Human IL-18 crystal structure

Abstract

A novel human IL-18 native crystalline structure is identified.

Description

TECHNICAL FIELD OF THE INVENTION

[0002] The invention relates to the identification of a novel crystalline structure of the human IL-18 (hIL-18) cytokine, its mode of binding to its receptor, and methods enabling further design and selection of molecules with hIL-18-like activity.

BACKGROUND OF THE INVENTION

[0003] IL-18 is a type of cytokine or substance that mediates signal transduction in the immune system. As seen in Japanese Patent Kokai Nos.27,189/96 and 193,098/96 and Okamura et al., Nature, Vol. 378, No. 6,552, pp. 88-91 (1995), IL-18 was provisionally designated as “interferon-gamma inducing factor” immediately after its discovery. This designation was later changed into “IL-18” in accordance with the proposal in Ushio, et al., Journal of Immunology, Vol. 156, pp. 4,274-4,279 (1996). IL-18 in its mature form consists of 157 amino acids. It induces immunocompetent cells in the production of interferon-gamma (hereinafter abbreviated as “IFN-gamma.”), which is a useful biologically-active protein capable of inducing and enhancing the generation and cytotoxicity of killer cells. Extensive research is currently underway to develop and explore the various utility of IL-18 in pharmaceuticals. These greatly expected applications include using IL-18 as antiviral, antimicrobial, antitumor and anti-immunopathic agents.

[0004] In nature, cytokines, including IL-18, are produced and secreted as substances responsible for signal transduction in the immune system. Therefore, when cytokines are administered to the body of mammals, they disturb the naturally existing equilibrium in the mammal's immune system. The surfaces of mammalian cells bear sites or “receptors” that are responsible for recognition of cytokines and secreted cytokines transduce no signal in cells until they are bound to the receptors. In a normal immune system, a definite equilibrium exists between respective cytokines and their receptors. There are currently unmet needs in finding and learning the biological and structural properties of IL-18 and its receptors and using such knowledge in designing drugs for treatment and ameliorating diseases and disorders such as viral and microbial infections, cancer, inflammation, etc.

SUMMARY OF THE INVENTION

[0005] In one aspect, the present invention relates to a human IL-18 protein molecule having the coordinates of Table I in an essentially pure native form or a homolog thereof.

[0006] In another aspect, the present invention provides a novel crystalline form of the human IL-18 molecule.

[0007] In yet another aspect, the present invention provides direct information on the specific role played by the residues responsible for the binding of human IL-18 to its receptor.

[0008] In a further aspect, the present invention includes machine-readable media encoded with data representing the coordinates of the three-dimensional structure of the IL-18 crystal.

BRIEF DESCRIPTION OF THE FIGURES

[0009] The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application with color drawings will be provided by the Office upon request and payment of the necessary fee.

[0010] FIG. 1 provides a ribbon diagram of native human IL-18 (C38S) of this invention with the view taken down the axis of the β-barrel and the helical segments represented as ribbons and the β-sheets represented as arrows. The polypeptide chain is rainbow colored with the color blue at the N- and the color red at the C-terminus.

[0011] FIG. 2 provides a ribbon diagram of the secondary structure elements of human IL-18. These secondary structural elements of hIL-18 are: β1 2-14, β2 19-22, β3 28-31, α1 38-41, 310 helix 42-44, β4 47-54, β5 60-67, β6 71-75, β10 helix 77-79, β7 82-84, β8 91-92, β9 101-106, β10 109-117, β11 123-130, β12 133-140, 310 helix 147-149, β13 151-154.

[0012] FIG. 3 provides diagrams of murine IL-18, human IL-1β, and human IL-18 structures. Side-by-side comparison of these structures shows the conformational similarities between these structurally related cytokines.

[0013] FIG. 4 provides a diagram where the hIL-18 model is superimposed on the IL1β-IL1 receptor complex. Human IL-18 is drawn in a thin yellow line and the IL 1β-IL1 is drawn in a thin green line as the cytokine and a red line as the receptor. The diagram sheds light on the manner hIL-18 binds to its receptor, as well as the involvement of amino acid residues in receptor interactions and biological activity.

DETAILED DESCRIPTION OF THE INVENTION

[0014] The present invention provides a novel human IL-18 crystalline structure of the native protein. Based on this structure and molecular models built using related proteins, it provides ways of determining the most likely places to modify the molecule of hIL-18 without compromising its biological activity and methods to use this crystalline form in identifying, improving or antagonizing the biological activity of hIL-18.

[0015] The Novel human IL-18 Crystalline Three-Dimensional Structure.

[0016] The crystal structure of the human IL-18 in its native form has been determined by molecular replacement and refined to 2.06A resolution. The novel human IL-18, like IL1β, is folded into a central, closed β-barrel with an overall β-trefoil fold. The following residues form the three parts of the clover-leaf: (i)10-47 and 150-156, (ii)103-149, and (iii) 47-102 and 1-9. The structure of human IL-18 is expected to be similar to that of the murine IL-18 since the sequences of these IL-18s are highly homologous (65% identity). The information derived from the structure of human IL-18 sheds light on how complexes with pharmacological agents may be formed that would alter the properties of human IL-18, such as half-life and immunogenicity, while maintaining its biological activity. In the absence of structural information of hIL-18-receptor complex, the hIL-18 structure and that of the IL1β-IL1β receptor complex are used as models for interactions between hIL-18 and its receptor and provide rational guidance as to where to place potential agents in the hIL18 molecule. IL1β and hIL-18 have similar overall fold and structures, but large differences in the two structures are apparent near and at the positions of loops. In the IL1β-receptor complex, the residues in the IL1β loops establish important interactions with the receptor, mainly through two surfaces. To identify the residues of IL-18 that may interact with IL-18 receptor, residues of IL-18 were mapped onto the IL1β structure by superimposing 153 Cα atoms of IL1β with IL-18 to achieve an overall root mean square, r.m.s. and deviation of 9 Å. Based on this superposition, hIL-18 is predicted to interact with its receptor via several surfaces. On one of the proposed interacting surfaces, the receptor-IL-18 interface is lined by IL-18 residues: 4-18, 30-37, 107-112, 128-135, and 145-148. On another proposed surface located on the other side of the molecule, the interface is lined by residues: 1-8, 50-55, 89-93, 103-105, and 155-156. This leaves residues 103-149 in hIL-18 free from any interaction with the receptor, and these residues are mostly solvent exposed. This is then proposed to be the best place to attach a derivatization agent (for example, a polyethyleneglycol molecule) that would not compromise hIL-18's receptor binding activity. This proposal is backed up by the observations by Kim, et al., where Glu42 and Lys89 are found to be critical for the interaction of human IL-18 with its receptor. J. Biol Chem 277(13):10998-1003 (2002). Glu42 and Lys89 are likewise positioned for interaction with the IL-18 receptor in our model, further validating the use of crystallography modeling in predicting the interacting surfaces and interactions between the cytokine and its receptor.

[0017] Table I provides the atomic coordinates of the native human IL-18 (C38S). These coordinates were obtained using a model encompassing residues 1 to 156 in the crystallographic asymmetric unit. The amino acid sequence of the native human IL-18 is provided in SEQ ID NO: 1. However, for the studies described herein, C38S mutant was used.

[0018] The atomic coordinates shown in Table I are expected to change upon refinement of the crystal structure, but the deviation that would incur as a result with regard to the Cα atoms is not expected to substantially exceed an r.m.s. of 1.0-1.5 Å. Similarly, bond angles and bond lengths will vary insignificantly as routinely observed with other proteins. Engh, et al. (1991) Acta Crystallogr. A47, 392-400. The inter-atomic interactions will remain unchanged, within experimental error. The relative conformation and orientation or the positioning of residues in the receptor binding site will likewise be unaffected.

[0019] Mutants and Derivatives

[0020] The invention further provides homologues, co-complexes, mutants and derivatives of the human IL-18 crystal structure of the invention.

[0021] The term “cytokine”, as used herein, means a protein modulating the growth and functional activities of immune cells.

[0022] The term “homolog”, as used herein, means a protein having at least 30% amino acid sequence identity with a functional domain of human IL-18. Preferably the percentage identity will be 40, or 50%, more preferably 60 or 70% and most preferably 80 or 90%. A 95% identity is most particularly preferred.

[0023] The term “co-complex”, as used herein, means the human IL-18 or a mutant or homologue of the human IL-18 in covalent or non-covalent association with a chemical entity or compound.

[0024] The term “mutant”, as used herein, means the Human IL-18 polypeptide, i.e., a polypeptide displaying the biological activity of wild-type Human IL-18 activity, characterized by the replacement of at least one amino acid from the wild-type IL-18 sequence. Such a mutant may be prepared, for example, by expression of the human IL-18 cDNA previously altered in its coding sequence by oligonucleotide-directed mutagenesis.

[0025] The term “r.m.s.”, as used herein, means root mean square. It represents the standard deviation of the data collection.

[0026] The term “pro-IL18”, as used herein, means the inactive, precursor form of mature IL18. Mature IL18 does not contain the “pro-fragment” and is biologically active.

[0027] The term “molecular replacement”, as used herein, means a method of solving crystal structure using the atomic coordinates of a structurally related molecule.

[0028] Human IL-18 mutants may also be generated by site-specific incorporation of unnatural amino acids into the Human IL-18 protein using the general biosynthetic method of Noren, et al., Science, 244:182-188 (1989). In this method, the nucleotides encoding the amino acid of interest in wild-type Human IL-18 is replaced by a “blank” nonsense codon, TAG, using oligonucleotide-directed mutagenesis. A suppressor directed against this codon is then chemically aminoacylated in vitro with the desired unnatural amino acid. The aminoacylated residue is then added to an in vitro translation system to yield a mutant Human IL-18 enzyme with the site-specific incorporated unnatural amino acid.

[0029] Selenocysteine or selenomethionine may be incorporated into wild-type or mutant cytokine by expression of Human IL-18-encoding cDNAs in auxotrophic E. coli strains. Hendrickson, et al., EMBO J., 9(5):1665-1672 (1990). In this embodiment, the wild-type or mutated cytokine cDNA may be expressed in a host organism on a growth medium depleted of either natural cysteine or methionine or both, but enriched with selenocysteine or selenomethionine or both.

[0030] The term “heavy atom derivative” refers to derivatives of Human IL-18 produced by chemically modifying a crystal of Human IL-18. In practice, a crystal is immersed in a solution containing the desired metal salt, or organometallic compound, e.g., lead chloride, gold thiomalate, thimerosal or uranyl acetate, which upon diffusion into the protein crystal can bind to the protein. The location of the bound heavy metal atom site(s) can be determined by X-ray diffraction analysis of the soaked crystal. This information, in turn, is used to generate the phase angle information needed to construct a three-dimensional electron density map from which a model of the atomic structure of the enzyme is derived Blundell, et al., PROTEIN CRYSTALLOGRAPHY, Academic Press (1976).

[0031] Methods of Identifying Agonist or Antagonists of the Novel Human IL-18

[0032] Crystalline Structure

[0033] Another aspect of this invention involves a method for identifying agonists or antagonists of a human IL-18 through the crystal structure described herein. The novel human IL-18 crystalline structure of the invention permits the identification of agonists or antagonists of its cytokine activity. Such agonist/antagonists may be competitive, binding to all or a portion of the receptor for the human IL-18; or non-competitive and bind to and inhibit IL-18 activity whether or not it is bound to the receptor.

[0034] One embodiment probes the human IL-18 crystal of the invention with a variety of different chemical molecules to determine optimal sites either for interactions between such candidate angonist/antagonist molecules and hIL-18, or alternatively, for cellular activities. For example, high resolution X-ray diffraction data collected from crystals saturated with solvent allows the determination of binding positions for solvent molecule. Small molecules that would bind tightly to those sites can then be designed, synthesized and tested for their human IL-18 agonist/antagonist activities.

[0035] Another embodiment screens computationally small molecule databases for chemical entities or compounds that can bind in whole, or in part, to human IL-18 or human IL-18 receptor, or both. This screening method and its utility is well known in the art. For example, such computer modeling techniques were described in a PCT application WO 97/16177, published on May 9, 1997.

[0036] Once identified by modeling, the agonist/antagonist may then be tested for biological activity. For example, the molecules identified may be introduced via standard screening formats into enzymatic activity assays to determine the inhibitory activity of the compounds, or alternatively, binding assays to determine binding. One particularly preferred assay format is the enzyme-linked immunosorbent assay (ELISA). This and other assay formats are well known in the art and thus are not limitations to the present invention.

[0037] The following examples illustrate various aspects of this invention. This invention is not to be limited in scope by the specific embodiments described below. Indeed, various modifications of the invention in addition to those described herein will become apparent to those skilled in the art from the foregoing description. Such modifications are intended to fall within the scope of the appended claims. The disclosures of patents, patent applications and publications cited herein are incorporated by reference in their entireties.

EXAMPLES

Biological Methods

Example 1

The Purification of the Human IL-18 C38S Mutant in Escherichia coli.

[0038] Human proIL-18 was expressed in E. coli as a soluble protein with an N-terminal hexa-His tag. ProIL-18 was purified with a Ni-NTA agarose column and mature IL-18 was obtained by cleaving the pro-domain with Caspase 5. The C38S mutant of IL-18 was engineered to prevent the usual occurrence of an intra-disulfide bond between C38 and C68 in wild type IL-18 at neutral pH.

[0039] E. coli cells were suspended (10 ml/g) in 50 mM Tris (pH 8), 500 mM NaCl, 5% Glycerol, 10 mM 2-mercaptoethanol (buffer A) containing 1 ug/mL pepstatin A and 0.4 mM phenylmethylsulfonyl flouride. Cells were homogenized and then lysed by two passes through a microfluidizer (M110-Y, Microfludics) at 12,000 psi. Cell debris was removed by centrifugation at 30,000 g for 30 min. The supernatant was applied to a Ni-NTA agarose column and washed with 3 column volumes of buffer A. The column was then washed with 3 column volumes of 30 mM imidazole in buffer A and proIL-18 was eluted with 300 mM imidazole in buffer A, which was then dialyzed into 25 mM HEPES (pH 7.5), 100 mM NaCl, 10 mM 2-mercaptoethanol. The hexa-His tagged “pro” domain was removed by cleavage with hexa-His tagged Caspase 5 at a proIL-18:Caspase 5 ratio of 50:1 by weight for 2 hours at room temperature. The salt concentration of the protein mixture was adjusted to 0.5M NaCl and the mixture was then applied to a Ni-NTA agarose column. Mature IL-18 flowed through the column, while trace amount of intact proIL-18, the “pro” domain, Caspase5 and other minor contaminants were bound to the Ni-NTA column. Mature hIL-18 in the Ni-NTA flow-through fraction was diluted 1:10 with 25 mM Tris (pH 7.5), 5 mM 2-mercaptoethanol (buffer B). The protein solution was then applied to a MonoQ column, and elution was carried out with a linear gradient of 0-0.3M NaCl in Buffer B, preferably in 20 column volumes. Fractions collected after the column containing IL-18 were pooled based on absorbance at 280 nm wavelength and results of SDS-PAGE. The pool was then applied to a HiLoad 26/60 Superdex 75 prep grade column, which was pre-equilibrated with 25 mM Tris (pH 8), 50 mM NaCl, 5 mM 2-mercaptoethanol, 0.1 mM EDTA, and the elution of the desired protein was carried out at a flow rate of 2.5 mL/min. IL-18 was eluted as a single symmetrical peak. Fractions corresponding to this peak were pooled and the protein in the pool was then concentrated to 10.2 mg/mL for crystallization. This resulting product was greater than 95% pure by SDS-PAGE and has the desired activity. N-terminal amino acid analysis was used to confirm its identity.

[0040] The invention described herein provides a method for defining ligand interactions with IL-18 and its receptor:

[0041] 1.A. Effects of ligand binding upon enzyme intrinsicfluorescence generated by tryptophan residues. Binding of either a natural ligand or a derivatized molecule may result in conformational changes that alter protein intrinsic fluorescence. Using stopped-flow fluorescence technology, one can use this change in intrinsic fluorescence to define the microscopic rate constants that are associated with ligand binding. Alternatively, one can use steady-state fluorescence titration methods to generate the overall dissociation constant for binding. Standard methods are applied in assessing the acquired parameters.

Example 2

Crystallization, Structure Determination and Refinement of the Crystal Structure of the Human IL-18

[0042] 2.A. Crystallization

[0043] The human IL-18 C38S crystals grew as hexagonal rods from sitting drops equilibrated through the vapor phase at room temperature against a reservoir of 500 μL solution containing 20% polyethylene glycol (PEG), 0.07 mM sodium citrate at pH 5.6, and 0.133 M ammonium acetate for 2-3 weeks in Cryschem plates. The drops contained 2 ul of protein at 10 mg/ml in 50 mM NaCl, 25 mM tris at pH 8, 0.1 mM EDTA and 5 mM·−mercaptoethanol. The crystals belong to the space group P6(1) with unit cell dimensions a=71.4 Å, b=71.4 Å, c=88.7 Å, α=β=90°, γ120°, and one copy of the Human IL-18 in the asymmetric unit.

[0044] 2.B. X-Ray Diffraction Data Collection

[0045] We collected the x-ray diffraction data through a single human IL-18 (C38S) crystal suspended by a nylon loop and flash frozen under the cold stream of nitrogen gas. The diffraction parameters were generated by an ADSC Quantum 210 charge-coupled device at the 171D beamline at the Advanced Photon Source, Argonne National Laboratory, Illinois. The wavelength of the monochromatic x-ray beam was set at 1.000 Å. The reciprocal space was sampled at 1.0° oscillation steps around the φ goniostat's axis. The data were processed with HKL2000. Otwinowski, Z. in Proceedings of the CCP4 Study Weekend: “Data Collection and Processing”, 29-30 January, SERC Daresbury Laboratory, England (1993).

[0046] 2.C. Structure Determination

[0047] The crystal structure of human IL-18 was determined by molecular replacement with the program package AMoRe [Navaza, J. Acta Cryst. A50, 157-163 (1994)] using the crystal structure of murine IL-18 stripped of solvent molecules as search model as the murine and the human IL-18 proteins share 65% amino acid sequence identity. The search molecule was placed in an orthogonal cell of dimensions 100 Å×100 Å×100 Å. The cross rotation and translation searches were carried out using data from 20 Å to 4 Å resolutions and a radius of integration of 25 Å. The top solution of the cross rotation function corresponded to the IL-18 molecule in the asymmetric unit and was unambiguously discriminated from the noise peaks. The search for correct translation yielded a solution with an R-factor of 0.45 and a correlation coefficient of 0.47 after rigid body refinement in AMoRe.

[0048] 2.D. Model Building and Refinement

[0049] The native hIL-18 structure was built from the rotation and translation operations found by molecular replacement using the murine IL-18 structure. The human IL-18 structure was built following the 2Fo-Fc and Fo-Fc electron density maps. According to these maps, one can establish the human IL-18 rough model by replacing the amino acids present in the murine structure with those in the human protein, as well as by adding or deleting residues. We used the interactive computer graphics program XTALVIEW to perform these manipulations. McRee J. Structural Biology 125, 156-165 (1999). This rough model was then subjected to rounds of simulated annealing, positional and B-factor refinement using CNX [Brunger, et al., Science, 235, 458-460 (1987)] and REFMAC [Murshudov, et al. Acta Crystallographica D5, 240-255 (1997)] followed by manual intervention. The refinement and manual rebuilding was monitored by the quality of the 2Fo-Fc and Fo-Fc electron density maps, as well as the value of the crystallographic R and Rfree. Throughout the refinement, reflection data from infinity to 2.06A were used, when necessary, accounting for the bulk solvent inside the crystal, which may contribute to the diffraction intensity. The final model of the human IL-18 (C38S) encompasses residues 1 to 156 [SEQ ID NO: 1], and 208 water molecules. The R-factor of the model is 0.16 and the Rfree is 0.19 for 15,011 reflections. The r.m.s. deviations from the standard geometry [Engh, et al., Acta Cryst. A47, 392-400 (1991)] are 0.013 Å for bond lengths, and 1.5° for bond angles.

