312
52.391
68.794
1.00
11.08
DIC

ATOM
1192
C
ASN
153
30.492
49.795
70.910
1.00
8.26
DIC

ATOM
1193
O
ASN
153
31.691
49.724
71.174
1.00
6.77
DIC

ATOM
1194
N
ALA
154
29.856
48.885
70.180
1.00
7.02
DIC

ATOM
1195
CA
ALA
154
30.547
47.702
69.676
1.00
7.92
DIC

ATOM
1196
CB
ALA
154
29.551
46.551
69.529
1.00
6.96
DIC

ATOM
1197
C
ALA
154
31.300
47.902
68.365
1.00
7.01
DIC

ATOM
1198
O
ALA
154
31.819
46.938
67.795
1.00
7.48
DIC

ATOM
1199
N
GLY
155
31.376
49.143
67.901
1.00
6.72
DIC

ATOM
1200
CA
GLY
155
32.053
49.426
66.647
1.00
7.21
DIC

ATOM
1201
C
GLY
155
33.573
49.409
66.635
1.00
7.94
DIC

ATOM
1202
O
GLY
155
34.185
49.242
65.575
1.00
7.30
DIC

ATOM
1203
N
VAL
156
34.183
49.606
67.800
1.00
7.67
DIC

ATOM
1204
CA
VAL
156
35.634
49.604
67.930
1.00
6.73
DIC

ATOM
1205
CB
VAL
156
36.183
51.053
68.035
1.00
8.07
DIC

ATOM
1206
CG1
VAL
156
37.705
51.044
68.190
1.00
8.55
DIC

ATOM
1207
CG2
VAL
156
35.794
51.846
66.784
1.00
6.66
DIC

ATOM
1208
C
VAL
156
35.928
48.834
69.210
1.00
6.86
DIC

ATOM
1209
O
VAL
156
35.639
49.306
70.304
1.00
5.93
DIC

ATOM
1210
N
LEU
157
36.493
47.640
69.066
1.00
5.63
DIC

ATOM
1211
CA
LEU
157
36.789
46.791
70.215
1.00
6.45
DIC

ATOM
1212
CB
LEU
157
35.818
45.607
70.246
1.00
5.76
DIC

ATOM
1213
CG
LEU
157
34.328
45.916
70.075
1.00
5.74
DIC

ATOM
1214
CD1
LEU
157
33.585
44.625
69.840
1.00
4.70
DIC

ATOM
1215
CD2
LEU
157
33.783
46.662
71.291
1.00
3.22
DIC

ATOM
1216
C
LEU
157
38.195
46.231
70.244
1.00
7.54
DIC

ATOM
1217
O
LEU
157
38.614
45.559
69.301
1.00
8.36
DIC

ATOM
1218
N
LEU
158
38.927
46.509
71.320
1.00
8.42
DIC

ATOM
1219
CA
LEU
158
40.264
45.947
71.486
1.00
9.61
DIC

ATOM
1220
CB
LEU
158
41.177
46.886
72.285
1.00
10.49
DIC

ATOM
1221
CG
LEU
158
42.640
46.441
72.402
1.00
10.54
DIC

ATOM
1222
CD1
LEU
158
43.281
46.378
71.022
1.00
11.43
DIC

ATOM
1223
CD2
LEU
158
43.394
47.419
73.282
1.00
12.79
DIC

ATOM
1224
C
LEU
158
39.940
44.695
72.291
1.00
10.50
DIC

ATOM
1225
O
LEU
158
39.581
44.772
73.466
1.00
10.19
DIC

ATOM
1226
N
ILE
159
40.074
43.538
71.656
1.00
11.09
DIC

ATOM
1227
CA
ILE
159
39.703
42.284
72.287
1.00
11.44
DIC

ATOM
1228
CB
ILE
159
38.855
41.459
71.277
1.00
12.05
DIC

ATOM
1229
CG2
ILE
159
38.540
40.069
71.821
1.00
11.71
DIC

ATOM
1230
CG1
ILE
159
37.575
42.247
70.961
1.00
12.04
DIC

ATOM
1231
CD
ILE
159
36.693
41.637
69.916
1.00
13.91
DIC

ATOM
1232
C
ILE
159
40.817
41.422
72.877
1.00
12.11
DIC

ATOM
1233
O
ILE
159
41.846
41.179
72.253
1.00
10.85
DIC

ATOM
1234
N
ASN
160
40.594
40.974
74.108
1.00
12.74
DIC

ATOM
1235
CA
ASN
160
41.542
40.110
74.800
1.00
12.51
DIC

ATOM
1236
CB
ASN
160
41.325
40.243
76.309
1.00
12.70
DIC

ATOM
1237
CG
ASN
160
42.282
39.404
77.119
1.00
12.50
DIC

ATOM
1238
OD1
ASN
160
42.920
38.492
76.600
1.00
12.15
DIC

ATOM
1239
ND2
ASN
160
42.378
39.703
78.405
1.00
10.49
DIC

ATOM
1240
C
ASN
160
41.178
38.701
74.325
1.00
13.36
DIC

ATOM
1241
O
ASN
160
40.512
37.956
75.041
1.00
13.18
DIC

ATOM
1242
N
LEU
161
41.601
38.342
73.112
1.00
14.44
DIC

ATOM
1243
CA
LEU
161
41.266
37.032
72.552
1.00
15.68
DIC

ATOM
1244
CB
LEU
161
41.846
36.856
71.142
1.00
15.57
DIC

ATOM
1245
CG
LEU
161
40.891
37.070
69.962
1.00
17.77
DIC

ATOM
1246
CD1
LEU
161
41.565
36.578
68.692
1.00
16.72
DIC

ATOM
1247
CD2
LEU
161
39.576
36.321
70.180
1.00
16.73
DIC

ATOM
1248
C
LEU
161
41.696
35.858
73.407
1.00
16.42
DIC

ATOM
1249
O
LEU
161
40.977
34.865
73.500
1.00
15.59
DIC

ATOM
1250
N
LYS
162
42.877
35.955
74.007
1.00
17.58
DIC

ATOM
1251
CA
LYS
162
43.365
34.883
74.865
1.00
18.16
DIC

ATOM
1252
CB
LYS
162
44.683
35.297
75.528
1.00
20.45
DIC

ATOM
1253
CG
LYS
162
45.123
34.368
76.643
1.00
22.89
DIC

ATOM
1254
CD
LYS
162
46.599
34.511
76.971
1.00
24.41
DIC

ATOM
1255
CE
LYS
162
47.470
33.764
75.961
1.00
25.88
DIC

ATOM
1256
NZ
LYS
162
48.892
33.703
76.422
1.00
26.93
DIC

ATOM
1257
C
LYS
162
42.303
34.568
75.927
1.00
17.16
DIC

ATOM
1258
O
LYS
162
42.020
33.406
76.210
1.00
16.94
DIC

ATOM
1259
N
LYS
163
41.705
35.608
76.506
1.00
16.20
DIC

ATOM
1260
CA
LYS
163
40.670
35.407
77.514
1.00
13.83
DIC

ATOM
1261
CB
LYS
163
40.291
36.728
78.189
1.00
13.03
DIC

ATOM
1262
CG
LYS
163
39.242
36.563
79.297
1.00
13.52
DIC

ATOM
1263
CD
LYS
163
39.031
37.864
80.064
1.00
13.40
DIC

ATOM
1264
CE
LYS
163
37.998
37.714
81.172
1.00
13.29
DIC

ATOM
1265
NZ
LYS
163
38.407
36.647
82.124
1.00
16.98
DIC

ATOM
1266
C
LYS
163
39.428
34.792
76.877
1.00
13.30
DIC

ATOM
1267
O
LYS
163
38.870
33.826
77.394
1.00
13.39
DIC

ATOM
1268
N
TRP
164
38.995
35.352
75.751
1.00
12.69
DIC

ATOM
1269
CA
TRP
164
37.817
34.832
75.056
1.00
12.44
DIC

ATOM
1270
CB
TRP
164
37.608
35.582
73.743
1.00
11.58
DIC

ATOM
1271
CG
TRP
164
37.001
36.958
73.891
1.00
10.67
DIC

ATOM
1272
CD2
TRP
164
36.032
37.560
73.025
1.00
10.33
DIC

ATOM
1273
CE2
TRP
164
35.796
38.867
73.502
1.00
10.22
DIC

ATOM
1274
CE3
TRP
164
35.341
37.119
71.886
1.00
10.89
DIC

ATOM
1275
CD1
TRP
164
37.304
37.895
74.833
1.00
10.43
DIC

ATOM
1276
NE1
TRP
164
36.584
39.048
74.607
1.00
9.98
DIC

ATOM
1277
CZ2
TRP
164
34.896
39.743
72.880
1.00
10.17
DIC

ATOM
1278
CZ3
TRP
164
34.446
37.989
71.270
1.00
9.91
DIC

ATOM
1279
CH2
TRP
164
34.234
39.286
71.769
1.00
9.87
DIC

ATOM
1280
C
TRP
164
37.923
33.329
74.766
1.00
13.17
DIC

ATOM
1281
O
TRP
164
36.961
32.580
74.959
1.00
10.76
DIC

ATOM
1282
N
ARG
165
39.090
32.882
74.311
1.00
13.97
DIC

ATOM
1283
CA
ARG
165
39.248
31.473
73.984
1.00
15.74
DIC

ATOM
1284
CB
ARG
165
40.576
31.242
73.250
1.00
16.55
DIC

ATOM
1285
CG
ARG
165
40.579
31.829
71.833
1.00
17.08
DIC

ATOM
1286
CD
ARG
165
41.687
31.245
70.956
1.00
16.86
DIC

ATOM
1287
NE
ARG
165
43.006
31.584
71.473
1.00
17.35
DIC

ATOM
1288
CZ
ARG
165
43.679
32.678
71.144
1.00
16.72
DIC

ATOM
1289
NH1
ARG
165
44.865
32.907
71.678
1.00
17.09
DIC

ATOM
1290
NH2
ARG
165
43.177
33.528
70.259
1.00
17.44
DIC

ATOM
1291
C
ARG
165
39.099
30.534
75.180
1.00
16.13
DIC

ATOM
1292
O
ARG
165
38.938
29.332
75.008
1.00
16.33
DIC

ATOM
1293
N
ARG
166
39.124
31.086
76.389
1.00
16.52
DIC

ATOM
1294
CA
ARG
166
38.959
30.282
77.597
1.00
17.40
DIC

ATOM
1295
CB
ARG
166
39.581
30.988
78.803
1.00
18.34
DIC

ATOM
1296
CG
ARG
166
41.089
31.074
78.767
1.00
20.01
DIC

ATOM
1297
CD
ARG
166
41.598
31.993
79.856
1.00
21.20
DIC

ATOM
1298
NE
ARG
166
43.045
32.146
79.773
1.00
23.88
DIC

ATOM
1299
CZ
ARG
166
43.688
33.305
79.868
1.00
24.44
DIC

ATOM
1300
NH1
ARG
166
43.015
34.436
80.051
1.00
24.80
DIC

ATOM
1301
NH2
ARG
166
45.010
33.334
79.770
1.00
24.70
DIC

ATOM
1302
C
ARG
166
37.480
30.033
77.889
1.00
17.20
DIC

ATOM
1303
O
ARG
166
37.145
29.220
78.745
1.00
16.99
DIC

ATOM
1304
N
HIS
167
36.595
30.726
77.177
1.00
16.51
DIC

ATOM
1305
CA
HIS
167
35.164
30.572
77.403
1.00
15.83
DIC

ATOM
1306
CB
HIS
167
34.609
31.848
78.055
1.00
15.92
DIC

ATOM
1307
CG
HIS
167
35.323
32.253
79.311
1.00
16.65
DIC

ATOM
1308
CD2
HIS
167
36.463
32.960
79.499
1.00
16.23
DIC

ATOM
1309
ND1
HIS
167
34.866
31.924
80.570
1.00
15.62
DIC

ATOM
1310
CE1
HIS
167
35.693
32.412
81.478
1.00
16.49
DIC

ATOM
1311
NE2
HIS
167
36.670
33.046
80.854
1.00
15.49
DIC

ATOM
1312
C
HIS
167
34.397
30.288
76.106
1.00
15.86
DIC

ATOM
1313
O
HIS
167
34.953
30.360
75.005
1.00
16.09
DIC

ATOM
1314
N
ASP
168
33.118
29.956
76.248
1.00
14.42
DIC

ATOM
1315
CA
ASP
168
32.261
29.687
75.097
1.00
14.22
DIC

ATOM
1316
CB
ASP
168
31.425
28.416
75.310
1.00
13.99
DIC

ATOM
1317
CG
ASP
168
30.692
27.981
74.049
1.00
13.84
DIC

ATOM
1318
OD1
ASP
168
30.323
26.791
73.944
1.00
14.98
DIC

ATOM
1319
OD2
ASP
168
30.475
28.829
73.159
1.00
12.73
DIC

ATOM
1320
C
ASP
168
31.352
30.896
74.951
1.00
13.64
DIC

ATOM
1321
O
ASP
168
30.215
30.897
75.423
1.00
13.29
DIC

ATOM
1322
N
ILE
169
31.882
31.922
74.292
1.00
12.99
DIC

ATOM
1323
CA
ILE
169
31.187
33.188
74.070
1.00
12.79
DIC

ATOM
1324
CB
ILE
169
32.093
34.169
73.286
1.00
12.63
DIC

ATOM
1325
CG2
ILE
169
31.461
35.565
73.260
1.00
12.96
DIC

ATOM
1326
CG1
ILE
169
33.471
34.242
73.952
1.00
12.18
DIC

ATOM
1327
CD
ILE
169
33.437
34.760
75.384
1.00
12.46
DIC

ATOM
1328
C
ILE
169
29.848
33.051
73.342
1.00
12.16
DIC

ATOM
1329
O
ILE
169
28.882
33.745
73.671
1.00
11.43
DIC

ATOM
1330
N
PHE
170
29.785
32.157
72.361
1.00
12.91
DIC

ATOM
1331
CA
PHE
170
28.545
31.953
71.618
1.00
13.05
DIC

ATOM
1332
CB
PHE
170
28.789
31.044
70.407
1.00
13.59
DIC

ATOM
1333
CG
PHE
170
27.558
30.804
69.569
1.00
13.99
DIC

ATOM
1334
CD1
PHE
170
26.952
29.549
69.536
1.00
15.41
DIC

ATOM
1335
CD2
PHE
170
26.987
31.839
68.838
1.00
14.92
DIC

ATOM
1336
CE1
PHE
170
25.782
29.327
68.779
1.00
16.57
DIC

ATOM
1337
CE2
PHE
170
25.822
31.633
68.081
1.00
15.52
DIC

ATOM
1338
CZ
PHE
170
25.218
30.375
68.052
1.00
15.31
DIC

ATOM
1339
C
PHE
170
27.473
31.350
72.528
1.00
13.66
DIC

ATOM
1340
O
PHE
170
26.303
31.756
72.491
1.00
13.17
DIC

ATOM
1341
N
LYS
171
27.871
30.392
73.358
1.00
13.51
DIC

ATOM
1342
CA
LYS
171
26.927
29.761
74.267
1.00
14.35
DIC

ATOM
1343
CB
LYS
171
27.601
28.601
75.009
1.00
16.69
DIC

ATOM
1344
CG
LYS
171
26.639
27.736
75.820
1.00
19.33
DIC

ATOM
1345
CD
LYS
171
27.224
26.351
76.092
1.00
22.68
DIC

ATOM
1346
CE
LYS
171
27.426
25.569
74.799
1.00
24.24
DIC

ATOM
1347
NZ
LYS
171
28.095
24.259
75.028
1.00
27.40
DIC

ATOM
1348
C
LYS
171
26.422
30.826
75.243
1.00
13.97
DIC

ATOM
1349
O
LYS
171
25.219
30.987
75.429
1.00
13.72
DIC

ATOM
1350
N
MSE
172
27.346
31.565
75.846
1.00
12.85
DIC

ATOM
1351
CA
MSE
172
26.983
32.632
76.770
1.00
13.48
DIC

ATOM
1352
CB
MSE
172
28.248
33.312
77.300
1.00
14.61
DIC

ATOM
1353
CG
MSE
172
29.085
32.439
78.237
1.00
15.80
DIC

ATOM
1354
SE
MSE
172
30.883
33.124
78.407
1.00
17.35
DIC

ATOM
1355
CE
MSE
172
30.480
34.735
79.370
1.00
14.60
DIC

ATOM
1356
C
MSE
172
26.089
33.671
76.076
1.00
13.42
DIC

ATOM
1357
O
MSE
172
25.210
34.261
76.708
1.00
13.11
DIC

ATOM
1358
N
SER
173
26.317
33.890
74.781
1.00
11.96
DIC

ATOM
1359
CA
SER
173
25.529
34.862
74.013
1.00
12.42
DIC

ATOM
1360
CB
SER
173
26.161
35.115
72.641
1.00
12.29
DIC

ATOM
1361
OG
SER
173
27.392
35.813
72.743
1.00
11.94
DIC

ATOM
1362
C
SER
173
24.097
34.376
73.813
1.00
12.80
DIC

ATOM
1363
O
SER
173
23.137
35.135
73.994
1.00
12.03
DIC

ATOM
1364
N
SER
174
23.966
33.109
73.429
1.00
12.50
DIC

ATOM
1365
CA
SER
174
22.663
32.504
73.200
1.00
12.95
DIC

ATOM
1366
CB
SER
174
22.816
31.058
72.726
1.00
12.51
DIC

ATOM
1367
OG
SER
174
23.397
31.000
71.439
1.00
14.05
DIC

ATOM
1368
C
SER
174
21.825
32.531
74.467
1.00
13.04
DIC

ATOM
1369
O
SER
174
20.634
32.843
74.422
1.00
11.55
DIC

ATOM
1370
N
GLU
175
22.444
32.187
75.593
1.00
13.58
DIC

ATOM
1371
CA
GLU
175
21.734
32.178
76.862
1.00
13.73
DIC

ATOM
1372
CB
GLU
175
22.609
31.558
77.957
1.00
15.98
DIC

ATOM
1373
CG
GLU
175
23.177
30.204
77.547
1.00
18.50
DIC

ATOM
1374
CD
GLU
175
23.988
29.525
78.638
1.00
20.33
DIC

ATOM
1375
OE1
GLU
175
24.647
30.230
79.434
1.00
20.34
DIC

ATOM
1376
OE2
GLU
175
23.977
28.272
78.681
1.00
21.97
DIC

ATOM
1377
C
GLU
175
21.332
33.598
77.238
1.00
12.97
DIC

ATOM
1378
O
GLU
175
20.244
33.818
77.762
1.00
12.29
DIC

ATOM
1379
N
TRP
176
22.199
34.568
76.954
1.00
12.77
DIC

ATOM
1380
CA
TRP
176
21.880
35.955
77.276
1.00
13.08
DIC

ATOM
1381
CB
TRP
176
23.105
36.853
77.085
1.00
13.64
DIC

ATOM
1382
CG
TRP
176
22.948
38.199
77.725
1.00
12.77
DIC

ATOM
1383
CD2
TRP
176
22.404
39.376
77.125
1.00
12.50
DIC

ATOM
1384
CE2
TRP
176
22.415
40.390
78.107
1.00
13.44
DIC

ATOM
1385
CE3
TRP
176
21.904
39.674
75.852
1.00
12.57
DIC

ATOM
1386
CD1
TRP
176
23.261
38.537
79.011
1.00
14.02
DIC

ATOM
1387
NE1
TRP
176
22.945
39.849
79.249
1.00
13.70
DIC

ATOM
1388
CZ2
TRP
176
21.942
41.685
77.855
1.00
13.81
DIC

ATOM
1389
CZ3
TRP
176
21.432
40.962
75.601
1.00
11.62
DIC

ATOM
1390
CH2
TRP
176
21.456
41.949
76.598
1.00
13.55
DIC

ATOM
1391
C
TRP
176
20.732
36.450
76.394
1.00
13.25
DIC

ATOM
1392
O
TRP
176
19.836
37.154
76.866
1.00
13.29
DIC

ATOM
1393
N
VAL
177
20.761
36.085
75.114
1.00
13.68
DIC

ATOM
1394
CA
VAL
177
19.708
36.493
74.188
1.00
13.26
DIC

ATOM
1395
CB
VAL
177
20.012
36.021
72.750
1.00
12.93
DIC

ATOM
1396
CG1
VAL
177
18.760
36.146
71.874
1.00
12.53
DIC

ATOM
1397
CG2
VAL
177
21.128
36.862
72.155
1.00
12.01
DIC

ATOM
1398
C
VAL
177
18.378
35.906
74.649
1.00
15.29
DIC

ATOM
1399
O
VAL
177
17.327
36.554
74.580
1.00
14.53
DIC

ATOM
1400
N
GLU
178
18.428
34.676
75.139
1.00
16.30
DIC

ATOM
1401
CA
GLU
178
17.221
34.021
75.607
1.00
19.15
DIC

ATOM
1402
CB
GLU
178
17.537
32.573
76.001
1.00
21.26
DIC

ATOM
1403
CG
GLU
178
16.313
31.704
76.275
1.00
25.37
DIC

ATOM
1404
CD
GLU
178
15.292
31.740
75.144
1.00
26.83
DIC

ATOM
1405
OE1
GLU
178
15.687
31.622
73.960
1.00
28.31
DIC

ATOM
1406
OE2
GLU
178
14.087
31.883
75.445
1.00
28.46
DIC

ATOM
1407
C
GLU
178
16.656
34.792
76.798
1.00
18.93
DIC

ATOM
1408
O
GLU
178
15.442
34.896
76.964
1.00
19.05
DIC

ATOM
1409
N
GLN
179
17.544
35.360
77.605
1.00
18.25
DIC

ATOM
1410
CA
GLN
179
17.141
36.105
78.790
1.00
20.06
DIC

ATOM
1411
CB
GLN
179
18.308
36.134
79.784
1.00
21.74
DIC

ATOM
1412
CG
GLN
179
18.013
36.801
81.119
1.00
25.00
DIC

ATOM
1413
CD
GLN
179
19.274
37.041
81.937
1.00
27.00
DIC

ATOM
1414
OE1
GLN
179
19.221
37.576
83.050
1.00
29.16
DIC

ATOM
1415
NE2
GLN
179
20.416
36.651
81.386
1.00
27.67
DIC

ATOM
1416
C
GLN
179
16.655
37.536
78.538
1.00
19.68
DIC

ATOM
1417
O
GLN
179
15.815
38.044
79.279
1.00
19.99
DIC

ATOM
1418
N
TYR
180
17.178
38.189
77.503
1.00
19.03
DIC

ATOM
1419
CA
TYR
180
16.799
39.570
77.217
1.00
18.49
DIC

ATOM
1420
CB
TYR
180
18.011
40.483
77.409
1.00
17.86
DIC

ATOM
1421
CG
TYR
180
18.475
40.591
78.840
1.00
16.21
DIC

ATOM
1422
CD1
TYR
180
19.408
39.703
79.362
1.00
16.33
DIC

ATOM
1423
CE1
TYR
180
19.840
39.811
80.679
1.00
16.04
DIC

ATOM
1424
CD2
TYR
180
17.979
41.586
79.672
1.00
15.98
DIC

ATOM
1425
CE2
TYR
180
18.400
41.698
80.988
1.00
15.72
DIC

ATOM
1426
CZ
TYR
180
19.330
40.812
81.485
1.00
15.22
DIC

ATOM
1427
OH
TYR
180
19.755
40.931
82.789
1.00
16.65
DIC

ATOM
1428
C
TYR
180
16.215
39.824
75.831
1.00
19.02
DIC

ATOM
1429
O
TYR
180
16.109
40.972
75.409
1.00
18.33
DIC

ATOM
1430
N
LYS
181
15.837
38.760
75.132
1.00
19.32
DIC

ATOM
1431
CA
LYS
181
15.291
38.879
73.785
1.00
20.45
DIC

ATOM
1432
CB
LYS
181
14.848
37.496
73.299
1.00
21.34
DIC

ATOM
1433
CG
LYS
181
14.196
37.475
71.922
1.00
24.95
DIC

ATOM
1434
CD
LYS
181
15.149
37.926
70.818
1.00
26.37
DIC

ATOM
1435
CE
LYS
181
14.466
37.879
69.456
1.00
27.47
DIC

ATOM
1436
NZ
LYS
181
14.072
36.492
69.067
1.00
29.43
DIC

ATOM
1437
C
LYS
181
14.133
39.870
73.619
1.00
20.56
DIC

ATOM
1438
O
LYS
181
14.045
40.560
72.608
1.00
21.00
DIC

ATOM
1439
N
ASP
182
13.253
39.947
74.610
1.00
20.10
DIC

ATOM
1440
CA
ASP
182
12.088
40.823
74.519
1.00
20.96
DIC

ATOM
1441
CB
ASP
182
10.964
40.275
75.402
1.00
21.98
DIC

ATOM
1442
CG
ASP
182
10.374
38.968
74.873
1.00
23.22
DIC

ATOM
1443
OD1
ASP
182
9.574
38.346
75.602
1.00
24.34
DIC

ATOM
1444
OD2
ASP
182
10.691
38.560
73.734
1.00
24.33
DIC

ATOM
1445
C
ASP
182
12.334
42.288
74.881
1.00
20.33
DIC

ATOM
1446
O
ASP
182
11.398
43.086
74.906
1.00
20.87
DIC

ATOM
1447
N
VAL
183
13.580
42.652
75.151
1.00
18.31
DIC

ATOM
1448
CA
VAL
183
13.866
44.023
75.532
1.00
17.11
DIC

ATOM
1449
CB
VAL
183
14.052
44.116
77.064
1.00
17.36
DIC

ATOM
1450
CG1
VAL
183
15.351
43.427
77.482
1.00
15.90
DIC

ATOM
1451
CG2
VAL
183
14.031
45.558
77.501
1.00
18.60
DIC

ATOM
1452
C
VAL
183
15.091
44.619
74.843
1.00
16.46
DIC

ATOM
1453
O
VAL
183
15.213
45.836
74.743
1.00
15.97
DIC

ATOM
1454
N
MSE
184
16.002
43.775
74.370
1.00
15.66
DIC

ATOM
1455
CA
MSE
184
17.195
44.292
73.714
1.00
14.63
DIC

ATOM
1456
CB
MSE
184
18.193
43.153
73.422
1.00
15.84
DIC

ATOM
1457
CG
MSE
184
17.673
41.995
72.601
1.00
15.47
DIC

ATOM
1458
SE
MSE
184
18.875
40.472
72.749
1.00
16.06
DIC

ATOM
1459
CE
MSE
184
20.077
40.875
71.295
1.00
14.11
DIC

ATOM
1460
C
MSE
184
16.816
45.053
72.448
1.00
14.45
DIC

ATOM
1461
O
MSE
184
15.944
44.623
71.683
1.00
13.76
DIC

ATOM
1462
N
GLN
185
17.456
46.203
72.248
1.00
12.74
DIC

ATOM
1463
CA
GLN
185
17.183
47.050
71.094
1.00
11.64
DIC

ATOM
1464
CB
GLN
185
16.728
48.438
71.565
1.00
13.80
DIC

ATOM
1465
CG
GLN
185
15.491
48.436
72.469
1.00
12.21
DIC

ATOM
1466
CD
GLN
185
15.125
49.825
72.981
1.00
13.45
DIC

ATOM
1467
OE1
GLN
185
15.701
50.831
72.565
1.00
12.43
DIC

ATOM
1468
NE2
GLN
185
14.159
49.881
73.888
1.00
12.29
DIC

ATOM
1469
C
GLN
185
18.406
47.211
70.198
1.00
12.26
DIC

ATOM
1470
O
GLN
185
18.299
47.714
69.072
1.00
10.28
DIC

ATOM
1471
N
TYR
186
19.571
46.784
70.680
1.00
10.35
DIC

ATOM
1472
CA
TYR
186
20.773
46.965
69.884
1.00
11.71
DIC

ATOM
1473
CB
TYR
186
21.709
47.965
70.579
1.00
11.81
DIC

ATOM
1474
CG
TYR
186
21.052
49.319
70.763
1.00
13.33
DIC

ATOM
1475
CD1
TYR
186
20.566
49.720
72.007
1.00
13.33
DIC

ATOM
1476
CE1
TYR
186
19.883
50.927
72.160
1.00
13.45
DIC

ATOM
1477
CD2
TYR
186
20.844
50.165
69.669
1.00
14.56
DIC

ATOM
1478
CE2
TYR
186
20.161
51.371
69.809
1.00
14.44
DIC

ATOM
1479
CZ
TYR
186
19.683
51.745
71.059
1.00
14.43
DIC

ATOM
1480
OH
TYR
186
19.010
52.937
71.204
1.00
12.04
DIC

ATOM
1481
C
TYR
186
21.535
45.725
69.441
1.00
10.15
DIC

ATOM
1482
O
TYR
186
22.730
45.791
69.167
1.00
10.75
DIC

ATOM
1483
N
GLN
187
20.829
44.603
69.376
1.00
8.94
DIC

ATOM
1484
CA
GLN
187
21.379
43.349
68.878
1.00
8.88
DIC

ATOM
1485
CB
GLN
187
21.399
43.447
67.342
1.00
9.31
DIC

ATOM
1486
CG
GLN
187
19.987
43.785
66.826
1.00
10.51
DIC

ATOM
1487
CD
GLN
187
19.891
44.176
65.360
1.00
10.67
DIC

ATOM
1488
OE1
GLN
187
18.788
44.374
64.849
1.00
12.93
DIC

ATOM
1489
NE2
GLN
187
21.021
44.303
64.684
1.00
10.73
DIC

ATOM
1490
C
GLN
187
22.726
42.898
69.458
1.00
8.99
DIC

ATOM
1491
O
GLN
187
22.833
42.742
70.671
1.00
9.41
DIC

ATOM
1492
N
ASP
188
23.742
42.675
68.618
1.00
8.46
DIC

ATOM
1493
CA
ASP
188
25.040
42.207
69.112
1.00
9.37
DIC

ATOM
1494
CB
ASP
188
26.017
41.980
67.951
1.00
10.94
DIC

ATOM
1495
CG
ASP
188
26.258
43.231
67.147
1.00
11.67
DIC

ATOM
1496
OD1
ASP
188
25.359
43.619
66.370
1.00
12.99
DIC

ATOM
1497
OD2
ASP
188
27.340
43.832
67.298
1.00
12.63
DIC

ATOM
1498
C
ASP
188
25.692
43.140
70.131
1.00
9.34
DIC

ATOM
1499
O
ASP
188
26.444
42.707
71.006
1.00
8.86
DIC

ATOM
1500
N
GLN
189
25.393
44.422
70.020
1.00
8.62
DIC

ATOM
1501
CA
GLN
189
25.955
45.401
70.928
1.00
9.00
DIC

ATOM
1502
CB
GLN
189
25.620
46.803
70.419
1.00
8.38
DIC

ATOM
1503
CG
GLN
189
26.246
47.941
71.193
1.00
8.88
DIC

ATOM
1504
CD
GLN
189
26.110
49.255
70.445
1.00
9.01
DIC

ATOM
1505
OE1
GLN
189
27.025
49.673
69.730
1.00
10.27
DIC

ATOM
1506
NE2
GLN
189
24.953
49.898
70.583
1.00
7.31
DIC

ATOM
1507
C
GLN
189
25.406
45.165
72.337
1.00
9.05
DIC

ATOM
1508
O
GLN
189
26.139
45.269
73.318
1.00
8.94
DIC

ATOM
1509
N
ASP
190
24.118
44.841
72.438
1.00
9.37
DIC

ATOM
1510
CA
ASP
190
23.527
44.569
73.739
1.00
9.91
DIC

ATOM
1511
CB
ASP
190
22.029
44.301
73.623
1.00
9.65
DIC

ATOM
1512
CG
ASP
190
21.222
45.563
73.412
1.00
10.87
DIC

ATOM
1513
OD1
ASP
190
20.179
45.475
72.740
1.00
8.70
DIC

ATOM
1514
OD2
ASP
190
21.618
46.632
73.928
1.00
10.04
DIC

ATOM
1515
C
ASP
190
24.196
43.346
74.341
1.00
9.18
DIC

ATOM
1516
O
ASP
190
24.581
43.365
75.497
1.00
10.40
DIC

ATOM
1517
N
ILE
191
24.331
42.284
73.554
1.00
9.00
DIC

ATOM
1518
CA
ILE
191
24.951
41.056
74.042
1.00
8.87
DIC

ATOM
1519
CB
ILE
191
25.086
40.023
72.917
1.00
8.34
DIC

ATOM
1520
CG2
ILE
191
25.767
38.761
73.448
1.00
7.88
DIC

ATOM
1521
CG1
ILE
191
23.699
39.689
72.363
1.00
8.24
DIC

ATOM
1522
CD
ILE
191
23.732
38.844
71.104
1.00
7.49
DIC

ATOM
1523
C
ILE
191
26.327
41.283
74.662
1.00
9.65
DIC

ATOM
1524
O
ILE
191
26.589
40.839
75.783
1.00
9.14
DIC

ATOM
1525
N
LEU
192
27.201
41.979
73.936
1.00
9.83
DIC

ATOM
1526
CA
LEU
192
28.550
42.260
74.413
1.00
9.59
DIC

ATOM
1527
CB
LEU
192
29.331
43.055
73.362
1.00
9.02
DIC

ATOM
1528
CG
LEU
192
29.555
42.376
72.012
1.00
8.81
DIC

ATOM
1529
CD1
LEU
192
30.078
43.409
71.009
1.00
7.76
DIC

ATOM
1530
CD2
LEU
192
30.530
41.225
72.167
1.00
9.35
DIC

ATOM
1531
C
LEU
192
28.538
43.030
75.733
1.00
9.85
DIC

ATOM
1532
O
LEU
192
29.276
42.695
76.656
1.00
9.13
DIC

ATOM
1533
N
ASN
193
27.706
44.062
75.823
1.00
9.48
DIC

ATOM
1534
CA
ASN
193
27.612
44.850
77.052
1.00
9.51
DIC

ATOM
1535
CB
ASN
193
26.676
46.045
76.849
1.00
9.70
DIC

ATOM
1536
CG
ASN
193
27.394
47.256
76.290
1.00
10.74
DIC

ATOM
1537
OD1
ASN
193
28.041
47.996
77.033
1.00
8.96
DIC

ATOM
1538
ND2
ASN
193
27.297
47.461
74.972
1.00
10.60
DIC

ATOM
1539
C
ASN
193
27.102
44.011
78.221
1.00
9.96
DIC

ATOM
1540
O
ASN
193
27.620
44.109
79.334
1.00
9.61
DIC

ATOM
1541
N
GLY
194
26.079
43.199
77.963
1.00
10.54
DIC

ATOM
1542
CA
GLY
194
25.513
42.369
79.011
1.00
11.12
DIC

ATOM
1543
C
GLY
194
26.479
41.326
79.532
1.00
11.80
DIC

ATOM
1544
O
GLY
194
26.612
41.139
80.746
1.00
11.37
DIC

ATOM
1545
N
LEU
195
27.162
40.643
78.618
1.00
11.19
DIC

ATOM
1546
CA
LEU
195
28.111
39.605
79.004
1.00
10.80
DIC

ATOM
1547
CB
LEU
195
28.557
38.788
77.785
1.00
7.99
DIC

ATOM
1548
CG
LEU
195
27.589
37.864
77.048
1.00
7.39
DIC

ATOM
1549
CD1
LEU
195
28.334
37.170
75.910
1.00
6.05
DIC

ATOM
1550
CD2
LEU
195
27.021
36.821
78.012
1.00
6.98
DIC

ATOM
1551
C
LEU
195
29.370
40.111
79.702
1.00
11.37
DIC

ATOM
1552
O
LEU
195
29.864
39.464
80.623
1.00
11.30
DIC

ATOM
1553
N
PHE
196
29.889
41.259
79.271
1.00
11.32
DIC

ATOM
1554
CA
PHE
196
31.143
41.763
79.831
1.00
11.00
DIC

ATOM
1555
CB
PHE
196
32.106
42.123
78.690
1.00
10.77
DIC

ATOM
1556
CG
PHE
196
32.297
41.017
77.689
1.00
11.74
DIC

ATOM
1557
CD1
PHE
196
32.353
39.690
78.102
1.00
10.22
DIC

ATOM
1558
CD2
PHE
196
32.445
41.302
76.339
1.00
10.79
DIC

ATOM
1559
CE1
PHE
196
32.560
38.658
77.184
1.00
11.95
DIC

ATOM
1560
CE2
PHE
196
32.649
40.278
75.411
1.00
11.65
DIC

ATOM
1561
CZ
PHE
196
32.708
38.955
75.836
1.00
11.34
DIC

ATOM
1562
C
PHE
196
31.103
42.923
80.812
1.00
11.21
DIC

ATOM
1563
O
PHE
196
32.154
43.356
81.280
1.00
10.49
DIC

ATOM
1564
N
LYS
197
29.912
43.428
81.119
1.00
11.58
DIC

ATOM
1565
CA
LYS
197
29.773
44.544
82.050
1.00
11.43
DIC

ATOM
1566
CB
LYS
197
28.291
44.737
82.417
1.00
11.39
DIC

ATOM
1567
CG
LYS
197
27.594
43.539
83.091
1.00
12.71
DIC

ATOM
1568
CD
LYS
197
26.097
43.828
83.262
1.00
11.95
DIC

ATOM
1569
CE
LYS
197
25.351
42.749
84.053
1.00
12.18
DIC

ATOM
1570
NZ
LYS
197
25.288
41.442
83.336
1.00
10.84
DIC

ATOM
1571
C
LYS
197
30.612
44.304
83.305
1.00
12.30
DIC

ATOM
1572
O
LYS
197
30.632
43.199
83.846
1.00
11.29
DIC

ATOM
1573
N
GLY
198
31.321
45.333
83.758
1.00
12.29
DIC

ATOM
1574
CA
GLY
198
32.153
45.182
84.942
1.00
13.17
DIC

ATOM
1575
C
GLY
198
33.546
44.680
84.614
1.00
13.23
DIC

ATOM
1576
O
GLY
198
34.450
44.733
85.453
1.00
12.63
DIC

ATOM
1577
N
GLY
199
33.718
44.184
83.390
1.00
13.28
DIC

ATOM
1578
CA
GLY
199
35.011
43.688
82.952
1.00
13.74
DIC

ATOM
1579
C
GLY
199
35.387
44.341
81.628
1.00
14.37
DIC

ATOM
1580
O
GLY
199
35.845
43.680
80.696
1.00
13.49
DIC

ATOM
1581
N
VAL
200
35.176
45.651
81.560
1.00
13.59
DIC

ATOM
1582
CA
VAL
200
35.468
46.446
80.374
1.00
14.48
DIC

ATOM
1583
CB
VAL
200
34.172
47.103
79.823
1.00
14.24
DIC

ATOM
1584
CG1
VAL
200
34.506
48.063
78.700
1.00
16.87
DIC

ATOM
1585
CG2
VAL
200
33.206
46.040
79.332
1.00
15.73
DIC

ATOM
1586
C
VAL
200
36.455
47.578
80.678
1.00
14.42
DIC

ATOM
1587
O
VAL
200
36.314
48.282
81.673
1.00
14.37
DIC

ATOM
1588
N
CYS
201
37.451
47.737
79.813
1.00
14.62
DIC

ATOM
1589
CA
CYS
201
38.426
48.814
79.935
1.00
15.36
DIC

ATOM
1590
CB
CYS
201
39.797
48.346
79.445
1.00
17.87
DIC

ATOM
1591
SG
CYS
201
41.042
49.652
79.343
1.00
24.36
DIC

ATOM
1592
C
CYS
201
37.877
49.890
79.005
1.00
14.95
DIC

ATOM
1593
O
CYS
201
37.561
49.599
77.856
1.00
14.31
DIC

ATOM
1594
N
TYR
202
37.729
51.122
79.479
1.00
14.76
DIC

ATOM
1595
CA
TYR
202
37.184
52.146
78.598
1.00
14.81
DIC

ATOM
1596
CB
TYR
202
36.228
53.076
79.346
1.00
16.13
DIC

ATOM
1597
CG
TYR
202
35.108
52.377
80.083
1.00
16.70
DIC

ATOM
1598
CD1
TYR
202
35.199
52.148
81.455
1.00
16.70
DIC

ATOM
1599
CE1
TYR
202
34.166
51.540
82.156
1.00
17.89
DIC

ATOM
1600
CD2
TYR
202
33.948
51.967
79.418
1.00
17.16
DIC

ATOM
1601
CE2
TYR
202
32.900
51.347
80.113
1.00
17.82
DIC

ATOM
1602
CZ
TYR
202
33.020
51.143
81.486
1.00
18.36
DIC

ATOM
1603
OH
TYR
202
31.997
50.566
82.208
1.00
18.52
DIC

ATOM
1604
C
TYR
202
38.264
52.974
77.923
1.00
14.97
DIC

ATOM
1605
O
TYR
202
39.193
53.447
78.571
1.00
15.35
DIC

ATOM
1606
N
ALA
203
38.128
53.132
76.609
1.00
13.97
DIC

ATOM
1607
CA
ALA
203
39.068
53.902
75.801
1.00
13.45
DIC

ATOM
1608
CB
ALA
203
39.284
53.210
74.463
1.00
14.46
DIC

ATOM
1609
C
ALA
203
38.490
55.293
75.579
1.00
12.66
DIC

ATOM
1610
O
ALA
203
37.290
55.495
75.748
1.00
12.27
DIC

ATOM
1611
N
ASN
204
39.331
56.252
75.201
1.00
11.38
DIC

ATOM
1612
CA
ASN
204
38.856
57.612
74.964
1.00
10.72
DIC

ATOM
1613
CB
ASN
204
40.036
58.556
74.754
1.00
11.13
DIC

ATOM
1614
CG
ASN
204
39.620
59.996
74.762
1.00
10.71
DIC

ATOM
1615
OD1
ASN
204
39.380
60.578
75.827
1.00
12.74
DIC

ATOM
1616
ND2
ASN
204
39.503
60.584
73.578
1.00
10.78
DIC

ATOM
1617
C
ASN
204
37.945
57.645
73.734
1.00
10.83
DIC

ATOM
1618
O
ASN
204
38.100
56.833
72.815
1.00
9.54
DIC

ATOM
1619
N
SER
205
37.006
58.587
73.701
1.00
9.57
DIC

ATOM
1620
CA
SER
205
36.088
58.668
72.569
1.00
10.79
DIC

ATOM
1621
CB
SER
205
34.931
59.621
72.891
1.00
10.23
DIC

ATOM
1622
OG
SER
205
34.046
59.008
73.826
1.00
7.16
DIC

ATOM
1623
C
SER
205
36.740
59.052
71.251
1.00
10.81
DIC

ATOM
1624
O