TABLE I
Atomic coordinates of the native human IL-18 structure (C38S mutant)
ATOM	1	N	TYR	A	1	8.630	49.746	−20.359	1.00	14.94	N
ATOM	3	CA	TYR	A	1	7.622	50.752	−19.957	1.00	14.81	C
ATOM	5	CB	TYR	A	1	7.014	51.448	−21.187	1.00	15.67	C
ATOM	8	CG	TYR	A	1	6.353	50.513	−22.163	1.00	15.20	C
ATOM	9	CD1	TYR	A	1	5.018	50.210	−22.052	1.00	16.18	C
ATOM	11	CE1	TYR	A	1	4.398	49.361	−22.952	1.00	15.83	C
ATOM	13	CZ	TYR	A	1	5.131	48.807	−23.970	1.00	17.36	C
ATOM	14	OH	TYR	A	1	4.512	47.958	−24.847	1.00	18.90	O
ATOM	16	CE2	TYR	A	1	6.473	49.093	−24.104	1.00	17.52	C
ATOM	18	CD2	TYR	A	1	7.071	49.951	−23.208	1.00	17.35	C
ATOM	20	C	TYR	A	1	6.532	50.086	−19.120	1.00	14.70	C
ATOM	21	O	TYR	A	1	6.242	48.889	−19.271	1.00	16.08	O
ATOM	24	N	PHE	A	2	6.032	50.833	−18.155	1.00	14.03	N
ATOM	26	CA	PHE	A	2	4.963	50.411	−17.278	1.00	13.54	C
ATOM	28	CB	PHE	A	2	5.378	50.722	−15.844	1.00	13.04	C
ATOM	31	CG	PHE	A	2	6.744	50.244	−15.468	1.00	12.18	C
ATOM	32	CD1	PHE	A	2	6.915	49.016	−14.847	1.00	13.65	C
ATOM	34	GE1	PHE	A	2	8.160	48.576	−14.433	1.00	12.75	C
ATOM	36	CZ	PHE	A	2	9.269	49.381	−14.620	1.00	14.76	C
ATOM	38	CE2	PHE	A	2	9.127	50.623	−15.241	1.00	13.52	C
ATOM	40	CD2	PHE	A	2	7.854	51.057	−15.649	1.00	12.68	C
ATOM	42	C	PHE	A	2	3.606	51.076	−17.477	1.00	14.09	C
ATOM	43	O	PHE	A	2	3.511	52.287	−17.726	1.00	13.42	O
ATOM	44	N	GLY	A	3	2.547	50.290	−17.294	1.00	14.44	N
ATOM	46	CA	GLY	A	3	1.187	50.806	−17.348	1.00	14.64	C
ATOM	49	C	GLY	A	3	0.397	50.402	−16.119	1.00	14.74	C
ATOM	50	O	GLY	A	3	0.292	49.232	−15.795	1.00	14.03	O
ATOM	51	N	LYS	A	4	−0.204	51.371	−15.444	1.00	15.75	N
ATOM	53	CA	LYS	A	4	−0.942	51.083	−14.222	1.00	17.05	C
ATOM	55	CB	LYS	A	4	−1.367	52.366	−13.504	1.00	17.49	C
ATOM	58	CG	LYS	A	4	−1.976	52.087	−12.151	1.00	19.63	C
ATOM	61	CD	LYS	A	4	−2.051	53.336	−11.284	1.00	24.07	C
ATOM	64	CE	LYS	A	4	−3.193	54.244	−11.670	1.00	26.40	C
ATOM	67	NZ	LYS	A	4	−3.087	55.505	−10.873	1.00	31.21	N
ATOM	71	C	LYS	A	4	−2.157	50.208	−14.457	1.00	17.39	C
ATOM	72	O	LYS	A	4	−2.955	50.480	−15.345	1.00	16.52	O
ATOM	73	N	LEU	A	5	−2.298	49.173	−13.627	1.00	17.66	N
ATOM	75	CA	LEU	A	5	−3.398	48.220	−13.739	1.00	19.03	C
ATOM	77	CB	LEU	A	5	−2.855	46.800	−13.671	1.00	19.09	C
ATOM	80	CG	LEU	A	5	−2.134	46.301	−14.916	1.00	19.65	C
ATOM	82	CD1	LEU	A	5	−1.691	44.853	−14.704	1.00	21.62	C
ATOM	86	CD2	LEU	A	5	−3.046	46.419	−16.101	1.00	19.89	C
ATOM	90	C	LEU	A	5	−4.497	48.348	−12.678	1.00	20.37	C
ATOM	91	O	LEU	A	5	−5.690	48.249	−12.987	1.00	21.59	O
ATOM	92	N	GLU	A	6	−4.097	48.516	−11.436	1.00	20.59	N
ATOM	94	CA	GLU	A	6	−5.034	48.628	−10.325	1.00	21.77	C
ATOM	96	CB	GLU	A	6	−5.712	47.296	−10.065	1.00	22.73	C
ATOM	99	CG	GLU	A	6	−4.724	46.187	−9.798	1.00	26.49	C
ATOM	102	CD	GLU	A	6	−5.382	44.911	−9.318	1.00	31.62	C
ATOM	103	OE1	GLU	A	6	−4.684	43.887	−9.245	1.00	32.77	O
ATOM	104	OE2	GLU	A	6	−6.595	44.930	−9.000	1.00	36.73	O
ATOM	105	C	GLU	A	6	−4.268	49.047	−9.080	1.00	20.79	C
ATOM	106	O	GLU	A	6	−3.034	48.979	−9.040	1.00	20.65	O
ATOM	107	N	SER	A	7	−5.017	49.490	−8.086	1.00	20.46	N
ATOM	109	CA	SER	A	7	−4.492	49.930	−6.811	1.00	20.67	C
ATOM	111	CB	SER	A	7	−4.672	51.438	−6.642	1.00	20.28	C
ATOM	114	OG	SER	A	7	−3.791	52.137	−7.506	1.00	24.79	O
ATOM	116	C	SER	A	7	−5.276	49.228	−5.710	1.00	20.43	C
ATOM	117	O	SER	A	7	−6.474	49.004	−5.856	1.00	19.94	O
ATOM	118	N	LYS	A	8	−4.587	48.889	−4.624	1.00	19.55	N
ATOM	120	CA	LYS	A	8	−5.213	48.272	−3.458	1.00	19.39	C
ATOM	122	CB	LYS	A	8	−4.888	46.787	−3.412	1.00	20.02	C
ATOM	125	CG	LYS	A	8	−5.493	45.978	−4.540	1.00	21.94	C
ATOM	128	CD	LYS	A	8	−5.161	44.528	−4.333	1.00	24.93	C
ATOM	131	CE	LYS	A	8	−5.776	43.657	−5.419	1.00	26.32	C
ATOM	134	NZ	LYS	A	8	−5.403	42.241	−5.206	1.00	27.21	N
ATOM	138	C	LYS	A	8	−4.701	48.922	−2.174	1.00	18.17	C
ATOM	139	O	LYS	A	8	−3.485	49.106	−2.006	1.00	16.83	O
ATOM	140	N	LEU	A	9	−5.629	49.254	−1.278	1.00	17.07	N
ATOM	142	CA	LEU	A	9	−5.296	49.794	0.032	1.00	16.73	C
ATOM	144	CB	LEU	A	9	−6.529	50.363	0.704	1.00	17.11	C
ATOM	147	CG	LEU	A	9	−7.184	51.496	−0.085	1.00	19.58	C
ATOM	149	CD1	LEU	A	9	−8.444	52.030	0.604	1.00	22.37	C
ATOM	153	CD2	LEU	A	9	−6.196	52.621	−0.295	1.00	20.80	C
ATOM	157	C	LEU	A	9	−4.749	48.596	0.821	1.00	15.48	C
ATOM	158	O	LEU	A	9	−5.378	47.536	0.889	1.00	15.33	O
ATOM	159	N	SER	A	10	−3.583	48.802	1.401	1.00	13.41	N
ATOM	161	CA	SER	A	10	−2.827	47.716	1.965	1.00	13.59	C
ATOM	163	CB	SER	A	10	−1.726	47.297	0.989	1.00	13.55	C
ATOM	166	OG	SER	A	10	−2.220	47.028	−0.310	1.00	14.09	O
ATOM	168	C	SER	A	10	−2.140	48.081	3.251	1.00	12.56	C
ATOM	169	O	SER	A	10	−1.846	49.255	3.499	1.00	12.15	O
ATOM	170	N	VAL	A	11	−1.897	47.050	4.050	1.00	11.93	N
ATOM	172	CA	VAL	A	11	−1.124	47.153	5.279	1.00	12.46	C
ATOM	174	CB	VAL	A	11	−1.925	46.668	6.502	1.00	12.74	C
ATOM	176	CG1	VAL	A	11	−1.025	46.547	7.736	1.00	13.13	C
ATOM	180	CG2	VAL	A	11	−3.047	47.635	6.788	1.00	13.37	C
ATOM	184	C	VAL	A	11	0.124	46.292	5.120	1.00	12.52	C
ATOM	185	O	VAL	A	11	0.050	45.111	4.755	1.00	12.52	O
ATOM	186	N	ILE	A	12	1.275	46.880	5.395	1.00	12.68	N
ATOM	188	CA	ILE	A	12	2.537	46.173	5.242	1.00	12.62	C
ATOM	190	CB	ILE	A	12	3.509	47.034	4.439	1.00	12.98	C
ATOM	192	CG1	ILE	A	12	2.979	47.227	3.022	1.00	13.10	C
ATOM	195	CD1	ILE	A	12	3.709	48.301	2.231	1.00	14.66	C
ATOM	199	CG2	ILE	A	12	4.890	46.401	4.443	1.00	13.83	C
ATOM	203	C	ILE	A	12	3.120	45.900	6.625	1.00	12.91	C
ATOM	204	O	ILE	A	12	3.212	46.819	7.446	1.00	12.37	O
ATOM	205	N	ARG	A	13	3.520	44.657	6.869	1.00	12.43	N
ATOM	207	CA	ARG	A	13	4.105	44.265	8.153	1.00	13.04	C
ATOM	209	CB	ARG	A	13	3.184	43.292	8.899	1.00	13.05	C
ATOM	212	CG	ARG	A	13	1.818	43.843	9.322	1.00	14.08	C
ATOM	215	CD	ARG	A	13	0.904	42.765	9.928	1.00	13.91	C
ATOM	218	NE	ARG	A	13	−0.351	43.276	10.454	1.00	13.75	N
ATOM	220	CZ	ARG	A	13	−1.458	43.447	9.737	1.00	15.14	C
ATOM	221	NH1	ARG	A	13	−1.462	43.161	8.440	1.00	14.09	N
ATOM	224	NH2	ARG	A	13	−2.567	43.901	10.321	1.00	13.65	N
ATOM	227	C	ARG	A	13	5.447	43.569	7.954	1.00	13.59	C
ATOM	228	O	ARG	A	13	5.634	42.851	6.975	1.00	12.69	O
ATOM	229	N	ASN	A	14	6.379	43.792	8.880	1.00	15.35	N
ATOM	231	CA	ASN	A	14	7.633	43.049	8.867	1.00	16.85	C
ATOM	233	CB	ASN	A	14	8.780	43.805	9.553	1.00	16.93	C
ATOM	236	CG	ASN	A	14	8.556	44.042	11.034	1.00	16.46	C
ATOM	237	OD1	ASN	A	14	7.799	43.336	11.697	1.00	13.43	O
ATOM	238	ND2	ASN	A	14	9.263	45.048	11.568	1.00	16.09	N
ATOM	241	C	ASN	A	14	7.368	41.676	9.499	1.00	18.25	C
ATOM	242	O	ASN	A	14	6.252	41.390	9.918	1.00	18.18	O
ATOM	243	N	LEU	A	15	8.375	40.826	9.576	1.00	20.32	N
ATOM	245	CA	LEU	A	15	8.124	39.467	10.062	1.00	21.88	C
ATOM	247	CB	LEU	A	15	9.234	38.507	9.627	1.00	22.23	C
ATOM	250	CG	LEU	A	15	9.353	38.222	8.114	1.00	22.83	C
ATOM	252	CD1	LEU	A	15	9.887	36.778	7.890	1.00	22.15	C
ATOM	256	CD2	LEU	A	15	8.051	38.413	7.366	1.00	22.19	C
ATOM	260	C	LEU	A	15	7.895	39.420	11.582	1.00	22.33	C
ATOM	261	O	LEU	A	15	7.426	38.423	12.109	1.00	23.76	O
ATOM	262	N	ASN	A	16	8.195	40.504	12.278	1.00	22.29	N
ATOM	264	CA	ASN	A	16	7.878	40.564	13.697	1.00	21.75	C
ATOM	266	CB	ASN	A	16	8.905	41.415	14.418	1.00	21.71	C
ATOM	269	CG	ASN	A	16	10.266	40.727	14.533	1.00	22.48	C
ATOM	270	OD1	ASN	A	16	11.306	41.387	14.586	1.00	22.21	O
ATOM	271	ND2	ASN	A	16	10.252	39.402	14.596	1.00	21.88	N
ATOM	274	C	ASN	A	16	6.480	41.133	13.903	1.00	21.33	C
ATOM	275	O	ASN	A	16	6.118	41.509	14.999	1.00	20.43	O
ATOM	276	N	ASP	A	17	5.705	41.215	12.832	1.00	20.83	N
ATOM	278	CA	ASP	A	17	4.334	41.740	12.884	1.00	20.97	C
ATOM	280	CB	ASP	A	17	3.430	40.834	13.697	1.00	22.16	C
ATOM	283	CG	ASP	A	17	3.011	39.651	12.901	1.00	26.40	C
ATOM	284	OD1	ASP	A	17	2.402	39.847	11.812	1.00	32.51	O
ATOM	285	OD2	ASP	A	17	3.303	38.496	13.221	1.00	30.36	O
ATOM	286	C	ASP	A	17	4.186	43.207	13.315	1.00	18.94	C
ATOM	287	O	ASP	A	17	3.136	43.632	13.802	1.00	18.69	O
ATOM	288	N	GLN	A	18	5.247	43.964	13.108	1.00	17.49	N
ATOM	290	CA	GLN	A	18	5.198	45.399	13.285	1.00	16.92	C
ATOM	292	CB	GLN	A	18	6.590	45.923	13.586	1.00	16.50	C
ATOM	295	CG	GLN	A	18	7.108	45.430	14.943	1.00	17.24	C
ATOM	298	CD	GLN	A	18	8.544	45.802	15.159	1.00	19.07	C
ATOM	299	OE1	GLN	A	18	9.351	45.673	14.238	1.00	19.30	O
ATOM	300	NE2	GLN	A	18	8.874	46.289	16.354	1.00	20.48	N
ATOM	303	C	GLN	A	18	4.626	46.021	12.013	1.00	16.02	C
ATOM	304	O	GLN	A	18	4.992	45.613	10.904	1.00	16.32	O
ATOM	305	N	VAL	A	19	3.750	47.011	12.178	1.00	15.43	N
ATOM	307	CA	VAL	A	19	3.060	47.647	11.055	1.00	14.72	C
ATOM	309	CB	VAL	A	19	1.563	48.003	11.380	1.00	14.93	C
ATOM	311	CG1A	VAL	A	19	0.810	48.788	10.288	0.50	14.38	C
ATOM	312	CG1B	VAL	A	19	1.347	48.282	12.814	0.50	15.70	C
ATOM	319	CG2A	VAL	A	19	0.845	47.018	12.321	0.50	14.75	C
ATOM	320	CG2B	VAL	A	19	1.068	49.159	10.542	0.50	14.36	C
ATOM	327	C	VAL	A	19	3.779	48.896	10.566	1.00	14.47	C
ATOM	328	O	VAL	A	19	4.161	49.761	11.354	1.00	13.42	O
ATOM	329	N	LEU	A	20	3.964	48.963	9.259	1.00	14.08	N
ATOM	331	CA	LEU	A	20	4.587	50.111	8.636	1.00	14.51	C
ATOM	333	CB	LEU	A	20	4.888	49.830	7.170	1.00	14.38	C
ATOM	336	CG	LEU	A	20	5.474	51.015	6.388	1.00	14.85	C
ATOM	338	CD1	LEU	A	20	6.883	51.390	6.861	1.00	14.80	C
ATOM	342	CD2	LEU	A	20	5.491	50.702	4.932	1.00	14.95	C
ATOM	346	C	LEU	A	20	3.655	51.306	8.766	1.00	15.20	C
ATOM	347	O	LEU	A	20	2.445	51.191	8.524	1.00	15.29	O
ATOM	348	N	PHE	A	21	4.212	52.444	9.169	1.00	15.37	N
ATOM	350	CA	PHE	A	21	3.454	53.695	9.231	1.00	16.45	C
ATOM	352	CB	PHE	A	21	2.786	53.894	10.604	1.00	16.28	C
ATOM	355	CG	PHE	A	21	3.720	54.366	11.701	1.00	16.48	C
ATOM	356	CD1	PHE	A	21	4.552	53.483	12.370	1.00	17.40	C
ATOM	358	CE1	PHE	A	21	5.419	53.941	13.411	1.00	18.30	C
ATOM	360	CZ	PHE	A	21	5.412	55.294	13.771	1.00	18.26	C
ATOM	362	CE2	PHE	A	21	4.593	56.183	13.086	1.00	18.61	C
ATOM	364	CD2	PHE	A	21	3.738	55.711	12.078	1.00	19.14	C
ATOM	366	C	PHE	A	21	4.352	54.889	8.909	1.00	17.19	C
ATOM	367	O	PHE	A	21	5.582	54.794	8.984	1.00	17.08	O
ATOM	368	N	ILE	A	22	3.735	56.006	8.551	1.00	18.19	N
ATOM	370	CA	ILE	A	22	4.473	57.247	8.310	1.00	19.74	C
ATOM	372	CB	ILE	A	22	3.975	57.931	7.039	1.00	20.03	C
ATOM	374	CG1	ILE	A	22	4.374	57.152	5.775	1.00	21.05	C
ATOM	377	CD1	ILE	A	22	5.115	55.901	5.962	1.00	22.97	C
ATOM	381	CG2	ILE	A	22	4.606	59.310	6.897	1.00	20.32	C
ATOM	385	C	ILE	A	22	4.289	58.164	9.527	1.00	20.68	C
ATOM	386	O	ILE	A	22	3.165	58.487	9.894	1.00	20.48	O
ATOM	387	N	ASP	A	23	5.374	58.570	10.174	1.00	21.90	N
ATOM	389	CA	ASP	A	23	5.210	59.413	11.345	1.00	23.59	C
ATOM	391	CB	ASP	A	23	6.371	59.282	12.290	1.00	23.31	C
ATOM	394	CG	ASP	A	23	7.588	60.112	11.860	1.00	23.99	C
ATOM	395	OD1	ASP	A	23	7.524	60.875	10.853	1.00	20.95	O
ATOM	396	OD2	ASP	A	23	8.660	60.019	12.484	1.00	22.12	O
ATOM	397	C	ASP	A	23	5.022	60.863	10.988	1.00	25.67	C
ATOM	398	O	ASP	A	23	4.902	61.241	9.819	1.00	25.35	O
ATOM	399	N	GLN	A	24	5.013	61.682	12.023	1.00	28.27	N
ATOM	401	CA	GLN	A	24	4.730	63.084	11.851	1.00	30.16	C
ATOM	403	CB	GLN	A	24	4.695	63.768	13.193	1.00	31.23	C
ATOM	406	CG	GLN	A	24	3.617	64.750	13.185	1.00	34.46	C
ATOM	409	CD	GLN	A	24	2.313	64.046	13.001	1.00	38.96	C
ATOM	410	OE1	GLN	A	24	2.017	63.133	13.772	1.00	43.16	O
ATOM	411	NE2	GLN	A	24	1.537	64.425	11.978	1.00	40.28	N
ATOM	414	C	GLN	A	24	5.715	63.792	10.963	1.00	30.13	C
ATOM	415	O	GLN	A	24	5.349	64.732	10.259	1.00	31.25	O
ATOM	416	N	GLY	A	25	6.962	63.353	10.998	1.00	30.11	N
ATOM	418	CA	GLY	A	25	7.996	63.952	10.180	1.00	29.92	C
ATOM	421	C	GLY	A	25	8.146	63.264	8.843	1.00	29.87	C
ATOM	422	O	GLY	A	25	9.175	63.397	8.183	1.00	29.58	O
ATOM	423	N	ASN	A	26	7.118	62.522	8.442	1.00	29.58	N
ATOM	425	CA	ASN	A	26	7.136	61.802	7.178	1.00	29.55	C
ATOM	427	CB	ASN	A	26	7.384	62.756	6.012	1.00	30.28	C
ATOM	430	CG	ASN	A	26	6.170	63.575	5.684	1.00	33.62	C
ATOM	431	OD1	ASN	A	26	5.067	63.042	5.573	1.00	37.65	O
ATOM	432	ND2	ASN	A	26	6.357	64.886	5.532	1.00	38.42	N
ATOM	435	C	ASN	A	26	8.143	60.675	7.118	1.00	28.05	C
ATOM	436	O	ASN	A	26	8.494	60.248	6.033	1.00	28.17	O
ATOM	437	N	ARG	A	27	8.618	60.200	8.262	1.00	26.49	N
ATOM	439	CA	ARG	A	27	9.525	59.062	8.268	1.00	25.79	C
ATOM	441	CB	ARG	A	27	10.450	59.084	9.483	1.00	26.33	C
ATOM	444	CG	ARG	A	27	11.225	60.360	9.668	1.00	30.28	C
ATOM	447	CD	ARG	A	27	12.200	60.298	10.846	1.00	34.79	C
ATOM	450	NE	ARG	A	27	11.489	60.110	12.114	1.00	38.56	N
ATOM	452	CZ	ARG	A	27	12.070	59.977	13.308	1.00	40.76	C
ATOM	453	NH1	ARG	A	27	13.398	59.987	13.428	1.00	41.30	N
ATOM	456	NH2	ARG	A	27	11.307	59.835	14.388	1.00	41.91	N
ATOM	459	C	ARG	A	27	8.710	57.765	8.315	1.00	23.60	C
ATOM	460	O	ARG	A	27	7.772	57.651	9.103	1.00	22.10	O
ATOM	461	N	PRO	A	28	9.058	56.812	7.456	1.00	21.49	N
ATOM	462	CA	PRO	A	28	8.430	55.488	7.468	1.00	20.18	C
ATOM	464	CB	PRO	A	28	8.748	54.928	6.085	1.00	20.54	C
ATOM	467	CG	PRO	A	28	10.020	55.613	5.664	1.00	21.03	C
ATOM	470	CD	PRO	A	28	10.067	56.940	6.389	1.00	22.11	C
ATOM	473	C	PRO	A	28	9.069	54.647	8.556	1.00	18.85	C
ATOM	474	O	PRO	A	28	10.279	54.417	8.523	1.00	17.72	O
ATOM	475	N	LEU	A	29	8.258	54.232	9.522	1.00	17.18	N
ATOM	477	CA	LEU	A	29	8.709	53.458	10.666	1.00	16.68	C
ATOM	479	CB	LEU	A	29	8.681	54.327	11.923	1.00	16.73	C
ATOM	482	CG	LEU	A	29	9.498	55.626	11.931	1.00	18.13	C
ATOM	484	CD1	LEU	A	29	9.300	56.348	13.249	1.00	19.44	C
ATOM	488	CD2	LEU	A	29	10.967	55.328	11.726	1.00	20.09	C
ATOM	492	C	LEU	A	29	7.768	52.268	10.876	1.00	16.01	C
ATOM	493	O	LEU	A	29	6.731	52.174	10.233	1.00	15.65	O
ATOM	494	N	PHE	A	30	8.134	51.365	11.775	1.00	15.25	N
ATOM	496	CA	PHE	A	30	7.296	50.224	12.086	1.00	15.64	C
ATOM	498	CB	PHE	A	30	8.053	48.932	11.839	1.00	15.29	C
ATOM	501	CG	PHE	A	30	8.347	48.671	10.393	1.00	16.95	C
ATOM	502	CD1	PHE	A	30	7.470	47.944	9.628	1.00	16.18	C
ATOM	504	CE1	PHE	A	30	7.743	47.696	8.310	1.00	17.73	C
ATOM	506	CZ	PHE	A	30	8.916	48.173	7.741	1.00	15.84	C
ATOM	508	CE2	PHE	A	30	9.786	48.907	8.498	1.00	17.01	C
ATOM	510	CD2	PHE	A	30	9.506	49.158	9.803	1.00	17.48	C
ATOM	512	C	PHE	A	30	6.890	50.292	13.542	1.00	15.79	C
ATOM	513	O	PHE	A	30	7.754	50.559	14.411	1.00	15.41	O
ATOM	514	N	GLU	A	31	5.604	50.046	13.824	1.00	15.45	N
ATOM	516	CA	GLU	A	31	5.104	50.071	15.198	1.00	15.66	C
ATOM	518	CB	GLU	A	31	3.888	51.010	15.305	1.00	15.53	C
ATOM	521	CG	GLU	A	31	2.754	50.570	14.412	1.00	15.41	C
ATOM	524	CD	GLU	A	31	1.442	51.322	14.572	1.00	16.44	C
ATOM	525	OE1	GLU	A	31	1.359	52.266	15.387	1.00	13.75	O
ATOM	526	OE2	GLU	A	31	0.479	50.938	13.843	1.00	14.63	O
ATOM	527	C	GLU	A	31	4.678	48.693	15.726	1.00	15.83	C
ATOM	528	O	GLU	A	31	4.139	47.873	14.994	1.00	15.40	O
ATOM	529	N	ASP	A	32	4.941	48.435	16.999	1.00	16.09	N
ATOM	531	CA	ASP	A	32	4.344	47.287	17.662	1.00	17.04	C
ATOM	533	CB	ASP	A	32	5.025	47.017	18.992	1.00	17.47	C
ATOM	536	CG	ASP	A	32	6.428	46.518	18.810	1.00	19.12	C
ATOM	537	OD1	ASP	A	32	6.606	45.401	18.291	1.00	21.41	O
ATOM	538	OD2	ASP	A	32	7.406	47.198	19.108	1.00	25.01	O
ATOM	539	C	ASP	A	32	2.895	47.694	17.876	1.00	16.81	C
ATOM	540	O	ASP	A	32	2.629	48.861	18.102	1.00	16.58	O
ATOM	541	N	MET	A	33	1.954	46.762	17.800	1.00	17.50	N
ATOM	543	CA	MET	A	33	0.554	47.168	17.893	1.00	17.48	C
ATOM	545	CB	MET	A	33	−0.393	46.143	17.275	1.00	18.16	C
ATOM	548	CG	MET	A	33	−0.360	46.163	15.700	1.00	18.54	C
ATOM	551	SD	MET	A	33	−0.191	47.820	14.901	1.00	18.88	S
ATOM	552	CE	MET	A	33	−1.646	48.558	15.544	1.00	18.31	C
ATOM	556	C	MET	A	33	0.124	47.608	19.291	1.00	17.13	C
ATOM	557	O	MET	A	33	−0.888	48.290	19.406	1.00	16.82	O
ATOM	558	N	THR	A	34	0.888	47.277	20.334	1.00	16.03	N
ATOM	560	CA	THR	A	34	0.594	47.843	21.661	1.00	16.95	C
ATOM	562	CB	THR	A	34	1.067	46.922	22.810	1.00	17.06	C
ATOM	564	OG1	THR	A	34	2.437	46.535	22.601	1.00	17.60	O
ATOM	566	CG2	THR	A	34	0.295	45.631	22.830	1.00	17.37	C
ATOM	570	C	THR	A	34	1.226	49.233	21.892	1.00	16.97	C
ATOM	571	O	THR	A	34	1.063	49.809	22.967	1.00	16.35	O
ATOM	572	N	ASP	A	35	1.959	49.764	20.913	1.00	17.24	N
ATOM	574	CA	ASP	A	35	2.607	51.077	21.085	1.00	17.24	C
ATOM	576	CB	AASP	A	35	3.396	51.495	19.826	0.65	18.25	C
ATOM	577	CB	BASP	A	35	3.292	51.498	19.791	0.35	17.62	C
ATOM	582	CG	AASP	A	35	4.768	50.803	19.725	0.65	19.33	C
ATOM	583	CG	BASP	A	35	4.269	52.628	19.991	0.35	16.99	C
ATOM	584	OD1	AASP	A	35	5.171	50.175	20.724	0.65	21.32	O
ATOM	585	OD1	BASP	A	35	3.849	53.771	20.278	0.35	17.45	O
ATOM	586	OD2	AASP	A	35	5.517	50.829	18.704	0.65	18.98	O
ATOM	587	OD2	BASP	A	35	5.489	52.452	19.877	0.35	18.50	O
ATOM	588	C	ASP	A	35	1.568	52.125	21.447	1.00	16.93	C
ATOM	589	O	ASP	A	35	0.458	52.119	20.920	1.00	15.87	O
ATOM	590	N	SER	A	36	1.916	53.014	22.368	1.00	16.95	N
ATOM	592	CA	SER	A	36	0.993	54.048	22.803	1.00	17.78	C
ATOM	594	CB	SER	A	36	1.609	54.870	23.941	1.00	18.53	C
ATOM	597	OG	SER	A	36	2.790	55.507	23.522	1.00	17.91	O
ATOM	599	C	SER	A	36	0.592	54.969	21.660	1.00	18.33	C
ATOM	600	O	SER	A	36	−0.480	55.563	21.689	1.00	18.76	O
ATOM	601	N	ASP	A	37	1.430	55.078	20.638	1.00	18.42	N
ATOM	603	CA	ASP	A	37	1.096	55.940	19.497	1.00	18.89	C
ATOM	605	CB	ASP	A	37	2.360	56.489	18.847	1.00	19.65	C
ATOM	608	CG	ASP	A	37	3.039	57.516	19.707	1.00	22.76	C
ATOM	609	OD1	ASP	A	37	4.262	57.695	19.544	1.00	27.47	O
ATOM	610	OD2	ASP	A	37	2.422	58.204	20.552	1.00	26.72	O
ATOM	611	C	ASP	A	37	0.281	55.266	18.423	1.00	17.96	C
ATOM	612	O	ASP	A	37	−0.019	55.885	17.402	1.00	17.62	O
ATOM	613	N	SER	A	38	−0.086	54.008	18.648	1.00	17.23	N
ATOM	615	CA	SER	A	38	−0.855	53.253	17.663	1.00	16.77	C
ATOM	617	CB	SER	A	38	−1.110	51.809	18.147	1.00	16.61	C
ATOM	620	OG	SER	A	38	−1.901	51.787	19.318	1.00	15.78	O
ATOM	622	C	SER	A	38	−2.158	53.959	17.301	1.00	16.78	C
ATOM	623	O	SER	A	38	−2.576	53.934	16.147	1.00	15.87	O
ATOM	624	N	ARG	A	39	−2.785	54.616	18.275	1.00	17.65	N
ATOM	626	CA	ARG	A	39	−4.044	55.326	18.024	1.00	18.06	C
ATOM	628	CB	ARG	A	39	−4.640	55.883	19.328	1.00	18.14	C
ATOM	631	CG	ARG	A	39	−6.006	56.571	19.182	1.00	18.93	C
ATOM	634	CD	ARG	A	39	−6.551	57.235	20.488	1.00	19.91	C
ATOM	637	NE	ARG	A	39	−6.722	56.293	21.606	1.00	18.54	N
ATOM	639	CZ	ARG	A	39	−5.807	56.072	22.546	1.00	19.94	C
ATOM	640	NH1	ARG	A	39	−4.664	56.729	22.529	1.00	20.80	N
ATOM	643	NH2	ARG	A	39	−6.022	55.189	23.516	1.00	20.49	N
ATOM	646	C	ARG	A	39	−3.819	56.465	17.038	1.00	18.21	C
ATOM	647	O	ARG	A	39	−4.537	56.602	16.072	1.00	17.63	O
ATOM	648	N	ASP	A	40	−2.822	57.288	17.317	1.00	19.30	N
ATOM	650	CA	ASP	A	40	−2.525	58.434	16.480	1.00	20.14	C
ATOM	652	CB	ASP	A	40	−1.552	59.372	17.182	1.00	21.06	C
ATOM	655	CG	ASP	A	40	−2.177	60.106	18.356	1.00	24.15	C
ATOM	656	OD1	ASP	A	40	−3.412	60.293	18.387	1.00	28.34	O
ATOM	657	OD2	ASP	A	40	−1.484	60.523	19.302	1.00	29.23	O
ATOM	658	C	ASP	A	40	−1.914	58.004	15.150	1.00	19.89	C
ATOM	659	O	ASP	A	40	−2.141	58.647	14.152	1.00	20.00	O
ATOM	660	N	ASN	A	41	−1.128	56.933	15.132	1.00	19.31	N
ATOM	662	CA	ASN	A	41	−0.520	56.462	13.870	1.00	19.51	C
ATOM	664	CB	ASN	A	41	0.592	55.445	14.159	1.00	19.05	C
ATOM	667	CG	ASN	A	41	1.764	56.052	14.898	1.00	21.10	C
ATOM	668	OD1	ASN	A	41	1.961	57.255	14.870	1.00	20.31	O
ATOM	669	ND2	ASN	A	41	2.560	55.214	15.550	1.00	24.49	N
ATOM	672	C	ASN	A	41	−1.505	55.855	12.864	1.00	19.21	C
ATOM	673	O	ASN	A	41	−1.174	55.753	11.682	1.00	19.13	O
ATOM	674	N	ALA	A	42	−2.695	55.457	13.319	1.00	19.36	N
ATOM	676	CA	ALA	A	42	−3.618	54.653	12.509	1.00	19.44	C
ATOM	678	CB	ALA	A	42	−4.903	54.387	13.256	1.00	19.48	C
ATOM	682	C	ALA	A	42	−3.915	55.138	11.103	1.00	19.95	C
ATOM	683	O	ALA	A	42	−3.876	54.353	10.154	1.00	19.84	O
ATOM	684	N	PRO	A	43	−4.203	56.417	10.955	1.00	20.71	N
ATOM	685	CA	PRO	A	43	−4.505	56.971	9.637	1.00	21.20	C
ATOM	687	CB	PRO	A	43	−4.759	58.460	9.927	1.00	21.84	C
ATOM	690	CG	PRO	A	43	−5.037	58.543	11.381	1.00	22.39	C
ATOM	693	CD	PRO	A	43	−4.254	57.436	12.019	1.00	21.04	C
ATOM	696	C	PRO	A	43	−3.333	56.841	8.672	1.00	21.53	C
ATOM	697	O	PRO	A	43	−3.550	56.857	7.469	1.00	22.82	O
ATOM	698	N	ARG	A	44	−2.118	56.686	9.179	1.00	20.57	N
ATOM	700	CA	ARG	A	44	−0.959	56.606	8.304	1.00	20.37	C
ATOM	702	CB	ARG	A	44	0.087	57.576	8.814	1.00	21.51	C
ATOM	705	CG	ARG	A	44	−0.541	58.875	9.220	1.00	26.78	C
ATOM	708	CD	ARG	A	44	−0.279	59.996	8.301	1.00	33.29	C
ATOM	711	NE	ARG	A	44	0.915	60.767	8.640	1.00	38.91	N
ATOM	713	CZ	ARG	A	44	1.625	60.674	9.768	1.00	43.23	C
ATOM	714	NH1	ARG	A	44	1.303	59.841	10.755	1.00	44.56	N
ATOM	717	NH2	ARG	A	44	2.695	61.448	9.914	1.00	46.10	N
ATOM	720	C	ARG	A	44	−0.353	55.215	8.205	1.00	18.39	C
ATOM	721	O	ARG	A	44	0.863	55.074	7.974	1.00	16.70	O
ATOM	722	N	THR	A	45	−1.190	54.197	8.389	1.00	17.18	N
ATOM	724	CA	THR	A	45	−0.753	52.810	8.223	1.00	15.95	C
ATOM	726	CB	THR	A	45	−1.224	51.926	9.383	1.00	15.81	C
ATOM	728	OG1	THR	A	45	−2.651	51.973	9.481	1.00	13.66	O
ATOM	730	CG2	THR	A	45	−0.714	52.419	10.721	1.00	15.45	C
ATOM	734	C	THR	A	45	−1.324	52.214	6.943	1.00	16.30	C
ATOM	735	O	THR	A	45	−1.043	51.068	6.625	1.00	15.65	O
ATOM	736	N	ILE	A	46	−2.133	52.979	6.215	1.00	16.29	N
ATOM	738	CA	ILE	A	46	−2.794	52.459	5.022	1.00	16.92	C
ATOM	740	CB	ILE	A	46	−4.253	52.921	4.967	1.00	17.44	C
ATOM	742	CG1	ILE	A	46	−5.014	52.549	6.245	1.00	19.36	C
ATOM	745	CD1	ILE	A	46	−5.026	51.072	6.561	1.00	19.22	C
ATOM	749	CG2	ILE	A	46	−4.961	52.323	3.734	1.00	19.55	C
ATOM	753	C	ILE	A	46	−2.057	52.941	3.778	1.00	16.31	C
ATOM	754	O	ILE	A	46	−1.936	54.137	3.553	1.00	16.76	O
ATOM	755	N	PHE	A	47	−1.542	52.008	2.987	1.00	15.89	N
ATOM	757	CA	PHE	A	47	−0.780	52.356	1.806	1.00	15.36	C
ATOM	759	CB	PHE	A	47	0.605	51.716	1.847	1.00	15.78	C
ATOM	762	CG	PHE	A	47	1.456	52.253	2.948	1.00	15.47	C
ATOM	763	CD1	PHE	A	47	1.353	51.733	4.223	1.00	15.36	C
ATOM	765	CE1	PHE	A	47	2.082	52.258	5.268	1.00	15.99	C
ATOM	767	CZ	PHE	A	47	2.933	53.336	5.052	1.00	17.18	C
ATOM	769	CE2	PHE	A	47	3.034	53.890	3.787	1.00	17.05	C
ATOM	771	CD2	PHE	A	47	2.284	53.349	2.736	1.00	16.13	C
ATOM	773	C	PHE	A	47	−1.512	51.974	0.554	1.00	15.47	C
ATOM	774	O	PHE	A	47	−2.258	50.995	0.523	1.00	15.63	O
ATOM	775	N	ILE	A	48	−1.328	52.799	−0.471	1.00	14.27	N
ATOM	777	CA	ILE	A	48	−1.888	52.544	−1.758	1.00	14.07	C
ATOM	779	CB	ILE	A	48	−2.283	53.858	−2.449	1.00	14.65	C
ATOM	781	CG1	ILE	A	48	−3.246	54.684	−1.591	1.00	16.00	C
ATOM	784	CD1	ILE	A	48	−3.418	56.115	−2.067	1.00	17.30	C
ATOM	788	CG2	ILE	A	48	−2.936	53.550	−3.782	1.00	14.34	C
ATOM	792	C	ILE	A	48	−0.803	51.829	−2.572	1.00	14.12	C
ATOM	793	O	ILE	A	48	0.228	52.414	−2.907	1.00	14.11	O
ATOM	794	N	ILE	A	49	−1.003	50.544	−2.823	1.00	13.76	N
ATOM	796	CA	ILE	A	49	−0.071	49.790	−3.630	1.00	13.76	C
ATOM	798	CB	ILE	A	49	0.212	48.405	−3.032	1.00	13.61	C
ATOM	800	CG1	ILE	A	49	0.795	48.551	−1.629	1.00	15.49	C
ATOM	803	CD1	ILE	A	49	1.141	47.218	−0.962	1.00	15.57	C
ATOM	807	CG2	ILE	A	49	1.205	47.659	−3.897	1.00	14.76	C
ATOM	811	C	ILE	A	49	−0.676	49.689	−5.023	1.00	13.36	C
ATOM	812	O	ILE	A	49	−1.755	49.116	−5.193	1.00	12.10	O
ATOM	813	N	SER	A	50	0.010	50.290	−5.997	1.00	13.17	N
ATOM	815	CA	SER	A	50	−0.438	50.256	−7.379	1.00	13.46	C
ATOM	817	CB	SER	A	50	−0.349	51.637	−8.025	1.00	13.51	C
ATOM	820	OG	SER	A	50	−1.083	52.599	−7.278	1.00	12.74	O
ATOM	822	C	SER	A	50	0.401	49.255	−8.159	1.00	14.11	C
ATOM	823	O	SER	A	50	1.622	49.267	−8.079	1.00	14.03	O
ATOM	824	N	MET	A	51	−0.282	48.374	−8.883	1.00	14.13	N
ATOM	826	CA	MET	A	51	0.361	47.339	−9.693	1.00	15.12	C