SER
205
36.094
59.018
70.197
1.00
11.42
DIC

ATOM
1625
N
ARG
206
38.022
59.400
71.293
1.00
10.42
DIC

ATOM
1626
CA
ARG
206
38.728
59.759
70.064
1.00
10.38
DIC

ATOM
1627
CB
ARG
206
40.122
60.324
70.392
1.00
10.54
DIC

ATOM
1628
CG
ARG
206
41.103
59.329
70.992
1.00
11.01
DIC

ATOM
1629
CD
ARG
206
42.438
60.012
71.352
1.00
10.35
DIC

ATOM
1630
NE
ARG
206
42.972
60.735
70.200
1.00
11.14
DIC

ATOM
1631
CZ
ARG
206
44.020
60.350
69.477
1.00
9.85
DIC

ATOM
1632
NH1
ARG
206
44.684
59.240
69.783
1.00
9.03
DIC

ATOM
1633
NH2
ARG
206
44.389
61.069
68.426
1.00
7.77
DIC

ATOM
1634
C
ARG
206
38.854
58.508
69.188
1.00
9.72
DIC

ATOM
1635
O
ARG
206
39.059
58.593
67.973
1.00
8.91
DIC

ATOM
1636
N
PHE
207
38.719
57.341
69.812
1.00
9.74
DIC

ATOM
1637
CA
PHE
207
38.834
56.079
69.090
1.00
10.15
DIC

ATOM
1638
CB
PHE
207
39.583
55.053
69.947
1.00
10.78
DIC

ATOM
1639
CG
PHE
207
41.017
55.423
70.194
1.00
10.31
DIC

ATOM
1640
CD1
PHE
207
41.452
55.792
71.465
1.00
10.66
DIC

ATOM
1641
CD2
PHE
207
41.923
55.472
69.137
1.00
10.73
DIC

ATOM
1642
CE1
PHE
207
42.771
56.215
71.674
1.00
10.88
DIC

ATOM
1643
CE2
PHE
207
43.234
55.888
69.331
1.00
10.86
DIC

ATOM
1644
CZ
PHE
207
43.661
56.263
70.605
1.00
11.25
DIC

ATOM
1645
C
PHE
207
37.494
55.518
68.624
1.00
9.68
DIC

ATOM
1646
O
PHE
207
37.411
54.387
68.144
1.00
10.10
DIC

ATOM
1647
N
ASN
208
36.445
56.315
68.783
1.00
8.88
DIC

ATOM
1648
CA
ASN
208
35.114
55.936
68.335
1.00
9.98
DIC

ATOM
1649
CB
ASN
208
34.513
54.832
69.205
1.00
8.57
DIC

ATOM
1650
CG
ASN
208
33.371
54.116
68.507
1.00
7.87
DIC

ATOM
1651
OD1
ASN
208
32.827
54.625
67.530
1.00
7.69
DIC

ATOM
1652
ND2
ASN
208
33.002
52.939
69.000
1.00
6.25
DIC

ATOM
1653
C
ASN
208
34.253
57.188
68.397
1.00
10.42
DIC

ATOM
1654
O
ASN
208
33.368
57.316
69.240
1.00
11.59
DIC

ATOM
1655
N
PHE
209
34.532
58.109
67.482
1.00
10.12
DIC

ATOM
1656
CA
PHE
209
33.841
59.385
67.405
1.00
10.68
DIC

ATOM
1657
CB
PHE
209
34.788
60.421
66.784
1.00
10.56
DIC

ATOM
1658
CG
PHE
209
34.392
61.853
67.036
1.00
10.98
DIC

ATOM
1659
CD1
PHE
209
34.475
62.401
68.311
1.00
12.28
DIC

ATOM
1660
CD2
PHE
209
33.969
62.662
65.990
1.00
12.06
DIC

ATOM
1661
CE1
PHE
209
34.141
63.742
68.545
1.00
12.45
DIC

ATOM
1662
CE2
PHE
209
33.633
63.996
66.206
1.00
11.37
DIC

ATOM
1663
CZ
PHE
209
33.720
64.540
67.488
1.00
12.90
DIC

ATOM
1664
C
PHE
209
32.596
59.212
66.540
1.00
10.70
DIC

ATOM
1665
O
PHE
209
32.687
59.137
65.323
1.00
10.09
DIC

ATOM
1666
N
MSE
210
31.433
59.156
67.174
1.00
11.63
DIC

ATOM
1667
CA
MSE
210
30.178
58.963
66.446
1.00
12.51
DIC

ATOM
1668
CB
MSE
210
29.380
57.850
67.136
1.00
13.04
DIC

ATOM
1669
CG
MSE
210
30.140
56.526
67.190
1.00
12.66
DIC

ATOM
1670
SE
MSE
210
29.418
55.246
68.442
1.00
12.85
DIC

ATOM
1671
CE
MSE
210
30.266
55.875
70.045
1.00
11.55
DIC

ATOM
1672
C
MSE
210
29.364
60.253
66.363
1.00
12.05
DIC

ATOM
1673
O
MSE
210
29.735
61.265
66.958
1.00
12.49
DIC

ATOM
1674
N
PRO
211
28.245
60.240
65.613
1.00
12.41
DIC

ATOM
1675
CD
PRO
211
27.699
59.141
64.800
1.00
11.47
DIC

ATOM
1676
CA
PRO
211
27.408
61.439
65.482
1.00
11.06
DIC

ATOM
1677
CB
PRO
211
26.163
60.907
64.784
1.00
11.44
DIC

ATOM
1678
CG
PRO
211
26.732
59.865
63.882
1.00
11.64
DIC

ATOM
1679
C
PRO
211
27.074
62.121
66.817
1.00
11.44
DIC

ATOM
1680
O
PRO
211
27.073
63.355
66.915
1.00
11.07
DIC

ATOM
1681
N
THR
212
26.792
61.328
67.844
1.00
9.80
DIC

ATOM
1682
CA
THR
212
26.457
61.907
69.140
1.00
10.60
DIC

ATOM
1683
CB
THR
212
25.852
60.838
70.097
1.00
10.93
DIC

ATOM
1684
OG1
THR
212
24.707
60.240
69.476
1.00
10.74
DIC

ATOM
1685
CG2
THR
212
25.379
61.488
71.403
1.00
11.50
DIC

ATOM
1686
C
THR
212
27.656
62.609
69.798
1.00
11.02
DIC

ATOM
1687
O
THR
212
27.480
63.613
70.499
1.00
10.65
DIC

ATOM
1688
N
ASN
213
28.869
62.100
69.574
1.00
10.18
DIC

ATOM
1689
CA
ASN
213
30.064
62.725
70.148
1.00
10.69
DIC

ATOM
1690
CB
ASN
213
31.316
61.878
69.884
1.00
9.50
DIC

ATOM
1691
CG
ASN
213
31.212
60.462
70.459
1.00
8.75
DIC

ATOM
1692
OD1
ASN
213
31.624
60.196
71.595
1.00
9.99
DIC

ATOM
1693
ND2
ASN
213
30.651
59.556
69.677
1.00
5.77
DIC

ATOM
1694
C
ASN
213
30.229
64.083
69.482
1.00
12.35
DIC

ATOM
1695
O
ASN
213
30.591
65.068
70.130
1.00
12.36
DIC

ATOM
1696
N
TYR
214
29.961
64.128
68.180
1.00
12.87
DIC

ATOM
1697
CA
TYR
214
30.075
65.365
67.429
1.00
15.87
DIC

ATOM
1698
CB
TYR
214
29.837
65.117
65.940
1.00
17.04
DIC

ATOM
1699
CG
TYR
214
29.964
66.370
65.106
1.00
19.24
DIC

ATOM
1700
CD1
TYR
214
31.212
66.888
64.777
1.00
19.84
DIC

ATOM
1701
CE1
TYR
214
31.335
68.067
64.043
1.00
21.17
DIC

ATOM
1702
CD2
TYR
214
28.834
67.062
64.683
1.00
20.61
DIC

ATOM
1703
CE2
TYR
214
28.943
68.243
63.954
1.00
22.48
DIC

ATOM
1704
CZ
TYR
214
30.196
68.740
63.637
1.00
22.15
DIC

ATOM
1705
OH
TYR
214
30.304
69.912
62.914
1.00
23.53
DIC

ATOM
1706
C
TYR
214
29.045
66.363
67.939
1.00
16.93
DIC

ATOM
1707
O
TYR
214
29.375
67.506
68.254
1.00
16.76
DIC

ATOM
1708
N
ALA
215
27.792
65.929
68.011
1.00
18.68
DIC

ATOM
1709
CA
ALA
215
26.725
66.800
68.489
1.00
20.37
DIC

ATOM
1710
CB
ALA
215
25.399
66.039
68.505
1.00
20.09
DIC

ATOM
1711
C
ALA
215
27.064
67.326
69.888
1.00
22.19
DIC

ATOM
1712
O
ALA
215
26.742
68.465
70.229
1.00
22.00
DIC

ATOM
1713
N
ALA
216
27.734
66.501
70.686
1.00
23.55
DIC

ATOM
1714
CA
ALA
216
28.111
66.894
72.040
1.00
26.87
DIC

ATOM
1715
CB
ALA
216
28.597
65.676
72.822
1.00
26.18
DIC

ATOM
1716
C
ALA
216
29.176
67.995
72.060
1.00
29.18
DIC

ATOM
1717
O
ALA
216
29.416
68.606
73.097
1.00
29.39
DIC

ATOM
1718
N
MSE
217
29.814
68.244
70.919
1.00
31.87
DIC

ATOM
1719
CA
MSE
217
30.840
69.284
70.822
1.00
34.52
DIC

ATOM
1720
CB
MSE
217
31.525
69.245
69.453
1.00
37.00
DIC

ATOM
1721
CG
MSE
217
32.334
67.995
69.149
1.00
40.08
DIC

ATOM
1722
SE
MSE
217
33.910
67.778
70.249
1.00
46.50
DIC

ATOM
1723
CE
MSE
217
34.937
69.288
69.631
1.00
45.06
DIC

ATOM
1724
C
MSE
217
30.203
70.658
71.002
1.00
35.07
DIC

ATOM
1725
OT1
MSE
217
30.688
71.459
71.837
1.00
15.87
DIC

ATOM
1726
OT2
MSE
217
29.223
70.927
70.278
1.00
15.87
DIC

ATOM
1727
CB
PRO
222
24.458
67.558
78.759
1.00
28.83
DIC

ATOM
1728
CG
PRO
222
25.198
67.311
77.451
1.00
28.89
DIC

ATOM
1729
C
PRO
222
26.376
67.968
80.306
1.00
28.22
DIC

ATOM
1730
O
PRO
222
27.322
68.622
80.771
1.00
29.45
DIC

ATOM
1731
N
PRO
222
25.993
69.355
78.294
1.00
28.60
DIC

ATOM
1732
CD
PRO
222
25.675
68.707
77.009
1.00
29.20
DIC

ATOM
1733
CA
PRO
222
25.342
68.618
79.398
1.00
28.68
DIC

ATOM
1734
N
ALA
223
26.184
66.671
80.525
1.00
28.20
DIC

ATOM
1735
CA
ALA
223
27.038
65.838
81.366
1.00
27.95
DIC

ATOM
1736
CB
ALA
223
27.638
66.659
82.509
1.00
27.92
DIC

ATOM
1737
C
ALA
223
26.116
64.764
81.925
1.00
27.33
DIC

ATOM
1738
O
ALA
223
25.370
65.009
82.871
1.00
27.98
DIC

ATOM
1739
N
THR
224
26.158
63.578
81.335
1.00
27.53
DIC

ATOM
1740
CA
THR
224
25.294
62.494
81.787
1.00
27.74
DIC

ATOM
1741
CB
THR
224
25.194
61.402
80.692
1.00
27.45
DIC

ATOM
1742
OG1
THR
224
25.090
60.106
81.294
1.00
28.28
DIC

ATOM
1743
CG2
THR
224
26.408
61.470
79.761
1.00
29.04
DIC

ATOM
1744
C
THR
224
25.700
61.883
83.136
1.00
27.43
DIC

ATOM
1745
O
THR
224
24.856
61.344
83.856
1.00
28.04
DIC

ATOM
1746
N
HIS
225
26.981
61.983
83.480
1.00
26.82
DIC

ATOM
1747
CA
HIS
225
27.491
61.455
84.746
1.00
25.60
DIC

ATOM
1748
CB
HIS
225
28.100
60.070
84.541
1.00
25.60
DIC

ATOM
1749
CG
HIS
225
27.095
59.000
84.263
1.00
25.36
DIC

ATOM
1750
CD2
HIS
225
26.818
58.309
83.132
1.00
24.64
DIC

ATOM
1751
ND1
HIS
225
26.231
58.525
85.225
1.00
25.09
DIC

ATOM
1752
CE1
HIS
225
25.466
57.585
84.700
1.00
24.96
DIC

ATOM
1753
NE2
HIS
225
25.801
57.435
83.431
1.00
25.41
DIC

ATOM
1754
C
HIS
225
28.565
62.391
85.289
1.00
25.02
DIC

ATOM
1755
O
HIS
225
29.326
62.967
84.516
1.00
25.07
DIC

ATOM
1756
N
THR
226
28.634
62.535
86.613
1.00
24.57
DIC

ATOM
1757
CA
THR
226
29.633
63.410
87.231
1.00
23.66
DIC

ATOM
1758
CB
THR
226
29.152
63.957
88.600
1.00
23.68
DIC

ATOM
1759
OG1
THR
226
28.822
62.867
89.470
1.00
23.32
DIC

ATOM
1760
CG2
THR
226
27.930
64.841
88.419
1.00
24.26
DIC

ATOM
1761
C
THR
226
30.958
62.676
87.430
1.00
22.94
DIC

ATOM
1762
O
THR
226
32.015
63.300
87.558
1.00
22.50
DIC

ATOM
1763
N
ASP
227
30.889
61.348
87.454
1.00
22.21
DIC

ATOM
1764
CA
ASP
227
32.071
60.509
87.616
1.00
21.20
DIC

ATOM
1765
CB
ASP
227
31.749
59.079
87.179
1.00
22.48
DIC

ATOM
1766
CG
ASP
227
32.969
58.177
87.182
1.00
22.78
DIC

ATOM
1767
OD1
ASP
227
32.906
57.089
86.574
1.00
23.40
DIC

ATOM
1768
OD2
ASP
227
33.988
58.551
87.795
1.00
23.59
DIC

ATOM
1769
C
ASP
227
33.226
61.044
86.767
1.00
21.18
DIC

ATOM
1770
O
ASP
227
33.110
61.149
85.551
1.00
20.24
DIC

ATOM
1771
N
PRO
228
34.358
61.381
87.401
1.00
20.52
DIC

ATOM
1772
CD
PRO
228
34.630
61.341
88.848
1.00
20.97
DIC

ATOM
1773
CA
PRO
228
35.514
61.901
86.662
1.00
19.86
DIC

ATOM
1774
CB
PRO
228
36.526
62.205
87.768
1.00
21.04
DIC

ATOM
1775
CG
PRO
228
36.130
61.267
88.878
1.00
21.72
DIC

ATOM
1776
C
PRO
228
36.061
60.959
85.589
1.00
19.43
DIC

ATOM
1777
O
PRO
228
36.535
61.411
84.548
1.00
18.48
DIC

ATOM
1778
N
LEU
229
35.996
59.653
85.827
1.00
18.78
DIC

ATOM
1779
CA
LEU
229
36.489
58.703
84.832
1.00
18.33
DIC

ATOM
1780
CB
LEU
229
36.450
57.279
85.382
1.00
18.37
DIC

ATOM
1781
CG
LEU
229
36.958
56.164
84.464
1.00
19.20
DIC

ATOM
1782
CD1
LEU
229
37.498
55.030
85.319
1.00
19.93
DIC

ATOM
1783
CD2
LEU
229
35.842
55.677
83.540
1.00
19.78
DIC

ATOM
1784
C
LEU
229
35.618
58.800
83.588
1.00
17.34
DIC

ATOM
1785
O
LEU
229
36.119
58.932
82.467
1.00
17.32
DIC

ATOM
1786
N
TYR
230
34.308
58.742
83.802
1.00
17.15
DIC

ATOM
1787
CA
TYR
230
33.335
58.832
82.724
1.00
15.74
DIC

ATOM
1788
CB
TYR
230
31.919
58.923
83.292
1.00
16.08
DIC

ATOM
1789
CG
TYR
230
30.850
58.982
82.225
1.00
14.76
DIC

ATOM
1790
CD1
TYR
230
30.422
57.827
81.580
1.00
14.83
DIC

ATOM
1791
CE1
TYR
230
29.469
57.877
80.569
1.00
14.30
DIC

ATOM
1792
CD2
TYR
230
30.296
60.199
81.835
1.00
14.34
DIC

ATOM
1793
CE2
TYR
230
29.345
60.261
80.827
1.00
15.23
DIC

ATOM
1794
CZ
TYR
230
28.935
59.093
80.196
1.00
14.70
DIC

ATOM
1795
OH
TYR
230
27.993
59.146
79.190
1.00
14.53
DIC

ATOM
1796
C
TYR
230
33.601
60.075
81.892
1.00
16.16
DIC

ATOM
1797
O
TYR
230
33.603
60.027
80.665
1.00
15.11
DIC

ATOM
1798
N
ARG
231
33.809
61.195
82.574
1.00
16.82
DIC

ATOM
1799
CA
ARG
231
34.068
62.460
81.896
1.00
17.72
DIC

ATOM
1800
CB
ARG
231
34.045
63.606
82.915
1.00
20.64
DIC

ATOM
1801
CG
ARG
231
32.640
63.909
83.459
1.00
24.03
DIC

ATOM
1802
CD
ARG
231
32.702
64.690
84.769
1.00
27.73
DIC

ATOM
1803
NE
ARG
231
33.599
65.839
84.672
1.00
31.57
DIC

ATOM
1804
CZ
ARG
231
33.335
66.937
83.971
1.00
32.63
DIC

ATOM
1805
NH1
ARG
231
34.216
67.930
83.933
1.00
33.24
DIC

ATOM
1806
NH2
ARG
231
32.182
67.048
83.321
1.00
33.69
DIC

ATOM
1807
C
ARG
231
35.394
62.429
81.143
1.00
17.46
DIC

ATOM
1808
O
ARG
231
35.499
62.956
80.036
1.00
16.04
DIC

ATOM
1809
N
ASP
232
36.402
61.798
81.736
1.00
16.62
DIC

ATOM
1810
CA
ASP
232
37.708
61.710
81.097
1.00
17.02
DIC

ATOM
1811
CB
ASP
232
38.698
61.039
82.055
1.00
16.63
DIC

ATOM
1812
CG
ASP
232
40.058
60.792
81.425
1.00
18.06
DIC

ATOM
1813
OD1
ASP
232
40.216
59.786
80.698
1.00
18.50
DIC

ATOM
1814
OD2
ASP
232
40.976
61.602
81.662
1.00
17.41
DIC

ATOM
1815
C
ASP
232
37.625
60.939
79.771
1.00
16.91
DIC

ATOM
1816
O
ASP
232
38.189
61.362
78.755
1.00
16.81
DIC

ATOM
1817
N
ARG
233
36.897
59.825
79.781
1.00
16.06
DIC

ATOM
1818
CA
ARG
233
36.748
58.985
78.598
1.00
14.55
DIC

ATOM
1819
CB
ARG
233
36.210
57.605
78.993
1.00
14.82
DIC

ATOM
1820
CG
ARG
233
37.033
56.881
80.036
1.00
13.79
DIC

ATOM
1821
CD
ARG
233
38.393
56.443
79.515
1.00
13.23
DIC

ATOM
1822
NE
ARG
233
39.008
55.517
80.460
1.00
13.51
DIC

ATOM
1823
CZ
ARG
233
39.560
55.875
81.618
1.00
14.87
DIC

ATOM
1824
NH1
ARG
233
39.596
57.151
81.982
1.00
13.99
DIC

ATOM
1825
NH2
ARG
233
40.042
54.947
82.435
1.00
13.15
DIC

ATOM
1826
C
ARG
233
35.830
59.572
77.533
1.00
14.38
DIC

ATOM
1827
O
ARG
233
36.076
59.396
76.341
1.00
14.52
DIC

ATOM
1828
N
THR
234
34.774
60.262
77.955
1.00
13.26
DIC

ATOM
1829
CA
THR
234
33.830
60.831
77.000
1.00
12.89
DIC

ATOM
1830
CB
THR
234
32.419
60.981
77.622
1.00
11.52
DIC

ATOM
1831
OG1
THR
234
32.512
61.637
78.893
1.00
9.01
DIC

ATOM
1832
CG2
THR
234
31.782
59.605
77.807
1.00
10.76
DIC

ATOM
1833
C
THR
234
34.283
62.153
76.399
1.00
13.61
DIC

ATOM
1834
O
THR
234
33.754
62.577
75.384
1.00
13.22
DIC

ATOM
1835
N
ASN
235
35.258
62.802
77.028
1.00
14.53
DIC

ATOM
1836
CA
ASN
235
35.802
64.048
76.501
1.00
15.83
DIC

ATOM
1837
CB
ASN
235
36.519
64.854
77.590
1.00
18.71
DIC

ATOM
1838
CG
ASN
235
37.384
65.976
77.009
1.00
20.95
DIC

ATOM
1839
OD1
ASN
235
36.880
67.030
76.616
1.00
22.71
DIC

ATOM
1840
ND2
ASN
235
38.693
65.739
76.935
1.00
23.01
DIC

ATOM
1841
C
ASN
235
36.822
63.618
75.457
1.00
15.52
DIC

ATOM
1842
O
ASN
235
37.901
63.125
75.794
1.00
13.95
DIC

ATOM
1843
N
THR
236
36.485
63.795
74.188
1.00
14.36
DIC

ATOM
1844
CA
THR
236
37.396
63.397
73.135
1.00
14.17
DIC

ATOM
1845
CB
THR
236
36.711
63.494
71.754
1.00
14.16
DIC

ATOM
1846
OG1
THR
236
35.656
62.523
71.690
1.00
12.60
DIC

ATOM
1847
CG2
THR
236
37.716
63.234
70.622
1.00
13.57
DIC

ATOM
1848
C
THR
236
38.667
64.228
73.142
1.00
14.15
DIC

ATOM
1849
O
THR
236
38.619
65.460
73.213
1.00
15.30
DIC

ATOM
1850
N
VAL
237
39.808
63.546
73.105
1.00
13.96
DIC

ATOM
1851
CA
VAL
237
41.094
64.227
73.070
1.00
14.29
DIC

ATOM
1852
CB
VAL
237
42.190
63.454
73.866
1.00
14.32
DIC

ATOM
1853
CG1
VAL
237
43.530
64.173
73.749
1.00
14.22
DIC

ATOM
1854
CG2
VAL
237
41.794
63.349
75.335
1.00
13.45
DIC

ATOM
1855
C
VAL
237
41.471
64.268
71.594
1.00
14.08
DIC

ATOM
1856
O
VAL
237
41.763
63.231
70.996
1.00
13.74
DIC

ATOM
1857
N
MSE
238
41.423
65.461
71.004
1.00
14.13
DIC

ATOM
1858
CA
MSE
238
41.753
65.636
69.593
1.00
14.57
DIC

ATOM
1859
CB
MSE
238
41.525
67.095
69.170
1.00
15.84
DIC

ATOM
1860
CG
MSE
238
40.078
67.574
69.271
1.00
18.43
DIC

ATOM
1861
SE
MSE
238
38.879
66.542
68.173
1.00
23.28
DIC

ATOM
1862
CE
MSE
238
37.208
66.992
69.030
1.00
22.22
DIC

ATOM
1863
C
MSE
238
43.205
65.251
69.313
1.00
13.92
DIC

ATOM
1864
O
MSE
238
44.050
65.297
70.208
1.00
13.64
DIC

ATOM
1865
N
PRO
239
43.508
64.845
68.066
1.00
13.35
DIC

ATOM
1866
CD
PRO
239
44.889
64.645
67.591
1.00
14.11
DIC

ATOM
1867
CA
PRO
239
42.566
64.743
66.949
1.00
13.23
DIC

ATOM
1868
CB
PRO
239
43.477
64.777
65.728
1.00
14.00
DIC

ATOM
1869
CG
PRO
239
44.675
64.036
66.220
1.00
14.44
DIC

ATOM
1870
C
PRO
239
41.761
63.452
67.009
1.00
13.04
DIC

ATOM
1871
O
PRO
239
42.125
62.512
67.721
1.00
12.63
DIC

ATOM
1872
N
VAL
240
40.668
63.417
66.253
1.00
12.39
DIC

ATOM
1873
CA
VAL
240
39.824
62.240
66.199
1.00
11.18
DIC

ATOM
1874
CB
VAL
240
38.567
62.506
65.352
1.00
11.67
DIC

ATOM
1875
CG1
VAL
240
37.728
61.238
65.244
1.00
11.57
DIC

ATOM
1876
CG2
VAL
240
37.755
63.641
65.980
1.00
11.98
DIC

ATOM
1877
C
VAL
240
40.660
61.150
65.550
1.00
10.08
DIC

ATOM
1878
O
VAL
240
41.329
61.403
64.553
1.00
9.26
DIC

ATOM
1879
N
ALA
241
40.645
59.951
66.125
1.00
8.61
DIC

ATOM
1880
CA
ALA
241
41.423
58.834
65.582
1.00
8.11
DIC

ATOM
1881
CB
ALA
241
42.072
58.040
66.716
1.00
8.10
DIC

ATOM
1882
C
ALA
241
40.545
57.916
64.739
1.00
7.76
DIC

ATOM
1883
O
ALA
241
41.000
57.341
63.749
1.00
7.78
DIC

ATOM
1884
N
VAL
242
39.282
57.788
65.133
1.00
7.63
DIC

ATOM
1885
CA
VAL
242
38.334
56.948
64.410
1.00
7.88
DIC

ATOM
1886
CB
VAL
242
38.101
55.605
65.152
1.00
6.91
DIC

ATOM
1887
CG1
VAL
242
37.159
54.716
64.334
1.00
7.05
DIC

ATOM
1888
CG2
VAL
242
39.435
54.894
65.400
1.00
5.82
DIC

ATOM
1889
C
VAL
242
36.965
57.599
64.228
1.00
9.17
DIC

ATOM
1890
O
VAL
242
36.296
57.908
65.207
1.00
9.42
DIC

ATOM
1891
N
SER
243
36.560
57.818
62.979
1.00
10.01
DIC

ATOM
1892
CA
SER
243
35.235
58.359
62.692
1.00
10.35
DIC

ATOM
1893
CB
SER
243
35.219
59.157
61.379
1.00
11.55
DIC

ATOM
1894
OG
SER
243
35.705
60.470
61.551
1.00
13.46
DIC

ATOM
1895
C
SER
243
34.356
57.133
62.530
1.00
10.90
DIC

ATOM
1896
O
SER
243
34.697
56.221
61.774
1.00
12.28
DIC

ATOM
1897
N
HIS
244
33.248
57.087
63.260
1.00
10.40
DIC

ATOM
1898
CA
HIS
244
32.335
55.955
63.157
1.00
9.48
DIC

ATOM
1899
CB
HIS
244
32.258
55.211
64.491
1.00
8.63
DIC

ATOM
1900
CG
HIS
244
31.406
53.969
64.457
1.00
7.07
DIC

ATOM
1901
CD2
HIS
244
30.800
53.324
63.430
1.00
6.40
DIC

ATOM
1902
ND1
HIS
244
31.109
53.242
65.593
1.00
5.32
DIC

ATOM
1903
CE1
HIS
244
30.358
52.203
65.268
1.00
6.23
DIC

ATOM
1904
NE2
HIS
244
30.155
52.228
63.961
1.00
5.08
DIC

ATOM
1905
C
HIS
244
30.962
56.518
62.778
1.00
9.32
DIC

ATOM
1906
O
HIS
244
30.357
57.262
63.518
1.00
9.29
DIC

ATOM
1907
N
TYR
245
30.491
56.106
61.614
1.00
10.23
DIC

ATOM
1908
CA
TYR
245
29.229
56.554
61.093
1.00
11.52
DIC

ATOM
1909
CB
TYR
245
29.385
56.723
59.580
1.00
12.42
DIC

ATOM
1910
CG
TYR
245
30.457
57.727
59.231
1.00
13.35
DIC

ATOM
1911
CD1
TYR
245
30.201
59.088
59.354
1.00
14.28
DIC

ATOM
1912
CE1
TYR
245
31.183
60.030
59.167
1.00
14.76
DIC

ATOM
1913
CD2
TYR
245
31.750
57.323
58.888
1.00
13.50
DIC

ATOM
1914
CE2
TYR
245
32.760
58.273
58.692
1.00
14.51
DIC

ATOM
1915
CZ
TYR
245
32.455
59.626
58.845
1.00
14.66
DIC

ATOM
1916
OH
TYR
245
33.392
60.623
58.735
1.00
16.02
DIC

ATOM
1917
C
TYR
245
28.023
55.657
61.442
1.00
12.60
DIC

ATOM
1918
O
TYR
245
27.217
55.324
60.565
1.00
10.16
DIC

ATOM
1919
N
CYS
246
27.868
55.278
62.716
1.00
14.89
DIC

ATOM
1920
CA
CYS
246
26.747
54.389
63.105
1.00
14.89
DIC

ATOM
1921
CB
CYS
246
26.837
54.053
64.586
1.00
14.89
DIC

ATOM
1922
SG
CYS
246
26.840
55.482
65.652
1.00
14.89
DIC

ATOM
1923
C
CYS
246
25.358
54.973
62.774
1.00
14.89
DIC

ATOM
1924
O
CYS
246
25.166
56.192
62.672
1.00
17.31
DIC

ATOM
1925
N
GLY
247
24.386
54.085
62.600
1.00
17.22
DIC

ATOM
1926
CA
GLY
247
23.050
54.509
62.224
1.00
15.49
DIC

ATOM
1927
C
GLY
247
22.836
54.344
60.719
1.00
15.79
DIC

ATOM
1928
O
GLY
247
23.737
53.891
60.024
1.00
14.94
DIC

ATOM
1929
N
PRO
248
21.638
54.668
60.197
1.00
15.38
DIC

ATOM
1930
CD
PRO
248
20.497
55.170
60.986
1.00
15.79
DIC

ATOM
1931
CA
PRO
248
21.275
54.566
58.776
1.00
15.64
DIC

ATOM
1932
CB
PRO
248
19.790
54.933
58.781
1.00
16.59
DIC

ATOM
1933
CG
PRO
248
19.691
55.890
59.926
1.00
16.76
DIC

ATOM
1934
C
PRO
248
22.078
55.449
57.812
1.00
15.27
DIC

ATOM
1935
O
PRO
248
22.254
55.102
56.643
1.00
14.87
DIC

ATOM
1936
N
ALA
249
22.558
56.590
58.301
1.00
15.42
DIC

ATOM
1937
CA
ALA
249
23.315
57.528
57.468
1.00
15.19
DIC

ATOM
1938
CB
ALA
249
23.165
58.938
58.029
1.00
15.27
DIC

ATOM
1939
C
ALA
249
24.793
57.173
57.328
1.00
15.38
DIC

ATOM
1940
O
ALA
249
25.592
57.446
58.220
1.00
15.05
DIC

ATOM
1941
N
LYS
250
25.152
56.584
56.188
1.00
14.72
DIC

ATOM
1942
CA
LYS
250
26.531
56.180
55.938
1.00
15.73
DIC

ATOM
1943
CB
LYS
250
26.566
54.754
55.382
1.00
13.72
DIC

ATOM
1944
CG
LYS
250
25.816
53.722
56.234
1.00
12.46
DIC

ATOM
1945
CD
LYS
250
26.365
53.637
57.655
1.00
11.65
DIC

ATOM
1946
CE
LYS
250
25.760
52.454
58.410
1.00
10.42
DIC

ATOM
1947
NZ
LYS
250
26.120
52.501
59.856
1.00
8.32
DIC

ATOM
1948
C
LYS
250
27.238
57.129
54.968
1.00
16.91
DIC

ATOM
1949
O
LYS
250
26.590
57.809
54.180
1.00
17.59
DIC

ATOM
1950
N
PRO
251
28.582
57.170
55.006
1.00
18.44
DIC

ATOM
1951
CD
PRO
251
29.488
56.380
55.861
1.00
18.27
DIC

ATOM
1952
CA
PRO
251
29.348
58.049
54.118
1.00
19.06
DIC

ATOM
1953
CB
PRO
251
30.767
57.936
54.663
1.00
18.51
DIC

ATOM
1954
CG
PRO
251
30.820
56.527
55.144
1.00
19.13
DIC

ATOM
1955
C
PRO
251
29.261
57.682
52.641
1.00
20.28
DIC

ATOM
1956
O
PRO
251
29.504
58.531
51.781
1.00
20.27
DIC

ATOM
1957
N
TRP
252
28.919
56.429
52.341
1.00
20.96
DIC

ATOM
1958
CA
TRP
252
28.799
55.997
50.945
1.00
21.97
DIC

ATOM
1959
CB
TRP
252
29.103
54.497
50.803
1.00
19.99
DIC

ATOM
1960
CG
TRP
252
28.408
53.601
51.785
1.00
17.82
DIC

ATOM
1961
CD2
TRP
252
28.983
53.017
52.960
1.00
17.40
DIC

ATOM
1962
CE2
TRP
252
27.976
52.253
53.581
1.00
16.50
DIC

ATOM
1963
CE3
TRP
252
30.254
53.069
53.548
1.00
15.92
DIC

ATOM
1964
CD1
TRP
252
27.113
53.180
51.743
1.00
17.54
DIC

ATOM
1965
NE1
TRP
252
26.846
52.370
52.819
1.00
16.77
DIC

ATOM
1966
CZ2
TRP
252
28.198
51.545
54.760
1.00
16.16
DIC

ATOM
1967
CZ3
TRP
252
30.474
52.363
54.723
1.00
15.63
DIC

ATOM
1968
CH2
TRP
252
29.451
51.612
55.316
1.00
16.00
DIC

ATOM
1969
C
TRP
252
27.420
56.320
50.375
1.00
23.39
DIC

ATOM
1970
O
TRP
252
27.060
55.873
49.284
1.00
23.70
DIC

ATOM
1971
N
HIS
253
26.666
57.117
51.125
1.00
25.29
DIC

ATOM
1972
CA
HIS
253
25.328
57.546
50.735
1.00
27.91
DIC

ATOM
1973
CB
HIS
253
24.389
57.480
51.941
1.00
28.69
DIC

ATOM
1974
CG
HIS
253
23.900
56.102
52.247
1.00
29.56
DIC

ATOM
1975
CD2
HIS
253
23.892
54.973
51.499
1.00
29.18
DIC

ATOM
1976
ND1
HIS
253
23.314
55.769
53.451
1.00
29.91
DIC

ATOM
1977
CE1
HIS
253
22.969
54.494
53.431
1.00
30.98
DIC

ATOM
1978
NE2
HIS
253
23.310
53.988
52.258
1.00
30.37
DIC

ATOM
1979
C
HIS
253
25.353
58.972
50.187
1.00
28.54
DIC

ATOM
1980
OT1
HIS
253
26.453
59.565
50.159
1.00
15.87
DIC

ATOM
1981
OT2
HIS
253
24.275
59.480
49.790
1.00
15.87
DIC

ATOM
1982
CB
ALA
258
28.094
61.904
58.825
1.00
28.44
DIC

ATOM
1983
C
ALA
258
29.433
64.012
58.929
1.00
27.58
DIC

ATOM
1984
O
ALA
258
29.918
64.149
57.808
1.00
27.40
DIC

ATOM
1985
N
ALA
258
27.094
64.069
58.174
1.00
28.06
DIC

ATOM
1986
CA
ALA
258
28.048
63.405
59.105
1.00
27.73
DIC

ATOM
1987
N
TRP
259
30.068
64.366
60.042
1.00
27.44
DIC

ATOM
1988
CA
TRP
259
31.396
64.976
60.013
1.00
26.88
DIC

ATOM
1989
CB
TRP
259
31.824
65.387
61.426
1.00
27.00
DIC

ATOM
1990
CG
TRP
259
33.185
66.030
61.464
1.00
26.63
DIC

ATOM
1991
CD2
TRP
259
34.417
65.401
61.831
1.00
26.39
DIC

ATOM
1992
CE2
TRP
259
35.440
66.363
61.676
1.00
26.47
DIC

ATOM
1993
CE3
TRP
259
34.758
64.117
62.276
1.00
26.52
DIC

ATOM
1994
CD1
TRP
259
33.499
67.312
61.111
1.00
26.17
DIC

ATOM
1995
NE1
TRP
259
34.853
67.520
61.236
1.00
26.25
DIC

ATOM
1996
CZ2
TRP
259
36.779
66.080
61.948
1.00
26.25
DIC

ATOM
1997
CZ3
TRP
259
36.090
63.837
62.546
1.00
25.96
DIC

ATOM
1998
CH2
TRP
259
37.083
64.815
62.381
1.00
26.60
DIC

ATOM
1999
C
TRP
259
32.465
64.060
59.419
1.00
26.25
DIC

ATOM
2000
O
TRP
259
32.511
62.869
59.723
1.00
26.62
DIC

ATOM
2001
N
GLY
260
33.314
64.632
58.570
1.00
25.54
DIC

ATOM
2002
CA
GLY
260
34.400
63.889
57.949
1.00
24.64
DIC

ATOM
2003
C
GLY
260
34.002
62.871
56.898
1.00
24.46
DIC

ATOM
2004
O
GLY
260
34.833
62.072
56.462
1.00
25.49
DIC

ATOM
2005
N
ALA
261
32.742
62.899
56.479
1.00
24.06
DIC

ATOM
2006
CA
ALA
261
32.247
61.958
55.484
1.00
23.45
DIC

ATOM
2007
CB
ALA
261
30.744
62.142
55.310
1.00
23.85
DIC

ATOM
2008
C
ALA
261
32.946
62.072
54.131
1.00
23.44
DIC

ATOM
2009
O
ALA
261
32.868
61.161
53.315
1.00
24.03
DIC

ATOM
2010
N
ALA
262
33.631
63.185
53.889
1.00
23.25
DIC

ATOM
2011
CA
ALA
262
34.318
63.387
52.615
1.00
23.00
DIC

ATOM
2012
CB
ALA
262
34.643
64.869
52.415
1.00
23.30
DIC

ATOM
2013
C
ALA
262
35.589
62.560
52.484
1.00
22.59
DIC

ATOM
2014
O
ALA
262
36.061
62.312
51.374
1.00
22.28
DIC

ATOM
2015
N
ARG
263
36.159
62.144
53.607
1.00
21.93
DIC

ATOM
2016
CA
ARG
263
37.370
61.347
53.550
1.00
21.92
DIC

ATOM
2017
CB
ARG
263
37.959
61.155
54.950
1.00
24.12
DIC

ATOM
2018
CG
ARG
263
39.231
60.298
54.987
1.00
27.56
DIC

ATOM
2019
CD
ARG
263
39.921
60.412
56.350
1.00
30.65
DIC

ATOM
2020
NE
ARG
263
40.887
59.343
56.622
1.00
33.18
DIC

ATOM
2021
CZ
ARG
263
41.943
59.055
55.862
1.00
34.55
DIC

ATOM
2022
NH1
ARG
263
42.757
58.064
56.210
1.00
35.10
DIC

ATOM
2023
NH2
ARG
263
42.183
59.748
54.751
1.00
35.66
DIC

ATOM
2024
C
ARG
263
37.062
59.998
52.906
1.00
20.84
DIC

ATOM
2025
O
ARG
263
37.951
59.357
52.359
1.00
19.59
DIC

ATOM
2026
N
PHE
264
35.803
59.569
52.971
1.00
20.19
DIC

ATOM
2027
CA
PHE
264
35.403
58.300
52.360
1.00
19.21
DIC

ATOM
2028
CB
PHE
264
33.941
57.972
52.676
1.00
19.33
DIC

ATOM
2029
CG
PHE
264
33.437
56.740
51.971
1.00
18.65
DIC

ATOM
2030
CD1
PHE
264
33.600
55.480
52.536
1.00
17.83
DIC

ATOM
2031
CD2
PHE
264
32.844
56.835
50.712
1.00
17.86
DIC

ATOM
2032
CE1
PHE
264
33.182
54.329
51.857
1.00
17.13
DIC

ATOM
2033
CE2
PHE
264
32.427
55.694
50.031
1.00
18.25
DIC

ATOM
2034
CZ
PHE
264
32.596
54.440
50.604
1.00
16.55
DIC

ATOM
2035
C
PHE
264
35.560
58.371
50.844
1.00
19.58
DIC

ATOM
2036
O
PHE
264
36.246
57.545
50.235
1.00
18.31
DIC

ATOM
2037
N
THR
265
34.909
59.357
50.233
1.00
20.22
DIC

ATOM
2038
CA
THR
265
34.976
59.523
48.783
1.00
21.42
DIC

ATOM
2039
CB
THR
265
34.038
60.674
48.309
1.00
22.32
DIC

ATOM
2040
OG1
THR
265
34.270
60.945
46.920
1.00
23.37
DIC

ATOM
2041
CG2
THR
265
34.268
61.927
49.111
1.00
23.03
DIC

ATOM
2042
C
THR
265
36.419
59.780
48.342
1.00
21.65
DIC

ATOM
2043
O
THR
265
36.855
59.319
47.287
1.00
20.87
DIC

ATOM
2044
N
GLU
266
37.167
60.485
49.180
1.00
21.89
DIC

ATOM
2045
CA
GLU
266
38.560
60.794
48.899
1.00
22.68
DIC

ATOM
2046
CB
GLU
266
39.086
61.722
49.989
1.00
24.83
DIC

ATOM
2047
CG
GLU
266
40.501
62.213
49.792
1.00
29.43
DIC

ATOM
2048
CD
GLU
266
40.812
63.387
50.704
1.00
31.88
DIC

ATOM
2049
OE1
GLU
266
40.454
63.314
51.903
1.00
32.56
DIC

ATOM
2050
OE2
GLU
266
41.410
64.380
50.223
1.00
33.53
DIC

ATOM
2051
C
GLU
266
39.394
59.504
48.824
1.00
21.84
DIC

ATOM
2052
O
GLU
266
40.229
59.348
47.935
1.00
20.75
DIC

ATOM
2053
N
LEU
267
39.162
58.584
49.760
1.00
19.85
DIC

ATOM
2054
CA
LEU
267
39.874
57.308
49.780
1.00
19.01
DIC

ATOM
2055
CB
LEU
267
39.643
56.581
51.105
1.00
18.80
DIC

ATOM
2056
CG
LEU