ATOM	828	CB	BMET	A	51	−0.394	46.000	−9.589	0.35	15.12	C
ATOM	829	CB	AMET	A	51	−0.407	46.029	−9.572	0.65	14.93	C
ATOM	834	CG	BMET	A	51	−0.328	45.128	−10.870	0.35	17.73	C
ATOM	835	CG	AMET	A	51	−0.029	45.207	−8.357	0.65	18.28	C
ATOM	840	SD	BMET	A	51	−0.785	43.365	−10.693	0.35	22.63	S
ATOM	841	SD	AMET	A	51	−0.357	45.980	−6.772	0.65	23.51	S
ATOM	842	CE	BMET	A	51	−2.496	43.412	−10.740	0.35	21.88	C
ATOM	843	CE	AMET	A	51	−2.160	45.935	−6.666	0.65	22.29	C
ATOM	850	C	MET	A	51	0.440	47.780	−11.150	1.00	14.22	C
ATOM	851	O	MET	A	51	−0.516	48.340	−11.679	1.00	13.92	O
ATOM	852	N	TYR	A	52	1.568	47.499	−11.782	1.00	13.17	N
ATOM	854	CA	TYR	A	52	1.818	47.908	−13.159	1.00	13.42	C
ATOM	856	CB	TYR	A	52	2.991	48.887	−13.227	1.00	13.08	C
ATOM	859	CG	TYR	A	52	2.700	50.250	−12.644	1.00	13.49	C
ATOM	860	CD1	TYR	A	52	2.618	50.434	−11.278	1.00	13.31	C
ATOM	862	CE1	TYR	A	52	2.336	51.673	−10.734	1.00	11.89	C
ATOM	864	CZ	TYR	A	52	2.114	52.740	−11.574	1.00	13.12	C
ATOM	865	OH	TYR	A	52	1.820	53.970	−11.049	1.00	13.72	O
ATOM	867	CE2	TYR	A	52	2.206	52.580	−12.949	1.00	13.05	C
ATOM	869	CD2	TYR	A	52	2.485	51.351	−13.470	1.00	13.56	C
ATOM	871	C	TYR	A	52	2.138	46.726	−14.073	1.00	13.83	C
ATOM	872	O	TYR	A	52	2.813	45.794	−13.691	1.00	12.81	O
ATOM	873	N	LYS	A	53	1.606	46.775	−15.284	1.00	14.14	N
ATOM	875	CA	LYS	A	53	2.012	45.888	−16.327	1.00	14.63	C
ATOM	877	CB	LYS	A	53	1.015	45.980	−17.481	1.00	15.35	C
ATOM	880	CG	LYS	A	53	1.249	45.010	−18.641	1.00	17.12	C
ATOM	883	CD	LYS	A	53	0.183	45.252	−19.745	1.00	20.65	C
ATOM	886	CE	LYS	A	53	0.117	44.118	−20.741	1.00	23.88	C
ATOM	889	NZ	LYS	A	53	−0.805	44.414	−21.904	1.00	26.89	N
ATOM	893	C	LYS	A	53	3.370	46.409	−16.802	1.00	14.60	C
ATOM	894	O	LYS	A	53	3.528	47.608	−17.031	1.00	15.32	O
ATOM	895	N	ASP	A	54	4.327	45.505	−16.987	1.00	13.67	N
ATOM	897	CA	ASP	A	54	5.660	45.844	−17.389	1.00	13.60	C
ATOM	899	CB	ASP	A	54	6.586	45.322	−16.301	1.00	13.42	C
ATOM	902	CG	ASP	A	54	8.012	45.758	−16.450	1.00	13.39	C
ATOM	903	OD1	ASP	A	54	8.430	46.291	−17.496	1.00	11.84	O
ATOM	904	OD2	ASP	A	54	8.810	45.564	−15.494	1.00	12.26	O
ATOM	905	C	ASP	A	54	5.965	45.175	−18.720	1.00	13.35	C
ATOM	906	O	ASP	A	54	5.737	43.979	−18.883	1.00	12.28	O
ATOM	907	N	SER	A	55	6.488	45.946	−19.663	1.00	13.06	N
ATOM	909	CA	SER	A	55	6.871	45.407	−20.972	1.00	13.70	C
ATOM	911	CB	SER	A	55	7.161	46.546	−21.957	1.00	13.57	C
ATOM	914	OG	SER	A	55	8.241	47.346	−21.501	1.00	14.01	O
ATOM	916	C	SER	A	55	8.077	44.473	−20.899	1.00	14.21	C
ATOM	917	O	SER	A	55	8.327	43.730	−21.849	1.00	14.21	O
ATOM	918	N	GLN	A	56	8.811	44.520	−19.774	1.00	14.99	N
ATOM	920	CA	GLN	A	56	9.955	43.652	−19.499	1.00	15.58	C
ATOM	922	CB	GLN	A	56	11.228	44.475	−19.426	1.00	16.60	C
ATOM	925	CG	GLN	A	56	12.032	44.503	−20.712	1.00	21.81	C
ATOM	928	CD	GLN	A	56	13.223	45.462	−20.632	1.00	25.90	C
ATOM	929	OE1	GLN	A	56	13.952	45.472	−19.632	1.00	29.00	O
ATOM	930	NE2	GLN	A	56	13.385	46.295	−21.660	1.00	27.25	N
ATOM	933	C	GLN	A	56	9.762	42.947	−18.145	1.00	14.96	C
ATOM	934	O	GLN	A	56	10.292	43.378	−17.100	1.00	13.21	O
ATOM	935	N	PRO	A	57	8.975	41.886	−18.148	1.00	14.87	N
ATOM	936	CA	PRO	A	57	8.604	41.230	−16.897	1.00	14.94	C
ATOM	938	CB	PRO	A	57	7.687	40.101	−17.344	1.00	15.26	C
ATOM	941	CG	PRO	A	57	7.246	40.492	−18.701	1.00	15.17	C
ATOM	944	CD	PRO	A	57	8.347	41.253	−19.314	1.00	15.02	C
ATOM	947	C	PRO	A	57	9.791	40.716	−16.104	1.00	14.55	C
ATOM	948	O	PRO	A	57	10.569	39.897	−16.593	1.00	15.16	O
ATOM	949	N	ARG	A	58	9.916	41.208	−14.886	1.00	14.38	N
ATOM	951	CA	ARG	A	58	11.049	40.887	−13.989	1.00	14.78	C
ATOM	953	CB	ARG	A	58	11.992	42.094	−13.898	1.00	14.70	C
ATOM	956	CG	ARG	A	58	12.872	42.266	−15.132	1.00	15.88	C
ATOM	959	CD	ARG	A	58	13.405	43.701	−15.364	1.00	16.69	C
ATOM	962	NE	ARG	A	58	12.345	44.611	−15.778	1.00	16.02	N
ATOM	964	CZ	ARG	A	58	12.481	45.919	−15.872	1.00	14.64	C
ATOM	965	NH1	ARG	A	58	13.640	46.506	−15.574	1.00	13.09	N
ATOM	968	NH2	ARG	A	58	11.448	46.655	−16.227	1.00	14.67	N
ATOM	971	C	ARG	A	58	10.583	40.491	−12.584	1.00	15.27	C
ATOM	972	O	ARG	A	58	11.339	39.871	−11.826	1.00	15.40	O
ATOM	973	N	GLY	A	59	9.337	40.849	−12.260	1.00	15.27	N
ATOM	975	CA	GLY	A	59	8.726	40.598	−10.967	1.00	15.75	C
ATOM	978	C	GLY	A	59	7.481	41.472	−10.915	1.00	15.07	C
ATOM	979	O	GLY	A	59	7.238	42.193	−11.866	1.00	16.33	O
ATOM	980	N	MET	A	60	6.676	41.430	−9.860	1.00	14.19	N
ATOM	982	CA	MET	A	60	5.465	42.255	−9.869	1.00	13.82	C
ATOM	984	CB	MET	A	60	4.438	41.778	−8.854	1.00	14.80	C
ATOM	987	CG	MET	A	60	3.062	42.458	−9.063	1.00	16.06	C
ATOM	990	SD	MET	A	60	1.705	41.789	−8.055	1.00	22.71	S
ATOM	991	CE	MET	A	60	2.266	42.118	−6.460	1.00	21.67	C
ATOM	995	C	MET	A	60	5.800	43.733	−9.628	1.00	13.15	C
ATOM	996	O	MET	A	60	6.228	44.119	−8.540	1.00	11.40	O
ATOM	997	N	ALA	A	61	5.611	44.550	−10.657	1.00	12.27	N
ATOM	999	CA	ALA	A	61	5.946	45.978	−10.568	1.00	12.12	C
ATOM	1001	CB	ALA	A	61	6.105	46.548	−11.936	1.00	12.34	C
ATOM	1005	C	ALA	A	61	4.912	46.759	−9.786	1.00	11.69	C
ATOM	1006	O	ALA	A	61	3.730	46.743	−10.119	1.00	12.80	O
ATOM	1007	N	VAL	A	62	5.355	47.442	−8.743	1.00	11.59	N
ATOM	1009	CA	VAL	A	62	4.457	48.216	−7.909	1.00	10.97	C
ATOM	1011	CB	VAL	A	62	4.101	47.489	−6.601	1.00	10.99	C
ATOM	1013	CG1	VAL	A	62	3.420	46.138	−6.868	1.00	11.40	C
ATOM	1017	CG2	VAL	A	62	5.345	47.293	−5.711	1.00	11.11	C
ATOM	1021	C	VAL	A	62	5.045	49.527	−7.480	1.00	11.09	C
ATOM	1022	O	VAL	A	62	6.253	49.684	−7.435	1.00	10.73	O
ATOM	1023	N	THR	A	63	4.156	50.473	−7.177	1.00	11.51	N
ATOM	1025	CA	THR	A	63	4.528	51.692	−6.489	1.00	11.73	C
ATOM	1027	CB	THR	A	63	4.070	52.961	−7.236	1.00	12.36	C
ATOM	1029	OG1	THR	A	63	2.651	52.917	−7.436	1.00	10.48	O
ATOM	1031	CG2	THR	A	63	4.673	53.040	−8.603	1.00	11.83	C
ATOM	1035	C	THR	A	63	3.792	51.642	−5.152	1.00	12.38	C
ATOM	1036	O	THR	A	63	2.739	51.010	−5.034	1.00	12.60	O
ATOM	1037	N	ILE	A	64	4.345	52.328	−4.167	1.00	12.32	N
ATOM	1039	CA	ILE	A	64	3.781	52.380	−2.843	1.00	13.31	C
ATOM	1041	CB	ILE	A	64	4.742	51.754	−1.844	1.00	13.48	C
ATOM	1043	CG1	ILE	A	64	4.912	50.271	−2.133	1.00	14.30	C
ATOM	1046	CD1	ILE	A	64	6.089	49.643	−1.370	1.00	15.77	C
ATOM	1050	CG2	ILE	A	64	4.223	51.942	−0.437	1.00	15.38	C
ATOM	1054	C	ILE	A	64	3.557	53.836	−2.498	1.00	13.39	C
ATOM	1055	O	ILE	A	64	4.521	54.617	−2.404	1.00	13.39	O
ATOM	1056	N	SER	A	65	2.295	54.188	−2.290	1.00	14.03	N
ATOM	1058	CA	SER	A	65	1.895	55.560	−1.996	1.00	15.17	C
ATOM	1060	CB	SER	A	65	1.114	56.167	−3.180	1.00	14.68	C
ATOM	1063	OG	SER	A	65	1.783	55.984	−4.419	1.00	13.32	O
ATOM	1065	C	SER	A	65	1.061	55.674	−0.704	1.00	17.01	C
ATOM	1066	O	SER	A	65	0.544	54.663	−0.129	1.00	15.87	O
ATOM	1067	N	VAL	A	66	0.979	56.923	−0.241	1.00	19.37	N
ATOM	1069	CA	VAL	A	66	0.260	57.284	0.981	1.00	22.27	C
ATOM	1071	CB	VAL	A	66	1.175	57.628	2.159	1.00	22.39	C
ATOM	1073	CG1	AVAL	A	66	1.651	56.424	2.895	0.50	22.78	C
ATOM	1074	CG1	BVAL	A	66	0.554	56.963	3.366	0.50	22.35	C
ATOM	1081	CG2	AVAL	A	66	2.427	58.300	1.646	0.50	22.51	C
ATOM	1082	CG2	BVAL	A	66	2.559	57.082	1.990	0.50	23.29	C
ATOM	1089	C	VAL	A	66	−0.520	58.555	0.802	1.00	24.38	C
ATOM	1090	O	VAL	A	66	−0.009	59.513	0.227	1.00	24.82	O
ATOM	1091	N	LYS	A	67	−1.739	58.547	1.310	1.00	27.09	N
ATOM	1093	CA	LYS	A	67	−2.602	59.711	1.263	1.00	29.97	C
ATOM	1095	CB	LYS	A	67	−4.034	59.347	0.890	1.00	30.64	C
ATOM	1098	CG	LYS	A	67	−4.957	60.580	0.889	1.00	32.37	C
ATOM	1101	CD	LYS	A	67	−6.037	60.470	−0.187	1.00	34.82	C
ATOM	1104	CE	LYS	A	67	−6.613	61.848	−0.555	1.00	36.52	C
ATOM	1107	NZ	LYS	A	67	−7.719	61.705	−1.551	1.00	38.38	N
ATOM	1111	C	LYS	A	67	−2.642	60.443	2.591	1.00	31.87	C
ATOM	1112	O	LYS	A	67	−3.165	59.931	3.580	1.00	31.42	O
ATOM	1113	N	CYS	A	68	−2.049	61.630	2.609	1.00	34.05	N
ATOM	1115	CA	CYS	A	68	−2.145	62.515	3.757	1.00	35.95	C
ATOM	1117	CB	CYS	A	68	−0.777	63.070	4.139	1.00	36.35	C
ATOM	1120	SG	CYS	A	68	0.401	61.820	4.732	1.00	42.65	S
ATOM	1121	C	CYS	A	68	−3.095	63.597	3.257	1.00	35.69	C
ATOM	1122	O	CYS	A	68	−4.222	63.307	2.849	1.00	36.11	O
ATOM	1123	N	GLU	A	69	−2.651	64.840	3.246	1.00	35.99	N
ATOM	1125	CA	GLU	A	69	−3.469	65.883	2.655	1.00	35.80	C
ATOM	1127	CB	GLU	A	69	−2.783	67.240	2.774	1.00	36.43	C
ATOM	1130	CG	GLU	A	69	−3.624	68.392	2.242	1.00	37.99	C
ATOM	1133	CD	GLU	A	69	−2.977	69.746	2.479	0.50	39.45	C
ATOM	1134	OE1	GLU	A	69	−3.573	70.763	2.067	0.50	40.45	O
ATOM	1135	OE2	GLU	A	69	−1.878	69.794	3.076	0.50	41.24	O
ATOM	1136	C	GLU	A	69	−3.583	65.494	1.197	1.00	34.78	C
ATOM	1137	O	GLU	A	69	−4.668	65.399	0.630	1.00	35.20	O
ATOM	1138	N	LYS	A	70	−2.425	65.248	0.603	1.00	33.25	N
ATOM	1140	CA	LYS	A	70	−2.327	64.860	−0.795	1.00	31.85	C
ATOM	1142	CB	LYS	A	70	−1.452	65.863	−1.542	1.00	32.57	C
ATOM	1145	CG	LYS	A	70	−1.667	67.317	−1.129	1.00	35.54	C
ATOM	1148	CD	LYS	A	70	−2.766	67.951	−1.952	1.00	39.46	C
ATOM	1151	CE	LYS	A	70	−2.263	68.396	−3.324	1.00	41.73	C
ATOM	1154	NZ	LYS	A	70	−1.410	69.623	−3.249	1.00	44.57	N
ATOM	1158	C	LYS	A	70	−1.642	63.499	−0.844	1.00	29.20	C
ATOM	1159	O	LYS	A	70	−1.165	63.017	0.169	1.00	28.17	O
ATOM	1160	N	ILE	A	71	−1.562	62.912	−2.032	1.00	26.34	N
ATOM	1162	CA	ILE	A	71	−0.890	61.626	−2.197	1.00	24.51	C
ATOM	1164	CB	ILE	A	71	−1.541	60.822	−3.321	1.00	24.58	C
ATOM	1166	CG1	ILE	A	71	−2.990	60.475	−2.937	1.00	25.08	C
ATOM	1169	CD1	ILE	A	71	−3.836	59.945	−4.074	1.00	25.58	C
ATOM	1173	CG2	ILE	A	71	−0.731	59.562	−3.608	1.00	24.28	C
ATOM	1177	C	ILE	A	71	0.586	61.808	−2.496	1.00	23.04	C
ATOM	1178	O	ILE	A	71	0.980	62.620	−3.354	1.00	21.98	O
ATOM	1179	N	SER	A	72	1.400	61.060	−1.770	1.00	20.97	N
ATOM	1181	CA	SER	A	72	2.820	61.012	−2.013	1.00	20.47	C
ATOM	1183	CB	ASER	A	72	3.558	61.588	−0.814	0.50	20.49	C
ATOM	1184	CB	BSER	A	72	3.581	61.584	−0.825	0.50	20.51	C
ATOM	1189	OG	ASER	A	72	3.373	62.994	−0.777	0.50	22.61	O
ATOM	1190	OG	BSER	A	72	3.756	62.980	−0.997	0.50	22.76	O
ATOM	1193	C	SER	A	72	3.265	59.578	−2.293	1.00	18.71	C
ATOM	1194	O	SER	A	72	2.617	58.625	−1.872	1.00	18.18	O
ATOM	1195	N	THR	A	73	4.370	59.433	−3.007	1.00	17.03	N
ATOM	1197	CA	THR	A	73	4.832	58.125	−3.427	1.00	16.16	C
ATOM	1199	CB	THR	A	73	4.716	58.017	−4.951	1.00	15.82	C
ATOM	1201	OG1	THR	A	73	3.331	58.095	−5.342	1.00	13.69	O
ATOM	1203	CG2	THR	A	73	5.210	56.665	−5.449	1.00	15.20	C
ATOM	1207	C	THR	A	73	6.259	57.847	−3.005	1.00	16.42	C
ATOM	1208	O	THR	A	73	7.169	58.685	−3.169	1.00	15.32	O
ATOM	1209	N	LEU	A	74	6.458	56.641	−2.488	1.00	16.48	N
ATOM	1211	CA	LEU	A	74	7.755	56.208	−2.023	1.00	16.72	C
ATOM	1213	CB	LEU	A	74	7.613	54.842	−1.399	1.00	17.31	C
ATOM	1216	CG	LEU	A	74	8.845	54.309	−0.712	1.00	19.67	C
ATOM	1218	CD1	LEU	A	74	8.986	55.021	0.604	1.00	22.08	C
ATOM	1222	CD2	LEU	A	74	8.677	52.824	−0.507	1.00	23.17	C
ATOM	1226	C	LEU	A	74	8.757	56.146	−3.155	1.00	16.59	C
ATOM	1227	O	LEU	A	74	8.453	55.638	−4.230	1.00	15.98	O
ATOM	1228	N	SER	A	75	9.965	56.626	−2.883	1.00	16.71	N
ATOM	1230	CA	SER	A	75	11.020	56.701	−3.864	1.00	17.09	C
ATOM	1232	CB	SER	A	75	11.152	58.152	−4.359	1.00	17.22	C
ATOM	1235	OG	SER	A	75	12.363	58.340	−5.075	1.00	15.74	O
ATOM	1237	C	SER	A	75	12.354	56.275	−3.290	1.00	18.53	C
ATOM	1238	O	SER	A	75	12.638	56.491	−2.105	1.00	19.00	O
ATOM	1239	N	CYS	A	76	13.196	55.665	−4.100	1.00	19.50	N
ATOM	1241	CA	CYS	A	76	14.527	55.369	−3.594	1.00	21.42	C
ATOM	1243	CB	CYS	A	76	14.787	53.892	−3.555	1.00	21.92	C
ATOM	1246	SG	CYS	A	76	14.533	53.116	−5.113	1.00	26.94	S
ATOM	1247	C	CYS	A	76	15.631	56.111	−4.349	1.00	21.61	C
ATOM	1248	O	CYS	A	76	16.777	55.678	−4.398	1.00	21.33	O
ATOM	1249	N	GLU	A	77	15.280	57.257	−4.910	1.00	22.66	N
ATOM	1251	CA	GLU	A	77	16.255	58.060	−5.618	1.00	23.70	C
ATOM	1253	CB	GLU	A	77	15.678	59.418	−5.978	1.00	24.40	C
ATOM	1256	CG	GLU	A	77	16.667	60.248	−6.796	1.00	27.41	C
ATOM	1259	CD	GLU	A	77	16.161	61.617	−7.190	1.00	30.89	C
ATOM	1260	OE1	GLU	A	77	16.844	62.266	−8.022	1.00	35.70	O
ATOM	1261	OE2	GLU	A	77	15.105	62.051	−6.689	1.00	33.74	O
ATOM	1262	C	GLU	A	77	17.498	58.261	−4.752	1.00	23.98	C
ATOM	1263	O	GLU	A	77	17.391	58.482	−3.542	1.00	22.55	O
ATOM	1264	N	ASN	A	78	18.666	58.162	−5.386	1.00	24.68	N
ATOM	1266	CA	ASN	A	78	19.950	58.344	−4.722	1.00	25.56	C
ATOM	1268	CB	ASN	A	78	20.070	59.764	−4.153	1.00	26.17	C
ATOM	1271	CG	ASN	A	78	20.049	60.832	−5.243	1.00	28.42	C
ATOM	1272	OD1	ASN	A	78	19.688	61.980	−4.992	1.00	33.38	O
ATOM	1273	ND2	ASN	A	78	20.418	60.450	−6.460	1.00	30.26	N
ATOM	1276	C	ASN	A	78	20.165	57.304	−3.637	1.00	25.79	C
ATOM	1277	O	ASN	A	78	20.868	57.549	−2.664	1.00	25.20	O
ATOM	1278	N	LYS	A	79	19.549	56.139	−3.832	1.00	26.08	N
ATOM	1280	CA	LYS	A	79	19.638	55.018	−2.915	1.00	26.95	C
ATOM	1282	CB	LYS	A	79	21.065	54.437	−2.891	1.00	27.51	C
ATOM	1285	CG	LYS	A	79	21.557	53.889	−4.238	1.00	29.89	C
ATOM	1288	CD	LYS	A	79	22.986	53.341	−4.137	1.00	32.67	C
ATOM	1291	CE	LYS	A	79	23.482	52.764	−5.455	1.00	34.42	C
ATOM	1294	NZ	LYS	A	79	24.788	52.032	−5.321	1.00	35.62	N
ATOM	1298	C	LYS	A	79	19.184	55.368	−1.500	1.00	26.68	C
ATOM	1299	O	LYS	A	79	19.651	54.793	−0.554	1.00	26.91	O
ATOM	1300	N	ILE	A	80	18.279	56.313	−1.359	1.00	27.19	N
ATOM	1302	CA	ILE	A	80	17.770	56.677	−0.052	1.00	28.15	C
ATOM	1304	CB	ILE	A	80	18.224	58.089	0.330	1.00	28.96	C
ATOM	1306	CG1	ILE	A	80	17.751	58.436	1.720	1.00	31.62	C
ATOM	1309	CD1	ILE	A	80	18.388	59.696	2.208	1.00	34.47	C
ATOM	1313	CG2	ILE	A	80	17.599	59.113	−0.542	1.00	30.48	C
ATOM	1317	C	ILE	A	80	16.262	56.661	−0.118	1.00	27.36	C
ATOM	1318	O	ILE	A	80	15.698	56.961	−1.164	1.00	26.85	O
ATOM	1319	N	ILE	A	81	15.619	56.316	0.987	1.00	26.61	N
ATOM	1321	CA	ILE	A	81	14.167	56.358	1.044	1.00	26.49	C
ATOM	1323	CB	ILE	A	81	13.660	55.473	2.187	1.00	26.75	C
ATOM	1325	CG1	ILE	A	81	14.009	54.011	1.927	1.00	27.58	C
ATOM	1328	CD1	ILE	A	81	13.408	53.480	0.678	1.00	29.35	C
ATOM	1332	CG2	ILE	A	81	12.164	55.638	2.330	1.00	27.41	C
ATOM	1336	C	ILE	A	81	13.612	57.751	1.278	1.00	25.97	C
ATOM	1337	O	ILE	A	81	14.008	58.440	2.208	1.00	25.07	O
ATOM	1338	N	SER	A	82	12.645	58.151	0.461	1.00	25.49	N
ATOM	1340	CA	SER	A	82	11.967	59.416	0.654	1.00	25.49	C
ATOM	1342	CB	SER	A	82	12.760	60.528	−0.033	1.00	25.97	C
ATOM	1345	OG	SER	A	82	12.788	60.309	−1.451	1.00	25.78	O
ATOM	1347	C	SER	A	82	10.599	59.314	−0.004	1.00	25.52	C
ATOM	1348	O	SER	A	82	10.288	58.304	−0.646	1.00	24.44	O
ATOM	1349	N	PHE	A	83	9.784	60.348	0.155	1.00	25.53	N
ATOM	1351	CA	PHE	A	83	8.516	60.407	−0.543	1.00	26.14	C
ATOM	1353	CB	PHE	A	83	7.396	60.678	0.420	1.00	26.66	C
ATOM	1356	CG	PHE	A	83	6.986	59.472	1.166	1.00	27.86	C
ATOM	1357	CD1	PHE	A	83	7.569	59.171	2.380	1.00	30.53	C
ATOM	1359	CE1	PHE	A	83	7.213	58.035	3.058	1.00	30.18	C
ATOM	1361	CZ	PHE	A	83	6.281	57.192	2.521	1.00	30.58	C
ATOM	1363	CE2	PHE	A	83	5.704	57.485	1.309	1.00	29.81	C
ATOM	1365	CD2	PHE	A	83	6.058	58.604	0.638	1.00	29.19	C
ATOM	1367	C	PHE	A	83	8.507	61.464	−1.625	1.00	26.10	C
ATOM	1368	O	PHE	A	83	8.831	62.619	−1.376	1.00	27.01	O
ATOM	1369	N	LYS	A	84	8.171	61.060	−2.839	1.00	25.29	N
ATOM	1371	CA	LYS	A	84	8.028	62.003	−3.936	1.00	25.20	C
ATOM	1373	CB	LYS	A	84	8.220	61.299	−5.281	1.00	25.91	C
ATOM	1376	CG	LYS	A	84	9.461	61.685	−6.053	1.00	28.54	C
ATOM	1379	CD	LYS	A	84	9.249	61.534	−7.571	1.00	31.41	C
ATOM	1382	CE	LYS	A	84	10.361	62.265	−8.363	1.00	34.15	C
ATOM	1385	NZ	LYS	A	84	10.094	62.387	−9.800	1.00	32.15	N
ATOM	1389	C	LYS	A	84	6.618	62.578	−3.836	1.00	24.05	C
ATOM	1390	O	LYS	A	84	5.665	61.836	−3.581	1.00	22.96	O
ATOM	1391	N	GLU	A	85	6.481	63.884	−4.051	1.00	23.01	N
ATOM	1393	CA	GLU	A	85	5.185	64.550	−3.981	1.00	22.72	C
ATOM	1395	CB	GLU	A	85	5.354	66.047	−3.705	1.00	23.58	C
ATOM	1398	CG	GLU	A	85	6.046	66.346	−2.389	1.00	27.04	C
ATOM	1401	CD	GLU	A	85	5.170	66.090	−1.183	1.00	31.68	C
ATOM	1402	OE1	GLU	A	85	5.730	65.709	−0.132	1.00	38.63	O
ATOM	1403	OE2	GLU	A	85	3.929	66.263	−1.262	1.00	35.20	O
ATOM	1404	C	GLU	A	85	4.430	64.344	−5.281	1.00	21.30	C
ATOM	1405	O	GLU	A	85	4.342	65.241	−6.122	1.00	20.65	O
ATOM	1406	N	MET	A	86	3.888	63.148	−5.447	1.00	19.77	N
ATOM	1408	CA	MET	A	86	3.207	62.792	−6.677	1.00	19.20	C
ATOM	1410	CB	MET	A	86	4.220	62.395	−7.757	1.00	19.02	C
ATOM	1413	CG	MET	A	86	4.969	61.093	−7.477	1.00	19.07	C
ATOM	1416	SD	MET	A	86	6.203	60.635	−8.742	1.00	19.48	S
ATOM	1417	CE	MET	A	86	5.127	60.071	−9.966	1.00	20.83	C
ATOM	1421	C	MET	A	86	2.270	61.614	−6.456	1.00	18.53	C
ATOM	1422	O	MET	A	86	2.508	60.780	−5.579	1.00	17.44	O
ATOM	1423	N	ASN	A	87	1.205	61.593	−7.253	1.00	18.15	N
ATOM	1425	CA	ASN	A	87	0.309	60.464	−7.344	1.00	17.91	C
ATOM	1427	CB	ASN	A	87	−0.961	60.840	−8.130	1.00	18.22	C
ATOM	1430	CG	ASN	A	87	−1.787	61.927	−7.453	1.00	19.32	C
ATOM	1431	OD1	ASN	A	87	−1.529	62.311	−6.312	1.00	21.74	O
ATOM	1432	ND2	ASN	A	87	−2.772	62.441	−8.170	1.00	20.57	N
ATOM	1435	C	ASN	A	87	1.040	59.380	−8.135	1.00	17.63	C
ATOM	1436	O	ASN	A	87	1.931	59.669	−8.920	1.00	17.03	O
ATOM	1437	N	PRO	A	88	0.656	58.131	−7.944	1.00	17.44	N
ATOM	1438	CA	PRO	A	88	1.208	57.053	−8.751	1.00	17.30	C
ATOM	1440	CB	PRO	A	88	0.520	55.801	−8.214	1.00	17.52	C
ATOM	1443	CG	PRO	A	88	−0.272	56.205	−7.082	1.00	18.64	C
ATOM	1446	CD	PRO	A	88	−0.366	57.670	−6.998	1.00	17.66	C
ATOM	1449	C	PRO	A	88	0.754	57.323	−10.186	1.00	16.55	C
ATOM	1450	O	PRO	A	88	−0.418	57.560	−10.386	1.00	16.30	O
ATOM	1451	N	PRO	A	89	1.656	57.290	−11.156	1.00	16.34	N
ATOM	1452	CA	PRO	A	89	1.322	57.661	−12.534	1.00	16.31	C
ATOM	1454	CB	PRO	A	89	2.690	57.900	−13.158	1.00	16.34	C
ATOM	1457	CG	PRO	A	89	3.613	56.984	−12.418	1.00	16.09	C
ATOM	1460	CD	PRO	A	89	3.068	56.908	−11.006	1.00	15.95	C
ATOM	1463	C	PRO	A	89	0.594	56.578	−13.320	1.00	16.81	C
ATOM	1464	O	PRO	A	89	0.684	55.401	−12.971	1.00	16.72	O
ATOM	1465	N	ASP	A	90	−0.104	56.970	−14.382	1.00	16.66	N
ATOM	1467	CA	ASP	A	90	−0.786	55.993	−15.228	1.00	16.97	C
ATOM	1469	CB	ASP	A	90	−1.794	56.650	−16.146	1.00	17.34	C
ATOM	1472	CG	ASP	A	90	−2.910	57.279	−15.396	1.00	19.82	C
ATOM	1473	OD1	ASP	A	90	−3.399	56.719	−14.391	1.00	23.87	O
ATOM	1474	OD2	ASP	A	90	−3.364	58.356	−15.751	1.00	24.07	O
ATOM	1475	C	ASP	A	90	0.177	55.247	−16.085	1.00	16.16	C
ATOM	1476	O	ASP	A	90	−0.050	54.103	−16.356	1.00	15.59	O
ATOM	1477	N	ASN	A	91	1.239	55.903	−16.521	1.00	16.99	N
ATOM	1479	CA	ASN	A	91	2.219	55.277	−17.396	1.00	17.75	C
ATOM	1481	CB	ASN	A	91	1.943	55.637	−18.861	1.00	18.43	C
ATOM	1484	CG	ASN	A	91	0.623	55.090	−19.349	1.00	20.34	C
ATOM	1485	OD1	ASN	A	91	0.507	53.899	−19.642	1.00	21.93	O
ATOM	1486	ND2	ASN	A	91	−0.392	55.946	−19.402	1.00	20.01	N
ATOM	1489	C	ASN	A	91	3.597	55.744	−17.052	1.00	18.08	C
ATOM	1490	O	ASN	A	91	3.754	56.894	−16.650	1.00	18.65	O
ATOM	1491	N	ILE	A	92	4.593	54.882	−17.237	1.00	17.65	N
ATOM	1493	CA	ILE	A	92	5.991	55.236	−17.022	1.00	17.66	C
ATOM	1495	CB	ILE	A	92	6.547	54.583	−15.744	1.00	17.40	C
ATOM	1497	CG1	ILE	A	92	5.853	55.134	−14.506	1.00	16.97	C
ATOM	1500	CD1	ILE	A	92	6.186	54.375	−13.204	1.00	16.36	C
ATOM	1504	CG2	ILE	A	92	8.031	54.791	−15.643	1.00	17.36	C
ATOM	1508	C	ILE	A	92	6.728	54.729	−18.245	1.00	18.49	C
ATOM	1509	O	ILE	A	92	6.680	53.535	−18.557	1.00	17.20	O
ATOM	1510	N	LYS	A	93	7.401	55.638	−18.943	1.00	19.65	N
ATOM	1512	CA	LYS	A	93	8.048	55.309	−20.214	1.00	21.53	C
ATOM	1514	CB	LYS	A	93	8.331	56.599	−21.012	1.00	22.25	C
ATOM	1517	CG	LYS	A	93	7.081	57.281	−21.541	1.00	26.39	C
ATOM	1520	CD	LYS	A	93	7.411	58.593	−22.282	1.00	30.93	C
ATOM	1523	CE	LYS	A	93	6.140	59.348	−22.682	1.00	33.76	C
ATOM	1526	NZ	LYS	A	93	6.438	60.689	−23.279	1.00	37.26	N
ATOM	1530	C	LYS	A	93	9.337	54.478	−20.119	1.00	20.78	C
ATOM	1531	O	LYS	A	93	9.603	53.679	−21.000	1.00	21.45	O
ATOM	1532	N	ASP	A	94	10.143	54.660	−19.085	1.00	20.83	N
ATOM	1534	CA	ASP	A	94	11.408	53.916	−18.992	1.00	21.01	C
ATOM	1536	CB	ASP	A	94	12.419	54.672	−18.113	1.00	22.05	C
ATOM	1539	CG	ASP	A	94	13.870	54.247	−18.385	1.00	26.32	C
ATOM	1540	OD1	ASP	A	94	14.167	53.837	−19.535	1.00	30.63	O
ATOM	1541	OD2	ASP	A	94	14.779	54.261	−17.516	1.00	33.43	O
ATOM	1542	C	ASP	A	94	11.193	52.501	−18.439	1.00	19.94	C
ATOM	1543	O	ASP	A	94	10.089	52.161	−18.016	1.00	18.21	O
ATOM	1544	N	THR	A	95	12.252	51.692	−18.449	1.00	19.38	N
ATOM	1546	CA	THR	A	95	12.204	50.335	−17.914	1.00	19.69	C
ATOM	1548	CB	THR	A	95	13.134	49.398	−18.670	1.00	19.65	C
ATOM	1550	OG1	THR	A	95	14.452	49.951	−18.684	1.00	19.63	O
ATOM	1552	CG2	THR	A	95	12.754	49.261	−20.128	1.00	20.76	C
ATOM	1556	C	THR	A	95	12.620	50.276	−16.452	1.00	19.43	C
ATOM	1557	O	THR	A	95	12.561	49.215	−15.855	1.00	19.07	O
ATOM	1558	N	LYS	A	96	13.085	51.396	−15.907	1.00	19.31	N
ATOM	1560	CA	LYS	A	96	13.451	51.497	−14.504	1.00	19.73	C
ATOM	1562	CB	LYS	A	96	14.962	51.493	−14.337	1.00	20.55	C
ATOM	1565	CG	LYS	A	96	15.645	50.230	−14.804	1.00	24.38	C
ATOM	1568	CD	LYS	A	96	17.157	50.457	−14.852	1.00	29.05	C
ATOM	1571	CE	LYS	A	96	17.911	49.261	−15.397	1.00	32.09	C
ATOM	1574	NZ	LYS	A	96	17.856	48.101	−14.448	1.00	35.50	N
ATOM	1578	C	LYS	A	96	12.896	52.808	−13.963	1.00	18.61	C
ATOM	1579	O	LYS	A	96	12.733	53.777	−14.710	1.00	18.81	O
ATOM	1580	N	SER	A	97	12.624	52.852	−12.669	1.00	17.12	N
ATOM	1582	CA	SER	A	97	12.101	54.061	−12.056	1.00	16.69	C
ATOM	1584	CB	SER	A	97	10.606	54.179	−12.308	1.00	16.53	C
ATOM	1587	OG	SER	A	97	10.035	55.180	−11.490	1.00	15.88	O
ATOM	1589	C	SER	A	97	12.343	54.056	−10.561	1.00	16.60	C
ATOM	1590	O	SER	A	97	12.147	53.019	−9.898	1.00	15.71	O
ATOM	1591	N	ASP	A	98	12.745	55.213	−10.033	1.00	16.12	N
ATOM	1593	CA	ASP	A	98	12.958	55.385	−8.599	1.00	16.77	C
ATOM	1595	CB	ASP	A	98	13.420	56.810	−8.288	1.00	17.52	C
ATOM	1598	CG	ASP	A	98	14.836	57.100	−8.780	1.00	20.61	C
ATOM	1599	OD1	ASP	A	98	15.595	56.159	−9.082	1.00	23.09	O
ATOM	1600	OD2	ASP	A	98	15.267	58.264	−8.903	1.00	26.80	O
ATOM	1601	C	ASP	A	98	11.707	55.073	−7.745	1.00	15.80	C
ATOM	1602	O	ASP	A	98	11.835	54.865	−6.543	1.00	16.33	O
ATOM	1603	N	ILE	A	99	10.516	55.055	−8.347	1.00	14.68	N
ATOM	1605	CA	ILE	A	99	9.285	54.718	−7.608	1.00	13.94	C
ATOM	1607	CB	ILE	A	99	8.184	55.748	−7.843	1.00	13.90	C
ATOM	1609	CG1	ILE	A	99	7.784	55.789	−9.314	1.00	15.06	C
ATOM	1612	CD1	ILE	A	99	6.509	56.521	−9.523	1.00	16.61	C
ATOM	1616	CG2	ILE	A	99	8.611	57.133	−7.322	1.00	13.31	C
ATOM	1620	C	ILE	A	99	8.740	53.306	−7.900	1.00	13.36	C
ATOM	1621	O	ILE	A	99	7.748	52.872	−7.321	1.00	12.61	O
ATOM	1622	N	ILE	A	100	9.398	52.562	−8.766	1.00	12.80	N
ATOM	1624	CA	ILE	A	100	8.914	51.229	−9.058	1.00	12.44	C
ATOM	1626	CB	ILE	A	100	8.900	50.948	−10.574	1.00	12.60	C
ATOM	1628	CG1	ILE	A	100	7.762	51.701	−11.254	1.00	12.35	C
ATOM	1631	CD1	ILE	A	100	6.408	51.100	−10.984	1.00	13.67	C
ATOM	1635	CG2	ILE	A	100	8.795	49.424	−10.850	1.00	12.45	C
ATOM	1639	C	ILE	A	100	9.791	50.215	−8.364	1.00	12.45	C
ATOM	1640	O	ILE	A	100	11.016	50.256	−8.487	1.00	12.10	O
ATOM	1641	N	PHE	A	101	9.145	49.322	−7.625	1.00	12.17	N
ATOM	1643	CA	PHE	A	101	9.812	48.163	−7.017	1.00	12.36	C
ATOM	1645	CB	PHE	A	101	9.500	48.115	−5.534	1.00	12.44	C
ATOM	1648	CG	PHE	A	101	10.006	49.293	−4.797	1.00	13.57	C
ATOM	1649	CD1	PHE	A	101	9.281	50.467	−4.768	1.00	15.70	C
ATOM	1651	CE1	PHE	A	101	9.783	51.592	−4.109	1.00	16.59	C
ATOM	1653	CZ	PHE	A	101	11.001	51.523	−3.481	1.00	15.46	C
ATOM	1655	CE2	PHE	A	101	11.741	50.349	−3.530	1.00	14.93	C
ATOM	1657	CD2	PHE	A	101	11.249	49.255	−4.189	1.00	15.36	C