267
40.471
57.095
52.276
1.00
18.91
DIC

ATOM
2057
CD1
LEU
267
39.894
56.591
53.588
1.00
18.99
DIC

ATOM
2058
CD2
LEU
267
41.914
56.654
52.082
1.00
19.67
DIC

ATOM
2059
C
LEU
267
39.406
56.425
48.639
1.00
18.45
DIC

ATOM
2060
O
LEU
267
40.215
55.764
47.992
1.00
16.88
DIC

ATOM
2061
N
ALA
268
38.095
56.408
48.398
1.00
18.86
DIC

ATOM
2062
CA
ALA
268
37.532
55.607
47.318
1.00
20.48
DIC

ATOM
2063
CB
ALA
268
36.018
55.792
47.254
1.00
21.06
DIC

ATOM
2064
C
ALA
268
38.169
56.024
45.996
1.00
21.58
DIC

ATOM
2065
O
ALA
268
38.481
55.185
45.157
1.00
20.74
DIC

ATOM
2066
N
GLY
269
38.376
57.324
45.820
1.00
22.51
DIC

ATOM
2067
CA
GLY
269
38.979
57.805
44.590
1.00
24.41
DIC

ATOM
2068
C
GLY
269
40.444
57.429
44.473
1.00
25.41
DIC

ATOM
2069
O
GLY
269
41.007
57.421
43.379
1.00
25.74
DIC

ATOM
2070
N
SER
270
41.069
57.114
45.600
1.00
25.49
DIC

ATOM
2071
CA
SER
270
42.479
56.748
45.598
1.00
26.14
DIC

ATOM
2072
CB
SER
270
43.117
57.107
46.939
1.00
25.67
DIC

ATOM
2073
OG
SER
270
42.648
56.249
47.965
1.00
25.26
DIC

ATOM
2074
C
SER
270
42.689
55.263
45.329
1.00
26.42
DIC

ATOM
2075
O
SER
270
43.821
54.815
45.155
1.00
26.83
DIC

ATOM
2076
N
LEU
271
41.603
54.498
45.298
1.00
26.90
DIC

ATOM
2077
CA
LEU
271
41.708
53.063
45.065
1.00
27.83
DIC

ATOM
2078
CB
LEU
271
40.319
52.417
45.034
1.00
27.48
DIC

ATOM
2079
CG
LEU
271
39.575
52.392
46.367
1.00
27.23
DIC

ATOM
2080
CD1
LEU
271
38.288
51.595
46.216
1.00
26.49
DIC

ATOM
2081
CD2
LEU
271
40.470
51.778
47.435
1.00
26.56
DIC

ATOM
2082
C
LEU
271
42.460
52.696
43.793
1.00
28.34
DIC

ATOM
2083
O
LEU
271
42.286
53.314
42.744
1.00
28.17
DIC

ATOM
2084
N
THR
272
43.289
51.665
43.907
1.00
29.25
DIC

ATOM
2085
CA
THR
272
44.088
51.166
42.799
1.00
29.35
DIC

ATOM
2086
CB
THR
272
45.106
50.129
43.293
1.00
29.61
DIC

ATOM
2087
OG1
THR
272
45.930
50.712
44.312
1.00
30.29
DIC

ATOM
2088
CG2
THR
272
45.974
49.654
42.142
1.00
29.87
DIC

ATOM
2089
C
THR
272
43.229
50.500
41.728
1.00
29.37
DIC

ATOM
2090
O
THR
272
43.324
50.838
40.548
1.00
29.51
DIC

ATOM
2091
N
THR
273
42.409
49.541
42.151
1.00
28.69
DIC

ATOM
2092
CA
THR
273
41.533
48.798
41.248
1.00
28.59
DIC

ATOM
2093
CB
THR
273
41.892
47.297
41.218
1.00
30.32
DIC

ATOM
2094
OG1
THR
273
43.302
47.137
41.014
1.00
32.39
DIC

ATOM
2095
CG2
THR
273
41.140
46.602
40.096
1.00
31.41
DIC

ATOM
2096
C
THR
273
40.077
48.896
41.690
1.00
27.15
DIC

ATOM
2097
O
THR
273
39.746
48.572
42.831
1.00
26.61
DIC

ATOM
2098
N
VAL
274
39.204
49.334
40.789
1.00
24.82
DIC

ATOM
2099
CA
VAL
274
37.792
49.445
41.128
1.00
23.71
DIC

ATOM
2100
CB
VAL
274
37.361
50.924
41.261
1.00
24.47
DIC

ATOM
2101
CG1
VAL
274
37.742
51.692
40.014
1.00
24.70
DIC

ATOM
2102
CG2
VAL
274
35.862
51.005
41.509
1.00
24.49
DIC

ATOM
2103
C
VAL
274
36.917
48.739
40.095
1.00
22.44
DIC

ATOM
2104
O
VAL
274
36.769
49.202
38.964
1.00
21.71
DIC

ATOM
2105
N
PRO
275
36.341
47.587
40.477
1.00
21.18
DIC

ATOM
2106
CD
PRO
275
36.537
46.929
41.779
1.00
20.08
DIC

ATOM
2107
CA
PRO
275
35.472
46.778
39.619
1.00
20.90
DIC

ATOM
2108
CB
PRO
275
35.053
45.630
40.534
1.00
20.65
DIC

ATOM
2109
CG
PRO
275
36.203
45.498
41.464
1.00
20.01
DIC

ATOM
2110
C
PRO
275
34.267
47.558
39.120
1.00
20.92
DIC

ATOM
2111
O
PRO
275
33.714
48.397
39.835
1.00
20.31
DIC

ATOM
2112
N
GLU
276
33.859
47.273
37.890
1.00
22.03
DIC

ATOM
2113
CA
GLU
276
32.701
47.938
37.312
1.00
22.81
DIC

ATOM
2114
CB
GLU
276
32.317
47.269
35.987
1.00
23.16
DIC

ATOM
2115
CG
GLU
276
30.944
47.665
35.449
1.00
23.75
DIC

ATOM
2116
CD
GLU
276
30.859
49.123
35.047
1.00
23.43
DIC

ATOM
2117
OE1
GLU
276
31.868
49.846
35.176
1.00
24.18
DIC

ATOM
2118
OE2
GLU
276
29.774
49.547
34.598
1.00
24.32
DIC

ATOM
2119
C
GLU
276
31.540
47.843
38.293
1.00
23.40
DIC

ATOM
2120
O
GLU
276
30.810
48.811
38.496
1.00
24.06
DIC

ATOM
2121
N
GLU
277
31.395
46.683
38.928
1.00
23.55
DIC

ATOM
2122
CA
GLU
277
30.303
46.472
39.865
1.00
24.83
DIC

ATOM
2123
CB
GLU
277
30.148
44.976
40.157
1.00
27.38
DIC

ATOM
2124
CG
GLU
277
28.685
44.509
40.248
1.00
31.14
DIC

ATOM
2125
CD
GLU
277
28.029
44.257
38.882
1.00
33.24
DIC

ATOM
2126
OE1
GLU
277
28.023
45.164
38.017
1.00
34.02
DIC

ATOM
2127
OE2
GLU
277
27.508
43.136
38.679
1.00
34.95
DIC

ATOM
2128
C
GLU
277
30.419
47.255
41.180
1.00
23.83
DIC

ATOM
2129
O
GLU
277
29.507
47.209
42.009
1.00
24.63
DIC

ATOM
2130
N
TRP
278
31.532
47.964
41.373
1.00
22.09
DIC

ATOM
2131
CA
TRP
278
31.735
48.775
42.580
1.00
20.45
DIC

ATOM
2132
CB
TRP
278
33.183
48.680
43.078
1.00
17.96
DIC

ATOM
2133
CG
TRP
278
33.544
47.431
43.835
1.00
16.02
DIC

ATOM
2134
CD2
TRP
278
34.693
47.245
44.677
1.00
16.17
DIC

ATOM
2135
CE2
TRP
278
34.676
45.906
45.117
1.00
16.04
DIC

ATOM
2136
CE3
TRP
278
35.738
48.084
45.101
1.00
16.30
DIC

ATOM
2137
CD1
TRP
278
32.897
46.235
43.804
1.00
15.72
DIC

ATOM
2138
NE1
TRP
278
33.569
45.312
44.568
1.00
15.84
DIC

ATOM
2139
CZ2
TRP
278
35.665
45.378
45.959
1.00
15.03
DIC

ATOM
2140
CZ3
TRP
278
36.728
47.557
45.941
1.00
15.75
DIC

ATOM
2141
CH2
TRP
278
36.679
46.216
46.360
1.00
16.12
DIC

ATOM
2142
C
TRP
278
31.453
50.236
42.248
1.00
20.70
DIC

ATOM
2143
O
TRP
278
31.281
51.066
43.141
1.00
20.71
DIC

ATOM
2144
N
ALA
279
31.416
50.542
40.955
1.00
21.39
DIC

ATOM
2145
CA
ALA
279
31.190
51.904
40.479
1.00
22.71
DIC

ATOM
2146
CB
ALA
279
31.084
51.910
38.954
1.00
23.51
DIC

ATOM
2147
C
ALA
279
29.965
52.563
41.087
1.00
23.55
DIC

ATOM
2148
O
ALA
279
29.959
53.771
41.323
1.00
24.28
DIC

ATOM
2149
N
GLY
280
28.929
51.768
41.333
1.00
24.37
DIC

ATOM
2150
CA
GLY
280
27.705
52.294
41.913
1.00
25.98
DIC

ATOM
2151
C
GLY
280
27.849
52.651
43.383
1.00
26.65
DIC

ATOM
2152
O
GLY
280
27.674
53.808
43.770
1.00
27.02
DIC

ATOM
2153
N
ALA
281
28.165
51.657
44.208
1.00
27.42
DIC

ATOM
2154
CA
ALA
281
28.337
51.874
45.639
1.00
28.02
DIC

ATOM
2155
CB
ALA
281
28.645
50.550
46.334
1.00
27.29
DIC

ATOM
2156
C
ALA
281
29.477
52.860
45.857
1.00
28.66
DIC

ATOM
2157
O
ALA
281
29.529
53.550
46.874
1.00
29.25
DIC

ATOM
2158
N
ALA
282
30.377
52.912
44.879
1.00
29.42
DIC

ATOM
2159
CA
ALA
282
31.552
53.784
44.887
1.00
30.55
DIC

ATOM
2160
CB
ALA
282
31.121
55.261
44.884
1.00
30.21
DIC

ATOM
2161
C
ALA
282
32.458
53.501
46.078
1.00
31.20
DIC

ATOM
2162
OT1
ALA
282
33.390
52.669
45.938
1.00
32.04
DIC

ATOM
2163
OT2
ALA
282
32.207
54.100
47.145
1.00
31.25
DIC

ATOM
2164
N1
UPG
341
27.240
44.499
57.825
1.00
10.18

ATOM
2165
C2
UPG
341
27.623
43.818
56.650
1.00
9.69

ATOM
2166
N3
UPG
341
26.746
44.059
55.575
1.00
8.84

ATOM
2167
C4
UPG
341
25.566
44.894
55.582
1.00
8.96

ATOM
2168
C5
UPG
341
25.252
45.558
56.815
1.00
8.24

ATOM
2169
C6
UPG
341
26.056
45.357
57.869
1.00
8.97

ATOM
2170
O2
UPG
341
28.602
43.097
56.579
1.00
9.27

ATOM
2171
O4
UPG
341
24.905
44.993
54.563
1.00
11.09

ATOM
2172
C4*
UPG
341
28.140
45.874
61.110
1.00
9.66

ATOM
2173
O4*
UPG
341
27.321
44.837
60.426
1.00
9.94

ATOM
2174
C3*
UPG
341
28.902
46.508
59.951
1.00
8.28

ATOM
2175
O3*
UPG
341
29.996
47.267
60.429
1.00
10.54

ATOM
2176
C2*
UPG
341
29.173
45.283
59.098
1.00
9.24

ATOM
2177
O2*
UPG
341
30.290
44.505
59.538
1.00
9.22

ATOM
2178
C1*
UPG
341
27.913
44.478
59.203
1.00
10.37

ATOM
2179
C5*
UPG
341
26.834
46.274
61.715
1.00
8.33

ATOM
2180
O5*
UPG
341
26.278
47.636
61.455
1.00
14.17

ATOM
2181
PA
UPG
341
26.757
49.151
61.231
1.00
11.35

ATOM
2182
O1A
UPG
341
28.224
49.345
61.258
1.00
12.96

ATOM
2183
O2A
UPG
341
26.106
49.722
60.020
1.00
14.14

ATOM
2184
O3A
UPG
341
25.990
49.305
62.626
1.00
12.31

ATOM
2185
PB
UPG
341
25.718
50.499
63.635
1.00
14.51

ATOM
2186
O1B
UPG
341
27.055
51.134
63.729
1.00
11.54

ATOM
2187
O2B
UPG
341
24.736
51.411
63.036
1.00
15.63

ATOM
2188
O3B
UPG
341
25.289
49.955
65.021
1.00
15.47

ATOM
2189
C1′
UPG
341
25.701
49.765
66.543
1.00
20.67

ATOM
2190
C2′
UPG
341
27.182
49.323
66.490
1.00
19.41

ATOM
2191
C3′
UPG
341
27.600
48.129
65.515
1.00
20.26

ATOM
2192
C4′
UPG
341
26.609
46.923
65.726
1.00
19.77

ATOM
2193
C5′
UPG
341
25.121
47.545
65.719
1.00
20.08

ATOM
2194
C6′
UPG
341
24.111
46.486
66.179
1.00
21.34

ATOM
2195
F2′
UPG
341
28.054
50.401
66.263
1.00
22.29

ATOM
2196
O3′
UPG
341
28.884
47.722
65.901
1.00
19.02

ATOM
2197
O4′
UPG
341
26.927
46.281
66.991
1.00
18.02

ATOM
2198
O5′
UPG
341
24.861
48.621
66.750
1.00
20.07

ATOM
2199
O6′
UPG
341
23.853
45.237
65.594
1.00
20.34

ATOM
2200
MN
MN
400
29.038
50.750
62.751
1.00
6.12
MN

ATOM
2201
C1
LAT
1347
21.862
53.689
65.707
1.00
20.18

ATOM
2202
C2
LAT
1347
22.118
52.340
65.066
1.00
20.18

ATOM
2203
C3
LAT
1347
22.177
51.325
66.179
1.00
20.18

ATOM
2204
C4
LAT
1347
23.332
51.731
67.165
1.00
20.18

ATOM
2205
C5
LAT
1347
23.165
53.016
67.800
1.00
20.18

ATOM
2206
C6
LAT
1347
24.129
53.435
68.634
1.00
20.18

ATOM
2207
O1
LAT
1347
21.580
54.987
65.275
1.00
19.89

ATOM
2208
O2
LAT
1347
21.058
51.980
64.134
1.00
20.18

ATOM
2209
O3
LAT
1347
22.433
50.083
65.582
1.00
20.18

ATOM
2210
O5
LAT
1347
22.941
54.020
66.702
1.00
20.18

ATOM
2211
O6
LAT
1347
24.638
52.525
69.648
1.00
20.18

ATOM
2212
C1′
LAT
1347
20.888
59.061
65.028
1.00
19.89

ATOM
2213
C2′
LAT
1347
22.121
58.647
65.845
1.00
19.89

ATOM
2214
C3′
LAT
1347
22.505
57.214
65.448
1.00
19.89

ATOM
2215
C4′
LAT
1347
21.315
56.296
65.729
1.00
19.89

ATOM
2216
C5′
LAT
1347
20.008
56.750
65.020
1.00
19.89

ATOM
2217
C6′
LAT
1347
18.753
55.952
65.464
1.00
19.89

ATOM
2218
O1′
LAT
1347
20.572
60.386
65.395
1.00
19.89

ATOM
2219
O2′
LAT
1347
23.194
59.542
65.568
1.00
19.89

ATOM
2220
O3′
LAT
1347
23.637
56.854
66.255
1.00
19.89

ATOM
2221
O5′
LAT
1347
19.798
58.147
65.342
1.00
19.89

ATOM
2222
O6′
LAT
1347
18.292
55.063
64.439
1.00
19.89

[0496]

8

TABLE 6

REMARK coordinates from minimization refinement

REMARK refinement resolution: 20.0-2.0 A

REMARK starting r = .1986 free_r = .2234

REMARK final r = .1949 free_r = .2236

REMARK rmsd bonds = .006530 rmsd angles = 1.33814

REMARK wa = 1.2

REMARK target = mlf cycles = 1 steps = 20

REMARK sg = P2(1)2(1)2(1) a = 39.953 b = 76.126 c = 87.163

alpha = 90 beta = 90 gamma = 90

REMARK parameter file 1: CNS_TOPPAR:protein_rep.param

REMARK parameter file 2: ../rnd5/upg.par

REMARK parameter file 3: CNS_TOPPAR:ion.param

REMARK parameter file 4: CNS_TOPPAR:water_rep.param

REMARK parameter file 5: ../lat.par

REMARK molecular structure file: generate8_2.mtf

REMARK input coordinates: generate8_2.pdb

REMARK reflection file = ../lac1.cv

REMARK ncs = none

REMARK B-correction resolution: 6.0-2.0

REMARK initial B-factor correction applied to fobs:

REMARK B11 = 2.769 B22 = 1.768 B33 = −4.536

REMARK B12 = .000 B13 = .000 B23 = .000

REMARK B-factor correction applied to coordinate array B: .038

REMARK bulk solvent: density level = .333397 e/A{fraction ( )}3, B-factor = 34.3204 A{fraction ( )}2

REMARK reflections with |Fobs|/sigma_F <0.0 rejected

REMARK reflections with |Fobs| > 10000 * rms (Fobs) rejected

REMARK theoretical total number of refl. in resol. range:
18567 ( 100.0% )

REMARK number of unobserved reflections (no entry or |F| = 0):
337 ( 1.8% )

REMARK number of reflections rejected:
0 ( .0% )

REMARK total number of reflections used:
18230 ( 98.2% )

REMARK number of reflections in working set:
17343 ( 93.4% )

REMARK number of reflections in test set:
887 ( 4.8% )

CRYST1 39.953 76.126 87.163 90.00 90.00 90.00 P 21 21 21

REMARK FILENAME = “minimize8_2.pdb”

REMARK DATE: 8-Nov-00 23:09:42 created by user: karina

REMARK VERSION: 1.0

ATOM
1
CB
MSE
1
48.127
46.242
65.128
1.00
17.58
DIC

ATOM
2
CG
MSE
1
47.640
47.179
64.037
1.00
20.74
DIC

ATOM
3
SE
MSE
1
46.763
48.808
64.758
1.00
18.31
DIC

ATOM
4
CE
MSE
1
48.354
49.664
65.452
1.00
19.80
DIC

ATOM
5
C
MSE
1
47.777
44.093
63.871
1.00
13.39
DIC

ATOM
6
O
MSE
1
47.840
44.063
62.643
1.00
13.12
DIC

ATOM
7
N
MSE
1
49.999
45.167
63.882
1.00
14.29
DIC

ATOM
8
CA
MSE
1
48.769
44.914
64.676
1.00
14.05
DIC

ATOM
9
N
ASP
2
46.876
43.408
64.566
1.00
13.55
DIC

ATOM
10
CA
ASP
2
45.870
42.590
63.901
1.00
13.67
DIC

ATOM
11
CB
ASP
2
45.770
41.211
64.547
1.00
14.41
DIC

ATOM
12
CG
ASP
2
47.030
40.392
64.352
1.00
15.71
DIC

ATOM
13
OD1
ASP
2
47.932
40.477
65.207
1.00
14.07
DIC

ATOM
14
OD2
ASP
2
47.121
39.682
63.329
1.00
16.48
DIC

ATOM
15
C
ASP
2
44.519
43.273
63.942
1.00
14.09
DIC

ATOM
16
O
ASP
2
43.974
43.544
65.012
1.00
13.05
DIC

ATOM
17
N
ILE
3
43.994
43.562
62.758
1.00
12.65
DIC

ATOM
18
CA
ILE
3
42.707
44.217
62.624
1.00
11.17
DIC

ATOM
19
CB
ILE
3
42.748
45.331
61.560
1.00
10.15
DIC

ATOM
20
CG2
ILE
3
41.355
45.938
61.402
1.00
8.26
DIC

ATOM
21
CG1
ILE
3
43.816
46.371
61.921
1.00
9.18
DIC

ATOM
22
CD
ILE
3
43.553
47.140
63.221
1.00
10.15
DIC

ATOM
23
C
ILE
3
41.699
43.186
62.169
1.00
11.33
DIC

ATOM
24
O
ILE
3
42.021
42.313
61.364
1.00
12.76
DIC

ATOM
25
N
VAL
4
40.481
43.293
62.682
1.00
11.00
DIC

ATOM
26
CA
VAL
4
39.420
42.375
62.305
1.00
11.29
DIC

ATOM
27
CB
VAL
4
38.923
41.545
63.501
1.00
12.03
DIC

ATOM
28
CG1
VAL
4
37.776
40.629
63.046
1.00
13.87
DIC

ATOM
29
CG2
VAL
4
40.068
40.719
64.083
1.00
12.49
DIC

ATOM
30
C
VAL
4
38.226
43.144
61.758
1.00
10.90
DIC

ATOM
31
O
VAL
4
37.808
44.146
62.332
1.00
12.17
DIC

ATOM
32
N
PHE
5
37.704
42.676
60.630
1.00
11.30
DIC

ATOM
33
CA
PHE
5
36.524
43.259
59.998
1.00
9.47
DIC

ATOM
34
CB
PHE
5
36.862
43.876
58.635
1.00
11.11
DIC

ATOM
35
CG
PHE
5
37.513
45.229
58.702
1.00
9.37
DIC

ATOM
36
CD1
PHE
5
36.818
46.332
59.186
1.00
10.57
DIC

ATOM
37
CD2
PHE
5
38.799
45.412
58.204
1.00
10.04
DIC

ATOM
38
CE1
PHE
5
37.398
47.610
59.164
1.00
11.62
DIC

ATOM
39
CE2
PHE
5
39.386
46.674
58.178
1.00
11.49
DIC

ATOM
40
CZ
PHE
5
38.683
47.776
58.657
1.00
12.84
DIC

ATOM
41
C
PHE
5
35.589
42.074
59.748
1.00
10.75
DIC

ATOM
42
O
PHE
5
36.034
40.922
59.713
1.00
9.51
DIC

ATOM
43
N
ALA
6
34.305
42.364
59.581
1.00
8.88
DIC

ATOM
44
CA
ALA
6
33.296
41.353
59.281
1.00
9.05
DIC

ATOM
45
CB
ALA
6
32.408
41.090
60.493
1.00
7.20
DIC

ATOM
46
C
ALA
6
32.461
41.947
58.154
1.00
10.16
DIC

ATOM
47
O
ALA
6
32.012
43.093
58.247
1.00
9.64
DIC

ATOM
48
N
ALA
7
32.244
41.184
57.093
1.00
9.74
DIC

ATOM
49
CA
ALA
7
31.451
41.699
55.987
1.00
11.40
DIC

ATOM
50
CB
ALA
7
32.306
42.623
55.126
1.00
10.99
DIC

ATOM
51
C
ALA
7
30.852
40.616
55.113
1.00
11.73
DIC

ATOM
52
O
ALA
7
31.415
39.528
54.987
1.00
11.58
DIC

ATOM
53
N
ASP
8
29.686
40.914
54.542
1.00
11.95
DIC

ATOM
54
CA
ASP
8
29.040
40.005
53.609
1.00
10.87
DIC

ATOM
55
CB
ASP
8
27.516
39.942
53.812
1.00
11.16
DIC

ATOM
56
CG
ASP
8
26.892
41.297
54.079
1.00
11.92
DIC

ATOM
57
OD1
ASP
8
27.415
42.320
53.585
1.00
9.02
DIC

ATOM
58
OD2
ASP
8
25.855
41.326
54.779
1.00
12.31
DIC

ATOM
59
C
ASP
8
29.377
40.605
52.249
1.00
12.11
DIC

ATOM
60
O
ASP
8
30.072
41.621
52.176
1.00
12.03
DIC

ATOM
61
N
ASP
9
28.895
40.006
51.170
1.00
12.52
DIC

ATOM
62
CA
ASP
9
29.232
40.523
49.849
1.00
13.97
DIC

ATOM
63
CB
ASP
9
28.640
39.630
48.759
1.00
15.00
DIC

ATOM
64
CG
ASP
9
29.274
39.883
47.412
1.00
15.24
DIC

ATOM
65
OD1
ASP
9
30.490
39.628
47.269
1.00
16.40
DIC

ATOM
66
OD2
ASP
9
28.567
40.349
46.502
1.00
19.30
DIC

ATOM
67
C
ASP
9
28.808
41.970
49.613
1.00
14.35
DIC

ATOM
68
O
ASP
9
29.514
42.727
48.948
1.00
14.40
DIC

ATOM
69
N
ASN
10
27.660
42.352
50.164
1.00
14.55
DIC

ATOM
70
CA
ASN
10
27.135
43.704
50.010
1.00
15.08
DIC

ATOM
71
CB
ASN
10
25.792
43.817
50.738
1.00
15.92
DIC

ATOM
72
CG
ASN
10
25.151
45.191
50.593
1.00
16.37
DIC

ATOM
73
OD1
ASN
10
24.987
45.697
49.486
1.00
15.05
DIC

ATOM
74
ND2
ASN
10
24.772
45.791
51.719
1.00
15.34
DIC

ATOM
75
C
ASN
10
28.084
44.796
50.513
1.00
15.42
DIC

ATOM
76
O
ASN
10
28.065
45.922
50.007
1.00
14.99
DIC

ATOM
77
N
TYR
11
28.918
44.468
51.496
1.00
14.68
DIC,

ATOM
78
CA
TYR
11
29.846
45.453
52.063
1.00
13.78
DIC

ATOM
79
CB
TYR
11
29.746
45.436
53.592
1.00
13.14
DIC

ATOM
80
CG
TYR
11
28.744
46.423
54.138
1.00
15.36
DIC

ATOM
81
CD1
TYR
11
27.647
46.820
53.376
1.00
15.46
DIC

ATOM
82
CE1
TYR
11
26.735
47.745
53.859
1.00
16.70
DIC

ATOM
83
CD2
TYR
11
28.900
46.976
55.409
1.00
15.54
DIC

ATOM
84
CE2
TYR
11
27.988
47.902
55.904
1.00
18.09
DIC

ATOM
85
CZ
TYR
11
26.909
48.281
55.120
1.00
17.62
DIC

ATOM
86
OH
TYR
11
26.005
49.200
55.585
1.00
19.94
DIC

ATOM
87
C
TYR
11
31.300
45.295
51.647
1.00
13.79
DIC

ATOM
88
O
TYR
11
32.183
45.965
52.193
1.00
13.61
DIC

ATOM
89
N
ALA
12
31.553
44.428
50.672
1.00
13.51
DIC

ATOM
90
CA
ALA
12
32.917
44.197
50.211
1.00
13.12
DIC

ATOM
91
CB
ALA
12
32.929
43.146
49.089
1.00
13.34
DIC

ATOM
92
C
ALA
12
33.604
45.484
49.736
1.00
11.96
DIC

ATOM
93
O
ALA
12
34.774
45.713
50.038
1.00
9.55
DIC

ATOM
94
N
ALA
13
32.888
46.325
48.995
1.00
11.10
DIC

ATOM
95
CA
ALA
13
33.491
47.565
48.499
1.00
11.93
DIC

ATOM
96
CB
ALA
13
32.550
48.251
47.499
1.00
10.97
DIC

ATOM
97
C
ALA
13
33.832
48.507
49.660
1.00
11.31
DIC

ATOM
98
O
ALA
13
34.914
49.097
49.700
1.00
12.37
DIC

ATOM
99
N
TYR
14
32.915
48.625
50.613
1.00
12.09
DIC

ATOM
100
CA
TYR
14
33.114
49.479
51.782
1.00
10.69
DIC

ATOM
101
CB
TYR
14
31.813
49.571
52.590
1.00
10.74
DIC

ATOM
102
CG
TYR
14
30.615
49.952
51.743
1.00
13.01
DIC

ATOM
103
CD1
TYR
14
30.753
50.842
50.677
1.00
12.55
DIC

ATOM
104
CE1
TYR
14
29.669
51.210
49.896
1.00
13.46
DIC

ATOM
105
CD2
TYR
14
29.347
49.434
52.010
1.00
13.02
DIC

ATOM
106
CE2
TYR
14
28.245
49.799
51.232
1.00
16.28
DIC

ATOM
107
CZ
TYR
14
28.424
50.693
50.176
1.00
16.05
DIC

ATOM
108
OH
TYR
14
27.358
51.101
49.416
1.00
19.24
DIC

ATOM
109
C
TYR
14
34.246
48.951
52.659
1.00
10.96
DIC

ATOM
110
O
TYR
14
35.013
49.730
53.237
1.00
10.92
DIC

ATOM
111
N
LEU
15
34.339
47.626
52.770
1.00
10.75
DIC

ATOM
112
CA
LEU
15
35.396
46.994
53.550
1.00
10.52
DIC

ATOM
113
CB
LEU
15
35.303
45.466
53.434
1.00
11.98
DIC

ATOM
114
CG
LEU
15
36.572
44.675
53.789
1.00
14.65
DIC

ATOM
115
CD1
LEU
15
36.856
44.790
55.290
1.00
15.28
DIC

ATOM
116
CD2
LEU
15
36.396
43.209
53.395
1.00
13.71
DIC

ATOM
117
C
LEU
15
36.751
47.458
53.010
1.00
10.20
DIC

ATOM
118
O
LEU
15
37.645
47.823
53.771
1.00
10.38
DIC

ATOM
119
N
CYS
16
36.896
47.424
51.686
1.00
12.12
DIC

ATOM
120
CA
CYS
16
38.136
47.838
51.038
1.00
11.09
DIC

ATOM
121
CB
CYS
16
37.997
47.725
49.515
1.00
12.05
DIC

ATOM
122
SG
CYS
16
39.517
48.138
48.641
1.00
12.15
DIC

ATOM
123
C
CYS
16
38.519
49.274
51.415
1.00
10.93
DIC

ATOM
124
O
CYS
16
39.671
49.550
51.757
1.00
11.30
DIC

ATOM
125
N
VAL
17
37.553
50.185
51.353
1.00
10.79
DIC

ATOM
126
CA
VAL
17
37.805
51.585
51.695
1.00
12.24
DIC

ATOM
127
CB
VAL
17
36.549
52.448
51.438
1.00
12.01
DIC

ATOM
128
CG1
VAL
17
36.734
53.840
52.022
1.00
11.58
DIC

ATOM
129
CG2
VAL
17
36.282
52.531
49.929
1.00
12.39
DIC

ATOM
130
C
VAL
17
38.231
51.720
53.159
1.00
12.59
DIC

ATOM
131
O
VAL
17
39.192
52.422
53.478
1.00
14.20
DIC

ATOM
132
N
ALA
18
37.517
51.038
54.045
1.00
12.29
DIC

ATOM
133
CA
ALA
18
37.831
51.084
55.470
1.00
11.27
DIC

ATOM
134
CB
ALA
18
36.816
50.262
56.247
1.00
11.41
DIC

ATOM
135
C
ALA
18
39.237
50.539
55.723
1.00
12.12
DIC

ATOM
136
O
ALA
18
40.018
51.123
56.479
1.00
9.33
DIC

ATOM
137
N
ALA
19
39.545
49.416
55.081
1.00
11.56
DIC

ATOM
138
CA
ALA
19
40.840
48.772
55.234
1.00
12.42
DIC

ATOM
139
CB
ALA
19
40.883
47.481
54.418
1.00
12.78
DIC

ATOM
140
C
ALA
19
41.966
49.705
54.806
1.00
13.64
DIC

ATOM
141
O
ALA
19
42.970
49.834
55.507
1.00
12.89
DIC

ATOM
142
N
LYS
20
41.805
50.362
53.661
1.00
14.08
DIC

ATOM
143
CA
LYS
20
42.836
51.279
53.202
1.00
14.66
DIC

ATOM
144
CB
LYS
20
42.532
51.789
51.793
1.00
15.85
DIC

ATOM
145
CG
LYS
20
43.694
52.575
51.192
1.00
20.09
DIC

ATOM
146
CD
LYS
20
43.502
52.849
49.706
1.00
22.70
DIC

ATOM
147
CE
LYS
20
44.681
53.638
49.161
1.00
22.43
DIC

ATOM
148
NZ
LYS
20
44.540
53.943
47.712
1.00
24.73
DIC

ATOM
149
C
LYS
20
42.993
52.458
54.162
1.00
14.30
DIC

ATOM
150
O
LYS
20
44.098
52.980
54.329
1.00
13.09
DIC

ATOM
151
N
SER
21
41.906
52.883
54.809
1.00
13.25
DIC

ATOM
152
CA
SER
21
42.033
54.003
55.741
1.00
12.72
DIC

ATOM
153
CB
SER
21
40.660
54.440
56.283
1.00
12.54
DIC

ATOM
154
OG
SER
21
40.244
53.667
57.395
1.00
12.59
DIC

ATOM
155
C
SER
21
42.962
53.586
56.886
1.00
12.00
DIC

ATOM
156
O
SER
21
43.748
54.387
57.392
1.00
13.07
DIC

ATOM
157
N
VAL
22
42.890
52.319
57.279
1.00
11.25
DIC

ATOM
158
CA
VAL
22
43.747
51.816
58.348
1.00
11.30
DIC

ATOM
159
CB
VAL
22
43.360
50.374
58.752
1.00
11.76
DIC

ATOM
160
CG1
VAL
22
44.298
49.870
59.821
1.00
11.30
DIC

ATOM
161
CG2
VAL
22
41.921
50.339
59.241
1.00
11.48
DIC

ATOM
162
C
VAL
22
45.212
51.814
57.912
1.00
11.89
DIC

ATOM
163
O
VAL
22
46.095
52.246
58.662
1.00
12.69
DIC

ATOM
164
N
GLU
23
45.478
51.328
56.704
1.00
10.93
DIC

ATOM
165
CA
GLU
23
46.854
51.295
56.219
1.00
13.03
DIC

ATOM
166
CB
GLU
23
46.952
50.615
54.849
1.00
14.30
DIC

ATOM
167
CG
GLU
23
46.544
49.160
54.823
1.00
14.62
DIC

ATOM
168
CD
GLU
23
46.836
48.512
53.480
1.00
16.61
DIC

ATOM
169
OE1
GLU
23
46.678
49.196
52.449
1.00
17.40
DIC

ATOM
170
OE2
GLU
23
47.209
47.317
53.453
1.00
16.65
DIC

ATOM
171
C
GLU
23
47.407
52.707
56.104
1.00
12.51
DIC

ATOM
172
O
GLU
23
48.538
52.969
56.502
1.00
14.38
DIC

ATOM
173
N
ALA
24
46.603
53.620
55.572
1.00
11.76
DIC

ATOM
174
CA
ALA
24
47.046
54.997
55.397
1.00
12.06
DIC

ATOM
175
CB
ALA
24
45.945
55.827
54.716
1.00
11.87
DIC

ATOM
176
C
ALA
24
47.445
55.635
56.722
1.00
11.80
DIC

ATOM
177
O
ALA
24
48.393
56.425
56.775
1.00
11.54
DIC

ATOM
178
N
ALA
25
46.734
55.279
57.789
1.00
11.43
DIC

ATOM
179
CA
ALA
25
47.005
55.825
59.123
1.00
11.35
DIC

ATOM
180
CB
ALA
25
45.757
55.698
59.998
1.00
11.07
DIC

ATOM
181
C
ALA
25
48.194
55.180
59.836
1.00
11.54
DIC

ATOM
182
O
ALA
25
48.596
55.630
60.904
1.00
10.97
DIC

ATOM
183
N
HIS
26
48.753
54.123
59.264
1.00
11.65
DIC

ATOM
184
CA
HIS
26
49.899
53.464
59.893
1.00
13.56
DIC

ATOM
185
CB
HIS
26
49.452
52.198
60.628
1.00
13.72
DIC

ATOM
186
CG
HIS
26
48.350
52.425
61.617
1.00
14.14
DIC

ATOM
187
CD2
HIS
26
48.381
52.626
62.958
1.00
13.28
DIC

ATOM
188
ND1
HIS
26
47.020
52.455
61.255
1.00
11.89
DIC

ATOM
189
CE1
HIS
26
46.277
52.660
62.330
1.00
12.65
DIC

ATOM
190
NE2
HIS
26
47.078
52.768
63.375
1.00
14.11
DIC

ATOM
191
C
HIS
26
50.940
53.111
58.833
1.00
13.66
DIC

ATOM
192
O
HIS
26
51.151
51.941
58.512
1.00
13.39
DIC

ATOM
193
N
PRO
27
51.615
54.132
58.284
1.00
14.55
DIC

ATOM
194
CD
PRO
27
51.529
55.536
58.728
1.00
15.30
DIC

ATOM
195
CA
PRO
27
52.640
53.966
57.247
1.00
14.85
DIC

ATOM
196
CB
PRO
27
53.078
55.408
56.957
1.00
16.08
DIC

ATOM
197
CG
PRO
27
52.856
56.104
58.270
1.00
17.10
DIC

ATOM
198
C
PRO
27
53.810
53.046
57.592
1.00
15.06
DIC

ATOM
199
O
PRO
27
54.397
52.425
56.696
1.00
15.60
DIC

ATOM
200
N
ASP
28
54.149
52.936
58.874
1.00
13.42
DIC

ATOM
201
CA
ASP
28
55.265
52.074
59.251
1.00
13.91
DIC

ATOM
202
CB
ASP
28
56.401
52.896
59.867
1.00
12.65
DIC

ATOM
203
CG
ASP
28
57.698
52.099
59.970
1.00
13.98
DIC

ATOM
204
OD1
ASP
28
58.008
51.345
59.017
1.00
14.45
DIC

ATOM
205
OD2
ASP
28
58.405
52.229
60.988
1.00
11.69
DIC

ATOM
206
C
ASP
28
54.879
50.946
60.197
1.00
13.78
DIC

ATOM
207
O
ASP
28
55.708
50.445
60.950
1.00
13.88
DIC

ATOM
208
N
THR
29
53.617
50.546
60.160
1.00
14.27
DIC

ATOM
209
CA
THR
29
53.166
49.457
61.011
1.00
15.21
DIC

ATOM
210
CB
THR
29
52.082
49.917
62.001
1.00
15.30
DIC

ATOM
211
OG1
THR
29
52.567
51.025
62.772
1.00
15.73
DIC

ATOM
212
CG2
THR
29
51.732
48.782
62.948
1.00
17.03
DIC

ATOM
213
C
THR
29
52.594
48.339
60.149
1.00
15.61
DIC

ATOM
214
O
THR
29
51.884
48.596
59.176
1.00
14.30
DIC

ATOM
215
N
GLU
30
52.927
47.101
60.499
1.00
16.81
DIC

ATOM
216
CA
GLU
30
52.427
45.936
59.779
1.00
17.79
DIC

ATOM
217
CB
GLU
30
53.187
44.680
60.215
1.00
21.66
DIC

ATOM
218
CG
GLU
30
53.405
43.645
59.115
1.00
28.54
DIC

ATOM
219
CD
GLU
30
54.135
44.217
57.900
1.00
29.87
DIC

ATOM
220
OE1
GLU
30
53.472
44.811
57.024
1.00
31.57
DIC

ATOM
221
OE2
GLU
30
55.375
44.084
57.826
1.00
33.06
DIC

ATOM
222
C
GLU
30
50.957
45.790
60.147
1.00
16.87
DIC

ATOM
223
O
GLU
30
50.617
45.687
61.325
1.00
17.37
DIC

ATOM
224
N
ILE
31
50.082
45.800
59.151
1.00
15.55
DIC

ATOM
225
CA
ILE
31
48.658
45.652
59.418
1.00
15.24
DIC

ATOM
226
CB
ILE
31
47.821
46.802
58.782
1.00
14.65
DIC

ATOM
227
CG2
ILE
31
46.341
46.638
59.150
1.00
15.64
DIC

ATOM
228
CG1
ILE
31
48.323
48.163
59.278
1.00
14.25
DIC

ATOM
229
CD
ILE
31
48.159
48.389
60.765
1.00
15.14
DIC

ATOM
230
C
ILE
31
48.188
44.319
58.849
1.00
14.29
DIC

ATOM
231
O
ILE
31
48.129
44.132
57.634
1.00
14.29
DIC

ATOM
232
N
ARG
32
47.877
43.386
59.739
1.00
13.00
DIC

ATOM
233
CA
ARG
32
47.398
42.081
59.328
1.00
12.73
DIC

ATOM
234
CB
ARG
32
48.045
40.984
60.182
1.00
15.39
DIC

ATOM
235
CG
ARG
32
49.580
40.988
60.101
1.00
21.06
DIC

ATOM
236
CD
ARG
32
50.221
39.798
60.809
1.00
25.85
DIC

ATOM
237
NE
ARG
32
49.830
39.700
62.216
1.00
31.82
DIC

ATOM
238
CZ
ARG
32
50.327
38.808
63.069
1.00
35.29
DIC

ATOM
239
NH1
ARG
32
51.246
37.938
62.657
1.00
36.77
DIC

ATOM
240
NH2
ARG
32
49.897
38.772
64.329
1.00
34.04
DIC

ATOM
241
C
ARG
32
45.884
42.079
59.487
1.00
11.59
DIC

ATOM
242
O
ARG
32
45.365
42.130
60.604
1.00
10.59
DIC

ATOM
243
N
PHE
33
45.190
42.061
58.353
1.00
9.57
DIC

ATOM
244
CA
PHE
33
43.733
42.059
58.314
1.00
11.07
DIC

ATOM
245
CB
PHE
33
43.233
42.709
57.021
1.00
9.65
DIC

ATOM
246
CG
PHE
33
43.473
44.187
56.942
1.00
9.60
DIC

ATOM
247
CD1
PHE
33
42.751
45.069
57.741
1.00
8.83
DIC

ATOM
248
CD2
PHE
33
44.394
44.703
56.034
1.00
10.43
DIC

ATOM
249
CE1
PHE
33
42.939
46.449
57.634
1.00
9.43
DIC.