ATOM	1659	C	PHE	A	101	9.267	46.894	−7.620	1.00	12.29	C
ATOM	1660	O	PHE	A	101	8.111	46.876	−8.051	1.00	13.32	O
ATOM	1661	N	PHE	A	102	10.074	45.836	−7.637	1.00	12.07	N
ATOM	1663	CA	PHE	A	102	9.614	44.514	−8.048	1.00	11.87	C
ATOM	1665	CB	PHE	A	102	10.650	43.789	−8.904	1.00	12.23	C
ATOM	1668	CG	PHE	A	102	10.994	44.513	−10.170	1.00	12.55	C
ATOM	1669	CD1	PHE	A	102	10.010	44.844	−11.074	1.00	12.71	C
ATOM	1671	CE1	PHE	A	102	10.310	45.534	−12.251	1.00	12.56	C
ATOM	1673	CZ	PHE	A	102	11.603	45.883	−12.526	1.00	12.26	C
ATOM	1675	CE2	PHE	A	102	12.608	45.569	−11.628	1.00	13.73	C
ATOM	1677	CD2	PHE	A	102	12.298	44.881	−10.444	1.00	13.67	C
ATOM	1679	C	PHE	A	102	9.322	43.692	−6.804	1.00	12.04	C
ATOM	1680	O	PHE	A	102	10.238	43.372	−6.008	1.00	10.74	O
ATOM	1681	N	GLN	A	103	8.040	43.379	−6.634	1.00	12.14	N
ATOM	1683	CA	GLN	A	103	7.569	42.594	−5.498	1.00	12.54	C
ATOM	1685	CB	GLN	A	103	6.150	43.027	−5.067	1.00	12.77	C
ATOM	1688	CG	GLN	A	103	5.586	42.242	−3.874	1.00	13.09	C
ATOM	1691	CD	GLN	A	103	4.110	42.519	−3.613	1.00	15.81	C
ATOM	1692	OE1	GLN	A	103	3.644	43.636	−3.842	1.00	14.73	O
ATOM	1693	NE2	GLN	A	103	3.380	41.509	−3.117	1.00	12.31	N
ATOM	1696	C	GLN	A	103	7.558	41.129	−5.904	1.00	12.68	C
ATOM	1697	O	GLN	A	103	6.936	40.759	−6.924	1.00	11.91	O
ATOM	1698	N	ARG	A	104	8.246	40.309	−5.115	1.00	12.59	N
ATOM	1700	CA	ARG	A	104	8.312	38.882	−5.356	1.00	12.69	C
ATOM	1702	CB	ARG	A	104	9.641	38.520	−5.995	1.00	13.11	C
ATOM	1705	CG	ARG	A	104	9.971	39.273	−7.249	1.00	12.76	C
ATOM	1708	CD	ARG	A	104	11.322	38.865	−7.780	1.00	13.77	C
ATOM	1711	NE	ARG	A	104	11.823	39.587	−8.948	1.00	12.44	N
ATOM	1713	CZ	ARG	A	104	12.619	40.640	−8.900	1.00	14.71	C
ATOM	1714	NH1	ARG	A	104	12.980	41.176	−7.737	1.00	15.15	N
ATOM	1717	NH2	ARG	A	104	13.068	41.168	−10.027	1.00	16.82	N
ATOM	1720	C	ARG	A	104	8.208	38.127	−4.034	1.00	13.39	C
ATOM	1721	O	ARG	A	104	8.637	38.623	−2.994	1.00	12.61	O
ATOM	1722	N	SER	A	105	7.655	36.922	−4.084	1.00	13.60	N
ATOM	1724	CA	SER	A	105	7.547	36.095	−2.888	1.00	14.97	C
ATOM	1726	CB	SER	A	105	6.381	35.125	−3.024	1.00	14.57	C
ATOM	1729	OG	SER	A	105	6.630	34.230	−4.085	1.00	19.33	O
ATOM	1731	C	SER	A	105	8.864	35.346	−2.630	1.00	15.36	C
ATOM	1732	O	SER	A	105	9.699	35.198	−3.532	1.00	14.86	O
ATOM	1733	N	VAL	A	106	9.027	34.905	−1.385	1.00	15.75	N
ATOM	1735	CA	VAL	A	106	10.179	34.148	−0.919	1.00	16.79	C
ATOM	1737	CB	VAL	A	106	10.325	34.302	0.612	1.00	16.88	C
ATOM	1739	CG1	VAL	A	106	11.369	33.302	1.212	1.00	18.13	C
ATOM	1743	CG2	VAL	A	106	10.739	35.725	0.967	1.00	17.82	C
ATOM	1747	C	VAL	A	106	9.967	32.661	−1.261	1.00	17.26	C
ATOM	1748	O	VAL	A	106	8.890	32.128	−1.014	1.00	16.36	O
ATOM	1749	N	PRO	A	107	10.989	31.991	−1.787	1.00	18.48	N
ATOM	1750	CA	PRO	A	107	10.880	30.569	−2.122	1.00	19.71	C
ATOM	1752	CB	PRO	A	107	12.324	30.167	−2.458	1.00	20.21	C
ATOM	1755	CG	PRO	A	107	13.024	31.427	−2.795	1.00	20.09	C
ATOM	1758	CD	PRO	A	107	12.340	32.513	−2.039	1.00	19.23	C
ATOM	1761	C	PRO	A	107	10.362	29.762	−0.934	1.00	20.35	C
ATOM	1762	O	PRO	A	107	10.827	29.941	0.180	1.00	20.97	O
ATOM	1763	N	GLY	A	108	9.358	28.937	−1.156	1.00	21.08	N
ATOM	1765	CA	GLY	A	108	8.796	28.126	−0.093	1.00	21.86	C
ATOM	1768	C	GLY	A	108	7.875	28.915	0.824	1.00	22.31	C
ATOM	1769	O	GLY	A	108	7.304	28.362	1.768	1.00	22.33	O
ATOM	1770	N	HIS	A	109	7.726	30.215	0.581	1.00	21.77	N
ATOM	1772	CA	HIS	A	109	6.893	31.023	1.473	1.00	22.02	C
ATOM	1774	CB	HIS	A	109	7.775	31.695	2.523	1.00	22.31	C
ATOM	1777	CG	HIS	A	109	8.517	30.730	3.395	1.00	25.08	C
ATOM	1778	ND1	HIS	A	109	7.907	30.025	4.410	1.00	27.83	N
ATOM	1780	CE1	HIS	A	109	8.797	29.242	4.996	1.00	28.02	C
ATOM	1782	NE2	HIS	A	109	9.962	29.417	4.401	1.00	27.77	N
ATOM	1784	CD2	HIS	A	109	9.813	30.336	3.389	1.00	27.14	C
ATOM	1786	C	HIS	A	109	6.149	32.096	0.682	1.00	21.47	C
ATOM	1787	O	HIS	A	109	6.548	33.248	0.656	1.00	21.06	O
ATOM	1788	N	ASP	A	110	5.050	31.687	0.079	1.00	20.80	N
ATOM	1790	CA	ASP	A	110	4.313	32.526	−0.862	1.00	20.89	C
ATOM	1792	CB	ASP	A	110	3.156	31.734	−1.471	1.00	20.71	C
ATOM	1795	CG	ASP	A	110	3.628	30.630	−2.420	1.00	21.84	C
ATOM	1796	OD1	ASP	A	110	4.833	30.566	−2.752	1.00	21.04	O
ATOM	1797	OD2	ASP	A	110	2.851	29.779	−2.895	1.00	24.11	O
ATOM	1798	C	ASP	A	110	3.793	33.844	−0.286	1.00	20.30	C
ATOM	1799	O	ASP	A	110	3.680	34.824	−1.002	1.00	20.42	O
ATOM	1800	N	ASN	A	111	3.502	33.868	0.997	1.00	19.82	N
ATOM	1802	CA	ASN	A	111	2.993	35.067	1.631	1.00	20.23	C
ATOM	1804	CB	ASN	A	111	2.242	34.648	2.881	1.00	21.26	C
ATOM	1807	CG	ASN	A	111	3.125	33.856	3.828	1.00	25.09	C
ATOM	1808	OD1	ASN	A	111	3.862	32.934	3.401	1.00	29.93	O
ATOM	1809	ND2	ASN	A	111	3.073	34.203	5.117	1.00	30.79	N
ATOM	1812	C	ASN	A	111	4.071	36.062	2.056	1.00	19.06	C
ATOM	1813	O	ASN	A	111	3.765	37.179	2.460	1.00	18.64	O
ATOM	1814	N	LYS	A	112	5.325	35.647	2.025	1.00	17.77	N
ATOM	1816	CA	LYS	A	112	6.400	36.535	2.415	1.00	17.52	C
ATOM	1818	CB	LYS	A	112	7.486	35.767	3.147	1.00	18.06	C
ATOM	1821	CG	LYS	A	112	6.995	35.139	4.476	1.00	20.76	C
ATOM	1824	CD	LYS	A	112	8.137	34.434	5.175	1.00	26.65	C
ATOM	1827	CE	LYS	A	112	7.791	34.031	6.621	1.00	30.48	C
ATOM	1830	NZ	LYS	A	112	8.979	33.389	7.293	1.00	32.51	N
ATOM	1834	C	LYS	A	112	6.949	37.208	1.164	1.00	16.43	C
ATOM	1835	O	LYS	A	112	7.365	36.528	0.211	1.00	16.35	O
ATOM	1836	N	MET	A	113	6.948	38.528	1.186	1.00	15.04	N
ATOM	1838	CA	MET	A	113	7.370	39.344	0.053	1.00	14.21	C
ATOM	1840	CB	MET	A	113	6.189	40.262	−0.305	1.00	13.98	C
ATOM	1843	CG	MET	A	113	4.922	39.491	−0.557	1.00	13.92	C
ATOM	1846	SD	MET	A	113	4.959	38.666	−2.121	1.00	13.76	S
ATOM	1847	CE	MET	A	113	3.272	37.917	−2.118	1.00	16.42	C
ATOM	1851	C	MET	A	113	8.621	40.218	0.248	1.00	13.87	C
ATOM	1852	O	MET	A	113	8.915	40.713	1.356	1.00	14.54	O
ATOM	1853	N	GLN	A	114	9.360	40.416	−0.849	1.00	13.03	N
ATOM	1855	CA	GLN	A	114	10.529	41.289	−0.867	1.00	13.01	C
ATOM	1857	CB	GLN	A	114	11.823	40.493	−1.094	1.00	12.49	C
ATOM	1860	CG	GLN	A	114	12.016	39.398	−0.064	1.00	13.98	C
ATOM	1863	CD	GLN	A	114	13.271	38.583	−0.249	1.00	12.98	C
ATOM	1864	OE1	GLN	A	114	13.707	38.380	−1.368	1.00	16.00	O
ATOM	1865	NE2	GLN	A	114	13.836	38.081	0.865	1.00	13.37	N
ATOM	1868	C	GLN	A	114	10.319	42.283	−2.007	1.00	12.07	C
ATOM	1869	O	GLN	A	114	9.772	41.923	−3.052	1.00	12.02	O
ATOM	1870	N	PHE	A	115	10.792	43.501	−1.806	1.00	11.94	N
ATOM	1872	CA	PHE	A	115	10.632	44.605	−2.755	1.00	11.72	C
ATOM	1874	CB	PHE	A	115	9.881	45.780	−2.108	1.00	11.68	C
ATOM	1877	CG	PHE	A	115	8.477	45.457	−1.659	1.00	11.29	C
ATOM	1878	CD1	PHE	A	115	8.228	45.040	−0.373	1.00	13.40	C
ATOM	1880	CE1	PHE	A	115	6.930	44.747	0.052	1.00	13.23	C
ATOM	1882	CZ	PHE	A	115	5.863	44.889	−0.838	1.00	11.77	C
ATOM	1884	CE2	PHE	A	115	6.109	45.310	−2.115	1.00	11.16	C
ATOM	1886	CD2	PHE	A	115	7.407	45.593	−2.527	1.00	10.60	C
ATOM	1888	C	PHE	A	115	12.004	45.086	−3.183	1.00	11.91	C
ATOM	1889	O	PHE	A	115	12.724	45.735	−2.400	1.00	11.30	O
ATOM	1890	N	GLU	A	116	12.366	44.761	−4.420	1.00	12.11	N
ATOM	1892	CA	GLU	A	116	13.645	45.155	−4.978	1.00	12.59	C
ATOM	1894	CB	GLU	A	116	14.211	44.048	−5.855	1.00	12.65	C
ATOM	1897	CG	GLU	A	116	15.623	44.359	−6.297	1.00	13.88	C
ATOM	1900	CD	GLU	A	116	16.307	43.210	−6.996	1.00	17.12	C
ATOM	1901	OE1	GLU	A	116	15.651	42.174	−7.263	1.00	16.35	O
ATOM	1902	OE2	GLU	A	116	17.516	43.370	−7.278	1.00	18.56	O
ATOM	1903	C	GLU	A	116	13.509	46.436	−5.806	1.00	12.91	C
ATOM	1904	O	GLU	A	116	12.596	46.556	−6.614	1.00	12.73	O
ATOM	1905	N	SER	A	117	14.408	47.393	−5.592	1.00	13.50	N
ATOM	1907	CA	SER	A	117	14.411	48.620	−6.384	1.00	14.35	C
ATOM	1909	CB	SER	A	117	15.515	49.569	−5.892	1.00	15.10	C
ATOM	1912	OG	SER	A	117	15.714	50.667	−6.788	1.00	14.74	O
ATOM	1914	C	SER	A	117	14.631	48.296	−7.867	1.00	14.72	C
ATOM	1915	O	SER	A	117	15.538	47.538	−8.208	1.00	15.22	O
ATOM	1916	N	SER	A	118	13.778	48.830	−8.740	1.00	15.09	N
ATOM	1918	CA	SER	A	118	13.978	48.678	−10.171	1.00	14.99	C
ATOM	1920	CB	SER	A	118	12.705	49.022	−10.946	1.00	15.09	C
ATOM	1923	OG	SER	A	118	12.451	50.426	−11.012	1.00	11.74	O
ATOM	1925	C	SER	A	118	15.136	49.578	−10.636	1.00	16.66	C
ATOM	1926	O	SER	A	118	15.805	49.276	−11.606	1.00	16.60	O
ATOM	1927	N	SER	A	119	15.344	50.706	−9.960	1.00	17.88	N
ATOM	1929	CA	SER	A	119	16.457	51.595	−10.288	1.00	19.19	C
ATOM	1931	CB	SER	A	119	16.272	52.944	−9.598	1.00	19.61	C
ATOM	1934	OG	SER	A	119	15.222	53.666	−10.200	1.00	22.09	O
ATOM	1936	C	SER	A	119	17.814	51.035	−9.863	1.00	19.56	C
ATOM	1937	O	SER	A	119	18.805	51.193	−10.556	1.00	19.51	O
ATOM	1938	N	TYR	A	120	17.850	50.394	−8.707	1.00	19.94	N
ATOM	1940	CA	TYR	A	120	19.100	49.907	−8.155	1.00	20.38	C
ATOM	1942	CB	TYR	A	120	19.450	50.716	−6.912	1.00	20.58	C
ATOM	1945	CG	TYR	A	120	19.531	52.193	−7.167	1.00	22.52	C
ATOM	1946	CD1	TYR	A	120	20.598	52.743	−7.862	1.00	24.80	C
ATOM	1948	CE1	TYR	A	120	20.673	54.100	−8.093	1.00	25.50	C
ATOM	1950	CZ	TYR	A	120	19.673	54.911	−7.625	1.00	27.56	C
ATOM	1951	OH	TYR	A	120	19.709	56.273	−7.831	1.00	30.87	O
ATOM	1953	CE2	TYR	A	120	18.612	54.375	−6.928	1.00	26.60	C
ATOM	1955	CD2	TYR	A	120	18.551	53.037	−6.707	1.00	24.11	C
ATOM	1957	C	TYR	A	120	19.029	48.419	−7.812	1.00	20.60	C
ATOM	1958	O	TYR	A	120	18.608	48.032	−6.720	1.00	19.19	O
ATOM	1959	N	GLU	A	121	19.458	47.594	−8.765	1.00	21.07	N
ATOM	1961	CA	GLU	A	121	19.440	46.159	−8.612	1.00	21.63	C
ATOM	1963	CB	GLU	A	121	20.069	45.522	−9.845	1.00	22.73	C
ATOM	1966	CG	GLU	A	121	19.781	44.044	−9.995	1.00	26.38	C
ATOM	1969	CD	GLU	A	121	20.300	43.492	−11.314	1.00	32.06	C
ATOM	1970	OE1	GLU	A	121	21.219	44.116	−11.897	1.00	35.93	O
ATOM	1971	OE2	GLU	A	121	19.796	42.431	−11.759	1.00	35.78	O
ATOM	1972	C	GLU	A	121	20.235	45.795	−7.363	1.00	20.72	C
ATOM	1973	O	GLU	A	121	21.236	46.429	−7.070	1.00	20.21	O
ATOM	1974	N	GLY	A	122	19.776	44.799	−6.614	1.00	19.88	N
ATOM	1976	CA	GLY	A	122	20.480	44.377	−5.418	1.00	19.28	C
ATOM	1979	C	GLY	A	122	20.122	45.173	−4.174	1.00	18.88	C
ATOM	1980	O	GLY	A	122	20.586	44.843	−3.074	1.00	19.51	O
ATOM	1981	N	TYR	A	123	19.304	46.207	−4.334	1.00	17.36	N
ATOM	1983	CA	TYR	A	123	18.830	46.995	−3.210	1.00	17.27	C
ATOM	1985	CB	TYR	A	123	19.013	48.481	−3.472	1.00	17.67	C
ATOM	1988	CG	TYR	A	123	20.445	48.940	−3.412	1.00	19.94	C
ATOM	1989	CD1	TYR	A	123	21.364	48.553	−4.384	1.00	22.10	C
ATOM	1991	CE1	TYR	A	123	22.686	48.980	−4.334	1.00	23.22	C
ATOM	1993	CZ	TYR	A	123	23.090	49.814	−3.306	1.00	23.86	C
ATOM	1994	OH	TYR	A	123	24.383	50.248	−3.249	1.00	26.72	O
ATOM	1996	CE2	TYR	A	123	22.204	50.214	−2.334	1.00	23.71	C
ATOM	1998	CD2	TYR	A	123	20.879	49.777	−2.395	1.00	22.89	C
ATOM	2000	C	TYR	A	123	17.360	46.711	−2.926	1.00	16.35	C
ATOM	2001	O	TYR	A	123	16.541	46.652	−3.858	1.00	15.82	O
ATOM	2002	N	PHE	A	124	17.030	46.582	−1.643	1.00	14.95	N
ATOM	2004	CA	PHE	A	124	15.686	46.193	−1.217	1.00	14.48	C
ATOM	2006	CB	PHE	A	124	15.677	44.725	−0.735	1.00	14.44	C
ATOM	2009	CG	PHE	A	124	16.008	43.690	−1.802	1.00	14.62	C
ATOM	2010	CD1	PHE	A	124	17.315	43.465	−2.196	1.00	14.70	C
ATOM	2012	CE1	PHE	A	124	17.625	42.498	−3.141	1.00	15.20	C
ATOM	2014	CZ	PHE	A	124	16.617	41.736	−3.720	1.00	15.64	C
ATOM	2016	CE2	PHE	A	124	15.314	41.941	−3.330	1.00	15.03	C
ATOM	2018	CD2	PHE	A	124	15.010	42.915	−2.367	1.00	13.83	C
ATOM	2020	C	PHE	A	124	15.174	47.040	−0.051	1.00	14.20	C
ATOM	2021	O	PHE	A	124	15.941	47.599	0.748	1.00	13.50	O
ATOM	2022	N	LEU	A	125	13.855	47.111	0.046	1.00	13.56	N
ATOM	2024	CA	LEU	A	125	13.214	47.690	1.194	1.00	14.11	C
ATOM	2026	CB	LEU	A	125	11.709	47.752	0.999	1.00	14.06	C
ATOM	2029	CG	LEU	A	125	11.236	48.727	−0.070	1.00	15.16	C