ATOM
250
CE2
PHE
33
44.590
46.078
55.918
1.00
9.57
DIC

ATOM
251
CZ
PHE
33
43.861
46.953
56.718
1.00
9.32
DIC

ATOM
252
C
PHE
33
43.142
40.652
58.391
1.00
11.46
DIC

ATOM
253
O
PHE
33
43.577
39.741
57.678
1.00
12.46
DIC

ATOM
254
N
HIS
34
42.138
40.495
59.246
1.00
10.60
DIC

ATOM
255
CA
HIS
34
41.437
39.222
59.414
1.00
12.40
DIC

ATOM
256
CB
HIS
34
41.567
38.728
60.859
1.00
11.10
DIC

ATOM
257
CG
HIS
34
42.983
38.591
61.328
1.00
12.97
DIC

ATOM
258
CD2
HIS
34
43.844
39.503
61.841
1.00
12.88
DIC

ATOM
259
ND1
HIS
34
43.667
37.394
61.300
1.00
14.47
DIC

ATOM
260
CE1
HIS
34
44.887
37.574
61.776
1.00
14.13
DIC

ATOM
261
NE2
HIS
34
45.019
38.845
62.113
1.00
14.30
DIC

ATOM
262
C
HIS
34
39.978
39.545
59.103
1.00
12.39
DIC

ATOM
263
O
HIS
34
39.337
40.294
59.840
1.00
12.46
DIC

ATOM
264
N
VAL
35
39.449
38.987
58.019
1.00
10.81
DIC

ATOM
265
CA
VAL
35
38.073
39.280
57.643
1.00
10.52
DIC

ATOM
266
CB
VAL
35
37.991
39.696
56.150
1.00
11.67
DIC

ATOM
267
CG1
VAL
35
36.571
40.115
55.793
1.00
12.07
DIC

ATOM
268
CG2
VAL
35
38.970
40.838
55.875
1.00
11.00
DIC

ATOM
269
C
VAL
35
37.088
38.141
57.878
1.00
11.06
DIC

ATOM
270
O
VAL
35
37.229
37.055
57.307
1.00
10.52
DIC

ATOM
271
N
LEU
36
36.096
38.391
58.730
1.00
10.89
DIC

ATOM
272
CA
LEU
36
35.057
37.401
58.994
1.00
11.46
DIC

ATOM
273
CB
LEU
36
34.272
37.769
60.262
1.00
11.18
DIC

ATOM
274
CG
LEU
36
35.134
37.949
61.527
1.00
11.27
DIC

ATOM
275
CD1
LEU
36
34.224
38.089
62.748
1.00
10.72
DIC

ATOM
276
CD2
LEU
36
36.061
36.750
61.721
1.00
9.09
DIC

ATOM
277
C
LEU
36
34.201
37.528
57.732
1.00
12.89
DIC

ATOM
278
O
LEU
36
33.465
38.501
57.556
1.00
11.93
DIC

ATOM
279
N
ASP
37
34.351
36.547
56.845
1.00
14.29
DIC

ATOM
280
CA
ASP
37
33.694
36.513
55.538
1.00
14.87
DIC

ATOM
281
CB
ASP
37
34.654
35.854
54.538
1.00
17.19
DIC

ATOM
282
CG
ASP
37
34.122
35.845
53.120
1.00
15.95
DIC

ATOM
283
OD1
ASP
37
32.917
36.093
52.917
1.00
16.13
DIC

ATOM
284
OD2
ASP
37
34.920
35.571
52.207
1.00
19.63
DIC

ATOM
285
C
ASP
37
32.362
35.774
55.545
1.00
16.83
DIC

ATOM
286
O
ASP
37
32.320
34.539
55.625
1.00
14.89
DIC

ATOM
287
N
ALA
38
31.275
36.531
55.429
1.00
15.59
DIC

ATOM
288
CA
ALA
38
29.947
35.941
55.447
1.00
18.57
DIC

ATOM
289
CB
ALA
38
29.010
36.795
56.307
1.00
19.77
DIC

ATOM
290
C
ALA
38
29.330
35.719
54.069
1.00
19.75
DIC

ATOM
291
O
ALA
38
28.111
35.689
53.937
1.00
23.40
DIC

ATOM
292
N
GLY
39
30.161
35.560
53.045
1.00
19.13
DIC

ATOM
293
CA
GLY
39
29.627
35.321
51.717
1.00
17.91
DIC

ATOM
294
C
GLY
39
30.163
36.247
50.641
1.00
16.51
DIC

ATOM
295
O
GLY
39
29.486
36.494
49.649
1.00
18.04
DIC

ATOM
296
N
ILE
40
31.371
36.768
50.832
1.00
14.45
DIC

ATOM
297
CA
ILE
40
31.975
37.662
49.848
1.00
14.34
DIC

ATOM
298
CB
ILE
40
33.195
38.400
50.450
1.00
13.99
DIC

ATOM
299
CG2
ILE
40
33.718
39.424
49.460
1.00
13.81
DIC

ATOM
300
CG1
ILE
40
32.788
39.096
51.760
1.00
13.39
DIC

ATOM
301
CD
ILE
40
33.946
39.762
52.517
1.00
13.39
DIC

ATOM
302
C
ILE
40
32.407
36.846
48.621
1.00
14.46
DIC

ATOM
303
O
ILE
40
33.064
35.817
48.751
1.00
14.76
DIC

ATOM
304
N
SER
41
32.029
37.299
47.429
1.00
14.97
DIC

ATOM
305
CA
SER
41
32.376
36.573
46.207
1.00
15.36
DIC

ATOM
306
CB
SER
41
31.711
37.221
44.987
1.00
15.16
DIC

ATOM
307
OG
SER
41
32.356
38.436
44.642
1.00
14.14
DIC

ATOM
308
C
SER
41
33.880
36.531
45.988
1.00
16.18
DIC

ATOM
309
O
SER
41
34.615
37.374
46.504
1.00
17.61
DIC

ATOM
310
N
GLU
42
34.334
35.546
45.219
1.00
16.89
DIC

ATOM
311
CA
GLU
42
35.754
35.406
44.922
1.00
16.48
DIC

ATOM
312
CB
GLU
42
36.008
34.191
44.018
1.00
18.56
DIC

ATOM
313
CG
GLU
42
37.468
34.005
43.605
1.00
20.32
DIC

ATOM
314
CD
GLU
42
37.919
34.923
42.467
1.00
24.54
DIC

ATOM
315
OE1
GLU
42
39.149
35.117
42.326
1.00
27.22
DIC

ATOM
316
OE2
GLU
42
37.064
35.440
41.707
1.00
24.68
DIC

ATOM
317
C
GLU
42
36.249
36.654
44.217
1.00
15.88
DIC

ATOM
318
O
GLU
42
37.381
37.083
44.423
1.00
14.39
DIC

ATOM
319
N
ALA
43
35.399
37.234
43.378
1.00
17.03
DIC

ATOM
320
CA
ALA
43
35.792
38.427
42.640
1.00
17.82
DIC

ATOM
321
CB
ALA
43
34.752
38.758
41.562
1.00
18.48
DIC

ATOM
322
C
ALA
43
35.966
39.605
43.587
1.00
16.49
DIC

ATOM
323
O
ALA
43
36.898
40.396
43.440
1.00
15.18
DIC

ATOM
324
N
ASN
44
35.086
39.717
44.574
1.00
15.20
DIC

ATOM
325
CA
ASN
44
35.200
40.836
45.500
1.00
16.12
DIC

ATOM
326
CB
ASN
44
33.880
41.055
46.248
1.00
15.18
DIC

ATOM
327
CG
ASN
44
32.838
41.754
45.385
1.00
19.28
DIC

ATOM
328
OD1
ASN
44
33.171
42.636
44.586
1.00
19.46
DIC

ATOM
329
ND2
ASN
44
31.571
41.378
45.551
1.00
18.90
DIC

ATOM
330
C
ASN
44
36.372
40.684
46.470
1.00
15.26
DIC

ATOM
331
O
ASN
44
36.961
41.673
46.888
1.00
15.20
DIC

ATOM
332
N
ARG
45
36.724
39.449
46.817
1.00
16.07
DIC

ATOM
333
CA
ARG
45
37.851
39.234
47.712
1.00
16.99
DIC

ATOM
334
CB
ARG
45
37.909
37.769
48.167
1.00
19.65
DIC

ATOM
335
CG
ARG
45
36.581
37.274
48.728
1.00
24.95
DIC

ATOM
336
CD
ARG
45
36.731
36.329
49.909
1.00
30.41
DIC

ATOM
337
NE
ARG
45
37.494
35.125
49.592
1.00
34.93
DIC

ATOM
338
CZ
ARG
45
37.562
34.059
50.387
1.00
38.05
DIC

ATOM
339
NH1
ARG
45
36.907
34.046
51.542
1.00
39.62
DIC

ATOM
340
NH2
ARG
45
38.294
33.007
50.037
1.00
39.66
DIC

ATOM
341
C
ARG
45
39.128
39.620
46.963
1.00
16.64
DIC

ATOM
342
O
ARG
45
40.009
40.267
47.522
1.00
15.53
DIC

ATOM
343
N
ALA
46
39.218
39.242
45.690
1.00
14.76
DIC

ATOM
344
CA
ALA
46
40.396
39.582
44.901
1.00
15.52
DIC

ATOM
345
CB
ALA
46
40.321
38.933
43.514
1.00
16.34
DIC

ATOM
346
C
ALA
46
40.499
41.099
44.763
1.00
15.93
DIC

ATOM
347
O
ALA
46
41.581
41.669
44.890
1.00
16.56
DIC

ATOM
348
N
ALA
47
39.367
41.753
44.514
1.00
15.64
DIC

ATOM
349
CA
ALA
47
39.358
43.204
44.355
1.00
15.26
DIC

ATOM
350
CB
ALA
47
37.985
43.671
43.903
1.00
14.76
DIC

ATOM
351
C
ALA
47
39.762
43.918
45.643
1.00
14.97
DIC

ATOM
352
O
ALA
47
40.498
44.897
45.612
1.00
15.32
DIC

ATOM
353
N
VAL
48
39.274
43.435
46.781
1.00
14.13
DIC

ATOM
354
CA
VAL
48
39.632
44.054
48.048
1.00
12.62
DIC

ATOM
355
CB
VAL
48
38.887
43.393
49.229
1.00
11.63
DIC

ATOM
356
CG1
VAL
48
39.427
43.922
50.543
1.00
10.65
DIC

ATOM
357
CG2
VAL
48
37.391
43.675
49.127
1.00
10.00
DIC

ATOM
358
C
VAL
48
41.142
43.927
48.271
1.00
13.29
DIC

ATOM
359
O
VAL
48
41.810
44.899
48.612
1.00
12.89
DIC

ATOM
360
N
ALA
49
41.676
42.726
48.062
1.00
13.20
DIC

ATOM
361
CA
ALA
49
43.099
42.476
48.257
1.00
15.72
DIC

ATOM
362
CB
ALA
49
43.389
40.974
48.140
1.00
14.62
DIC

ATOM
363
C
ALA
49
43.977
43.255
47.282
1.00
17.17
DIC

ATOM
364
O
ALA
49
45.025
43.776
47.666
1.00
18.51
DIC

ATOM
365
N
ALA
50
43.549
43.342
46.026
1.00
17.97
DIC

ATOM
366
CA
ALA
50
44.321
44.057
45.012
1.00
19.51
DIC

ATOM
367
CB
ALA
50
43.651
43.915
43.643
1.00
19.91
DIC

ATOM
368
C
ALA
50
44.514
45.539
45.335
1.00
19.92
DIC

ATOM
369
O
ALA
50
45.414
46.178
44.796
1.00
20.21
DIC

ATOM
370
N
ASN
51
43.666
46.089
46.200
1.00
19.48
DIC

ATOM
371
CA
ASN
51
43.770
47.505
46.565
1.00
18.23
DIC

ATOM
372
CB
ASN
51
42.379
48.125
46.722
1.00
16.61
DIC

ATOM
373
CG
ASN
51
41.690
48.369
45.391
1.00
17.51
DIC

ATOM
374
OD1
ASN
51
42.160
49.161
44.577
1.00
18.25
DIC

ATOM
375
ND2
ASN
51
40.570
47.689
45.165
1.00
15.70
DIC

ATOM
376
C
ASN
51
44.551
47.733
47.855
1.00
18.98
DIC

ATOM
377
O
ASN
51
44.802
48.877
48.241
1.00
18.73
DIC

ATOM
378
N
LEU
52
44.929
46.657
48.533
1.00
18.72
DIC

ATOM
379
CA
LEU
52
45.671
46.812
49.778
1.00
20.64
DIC

ATOM
380
CB
LEU
52
45.208
45.778
50.805
1.00
18.56
DIC

ATOM
381
CG
LEU
52
43.701
45.819
51.069
1.00
18.19
DIC

ATOM
382
CD1
LEU
52
43.336
44.772
52.106
1.00
19.78
DIC

ATOM
383
CD2
LEU
52
43.292
47.202
51.529
1.00
18.99
DIC

ATOM
384
C
LEU
52
47.171
46.702
49.554
1.00
22.97
DIC

ATOM
385
O
LEU
52
47.626
46.310
48.476
1.00
21.94
DIC

ATOM
386
N
ARG
53
47.931
47.057
50.583
1.00
24.82
DIC

ATOM
387
CA
ARG
53
49.387
47.024
50.523
1.00
28.21
DIC

ATOM
388
CB
ARG
53
49.966
47.479
51.878
1.00
27.92
DIC

ATOM
389
CG
ARG
53
50.738
48.796
51.811
1.00
26.01
DIC

ATOM
390
CD
ARG
53
50.572
49.669
53.069
1.00
26.38
DIC

ATOM
391
NE
ARG
53
50.831
48.945
54.310
1.00
21.46
DIC

ATOM
392
CZ
ARG
53
50.875
49.507
55.516
1.00
22.17
DIC

ATOM
393
NH1
ARG
53
50.682
50.814
55.662
1.00
22.29
DIC

ATOM
394
NH2
ARG
53
51.098
48.757
56.585
1.00
18.63
DIC

ATOM
395
C
ARG
53
49.931
45.650
50.136
1.00
29.98
DIC

ATOM
396
O
ARG
53
49.397
44.613
50.534
1.00
30.96
DIC

ATOM
397
N
GLY
54
50.989
45.655
49.333
1.00
32.74
DIC

ATOM
398
CA
GLY
54
51.606
44.414
48.903
1.00
34.79
DIC

ATOM
399
C
GLY
54
50.684
43.486
48.136
1.00
37.38
DIC

ATOM
400
O
GLY
54
50.848
42.263
48.190
1.00
37.61
DIC

ATOM
401
N
GLY
55
49.718
44.061
47.421
1.00
37.91
DIC

ATOM
402
CA
GLY
55
48.782
43.259
46.654
1.00
38.40
DIC

ATOM
403
C
GLY
55
47.822
42.468
47.526
1.00
38.63
DIC

ATOM
404
O
GLY
55
47.220
41.492
47.077
1.00
38.78
DIC

ATOM
405
N
GLY
56
47.678
42.887
48.779
1.00
38.50
DIC

ATOM
406
CA
GLY
56
46.780
42.198
49.685
1.00
38.47
DIC

ATOM
407
C
GLY
56
47.417
40.973
50.309
1.00
38.75
DIC

ATOM
408
O
GLY
56
46.747
39.964
50.534
1.00
40.02
DIC

ATOM
409
N
GLY
57
48.716
41.061
50.586
1.00
37.85
DIC

ATOM
410
CA
GLY
57
49.424
39.948
51.193
1.00
35.96
DIC

ATOM
411
C
GLY
57
49.144
39.855
52.682
1.00
34.60
DIC

ATOM
412
O
GLY
57
49.441
38.845
53.321
1.00
34.23
DIC

ATOM
413
N
ASN
58
48.568
40.914
53.241
1.00
33.21
DIC

ATOM
414
CA
ASN
58
48.250
40.933
54.664
1.00
31.01
DIC

ATOM
415
CB
ASN
58
48.877
42.154
55.328
1.00
33.87
DIC

ATOM
416
CG
ASN
58
50.322
41.922
55.706
1.00
37.81
DIC

ATOM
417
OD1
ASN
58
50.618
41.127
56.604
1.00
38.68
DIC

ATOM
418
ND2
ASN
58
51.234
42.603
55.016
1.00
39.42
DIC

ATOM
419
C
ASN
58
46.763
40.889
54.965
1.00
28.44
DIC

ATOM
420
O
ASN
58
46.279
41.588
55.861
1.00
25.75
DIC

ATOM
421
N
ILE
59
46.035
40.070
54.211
1.00
24.88
DIC

ATOM
422
CA
ILE
59
44.607
39.927
54.445
1.00
23.41
DIC

ATOM
423
CB
ILE
59
43.763
40.859
53.526
1.00
23.71
DIC

ATOM
424
CG2
ILE
59
43.989
40.514
52.055
1.00
22.32
DIC

ATOM
425
CG1
ILE
59
42.282
40.740
53.909
1.00
21.89
DIC

ATOM
426
CD
ILE
59
41.398
41.852
53.361
1.00
22.80
DIC

ATOM
427
C
ILE
59
44.167
38.482
54.264
1.00
22.27
DIC

ATOM
428
O
ILE
59
44.400
37.863
53.221
1.00
21.93
DIC

ATOM
429
N
ARG
60
43.550
37.945
55.308
1.00
20.40
DIC

ATOM
430
CA
ARG
60
43.062
36.574
55.300
1.00
19.40
DIC

ATOM
431
CB
ARG
60
43.748
35.769
56.417
1.00
20.70
DIC

ATOM
432
CG
ARG
60
43.338
34.300
56.513
1.00
25.16
DIC

ATOM
433
CD
ARG
60
44.461
33.403
57.069
1.00
29.20
DIC

ATOM
434
NE
ARG
60
44.896
33.763
58.418
1.00
33.94
DIC

ATOM
435
CZ
ARG
60
45.736
34.757
58.707
1.00
36.79
DIC

ATOM
436
NH1
ARG
60
46.250
35.507
57.740
1.00
38.29
DIC

ATOM
437
NH2
ARG
60
46.068
35.000
59.971
1.00
36.32
DIC

ATOM
438
C
ARG
60
41.554
36.613
55.508
1.00
18.67
DIC

ATOM
439
O
ARG
60
41.062
37.256
56.441
1.00
19.14
DIC

ATOM
440
N
PHE
61
40.820
35.959
54.615
1.00
15.54
DIC

ATOM
441
CA
PHE
61
39.369
35.904
54.722
1.00
16.16
DIC

ATOM
442
CB
PHE
61
38.713
35.924
53.333
1.00
14.93
DIC

ATOM
443
CG
PHE
61
38.885
37.230
52.601
1.00
12.73
DIC

ATOM
444
CD1
PHE
61
39.989
37.448
51.786
1.00
13.77
DIC

ATOM
445
CD2
PHE
61
37.958
38.258
52.763
1.00
11.24
DIC

ATOM
446
CE1
PHE
61
40.170
38.677
51.143
1.00
14.58
DIC

ATOM
447
CE2
PHE
61
38.128
39.482
52.131
1.00
12.41
DIC

ATOM
448
CZ
PHE
61
39.236
39.696
51.319
1.00
11.76
DIC

ATOM
449
C
PHE
61
39.026
34.613
55.448
1.00
16.95
DIC

ATOM
450
O
PHE
61
39.542
33.554
55.105
1.00
18.27
DIC

ATOM
451
N
ILE
62
38.176
34.714
56.467
1.00
17.58
DIC

ATOM
452
CA
ILE
62
37.767
33.560
57.264
1.00
16.19
DIC

ATOM
453
CB
ILE
62
38.022
33.809
58.770
1.00
16.81
DIC

ATOM
454
CG2
ILE
62
37.808
32.521
59.560
1.00
15.43
DIC

ATOM
455
CG1
ILE
62
39.443
34.321
58.987
1.00
17.10
DIC

ATOM
456
CD
ILE
62
39.684
34.852
60.390
1.00
19.03
DIC

ATOM
457
C
ILE
62
36.271
33.328
57.075
1.00
16.68
DIC

ATOM
458
O
ILE
62
35.456
34.150
57.495
1.00
13.95
DIC

ATOM
459
N
ASP
63
35.911
32.207
56.457
1.00
17.73
DIC

ATOM
460
CA
ASP
63
34.507
31.906
56.219
1.00
20.50
DIC

ATOM
461
CB
ASP
63
34.354
30.648
55.352
1.00
24.57
DIC

ATOM
462
CG
ASP
63
34.848
30.853
53.926
1.00
28.34
DIC

ATOM
463
OD1
ASP
63
34.508
31.890
53.317
1.00
31.73
DIC

ATOM
464
OD2
ASP
63
35.566
29.971
53.412
1.00
32.70
DIC

ATOM
465
C
ASP
63
33.716
31.723
57.504
1.00
20.66
DIC

ATOM
466
O
ASP
63
34.147
31.036
58.436
1.00
20.12
DIC

ATOM
467
N
VAL
64
32.557
32.363
57.549
1.00
20.64
DIC

ATOM
468
CA
VAL
64
31.662
32.254
58.686
1.00
20.45
DIC

ATOM
469
CB
VAL
64
31.601
33.569
59.498
1.00
22.06
DIC

ATOM
470
CG1
VAL
64
32.985
33.917
60.013
1.00
22.97
DIC

ATOM
471
CG2
VAL
64
31.056
34.696
58.645
1.00
22.72
DIC

ATOM
472
C
VAL
64
30.290
31.924
58.116
1.00
20.57
DIC

ATOM
473
O
VAL
64
29.936
32.377
57.024
1.00
20.54
DIC

ATOM
474
N
ASN
65
29.536
31.107
58.840
1.00
19.87
DIC

ATOM
475
CA
ASN
65
28.203
30.709
58.406
1.00
20.85
DIC

ATOM
476
CB
ASN
65
27.898
29.282
58.869
1.00
21.23
DIC

ATOM
477
CG
ASN
65
26.615
28.732
58.264
1.00
24.15
DIC

ATOM
478
OD1
ASN
65
25.670
29.478
57.988
1.00
24.03
DIC

ATOM
479
ND2
ASN
65
26.572
27.418
58.067
1.00
22.28
DIC

ATOM
480
C
ASN
65
27.195
31.666
59.034
1.00
21.32
DIC

ATOM
481
O
ASN
65
26.916
31.586
60.229
1.00
20.43
DIC

ATOM
482
N
PRO
66
26.625
32.575
58.231
1.00
21.57
DIC

ATOM
483
CD
PRO
66
26.755
32.695
56.768
1.00
22.50
DIC

ATOM
484
CA
PRO
66
25.649
33.535
58.754
1.00
22.52
DIC

ATOM
485
CB
PRO
66
25.280
34.359
57.519
1.00
23.12
DIC

ATOM
486
CG
PRO
66
25.471
33.391
56.392
1.00
22.95
DIC

ATOM
487
C
PRO
66
24.440
32.880
59.421
1.00
21.35
DIC

ATOM
488
O
PRO
66
23.817
33.467
60.306
1.00
20.47
DIC

ATOM
489
N
ALA
67
24.124
31.657
59.009
1.00
20.26
DIC

ATOM
490
CA
ALA
67
22.992
30.937
59.577
1.00
20.00
DIC

ATOM
491
CB
ALA
67
22.771
29.619
58.823
1.00
21.70
DIC

ATOM
492
C
ALA
67
23.180
30.662
61.069
1.00
20.28
DIC

ATOM
493
O
ALA
67
22.202
30.487
61.797
1.00
19.39
DIC

ATOM
494
N
ASP
68
24.430
30.624
61.527
1.00
18.25
DIC

ATOM
495
CA
ASP
68
24.702
30.366
62.937
1.00
17.98
DIC

ATOM
496
CB
ASP
68
26.196
30.512
63.249
1.00
18.00
DIC

ATOM
497
CG
ASP
68
27.037
29.385
62.680
1.00
19.22
DIC

ATOM
498
OD1
ASP
68
28.264
29.391
62.924
1.00
20.73
DIC

ATOM
499
OD2
ASP
68
26.488
28.500
61.994
1.00
21.66
DIC

ATOM
500
C
ASP
68
23.941
31.323
63.853
1.00
17.42
DIC

ATOM
501
O
ASP
68
23.596
30.971
64.981
1.00
16.39
DIC

ATOM
502
N
PHE
69
23.679
32.531
63.371
1.00
16.56
DIC

ATOM
503
CA
PHE
69
23.005
33.527
64.192
1.00
18.20
DIC

ATOM
504
CB
PHE
69
23.823
34.821
64.160
1.00
18.04
DIC

ATOM
505
CG
PHE
69
25.314
34.583
64.118
1.00
18.37
DIC

ATOM
506
CD1
PHE
69
25.983
34.473
62.898
1.00
18.98
DIC

ATOM
507
CD2
PHE
69
26.039
34.431
65.293
1.00
16.47
DIC

ATOM
508
CE1
PHE
69
27.354
34.215
62.852
1.00
18.40
DIC

ATOM
509
CE2
PHE
69
27.410
34.172
65.264
1.00
16.90
DIC

ATOM
510
CZ
PHE
69
28.071
34.063
64.039
1.00
18.55
DIC

ATOM
511
C
PHE
69
21.565
33.796
63.778
1.00
20.05
DIC

ATOM
512
O
PHE
69
20.965
34.796
64.181
1.00
19.59
DIC

ATOM
513
N
ALA
70
21.004
32.884
62.995
1.00
21.70
DIC

ATOM
514
CA
ALA
70
19.638
33.030
62.509
1.00
23.13
DIC

ATOM
515
CB
ALA
70
19.253
31.812
61.678
1.00
24.32
DIC

ATOM
516
C
ALA
70
18.597
33.257
63.603
1.00
24.21
DIC

ATOM
517
O
ALA
70
17.553
33.857
63.348
1.00
25.81
DIC

ATOM
518
N
GLY
71
18.867
32.782
64.814
1.00
23.19
DIC

ATOM
519
CA
GLY
71
17.901
32.964
65.883
1.00
23.35
DIC

ATOM
520
C
GLY
71
17.929
34.315
66.583
1.00
22.92
DIC

ATOM
521
O
GLY
71
17.009
34.642
67.338
1.00
21.65
DIC

ATOM
522
N
PHE
72
18.966
35.109
66.331
1.00
21.05
DIC

ATOM
523
CA
PHE
72
19.105
36.415
66.976
1.00
20.69
DIC

ATOM
524
CB
PHE
72
20.592
36.786
67.069
1.00
20.82
DIC

ATOM
525
CG
PHE
72
21.414
35.823
67.901
1.00
22.40
DIC

ATOM
526
CD1
PHE
72
22.787
36.003
68.041
1.00
21.53
DIC

ATOM
527
CD2
PHE
72
20.817
34.737
68.540
1.00
22.26
DIC

ATOM
528
CE1
PHE
72
23.554
35.116
68.803
1.00
23.86
DIC

ATOM
529
CE2
PHE
72
21.573
33.843
69.305
1.00
23.97
DIC

ATOM
530
CZ
PHE
72
22.946
34.033
69.437
1.00
23.46
DIC

ATOM
531
C
PHE
72
18.316
37.539
66.296
1.00
20.09
DIC

ATOM
532
O
PHE
72
18.196
37.579
65.074
1.00
21.80
DIC

ATOM
533
N
PRO
73
17.783
38.480
67.090
1.00
19.37
DIC

ATOM
534
CD
PRO
73
18.031
38.670
68.529
1.00
19.40
DIC

ATOM
535
CA
PRO
73
17.002
39.599
66.558
1.00
18.84
DIC

ATOM
536
CB
PRO
73
16.675
40.418
67.807
1.00
19.67
DIC

ATOM
537
CG
PRO
73
17.826
40.159
68.687
1.00
19.66
DIC

ATOM
538
C
PRO
73
17.711
40.418
65.495
1.00
18.90
DIC

ATOM
539
O
PRO
73
18.905
40.705
65.596
1.00
16.76
DIC

ATOM
540
N
LEU
74
16.956
40.790
64.470
1.00
18.84
DIC

ATOM
541
CA
LEU
74
17.493
41.583
63.378
1.00
21.06
DIC

ATOM
542
CB
LEU
74
17.769
40.673
62.176
1.00
22.16
DIC

ATOM
543
CG
LEU
74
18.916
41.043
61.231
1.00
22.74
DIC

ATOM
544
CD1
LEU
74
20.240
41.080
61.989
1.00
23.10
DIC

ATOM
545
CD2
LEU
74
18.983
40.026
60.114
1.00
23.73
DIC

ATOM
546
C
LEU
74
16.438
42.637
63.040
1.00
21.30
DIC

ATOM
547
O
LEU
74
15.758
42.540
62.021
1.00
22.75
DIC

ATOM
548
N
ASN
75
16.308
43.634
63.915
1.00
21.53
DIC

ATOM
549
CA
ASN
75
15.329
44.708
63.749
1.00
20.41
DIC

ATOM
550
CB
ASN
75
14.716
45.101
65.125
1.00
22.53
DIC

ATOM
551
CG
ASN
75
15.767
45.292
66.259
1.00
25.80
DIC

ATOM
552
OD1
ASN
75
16.458
44.349
66.665
1.00
23.29
DIC

ATOM
553
ND2
ASN
75
15.854
46.520
66.791
1.00
26.49
DIC

ATOM
554
C
ASN
75
15.822
45.968
63.012
1.00
20.20
DIC

ATOM
555
O
ASN
75
15.036
46.654
62.355
1.00
18.24
DIC

ATOM
556
N
ILE
76
17.116
46.265
63.111
1.00
16.30
DIC

ATOM
557
CA
ILE
76
17.676
47.450
62.467
1.00
14.30
DIC

ATOM
558
CB
ILE
76
18.998
47.836
63.155
1.00
15.53
DIC

ATOM
559
CG2
ILE
76
19.496
49.183
62.643
1.00
14.83
DIC

ATOM
560
CG1
ILE
76
18.753
47.925
64.668
1.00
15.63
DIC

ATOM
561
CD
ILE
76
20.000
48.191
65.496
1.00
16.08
DIC

ATOM
562
C
ILE
76
17.869
47.172
60.976
1.00
13.06
DIC

ATOM
563
O
ILE
76
18.732
46.398
60.578
1.00
11.46
DIC

ATOM
564
N
ARG
77
17.036
47.813
60.161
1.00
12.41
DIC

ATOM
565
CA
ARG
77
17.033
47.606
58.719
1.00
11.27
DIC

ATOM
566
CB
ARG
77
16.016
48.544
58.071
1.00
11.91
DIC

ATOM
567
CG
ARG
77
15.774
48.285
56.589
1.00
14.32
DIC

ATOM
568
CD
ARG
77
14.766
49.291
56.023
1.00
17.97
DIC

ATOM
569
NE
ARG
77
14.418
48.999
54.637
1.00
19.40
DIC

ATOM
570
CZ
ARG
77
14.017
49.909
53.755
1.00
20.80
DIC

ATOM
571
NH1
ARG
77
13.910
51.182
54.108
1.00
20.49
DIC

ATOM
572
NH2
ARG
77
13.730
49.543
52.512
1.00
20.14
DIC

ATOM
573
C
ARG
77
18.363
47.718
57.980
1.00
10.68
DIC

ATOM
574
O
ARG
77
18.642
46.905
57.102
1.00
9.93
DIC

ATOM
575
N
HIS
78
19.184
48.709
58.318
1.00
9.86
DIC

ATOM
576
CA
HIS
78
20.455
48.876
57.613
1.00
11.66
DIC

ATOM
577
CB
HIS
78
20.975
50.316
57.782
1.00
12.15
DIC

ATOM
578
CG
HIS
78
21.469
50.635
59.160
1.00
11.23
DIC

ATOM
579
CD2
HIS
78
20.830
51.149
60.238
1.00
9.90
DIC

ATOM
580
ND1
HIS
78
22.779
50.447
59.545
1.00
14.19
DIC

ATOM
581
CE1
HIS
78
22.927
50.834
60.801
1.00
11.70
DIC

ATOM
582
NE2
HIS
78
21.758
51.264
61.244
1.00
13.16
DIC

ATOM
583
C
HIS
78
21.537
47.879
58.022
1.00
11.09
DIC

ATOM
584
O
HIS
78
22.637
47.898
57.474
1.00
10.55
DIC

ATOM
585
N
ILE
79
21.219
46.989
58.961
1.00
9.64
DIC

ATOM
586
CA
ILE
79
22.199
46.016
59.438
1.00
8.79
DIC

ATOM
587
CB
ILE
79
22.327
46.110
60.980
1.00
8.64
DIC

ATOM
588
CG2
ILE
79
23.316
45.068
61.493
1.00
7.07
DIC

ATOM
589
CG1
ILE
79
22.762
47.529
61.374
1.00
8.17
DIC

ATOM
590
CD
ILE
79
22.723
47.807
62.875
1.00
9.48
DIC

ATOM
591
C
ILE
79
21.874
44.568
59.053
1.00
10.57
DIC

ATOM
592
O
ILE
79
20.769
44.088
59.298
1.00
10.81
DIC

ATOM
593
N
SER
80
22.838
43.871
58.453
1.00
11.32
DIC

ATOM
594
CA
SER
80
22.632
42.473
58.065
1.00
10.85
DIC

ATOM
595
CB
SER
80
23.416
42.135
56.800
1.00
11.37
DIC

ATOM
596
OG
SER
80
24.804
42.239
57.045
1.00
11.89
DIC

ATOM
597
C
SER
80
23.098
41.556
59.193
1.00
11.08
DIC

ATOM
598
O
SER
80
23.788
41.999
60.117
1.00
11.39
DIC

ATOM
599
N
ILE
81
22.722
40.281
59.094
1.00
10.23
DIC

ATOM
600
CA
ILE
81
23.038
39.251
60.087
1.00
12.43
DIC

ATOM
601
CB
ILE
81
22.449
37.868
59.640
1.00
13.92
DIC

ATOM
602
CG2
ILE
81
23.114
37.404
58.354
1.00
14.49
DIC

ATOM
603
CG1
ILE
81
22.637
36.816
60.738
1.00
16.79
DIC

ATOM
604
CD
ILE
81
21.858
37.101
62.008
1.00
21.00
DIC

ATOM
605
C
ILE
81
24.533
39.113
60.388
1.00
11.38
DIC

ATOM
606
O
ILE
81
24.921
38.716
61.483
1.00
11.02
DIC

ATOM
607
N
THR
82
25.368
39.460
59.421
1.00
11.66
DIC

ATOM
608
CA
THR
82
26.816
39.382
59.590
1.00
13.55
DIC

ATOM
609
CB
THR
82
27.525
39.881
58.309
1.00
12.95
DIC

ATOM
610
OG1
THR
82
27.238
38.981
57.235
1.00
15.78
DIC

ATOM
611
OG2
THR
82
29.027
39.953
58.505
1.00
13.95
DIC

ATOM
612
C
THR
82
27.305
40.193
60.801
1.00
13.04
DIC

ATOM
613
O
THR
82
28.423
40.001
61.283
1.00
14.43
DIC

ATOM
614
N
THR
83
26.468
41.100
61.293
1.00
12.94
DIC

ATOM
615
CA
THR
83
26.843
41.925
62.444
1.00
10.16
DIC

ATOM
616
CB
THR
83
25.762
42.993
62.736
1.00
8.84
DIC

ATOM
617
OG1
THR
83
26.255
43.900
63.729
1.00
8.21
DIC

ATOM
618
CG2
THR
83
24.473
42.345
63.242
1.00
7.30
DIC

ATOM
619
C
THR
83
27.079
41.088
63.712
1.00
9.87
DIC

ATOM
620
O
THR
83
27.744
41.536
64.654
1.00
8.73
DIC

ATOM
621
N
TYR
84
26.545
39.869
63.732
1.00
8.10
DIC

ATOM
622
CA
TYR
84
26.719
38.990
64.889
1.00
9.50
DIC

ATOM
623
CB
TYR
84
25.508
38.073
65.061
1.00
8.94
DIC

ATOM
624
CG
TYR
84
24.278
38.731
65.627
1.00
10.26
DIC

ATOM
625
CD1
TYR
84
23.194
39.044
64.805
1.00
10.22
DIC

ATOM
626
CE1
TYR
84
22.036
39.613
65.327
1.00
10.08
DIC

ATOM
627
CD2
TYR
84
24.179
39.011
66.994
1.00
10.47
DIC

ATOM
628
CE2
TYR
84
23.028
39.581
67.527
1.00
9.14
DIC

ATOM
629
CZ
TYR
84
21.959
39.875
66.685
1.00
10.95
DIC

ATOM
630
OH
TYR
84
20.806
40.406
67.205
1.00
13.06
DIC

ATOM
631
C
TYR
84
27.965
38.104
64.835
1.00
9.18
DIC

ATOM
632
O
TYR
84
28.314
37.471
65.832
1.00
10.15
DIC

ATOM
633
N
ALA
85
28.641
38.054
63.689
1.00
9.06
DIC

ATOM
634
CA
ALA
85
29.814
37.185
63.554
1.00
8.72
DIC

ATOM
635
CB
ALA
85
30.394
37.294
62.145
1.00
9.77
DIC

ATOM
636
C
ALA
85
30.912
37.423
64.581
1.00
9.19
DIC

ATOM
637
O
ALA
85
31.599
36.486
64.993
1.00
8.82
DIC

ATOM
638
N
ARG
86
31.074
38.669
65.003
1.00
9.47
DIC

ATOM
639
CA
ARG
86
32.111
39.003
65.966
1.00
9.96
DIC

ATOM
640
CB
ARG
86
32.051
40.502
66.294
1.00
9.71
DIC

ATOM
641
CG
ARG
86
30.811
40.949
67.048
1.00
9.90
DIC

ATOM
642
CD
ARG
86
30.656
42.466
67.001
1.00
8.17
DIC

ATOM
643
NE
ARG
86
29.919
42.902
65.815
1.00
7.34
DIC

ATOM
644
CZ
ARG
86
29.791
44.169
65.430
1.00
8.06
DIC

ATOM
645
NH1
ARG
86
30.357
45.142
66.133
1.00
6.00
DIC

ATOM
646
NH2
ARG
86
29.079
44.464
64.347
1.00
8.41
DIC

ATOM
647
C
ARG
86
32.016
38.165
67.243
1.00
9.15
DIC

ATOM
648
O
ARG
86
33.030
37.911
67.896
1.00
9.85
DIC

ATOM
649
N
LEU
87
30.809
37.724
67.593
1.00
10.06
DIC

ATOM
650
CA
LEU
87
30.607
36.909
68.799
1.00
10.59
DIC

ATOM
651
CB
LEU
87
29.124
36.563
68.957
1.00
11.67
DIC

ATOM
652
CG
LEU
87
28.147
37.736
69.102
1.00
12.74
DIC

ATOM
653
CD1
LEU
87
26.726
37.198
69.137
1.00
13.49
DIC

ATOM
654
CD2
LEU
87
28.456
38.527
70.368
1.00
11.69
DIC

ATOM
655
C
LEU
87
31.435
35.613
68.832
1.00
11.32
DIC

ATOM
656
O
LEU
87
31.747
35.096
69.907
1.00
9.34
DIC

ATOM
657
N
LYS
88
31.781
35.085
67.658
1.00
12.29
DIC

ATOM
658
CA
LYS
88
32.575
33.849
67.575
1.00
12.77
DIC

ATOM
659
CB
LYS
88
31.995
32.914
66.506
1.00
13.12
DIC

ATOM
660
CG
LYS
88
30.724
32.181
66.926
1.00
14.09
DIC

ATOM
661
CD
LYS
88
30.390
31.098
65.907
1.00
14.18
DIC

ATOM
662
CE
LYS
88
29.287
30.182
66.387
1.00
16.96
DIC

ATOM
663
NZ
LYS
88
29.049
29.101
65.386
1.00
15.57
DIC

ATOM
664
C
LYS
88
34.043
34.120
67.252
1.00
12.47
DIC

ATOM
665
O
LYS
88
34.755
33.247
66.754
1.00
13.10
DIC

ATOM
666
N
LEU
89
34.495
35.332
67.540
1.00
11.63
DIC

ATOM
667
CA
LEU
89
35.874
35.710
67.263
1.00
13.26
DIC

ATOM
668
CB
LEU
89
36.117
37.141
67.760
1.00
14.71
DIC

ATOM
669
CG
LEU
89
36.901
38.093
66.853
1.00
18.28
DIC

ATOM
670
CD1
LEU
89
36.517
37.918
65.401
1.00
18.01
DIC

ATOM
671
CD2
LEU
89
36.632
39.520
67.302
1.00
19.23
DIC

ATOM
672
C
LEU
89
36.854
34.725
67.906
1.00
13.22
DIC

ATOM
673
O
LEU
89
37.878
34.378
67.314
1.00
14.28
DIC

ATOM
674
N
GLY
90
36.528
34.262
69.109
1.00
12.35
DIC

ATOM
675
CA
GLY
90
37.381
33.310
69.797
1.00
12.11
DIC

ATOM
676
C
GLY
90
37.553
32.001
69.041
1.00
14.28
DIC

ATOM
677
O
GLY
90
38.561
31.310
69.213
1.00
12.59
DIC

ATOM
678
N
GLU
91
36.577
31.667
68.197
1.00
14.29
DIC

ATOM
679
CA
GLU
91
36.612
30.440
67.395
1.00
15.06
DIC

ATOM
680
CB
GLU
91
35.194
29.912
67.159
1.00
16.79
DIC

ATOM
681
CG
GLU
91
34.447
29.384
68.383
1.00
19.76
DIC

ATOM
682
CD
GLU
91
33.104
28.774
67.992
1.00
23.18
DIC

ATOM
683
OE1
GLU
91
33.086
27.933
67.064
1.00
22.19
DIC

ATOM
684
OE2
GLU
91
32.071
29.132
68.606
1.00
23.20
DIC

ATOM
685
C
GLU
91
37.259
30.635
66.016
1.00
14.78
DIC

ATOM
686
O
GLU
91
37.855
29.705
65.465
1.00
14.56
DIC

ATOM
687
N
TYR
92
37.119
31.839
65.467
1.00
14.84
DIC

ATOM
688
CA
TYR
92
37.636
32.175
64.140
1.00
16.06
DIC

ATOM
689
CB
TYR
92
36.850
33.354
63.549
1.00
14.49
DIC

ATOM
690
CG
TYR
92
35.356
33.128
63.399
1.00
15.73
DIC

ATOM
691
CD1
TYR
92
34.856
31.930
62.889
1.00
15.13
DIC

ATOM
692
CE1
TYR
92
33.483
31.741
62.698
1.00
16.39
DIC

ATOM
693
CD2
TYR
92
34.445
34.139
63.720
1.00
15.08
DIC

ATOM
694
CE2
TYR
92
33.073
33.962
63.532
1.00
16.55
DIC

ATOM
695
CZ
TYR
92
32.601
32.762
63.019
1.00
15.33
DIC

ATOM
696
OH
TYR
92
31.254
32.591
62.813
1.00
15.89
DIC

ATOM
697
C
TYR
92
39.122
32.516
64.050
1.00
16.64
DIC

ATOM
698
O
TYR
92
39.749
32.286
63.025
1.00
18.19
DIC

ATOM
699
N
ILE
93
39.680
33.084
65.109
1.00
18.45
DIC

ATOM
700
CA
ILE
93
41.085
33.468
65.089
1.00
19.66
DIC

ATOM
701
CB
ILE
93
41.221
35.001
65.239
1.00
20.11
DIC

ATOM
702
CG2
ILE
93
42.690
35.389
65.380
1.00
18.82
DIC

ATOM
703
CG1
ILE
93
40.562
35.684
64.031
1.00
19.68
DIC

ATOM
704
CD
ILE
93
40.589
37.195
64.072
1.00
20.89
DIC

ATOM
705
C
ILE
93
41.880
32.761
66.175
1.00
20.25
DIC

ATOM
706
O
ILE
93
41.553
32.845
67.361
1.00
19.56
DIC

ATOM
707
N
ALA
94
42.934
32.070
65.763
1.00
20.40
DIC

ATOM
708
CA
ALA
94
43.753
31.323
66.705
1.00
23.20
DIC

ATOM
709
CB
ALA
94
43.888
29.890
66.226
1.00
23.20
DIC

ATOM
710
C
ALA
94
45.136
31.923
66.921
1.00
24.59
DIC

ATOM
711
O
ALA
94
45.707
31.804
68.009
1.00
24.30
DIC

ATOM
712
N
ASP
95
45.660
32.574
65.888
1.00
26.69
DIC

ATOM
713
CA
ASP
95
46.995
33.163
65.930
1.00
29.50
DIC

ATOM
714
CB
ASP
95
47.572
33.219
64.509
1.00
31.58
DIC

ATOM
715
CG
ASP
95
46.640
33.908
63.524
1.00
35.84
DIC

ATOM
716
OD1
ASP
95
47.039
34.104
62.355
1.00
38.60
DIC

ATOM
717
OD2
ASP
95
45.504
34.252
63.913
1.00
38.61
DIC

ATOM
718
C
ASP
95
47.147
34.542
66.580
1.00
29.37
DIC

ATOM
719
O
ASP
95
48.141
35.224
66.333
1.00
31.82
DIC

ATOM
720
N
GYS
96
46.193
34.958
67.408
1.00
26.90
DIC

ATOM
721
CA
GYS
96
46.298
36.268
68.052
1.00
25.49
DIC

ATOM
722
CB
GYS
96
45.516
37.325
67.260
1.00
25.52
DIC

ATOM
723
SG
GYS
96
46.072
37.567
65.572
1.00
24.86
DIC

ATOM
724
C
GYS
96
45.793
36.288
69.484
1.00
24.23
DIC

ATOM
725
O
GYS
96
44.733
35.738
69.785
1.00
25.00
DIC

ATOM
726
N
ASP
97
46.549
36.927
70.368
1.00
22.41
DIC

ATOM
727
CA
ASP
97
46.122
37.044
71.756
1.00
22.45
DIC

ATOM
728
CB
ASP
97
47.326
37.111
72.689
1.00
22.93
DIC

ATOM
729
CG
ASP
97
47.968
35.760
72.901
1.00
24.22
DIC

ATOM
730
OD1
ASP
97
49.053
35.713
73.516
1.00
26.27
DIC