ATOM	2031	CD1	LEU	A	125	9.739	48.789	−0.067	1.00	14.42	C
ATOM	2035	CD2	LEU	A	125	11.849	50.138	0.192	1.00	15.65	C
ATOM	2039	C	LEU	A	125	13.549	46.778	2.370	1.00	14.51	C
ATOM	2040	O	LEU	A	125	13.493	45.547	2.249	1.00	14.05	O
ATOM	2041	N	ALA	A	126	13.884	47.379	3.500	1.00	15.24	N
ATOM	2043	CA	ALA	A	126	14.255	46.625	4.680	1.00	15.67	C
ATOM	2045	CB	ALA	A	126	15.737	46.388	4.686	1.00	16.08	C
ATOM	2049	C	ALA	A	126	13.851	47.335	5.963	1.00	16.61	C
ATOM	2050	O	ALA	A	126	13.628	48.551	5.982	1.00	15.79	O
ATOM	2051	N	CYS	A	127	13.730	46.549	7.027	1.00	16.97	N
ATOM	2053	CA	CYS	A	127	13.480	47.091	8.343	1.00	18.16	C
ATOM	2055	CB	CYS	A	127	12.465	46.245	9.111	1.00	17.89	C
ATOM	2058	SG	CYS	A	127	12.136	46.914	10.744	1.00	17.43	S
ATOM	2059	C	CYS	A	127	14.806	47.070	9.080	1.00	19.26	C
ATOM	2060	O	CYS	A	127	15.488	46.049	9.098	1.00	17.87	O
ATOM	2061	N	GLU	A	128	15.173	48.193	9.669	1.00	21.56	N
ATOM	2063	CA	GLU	A	128	16.411	48.272	10.430	1.00	24.21	C
ATOM	2065	CB	GLU	A	128	17.484	49.021	9.651	1.00	24.99	C
ATOM	2068	CG	GLU	A	128	18.782	49.161	10.429	1.00	28.30	C
ATOM	2071	CD	GLU	A	128	19.923	49.638	9.561	1.00	32.20	C
ATOM	2072	OE1	GLU	A	128	20.405	48.843	8.720	1.00	34.84	O
ATOM	2073	OE2	GLU	A	128	20.322	50.808	9.713	1.00	35.17	O
ATOM	2074	C	GLU	A	128	16.179	48.983	11.747	1.00	25.58	C
ATOM	2075	O	GLU	A	128	15.650	50.086	11.790	1.00	25.14	O
ATOM	2076	N	LYS	A	129	16.561	48.339	12.834	1.00	28.08	N
ATOM	2078	CA	LYS	A	129	16.439	48.977	14.134	1.00	30.46	C
ATOM	2080	CB	LYS	A	129	16.544	47.962	15.276	1.00	30.82	C
ATOM	2083	CG	LYS	A	129	16.381	48.600	16.659	1.00	32.18	C
ATOM	2086	CD	LYS	A	129	16.068	47.583	17.744	1.00	34.34	C
ATOM	2089	CE	LYS	A	129	15.662	48.291	19.048	1.00	35.70	C
ATOM	2092	NZ	LYS	A	129	15.241	47.344	20.119	1.00	37.60	N
ATOM	2096	C	LYS	A	129	17.545	50.036	14.248	1.00	32.32	C
ATOM	2097	O	LYS	A	129	18.691	49.789	13.874	1.00	31.88	O
ATOM	2098	N	GLU	A	130	17.189	51.227	14.697	1.00	34.59	N
ATOM	2100	CA	GLU	A	130	18.178	52.264	14.919	1.00	37.12	C
ATOM	2102	CB	GLU	A	130	18.159	53.334	13.836	1.00	37.73	C
ATOM	2105	CG	GLU	A	130	19.219	54.410	14.035	1.00	40.54	C
ATOM	2108	CD	GLU	A	130	19.308	55.377	12.870	1.00	44.06	C
ATOM	2109	OE1	GLU	A	130	18.410	56.253	12.754	1.00	46.60	O
ATOM	2110	OE2	GLU	A	130	20.277	55.260	12.071	1.00	47.05	O
ATOM	2111	C	GLU	A	130	17.831	52.836	16.268	1.00	38.44	C
ATOM	2112	O	GLU	A	130	16.839	53.560	16.419	1.00	38.52	O
ATOM	2113	N	ARG	A	131	18.633	52.454	17.256	1.00	40.25	N
ATOM	2115	CA	ARG	A	131	18.379	52.807	18.633	1.00	41.48	C
ATOM	2117	CB	ARG	A	131	18.299	54.320	18.806	1.00	42.02	C
ATOM	2120	CG	ARG	A	131	19.653	54.994	18.747	1.00	45.34	C
ATOM	2123	CD	ARG	A	131	19.585	56.508	18.564	1.00	49.71	C
ATOM	2126	NE	ARG	A	131	19.061	57.195	19.747	1.00	53.66	N
ATOM	2128	CZ	ARG	A	131	18.894	58.514	19.832	1.00	57.36	C
ATOM	2129	NH1	ARG	A	131	19.206	59.294	18.800	1.00	58.89	N
ATOM	2132	NH2	ARG	A	131	18.411	59.061	20.946	1.00	58.63	N
ATOM	2135	C	ARG	A	131	17.070	52.163	18.997	1.00	41.33	C
ATOM	2136	O	ARG	A	131	16.872	50.957	18.955	1.00	41.59	O
ATOM	2137	OXT	ARG	A	131	16.139	52.864	19.330	1.00	41.93	O
ATOM	2138	N	ASP	A	132	15.684	53.375	19.402	1.00	34.96	N
ATOM	2140	CA	ASP	A	132	14.434	52.731	19.877	1.00	34.75	C
ATOM	2142	CB	ASP	A	132	13.824	53.590	20.981	1.00	35.47	C
ATOM	2145	CG	ASP	A	132	14.588	53.488	22.290	1.00	38.55	C
ATOM	2146	OD1	ASP	A	132	14.659	52.373	22.851	1.00	43.85	O
ATOM	2147	OD2	ASP	A	132	15.147	54.467	22.839	1.00	43.35	O
ATOM	2148	C	ASP	A	132	13.462	52.584	18.703	1.00	32.91	C
ATOM	2149	O	ASP	A	132	12.388	52.027	18.858	1.00	33.17	O
ATOM	2152	N	LEU	A	133	13.815	53.182	17.571	1.00	30.94	N
ATOM	2154	CA	LEU	A	133	13.060	53.071	16.326	1.00	29.27	C
ATOM	2156	CB	LEU	A	133	13.230	54.379	15.555	1.00	29.34	C
ATOM	2159	CG	LEU	A	133	13.010	55.632	16.413	1.00	30.29	C
ATOM	2161	CD1	LEU	A	133	13.148	56.893	15.603	1.00	31.03	C
ATOM	2165	CD2	LEU	A	133	11.644	55.594	17.084	1.00	31.79	C
ATOM	2169	C	LEU	A	133	13.371	51.884	15.386	1.00	27.63	C
ATOM	2170	O	LEU	A	133	14.487	51.349	15.335	1.00	26.59	O
ATOM	2171	N	PHE	A	134	12.333	51.507	14.641	1.00	25.38	N
ATOM	2173	CA	PHE	A	134	12.388	50.493	13.603	1.00	23.86	C
ATOM	2175	CB	PHE	A	134	11.371	49.409	13.902	1.00	23.84	C
ATOM	2178	CG	PHE	A	134	11.672	48.632	15.140	1.00	23.81	C
ATOM	2179	CD1	PHE	A	134	12.532	47.555	15.102	1.00	24.83	C
ATOM	2181	CE1	PHE	A	134	12.812	46.827	16.248	1.00	25.46	C
ATOM	2183	CZ	PHE	A	134	12.239	47.179	17.438	1.00	24.86	C
ATOM	2185	CE2	PHE	A	134	11.389	48.250	17.496	1.00	25.34	C
ATOM	2187	CD2	PHE	A	134	11.102	48.978	16.343	1.00	24.26	C
ATOM	2189	C	PHE	A	134	12.036	51.216	12.304	1.00	22.99	C
ATOM	2190	O	PHE	A	134	10.884	51.568	12.063	1.00	22.39	O
ATOM	2191	N	LYS	A	135	13.026	51.442	11.465	1.00	22.01	N
ATOM	2193	CA	LYS	A	135	12.784	52.222	10.260	1.00	21.96	C
ATOM	2195	CB	LYS	A	135	13.736	53.408	10.174	1.00	22.55	C
ATOM	2198	CG	LYS	A	135	15.114	53.150	10.614	1.00	27.17	C
ATOM	2201	CD	LYS	A	135	15.752	54.440	11.190	1.00	31.21	C
ATOM	2204	CE	LYS	A	135	15.641	55.625	10.238	1.00	34.01	C
ATOM	2207	NZ	LYS	A	135	16.573	56.760	10.608	1.00	38.74	N
ATOM	2211	C	LYS	A	135	12.834	51.428	8.982	1.00	19.95	C
ATOM	2212	O	LYS	A	135	13.459	50.371	8.905	1.00	19.00	O
ATOM	2213	N	LEU	A	136	12.125	51.954	7.996	1.00	18.98	N
ATOM	2215	CA	LEU	A	136	12.140	51.402	6.659	1.00	18.68	C
ATOM	2217	CB	LEU	A	136	10.849	51.738	5.911	1.00	18.73	C
ATOM	2220	CG	LEU	A	136	10.766	51.191	4.480	1.00	17.71	C
ATOM	2222	CD1	LEU	A	136	10.502	49.701	4.505	1.00	18.75	C
ATOM	2226	CD2	LEU	A	136	9.678	51.889	3.686	1.00	17.40	C
ATOM	2230	C	LEU	A	136	13.305	52.066	5.969	1.00	18.53	C
ATOM	2231	O	LEU	A	136	13.397	53.281	5.945	1.00	18.21	O
ATOM	2232	N	ILE	A	137	14.211	51.274	5.434	1.00	17.97	N
ATOM	2234	CA	ILE	A	137	15.321	51.821	4.702	1.00	18.57	C
ATOM	2236	CB	ILE	A	137	16.638	51.658	5.504	1.00	18.88	C
ATOM	2238	CG1	ILE	A	137	16.971	50.179	5.667	1.00	19.36	C
ATOM	2241	CD1	ILE	A	137	18.369	49.924	6.185	1.00	21.77	C
ATOM	2245	CG2	ILE	A	137	16.524	52.287	6.883	1.00	19.34	C
ATOM	2249	C	ILE	A	137	15.438	51.065	3.396	1.00	18.91	C
ATOM	2250	O	ILE	A	137	14.756	50.052	3.171	1.00	17.82	O
ATOM	2251	N	LEU	A	138	16.311	51.567	2.538	1.00	19.23	N
ATOM	2253	CA	LEU	A	138	16.684	50.842	1.352	1.00	20.34	C
ATOM	2255	CB	LEU	A	138	16.762	51.754	0.150	1.00	20.52	C
ATOM	2258	CG	LEU	A	138	17.104	51.009	−1.132	1.00	21.99	C
ATOM	2260	CD1	LEU	A	138	15.894	50.326	−1.683	1.00	22.14	C
ATOM	2264	CD2	LEU	A	138	17.676	51.971	−2.172	1.00	24.33	C
ATOM	2268	C	LEU	A	138	18.049	50.308	1.630	1.00	21.00	C
ATOM	2269	O	LEU	A	138	18.937	51.066	1.974	1.00	20.84	O
ATOM	2270	N	LYS	A	139	18.257	49.017	1.484	1.00	21.81	N
ATOM	2272	CA	LYS	A	139	19.588	48.549	1.722	1.00	22.88	C
ATOM	2274	CB	LYS	A	139	19.710	47.968	3.124	1.00	24.00	C
ATOM	2277	CG	LYS	A	139	19.222	46.582	3.278	1.00	26.46	C
ATOM	2280	CD	LYS	A	139	19.697	46.037	4.612	1.00	28.74	C
ATOM	2283	CE	LYS	A	139	19.184	44.649	4.858	1.00	29.57	C
ATOM	2286	NZ	LYS	A	139	19.522	44.134	6.236	1.00	29.04	N
ATOM	2290	C	LYS	A	139	20.078	47.566	0.707	1.00	22.74	C
ATOM	2291	O	LYS	A	139	19.302	46.814	0.115	1.00	21.42	O
ATOM	2292	N	LYS	A	140	21.387	47.599	0.487	1.00	22.53	N
ATOM	2294	CA	LYS	A	140	22.000	46.675	−0.432	1.00	23.48	C
ATOM	2296	CB	LYS	A	140	23.437	47.080	−0.768	1.00	23.90	C
ATOM	2299	CG	LYS	A	140	24.109	46.147	−1.755	1.00	26.16	C
ATOM	2302	CD	LYS	A	140	25.510	46.642	−2.168	1.00	29.72	C
ATOM	2305	CE	LYS	A	140	26.077	45.822	−3.335	1.00	32.07	C
ATOM	2308	NZ	LYS	A	140	25.928	44.344	−3.151	1.00	35.10	N
ATOM	2312	C	LYS	A	140	21.979	45.356	0.292	1.00	23.49	C
ATOM	2313	O	LYS	A	140	22.503	45.261	1.379	1.00	23.51	O
ATOM	2314	N	GLU	A	141	21.400	44.342	−0.305	1.00	23.54	N
ATOM	2316	CA	GLU	A	141	21.287	43.068	0.357	1.00	24.75	C
ATOM	2318	CB	GLU	A	141	19.825	42.816	0.709	1.00	24.91	C
ATOM	2321	CG	GLU	A	141	19.589	41.464	1.352	1.00	27.12	C
ATOM	2324	CD	GLU	A	141	20.296	41.339	2.679	1.00	28.59	C
ATOM	2325	OE1	GLU	A	141	21.302	40.621	2.760	1.00	23.69	O
ATOM	2326	OE2	GLU	A	141	19.829	41.977	3.642	1.00	33.25	O
ATOM	2327	C	GLU	A	141	21.775	41.963	−0.531	1.00	24.90	C
ATOM	2328	O	GLU	A	141	21.195	41.698	−1.583	1.00	25.79	O
ATOM	2329	N	ASP	A	142	22.822	41.284	−0.114	1.00	24.81	N
ATOM	2331	CA	ASP	A	142	23.311	40.174	−0.915	1.00	25.28	C
ATOM	2333	CB	ASP	A	142	24.832	40.085	−0.833	1.00	26.35	C
ATOM	2336	CG	ASP	A	142	25.497	41.343	−1.326	1.00	29.58	C
ATOM	2337	OD1	ASP	A	142	25.182	41.792	−2.457	1.00	34.14	O
ATOM	2338	OD2	ASP	A	142	26.317	41.976	−0.643	1.00	35.96	O
ATOM	2339	C	ASP	A	142	22.674	38.851	−0.510	1.00	24.08	C
ATOM	2340	O	ASP	A	142	22.721	37.883	−1.271	1.00	23.79	O
ATOM	2341	N	GLU	A	143	22.036	38.818	0.655	1.00	22.40	N
ATOM	2343	CA	GLU	A	143	21.439	37.576	1.138	1.00	21.65	C
ATOM	2345	CB	GLU	A	143	21.944	37.254	2.536	1.00	21.75	C
ATOM	2348	CG	GLU	A	143	23.433	36.965	2.596	1.00	22.62	C
ATOM	2351	CD	GLU	A	143	23.848	35.809	1.708	1.00	22.90	C
ATOM	2352	OE1	GLU	A	143	23.037	34.908	1.464	1.00	21.42	O
ATOM	2353	OE2	GLU	A	143	25.017	35.785	1.272	1.00	26.11	O
ATOM	2354	C	GLU	A	143	19.929	37.623	1.134	1.00	21.12	C
ATOM	2355	O	GLU	A	143	19.303	38.268	1.984	1.00	20.40	O
ATOM	2356	N	LEU	A	144	19.339	36.915	0.187	1.00	20.66	N
ATOM	2358	CA	LEU	A	144	17.900	36.955	0.034	1.00	21.04	C
ATOM	2360	CB	LEU	A	144	17.484	36.338	−1.298	1.00	21.46	C
ATOM	2363	CG	LEU	A	144	17.253	37.308	−2.456	1.00	24.60	C
ATOM	2365	CD1	LEU	A	144	18.245	38.440	−2.516	1.00	25.92	C
ATOM	2369	CD2	LEU	A	144	17.199	36.518	−3.775	1.00	26.20	C
ATOM	2373	C	LEU	A	144	17.196	36.250	1.183	1.00	20.25	C
ATOM	2374	O	LEU	A	144	15.998	36.444	1.381	1.00	19.65	O
ATOM	2375	N	GLY	A	145	17.950	35.468	1.955	1.00	19.06	N
ATOM	2377	CA	GLY	A	145	17.387	34.748	3.081	1.00	18.63	C
ATOM	2380	C	GLY	A	145	17.220	35.624	4.307	1.00	18.10	C
ATOM	2381	O	GLY	A	145	16.716	35.168	5.323	1.00	18.03	O
ATOM	2382	N	ASP	A	146	17.630	36.883	4.205	1.00	17.78	N
ATOM	2384	CA	ASP	A	146	17.529	37.829	5.308	1.00	18.41	C
ATOM	2386	CB	ASP	A	146	18.382	39.046	5.008	1.00	19.11	C
ATOM	2389	CG	ASP	A	146	18.651	39.902	6.233	1.00	22.22	C
ATOM	2390	OD1	ASP	A	146	17.793	40.025	7.130	1.00	22.44	O
ATOM	2391	OD2	ASP	A	146	19.725	40.512	6.373	1.00	29.90	O
ATOM	2392	C	ASP	A	146	16.084	38.269	5.559	1.00	18.16	C
ATOM	2393	O	ASP	A	146	15.470	38.924	4.723	1.00	17.37	O
ATOM	2394	N	ARG	A	147	15.567	37.909	6.727	1.00	18.11	N
ATOM	2396	CA	ARG	A	147	14.201	38.211	7.117	1.00	18.48	C
ATOM	2398	CB	ARG	A	147	13.861	37.561	8.457	1.00	18.61	C
ATOM	2401	CG	ARG	A	147	13.558	36.104	8.369	1.00	20.73	C
ATOM	2404	CD	ARG	A	147	13.348	35.404	9.744	1.00	23.31	C
ATOM	2407	NE	ARG	A	147	14.011	34.154	9.564	1.00	27.87	N
ATOM	2409	CZ	ARG	A	147	15.110	33.753	10.172	1.00	27.13	C
ATOM	2410	NH1	ARG	A	147	15.654	34.419	11.194	1.00	28.07	N
ATOM	2413	NH2	ARG	A	147	15.620	32.618	9.769	1.00	27.24	N
ATOM	2416	C	ARG	A	147	13.944	39.696	7.232	1.00	17.88	C
ATOM	2417	O	ARG	A	147	12.798	40.128	7.157	1.00	18.18	O
ATOM	2418	N	SER	A	148	14.992	40.482	7.418	1.00	17.16	N
ATOM	2420	CA	SER	A	148	14.822	41.919	7.551	1.00	17.22	C
ATOM	2422	CB	SER	A	148	16.129	42.604	7.962	1.00	17.56	C
ATOM	2425	OG	SER	A	148	17.131	42.385	6.983	1.00	20.70	O
ATOM	2427	C	SER	A	148	14.275	42.563	6.275	1.00	16.43	C
ATOM	2428	O	SER	A	148	13.790	43.699	6.336	1.00	16.13	O
ATOM	2429	N	ILE	A	149	14.365	41.869	5.132	1.00	15.25	N
ATOM	2431	CA	ILE	A	149	13.809	42.403	3.886	1.00	14.90	C
ATOM	2433	CB	ILE	A	149	14.823	42.397	2.745	1.00	15.35	C
ATOM	2435	CG1	ILE	A	149	15.226	40.981	2.346	1.00	14.55	C