ATOM
731
OD2
ASP
97
47.384
34.748
72.457
1.00
25.38
DIC

ATOM
732
C
ASP
97
45.297
38.317
71.891
1.00
21.90
DIC

ATOM
733
O
ASP
97
44.517
38.471
72.830
1.00
23.11
DIC

ATOM
734
N
LYS
98
45.473
39.226
70.939
1.00
19.23
DIC

ATOM
735
CA
LYS
98
44.749
40.494
70.948
1.00
18.34
DIC

ATOM
736
CB
LYS
98
45.573
41.576
71.657
1.00
20.35
DIC

ATOM
737
CG
LYS
98
44.979
42.983
71.560
1.00
22.09
DIC

ATOM
738
CD
LYS
98
45.971
44.075
71.993
1.00
22.26
DIC

ATOM
739
CE
LYS
98
46.314
43.997
73.472
1.00
22.69
DIC

ATOM
740
NZ
LYS
98
46.981
45.238
73.980
1.00
20.82
DIC

ATOM
741
C
LYS
98
44.471
40.933
69.519
1.00
16.18
DIC

ATOM
742
O
LYS
98
45.324
40.795
68.642
1.00
13.58
DIC

ATOM
743
N
VAL
99
43.264
41.434
69.284
1.00
14.00
DIC

ATOM
744
CA
VAL
99
42.891
41.917
67.963
1.00
13.34
DIC

ATOM
745
CB
VAL
99
42.064
40.881
67.170
1.00
12.63
DIC

ATOM
746
CG1
VAL
99
42.891
39.626
66.923
1.00
11.07
DIC

ATOM
747
CG2
VAL
99
40.782
40.546
67.922
1.00
13.64
DIC

ATOM
748
C
VAL
99
42.058
43.169
68.141
1.00
13.18
DIC

ATOM
749
O
VAL
99
41.428
43.361
69.180
1.00
12.75
DIC

ATOM
750
N
LEU
100
42.081
44.033
67.136
1.00
11.89
DIC

ATOM
751
CA
LEU
100
41.304
45.257
67.181
1.00
12.48
DIC

ATOM
752
CB
LEU
100
42.183
46.473
66.870
1.00
13.07
DIC

ATOM
753
CG
LEU
100
41.498
47.849
66.824
1.00
16.10
DIC

ATOM
754
CD1
LEU
100
40.525
47.996
67.984
1.00
15.54
DIC

ATOM
755
CD2
LEU
100
42.558
48.940
66.881
1.00
15.51
DIC

ATOM
756
C
LEU
100
40.200
45.122
66.153
1.00
12.39
DIC

ATOM
757
O
LEU
100
40.458
45.100
64.941
1.00
12.90
DIC

ATOM
758
N
TYR
101
38.972
45.014
66.651
1.00
11.19
DIC

ATOM
759
CA
TYR
101
37.802
44.862
65.804
1.00
11.19
DIC

ATOM
760
CB
TYR
101
36.703
44.095
66.539
1.00
13.00
DIC

ATOM
761
CG
TYR
101
35.517
43.788
65.652
1.00
15.87
DIC

ATOM
762
CD1
TYR
101
35.497
42.628
64.881
1.00
18.26
DIC

ATOM
763
CE1
TYR
101
34.440
42.343
64.035
1.00
21.70
DIC

ATOM
764
CD2
TYR
101
34.438
44.667
65.549
1.00
18.95
DIC

ATOM
765
CE2
TYR
101
33.360
44.389
64.690
1.00
21.15
DIC

ATOM
766
CZ
TYR
101
33.376
43.219
63.942
1.00
21.56
DIC

ATOM
767
OH
TYR
101
32.328
42.882
63.115
1.00
26.24
DIC

ATOM
768
C
TYR
101
37.236
46.214
65.392
1.00
10.61
DIC

ATOM
769
O
TYR
101
37.076
47.108
66.228
1.00
9.84
DIC

ATOM
770
N
LEU
102
36.922
46.354
64.108
1.00
9.31
DIC

ATOM
771
CA
LEU
102
36.345
47.588
63.601
1.00
9.32
DIC

ATOM
772
CB
LEU
102
37.359
48.365
62.762
1.00
10.13
DIC

ATOM
773
CG
LEU
102
38.698
48.757
63.390
1.00
11.91
DIC

ATOM
774
CD1
LEU
102
39.612
49.271
62.304
1.00
8.61
DIC

ATOM
775
CD2
LEU
102
38.488
49.797
64.484
1.00
9.84
DIC

ATOM
776
C
LEU
102
35.135
47.298
62.725
1.00
9.76
DIC

ATOM
777
O
LEU
102
35.123
46.319
61.970
1.00
10.61
DIC

ATOM
778
N
ASP
103
34.119
48.149
62.834
1.00
8.81
DIC

ATOM
779
CA
ASP
103
32.938
48.028
61.993
1.00
10.01
DIC

ATOM
780
CB
ASP
103
31.848
48.969
62.449
1.00
8.25
DIC

ATOM
781
CG
ASP
103
30.891
48.371
63.428
1.00
9.78
DIC

ATOM
782
OD1
ASP
103
29.964
49.092
63.841
1.00
8.38
DIC

ATOM
783
OD2
ASP
103
31.050
47.196
63.787
1.00
8.21
DIC

ATOM
784
C
ASP
103
33.408
48.465
60.607
1.00
9.24
DIC

ATOM
785
O
ASP
103
34.485
49.041
60.463
1.00
7.13
DIC

ATOM
786
N
ILE
104
32.591
48.218
59.594
1.00
11.58
DIC

ATOM
787
CA
ILE
104
32.946
48.594
58.226
1.00
10.90
DIC

ATOM
788
CB
ILE
104
32.103
47.800
57.203
1.00
11.09
DIC

ATOM
789
CG2
ILE
104
32.432
48.255
55.785
1.00
10.13
DIC

ATOM
790
CG1
ILE
104
32.361
46.295
57.365
1.00
9.33
DIC

ATOM
791
CD
ILE
104
33.764
45.856
57.023
1.00
8.77
DIC

ATOM
792
C
ILE
104
32.732
50.085
57.980
1.00
11.23
DIC

ATOM
793
O
ILE
104
33.430
50.691
57.164
1.00
10.66
DIC

ATOM
794
N
ASP
105
31.764
50.667
58.687
1.00
10.09
DIC

ATOM
795
CA
ASP
105
31.439
52.085
58.545
1.00
10.37
DIC

ATOM
796
CB
ASP
105
29.959
52.325
58.896
1.00
9.81
DIC

ATOM
797
CG
ASP
105
29.608
51.900
60.318
1.00
7.95
DIC

ATOM
798
OD1
ASP
105
30.413
51.181
60.955
1.00
10.48
DIC

ATOM
799
OD2
ASP
105
28.510
52.275
60.799
1.00
8.90
DIC

ATOM
800
C
ASP
105
32.328
52.996
59.397
1.00
11.29
DIC

ATOM
801
O
ASP
105
31.838
53.871
60.121
1.00
10.81
DIC

ATOM
802
N
VAL
106
33.637
52.774
59.323
1.00
12.07
DIC

ATOM
803
CA
VAL
106
34.582
53.600
60.061
1.00
12.81
DIC

ATOM
804
CB
VAL
106
35.307
52.818
61.191
1.00
14.09
DIC

ATOM
805
CG1
VAL
106
34.290
52.149
62.097
1.00
9.82
DIC

ATOM
806
CG2
VAL
106
36.278
51.805
60.588
1.00
13.66
DIC

ATOM
807
C
VAL
106
35.641
54.127
59.106
1.00
13.02
DIC

ATOM
808
O
VAL
106
35.901
53.545
58.050
1.00
12.85
DIC

ATOM
809
N
LEU
107
36.241
55.242
59.490
1.00
14.12
DIC

ATOM
810
CA
LEU
107
37.288
55.875
58.710
1.00
14.17
DIC

ATOM
811
CB
LEU
107
36.743
57.141
58.050
1.00
15.58
DIC

ATOM
812
CG
LEU
107
36.665
57.238
56.522
1.00
18.69
DIC

ATOM
813
CD1
LEU
107
36.107
55.963
55.914
1.00
19.47
DIC

ATOM
814
CD2
LEU
107
35.800
58.438
56.155
1.00
18.85
DIC

ATOM
815
C
LEU
107
38.364
56.220
59.734
1.00
13.89
DIC

ATOM
816
O
LEU
107
38.165
57.089
60.581
1.00
13.18
DIC

ATOM
817
N
VAL
108
39.485
55.511
59.686
1.00
14.30
DIC

ATOM
818
CA
VAL
106
40.575
55.766
60.625
1.00
14.74
DIC

ATOM
819
CB
VAL
108
41.566
54.581
60.654
1.00
14.99
DIC

ATOM
820
CG1
VAL
108
42.703
54.861
61.648
1.00
12.98
DIC

ATOM
821
CG2
VAL
108
40.825
53.316
61.039
1.00
14.00
DIC

ATOM
822
C
VAL
108
41.281
57.027
60.159
1.00
15.87
DIC

ATOM
823
O
VAL
108
41.740
57.093
59.015
1.00
17.65
DIC

ATOM
824
N
ARG
109
41.350
58.034
61.029
1.00
17.02
DIC

ATOM
825
CA
ARG
109
41.981
59.305
60.668
1.00
17.83
DIC

ATOM
826
CB
ARG
109
41.011
60.467
60.903
1.00
20.81
DIC

ATOM
827
CG
ARG
109
39.553
60.066
60.959
1.00
25.33
DIC

ATOM
828
CD
ARG
109
38.684
61.042
60.198
1.00
27.87
DIC

ATOM
829
NE
ARG
109
39.003
62.443
60.463
1.00
30.93
DIC

ATOM
830
CZ
ARG
109
38.574
63.450
59.702
1.00
31.43
DIC

ATOM
831
NH1
ARG
109
38.902
64.702
59.994
1.00
29.96
DIC

ATOM
832
NH2
ARG
109
37.817
63.198
58.640
1.00
29.66
DIC

ATOM
833
C
ARG
109
43.277
59.603
61.413
1.00
18.31
DIC

ATOM
834
O
ARG
109
43.945
60.597
61.127
1.00
18.37
DIC

ATOM
835
N
ASP
110
43.614
58.767
62.388
1.00
15.42
DIC

ATOM
836
CA
ASP
110
44.846
58.952
63.143
1.00
16.34
DIC

ATOM
837
CB
ASP
110
44.627
59.926
64.312
1.00
18.08
DIC

ATOM
838
CG
ASP
110
45.936
60.528
64.830
1.00
22.13
DIC

ATOM
839
OD1
ASP
110
46.857
60.743
64.015
1.00
21.78
DIC

ATOM
840
OD2
ASP
110
46.040
60.802
66.045
1.00
23.13
DIC

ATOM
841
C
ASP
110
45.303
57.590
63.653
1.00
14.85
DIC

ATOM
842
O
ASP
110
44.523
56.645
63.698
1.00
13.20
DIC

ATOM
843
N
ARG
111
46.571
57.499
64.028
1.00
15.06
DIC

ATOM
844
CA
ARG
111
47.146
56.255
64.510
1.00
15.16
DIC

ATOM
845
CB
ARG
111
48.553
56.524
65.030
1.00
18.81
DIC

ATOM
846
CG
ARG
111
49.217
55.331
65.622
1.00
18.92
DIC

ATOM
847
CD
ARG
111
49.846
55.728
66.938
1.00
31.56
DIC

ATOM
848
NE
ARG
111
50.989
56.627
66.821
1.00
33.85
DIC

ATOM
849
CZ
ARG
111
51.668
57.080
67.869
1.00
36.04
DIC

ATOM
850
NH1
ARG
111
51.307
56.709
69.092
1.00
34.31
DIC

ATOM
851
NH2
ARG
111
52.706
57.897
67.699
1.00
37.36
DIC

ATOM
852
C
ARG
111
46.315
55.573
65.596
1.00
13.47
DIC

ATOM
853
O
ARG
111
45.751
56.226
66.473
1.00
10.45
DIC

ATOM
854
N
LEU
112
46.268
54.248
65.534
1.00
11.22
DIC

ATOM
855
CA
LEU
112
45.520
53.445
66.493
1.00
12.34
DIC

ATOM
856
CB
LEU
112
44.797
52.318
65.747
1.00
13.02
DIC

ATOM
857
CG
LEU
112
43.282
52.409
65.491
1.00
17.78
DIC

ATOM
858
CD1
LEU
112
42.810
53.847
65.418
1.00
15.27
DIC

ATOM
859
CD2
LEU
112
42.951
51.643
64.218
1.00
14.01
DIC

ATOM
860
C
LEU
112
46.455
52.853
67.545
1.00
11.08
DIC

ATOM
861
O
LEU
112
46.013
52.187
68.481
1.00
10.55
DIC

ATOM
862
N
THR
113
47.749
53.105
67.397
1.00
10.99
DIC

ATOM
863
CA
THR
113
48.735
52.555
68.322
1.00
13.17
DIC

ATOM
864
CB
THR
113
50.146
53.084
67.987
1.00
14.67
DIC

ATOM
865
OG1
THR
113
50.429
52.810
66.607
1.00
15.24
DIC

ATOM
866
CG2
THR
113
51.203
52.421
68.863
1.00
14.83
DIC

ATOM
867
C
THR
113
48.423
52.788
69.802
1.00
13.22
DIC

ATOM
868
O
THR
113
48.550
51.869
70.616
1.00
13.60
DIC

ATOM
869
N
PRO
114
48.009
54.013
70.177
1.00
13.02
DIC

ATOM
870
CD
PRO
114
47.875
55.254
69.398
1.00
12.48
DIC

ATOM
871
CA
PRO
114
47.701
54.250
71.593
1.00
13.64
DIC

ATOM
872
CB
PRO
114
47.182
55.686
71.600
1.00
14.06
DIC

ATOM
873
CG
PRO
114
47.955
56.321
70.468
1.00
14.40
DIC

ATOM
874
C
PRO
114
46.651
53.268
72.098
1.00
12.02
DIC

ATOM
875
O
PRO
114
46.751
52.759
73.211
1.00
13.45
DIC

ATOM
876
N
LEU
115
45.643
53.003
71.272
1.00
11.75
DIC

ATOM
877
CA
LEU
115
44.582
52.076
71.659
1.00
11.54
DIC

ATOM
878
CB
LEU
115
43.389
52.193
70.696
1.00
10.01
DIC

ATOM
879
CG
LEU
115
42.236
51.214
70.936
1.00
11.01
DIC

ATOM
880
CD1
LEU
115
41.718
51.381
72.358
1.00
10.94
DIC

ATOM
881
CD2
LEU
115
41.116
51.460
69.921
1.00
11.28
DIC

ATOM
882
C
LEU
115
45.131
50.656
71.656
1.00
10.96
DIC

ATOM
883
O
LEU
115
44.949
49.905
72.613
1.00
12.79
DIC

ATOM
884
N
TRP
116
45.817
50.301
70.578
1.00
11.17
DIC

ATOM
885
CA
TRP
116
46.410
48.977
70.443
1.00
12.32
DIC

ATOM
886
CB
TRP
116
47.161
48.880
69.113
1.00
11.64
DIC

ATOM
887
CG
TRP
116
47.885
47.579
68.933
1.00
14.42
DIC

ATOM
888
CD2
TRP
116
47.304
46.314
68.595
1.00
12.78
DIC

ATOM
889
CE2
TRP
116
48.352
45.365
68.570
1.00
13.04
DIC

ATOM
890
CE3
TRP
116
45.996
45.887
68.312
1.00
13.68
DIC

ATOM
891
CD1
TRP
116
49.222
47.355
69.096
1.00
14.44
DIC

ATOM
892
NE1
TRP
116
49.511
46.027
68.878
1.00
14.14
DIC

ATOM
893
CZ2
TRP
116
48.137
44.014
68.272
1.00
12.47
DIC

ATOM
894
CZ3
TRP
116
45.782
44.539
68.014
1.00
13.84
DIC

ATOM
895
CH2
TRP
116
46.851
43.621
67.997
1.00
13.37
DIC

ATOM
896
C
TRP
116
47.356
48.645
71.599
1.00
12.95
DIC

ATOM
897
O
TRP
116
47.404
47.504
72.056
1.00
13.17
DIC

ATOM
898
N
ASP
117
48.092
49.641
72.082
1.00
14.18
DIC

ATOM
899
CA
ASP
117
49.038
49.416
73.173
1.00
13.65
DIC

ATOM
900
CB
ASP
117
50.122
50.502
73.180
1.00
12.84
DIC

ATOM
901
CG
ASP
117
51.066
50.395
71.998
1.00
15.20
DIC

ATOM
902
OD1
ASP
117
51.218
49.285
71.446
1.00
11.63
DIC

ATOM
903
OD2
ASP
117
51.668
51.423
71.631
1.00
16.23
DIC

ATOM
904
C
ASP
117
48.403
49.352
74.554
1.00
14.05
DIC

ATOM
905
O
ASP
117
49.089
49.088
75.546
1.00
13.05
DIC

ATOM
906
N
THR
118
47.099
49.593
74.624
1.00
14.89
DIC

ATOM
907
CA
THR
118
46.401
49.572
75.903
1.00
15.50
DIC

ATOM
908
CB
THR
118
44.935
50.017
75.736
1.00
16.17
DIC

ATOM
909
OG1
THR
118
44.902
51.379
75.272
1.00
16.94
DIC

ATOM
910
CG2
THR
118
44.197
49.922
77.066
1.00
16.68
DIC

ATOM
911
C
THR
118
46.440
48.189
76.542
1.00
16.76
DIC

ATOM
912
O
THR
118
46.188
47.181
75.885
1.00
16.13
DIC

ATOM
913
N
ASP
119
46.769
48.140
77.827
1.00
17.70
DIC

ATOM
914
CA
ASP
119
46.816
46.861
78.531
1.00
19.90
DIC

ATOM
915
CB
ASP
119
47.841
46.926
79.669
1.00
22.37
DIC

ATOM
916
CG
ASP
119
47.885
45.653
80.501
1.00
24.15
DIC

ATOM
917
OD1
ASP
119
47.539
44.567
79.989
1.00
22.37
DIC

ATOM
918
OD2
ASP
119
48.289
45.744
81.678
1.00
26.50
DIC

ATOM
919
C
ASP
119
45.422
46.543
79.066
1.00
19.45
DIC

ATOM
920
O
ASP
119
44.899
47.250
79.931
1.00
20.25
DIC

ATOM
921
N
LEU
120
44.823
45.484
78.528
1.00
19.08
DIC

ATOM
922
CA
LEU
120
43.480
45.051
78.916
1.00
19.39
DIC

ATOM
923
CB
LEU
120
42.906
44.117
77.846
1.00
16.25
DIC

ATOM
924
CG
LEU
120
42.192
44.700
76.623
1.00
18.43
DIC

ATOM
925
CD1
LEU
120
42.797
46.005
76.207
1.00
19.56
DIC

ATOM
926
CD2
LEU
120
42.246
43.680
75.502
1.00
14.56
DIC

ATOM
927
C
LEU
120
43.413
44.342
80.264
1.00
19.79
DIC

ATOM
928
O
LEU
120
42.337
44.230
80.852
1.00
21.22
DIC

ATOM
929
N
GLY
121
44.552
43.861
80.754
1.00
20.41
DIC

ATOM
930
CA
GLY
121
44.539
43.156
82.024
1.00
20.26
DIC

ATOM
931
C
GLY
121
43.648
41.934
81.880
1.00
20.32
DIC

ATOM
932
O
GLY
121
43.738
41.213
80.880
1.00
18.77
DIC

ATOM
933
N
ASN
122
42.778
41.695
82.855
1.00
20.30
DIC

ATOM
934
CA
ASN
122
41.891
40.540
82.772
1.00
21.26
DIC

ATOM
935
CB
ASN
122
41.778
39.852
84.135
1.00
23.94
DIC

ATOM
936
CG
ASN
122
41.067
38.510
84.054
1.00
27.72
DIC

ATOM
937
OD1
ASN
122
41.427
37.643
83.247
1.00
29.43
DIC

ATOM
938
ND2
ASN
122
40.056
38.329
84.893
1.00
29.68
DIC

ATOM
939
C
ASN
122
40.508
40.940
82.254
1.00
20.06
DIC

ATOM
940
O
ASN
122
39.545
40.173
82.356
1.00
19.14
DIC

ATOM
941
N
ASN
123
40.421
42.150
81.704
1.00
18.17
DIC

ATOM
942
CA
ASN
123
39.173
42.656
81.137
1.00
17.70
DIC

ATOM
943
CB
ASN
123
39.278
44.158
80.810
1.00
19.01
DIC

ATOM
944
CG
ASN
123
39.293
45.042
82.053
1.00
20.14
DIC

ATOM
945
OD1
ASN
123
40.257
45.769
82.303
1.00
19.33
DIC

ATOM
946
ND2
ASN
123
38.218
44.990
82.829
1.00
17.24
DIC

ATOM
947
C
ASN
123
38.894
41.891
79.842
1.00
17.42
DIC

ATOM
948
O
ASN
123
39.818
41.387
79.194
1.00
16.53
DIC

ATOM
949
N
TRP
124
37.619
41.823
79.469
1.00
16.21
DIC

ATOM
950
CA
TRP
124
37.191
41.136
78.260
1.00
13.67
DIC

ATOM
951
CB
TRP
124
35.675
40.980
78.246
1.00
13.09
DIC

ATOM
952
CG
TRP
124
35.140
40.061
79.278
1.00
14.06
DIC

ATOM
953
CD2
TRP
124
35.114
38.631
79.212
1.00
13.39
DIC

ATOM
954
CE2
TRP
124
34.475
38.169
80.389
1.00
14.28
DIC

ATOM
955
CE3
TRP
124
35.566
37.694
78.273
1.00
14.36
DIC

ATOM
956
CD1
TRP
124
34.535
40.406
80.461
1.00
11.88
DIC

ATOM
957
NE1
TRP
124
34.131
39.272
81.132
1.00
12.38
DIC

ATOM
958
CZ2
TRP
124
34.278
36.808
80.649
1.00
13.77
DIC

ATOM
959
CZ3
TRP
124
35.370
36.338
78.534
1.00
15.53
DIC

ATOM
960
CH2
TRP
124
34.730
35.911
79.714
1.00
15.41
DIC

ATOM
961
C
TRP
124
37.591
41.898
77.006
1.00
13.43
DIC

ATOM
962
O
TRP
124
37.899
41.303
75.979
1.00
12.54
DIC

ATOM
963
N
LEU
125
37.570
43.221
77.102
1.00
11.84
DIC

ATOM
964
CA
LEU
125
37.897
44.062
75.970
1.00
11.77
DIC

ATOM
965
CB
LEU
125
36.845
43.874
74.861
1.00
10.08
DIC

ATOM
966
CG
LEU
125
35.361
43.957
75.259
1.00
10.79
DIC

ATOM
967
CD1
LEU
125
35.006
45.378
75.672
1.00
14.40
DIC

ATOM
968
CD2
LEU
125
34.486
43.530
74.086
1.00
11.76
DIC

ATOM
969
C
LEU
125
37.958
45.524
76.368
1.00
11.36
DIC

ATOM
970
O
LEU
125
37.614
45.904
77.488
1.00
12.15
DIC

ATOM
971
N
GLY
126
38.419
46.336
75.432
1.00
11.25
DIC

ATOM
972
CA
GLY
126
38.492
47.763
75.651
1.00
11.38
DIC

ATOM
973
C
GLY
126
37.584
48.350
74.588
1.00
11.99
DIC

ATOM
974
O
GLY
126
37.600
47.893
73.435
1.00
11.61
DIC

ATOM
975
N
ALA
127
36.779
49.338
74.962
1.00
10.89
DIC

ATOM
976
CA
ALA
127
35.868
49.967
74.013
1.00
10.27
DIC

ATOM
977
CB
ALA
127
34.608
49.121
73.871
1.00
9.81
DIC

ATOM
978
C
ALA
127
35.499
51.383
74.444
1.00
11.20
DIC

ATOM
979
O
ALA
127
35.663
51.749
75.612
1.00
8.75
DIC

ATOM
980
N
SER
128
35.017
52.185
73.496
1.00
10.96
DIC

ATOM
981
CA
SER
128
34.622
53.551
73.811
1.00
12.41
DIC

ATOM
982
CB
SER
128
34.844
54.480
72.610
1.00
11.48
DIC

ATOM
983
OG
SER
128
36.228
54.600
72.303
1.00
12.36
DIC

ATOM
984
C
SER
128
33.153
53.563
74.220
1.00
13.04
DIC

ATOM
985
O
SER
128
32.362
52.717
73.783
1.00
11.02
DIC

ATOM
986
N
ILE
129
32.800
54.535
75.055
1.00
12.60
DIC

ATOM
987
CA
ILE
129
31.441
54.678
75.568
1.00
14.09
DIC

ATOM
988
CB
ILE
129
31.433
55.609
76.816
1.00
14.78
DIC

ATOM
989
CG2
ILE
129
30.009
55.993
77.195
1.00
15.61
DIC

ATOM
990
CG1
ILE
129
32.154
54.916
77.973
1.00
16.10
DIC

ATOM
991
CD
ILE
129
32.334
55.785
79.199
1.00
16.05
DIC

ATOM
992
C
ILE
129
30.484
55.232
74.519
1.00
14.40
DIC

ATOM
993
O
ILE
129
30.841
56.112
73.736
1.00
12.33
DIC

ATOM
994
N
ASP
130
29.263
54.708
74.513
1.00
14.40
DIC

ATOM
995
CA
ASP
130
28.253
55.155
73.571
1.00
14.93
DIC

ATOM
996
CB
ASP
130
27.396
53.972
73.127
1.00
13.65
DIC

ATOM
997
CG
ASP
130
26.533
54.305
71.936
1.00
12.84
DIC

ATOM
998
OD1
ASP
130
25.787
55.315
71.985
1.00
15.16
DIC

ATOM
999
OD2
ASP
130
26.605
53.556
70.953
1.00
12.26
DIC

ATOM
1000
C
ASP
130
27.359
56.209
74.228
1.00
14.81
DIC

ATOM
1001
O
ASP
130
26.458
55.868
74.991
1.00
15.34
DIC

ATOM
1002
N
LEU
131
27.605
57.482
73.932
1.00
15.23
DIC

ATOM
1003
CA
LEU
131
26.811
58.576
74.509
1.00
15.08
DIC

ATOM
1004
CB
LEU
131
27.344
59.936
74.049
1.00
15.03
DIC

ATOM
1005
CG
LEU
131
28.638
60.445
74.680
1.00
18.24
DIC

ATOM
1006
CD1
LEU
131
29.710
59.364
74.623
1.00
20.00
DIC

ATOM
1007
CD2
LEU
131
29.090
61.700
73.947
1.00
16.98
DIC

ATOM
1008
C
LEU
131
25.339
58.497
74.139
1.00
14.84
DIC

ATOM
1009
O
LEU
131
24.466
58.863
74.933
1.00
15.29
DIC

ATOM
1010
N
PHE
132
25.068
58.041
72.922
1.00
13.40
DIC

ATOM
1011
CA
PHE
132
23.700
57.930
72.440
1.00
15.19
DIC

ATOM
1012
CB
PHE
132
23.698
57.464
70.976
1.00
16.45
DIC

ATOM
1013
CG
PHE
132
22.325
57.299
70.391
1.00
18.23
DIC

ATOM
1014
CD1
PHE
132
21.657
56.079
70.480
1.00
19.03
DIC

ATOM
1015
CD2
PHE
132
21.680
58.371
69.793
1.00
19.73
DIC

ATOM
1016
CE1
PHE
132
20.365
55.931
69.984
1.00
18.68
DIC

ATOM
1017
CE2
PHE
132
20.381
58.235
69.292
1.00
21.22
DIC

ATOM
1018
CZ
PHE
132
19.723
57.010
69.389
1.00
19.92
DIC

ATOM
1019
C
PHE
132
22.898
56.971
73.320
1.00
15.39
DIC

ATOM
1020
O
PHE
132
21.812
57.316
73.791
1.00
17.07
DIC

ATOM
1021
N
VAL
133
23.446
55.781
73.553
1.00
12.91
DIC

ATOM
1022
CA
VAL
133
22.771
54.783
74.375
1.00
14.30
DIC

ATOM
1023
CB
VAL
133
23.439
53.399
74.241
1.00
13.72
DIC

ATOM
1024
CG1
VAL
133
22.727
52.386
75.138
1.00
14.53
DIC

ATOM
1025
CG2
VAL
133
23.375
52.939
72.794
1.00
13.31
DIC

ATOM
1026
C
VAL
133
22.741
55.184
75.845
1.00
15.10
DIC

ATOM
1027
O
VAL
133
21.710
55.049
76.503
1.00
15.38
DIC

ATOM
1028
N
GLU
134
23.867
55.682
76.352
1.00
16.89
DIC

ATOM
1029
CA
GLU
134
23.951
56.121
77.746
1.00
18.11
DIC

ATOM
1030
CB
GLU
134
25.334
56.708
78.058
1.00
17.79
DIC

ATOM
1031
CG
GLU
134
26.358
55.714
78.580
1.00
18.79
DIC

ATOM
1032
CD
GLU
134
25.943
55.071
79.893
1.00
15.84
DIC

ATOM
1033
OE1
GLU
134
25.534
55.790
80.828
1.00
18.93
DIC

ATOM
1034
OE2
GLU
134
26.035
53.838
79.993
1.00
16.91
DIC

ATOM
1035
C
GLU
134
22.904
57.169
78.092
1.00
18.74
DIC

ATOM
1036
O
GLU
134
22.397
57.196
79.207
1.00
19.62
DIC

ATOM
1037
N
ARG
135
22.583
58.054
77.163
1.00
20.18
DIC

ATOM
1038
CA
ARG
135
21.592
59.061
77.501
1.00
21.49
DIC

ATOM
1039
CB
ARG
135
21.898
60.402
76.820
1.00
22.17
DIC

ATOM
1040
CG
ARG
135
21.852
60.441
75.309
1.00
26.54
DIC

ATOM
1041
CD
ARG
135
22.447
61.769
74.834
1.00
30.72
DIC

ATOM
1042
NE
ARG
135
21.803
62.903
75.492
1.00
33.69
DIC

ATOM
1043
CZ
ARG
135
20.912
63.708
74.916
1.00
35.46
DIC

ATOM
1044
NH1
ARG
135
20.380
64.705
75.612
1.00
36.28
DIC

ATOM
1045
NH2
ARG
135
20.568
63.535
73.646
1.00
33.44
DIC

ATOM
1046
C
ARG
135
20.176
58.599
77.196
1.00
21.50
DIC

ATOM
1047
O
ARG
135
19.231
59.380
77.266
1.00
21.59
DIC

ATOM
1048
N
GLN
136
20.021
57.321
76.867
1.00
20.53
DIC

ATOM
1049
CA
GLN
136
18.689
56.790
76.600
1.00
21.69
DIC

ATOM
1050
CB
GLN
136
18.767
55.590
75.653
1.00
22.18
DIC

ATOM
1051
CG
GLN
136
17.408
55.118
75.147
1.00
24.69
DIC

ATOM
1052
CD
GLN
136
17.487
53.951
74.173
1.00
27.02
DIC

ATOM
1053
OE1
GLN
136
18.419
53.858
73.384
1.00
26.51
DIC

ATOM
1054
NE2
GLN
136
16.491
53.067
74.216
1.00
26.50
DIC

ATOM
1055
C
GLN
136
18.067
56.361
77.938
1.00
23.33
DIC

ATOM
1056
O
GLN
136
18.334
55.271
78.431
1.00
21.46
DIC

ATOM
1057
N
GLU
137
17.241
57.237
78.510
1.00
23.90
DIC

ATOM
1058
CA
GLU
137
16.549
57.028
79.789
1.00
26.86
DIC

ATOM
1059
CB
GLU
137
15.233
57.832
79.846
1.00
30.23
DIC

ATOM
1060
CG
GLU
137
15.271
59.120
80.663
1.00
35.53
DIC

ATOM
1061
CD
GLU
137
16.227
59.028
81.844
1.00
38.87
DIC

ATOM
1062
OE1
GLU
137
16.443
57.933
82.435
1.00
40.95
DIC

ATOM
1063
OE2
GLU
137
16.785
60.090
82.175
1.00
41.61
DIC

ATOM
1064
C
GLU
137
16.185
55.598
80.087
1.00
24.31
DIC

ATOM
1065
O
GLU
137
15.407
54.984
79.365
1.00
25.87
DIC

ATOM
1066
N
GLY
138
16.766
55.070
81.149
1.00
23.93
DIC

ATOM
1067
CA
GLY
138
16.451
53.729
81.594
1.00
22.33
DIC

ATOM
1068
C
GLY
138
16.756
52.535
80.724
1.00
21.12
DIC

ATOM
1069
O
GLY
138
16.509
51.410
81.164
1.00
22.81
DIC

ATOM
1070
N
TYR
139
17.289
52.734
79.526
1.00
18.91
DIC

ATOM
1071
CA
TYR
139
17.555
51.583
78.676
1.00
17.98
DIC

ATOM
1072
CB
TYR
139
18.002
52.012
77.282
1.00
17.34
DIC

ATOM
1073
CG
TYR
139
18.291
50.799
76.400
1.00
17.33
DIC

ATOM
1074
CD1
TYR
139
17.254
49.968
75.965
1.00
18.26
DIC

ATOM
1075
CE1
TYR
139
17.510
48.815
75.222
1.00
16.56
DIC

ATOM
1076
CD2
TYR
139
19.602
50.442
76.062
1.00
15.79
DIC

ATOM
1077
CE2
TYR
139
19.866
49.284
75.312
1.00
15.54
DIC

ATOM
1078
CZ
TYR
139
18.813
48.480
74.901
1.00
16.42
DIC

ATOM
1079
OH
TYR
139
19.045
47.340
74.165
1.00
15.74
DIC

ATOM
1080
C
TYR
139
18.584
50.596
79.212
1.00
17.11
DIC

ATOM
1081
O
TYR
139
18.348
49.386
79.242
1.00
17.36
DIC

ATOM
1082
N
LYS
140
19.744
51.130
79.571
1.00
15.75
DIC

ATOM
1083
CA
LYS
140
20.865
50.365
80.083
1.00
16.81
DIC

ATOM
1084
CB
LYS
140
21.894
51.354
80.635
1.00
19.79
DIC

ATOM
1085
CG
LYS
140
23.223
50.771
80.995
1.00
23.22
DIC

ATOM
1086
CD
LYS
140
24.253
51.863
81.267
1.00
21.44
DIC

ATOM
1087
CE
LYS
140
23.904
52.707
82.480
1.00
23.50
DIC

ATOM
1088
NZ
LYS
140
25.043
53.584
82.849
1.00
22.17
DIC

ATOM
1089
C
LYS
140
20.404
49.388
81.162
1.00
17.13
DIC

ATOM
1090
O
LYS
140
20.812
48.226
81.180
1.00
14.56
DIC

ATOM
1091
N
GLN
141
19.540
49.862
82.053
1.00
16.81
DIC

ATOM
1092
CA
GLN
141
19.027
49.029
83.130
1.00
18.98
DIC

ATOM
1093
CB
GLN
141
18.259
49.896
84.137
1.00
19.80
DIC

ATOM
1094
CG
GLN
141
19.152
50.846
84.948
1.00
18.45
DIC

ATOM
1095
CD
GLN
141
19.602
52.091
84.178
1.00
20.81
DIC

ATOM
1096
OE1
GLN
141
19.304
52.258
82.994
1.00
19.23
DIC

ATOM
1097
NE2
GLN
141
20.327
52.972
84.860
1.00
18.11
DIC

ATOM
1098
C
GLN
141
18.147
47.878
82.624
1.00
19.56
DIC

ATOM
1099
O
GLN
141
18.071
46.822
83.258
1.00
20.21
DIC

ATOM
1100
N
LYS
142
17.495
48.070
81.479
1.00
18.99
DIC

ATOM
1101
CA
LYS
142
16.653
47.019
80.915
1.00
18.42
DIC

ATOM
1102
CB
LYS
142
15.947
47.503
79.644
1.00
20.49
DIC

ATOM
1103
CG
LYS
142
14.882
48.562
79.871
1.00
23.32
DIC

ATOM
1104
CD
LYS
142
14.220
48.950
78.552
1.00
24.72
DIC

ATOM
1105
CE
LYS
142
13.110
49.968
78.761
1.00
26.12
DIC

ATOM
1106
NZ
LYS
142
12.037
49.424
79.644
1.00
26.72
DIC

ATOM
1107
C
LYS
142
17.477
45.778
80.580
1.00
18.39
DIC

ATOM
1108
O
LYS
142
16.951
44.661
80.557
1.00
17.06
DIC

ATOM
1109
N
ILE
143
18.764
45.957
80.294
1.00
16.69
DIC

ATOM
1110
CA
ILE
143
19.569
44.785
79.985
1.00
15.20
DIC

ATOM
1111
CB
ILE
143
20.389
44.964
78.680
1.00
14.48
DIC

ATOM
1112
CG2
ILE
143
19.438
45.218
77.519
1.00
15.42
DIC

ATOM
1113
CG1
ILE
143
21.384
46.112
78.811
1.00
14.17
DIC

ATOM
1114
CD
ILE
143
22.379
46.166
77.652
1.00
14.63
DIC

ATOM
1115
C
ILE
143
20.471
44.362
81.143
1.00
14.14
DIC

ATOM
1116
O
ILE
143
21.477
43.685
80.943
1.00
14.10
DIC

ATOM
1117
N
GLY
144
20.089
44.767
82.355
1.00
14.85
DIC

ATOM
1118
CA
GLY
144
20.816
44.381
83.557
1.00
13.42
DIC

ATOM
1119
C
GLY
144
22.048
45.154
83.984
1.00
15.34
DIC

ATOM
1120
O
GLY
144
22.775
44.721
84.884
1.00
14.31
DIC

ATOM
1121
N
MSE
145
22.295
46.298
83.361
1.00
14.04
DIC

ATOM
1122
CA
MSE
145
23.458
47.091
83.720
1.00
15.25
DIC

ATOM
1123
CB
MSE
145
23.997
47.815
82.485
1.00
14.45
DIC

ATOM
1124
CG
MSE
145
24.524
46.865
81.415
1.00
15.86
DIC

ATOM
1125
SE
MSE
145
25.126
47.799
79.831
1.00
16.27
DIC

ATOM
1126
CE
MSE
145
26.753
48.566
80.498
1.00
14.18
DIC

ATOM
1127
C
MSE
145
23.115
48.099
84.809
1.00
16.09
DIC

ATOM
1128
O
MSE
145
21.984
48.585
84.882
1.00
14.76
DIC

ATOM
1129
N
ALA
146
24.096
48.400
85.655
1.00
17.00
DIC

ATOM
1130
CA
ALA
146
23.903
49.366
86.728
1.00
18.41
DIC

ATOM
1131
CB
ALA
146
24.802
49.033
87.906
1.00
18.96
DIC

ATOM
1132
C
ALA
146
24.238
50.752
86.192
1.00
19.79
DIC

ATOM
1133
O
ALA
146
24.793
50.885
85.098
1.00
18.39
DIC

ATOM
1134
N
ASP
147
23.906
51.778
86.971
1.00
19.70
DIC

ATOM
1135
CA
ASP
147
24.168
53.155
86.576
1.00
20.75
DIC

ATOM
1136
CB
ASP
147
23.657
54.136
87.632
1.00
24.89
DIC

ATOM
1137
CG
ASP
147
23.905
55.584
87.242
1.00
28.79
DIC

ATOM
1138
OD1
ASP
147
23.171
56.108
86.380
1.00
32.14
DIC

ATOM
1139
OD2
ASP
147
24.845
56.199
87.787
1.00
33.35
DIC

ATOM
1140
C
ASP
147
25.643
53.421
86.355
1.00
18.89
DIC

ATOM
1141
O
ASP
147
26.007
54.205
85.472
1.00
19.38
DIC

ATOM
1142
N
GLY
148
26.483
52.771
87.158
1.00
16.62
DIC

ATOM
1143
CA
GLY
148
27.924
52.959
87.058
1.00
15.83
DIC

ATOM
1144
C
GLY
148
28.640
52.121
86.013
1.00
14.92
DIC

ATOM
1145
O
GLY
148
29.852
52.238
85.842
1.00
15.77
DIC

ATOM
1146
N
GLU
149
27.908
51.257
85.320
1.00
14.62
DIC

ATOM
1147
CA
GLU
149
28.512
50.434
84.280
1.00
13.91
DIC

ATOM
1148
CB
GLU
149
27.948
49.015
84.331
1.00
13.40
DIC

ATOM
1149
CG
GLU
149
28.174
48.342
85.680
1.00
16.25
DIC

ATOM
1150
CD
GLU
149
27.669
46.912
85.717
1.00
17.21
DIC

ATOM
1151
OE1
GLU
149
26.540
46.662
85.246
1.00
17.01
DIC

ATOM
1152
OE2
GLU
149
28.403
46.041
86.228
1.00
18.86
DIC

ATOM
1153
C
GLU
149
28.133
51.128
82.984
1.00
13.92
DIC

ATOM
1154
O
GLU
149
26.958
51.207
82.635
1.00
14.24
DIC

ATOM
1155
N
TYR
150
29.131
51.641
82.280
1.00
13.00
DIC

ATOM
1156
CA
TYR
150
28.880
52.386
81.056
1.00
14.46
DIC

ATOM
1157
CB
TYR
150
29.968
53.449
80.904
1.00
14.10
DIC

ATOM
1158
CG
TYR
150
30.069
54.308
82.151
1.00
14.23
DIC

ATOM
1159
CD1
TYR
150
31.304
54.579
82.734
1.00
14.50
DIC

ATOM
1160
CE1
TYR
150
31.401
55.298
83.924
1.00
15.54
DIC

ATOM
1161
CD2
TYR
150
28.920
54.787
82.789
1.00
14.65
DIC

ATOM
1162
CE2
TYR
150
29.006
55.510
83.987
1.00
15.14
DIC

ATOM
1163
CZ
TYR
150
30.256
55.756
84.545
1.00
16.39
DIC

ATOM
1164
OH
TYR
150
30.373
56.440
85.728
1.00
15.21
DIC

ATOM
1165
C
TYR
150
28.724
51.555
79.789
1.00
13.06
DIC

ATOM
1166
O
TYR
150
29.524
50.665
79.495
1.00
12.78
DIC

ATOM
1167
N
TYR
151
27.663
51.858
79.049
1.00
11.90
DIC

ATOM
1168
CA
TYR
151
27.351
51.143
77.819
1.00
12.53
DIC

ATOM
1169
CB
TYR
151
25.931
51.509
77.374
1.00
12.20
DIC

ATOM
1170
CG
TYR
151
25.352
50.644
76.274
1.00
11.21
DIC

ATOM
1171
CD1
TYR
151
25.752
50.802
74.951
1.00
9.91
DIC

ATOM
1172
CE1
TYR
151
25.195
50.034
73.930
1.00
10.32
DIC

ATOM
1173
CD2
TYR
151
24.373
49.687
76.557
1.00
11.48
DIC

ATOM
1174
CE2
TYR
151
23.810
48.911
75.546
1.00
11.82
DIC

ATOM
1175
CZ
TYR
151
24.225
49.090
74.230
1.00
12.60
DIC

ATOM
1176
OH
TYR
151
23.668
48.330
73.218
1.00
10.81
DIC

ATOM
1177
C
TYR
151
28.372
51.512
76.751
1.00
11.38
DIC

ATOM
1178
O
TYR
151
28.577
52.689
76.458
1.00
11.36
DIC

ATOM
1179
N
PHE
152
29.041
50.513
76.190
1.00
10.71
DIC

ATOM
1180
CA
PHE
152
30.030
50.812
75.168
1.00
10.99
DIC

ATOM
1181
CB
PHE
152
31.337
50.034
75.416
1.00
10.34
DIC

ATOM
1182
CG
PHE
152
31.193
48.533
75.372
1.00
10.77
DIC

ATOM
1183
CD1
PHE
152
30.968
47.802
76.539
1.00
9.58
DIC

ATOM
1184
CD2
PHE
152
31.324
47.844
74.166
1.00
10.11
DIC

ATOM
1185
CE1
PHE
152
30.879
46.399
76.507
1.00
12.23
DIC

ATOM
1186
CE2
PHE
152
31.236
46.445
74.122
1.00
11.41
DIC

ATOM
1187
CZ
PHE
152
31.015
45.720
75.291
1.00
10.68
DIC

ATOM
1188
C
PHE
152
29.502
50.541
73.768
1.00
11.13
DIC

ATOM
1189
O
PHE
152
28.519
49.813
73.597
1.00
12.61
DIC

ATOM
1190
N
ASN
153
30.131
51.161
72.772
1.00
10.37
DIC

ATOM
1191
CA
ASN
153
29.732
50.962
71.385
1.00
8.75
DIC

ATOM
1192
CB
ASN
153
29.969
52.231
70.553
1.00
10.03
DIC

ATOM
1193
CG
ASN
153
29.579
52.052
69.092
1.00
8.59
DIC

ATOM
1194
OD1
ASN
153
30.396
51.662
68.260
1.00
9.43
DIC

ATOM
1195
ND2
ASN
153
28.319
52.314
68.785
1.00
10.09
DIC

ATOM
1196
C
ASN
153
30.560
49.802
70.854
1.00
8.80
DIC

ATOM
1197
O
ASN
153
31.768
49.738
71.073
1.00
9.14
DIC

ATOM
1198
N
ALA
154
29.914
48.879
70.154
1.00
9.45
DIC

ATOM
1199
CA
ALA
154
30.617
47.702
69.651
1.00
10.62
DIC

ATOM
1200
CB
ALA
154
29.634
46.546
69.518
1.00
11.77
DIC

ATOM
1201
C
ALA
154
31.368
47.895
68.339
1.00
9.97
DIC

ATOM
1202
O
ALA
154
31.940
46.944
67.814
1.00
10.61
DIC

ATOM
1203
N
GLY
155
31.381
49.119
67.818
1.00
8.84
DIC

ATOM
1204
CA
GLY
155
32.054
49.377
66.553
1.00
9.49
DIC

ATOM
1205
C
GLY
155
33.575
49.396
66.545
1.00
9.26
DIC

ATOM
1206
O
GLY
155
34.193
49.248
65.485
1.00
9.60
DIC

ATOM
1207
N
VAL
156
34.183
49.589
67.715
1.00
8.00
DIC

ATOM
1208
CA
VAL
156
35.640
49.631
67.849
1.00
6.16
DIC

ATOM
1209
CB
VAL
156
36.152
51.095
67.977
1.00
8.60
DIC

ATOM
1210
CG1
VAL
156
37.667
51.111
68.200
1.00
8.18
DIC

ATOM
1211
CG2
VAL
156
35.788
51.887
66.708
1.00
4.42
DIC

ATOM
1212
C
VAL
156
35.968
48.869
69.120
1.00
7.98
DIC

ATOM
1213
O
VAL
156
35.711
49.351
70.225
1.00
7.64
DIC

ATOM
1214
N
LEU
157
36.540
47.679
68.973
1.00
7.93
DIC

ATOM
1215
CA
LEU
157
36.826
46.861
70.140
1.00
8.32
DIC

ATOM
1216
CB
LEU
157
35.812
45.714
70.216
1.00
8.82
DIC

ATOM
1217
CG
LEU
157
34.317
46.025
70.104
1.00
6.30
DIC

ATOM
1218
CD1
LEU
157
33.579
44.733
69.815
1.00
3.81
DIC

ATOM
1219
CD2
LEU
157
33.804
46.675
71.373
1.00
6.09
DIC

ATOM
1220
C
LEU
157
38.218
46.259
70.190
1.00
10.43
DIC

ATOM
1221
O
LEU
157
38.623
45.544
69.270
1.00
10.91
DIC

ATOM
1222
N
LEU
158
38.948
46.546
71.265
1.00
10.32
DIC

ATOM
1223
CA
LEU
158
40.270
45.967
71.444
1.00
11.68
DIC

ATOM
1224
CB
LEU
158
41.172
46.887
72.266
1.00
13.62
DIC

ATOM
1225
CG
LEU
158
42.617
46.400
72.369
1.00
14.82
DIC

ATOM
1226
CD1
LEU
158
43.239
46.368
70.981
1.00
14.39
DIC

ATOM
1227
CD2
LEU
158
43.409
47.323
73.283
1.00
16.11
DIC

ATOM
1228
C
LEU
158
39.929
44.705
72.227
1.00
12.27
DIC

ATOM
1229
O
LEU
158
39.531
44.767
73.396
1.00
13.47
DIC

ATOM
1230
N
ILE
159
40.082
43.557
71.586
1.00
12.60
DIC

ATOM
1231
CA
ILE
159
39.707
42.300
72.216
1.00
12.69
DIC

ATOM
1232
CB
ILE
159
38.874
41.471
71.212
1.00
12.19
DIC

ATOM
1233
CG2
ILE
159
38.528
40.093
71.792
1.00
9.38
DIC

ATOM
1234
CG1
ILE
159
37.630
42.286
70.843
1.00
9.30
DIC

ATOM
1235
CD
ILE
159
36.700
41.635
69.869
1.00
13.02
DIC

ATOM
1236
C
ILE
159
40.811
41.440
72.816
1.00
13.96
DIC

ATOM
1237
O
ILE
159
41.850
41.185
72.200
1.00
12.79
DIC

ATOM
1238
N
ASN
160
40.570
41.009
74.048
1.00
14.07
DIC

ATOM
1239
CA
ASN
160
41.498
40.142
74.757
1.00
13.56
DIC

ATOM
1240
CB
ASN
160
41.284
40.294
76.260
1.00
14.31
DIC

ATOM
1241
CG
ASN
160
42.227
39.443
77.074
1.00
13.83
DIC

ATOM
1242
OD1
ASN
160
42.806
38.490
76.571
1.00
13.36
DIC

ATOM
1243
ND2
ASN
160
42.374
39.778
78.347
1.00
12.66
DIC

ATOM
1244
C
ASN
160
41.120
38.730
74.301
1.00
13.20
DIC

ATOM
1245
O
ASN
160
40.485
37.980
75.041
1.00
12.35
DIC

ATOM
1246
N
LEU
161
41.497
38.380
73.073
1.00
14.48
DIC

ATOM
1247
CA
LEU
161
41.173
37.071
72.506
1.00
14.41
DIC

ATOM
1248
CB
LEU
161
41.772
36.927
71.103
1.00
15.27
DIC

ATOM
1249
CG
LEU
161
40.849
37.142
69.902
1.00
19.60
DIC

ATOM
1250
CD1
LEU
161
41.625
36.854
68.629
1.00
17.54
DIC

ATOM
1251
CD2
LEU
161
39.625
36.239
69.998
1.00
18.80
DIC

ATOM
1252
C
LEU
161
41.601
35.873
73.345
1.00
14.82
DIC

ATOM
1253
O
LEU
161
40.904
34.857
73.383
1.00
12.20
DIC

ATOM
1254
N
LYS
162
42.762
35.973
73.982
1.00
16.27
DIC

ATOM
1255
CA
LYS
162
43.248
34.885
74.819
1.00
18.17
DIC

ATOM
1256
CB
LYS
162
44.579
35.269
75.472
1.00
23.17
DIC

ATOM
1257
CG
LYS
162
45.039
34.285
76.535
1.00
28.53
DIC

ATOM
1258
CD
LYS
162
46.494
34.495
76.924
1.00
32.40
DIC

ATOM
1259
CE
LYS
162
47.429
33.990
75.829
1.00
36.43
DIC

ATOM
1260
NZ
LYS
162
48.845
33.936
76.294
1.00
38.35
DIC

ATOM
1261
C
LYS
162
42.204
34.572
75.891
1.00
18.73
DIC

ATOM
1262
O
LYS
162
41.927
33.406
76.178
1.00
17.49
DIC

ATOM
1263
N
LYS
163
41.622
35.618
76.481
1.00
16.83
DIC

ATOM
1264
CA
LYS
163
40.603
35.431
77.508
1.00
15.63
DIC

ATOM
1265
CB
LYS
163
40.269
36.762
78.188
1.00
14.80
DIC

ATOM
1266
CG
LYS
163
39.303
36.629
79.363
1.00
16.56
DIC

ATOM
1267
CD
LYS
163
39.014
37.984
79.999
1.00
17.80
DIC

ATOM
1268
CE
LYS
163
38.043
37.863
81.172
1.00
19.19
DIC

ATOM
1269
NZ
LYS
163
38.560
36.924
82.210
1.00
24.46
DIC

ATOM
1270
C
LYS
163
39.334
34.830
76.891
1.00
15.48
DIC

ATOM
1271
O
LYS
163
38.760
33.888
77.436
1.00
15.56
DIC

ATOM
1272
N
TRP
164
38.896
35.376
75.758
1.00
13.99
DIC

ATOM
1273
CA
TRP
164
37.703
34.857
75.088
1.00
14.31
DIC

ATOM
1274
CB
TRP
164
37.453
35.598
73.773
1.00
12.76
DIC

ATOM
1275
CG
TRP
164
36.885
36.979
73.909
1.00
12.61
DIC

ATOM
1276
CD2
TRP
164
35.948
37.604
73.024
1.00
11.45
DIC

ATOM
1277
CE2
TRP
164
35.742
38.923
73.493
1.00
10.90
DIC

ATOM
1278
CE3
TRP
164
35.265
37.179
71.876
1.00
11.56
DIC

ATOM
1279
CD1
TRP
164
37.200
37.914
74.855
1.00
12.23
DIC

ATOM
1280
NE1
TRP
164
36.518
39.084
74.612
1.00
12.19
DIC

ATOM
1281
CZ2
TRP
164
34.880
39.823
72.852
1.00
10.67
DIC

ATOM
1282
CZ3
TRP
164
34.406
38.076
71.238
1.00
10.59
DIC

ATOM
1283
CH2
TRP
164
34.224
39.382
71.729
1.00
11.25
DIC

ATOM
1284
C
TRP
164
37.828
33.359
74.782
1.00
14.32
DIC

ATOM
1285
O
TRP
164
36.862
32.607
74.925
1.00
12.37
DIC

ATOM
1286
N
ARG
165
39.009
32.927
74.349
1.00
14.03
DIC

ATOM
1287
CA
ARG
165
39.191
31.519
74.008
1.00
15.65
DIC

ATOM
1288
CB
ARG
165
40.515
31.307
73.260
1.00
17.22
DIC

ATOM
1289
CG
ARG
165
40.498
31.881
71.833
1.00
18.70
DIC

ATOM
1290
CD
ARG
165
41.599
31.285
70.945
1.00
20.78
DIC

ATOM
1291
NE
ARG
165
42.933
31.672
71.394
1.00
20.86
DIC

ATOM
1292
CZ
ARG
165
43.595
32.737
70.954
1.00
22.03
DIC

ATOM
1293
NH1
ARG
165
44.802
33.012
71.433
1.00
22.53
DIC

ATOM
1294
NH2
ARG
165
43.064
33.513
70.018
1.00
23.03
DIC

ATOM
1295
C
ARG
165
39.084
30.589
75.213
1.00
16.07
DIC

ATOM
1296
O
ARG
165
38.959
29.377
75.061
1.00
15.48
DIC

ATOM
1297
N
ARG
166
39.105
31.159
76.411
1.00
17.98
DIC

ATOM
1298
CA
ARG
166
38.971
30.364
77.623
1.00
18.39
DIC

ATOM
1299
CB
ARG
166
39.585
31.090
78.822
1.00
21.23
DIC

ATOM
1300
CG
ARG
166
41.090
31.236
78.787
1.00
23.66
DIC

ATOM
1301
CD
ARG
166
41.585
31.922
80.051
1.00
24.40
DIC

ATOM
1302
NE
ARG
166
43.031
32.101
80.017
1.00
28.45
DIC

ATOM
1303
CZ
ARG
166
43.644
33.276
79.929
1.00
28.36
DIC

ATOM
1304
NH1
ARG
166
42.940
34.403
79.870
1.00
28.09
DIC

ATOM
1305
NH2
ARG
166
44.968
33.321
79.885
1.00
30.30
DIC

ATOM
1306
C
ARG
166
37.489
30.141
77.906
1.00
18.07
DIC

ATOM
1307
O
ARG
166
37.133
29.484
78.879
1.00
16.59
DIC

ATOM
1308
N
HIS
167
36.625
30.688
77.056
1.00
16.94
DIC

ATOM
1309
CA
HIS
167
35.188
30.563
77.273
1.00
16.99
DIC

ATOM
1310
CB
HIS
167
34.652
31.848
77.920
1.00
17.50
DIC

ATOM
1311
CG
HIS
167
35.333
32.218
79.201
1.00
17.81
DIC

ATOM
1312
CD2
HIS
167
36.422
32.989
79.441
1.00
16.88
DIC

ATOM
1313
ND1
HIS
167
34.896
31.780
80.434
1.00
19.03
DIC

ATOM
1314
CE1
HIS
167
35.683
32.266
81.378
1.00
19.16
DIC

ATOM
1315
NE2
HIS
167
36.617
33.004
80.802
1.00
18.25
DIC

ATOM
1316
C
HIS
167
34.413
30.311
75.987
1.00
17.81
DIC

ATOM
1317
O
HIS
167
34.939
30.471
74.884
1.00
18.91
DIC

ATOM
1318
N
ASP
168
33.154
29.916
76.141
1.00
16.56
DIC

ATOM
1319
CA
ASP
168
32.287
29.682
74.997
1.00
15.52
DIC

ATOM
1320
CB
ASP
168
31.461
28.406
75.187
1.00
14.57
DIC

ATOM
1321
CG
ASP
168
30.727
28.001
73.921
1.00
16.35
DIC

ATOM
1322
OD1
ASP
168
30.399
26.806
73.768
1.00
16.74
DIC

ATOM
1323
OD2
ASP
168
30.473
28.886
73.075
1.00
16.42
DIC

ATOM
1324
C
ASP
168
31.377
30.900
74.878
1.00
14.56
DIC

ATOM
1325
O
ASP
168
30.244
30.905
75.361
1.00
15.15
DIC

ATOM
1326
N
ILE
169
31.893
31.934
74.221
1.00
14.02
DIC

ATOM
1327
CA
ILE
169
31.169
33.186
74.040
1.00
14.18
DIC

ATOM
1328
CB
ILE
169
32.044
34.220
73.308
1.00
13.81
DIC

ATOM
1329
CG2
ILE
169
31.311
35.554
73.224
1.00
12.37
DIC

ATOM
1330
CG1
ILE
169
33.388
34.373
74.032
1.00
14.52
DIC

ATOM
1331
CD
ILE
169
33.270
34.779
75.498
1.00
15.00
DIC

ATOM
1332
C
ILE
169
29.849
33.038
73.281
1.00
13.80
DIC

ATOM
1333
O
ILE
169
28.873
33.729
73.584
1.00
12.98
DIC

ATOM
1334
N
PHE
170
29.809
32.145
72.300
1.00
14.34
DIC

ATOM
1335
CA
PHE
170
28.576
31.957
71.539
1.00
14.12
DIC

ATOM
1336
CB
PHE
170
28.818
31.075
70.317
1.00
15.04
DIC

ATOM
1337
CG
PHE
170
27.591
30.866
69.482
1.00
16.16
DIC

ATOM
1338
CD1
PHE
170
26.936
29.636
69.476
1.00
18.23
DIC

ATOM
1339
CD2
PHE
170
27.067
31.909
68.732
1.00
17.64
DIC

ATOM
1340
CE1
PHE
170
25.770
29.449
68.733
1.00
19.07
DIC

ATOM
1341
CE2
PHE
170
25.903
31.738
67.987
1.00
18.59
DIC

ATOM
1342
CZ
PHE
170
25.250
30.502
67.987
1.00
19.29
DIC

ATOM
1343
C
PHE
170
27.485
31.343
72.412
1.00
14.67
DIC

ATOM
1344
O
PHE
170
26.321
31.738
72.342
1.00
14.40
DIC

ATOM
1345
N
LYS
171
27.860
30.380
73.244
1.00
14.30
DIC

ATOM
1346
CA
LYS
171
26.887
29.755
74.120
1.00
15.30
DIC

ATOM
1347
CB
LYS
171
27.521
28.566
74.841
1.00
17.59
DIC

ATOM
1348
CG
LYS
171
26.511
27.636
75.474
1.00
22.27
DIC

ATOM
1349
CD
LYS
171
27.160
26.339
75.928
1.00
24.47
DIC

ATOM
1350
CE
LYS
171
27.627
25.502
74.744
1.00
27.47
DIC

ATOM
1351
NZ
LYS
171
28.299
24.238
75.192
1.00
31.51
DIC

ATOM
1352
C
LYS
171
26.396
30.802
75.121
1.00
14.40
DIC

ATOM
1353
O
LYS
171
25.197
30.933
75.355
1.00
15.04
DIC

ATOM
1354
N
MSE
172
27.327
31.553
75.702
1.00
12.53
DIC

ATOM
1355
CA
MSE
172
26.969
32.599
76.656
1.00
12.42
DIC

ATOM
1356
CB
MSE
172
28.232
33.280
77.203
1.00
12.59
DIC

ATOM
1357
CG
MSE
172
29.087
32.407
78.120
1.00
14.48
DIC

ATOM
1358
SE
MSE
172
30.875
33.131
78.357
1.00
19.27
DIC

ATOM
1359
CE
MSE
172
30.437
34.845
79.143
1.00
17.17
DIC

ATOM
1360
C
MSE
172
26.082
33.640
75.963
1.00
12.96
DIC

ATOM
1361
O
MSE
172
25.175
34.199
76.583
1.00
12.64
DIC

ATOM
1362
N
SER
173
26.347
33.892
74.679
1.00
11.38
DIC

ATOM
1363
CA
SER
173
25.566
34.863
73.914
1.00
11.90
DIC

ATOM
1364
CB
SER
173
26.205
35.118
72.542
1.00
12.42
DIC

ATOM
1365
OG
SER
173
27.411
35.867
72.657
1.00
11.32
DIC

ATOM
1366
C
SER
173
24.141
34.356
73.724
1.00
12.64
DIC

ATOM
1367
O
SER
173
23.172
35.079
73.988
1.00
9.99
DIC

ATOM
1368
N
SER
174
24.026
33.107
73.275
1.00
12.51
DIC

ATOM
1369
CA
SER
174
22.730
32.489
73.040
1.00
13.32
DIC

ATOM
1370
CB
SER
174
22.921
31.065
72.510
1.00
13.27
DIC

ATOM
1371
OG
SER
174
23.581
31.100
71.259
1.00
14.11
DIC

ATOM
1372
C
SER
174
21.861
32.472
74.292
1.00
13.57
DIC

ATOM
1373
O
SER
174
20.647
32.711
74.221
1.00
13.23
DIC

ATOM
1374
N
GLU
175
22.480
32.187
75.434
1.00
13.02
DIC

ATOM
1375
CA
GLU
175
21.758
32.151
76.698
1.00
14.86
DIC

ATOM
1376
CB
GLU
175
22.638
31.542
77.797
1.00
17.57
DIC

ATOM
1377
CG
GLU
175
23.168
30.152
77.451
1.00
22.53
DIC

ATOM
1378
CD
GLU
175
23.838
29.457
78.626
1.00
25.32
DIC

ATOM
1379
OE1
GLU
175
24.535
30.136
79.413
1.00
26.06
DIC

ATOM
1380
OE2
GLU
175
23.673
28.222
78.753
1.00
28.49
DIC

ATOM
1381
C
GLU
175
21.311
33.557
77.109
1.00
14.41
DIC

ATOM
1382
O
GLU
175
20.216
33.737
77.648
1.00
15.15
DIC

ATOM
1383
N
TRP
176
22.158
34.550
76.851
1.00
14.00
DIC

ATOM
1384
CA
TRP
176
21.832
35.932
77.198
1.00
13.86
DIC

ATOM
1385
CB
TRP
176
23.041
36.841
76.957
1.00
14.76
DIC

ATOM
1386
CG
TRP
176
22.907
38.186
77.599
1.00
14.73
DIC

ATOM
1387
CD2
TRP
176
22.383
39.375
76.999
1.00
15.10
DIC

ATOM
1388
CE2
TRP
176
22.400
40.383
77.987
1.00
15.08
DIC

ATOM
1389
CE3
TRP
176
21.896
39.685
75.725
1.00
14.14
DIC

ATOM
1390
CD1
TRP
176
23.213
38.511
78.884
1.00
15.31
DIC

ATOM
1391
NE1
TRP
176
22.912
39.829
79.128
1.00
14.86
DIC

ATOM
1392
CZ2
TRP
176
21.949
41.684
77.738
1.00
15.02
DIC

ATOM
1393
CZ3
TRP
176
21.446
40.979
75.479
1.00
13.42
DIC

ATOM
1394
CH2
TRP
176
21.476
41.960
76.480
1.00
14.16
DIC

ATOM
1395
C
TRP
176
20.653
36.396
76.342
1.00
14.32
DIC

ATOM
1396
O
TRP
176
19.709
37.024
76.842
1.00
14.65
DIC

ATOM
1397
N
VAL
177
20.707
36.082
75.050
1.00
13.88
DIC

ATOM
1398
CA
VAL
177
19.633
36.463
74.144
1.00
13.78
DIC

ATOM
1399
CB
VAL
177
19.917
36.021
72.692
1.00
13.94
DIC

ATOM
1400
CG1
VAL
177
18.673
36.235
71.837
1.00
14.54
DIC

ATOM
1401
CG2
VAL
177
21.072
36.828
72.112
1.00
11.49
DIC

ATOM
1402
C
VAL
177
18.320
35.839
74.601
1.00
15.27
DIC

ATOM
1403
O
VAL
177
17.269
36.476
74.560
1.00
13.41
DIC

ATOM
1404
N
GLU
178
18.373
34.591
75.043
1.00
17.23
DIC

ATOM
1405
CA
GLU
178
17.157
33.933
75.491
1.00
20.02
DIC

ATOM
1406
CB
GLU
178
17.469
32.505
75.952
1.00
22.23
DIC

ATOM
1407
CG
GLU
178
16.236
31.648
76.208
1.00
27.72
DIC

ATOM
1408
CD
GLU
178
15.214
31.727
75.078
1.00
29.81
DIC

ATOM
1409
OE1
GLU
178
15.590
31.535
73.898
1.00
31.17
DIC

ATOM
1410
OE2
GLU
178
14.027
31.979
75.376
1.00
32.50
DIC

ATOM
1411
C
GLU
178
16.549
34.735
76.636
1.00
20.30
DIC

ATOM
1412
O
GLU
178
15.328
34.848
76.758
1.00
20.62
DIC

ATOM
1413
N
GLN
179
17.416
35.320
77.453
1.00
19.19
DIC

ATOM
1414
CA
GLN
179
16.988
36.093
78.609
1.00
21.07
DIC

ATOM
1415
CB
GLN
179
18.136
36.120
79.625
1.00
23.36
DIC

ATOM
1416
CG
GLN
179
17.829
36.793
80.943
1.00
29.17
DIC

ATOM
1417
CD
GLN
179
19.050
36.865
81.852
1.00
33.38
DIC

ATOM
1418
OE1
GLN
179
18.995
37.432
82.947
1.00
35.19
DIC

ATOM
1419
NE2
GLN
179
20.163
36.290
81.396
1.00
34.26
DIC

ATOM
1420
C
GLN
179
16.516
37.524
78.313
1.00
19.81
DIC

ATOM
1421
O
GLN
179
15.593
38.018
78.956
1.00
18.51
DIC

ATOM
1422
N
TYR
180
17.125
38.183
77.333
1.00
18.69
DIC

ATOM
1423
CA
TYR
180
16.758
39.561
77.038
1.00
17.26
DIC

ATOM
1424
CB
TYR
180
17.962
40.469
77.277
1.00
17.36
DIC

ATOM
1425
CG
TYR
180
18.421
40.529
78.710
1.00
18.17
DIC

ATOM
1426
CD1
TYR
180
19.325
39.598
79.214
1.00
18.19
DIC

ATOM
1427
CE1
TYR
180
19.773
39.675
80.528
1.00
19.56
DIC

ATOM
1428
CD2
TYR
180
17.966
41.535
79.560
1.00
19.48
DIC

ATOM
1429
CE2
TYR
180
18.404
41.618
80.873
1.00
19.98
DIC

ATOM
1430
CZ
TYR
180
19.310
40.685
81.351
1.00
19.10
DIC

ATOM
1431
OH
TYR
180
19.760
40.772
82.650
1.00
21.76
DIC

ATOM
1432
C
TYR
180
16.206
39.861
75.651
1.00
17.56
DIC

ATOM
1433
O
TYR
180
16.068
41.030
75.288
1.00
16.75
DIC

ATOM
1434
N
LYS
181
15.886
38.826
74.884
1.00
17.25
DIC

ATOM
1435
CA
LYS
181
15.382
39.004
73.523
1.00
19.55
DIC

ATOM
1436
CB
LYS
181
15.086
37.636
72.898
1.00
22.09
DIC

ATOM
1437
CG
LYS
181
13.950
36.875
73.566
1.00
24.42
DIC

ATOM
1438
CD
LYS
181
13.778
35.491
72.946
1.00
28.02
DIC

ATOM
1439
CE
LYS
181
12.475
34.847
73.395
1.00
28.32
DIC

ATOM
1440
NZ
LYS
181
12.358
34.833
74.878
1.00
31.53
DIC

ATOM
1441
C
LYS
181
14.150
39.902
73.367
1.00
20.33
DIC

ATOM
1442
O
LYS
181
13.940
40.489
72.304
1.00
19.96
DIC

ATOM
1443
N
ASP
182
13.336
40.012
74.410
1.00
19.39
DIC

ATOM
1444
CA
ASP
182
12.132
40.830
74.320
1.00
21.97
DIC

ATOM
1445
CB
ASP
182
11.053
40.288
75.258
1.00
23.67
DIC

ATOM
1446
CG
ASP
182
10.476
38.965
74.785
1.00
26.84
DIC

ATOM
1447
OD1
ASP
182
9.781
38.308
75.587
1.00
29.25
DIC

ATOM
1448
OD2
ASP
182
10.703
38.585
73.614
1.00
27.07
DIC

ATOM
1449
C
ASP
182
12.368
42.298
74.634
1.00
21.11
DIC

ATOM
1450
O
ASP
182
11.472
43.121
74.460
1.00
21.52
DIC

ATOM
1451
N
VAL
183
13.568
42.632
75.096
1.00
19.54
DIC

ATOM
1452
CA
VAL
183
13.861
44.015
75.435
1.00
18.64
DIC

ATOM
1453
CB
VAL
183
14.093
44.160
76.968
1.00
20.70
DIC

ATOM
1454
CG1
VAL
183
15.332
43.388
77.396
1.00
19.44
DIC

ATOM
1455
CG2
VAL
183
14.214
45.617
77.341
1.00
24.74
DIC

ATOM
1456
C
VAL
183
15.050
44.606
74.682
1.00
18.43
DIC

ATOM
1457
O
VAL
183
15.104
45.820
74.462
1.00
18.40
DIC

ATOM
1458
N
MSE
184
15.998
43.766
74.276
1.00
16.59
DIC

ATOM
1459
CA
MSE
184
17.173
44.276
73.573
1.00
15.96
DIC

ATOM
1460
CB
MSE
184
18.173
43.135
73.278
1.00
17.24
DIC

ATOM
1461
CG
MSE
184
17.620
41.917
72.564
1.00
18.77
DIC

ATOM
1462
SE
MSE
184
18.898
40.440
72.634
1.00
17.57
DIC

ATOM
1463
CE
MSE
184
20.063
40.984
71.194
1.00
13.79
DIC

ATOM
1464
C
MSE
184
16.804
45.050
72.305
1.00
15.73
DIC

ATOM
1465
O
MSE
184
15.940
44.637
71.525
1.00
13.50
DIC

ATOM
1466
N
GLN
185
17.460
46.195
72.125
1.00
13.82
DIC

ATOM
1467
CA
GLN
185
17.207
47.074
70.989
1.00
13.45
DIC

ATOM
1468
CB
GLN
185
16.781
48.460
71.496
1.00
15.92
DIC

ATOM
1469
CG
GLN
185
15.485
48.468
72.306
1.00
15.22
DIC

ATOM
1470
CD
GLN
185
15.126
49.847
72.864
1.00
18.20
DIC

ATOM
1471
OE1
GLN
185
15.648
50.875
72.417
1.00
16.73
DIC

ATOM
1472
NE2
GLN
185
14.215
49.870
73.836
1.00
15.67
DIC

ATOM
1473
C
GLN
185
18.426
47.231
70.084
1.00
13.75
DIC

ATOM
1474
O
GLN
185
18.301
47.694
68.945
1.00
12.35
DIC

ATOM
1475
N
TYR
186
19.602
46.849
70.580
1.00
10.80
DIC

ATOM
1476
CA
TYR
186
20.809
47.014
69.785
1.00
12.98
DIC

ATOM
1477
CB
TYR
186
21.742
48.010
70.479
1.00
14.55
DIC

ATOM
1478
CG
TYR
186
21.067
49.351
70.690
1.00
15.13
DIC

ATOM
1479
CD1
TYR
186
20.569
49.720
71.941
1.00
13.69
DIC

ATOM
1480
CE1
TYR
186
19.868
50.918
72.116
1.00
14.58
DIC

ATOM
1481
CD2
TYR
186
20.854
50.218
69.616
1.00
17.25
DIC

ATOM
1482
CE2
TYR
186
20.152
51.414
69.778
1.00
17.83
DIC

ATOM
1483
CZ
TYR
186
19.662
51.756
71.030
1.00
16.39
DIC

ATOM
1484
OH
TYR
186
18.958
52.928
71.182
1.00
17.08
DIC

ATOM
1485
C
TYR
186
21.564
45.764
69.345
1.00
11.95
DIC

ATOM
1486
O
TYR
186
22.758
45.813
69.056
1.00
10.67
DIC

ATOM
1487
N
GLN
187
20.853
44.644
69.313
1.00
10.94
DIC

ATOM
1488
CA
GLN
187
21.400
43.393
68.813
1.00
10.45
DIC

ATOM
1489
CB
GLN
187
21.435
43.521
67.281
1.00
11.05
DIC

ATOM
1490
CG
GLN
187
20.042
43.956
66.773
1.00
12.55
DIC

ATOM
1491
CD
GLN
187
19.927
44.215
65.279
1.00
13.86
DIC

ATOM
1492
OE1
GLN
187
18.821
44.351
64.766
1.00
16.40
DIC

ATOM
1493
NE2
GLN
187
21.048
44.293
64.582
1.00
12.57
DIC

ATOM
1494
C
GLN
187
22.735
42.929
69.407
1.00
9.77
DIC

ATOM
1495
O
GLN
187
22.850
42.793
70.627
1.00
9.45
DIC

ATOM
1496
N
ASP
188
23.741
42.683
68.568
1.00
8.20
DIC

ATOM
1497
CA
ASP
188
25.030
42.205
69.071
1.00
8.35
DIC

ATOM
1498
CB
ASP
188
25.999
41.978
67.916
1.00
9.13
DIC

ATOM
1499
CG
ASP
188
26.220
43.224
67.111
1.00
12.26
DIC

ATOM
1500
OD1
ASP
188
25.312
43.586
66.337
1.00
13.14
DIC

ATOM
1501
OD2
ASP
188
27.286
43.846
67.269
1.00
10.65
DIC

ATOM
1502
C
ASP
188
25.674
43.146
70.089
1.00
9.52
DIC

ATOM
1503
O
ASP
188
26.453
42.720
70.950
1.00
8.45
DIC

ATOM
1504
N
GLN
189
25.354
44.428
69.992
1.00
9.27
DIC

ATOM
1505
CA
GLN
189
25.910
45.409
70.915
1.00
9.53
DIC

ATOM
1506
CB
GLN
189
25.548
46.816
70.433
1.00
11.21
DIC

ATOM
1507
CG
GLN
189
26.252
47.950
71.140
1.00
13.73
DIC

ATOM
1508
CD
GLN
189
26.138
49.248
70.346
1.00
15.81
DIC

ATOM
1509
OE1
GLN
189
27.060
49.627
69.622
1.00
13.26
DIC

ATOM
1510
NE2
GLN
189
24.989
49.919
70.461
1.00
13.80
DIC

ATOM
1511
C
GLN
189
25.386
45.156
72.333
1.00
9.28
DIC

ATOM
1512
O
GLN
189
26.136
45.251
73.300
1.00
7.78
DIC

ATOM
1513
N
ASP
190
24.100
44.828
72.457
1.00
9.50
DIC

ATOM
1514
CA
ASP
190
23.521
44.542
73.771
1.00
10.89
DIC

ATOM
1515
CB
ASP
190
22.021
44.259
73.665
1.00
9.92
DIC

ATOM
1516
CG
ASP
190
21.208
45.499
73.357
1.00
11.74
DIC

ATOM
1517
OD1
ASP
190
20.197
45.360
72.639
1.00
10.56
DIC

ATOM
1518
OD2
ASP
190
21.570
46.600
73.841
1.00
9.10
DIC

ATOM
1519
C
ASP
190
24.186
43.310
74.362
1.00
9.43
DIC

ATOM
1520
O
ASP
190
24.483
43.263
75.553
1.00
10.61
DIC

ATOM
1521
N
ILE
191
24.389
42.302
73.524
1.00
8.72
DIC

ATOM
1522
CA
ILE
191
24.998
41.061
73.970
1.00
8.21
DIC

ATOM
1523
CB
ILE
191
25.125
40.056
72.811
1.00
8.37
DIC

ATOM
1524
CG2
ILE
191
25.797
38.766
73.316
1.00
6.32
DIC

ATOM
1525
CG1
ILE
191
23.737
39.736
72.252
1.00
6.91
DIC

ATOM
1526
CD
ILE
191
23.765
38.864
71.004
1.00
6.73
DIC

ATOM
1527
C
ILE
191
26.368
41.277
74.590
1.00
9.22
DIC

ATOM
1528
O
ILE
191
26.640
40.794
75.695
1.00
9.62
DIC

ATOM
1529
N
LEU
192
27.229
42.011
73.889
1.00
9.09
DIC

ATOM
1530
CA
LEU
192
28.574
42.276
74.391
1.00
9.40
DIC

ATOM
1531
CB
LEU
192
29.376
43.060
73.343
1.00
9.83
DIC

ATOM
1532
CG
LEU
192
29.588
42.326
72.011
1.00
11.31
DIC

ATOM
1533
CD1
LEU
192
29.942
43.307
70.901
1.00
12.97
DIC

ATOM
1534
CD2
LEU
192
30.678
41.286
72.188
1.00
12.52
DIC

ATOM
1535
C
LEU
192
28.529
43.047
75.715
1.00
11.04
DIC

ATOM
1536
O
LEU
192
29.272
42.734
76.652
1.00
9.18
DIC

ATOM
1537
N
ASN
193
27.662
44.053
75.797
1.00
10.74
DIC

ATOM
1538
CA
ASN
193
27.547
44.847
77.024
1.00
12.24
DIC

ATOM
1539
CB
ASN
193
26.619
46.054
76.808
1.00
10.61
DIC

ATOM
1540
CG
ASN
193
27.362
47.284
76.280
1.00
13.95
DIC

ATOM
1541
OD1
ASN
193
28.031
47.991
77.039
1.00
12.61
DIC

ATOM
1542
ND2
ASN
193
27.251
47.536
74.974
1.00
10.56
DIC

ATOM
1543
C
ASN
193
27.010
43.986
78.162
1.00
12.42
DIC

ATOM
1544
O
ASN
193
27.515
44.039
79.284
1.00
14.38
DIC

ATOM
1545
N
GLY
194
25.981
43.198
77.872
1.00
12.71
DIC

ATOM
1546
CA
GLY
194
25.407
42.348
78.898
1.00
13.05
DIC

ATOM
1547
C
GLY
194
26.403
41.342
79.443
1.00
13.73
DIC

ATOM
1548
O
GLY
194
26.541
41.172
80.656
1.00
12.77
DIC

ATOM
1549
N
LEU
195
27.122
40.679
78.547
1.00
12.99
DIC

ATOM
1550
CA
LEU
195
28.086
39.674
78.969
1.00
13.81
DIC

ATOM
1551
CB
LEU
195
28.533
38.826
77.769
1.00
11.07
DIC

ATOM
1552
CG
LEU
195
27.562
37.911
77.016
1.00
11.26
DIC

ATOM
1553
CD1
LEU
195
28.303
37.265
75.841
1.00
8.90
DIC

ATOM
1554
CD2
LEU
195
27.024
36.820
77.938
1.00
11.82
DIC

ATOM
1555
C
LEU
195
29.339
40.199
79.675
1.00
13.59
DIC

ATOM
1556
O
LEU
195
29.822
39.580
80.620
1.00
12.85
DIC

ATOM
1557
N
PHE
196
29.860
41.341
79.235
1.00
12.78
DIC

ATOM
1558
CA
PHE
196
31.110
41.842
79.797
1.00
12.08
DIC

ATOM
1559
CB
PHE
196
32.064
42.204
78.652
1.00
13.05
DIC

ATOM
1560
CG
PHE
196
32.214
41.119
77.624
1.00
13.16
DIC

ATOM
1561
CD1
PHE
196
32.244
39.780
78.004
1.00
10.72
DIC

ATOM
1562
CD2
PHE
196
32.359
41.436
76.275
1.00
13.59
DIC

ATOM
1563
CE1
PHE
196
32.419
38.766
77.058
1.00
13.82
DIC

ATOM
1564
CE2
PHE
196
32.534
40.430
75.318
1.00
12.70
DIC

ATOM
1565
CZ
PHE
196
32.565
39.095
75.709
1.00
11.81
DIC

ATOM
1566
C
PHE
196
31.071
42.993
80.786
1.00
13.04
DIC

ATOM
1567
O
PHE
196
32.125
43.434
81.257
1.00
11.71
DIC

ATOM
1568
N
LYS
197
29.875
43.480
81.095
1.00
11.55
DIC

ATOM
1569
CA
LYS
197
29.731
44.577
82.032
1.00
13.00
DIC

ATOM
1570
CB
LYS
197
28.250
44.784
82.381
1.00
12.60
DIC

ATOM
1571
CG
LYS
197
27.540
43.582
83.016
1.00
13.14
DIC

ATOM
1572
CD
LYS
197
26.063
43.899
83.223
1.00
11.03
DIC

ATOM
1573
CE
LYS
197
25.316
42.798
83.972
1.00
14.35
DIC

ATOM
1574
NZ
LYS
197
25.265
41.519
83.214
1.00
14.09
DIC

ATOM
1575
C
LYS
197
30.545
44.286
83.287
1.00
14.20
DIC

ATOM
1576
O
LYS
197
30.494
43.182
83.826
1.00
14.43
DIC

ATOM
1577
N
GLY
198
31.319
45.272
83.731
1.00
15.83
DIC

ATOM
1578
CA
GLY
198
32.146
45.094
84.914
1.00
16.30
DIC

ATOM
1579
C
GLY
198
33.546
44.622
84.566
1.00
16.73
DIC

ATOM
1580
O
GLY
198
34.457
44.678
85.395
1.00
15.89
DIC

ATOM
1581
N
GLY
199
33.718
44.158
83.330
1.00
15.83
DIC

ATOM
1582
CA
GLY
199
35.014
43.676
82.886
1.00
15.74
DIC

ATOM
1583
C
GLY
199
35.395
44.315
81.563
1.00
17.97
DIC

ATOM
1584
O
GLY
199
35.854
43.644
80.641
1.00
16.51
DIC

ATOM
1585
N
VAL
200
35.191
45.625
81.484
1.00
16.42
DIC

ATOM
1586
CA
VAL
200
35.498
46.397
80.292
1.00
17.21
DIC

ATOM
1587
CB
VAL
200
34.219
47.034
79.696
1.00
16.55
DIC

ATOM
1588
CG1
VAL
200
34.586
47.977
78.547
1.00
19.60
DIC

ATOM
1589
CG2
VAL
200
33.275
45.951
79.204
1.00
17.01
DIC

ATOM
1590
C
VAL
200
36.471
47.533
80.596
1.00
16.86
DIC

ATOM
1591
O
VAL
200
36.337
48.228
81.601
1.00
16.58
DIC

ATOM
1592
N
CYS
201
37.454
47.708
79.720
1.00
16.59
DIC

ATOM
1593
CA
CYS
201
38.412
48.793
79.853
1.00
17.05
DIC

ATOM
1594
CB
CYS
201
39.802
48.345
79.391
1.00
19.85
DIC

ATOM
1595
SG
CYS
201
41.031
49.677
79.319
1.00
29.46
DIC

ATOM
1596
C
CYS
201
37.847
49.848
78.912
1.00
15.68
DIC

ATOM
1597
O
CYS
201
37.519
49.543
77.765
1.00
15.05
DIC

ATOM
1598
N
TYR
202
37.697
51.079
79.386
1.00
15.85
DIC

ATOM
1599
CA
TYR
202
37.132
52.114
78.529
1.00
14.50
DIC

ATOM
1600
CB
TYR
202
36.236
53.054
79.333
1.00
15.59
DIC

ATOM
1601
CG
TYR
202
35.102
52.377
80.061
1.00
17.50
DIC

ATOM
1602
CD1
TYR
202
35.173
52.162
81.434
1.00
17.93
DIC

ATOM
1603
CE1
TYR
202
34.125
51.583
82.124
1.00
19.81
DIC

ATOM
1604
CD2
TYR
202
33.944
51.984
79.388
1.00
18.20
DIC

ATOM
1605
CE2
TYR
202
32.882
51.396
80.072
1.00
19.70
DIC

ATOM
1606
CZ
TYR
202
32.983
51.205
81.447
1.00
21.08
DIC

ATOM
1607
OH
TYR
202
31.941
50.670
82.163
1.00
20.73
DIC

ATOM
1608
C
TYR
202
38.206
52.933
77.831
1.00
14.93
DIC

ATOM
1609
O
TYR
202
39.161
53.372
78.462
1.00
15.02
DIC

ATOM
1610
N
ALA
203
38.038
53.130
76.525
1.00
13.78
DIC

ATOM
1611
CA
ALA
203
38.980
53.913
75.725
1.00
12.83
DIC

ATOM
1612
CB
ALA
203
39.210
53.243
74.377
1.00
11.34
DIC

ATOM
1613
C
ALA
203
38.402
55.306
75.514
1.00
13.01
DIC

ATOM
1614
O
ALA
203
37.196
55.506
75.643
1.00
12.43
DIC

ATOM
1615
N
ASN
204
39.257
56.272
75.195
1.00
12.21
DIC

ATOM
1616
CA
ASN
204
38.774
57.628
74.962
1.00
11.59
DIC

ATOM
1617
CB
ASN
204
39.936
58.587
74.745
1.00
11.55
DIC

ATOM
1618
CG
ASN
204
39.488
60.025
74.710
1.00
12.55
DIC

ATOM
1619
OD1
ASN
204
39.185
60.613
75.752
1.00
15.02
DIC

ATOM
1620
ND2
ASN
204
39.418
60.598
73.512
1.00
8.71
DIC

ATOM
1621
C
ASN
204
37.887
57.647
73.722
1.00
11.96
DIC

ATOM
1622
O
ASN
204
38.075
56.844
72.803
1.00
10.62
DIC

ATOM
1623
N
SER
205
36.927
58.566
73.690
1.00
9.54
DIC

ATOM
1624
CA
SER
205
36.031
58.653
72.550
1.00
11.60
DIC

ATOM
1625
CB
SER
205
34.888
59.634
72.853
1.00
11.61
DIC

ATOM
1626
OG
SER
205
33.979
59.055
73.784
1.00
10.36
DIC

ATOM
1627
C
SER
205
36.718
59.013
71.227
1.00
11.44
DIC

ATOM
1628
O
SER
205
36.099
58.920
70.166
1.00
11.98
DIC

ATOM
1629
N
ARG
206
37.994
59.396
71.270
1.00
10.73
DIC

ATOM
1630
CA
ARG
206
38.686
59.724
70.028
1.00
10.60
DIC

ATOM
1631
CB
ARG
206
40.089
60.297
70.305
1.00
10.09
DIC

ATOM
1632
CG
ARG
206
41.089
59.315
70.924
1.00
11.89
DIC

ATOM
1633
CD
ARG
206
42.374
60.043
71.336
1.00
12.09
DIC

ATOM
1634
NE
ARG
206
42.939
60.770
70.203
1.00
12.43
DIC

ATOM
1635
CZ
ARG
206
43.984
60.367
69.484
1.00
10.79
DIC

ATOM
1636
NH1
ARG
206
44.610
59.240
69.782
1.00
11.45
DIC

ATOM
1637
NH2
ARG
206
44.378
61.078
68.438
1.00
9.92
DIC

ATOM
1638
C
ARG
206
38.789
58.473
69.149
1.00
9.80
DIC

ATOM
1639
O
ARG
206
38.932
58.573
67.937
1.00
9.66
DIC

ATOM
1640
N
PHE
207
38.700
57.295
69.757
1.00
9.55
DIC

ATOM
1641
CA
PHE
207
38.801
56.056
68.989
1.00
9.03
DIC

ATOM
1642
CB
PHE
207
39.554
55.009
69.802
1.00
8.47
DIC

ATOM
1643
CG
PHE
207
40.980
55.386
70.082
1.00
7.54
DIC

ATOM
1644
CD1
PHE
207
41.388
55.703
71.368
1.00
7.40
DIC

ATOM
1645
CD2
PHE
207
41.906
55.455
69.048
1.00
7.60
DIC

ATOM
1646
CE1
PHE
207
42.701
56.087
71.626
1.00
9.11
DIC

ATOM
1647
CE2
PHE
207
43.217
55.837
69.290
1.00
10.35
DIC

ATOM
1648
CZ
PHE
207
43.616
56.156
70.588
1.00
9.62
DIC

ATOM
1649
C
PHE
207
37.472
55.488
68.495
1.00
9.66
DIC

ATOM
1650
O
PHE
207
37.416
54.376
67.966
1.00
10.94
DIC

ATOM
1651
N
ASN
208
36.404
56.254
68.683
1.00
9.27
DIC

ATOM
1652
CA
ASN
208
35.079
55.866
68.229
1.00
10.30
DIC

ATOM
1653
CB
ASN
208
34.475
54.792
69.140
1.00
9.11
DIC

ATOM
1654
CG
ASN
208
33.285
54.091
68.497
1.00
9.58
DIC

ATOM
1655
OD1
ASN
208
32.668
54.626
67.573
1.00
9.75
DIC

ATOM
1656
ND2
ASN
208
32.956
52.896
68.981
1.00
5.82
DIC

ATOM
1657
C
ASN
208
34.249
57.144
68.293
1.00
11.23
DIC

ATOM
1658
O
ASN
208
33.407
57.303
69.172
1.00
11.29
DIC

ATOM
1659
N
PHE
209
34.514
58.060
67.359
1.00
11.31
DIC

ATOM
1660
CA
PHE
209
33.835
59.357
67.300
1.00
11.35
DIC

ATOM
1661
CB
PHE
209
34.800
60.407
66.725
1.00
10.07
DIC

ATOM
1662
CG
PHE
209
34.402
61.833
67.007
1.00
10.65
DIC

ATOM
1663
CD1
PHE
209
34.457
62.348
68.300
1.00
12.23
DIC

ATOM
1664
CD2
PHE
209
33.991
62.669
65.972
1.00
12.03
DIC

ATOM
1665
CE1
PHE
209
34.110
63.682
68.558
1.00
14.04
DIC

ATOM
1666
CE2
PHE
209
33.646
63.991
66.213
1.00
12.22
DIC

ATOM
1667
CZ
PHE
209
33.705
64.504
67.512
1.00
13.59
DIC

ATOM
1668
C
PHE
209
32.585
59.241
66.422
1.00
11.70
DIC

ATOM
1669
O
PHE
209
32.676
59.193
65.198
1.00
10.06
DIC

ATOM
1670
N
MSE
210
31.419
59.214
67.057
1.00
11.79
DIC

ATOM
1671
CA
MSE
210
30.156
59.050
66.339
1.00
13.38
DIC

ATOM
1672
CB
MSE
210
29.343
57.935
67.022
1.00
13.32
DIC

ATOM
1673
CG
MSE
210
30.087
56.594
67.064
1.00
14.56
DIC

ATOM
1674
SE
MSE
210
29.331
55.241
68.266
1.00
14.26
DIC

ATOM
1675
CE
MSE
210
30.349
55.687
69.839
1.00
11.50
DIC

ATOM
1676
C
MSE
210
29.349
60.344
66.251
1.00
12.91
DIC

ATOM
1677
O
MSE
210
29.739
61.369
66.815
1.00
11.87
DIC

ATOM
1678
N
PRO
211
28.225
60.323
65.512
1.00
14.20
DIC

ATOM
1679
CD
PRO
211
27.659
59.232
64.699
1.00
12.16
DIC

ATOM
1680
CA
PRO
211
27.406
61.533
65.386
1.00
14.02
DIC

ATOM
1681
CB
PRO
211
26.159
61.028
64.667
1.00
13.37
DIC

ATOM
1682
CG
PRO
211
26.719
59.976
63.771
1.00
14.79
DIC

ATOM
1683
C
PRO
211
27.078
62.175
66.732
1.00
14.59
DIC

ATOM
1684
O
PRO
211
27.129
63.401
66.873
1.00
14.82
DIC

ATOM
1685
N
THR
212
26.747
61.356
67.724
1.00
12.84
DIC

ATOM
1686
CA
THR
212
26.415
61.915
69.026
1.00
12.38
DIC

ATOM
1687
CB
THR
212
25.861
60.847
69.985
1.00
11.66
DIC

ATOM
1688
OG1
THR
212
24.754
60.185
69.367
1.00
10.96
DIC

ATOM
1689
CG2
THR
212
25.354
61.505
71.274
1.00
12.45
DIC

ATOM
1690
C
THR
212
27.614
62.618
69.670
1.00
13.42
DIC

ATOM
1691
O
THR
212
27.448
63.662
70.307
1.00
12.42
DIC

ATOM
1692
N
ASN
213
28.813
62.056
69.511
1.00
11.99
DIC

ATOM
1693
CA
ASN
213
30.016
62.680
70.070
1.00
11.39
DIC

ATOM
1694
CB
ASN
213
31.268
61.848
69.759
1.00
10.41
DIC

ATOM
1695
CG
ASN
213
31.210
60.442
70.348
1.00
9.67
DIC

ATOM
1696
OD1
ASN
213
31.672
60.196
71.466
1.00
10.66
DIC

ATOM
1697
ND2
ASN
213
30.637
59.515
69.595
1.00
7.33
DIC

ATOM
1698
C
ASN
213
30.155
64.050
69.412
1.00
13.60
DIC

ATOM
1699
O
ASN
213
30.443
65.045
70.076
1.00
13.49
DIC

ATOM
1700
N
TYR
214
29.948
64.093
68.097
1.00
13.25
DIC

ATOM
1701
CA
TYR
214
30.042
65.345
67.358
1.00
16.71
DIC

ATOM
1702
CB
TYR
214
29.790
65.116
65.863
1.00
17.70
DIC

ATOM
1703
CG
TYR
214
29.918
66.380
65.041
1.00
21.47
DIC

ATOM
1704
CD1
TYR
214
31.165
66.831
64.609
1.00
23.78
DIC

ATOM
1705
CE1
TYR
214
31.297
68.018
63.888
1.00
24.82
DIC

ATOM
1706
CD2
TYP
214
28.798
67.147
64.732
1.00
24.77
DIC

ATOM
1707
CE2
TYR
214
28.915
68.339
64.013
1.00
26.67
DIC

ATOM
1708
CZ
TYR
214
30.168
68.768
63.594
1.00
27.64
DIC

ATOM
1709
OH
TYR
214
30.291
69.949
62.885
1.00
28.93
DIC

ATOM
1710
C
TYR
214
29.014
66.340
67.894
1.00
18.21
DIC

ATOM
1711
O
TYR
214
29.348
67.483
68.209
1.00
16.24
DIC

ATOM
1712
N
ALA
215
27.759
65.906
67.985
1.00
18.99
DIC

ATOM
1713
CA
ALA
215
26.700
66.774
68.488
1.00
21.66
DIC

ATOM
1714
CB
ALA
215
25.379
66.021
68.547
1.00
19.99
DIC

ATOM
1715
C
ALA
215
27.096
67.252
69.877
1.00
24.02
DIC

ATOM
1716
O
ALA
215
26.776
68.374
70.277
1.00
23.13
DIC

ATOM
1717
N
PHE
216
27.802
66.397
70.609
1.00
26.12
DIC

ATOM
1718
CA
PHE
216
28.240
66.755
71.945
1.00
31.30
DIC

ATOM
1719
CB
PHE
216
28.883
65.562
72.648
1.00
32.05
DIC

ATOM
1720
CG
PHE
216
29.073
65.769
74.123
1.00
34.39
DIC

ATOM
1721
CD1
PHE
216
27.973
65.938
74.960
1.00
34.65
DIC

ATOM
1722
CD2
PHE
216
30.350
65.808
74.677
1.00
33.95
DIC

ATOM
1723
CE1
PHE
216
28.141
66.146
76.328
1.00
34.98
DIC

ATOM
1724
CE2
PHE
216
30.528
66.016
76.046
1.00
35.12
DIC

ATOM
1725
CZ
PHE
216
29.422
66.186
76.871
1.00
34.75
DIC

ATOM
1726
C
PHE
216
29.237
67.905
71.839
1.00
34.43
DIC

ATOM
1727
O
PHE
216
29.444
68.639
72.802
1.00
34.68
DIC

ATOM
1728
N
MSE
217
29.862
68.048
70.670
1.00
37.59
DIC

ATOM
1729
CA
MSE
217
30.794
69.152
70.445
1.00
40.37
DIC

ATOM
1730
CB
MSE
217
31.572
68.981
69.134
1.00
42.90
DIC

ATOM
1731
CG
MSE
217
32.503
67.782
69.051
1.00
46.79
DIC

ATOM
1732
SE
MSE
217
33.962
67.801
70.312
1.00
54.87
DIC

ATOM
1733
CE
MSE
217
34.812
69.461
69.818
1.00
51.10
DIC

ATOM
1734
C
MSE
217
29.898
70.381
70.329
1.00
40.97
DIC

ATOM
1735
O
MSE
217
29.756
70.961
69.249
1.00
41.56
DIC

ATOM
1736
N
ALA
218
29.278
70.748
71.446
1.00
41.05
DIC

ATOM
1737
CA
ALA
218
28.374
71.890
71.526
1.00
40.94
DIC

ATOM
1738
CB
ALA
218
27.354
71.852
70.384
1.00
40.11
DIC

ATOM
1739
C
ALA
218
27.662
71.818
72.877
1.00
40.36
DIC

ATOM
1740
OT1
ALA
218
26.415
71.718
72.922
1.00
18.66
DIC

ATOM
1741
OT2
ALA
218
28.375
71.852
73.894
1.00
18.66
DIC

ATOM
1742
CB
ALA
222
25.959
69.432
79.985
1.00
40.17
DIC

ATOM
1743
C
ALA
222
25.843
67.067
79.228
1.00
40.29
DIC

ATOM
1744
O
ALA
222
24.922
66.318
78.894
1.00
42.05
DIC

ATOM
1745
N
ALA
222
24.590
68.826
78.056
1.00
38.20
DIC

ATOM
1746
CA
ALA
222
25.844
68.531
78.798
1.00
39.59
DIC

ATOM
1747
N
SER
223
26.884
66.669
79.959
1.00
39.44
DIC

ATOM
1748
CA
SER
223
27.149
65.301
80.439
1.00
38.81
DIC

ATOM
1749
CB
SER
223
28.411
65.284
81.274
1.00
39.72
DIC

ATOM
1750
OG
SER
223
28.906
63.978
81.237
1.00
41.10
DIC

ATOM
1751
C
SER
223
26.135
64.549
81.278
1.00
37.39
DIC

ATOM
1752
O
SER
223
25.489
65.136
82.124
1.00
36.31
DIC

ATOM
1753
N
ARG
224
26.103
63.225
81.092
1.00
35.52
DIC

ATOM
1754
CA
ARG
224
25.222
62.245
81.777
1.00
34.47
DIC

ATOM
1755
CB
ARG
224
25.124
60.971
80.896
1.00
33.95
DIC

ATOM
1756
CG
ARG
224
23.749
60.549
80.430
1.00
35.88
DIC

ATOM
1757
CD
ARG
224
23.144
59.698
81.482
1.00
36.44
DIC

ATOM
1758
NE
ARG
224
21.699
59.611
81.371
1.00
37.64
DIC

ATOM
1759
CZ
ARG
224
20.913
59.130
82.315
1.00
38.47
DIC

ATOM
1760
NH1
ARG
224
19.608
59.097
82.127
1.00
38.82
DIC

ATOM
1761
NH2
ARG
224
21.445
58.665
83.422
1.00
39.33
DIC

ATOM
1762
C
ARG
224
25.652
61.827
83.196
1.00
32.76
DIC

ATOM
1763
O
ARG
224
24.831
61.475
84.013
1.00
33.35
DIC

ATOM
1764
N
HIS
225
26.950
61.845
83.467
1.00
31.17
DIC

ATOM
1765
CA
HIS
225
27.465
61.469
84.792
1.00
28.74
DIC

ATOM
1766
CB
HIS
225
28.059
60.055
84.761
1.00
28.53
DIC

ATOM
1767
CG
HIS
225
27.099
59.000
84.295
1.00
28.65
DIC

ATOM
1768
CD2
HIS
225
26.931
58.416
83.083
1.00
28.14
DIC

ATOM
1769
ND1
HIS
225
26.140
58.451
85.118
1.00
26.79
DIC

ATOM
1770
CE1
HIS
225
25.422
57.576
84.435
1.00
27.52
DIC

ATOM
1771
NE2
HIS
225
25.881
57.537
83.197
1.00
27.77
DIC

ATOM
1772
C
HIS
225
28.535
62.441
85.283
1.00
28.61
DIC

ATOM
1773
O
HIS
225
29.209
63.061
84.468
1.00
28.11
DIC

ATOM
1774
N
THR
226
28.700
62.567
86.600
1.00
26.51
DIC

ATOM
1775
CA
THR
226
29.713
63.466
87.150
1.00
24.55
DIC

ATOM
1776
CB
THR
226
29.241
64.076
88.488
1.00
24.86
DIC

ATOM
1777
OG1
THR
226
28.907
63.025
89.402
1.00
25.94
DIC

ATOM
1778
CG2
THR
226
28.010
64.942
88.268
1.00
24.89
DIC

ATOM
1779
C
THR
226
31.007
62.678
87.360
1.00
23.42
DIC

ATOM
1780
O
THR
226
32.091
63.247
87.525
1.00
22.81
DIC

ATOM
1781
N
ASP
227
30.875
61.353
87.352
1.00
21.74
DIC

ATOM
1782
CA
ASP
227
32.014
60.456
87.515
1.00
20.74
DIC

ATOM
1783
CB
ASP
227
31.634
59.036
87.073
1.00
20.56
DIC

ATOM
1784
CG
ASP
227
32.817
58.091
87.067
1.00
20.53
DIC

ATOM
1785
OD1
ASP
227
32.691
56.986
86.495
1.00
22.53
DIC

ATOM
1786
OD2
ASP
227
33.872
58.442
87.633
1.00
21.73
DIC

ATOM
1787
C
ASP
227
33.188
60.957
86.672
1.00
20.76
DIC

ATOM
1788
O
ASP
227
33.118
60.985
85.440
1.00
17.27
DIC

ATOM
1789
N
PRO
228
34.288
61.351
87.331
1.00
21.29
DIC

ATOM
1790
CD
PRO
228
34.547
61.210
88.776
1.00
22.76
DIC

ATOM
1791
CA
PRO
228
35.476
61.853
86.634
1.00
21.24
DIC

ATOM
1792
CB
PRO
228
36.476
62.076
87.772
1.00
23.32
DIC

ATOM
1793
CG
PRO
228
36.047
61.074
88.809
1.00
24.69
DIC

ATOM
1794
C
PRO
228
36.010
60.921
85.549
1.00
21.24
DIC

ATOM
1795
O
PRO
228
36.503
61.383
84.518
1.00
20.14
DIC

ATOM
1796
N
LEU
229
35.913
59.612
85.766
1.00
20.48
DIC

ATOM
1797
CA
LEU
229
36.397
58.677
84.758
1.00
19.34
DIC

ATOM
1798
CB
LEU
229
36.439
57.257
85.318
1.00
20.42
DIC

ATOM
1799
CG
LEU
229
36.953
56.172
84.371
1.00
22.18
DIC

ATOM
1800
CD1
LEU
229
37.630
55.069
85.167
1.00
22.60
DIC

ATOM
1801
CD2
LEU
229
35.792
55.624
83.545
1.00
20.97
DIC

ATOM
1802
C
LEU
229
35.502
58.739
83.526
1.00
17.99
DIC

ATOM
1803
O
LEU
229
35.990
58.809
82.397
1.00
17.37
DIC

ATOM
1804
N
TYR
230
34.192
58.723
83.746
1.00
18.30
DIC

ATOM
1805
CA
TYR
230
33.234
58.796
82.647
1.00
17.44
DIC

ATOM
1806
CB
TYR
230
31.799
58.862
83.189
1.00
18.25
DIC

ATOM
1807
CG
TYR
230
30.741
58.971
82.109
1.00
16.68
DIC

ATOM
1808
CD1
TYR
230
30.333
57.850
81.385
1.00
18.08
DIC

ATOM
1809
CE1
TYR
230
29.388
57.953
80.370
1.00
16.04
DIC

ATOM
1810
CD2
TYR
230
30.173
60.202
81.788
1.00
16.80
DIC

ATOM
1811
CE2
TYR
230
29.232
60.320
80.777
1.00
16.57
DIC

ATOM
1812
CZ
TYR
230
28.842
59.192
80.070
1.00
17.59
DIC

ATOM
1813
OH
TYR
230
27.908
59.314
79.067
1.00
13.29
DIC

ATOM
1814
C
TYR
230
33.520
60.049
81.818
1.00
18.05
DIC

ATOM
1815
O
TYR
230
33.575
59.996
80.588
1.00
17.20
DIC

ATOM
1816
N
ARG
231
33.704
61.174
82.504
1.00
17.40
DIC

ATOM
1817
CA
ARG
231
33.979
62.438
81.829
1.00
18.57
DIC

ATOM
1818
CB
ARG
231
33.948
63.585
82.841
1.00
21.41
DIC

ATOM
1819
CG
ARG
231
32.535
63.903
83.336
1.00
27.36
DIC

ATOM
1820
CD
ARG
231
32.562
64.595
84.685
1.00
32.89
DIC

ATOM
1821
NE
ARG
231
33.446
65.755
84.670
1.00
39.04
DIC

ATOM
1822
CZ
ARG
231
33.229
66.848
83.946
1.00
41.47
DIC

ATOM
1823
NH1
ARG
231
34.092
67.858
83.988
1.00
42.86
DIC

ATOM
1824
NH2
ARG
231
32.142
66.936
83.187
1.00
43.95
DIC

ATOM
1825
C
ARG
231
35.307
62.420
81.079
1.00
18.13
DIC

ATOM
1826
O
ARG
231
35.407
62.943
79.972
1.00
16.25
DIC

ATOM
1827
N
ASP
232
36.328
61.821
81.678
1.00
16.04
DIC

ATOM
1828
CA
ASP
232
37.620
61.749
81.021
1.00
17.65
DIC

ATOM
1829
CB
ASP
232
38.646
61.092
81.948
1.00
19.41
DIC

ATOM
1830
CG
ASP
232
39.972
60.839
81.258
1.00
22.20
DIC

ATOM
1831
OD1
ASP
232
40.137
59.760
80.648
1.00
24.13
DIC

ATOM
1832
OD2
ASP
232
40.845
61.729
81.314
1.00
24.43
DIC

ATOM
1833
C
ASP
232
37.522
60.957
79.713
1.00
17.38
DIC

ATOM
1834
O
ASP
232
38.078
61.359
78.690
1.00
16.38
DIC

ATOM
1835
N
ARG
233
36.789
59.844
79.746
1.00
15.90
DIC

ATOM
1836
CA
ARG
233
36.647
58.992
78.574
1.00
14.22
DIC

ATOM
1837
CB
ARG
233
36.134
57.609
78.993
1.00
13.65
DIC

ATOM
1838
CG
ARG
233
36.992
56.898
80.042
1.00
12.06
DIC

ATOM
1839
CD
ARG
233
38.359
56.471
79.507
1.00
11.93
DIC

ATOM
1840
NE
ARG
233
38.994
55.502
80.393
1.00
12.99
DIC

ATOM
1841
CZ
ARG
233
39.587
55.800
81.549
1.00
18.67
DIC

ATOM
1842
NH1
ARG
233
39.647
57.056
81.976
1.00
15.62
DIC

ATOM
1843
NH2
ARG
233
40.096
54.829
82.301
1.00
19.37
DIC

ATOM
1844
C
ARG
233
35.745
59.560
77.477
1.00
14.94
DIC

ATOM
1845
O
ARG
233
36.042
59.407
76.291
1.00
13.66
DIC

ATOM
1846
N
THR
234
34.656
60.222
77.867
1.00
14.04
DIC

ATOM
1847
CA
THR
234
33.716
60.772
76.895
1.00
14.66
DIC

ATOM
1848
CB
THR
234
32.298
60.886
77.513
1.00
15.37
DIC

ATOM
1849
OG1
TSP
234
32.365
61.614
78.745
1.00
12.97
DIC

ATOM
1850
CG2
THR
234
31.725
59.474
77.789
1.00
14.09
DIC

ATOM
1851
C
THR
234
34.149
62.114
76.298
1.00
16.57
DIC

ATOM
1852
O
THR
234
33.618
62.555
75.282
1.00
15.27
DIC

ATOM
1853
N
ASN
235
35.115
62.767
76.926
1.00
16.09
DIC

ATOM
1854
CA
ASN
235
35.594
64.017
76.386
1.00
18.20
DIC

ATOM
1855
CB
ASN
235
36.034
64.941
77.519
1.00
22.89
DIC

ATOM
1856
CG
ASN
235
34.843
65.640
78.171
1.00
28.06
DIC

ATOM
1857
OD1
ASN
235
34.410
66.700
77.716
1.00
32.63
DIC

ATOM
1858
ND2
ASN
235
34.282
65.029
79.210
1.00
30.92
DIC

ATOM
1859
C
ASN
235
36.708
63.648
75.423
1.00
17.06
DIC

ATOM
1860
O
ASN
235
37.793
63.214
75.810
1.00
14.88
DIC

ATOM
1861
N
THR
236
36.389
63.780
74.142
1.00
16.31
DIC

ATOM
1862
CA
THR
236
37.308
63.421
73.084
1.00
14.87
DIC

ATOM
1863
CB
THR
236
36.623
63.547
71.714
1.00
15.58
DIC

ATOM
1864
OG1
THR
236
35.566
62.578
71.629
1.00
14.42
DIC

ATOM
1865
CG2
THR
236
37.619
63.309
70.588
1.00
13.74
DIC

ATOM
1866
C
THR
236
38.587
64.219
73.088
1.00
15.17
DIC

ATOM
1867
O
THR
236
38.567
65.454
73.120
1.00
15.92
DIC

ATOM
1868
N
VAL
237
39.706
63.503
73.086
1.00
13.08
DIC

ATOM
1869
CA
VAL
237
41.006
64.150
73.049
1.00
14.84
DIC

ATOM
1870
CB
VAL
237
42.080
63.350
73.818
1.00
16.34
DIC

ATOM
1871
CG1
VAL
237
43.444
64.022
73.635
1.00
16.24
DIC

ATOM
1872
CG2
VAL
237
41.723
63.279
75.308
1.00
16.15
DIC

ATOM
1873
C
VAL
237
41.388
64.205
71.574
1.00
14.29
DIC

ATOM
1874
O
VAL
237
41.667
63.174
70.954
1.00
13.91
DIC

ATOM
1875
N
MSE
238
41.380
65.408
71.015
1.00
14.48
DIC

ATOM
1876
CA
MSE
238
41.710
65.608
69.603
1.00
15.10
DIC

ATOM
1877
CB
MSE
238
41.462
67.065
69.223
1.00
16.28
DIC

ATOM
1878
CG
MSE
238
40.012
67.495
69.341
1.00
20.30
DIC

ATOM
1879
SE
MSE
238
38.859
66.527
68.131
1.00
22.47
DIC

ATOM
1880
CE
MSE
238
37.180
66.780
69.061
1.00
25.99
DIC

ATOM
1881
C
MSE
238
43.160
65.234
69.288
1.00
13.91
DIC

ATOM
1882
O
MSE
238
44.021
65.289
70.163
1.00
14.24
DIC

ATOM
1883
N
PRO
239
43.451
64.872
68.022
1.00
14.10
DIC

ATOM
1884
CD
PRO
239
44.832
64.616
67.570
1.00
14.78
DIC

ATOM
1885
CA
PRO
239
42.515
64.788
66.895
1.00
13.37
DIC

ATOM
1886
CB
PRO
239
43.438
64.848
65.682
1.00
14.16
DIC

ATOM
1887
CG
PRO
239
44.630
64.088
66.154
1.00
15.87
DIC

ATOM
1888
C
PRO
239
41.696
63.501
66.914
1.00
13.85
DIC

ATOM
1889
O
PRO
239
42.065
62.530
67.582
1.00
12.56
DIC

ATOM
1890
N
VAL
240
40.588
63.490
66.179
1.00
12.87
DIC

ATOM
1891
CA
VAL
240
39.758
62.296
66.118
1.00
12.68
DIC

ATOM
1892
CB
VAL
240
38.485
62.538
65.260
1.00
13.59
DIC

ATOM
1893
CG1
VAL
240
37.735
61.231
65.054
1.00
15.84
DIC

ATOM
1894
CG2
VAL
240
37.574
63.557
65.962
1.00
13.32
DIC

ATOM
1895
C
VAL
240
40.615
61.210
65.494
1.00
11.91
DIC

ATOM
1896
O
VAL
240
41.331
61.470
64.526
1.00
12.36
DIC

ATOM
1897
N
ALA
241
40.566
60.003
66.054
1.00
10.60
DIC

ATOM
1898
CA
ALA
241
41.366
58.887
65.529
1.00
9.24
DIC

ATOM
1899
CB
ALA
241
41.989
58.107
66.688
1.00
8.43
DIC

ATOM
1900
C
ALA
241
40.515
57.960
64.663
1.00
9.78
DIC

ATOM
1901
O
ALA
241
40.990
57.400
63.673
1.00
9.54
DIC

ATOM
1902
N
VAL
242
39.250
57.804
65.042
1.00
8.78
DIC

ATOM
1903
CA
VAL
242
38.327
56.961
64.296
1.00
8.01
DIC

ATOM
1904
CB
VAL
242
38.120
55.590
64.998
1.00
8.78
DIC

ATOM
1905
CG1
VAL
242
37.181
54.717
64.170
1.00
7.09
DIC

ATOM
1906
CG2
VAL
242
39.458
54.896
65.195
1.00
7.39
DIC

ATOM
1907
C
VAL
242
36.955
57.604
64.163
1.00
9.79
DIC

ATOM
1908
O
VAL
242
36.311
57.906
65.170
1.00
9.84
DIC

ATOM
1909
N
SER
243
36.521
57.830
62.924
1.00
10.04
DIC

ATOM
1910
CA
SER
243
35.194
58.371
62.658
1.00
11.61
DIC

ATOM
1911
CB
SER
243
35.153
59.147
61.331
1.00
12.32
DIC

ATOM
1912
OG
SER
243
35.555
60.495
61.486
1.00
16.91
DIC

ATOM
1913
C
SER
243
34.344
57.115
62.509
1.00
12.31
DIC

ATOM
1914
O
SER
243
34.747
56.183
61.820
1.00
13.73
DIC

ATOM
1915
N
HIS
244
33.189
57.078
63.165
1.00
11.25
DIC

ATOM
1916
CA
HIS
244
32.297
55.925
63.079
1.00
9.29
DIC

ATOM
1917
CB
HIS
244
32.266
55.187
64.429
1.00
7.53
DIC

ATOM
1918
CG
HIS
244
31.407
53.958
64.434
1.00
8.43
DIC

ATOM
1919
CD2
HIS
244
30.813
53.278
63.424
1.00
7.51
DIC

ATOM
1920
ND1
HIS
244
31.055
53.302
65.598
1.00
6.41
DIC

ATOM
1921
CE1
HIS
244
30.277
52.274
65.300
1.00
8.12
DIC

ATOM
1922
NE2
HIS
244
30.114
52.238
63.990
1.00
6.81
DIC

ATOM
1923
C
HIS
244
30.903
56.446
62.710
1.00
9.33
DIC

ATOM
1924
O
HIS
244
30.278
57.173
63.477
1.00
9.05
DIC

ATOM
1925
N
TYR
245
30.423
56.073
61.530
1.00
9.10
DIC

ATOM
1926
CA
TYR
245
29.120
56.524
61.051
1.00
10.38
DIC

ATOM
1927
CB
TYR
245
29.213
56.762
59.545
1.00
11.80
DIC

ATOM
1928
CG
TYR
245
30.308
57.747
59.216
1.00
13.82
DIC

ATOM
1929
CD1
TYR
245
30.092
59.118
59.344
1.00
14.45
DIC

ATOM
1930
CE1
TYR
245
31.127
60.035
59.150
1.00
16.51
DIC

ATOM
1931
CD2
TYR
245
31.591
57.308
58.875
1.00
14.05
DIC

ATOM
1932
CE2
TYR
245
32.636
58.217
58.679
1.00
15.80
DIC

ATOM
1933
CZ
TYR
245
32.396
59.579
58.822
1.00
16.33
DIC

ATOM
1934
OH
TYR
245
33.422
60.487
58.666
1.00
15.53
DIC

ATOM
1935
C
TYR
245
27.991
55.552
61.380
1.00
11.30
DIC

ATOM
1936
O
TYR
245
27.281
55.062
60.490
1.00
10.36
DIC

ATOM
1937
N
CYS
246
27.818
55.284
62.670
1.00
11.34
DIC

ATOM
1938
CA
CYS
246
26.781
54.363
63.101
1.00
13.80
DIC

ATOM
1939
CB
CYS
246
26.886
54.103
64.605
1.00
15.97
DIC

ATOM
1940
SG
CYS
246
26.808
55.590
65.610
1.00
19.68
DIC

ATOM
1941
C
CYS
246
25.422
54.947
62.763
1.00
15.08
DIC

ATOM
1942
O
CYS
246
25.254
56.167
62.704
1.00
14.66
DIC

ATOM
1943
N
GLY
247
24.453
54.071
62.529
1.00
14.33
DIC

ATOM
1944
CA
GLY
247
23.127
54.539
62.191
1.00
14.42
DIC

ATOM
1945
C
GLY
247
22.893
54.396
60.703
1.00
16.40
DIC

ATOM
1946
O
GLY
247
23.789
53.977
59.974
1.00
14.60
DIC

ATOM
1947
N
PRO
248
21.693
54.754
60.218
1.00
17.44
DIC

ATOM
1948
CD
PRO
248
20.586
55.331
61.001
1.00
17.20
DIC

ATOM
1949
CA
PRO
248
21.334
54.660
58.800
1.00
17.61
DIC

ATOM
1950
CB
PRO
248
19.845
55.009
58.809
1.00
19.08
DIC

ATOM
1951
CG
PRO
248
19.750
56.000
59.933
1.00
18.65
DIC

ATOM
1952
C
PRO
248
22.132
55.545
57.833
1.00
17.78
DIC

ATOM
1953
O
PRO
248
22.311
55.187
56.675
1.00
18.06
DIC

ATOM
1954
N
ALA
249
22.617
56.690
58.305
1.00
18.95
DIC

ATOM
1955
CA
ALA
249
23.362
57.612
57.444
1.00
18.77
DIC

ATOM
1956
CB
ALA
249
23.276
59.038
58.008
1.00
18.55
DIC

ATOM
1957
C
ALA
249
24.823
57.206
57.266
1.00
18.31
DIC

ATOM
1958
O
ALA
249
25.635
57.356
58.178
1.00
19.11
DIC

ATOM
1959
N
LYS
250
25.156
56.705
56.082
1.00
16.06
DIC

ATOM
1960
CA
LYS
250
26.515
56.269
55.808
1.00
16.76
DIC

ATOM
1961
CB
LYS
250
26.498
54.854
55.226
1.00
14.84
DIC

ATOM
1962
CG
LYS
250
25.771
53.836
56.093
1.00
14.31
DIC

ATOM
1963
CD
LYS
250
26.384
53.731
57.487
1.00
14.00
DIC

ATOM
1964
CE
LYS
250
25.797
52.551
58.272
1.00
11.62
DIC

ATOM
1965
NZ
LYS
250
26.190
52.604
59.721
1.00
9.99
DIC

ATOM
1966
C
LYS
250
27.246
57.213
54.857
1.00
17.98
DIC

ATOM
1967
O
LYS
250
26.621
57.890
54.036
1.00
17.45
DIC

ATOM
1968
N
PRO
251
28.588
57.251
54.943
1.00
18.59
DIC

ATOM
1969
CD
PRO
251
29.466
56.428
55.797
1.00
19.31
DIC

ATOM
1970
CA
PRO
251
29.379
58.126
54.076
1.00
19.82
DIC

ATOM
1971
CB
PRO
251
30.792
57.983
54.640
1.00
18.90
DIC

ATOM
1972
CG
PRO
251
30.815
56.562
55.106
1.00
19.40
DIC

ATOM
1973
C
PRO
251
29.278
57.761
52.594
1.00
21.72
DIC

ATOM
1974
O
PRO
251
29.544
58.602
51.731
1.00
22.19
DIC

ATOM
1975
N
TRP
252
28.885
56.521
52.298
1.00
22.68
DIC

ATOM
1976
CA
TRP
252
28.732
56.090
50.904
1.00
24.72
DIC

ATOM
1977
CB
TRP
252
29.053
54.599
50.751
1.00
22.37
DIC

ATOM
1978
CG
TRP
252
28.332
53.709
51.710
1.00
17.98
DIC

ATOM
1979
CD2
TRP
252
28.886
53.095
52.875
1.00
16.74
DIC

ATOM
1980
CE2
TRP
252
27.856
52.345
53.485
1.00
15.49
DIC

ATOM
1981
CE3
TRP
252
30.156
53.105
53.466
1.00
14.56
DIC

ATOM
1982
CD1
TRP
252
27.022
53.321
51.658
1.00
18.51
DIC

ATOM
1983
NE1
TRP
252
26.728
52.500
52.722
1.00
15.35
DIC

ATOM
1984
CZ2
TRP
252
28.058
51.613
54.657
1.00
15.42
DIC

ATOM
1985
CZ3
TRP
252
30.356
52.378
54.630
1.00
14.20
DIC

ATOM
1986
CH2
TRP
252
29.312
51.642
55.212
1.00
14.24
DIC

ATOM
1987
C
TRP
252
27.318
56.372
50.397
1.00
27.39
DIC

ATOM
1988
O
TRP
252
26.969
56.026
49.266
1.00
28.26
DIC

ATOM
1989
N
HIS
253
26.512
56.996
51.249
1.00
30.21
DIC

ATOM
1990
CA
HIS
253
25.140
57.358
50.909
1.00
34.07
DIC

ATOM
1991
CB
HIS
253
24.228
57.315
52.138
1.00
34.17
DIC

ATOM
1992
CG
HIS
253
23.745
55.947
52.498
1.00
34.88
DIC

ATOM
1993
CD2
HIS
253
23.210
55.469
53.644
1.00
34.49
DIC

ATOM
1994
ND1
HIS
253
23.731
54.903
51.598
1.00
33.80
DIC

ATOM
1995
CE1
HIS
253
23.206
53.837
52.178
1.00
35.02
DIC

ATOM
1996
NE2
HIS
253
22.881
54.152
53.419
1.00
35.95
DIC

ATOM
1997
C
HIS
253
25.102
58.778
50.364
1.00
36.66
DIC

ATOM
1998
O
HIS
253
26.079
59.525
50.464
1.00
37.76
DIC

ATOM
1999
N
ARG
254
23.954
59.144
49.803
1.00
38.76
DIC

ATOM
2000
CA
ARG
254
23.751
60.476
49.253
1.00
40.22
DIC

ATOM
2001
CB
ARG
254
22.605
60.449
48.238
1.00
41.70
DIC

ATOM
2002
CG
ARG
254
22.678
59.273
47.266
1.00
43.79
DIC

ATOM
2003
CD
ARG
254
21.435
59.178
46.392
1.00
44.39
DIC

ATOM
2004
NE
ARG
254
20.205
59.068
47.174
1.00
44.17
DIC

ATOM
2005
CZ
ARG
254
18.991
58.970
46.642
1.00
43.46
DIC

ATOM
2006
NH1
ARG
254
18.844
58.969
45.323
1.00
43.96
DIC

ATOM
2007
NH2
ARG
254
17.925
58.873
47.425
1.00
42.76
DIC

ATOM
2008
C
ARG
254
23.392
61.401
50.411
1.00
40.54
DIC

ATOM
2009
O
ARG
254
22.796
60.969
51.401
1.00
40.03
DIC

ATOM
2010
N
ASP
255
23.772
62.667
50.291
1.00
40.92
DIC

ATOM
2011
CA
ASP
255
23.477
63.659
51.315
1.00
41.47
DIC

ATOM
2012
CB
ASP
255
21.981
63.995
51.280
1.00
42.69
DIC

ATOM
2013
CG
ASP
255
21.555
64.612
49.953
1.00
43.75
DIC

ATOM
2014
OD1
ASP
255
21.950
65.766
49.678
1.00
43.58
DIC

ATOM
2015
OD2
ASP
255
20.835
63.939
49.181
1.00
44.62
DIC

ATOM
2016
C
ASP
255
23.894
63.273
52.738
1.00
41.91
DIC

ATOM
2017
O
ASP
255
23.144
63.491
53.694
1.00
41.85
DIC

ATOM
2018
N
CYS
256
25.086
62.696
52.882
1.00
41.35
DIC

ATOM
2019
CA
CYS
256
25.574
62.338
54.211
1.00
39.96
DIC

ATOM
2020
CB
CYS
256
26.664
61.266
54.133
1.00
39.72
DIC

ATOM
2021
SG
CYS
256
27.207
60.674
55.763
1.00
40.45
DIC

ATOM
2022
C
CYS
256
26.150
63.623
54.800
1.00
38.56
DIC

ATOM
2023
O
CYS
256
27.114
64.177
54.273
1.00
37.54
DIC

ATOM
2024
N
THR
257
25.547
64.103
55.883
1.00
38.47
DIC

ATOM
2025
CA
THR
257
25.996
65.339
56.515
1.00
36.95
DIC

ATOM
2026
CB
THR
257
24.795
66.183
56.963
1.00
37.26
DIC

ATOM
2027
OG1
THR
257
24.065
65.475
57.974
1.00
37.57
DIC

ATOM
2028
CG2
THR
257
23.875
66.459
55.780
1.00
36.79
DIC

ATOM
2029
C
THR
257
26.900
65.089
57.717
1.00
35.26
DIC

ATOM
2030
O
THR
257
27.333
66.027
58.384
1.00
35.00
DIC

ATOM
2031
N
ALA
258
27.178
63.820
57.994
1.00
33.98
DIC

ATOM
2032
CA
ALA
258
28.038
63.457
59.111
1.00
32.05
DIC

ATOM
2033
CB
ALA
258
28.131
61.943
59.231
1.00
31.18
DIC

ATOM
2034
C
ALA
258
29.421
64.052
58.889
1.00
31.39
DIC

ATOM
2035
O
ALA
258
29.867
64.220
57.751
1.00
30.13
DIC

ATOM
2036
N
TRP
259
30.098
64.362
59.986
1.00
31.29
DIC

ATOM
2037
CA
TRP
259
31.429
64.955
59.937
1.00
29.92
DIC

ATOM
2038
CB
TRP
259
31.868
65.341
61.351
1.00
31.14
DIC

ATOM
2039
CG
TRP
259
33.230
65.947
61.400
1.00
31.00
DIC

ATOM
2040
CD2
TRP
259
34.439
65.294
61.798
1.00
30.73
DIC

ATOM
2041
CE2
TRP
259
35.484
66.235
61.668
1.00
30.83
DIC

ATOM
2042
CE3
TRP
259
34.741
64.004
62.253
1.00
29.98
DIC

ATOM
2043
CD1
TRP
259
33.576
67.221
61.053
1.00
30.91
DIC

ATOM
2044
NE1
TRP
259
34.930
67.402
61.211
1.00
31.95
DIC

ATOM
2045
CZ2
TRP
259
36.811
65.928
61.978
1.00
30.08
DIC

ATOM
2046
CZ3
TRP
259
36.058
63.698
62.560
1.00
29.09
DIC

ATOM
2047
CH2
TRP
259
37.077
64.657
62.422
1.00
30.00
DIC

ATOM
2048
C
TRP
259
32.486
64.043
59.313
1.00
29.26
DIC

ATOM
2049
O
TRP
259
32.509
62.831
59.558
1.00
27.60
DIC

ATOM
2050
N
GLY
260
33.360
64.645
58.508
1.00
27.51
DIC

ATOM
2051
CA
GLY
260
34.436
63.912
57.861
1.00
26.27
DIC

ATOM
2052
C
GLY
260
34.050
62.911
56.788
1.00
26.05
DIC

ATOM
2053
O
GLY
260
34.909
62.189
56.281
1.00
25.46
DIC

ATOM
2054
N
ALA
261
32.772
62.862
56.431
1.00
25.27
DIC

ATOM
2055
CA
ALA
261
32.307
61.922
55.417
1.00
25.33
DIC

ATOM
2056
CB
ALA
261
30.805
62.112
55.182
1.00
25.36
DIC

ATOM
2057
C
ALA
261
33.066
62.078
54.101
1.00
25.94
DIC

ATOM
2058
O
ALA
261
33.265
61.106
53.373
1.00
26.13
DIC

ATOM
2059
N
ALA
262
33.497
63.300
53.804
1.00
25.58
DIC

ATOM
2060
CA
ALA
262
34.215
63.585
52.564
1.00
26.27
DIC

ATOM
2061
CB
ALA
262
34.544
65.078
52.476
1.00
26.51
DIC

ATOM
2062
C
ALA
262
35.482
62.762
52.350
1.00
26.63
DIC

ATOM
2063
O
ALA
262
35.900
62.566
51.205
1.00
26.59
DIC

ATOM
2064
N
ARG
263
36.109
62.275
53.418
1.00
25.79
DIC

ATOM
2065
CA
ARG
263
37.310
61.487
53.194
1.00
25.44
DIC

ATOM
2066
CB
ARG
263
38.201
61.364
54.435
1.00
28.92
DIC

ATOM
2067
CG
ARG
263
39.579
60.821
54.018
1.00
33.60
DIC

ATOM
2068
CD
ARG
263
40.483
60.390
55.155
1.00
37.93
DIC

ATOM
2069
NE
ARG
263
41.350
61.455
55.663
1.00
40.10
DIC

ATOM
2070
CZ
ARG
263
40.995
62.342
56.588
1.00
41.46
DIC

ATOM
2071
NH1
ARG
263
41.856
63.267
56.987
1.00
41.19
DIC

ATOM
2072
NH2
ARG
263
39.780
62.304
57.116
1.00
43.96
DIC

ATOM
2073
C
ARG
263
36.988
60.092
52.687
1.00
22.70
DIC

ATOM
2074
O
ARG
263
37.883
59.374
52.248
1.00
20.54
DIC

ATOM
2075
N
PHE
264
35.722
59.691
52.757
1.00
20.27
DIC

ATOM
2076
CA
PHE
264
35.354
58.373
52.245
1.00
19.95
DIC

ATOM
2077
CB
PHE
264
33.894
58.031
52.559
1.00
19.65
DIC

ATOM
2078
CG
PHE
264
33.433
56.738
51.934
1.00
18.28
DIC

ATOM
2079
CD1
PHE
264
33.634
55.522
52.582
1.00
17.29
DIC

ATOM
2080
CD2
PHE
264
32.835
56.734
50.674
1.00
18.28
DIC

ATOM
2081
CE1
PHE
264
33.248
54.321
51.986
1.00
18.07
DIC

ATOM
2082
CE2
PHE
264
32.446
55.534
50.069
1.00
17.91
DIC

ATOM
2083
CZ
PHE
264
32.654
54.328
50.729
1.00
17.29
DIC

ATOM
2084
C
PHE
264
35.526
58.425
50.728
1.00
19.57
DIC

ATOM
2085
O
PHE
264
36.140
57.548
50.126
1.00
18.73
DIC

ATOM
2086
N
THR
265
34.976
59.474
50.124
1.00
20.91
DIC

ATOM
2087
CA
THR
265
35.045
59.665
48.680
1.00
22.89
DIC

ATOM
2088
CB
THR
265
34.289
60.932
48.252
1.00
24.07
DIC

ATOM
2089
OG1
THR
265
32.974
60.922
48.820
1.00
27.93
DIC

ATOM
2090
CG2
THR
265
34.179
60.989
46.734
1.00
25.93
DIC

ATOM
2091
C
THR
265
36.496
59.810
48.252
1.00
23.30
DIC

ATOM
2092
O
THR
265
36.932
59.238
47.251
1.00
23.08
DIC

ATOM
2093
N
GLU
266
37.243
60.583
49.026
1.00
23.53
DIC

ATOM
2094
CA
GLU
266
38.646
60.804
48.733
1.00
25.20
DIC

ATOM
2095
CB
GLU
266
39.256
61.723
49.784
1.00
28.98
DIC

ATOM
2096
CG
GLU
266
40.736
61.936
49.607
1.00
36.19
DIC

ATOM
2097
CD
GLU
266
41.240
63.096
50.427
1.00
39.75
DIC

ATOM
2098
OE1
GLU
266
40.976
63.113
51.650
1.00
41.33
DIC

ATOM
2099
OE2
GLU
266
41.896
63.991
49.846
1.00
42.17
DIC

ATOM
2100
C
GLU
266
39.408
59.482
48.687
1.00
23.71
DIC

ATOM
2101
O
GLU
266
40.195
59.251
47.778
1.00
22.46
DIC

ATOM
2102
N
LEU
267
39.173
58.616
49.670
1.00
22.23
DIC

ATOM
2103
CA
LEU
267
39.842
57.320
49.701
1.00
21.24
DIC

ATOM
2104
CB
LEU
267
39.601
56.617
51.044
1.00
21.75
DIC

ATOM
2105
CG
LEU
267
40.509
57.054
52.195
1.00
22.58
DIC

ATOM
2106
CD1
LEU
267
39.979
56.545
53.520
1.00
23.20
DIC

ATOM
2107
CD2
LEU
267
41.918
56.531
51.938
1.00
24.01
DIC

ATOM
2108
C
LEU
267
39.346
56.443
48.562
1.00
19.60
DIC

ATOM
2109
O
LEU
267
40.137
55.786
47.888
1.00
19.14
DIC

ATOM
2110
N
ALA
268
38.035
56.436
48.340
1.00
19.54
DIC

ATOM
2111
CA
ALA
268
37.458
55.630
47.271
1.00
21.17
DIC

ATOM
2112
CB
ALA
268
35.949
55.838
47.209
1.00
22.40
DIC

ATOM
2113
C
ALA
266
38.091
55.999
45.933
1.00
23.39
DIC

ATOM
2114
O
ALA
268
38.382
55.127
45.108
1.00
23.18
DIC

ATOM
2115
N
GLY
269
38.306
57.295
45.727
1.00
23.42
DIC

ATOM
2116
CA
GLY
269
38.896
57.759
44.486
1.00
25.69
DIC

ATOM
2117
C
GLY
269
40.364
57.408
44.346
1.00
27.18
DIC

ATOM
2118
O
GLY
269
40.919
57.479
43.249
1.00
27.61
DIC

ATOM
2119
N
SER
270
40.995
57.029
45.452
1.00
27.80
DIC

ATOM
2120
CA
SER
270
42.409
56.670
45.438
1.00
28.87
DIC

ATOM
2121
CB
SER
270
43.065
57.070
46.757
1.00
29.06
DIC

ATOM
2122
OG
SER
270
42.560
56.279
47.818
1.00
31.44
DIC

ATOM
2123
C
SER
270
42.616
55.174
45.221
1.00
28.53
DIC

ATOM
2124
O
SER
270
43.750
54.704
45.156
1.00
28.86
DIC

ATOM
2125
N
LEU
271
41.525
54.425
45.105
1.00
27.87
DIC

ATOM
2126
CA
LEU
271
41.633
52.981
44.925
1.00
28.38
DIC

ATOM
2127
CB
LEU
271
40.240
52.337
44.928
1.00
26.77
DIC

ATOM
2128
CG
LEU
271
39.478
52.415
46.256
1.00
25.46
DIC

ATOM
2129
CD1
LEU
271
38.123
51.727
46.125
1.00
24.92
DIC

ATOM
2130
CD2
LEU
271
40.310
51.757
47.348
1.00
24.78
DIC

ATOM
2131
C
LEU
271
42.383
52.579
43.658
1.00
29.08
DIC

ATOM
2132
O
LEU
271
42.146
53.122
42.583
1.00
27.21
DIC

ATOM
2133
N
THR
272
43.288
51.616
43.804
1.00
29.70
DIC

ATOM
2134
CA
THR
272
44.075
51.115
42.687
1.00
30.05
DIC

ATOM
2135
CB
THR
272
45.091
50.055
43.158
1.00
30.32
DIC

ATOM
2136
OG1
THR
272
45.943
50.617
44.164
1.00
32.13
DIC

ATOM
2137
CG2
THR
272
45.935
49.578
41.996
1.00
32.54
DIC

ATOM
2138
C
THR
272
43.159
50.471
41.649
1.00
29.64
DIC

ATOM
2139
O
THR
272
43.195
50.830
40.471
1.00
29.15
DIC

ATOM
2140
N
THR
273
42.344
49.520
42.103
1.00
28.68
DIC

ATOM
2141
CA
THR
273
41.418
48.803
41.236
1.00
28.77
DIC

ATOM
2142
CB
THR
273
41.707
47.281
41.225
1.00
31.01
DIC

ATOM
2143
OG1
THR
273
43.095
47.050
40.955
1.00
33.16
DIC

ATOM
2144
CG2
THR
273
40.868
46.593
40.153
1.00
33.04
DIC

ATOM
2145
C
THR
273
39.967
48.984
41.675
1.00
26.88
DIC

ATOM
2146
O
THR
273
39.642
48.858
42.854
1.00
25.29
DIC

ATOM
2147
N
VAL
274
39.095
49.273
40.717
1.00
24.92
DIC

ATOM
2148
CA
VAL
274
37.683
49.449
41.025
1.00
23.86
DIC

ATOM
2149
CB
VAL
274
37.276
50.932
41.006
1.00
23.31
DIC

ATOM
2150
CG1
VAL
274
35.839
51.070
41.469
1.00
23.87
DIC

ATOM
2151
CG2
VAL
274
38.191
51.737
41.906
1.00
24.43
DIC

ATOM
2152
C
VAL
274
36.819
48.700
40.019
1.00
23.07
DIC

ATOM
2153
O
VAL
274
36.593
49.176
38.902
1.00
23.08
DIC

ATOM
2154
N
PRO
275
36.330
47.510
40.400
1.00
21.69
DIC

ATOM
2155
CD
PRO
275
36.566
46.776
41.654
1.00
20.50
DIC

ATOM
2156
CA
PRO
275
35.488
46.726
39.497
1.00
21.63
DIC

ATOM
2157
CB
PRO
275
35.088
45.524
40.352
1.00
21.49
DIC

ATOM
2158
CG
PRO
275
36.254
45.356
41.253
1.00
21.48
DIC

ATOM
2159
C
PRO
275
34.273
47.522
39.048
1.00
21.99
DIC

ATOM
2160
O
PRO
275
33.736
48.338
39.805
1.00
21.78
DIC

ATOM
2161
N
GLU
276
33.852
47.284
37.810
1.00
23.31
DIC

ATOM
2162
CA
GLU
276
32.683
47.943
37.249
1.00
23.31
DIC

ATOM
2163
CB
GLU
276
32.297
47.256
35.934
1.00
23.72
DIC

ATOM
2164
CG
GLU
276
30.950
47.667
35.362
1.00
26.81
DIC

ATOM
2165
CD
GLU
276
30.875
49.144
35.067
1.00
27.36
DIC

ATOM
2166
OE1
GLU
276
31.941
49.794
35.028
1.00
31.05
DIC

ATOM
2167
OE2
GLU
276
29.755
49.656
34.868
1.00
29.72
DIC

ATOM
2168
C
GLU
276
31.525
47.846
38.244
1.00
23.02
DIC

ATOM
2169
O
GLU
276
30.797
48.811
38.473
1.00
23.54
DIC

ATOM
2170
N
GLU
277
31.376
46.678
38.854
1.00
23.75
DIC

ATOM
2171
CA
GLU
277
30.294
46.464
39.804
1.00
25.40
DIC

ATOM
2172
CB
GLU
277
30.168
44.970
40.120
1.00
29.16
DIC

ATOM
2173
CG
GLU
277
28.715
44.493
40.230
1.00
35.80
DIC

ATOM
2174
CD
GLU
277
28.022
44.308
38.873
1.00
37.33
DIC

ATOM
2175
OE1
GLU
277
28.104
45.210
38.005
1.00
38.08
DIC

ATOM
2176
OE2
GLU
277
27.378
43.251
38.685
1.00
39.35
DIC

ATOM
2177
C
GLU
277
30.407
47.275
41.104
1.00
24.54
DIC

ATOM
2178
O
GLU
277
29.484
47.275
41.914
1.00
23.39
DIC

ATOM
2179
N
TRP
278
31.531
47.962
41.300
1.00
23.06
DIC

ATOM
2180
CA
TRP
278
31.732
48.795
42.489
1.00
20.91
DIC

ATOM
2181
CB
TRP
278
33.181
48.700
42.986
1.00
18.69
DIC

ATOM
2182
CG
TRP
278
33.521
47.467
43.781
1.00
17.97
DIC

ATOM
2183
CD2
TRP
278
34.676
47.279
44.613
1.00
16.79
DIC

ATOM
2184
CE2
TRP
278
34.610
45.970
45.130
1.00
15.02
DIC

ATOM
2185
CE3
TRP
278
35.763
48.095
44.970
1.00
16.53
DIC

ATOM
2186
CD1
TRP
278
32.822
46.294
43.828
1.00
16.18
DIC

ATOM
2187
NE1
TRP
278
33.470
45.390
44.636
1.00
16.36
DIC

ATOM
2188
CZ2
TRP
278
35.589
45.450
45.989
1.00
14.14
DIC

ATOM
2189
CZ3
TRP
278
36.742
47.577
45.828
1.00
14.30
DIC

ATOM
2190
CH2
TRP
278
36.644
46.268
46.324
1.00
13.79
DIC

ATOM
2191
C
TRP
278
31.441
50.258
42.152
1.00
21.28
DIC

ATOM
2192
O
TRP
278
31.315
51.093
43.046
1.00
20.17
DIC

ATOM
2193
N
ALA
279
31.344
50.563
40.860
1.00
22.70
DIC

ATOM
2194
CA
ALA
279
31.102
51.935
40.412
1.00
24.93
DIC

ATOM
2195
CB
ALA
279
30.915
51.972
38.899
1.00
27.07
DIC

ATOM
2196
C
ALA
279
29.903
52.563
41.098
1.00
25.99
DIC

ATOM
2197
O
ALA
279
29.976
53.690
41.590
1.00
25.88
DIC

ATOM
2198
N
GLY
280
28.795
51.834
41.134
1.00
27.56
DIC

ATOM
2199
CA
GLY
280
27.608
52.372
41.772
1.00
30.18
DIC

ATOM
2200
C
GLY
280
27.801
52.629
43.257
1.00
31.52
DIC

ATOM
2201
O
GLY
280
27.427
53.680
43.776
1.00
32.79
DIC

ATOM
2202
N
LYS
281
28.413
51.668
43.937
1.00
31.54
DIC

ATOM
2203
CA
LYS
281
28.656
51.766
45.370
1.00
32.16
DIC

ATOM
2204
CB
LYS
281
29.079
50.396
45.911
1.00
31.67
DIC

ATOM
2205
CG
LYS
281
27.951
49.386
46.055
1.00
33.55
DIC

ATOM
2206
CD
LYS
281
28.490
48.084
46.637
1.00
34.90
DIC

ATOM
2207
CE
LYS
281
27.450
47.351
47.477
1.00
36.99
DIC

ATOM
2208
NZ
LYS
281
26.693
46.315
46.724
1.00
38.19
DIC

ATOM
2209
C
LYS
281
29.664
52.815
45.826
1.00
32.48
DIC

ATOM
2210
O
LYS
281
29.484
53.440
46.867
1.00
32.45
DIC

ATOM
2211
N
LEU
282
30.717
53.007
45.044
1.00
31.92
DIC

ATOM
2212
CA
LEU
282
31.758
53.953
45.403
1.00
33.81
DIC

ATOM
2213
CB
LEU
282
33.121
53.402
44.968
1.00
32.92
DIC

ATOM
2214
CG
LEU
282
34.051
52.818
46.044
1.00
34.56
DIC

ATOM
2215
CD1
LEU
282
33.283
52.458
47.313
1.00
32.48
DIC

ATOM
2216
CD2
LEU
282
34.752
51.605
45.466
1.00
32.62
DIC

ATOM
2217
C
LEU
282
31.599
55.383
44.893
1.00
35.67
DIC

ATOM
2218
O
LEU
282
32.284
56.281
45.373
1.00
37.01
DIC

ATOM
2219
N
ALA
283
30.711
55.605
43.932
1.00
37.96
DIC

ATOM
2220
CA
ALA
283
30.501
56.944
43.381
1.00
40.04
DIC

ATOM
2221
CB
ALA
283
30.102
57.925
44.489
1.00
39.26
DIC

ATOM
2222
C
ALA
283
31.718
57.476
42.611
1.00
41.65
DIC

ATOM
2223
OT1
ALA
283
31.501
57.913
41.458
1.00
43.46
DIC

ATOM
2224
OT2
ALA
283
32.858
57.460
43.139
1.00
41.61
DIC

ATOM
2225
MN
MN
400
29.002
50.705
62.676
1.00
11.41

ATOM
2226
C1
LAT
1347
21.881
53.893
65.661
1.00
28.17

ATOM
2227
C2
LAT
1347
22.143
52.528
65.080
1.00
26.76

ATOM
2228
C3
LAT
1347
22.196
51.524
66.241
1.00
26.19

ATOM
2229
C4
LAT
1347
23.382
51.940
67.197
1.00
25.62

ATOM
2230
C5
LAT
1347
23.232
53.243
67.815
1.00
25.09

ATOM
2231
C6
LAT
1347
24.216
53.701
68.651
1.00
23.05

ATOM
2232
O1
LAT
1347
21.713
55.161
65.005
1.00
29.10

ATOM
2233
O2
LAT
1347
21.103
52.228
64.162
1.00
26.57

ATOM
2234
O3
LAT
1347
22.437
50.258
65.682
1.00
23.28

ATOM
2235
O4
LAT
1347
24.642
52.079
66.577
1.00
24.26

ATOM
2236
O5
LAT
1347
22.951
54.232
66.677
1.00
26.25

ATOM
2237
O6
LAT
1347
24.608
52.886
69.776
1.00
26.54

ATOM
2238
C1′
LAT
1347
20.966
59.301
65.099
1.00
32.51

ATOM
2239
C2′
LAT
1347
22.189
58.806
65.964
1.00
31.92

ATOM
2240
C3′
LAT
1347
22.654
57.435
65.390
1.00
31.34

ATOM
2241
C4′
LAT
1347
21.441
56.495
65.526
1.00
31.39

ATOM
2242
C5′
LAT
1347
20.188
56.938
64.702
1.00
32.37

ATOM
2243
C6′
LAT
1347
18.954
56.016
64.828
1.00
33.23

ATOM
2244
O1′
LAT
1347
20.519
60.547
65.593
1.00
33.36

ATOM
2245
O2′
LAT
1347
23.244
59.759
65.873
1.00
29.82

ATOM
2246
O3′
LAT
1347
23.772
56.970
66.183
1.00
32.03

ATOM
2247
O5′
LAT
1347
19.866
58.294
65.174
1.00
31.84

ATOM
2248
O6′
LAT
1347
18.076
56.261
63.749
1.00
37.37

ATOM
2249
N1
UPG
341
27.322
44.456
57.775
1.00
12.21

ATOM
2250
C2
UPG
341
27.705
43.789
56.548
1.00
12.58

ATOM
2251
N3
UPG
341
26.796
44.078
55.491
1.00
13.15

ATOM
2252
C4
UPG
341
25.580
44.942
55.533
1.00
11.78

ATOM
2253
C5
UPG
341
25.244
45.587
56.772
1.00
12.67

ATOM
2254
C6
UPG
341
26.069
45.358
57.842
1.00
12.46

ATOM
2255
O2
UPG
341
28.671
43.078
56.445
1.00
11.36

ATOM
2256
O4
UPG
341
24.924
45.060
54.495
1.00
13.21

ATOM
2257
C4*
UPG
341
28.139
45.820
61.018
1.00
13.58

ATOM
2258
O4*
UPG
341
27.383
44.722
60.301
1.00
11.69

ATOM
2259
C3*
UPG
341
28.971
46.440
59.908
1.00
10.52

ATOM
2260
O3*
UPG
341
30.005
47.173
60.471
1.00
11.62

ATOM
2261
C2*
UPG
341
29.272
45.220
59.097
1.00
11.03

ATOM
2262
O2*
UPG
341
30.400
44.483
59.548
1.00
9.93

ATOM
2263
C1*
UPG
341
28.051
44.379
59.135
1.00
12.83

ATOM
2264
C5*
UPG
341
26.814
46.217
61.487
1.00
13.32

ATOM
2265
O5*
UPG
341
26.265
47.573
61.238
1.00
16.42

ATOM
2266
PA
UPG
341
26.748
49.072
61.108
1.00
14.28

ATOM
2267
O1A
UPG
341
28.187
49.241
61.244
1.00
14.57

ATOM
2268
O2A
UPG
341
26.213
49.674
59.838
1.00
16.15

ATOM
2269
O3A
UPG
341
25.983
49.214
62.459
1.00
14.41

ATOM
2270
PB
UPG
341
25.800
50.467
63.365
1.00
14.57

ATOM
2271
O1B
UPG
341
27.120
51.044
63.507
1.00
12.20

ATOM
2272
O2B
UPG
341
24.933
51.389
62.659
1.00
14.49

ATOM
2273
O3B
UPG
341
24.918
50.295
64.666
1.00
17.88

ATOM
2274
C1′
UPG
341
25.388
49.351
65.853
1.00
24.44

ATOM
2275
C2′
UPG
341
26.854
49.185
66.369
1.00
27.13

ATOM
2276
C3′
UPG
341
27.779
48.150
65.490
1.00
26.87

ATOM
2277
C4′
UPG
341
27.069
46.698
65.546
1.00
27.54

ATOM
2278
C5′
UPG
341
25.562
47.005
64.928
1.00
27.76

ATOM
2279
C6′
UPG
341
24.646
45.802
64.906
1.00
29.63

ATOM
2280
F2′
UPG
341
27.412
50.500
66.415
1.00
26.09

ATOM
2281
O3′
UPG
341
29.067
48.093
66.053
1.00
26.84

ATOM
2282
O4′
UPG
341
26.972
46.296
66.918
1.00
26.57

ATOM
2283
O5′
UPG
341
24.748
48.031
65.729
1.00
26.37

ATOM
2284
O6′
UPG
341
23.367
45.385
65.355
1.00
28.54

ATOM
2285
O
HOH
512
54.673
48.356
65.523
1.00
25.15

ATOM
2286
O
HOH
513
57.867
51.960
56.478
1.00
18.24

ATOM
2287
O
HOH
514
25.903
36.241
53.371
1.00
23.04

ATOM
2288
O
HOH
515
43.782
40.049
44.203
1.00
19.20

ATOM
2289
O
HOH
516
25.269
48.689
57.913
1.00
20.10

ATOM
2290
O
HOH
517
33.923
31.711
71.928
1.00
18.55

ATOM
2291
O
HOH
518
30.388
30.310
61.293
1.00
22.80

ATOM
2292
O
HOH
519
43.430
56.956
57.195
1.00
15.05

ATOM
2293
O
HOH
520
49.150
58.809
68.184
1.00
22.34

ATOM
2294
O
HOH
521
46.243
43.905
76.655
1.00
17.00

ATOM
2295
O
HOH
522
26.676
56.544
69.515
1.00
16.47

ATOM
2296
O
HOH
523
30.000
48.381
81.295
1.00
22.90

ATOM
2297
O
HOH
524
44.731
41.738
76.380
1.00
28.37

ATOM
2298
O
HOH
525
43.888
30.365
73.504
1.00
30.03

ATOM
2299
O
HOH
526
38.608
33.989
82.252
1.00
31.63

ATOM
2300
O
HOH
527
45.486
58.476
72.471
1.00
17.02

ATOM
2301
O
HOH
528
36.439
60.989
58.566
1.00
21.83

ATOM
2302
O
HOH
529
22.558
57.605
60.909
1.00
22.34

ATOM
2303
O
HOH
510
22.910
48.263
67.559
1.00
27.02

ATOM
2304
O
HOH
342
33.837
51.323
71.040
1.00
10.52

ATOM
2305
O
HOH
343
33.436
45.012
60.346
1.00
11.03

ATOM
2306
O
HOH
344
41.858
32.593
61.292
1.00
14.48

ATOM
2307
O
HOH
345
30.314
40.780
63.189
1.00
10.46

ATOM
2308
O
HOH
346
26.633
38.049
51.120
1.00
13.67

ATOM
2309
O
HOH
347
25.661
58.468
67.699
1.00
17.94

ATOM
2310
O
HOH
348
26.776
40.465
85.536
1.00
21.27

ATOM
2311
O
HOH
349
34.269
66.072
73.361
1.00
16.12

ATOM
2312
O
HOH
350
42.055
55.697
75.118
1.00
15.08

ATOM
2313
O
HOH
351
24.932
44.993
86.462
1.00
15.36

ATOM
2314
O
HOH
352
32.634
57.485
71.956
1.00
7.12

ATOM
2315
O
HOH
353
41.424
63.579
62.874
1.00
10.82

ATOM
2316
O
HOH
354
34.311
34.079
70.575
1.00
12.06

ATOM
2317
O
HOH
355
31.944
30.308
71.197
1.00
16.77

ATOM
2318
O
HOH
356
31.522
46.216
65.787
1.00
15.52

ATOM
2319
O
HOH
357
34.596
56.735
75.449
1.00
12.10

ATOM
2320
O
HOH
358
20.938
53.671
79.071
1.00
14.85

ATOM
2321
O
HOH
359
42.846
60.054
74.844
1.00
14.85

ATOM
2322
O
HOH
360
33.043
62.643
72.666
1.00
13.35

ATOM
2323
O
HOH
361
31.465
47.811
83.263
1.00
19.48

ATOM
2324
O
HOH
362
17.810
43.979
69.451
1.00
13.43

ATOM
2325
O
HOH
363
44.880
61.186
73.189
1.00
13.38

ATOM
2326
O
HOH
364
52.815
48.765
69.102
1.00
13.97

ATOM
2327
O
HOH
365
20.792
39.749
57.158
1.00
11.23

ATOM
2328
O
HOH
366
38.954
52.211
81.847
1.00
16.78

ATOM
2329
O
HOH
367
22.941
41.574
81.754
1.00
17.53

ATOM
2330
O
HOH
368
39.526
27.671
66.454
1.00
19.67

ATOM
2331
O
HOH
369
13.108
47.479
74.594
1.00
15.51

ATOM
2332
O
HOH
370
19.447
44.093
61.807
1.00
16.50

ATOM
2333
O
HOH
371
30.399
40.374
82.936
1.00
9.51

ATOM
2334
O
HOH
372
19.157
32.432
71.731
1.00
21.71

ATOM
2335
O
HOH
374
40.516
58.977
78.099
1.00
16.53

ATOM
2336
O
HOH
375
25.173
34.444
79.349
1.00
15.37

ATOM
2337
O
HOH
376
46.578
58.693
67.532
1.00
13.15

ATOM
2338
O
HOH
377
14.471
52.264
70.498
1.00
18.62

ATOM
2339
O
HOH
378
39.660
63.544
78.200
1.00
16.08

ATOM
2340
O
HOH
379
55.295
50.486
64.035
1.00
16.60

ATOM
2341
O
HOH
381
48.181
45.311
54.971
1.00
17.29

ATOM
2342
O
HOH
382
43.505
31.236
76.092
1.00
19.33

ATOM
2343
O
HOH
383
32.590
44.068
37.933
1.00
27.84

ATOM
2344
O
HOH
384
37.969
40.917
41.166
1.00
21.67

ATOM
2345
O
HOH
385
31.948
51.058
85.079
1.00
18.57

ATOM
2346
O
HOH
386
28.224
60.122
88.185
1.00
23.70

ATOM
2347
O
HOH
387
45.297
40.751
78.746
1.00
19.73

ATOM
2348
O
HOH
389
18.713
51.902
66.002
1.00
16.80

ATOM
2349
O
HOH
390
24.809
39.213
56.261
1.00
19.74

ATOM
2350
O
HOH
391
38.859
65.613
79.857
1.00
21.35

ATOM
2351
O
HOH
392
23.682
28.524
65.843
1.00
25.37

ATOM
2352
O
HOH
393
30.619
45.293
47.694
1.00
19.83

ATOM
2353
O
HOH
395
16.069
54.647
63.765
1.00
21.81

ATOM
2354
O
HOH
396
26.626
51.713
89.753
1.00
22.40

ATOM
2355
O
HOH
397
28.064
49.899
39.247
1.00
26.58

ATOM
2356
O
HOH
398
47.650
50.646
79.240
1.00
25.75

ATOM
2357
O
HOH
399
27.302
61.880
78.488
1.00
23.12

ATOM
2358
O
HOH
401
52.702
53.348
61.415
1.00
15.81

ATOM
2359
O
HOH
402
41.238
60.307
45.671
1.00
21.78

ATOM
2360
O
HOH
403
48.221
59.205
72.644
1.00
20.33

ATOM
2361
O
HOH
404
32.922
39.506
83.843
1.00
26.81

ATOM
2362
O
HOH
405
33.647
51.875
54.608
1.00
26.78

ATOM
2363
O
HOH
406
34.729
27.098
73.772
1.00
24.68

ATOM
2364
O
HOH
407
47.014
45.510
42.850
1.00
28.16

ATOM
2365
O
HOH
409
46.142
41.147
44.690
1.00
22.35

ATOM
2366
O
HOH
410
12.827
43.035
64.396
1.00
17.06

ATOM
2367
O
HOH
411
45.907
38.504
58.159
1.00
25.94

ATOM
2368
O
HOH
414
29.975
27.632
68.843
1.00
21.59

ATOM
2369
O
HOH
416
49.328
45.517
72.009
1.00
16.75

ATOM
2370
O
HOH
417
37.408
65.908
57.617
1.00
27.94

ATOM
2371
O
HOH
418
43.941
57.374
74.443
1.00
14.75

ATOM
2372
O
HOH
419
29.018
46.583
79.445
1.00
10.62

ATOM
2373
O
HOH
420
28.318
58.314
71.194
1.00
13.85

ATOM
2374
O
HOH
421
17.267
52.333
63.327
1.00
23.92

ATOM
2375
O
HOH
422
11.697
46.878
72.387
1.00
18.34

ATOM
2376
O
HOH
423
25.498
40.253
50.998
1.00
13.87

ATOM
2377
O
HOH
424
17.533
50.046
67.514
1.00
16.25

ATOM
2378
O
HOH
425
14.824
50.534
68.599
1.00
21.93

ATOM
2379
O
HOH
426
45.832
63.034
71.218
1.00
26.79

ATOM
2380
O
HOH
429
54.376
51.863
65.883
1.00
18.45

ATOM
2381
O
HOH
430
50.977
47.216
76.379
1.00
23.22

ATOM
2382
O
HOH
431
42.874
53.348
76.065
1.00
19.36

ATOM
2383
O
HOH
432
43.449
34.666
60.899
1.00
17.96

ATOM
2384
O
HOH
433
34.130
67.571
75.561
1.00
24.13

ATOM
2385
O
HOH
434
27.453
42.471
87.224
1.00
32.46

ATOM
2386
O
HOH
435
52.158
48.653
66.492
1.00
20.64

ATOM
2387
O
HOH
436
34.404
47.778
83.422
1.00
19.34

ATOM
2388
O
HOH
437
25.914
58.255
60.777
1.00
23.62

ATOM
2389
O
HOH
438
24.526
68.909
75.214
1.00
33.24

ATOM
2390
O
HOH
440
28.786
26.819
61.937
1.00
25.45

ATOM
2391
O
HOH
441
41.960
34.523
52.538
1.00
19.68

ATOM
2392
O
HOH
442
53.720
46.358
69.854
1.00
21.67

ATOM
2393
O
HOH
445
28.804
38.524
84.456
1.00
25.60

ATOM
2394
O
HOH
446
43.669
62.480
59.056
1.00
24.50

ATOM
2395
O
HOH
447
13.951
50.958
82.440
1.00
34.99

ATOM
2396
O
HOH
448
36.623
67.353
73.056
1.00
18.09

ATOM
2397
O
HOH
449
23.895
37.020
54.976
1.00
23.23

ATOM
2398
O
HOH
450
31.251
53.568
87.928
1.00
24.41

ATOM
2399
O
HOH
452
21.273
33.232
57.364
1.00
24.12

ATOM
2400
O
HOH
453
30.982
60.462
63.192
1.00
31.37

ATOM
2401
O
HOH
454
45.825
39.919
74.932
1.00
33.02

ATOM
2402
O
HOH
458
47.378
51.451
51.491
1.00
28.58

ATOM
2403
O
HOH
459
42.709
47.306
81.851
1.00
31.79

ATOM
2404
O
HOH
461
31.207
27.302
65.372
1.00
22.14

ATOM
2405
O
HOH
462
28.964
26.675
71.181
1.00
28.72

ATOM
2406
O
HOH
463
39.686
64.266
81.983
1.00
31.45

ATOM
2407
O
HOH
466
42.215
44.109
85.084
1.00
39.24

ATOM
2408
O
HOH
469
43.225
37.756
80.665
1.00
31.08

ATOM
2409
O
HOH
477
33.002
24.938
70.787
1.00
44.27

ATOM
2410
O
HOH
497
47.753
62.512
67.276
1.00
31.26

ATOM
2411
O
HOH
611
14.151
39.876
64.132
1.00
26.85

ATOM
2412
O
HOH
612
41.690
31.049
59.011
1.00
25.32

ATOM
2413
O
HOH
613
52.238
45.010
68.097
1.00
25.29

ATOM
2414
O
HOH
614
41.963
62.794
78.957
1.00
25.34

ATOM
2415
O
HOH
615
18.316
43.721
58.649
1.00
23.51

ATOM
2416
O
HOH
616
30.695
46.612
87.680
1.00
32.98

ATOM
2417
O
HOH
617
24.606
40.630
48.428
1.00
28.20

ATOM
2418
O
HOH
618
41.654
52.764
78.344
1.00
27.63

ATOM
2419
O
HOH
620
45.215
49.791
80.776
1.00
31.54

ATOM
2420
O
HOH
621
33.859
53.902
56.156
1.00
28.15

ATOM
2421
O
HOH
622
36.203
37.715
83.838
1.00
31.32

ATOM
2422
O
HOH
623
20.511
54.964
81.434
1.00
30.95

ATOM
2423
O
HOH
624
44.439
51.283
46.458
1.00
27.81

ATOM
2424
O
HOH
625
26.468
26.377
71.132
1.00
27.97

ATOM
2425
O
HOH
626
41.327
54.925
84.791
1.00
35.97

ATOM
2426
O
HOH
627
50.663
46.031
56.545
1.00
33.15

ATOM
2427
O
HOH
628
49.607
45.005
75.531
1.00
29.21

ATOM
2428
O
HOH
530
49.701
50.415
80.874
1.00
34.92

ATOM
2429
O
HOH
531
29.995
55.495
89.602
1.00
30.40

ATOM
2430
O
HOH
532
18.278
55.827
85.115
1.00
29.80

ATOM
2431
O
HOH
533
34.321
52.394
85.636
1.00
31.13

ATOM
2432
O
HOH
534
17.335
58.634
66.816
1.00
32.18

ATOM
2433
O
HOH
535
37.008
41.209
84.114
1.00
33.40

ATOM
2434
O
HOH
536
22.018
35.145
55.681
1.00
33.42

ATOM
2435
O
HOH
537
23.707
41.537
52.919
1.00
35.31

ATOM
2436
O
HOH
538
21.046
31.384
65.966
1.00
29.47

ATOM
2437
O
HOH
543
20.341
47.928
87.042
1.00
29.97

ATOM
2438
O
HOH
545
37.912
28.687
70.597
1.00
29.70

ATOM
2439
O
HOH
546
22.366
34.826
80.821
1.00
30.63

ATOM
2440
O
HOH
547
47.995
43.524
52.725
1.00
39.01

ATOM
2441
O
HOH
548
41.270
50.998
82.378
1.00
34.24

ATOM
2442
O
HOH
550
14.319
46.589
53.840
1.00
33.32

ATOM
2443
O
HOH
552
34.230
42.579
42.029
1.00
29.38

ATOM
2444
O
HOH
554
26.628
36.503
48.890
1.00
28.95

ATOM
2445
O
HOH
557
25.845
65.038
64.799
1.00
31.69

ATOM
2446
O
HOH
560
13.335
52.360
50.917
1.00
34.81

ATOM
2447
O
HOH
561
24.566
50.832
53.862
1.00
29.06

ATOM
2448
O
HOH
562
15.990
59.624
77.366
1.00
35.62

ATOM
2449
O
HOH
563
36.875
51.110
84.792
1.00
36.48

ATOM
2450
O
HOH
565
33.575
33.855
50.824
1.00
33.97

ATOM
2451
O
HOH
570
22.705
37.189
50.422
1.00
34.04

ATOM
2452
O
HOH
582
33.723
54.774
87.078
1.00
20.22

ATOM
2453
O
HOH
583
31.373
44.992
62.477
1.00
31.80

ATOM
2454
O
HOH
584
23.792
53.593
49.409
1.00
35.49

END

[0497] List of References

[0498] 1. Tzeng, Y. L. & Stephens, D. S. Epidemiology and pathogenesis of Neisseria meningitidis. Microbes and Infection 2, 687-700 (2000).

[0499] 2. Wakarchuk, W. W., Martin, A., Jennings, M. P., Moxon, E. R. & Richards, J. C. Functional relationships of the genetic locus encoding the glycosyltransferase enzymes involved in expression of the lacto-N-neotetraose terminal lipopolysac-charide structure in Neisseria meningitidis. J. Biol. Chem. 271, 19166-19173 (1996).

[0500] 3. Moran, A. P., Prendergast, M. M. & Appelmelk, B. J. Molecular mimicry of host structures by bacterial lipopolysaccharides and its contribution to disease. FEMS Immunol. Med. Microbiol. 16, 105-115 (1996).

[0501] 4. Kahler, C. & Stephens, D. Genetic basis for biosynthesis, structure and function of meningococcal Lipooligosaccharide (endotoxin). Crit. Rev. Microbiol. 24, 281-334 (1998).

[0502] 5. Campbell, J. A., Davies, G. J., Bulone, V. & Henrissat, B. A classification of nucleotide-diphospho-sugar glycosyltransferase based on amino acid sequence similarities. Biochem. J. 329, 929-939 (1997).

[0503] 6. Wakarchuk, W., Cunningham, A., Watson, D. & Young, M. Role of paired basic residues in the expression of active recombinant galactosyltansferases from bacterial pathogen Neisseria meningitidis. Prot. Engineering 11, 295-302. (1998).

[0504] 7. Whitfield, C. & Roberts, I. S. Structure, assembly and regulation of expression of capsules in Escherichia coli. Mol. Microbiol. 31, 1307-1319 (1999).

[0505] 8. Takayama, S. et al. Selective inhibition of b-1,4 and a-1,3-galactosyltransferases: donor sugar-nucleotide based approach. Bioorg. Med. Chem. 7, 401-409 (1999).

[0506] 9. Sinnott, M. L. Catalytic Mechanisms of Enzymatic Glycosyl Transfer. Chem. Rev. 90, 1171-1202 (1990).

[0507] 10. Davies, G., Withers, S. G. & Sinnott M. L. in Comprehensive Biological Catalysis, Vol. 1 (ed.

[0508] Sinnott, M. L.) 119-208 (Academic Press, London, 1997).

[0509] 11. Zechel, D. L. & Withers, S. G. Glycosidase mechanisms: anatomy of a finely tuned catalyst Acc. Chem. Res. 33, 11-18 (2000).

[0510] 12. Vrielink, A., Ruger, W., Driessen, H. P. C. & Freemont P. S. Crystal structure of the DNA modifying enzyme b-glucosyltransferase in the presence and absence of the substrate uridine diphosphoglucose. EMBO J. 13, 3413-3422 (1994).

[0511] 13. Charnock, S. & Davies, G. Structure of the Nucleotide-Diphospho-Sugar transferase, SpSA from Bacillus subtilis, in native and Nucleotide-Complexed Forms. Biochemistry 38, 6380-6385 (1998).

[0512] 14. Gastinel, L., Cambillau, C. & Bourne, Y. Crystal structures of the bovine b4galactosyltransferse catalytic domain and its complex with uridine diphosphogalactose. EMBO J. 18, 3546-3557 (1999).

[0513] 15. Ha, S., Walker, D., Shi, Y. & S., W. The 1.9 Å crystal structure of Escherichia coli MurG, a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis. Protein Sci. 9, 1045-1052 (2000).

[0514] 16. Pedersen, L. C. et al. Heparan/Chondroitin Sulfate Biosynthesis: Structure and mechanism of human glucuronyltransferase I. J. Biol. Chem. 275, 34580-34585 (2000).

[0515] 17. Ünligil, U. M. et al. X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I; catalytic mechanism and a new protein superfamily. EMBO J. 19, 5269-5280 (2000).

[0516] 18. Lu, G. TOP: a new method for protein structure comparison and similarity searches. J. Appl. Crystallogr. 33, 176-183 (2000).

[0517] 19. Burkart, M. D. et al. Chemo-enzymatic synthesis of fluorinated sugar nucleotide: useful mechanistic probes for glycosyl transferases. Bioorg. Med. Chem. 8, 1937-1946 (2000).

[0518] 20. Thoden, J. B. & Holden, H. M. Dramatic differences in the binding of UDP-galactose and UDP-glucose to UDP-galactose 4-epimerase from Escherichia coli. Biochemistry 37, 11469-11477 (1998).

[0519] 21. Martin, J. L., Johnson, L. N. & Withers, S. G. Comparison of the binding of glucose and glucose 1-phosphate derivatives to T-state glycogen phosphorylase b. Biochemistry 29, 10745-10757 (1990).

[0520] 22. Uitdehaag, J. C. M. et al. Catalysis in the a-amylase family: X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase. Nature Struct Biol. 6,432436 (1999).

[0521] 23. Brayer, G. D. et al. Subsite mapping of the human pancreatic a-amylase active site through structural, kinetic, and mutagenesis techniques. Biochemistry 39, 4778-4791 (2000).

[0522] 24. Breton, C., Bettler, E., Joziasse, D. H., Geremia, R. A. & Imberty, A. Sequence-function relationships of prokaryotic and eukaryotic galactosyltransferases. J. Biochem. 123, 1000-1009 (1998).

[0523] 25. Kapitonov, D. & Yu, R. K. Conserved domains of glycosyltransferases. Glycobiology 9, 961-978 (1999).

[0524] 26. Busch, C. et al. A common motif of eukaryotic glycosyltransferases is essential for the enzymatic activity of large Clostridial cystotoxins. J. Biol. Chem. 273, 19566-19572 (1998).

[0525] 27. Shibayamam, K., Ohsuka, S., Toshihiko, T., Yoshickika, A. & Ohta, M. Conserved structural regions involved in the catalytic mechanism of Escherichia coli K-12 WaaO (Rfal). J. Bacteriol. 180, 5313-5318 (1998).

[0526] 28. Wiggins, C. A. R. & Munro, S. Activity of the yeast MNN1 a-1,3-mannosyltransferase requires a motif conserved in many other families of glycosyltransferases. Proc. Natl. Acad. Sci. USA 95, 7945-7950 (1998).

[0527] 29. Hagen, F. K., Hazes, B., Raffo, R., deSa, D. & Tabak, L. A. Structure-function analysis of the UDPN-acetyl-D-galactosamine: polypeptide N-acetylgalactosaminyltransferase. J. Biol. Chem. 274, 6797-6803 (1999).

[0528] 30. Moloney, D. J. et al. Fringe is a glycosyltransferase that modifies Notch. Nature 406, 369-375 (2000).

[0529] 31. Brackner, K., Perez, L., Clausen, H. & Cohen, S. Glycosyltransferase activity of Fringe modulates Notch-Delta interactions. Nature 406, 411-415 (2000).

[0530] 32. Lougheed, B. M. Sc., University of British Columbia (1998).

[0531] 33. Glusker, J. Structural aspects of metal liganding to functional groups in proteins. Adv. Protein Chem. 42, 1-76 (1991).

[0532] 34. Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).

[0533] 35. Burgi, H., Dunitz, J. & Shefter, E. Nucleophilic addition to a carbonyl group. J. Am. Chem. Soc. 95, 5065-5067 (1973).

[0534] 36. Mitchell, E. P. et al. Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states. Biochemistry 35, 7341-7355 (1996).

[0535] 37. Watson, K. A. et al. Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question. EMBO J. 18, 4619-4632 (1999).

[0536] 38. Artymuik, P. J., Rice, D. W., Poirrette, A. R & Willett, P. b-Glucosyltransferase and phophorylase reveal their common theme. Nature Struct. Biol. 2, 117-120 (1995).

[0537] 39. Holm, L. & Sander, C. Evolutionary linlc between glycogen phosphorylase and a DNA modifying enzyme. EMBO J. 14, 1287-1293 (1995).

[0538] 40. Ly, H. D. & Withers, S. G. Mutagenesis of glycosidases. Annu. Rev. Biochem. 68,487-522 (1999).

[0539] 41. Van Duyne, G. D., Standaert, R. F., Karplus, P. A., Schreiber, S. L. & Clardy, J. Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin. J. Mol. Biol. 229, 105-124 (1993).

[0540] 42. Gosselin, S., Alhussaini, M., Streiff, M. B., Takabayashi, K. & Palcic, M. M. A continuous spectrophotometric assay for glycosyltransferases. Anal. Biochem. 220, 92-97 (1994).

[0541] 43. Leatherbarrow, R. Grafit Version 3.0. (Erithacus Software Ltd., Staines, UK., 1990).

[0542] 44. Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).

[0543] 45. Terwilliger, T. C. & Berendzen, J. Automated structure solution for MIR and MAD. Acta Crystallogr. D 55, 849-861 (1999).

[0544] 46. Cowtan, K. DM: An automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31, 34-38 (1994).

[0545] 47. McRee, D. E. Practical protein crystallography. A visual protein crystallographic software system for X11/XView. J. Mol. Graphics 10,44-46 (1992).

[0546] 48. Brünger, A. et al. Crystallography and NMR system: A new software suit for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).

[0547] 49. Engh, R. & Huber, R. Accurate bond and angle parameter for X-ray protein structure refinement Acta Crystallogr. A 47, 392-400 (1991).

[0548] 50. Kleywegt, G. & Jones, T. Model building and refinement practice. Methods Enzymol. 277, 208-230 (1997).

[0549] 51. Laskowski, R., MacArthur, M., Moss, D. & Thornton, J. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. CrystaUogr. 26, 283-291 (1993).

[0550] 52. Kraulis, P. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950 (1991).

[0551] 53. Merritt, E. A. & Bacon, D. J. Raster3D: Photorealistic Molecular Graphics. Methods Enzymol. 277, 505-524 (1997).

[0552] 54. Nichols, A., Sharp, K. & Honig, B. Protein folding association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11(1991).

Crystal structures of retaining glycosytransferases

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