ATOM	2438	CD1	ILE	A	149	15.824	40.952	0.958	1.00	17.24	C
ATOM	2442	CG2	ILE	A	149	16.068	43.200	3.121	1.00	15.79	C
ATOM	2446	C	ILE	A	149	12.540	41.662	3.477	1.00	14.46	C
ATOM	2447	O	ILE	A	149	12.119	41.736	2.338	1.00	13.29	O
ATOM	2448	N	MET	A	150	11.934	40.966	4.432	1.00	14.06	N
ATOM	2450	CA	MET	A	150	10.728	40.211	4.180	1.00	14.01	C
ATOM	2452	CB	MET	A	150	10.881	38.785	4.689	1.00	14.32	C
ATOM	2455	CG	MET	A	150	11.968	38.009	3.970	1.00	14.36	C
ATOM	2458	SD	MET	A	150	11.979	36.322	4.490	1.00	15.53	S
ATOM	2459	CE	MET	A	150	13.509	35.730	3.646	1.00	15.34	C
ATOM	2463	C	MET	A	150	9.526	40.889	4.853	1.00	14.00	C
ATOM	2464	O	MET	A	150	9.632	41.407	5.975	1.00	14.37	O
ATOM	2465	N	PHE	A	151	8.407	40.922	4.137	1.00	13.04	N
ATOM	2467	CA	PHE	A	151	7.192	41.556	4.628	1.00	12.74	C
ATOM	2469	CB	PHE	A	151	7.057	42.963	4.032	1.00	12.76	C
ATOM	2472	CG	PHE	A	151	8.241	43.827	4.276	1.00	13.14	C
ATOM	2473	CD1	PHE	A	151	8.337	44.557	5.435	1.00	14.08	C
ATOM	2475	CE1	PHE	A	151	9.445	45.336	5.677	1.00	15.32	C
ATOM	2477	CZ	PHE	A	151	10.471	45.383	4.753	1.00	14.93	C
ATOM	2479	CE2	PHE	A	151	10.383	44.670	3.598	1.00	13.48	C
ATOM	2481	CD2	PHE	A	151	9.281	43.872	3.369	1.00	14.58	C
ATOM	2483	C	PHE	A	151	5.980	40.780	4.203	1.00	12.85	C
ATOM	2484	O	PHE	A	151	6.049	39.983	3.278	1.00	14.01	O
ATOM	2485	N	THR	A	152	4.860	41.019	4.875	1.00	12.94	N
ATOM	2487	CA	THR	A	152	3.578	40.523	4.415	1.00	13.01	C
ATOM	2489	CB	THR	A	152	2.829	39.760	5.502	1.00	13.46	C
ATOM	2491	OG1	THR	A	152	2.664	40.602	6.649	1.00	12.42	O
ATOM	2493	CG2	THR	A	152	3.660	38.562	5.997	1.00	14.76	C
ATOM	2497	C	THR	A	152	2.754	41.746	4.009	1.00	13.17	C
ATOM	2498	O	THR	A	152	2.960	42.847	4.525	1.00	11.75	O
ATOM	2499	N	VAL	A	153	1.836	41.535	3.076	1.00	13.24	N
ATOM	2501	CA	VAL	A	153	0.978	42.581	2.568	1.00	13.97	C
ATOM	2503	CB	VAL	A	153	1.249	42.830	1.076	1.00	13.95	C
ATOM	2505	CG1	VAL	A	153	0.366	43.928	0.541	1.00	15.22	C
ATOM	2509	CG2	VAL	A	153	2.699	43.177	0.849	1.00	13.88	C
ATOM	2513	C	VAL	A	153	−0.463	42.125	2.745	1.00	14.68	C
ATOM	2514	O	VAL	A	153	−0.835	41.053	2.271	1.00	14.18	O
ATOM	2515	N	GLN	A	154	−1.254	42.904	3.472	1.00	15.72	N
ATOM	2517	CA	GLN	A	154	−2.663	42.586	3.666	1.00	17.20	C
ATOM	2519	CB	GLN	A	154	−3.050	42.651	5.149	1.00	17.24	C
ATOM	2522	CG	GLN	A	154	−4.510	42.274	5.412	1.00	16.48	C
ATOM	2525	CD	GLN	A	154	−4.934	42.370	6.894	1.00	18.68	C
ATOM	2526	OE1	GLN	A	154	−6.003	41.850	7.280	1.00	19.11	O
ATOM	2527	NE2	GLN	A	154	−4.140	43.055	7.700	1.00	13.22	N
ATOM	2530	C	GLN	A	154	−3.537	43.559	2.858	1.00	19.13	C
ATOM	2531	O	GLN	A	154	−3.388	44.778	2.981	1.00	18.43	O
ATOM	2532	N	ASN	A	155	−4.411	43.001	2.019	1.00	21.35	N
ATOM	2534	CA	ASN	A	155	−5.410	43.747	1.239	1.00	24.39	C
ATOM	2536	CB	ASN	A	155	−4.797	44.514	0.060	1.00	24.41	C
ATOM	2539	CG	ASN	A	155	−3.922	43.649	−0.845	1.00	25.02	C
ATOM	2540	OD1	ASN	A	155	−4.247	42.506	−1.165	1.00	24.80	O
ATOM	2541	ND2	ASN	A	155	−2.801	44.223	−1.279	1.00	25.30	N
ATOM	2544	C	ASN	A	155	−6.477	42.772	0.718	1.00	27.08	C
ATOM	2545	O	ASN	A	155	−6.356	41.581	0.942	1.00	27.51	O
ATOM	2546	N	GLU	A	156	−7.521	43.254	0.041	1.00	30.12	N
ATOM	2548	CA	GLU	A	156	−8.536	42.326	−0.532	1.00	32.02	C
ATOM	2550	CB	GLU	A	156	−9.902	42.406	0.182	1.00	32.85	C
ATOM	2553	CG	GLU	A	156	−9.937	42.972	1.592	1.00	34.74	C
ATOM	2556	CD	GLU	A	156	−11.365	43.222	2.091	1.00	38.87	C
ATOM	2557	OE1	GLU	A	156	−11.677	44.388	2.438	1.00	39.69	O
ATOM	2558	OE2	GLU	A	156	−12.184	42.267	2.143	1.00	41.51	O
ATOM	2559	C	GLU	A	156	−8.756	42.510	−2.049	1.00	32.60	C
ATOM	2560	O	GLU	A	156	−8.229	43.443	−2.678	1.00	33.38	O
ATOM	2561	O	HOH	W	155	0.980	49.319	6.878	1.00	9.43	O
ATOM	2564	O	HOH	W	156	6.852	53.523	−4.835	1.00	11.31	O
ATOM	2567	O	HOH	W	157	13.147	38.636	−4.026	1.00	12.68	O
ATOM	2570	O	HOH	W	158	12.048	41.154	−5.103	1.00	10.20	O
ATOM	2573	O	HOH	W	159	3.964	43.534	−13.037	1.00	19.08	O
ATOM	2576	O	HOH	W	160	1.746	38.873	2.150	1.00	11.74	O
ATOM	2579	O	HOH	W	161	−1.920	52.126	14.250	1.00	12.72	O
ATOM	2582	O	HOH	W	162	3.650	47.805	−19.855	1.00	15.19	O
ATOM	2585	O	HOH	W	163	20.733	35.444	−1.932	1.00	18.64	O
ATOM	2588	O	HOH	W	165	16.360	32.547	5.947	1.00	17.78	O
ATOM	2591	O	HOH	W	166	9.483	48.733	−17.909	1.00	14.55	O
ATOM	2594	O	HOH	W	167	1.892	60.961	−11.209	1.00	14.17	O
ATOM	2597	O	HOH	W	168	10.573	51.182	−21.842	1.00	18.80	O
ATOM	2600	O	HOH	W	169	13.343	51.919	−7.674	1.00	18.63	O
ATOM	2603	O	HOH	W	170	9.723	52.434	15.366	1.00	19.49	O
ATOM	2606	O	HOH	W	171	−0.707	42.516	−23.635	1.00	26.55	O
ATOM	2609	O	HOH	W	172	17.390	54.299	3.115	1.00	27.63	O
ATOM	2612	O	HOH	W	173	1.373	58.800	−16.633	1.00	25.57	O
ATOM	2615	O	HOH	W	174	11.838	40.747	−19.018	1.00	18.21	O
ATOM	2618	O	HOH	W	175	−8.439	48.620	−1.993	1.00	24.14	O
ATOM	2621	O	HOH	W	176	2.129	52.148	−20.929	1.00	30.47	O
ATOM	2624	O	HOH	W	177	12.337	40.485	11.115	1.00	48.07	O
ATOM	2627	O	HOH	W	178	15.365	43.113	−10.306	1.00	16.94	O
ATOM	2630	O	HOH	W	179	−3.025	43.713	13.218	1.00	13.00	O
ATOM	2633	O	HOH	W	180	−2.693	63.911	−4.588	1.00	21.74	O
ATOM	2636	O	HOH	W	181	26.746	37.454	1.851	1.00	19.91	O
ATOM	2639	O	HOH	W	182	12.200	36.290	−3.878	1.00	25.10	O
ATOM	2642	O	HOH	W	183	6.208	45.904	−25.640	1.00	24.76	O
ATOM	2645	O	HOH	W	184	2.673	44.220	16.629	1.00	19.54	O
ATOM	2648	O	HOH	W	185	16.066	45.706	−10.179	1.00	17.23	O
ATOM	2651	O	HOH	W	186	24.328	41.803	2.140	1.00	31.05	O
ATOM	2654	O	HOH	W	187	20.825	40.387	−3.715	1.00	30.96	O
ATOM	2657	O	HOH	W	188	−0.157	60.059	−14.574	1.00	31.52	O
ATOM	2660	O	HOH	W	189	−3.496	54.252	−7.760	1.00	31.49	O
ATOM	2663	O	HOH	W	190	7.904	57.171	16.478	1.00	26.14	O
ATOM	2666	O	HOH	W	191	9.490	62.667	12.534	1.00	65.07	O
ATOM	2669	O	HOH	W	192	4.407	52.756	23.668	1.00	24.93	O
ATOM	2672	O	HOH	W	193	8.637	65.569	−5.132	1.00	28.22	O
ATOM	2675	O	HOH	W	194	0.085	54.952	−23.193	1.00	61.78	O
ATOM	2678	O	HOH	W	195	0.587	40.969	−2.347	1.00	20.74	O
ATOM	2681	O	HOH	W	196	−4.690	40.058	2.272	1.00	25.95	O
ATOM	2684	O	HOH	W	197	8.430	28.376	−3.973	1.00	37.40	O
ATOM	2687	O	HOH	W	198	−3.634	58.669	−7.708	1.00	34.27	O
ATOM	2690	O	HOH	W	199	16.894	46.819	−12.407	1.00	24.91	O
ATOM	2693	O	HOH	W	200	4.198	39.902	8.744	1.00	34.44	O
ATOM	2696	O	HOH	W	201	14.854	34.185	0.057	1.00	28.32	O
ATOM	2699	O	HOH	W	202	14.294	41.383	−19.006	1.00	36.69	O
ATOM	2702	O	HOH	W	203	−7.460	46.312	−0.048	1.00	23.37	O
ATOM	2705	O	HOH	W	205	16.445	31.061	3.569	1.00	30.69	O
ATOM	2708	O	HOH	W	206	20.610	48.824	−11.130	1.00	37.46	O
ATOM	2711	O	HOH	W	207	4.554	54.054	−20.941	1.00	34.43	O
ATOM	2714	O	HOH	W	208	22.716	49.620	2.171	1.00	44.73	O
ATOM	2717	O	HOH	W	209	−3.777	59.118	21.276	1.00	27.67	O
ATOM	2720	O	HOH	W	210	1.193	38.163	15.220	1.00	39.78	O
ATOM	2723	O	HOH	W	211	4.511	58.756	−19.600	1.00	39.54	O
ATOM	2726	O	HOH	W	212	0.825	47.701	−22.991	1.00	32.59	O
ATOM	2729	O	HOH	W	213	1.022	44.133	−3.659	1.00	23.31	O
ATOM	2732	O	HOH	W	214	−1.440	41.646	13.910	1.00	27.10	O
ATOM	2735	O	HOH	W	215	3.952	48.442	23.775	1.00	27.10	O
ATOM	2738	O	HOH	W	216	15.459	33.255	−5.580	1.00	33.32	O
ATOM	2741	O	HOH	W	217	5.420	30.640	5.291	1.00	48.75	O
ATOM	2744	O	HOH	W	218	−8.242	49.779	4.040	1.00	43.18	O
ATOM	2747	O	HOH	W	219	7.431	50.241	18.373	1.00	48.35	O
ATOM	2750	O	HOH	W	220	18.011	46.044	12.605	1.00	28.37	O
ATOM	2753	O	HOH	W	221	12.789	55.627	8.288	1.00	35.75	O
ATOM	2756	O	HOH	W	222	5.835	41.030	17.983	1.00	81.64	O
ATOM	2759	O	HOH	W	224	−4.461	43.343	−23.800	1.00	37.43	O
ATOM	2762	O	HOH	W	225	−1.665	52.565	−19.349	1.00	33.20	O
ATOM	2765	O	HOH	W	226	−1.205	48.642	−19.463	1.00	41.74	O
ATOM	2768	O	HOH	W	227	12.301	62.613	−2.979	1.00	38.97	O
ATOM	2771	O	HOH	W	228	16.655	41.020	−16.375	1.00	39.48	O
ATOM	2774	O	HOH	W	229	11.528	44.224	14.664	1.00	31.66	O
ATOM	2777	O	HOH	W	230	−6.936	53.638	−3.765	1.00	67.47	O
ATOM	2780	O	HOH	W	231	6.936	58.398	−18.190	1.00	23.19	O
ATOM	2783	O	HOH	W	232	27.067	53.984	−3.068	1.00	63.58	O
ATOM	2786	O	HOH	W	233	9.786	51.563	18.320	1.00	44.43	O
ATOM	2789	O	HOH	W	234	−0.115	58.692	−19.029	1.00	38.37	O
ATOM	2792	O	HOH	W	235	18.778	54.022	9.782	1.00	82.22	O
ATOM	2795	O	HOH	W	236	23.671	47.969	11.644	1.00	73.89	O
ATOM	2798	O	HOH	W	237	11.756	32.735	5.883	1.00	43.37	O
ATOM	2801	O	HOH	W	238	8.089	25.977	2.891	1.00	51.09	O
ATOM	2804	O	HOH	W	239	10.237	57.042	−17.293	1.00	21.75	O
ATOM	2807	O	HOH	W	240	10.289	47.280	−23.281	1.00	23.32	O
ATOM	2810	O	HOH	W	241	−6.000	51.764	−10.955	1.00	59.04	O
ATOM	2813	O	HOH	W	242	12.600	55.868	−21.300	1.00	54.68	O
ATOM	2816	O	HOH	W	243	13.305	30.107	1.090	1.00	32.20	O
ATOM	2819	O	HOH	W	244	13.639	60.367	−8.857	1.00	39.30	O
ATOM	2822	O	HOH	W	245	10.018	65.972	4.559	1.00	65.65	O
ATOM	2825	O	HOH	W	246	−7.160	54.898	3.843	1.00	37.98	O
ATOM	2828	O	HOH	W	248	14.798	43.742	11.446	1.00	44.58	O
ATOM	2831	O	HOH	W	249	11.344	43.768	17.684	1.00	43.94	O
ATOM	2834	O	HOH	W	250	4.159	28.986	0.597	1.00	29.63	O
ATOM	2837	O	HOH	W	251	18.107	58.024	−8.569	1.00	42.42	O
ATOM	2840	O	HOH	W	252	17.168	56.125	7.711	1.00	38.97	O
ATOM	2843	O	HOH	W	253	5.575	27.738	−1.350	1.00	63.72	O
ATOM	2846	O	HOH	W	254	14.064	32.232	7.272	1.00	23.52	O
ATOM	2849	O	HOH	W	255	7.205	31.672	−3.143	1.00	20.29	O
ATOM	2852	O	HOH	W	256	20.379	34.105	1.634	1.00	17.16	O
ATOM	2855	O	HOH	W	257	−2.052	56.203	23.818	1.00	23.02	O
ATOM	2858	O	HOH	W	259	1.620	49.332	−20.602	1.00	21.91	O
ATOM	2861	O	HOH	W	260	22.845	34.062	−1.085	1.00	22.09	O
ATOM	2864	O	HOH	W	261	28.445	38.320	−0.263	1.00	22.98	O
ATOM	2867	O	HOH	W	262	−1.709	57.495	20.049	1.00	26.80	O
ATOM	2870	O	HOH	W	263	8.157	54.423	16.370	1.00	26.04	O
ATOM	2873	O	HOH	W	264	−2.564	42.928	−25.602	1.00	28.10	O
ATOM	2876	O	HOH	W	265	11.093	43.070	7.633	1.00	21.20	O
ATOM	2879	O	HOH	W	266	0.138	39.356	−0.268	1.00	32.98	O
ATOM	2882	O	HOH	W	267	16.045	42.245	−12.562	1.00	38.36	O
ATOM	2885	O	HOH	W	268	−3.787	56.629	−6.218	1.00	27.65	O
ATOM	2888	O	HOH	W	270	16.150	45.707	−14.627	1.00	23.75	O
ATOM	2891	O	HOH	W	271	2.128	48.235	−25.659	1.00	37.19	O
ATOM	2894	O	HOH	W	272	−3.094	56.367	2.257	1.00	26.14	O
ATOM	2897	O	HOH	W	273	10.697	62.331	1.963	1.00	33.95	O
ATOM	2900	O	HOH	W	274	22.653	48.364	−8.018	1.00	31.60	O
ATOM	2903	O	HOH	W	275	8.398	53.786	−23.582	1.00	37.67	O
ATOM	2906	O	HOH	W	276	19.283	40.847	−6.259	1.00	35.65	O
ATOM	2909	O	HOH	W	277	0.169	39.380	−4.483	1.00	33.42	O
ATOM	2912	O	HOH	W	278	2.111	61.060	−15.055	1.00	29.84	O
ATOM	2915	O	HOH	W	279	15.097	55.521	5.773	1.00	33.36	O
ATOM	2918	O	HOH	W	280	5.620	53.447	17.365	1.00	35.04	O
ATOM	2921	O	HOH	W	281	4.359	60.922	14.694	1.00	42.51	O
ATOM	2924	O	HOH	W	282	1.486	41.997	−12.375	1.00	41.55	O
ATOM	2927	O	HOH	W	283	4.555	28.108	2.992	1.00	57.75	O
ATOM	2930	O	HOH	W	284	−7.657	49.878	−8.730	1.00	33.44	O
ATOM	2933	O	HOH	W	285	4.476	37.092	9.476	1.00	42.43	O
ATOM	2936	O	HOH	W	286	−5.313	52.381	−13.546	1.00	41.60	O
ATOM	2939	O	HOH	W	287	0.765	29.251	−0.110	1.00	65.18	O
ATOM	2942	O	HOH	W	288	−6.078	60.687	−6.919	1.00	57.64	O
ATOM	2945	O	HOH	W	291	20.695	42.372	8.288	1.00	43.89	O
ATOM	2948	O	HOH	W	292	13.717	57.299	−11.953	1.00	35.61	O
ATOM	2951	O	HOH	W	293	13.925	44.737	13.665	1.00	41.62	O
ATOM	2954	O	HOH	W	294	−0.578	39.882	12.936	1.00	37.74	O
ATOM	2957	O	HOH	W	295	24.945	56.425	−2.484	1.00	72.27	O
ATOM	2960	O	HOH	W	296	19.729	34.118	−3.457	1.00	44.59	O
ATOM	2963	O	HOH	W	297	23.875	46.595	3.411	1.00	61.64	O
ATOM	2966	O	HOH	W	298	19.296	63.370	−8.288	1.00	83.64	O
ATOM	2969	O	HOH	W	299	10.639	31.389	7.932	1.00	75.00	O
ATOM	2972	O	HOH	W	300	−5.807	56.048	1.672	1.00	37.68	O
ATOM	2975	O	HOH	W	301	−10.231	52.603	−2.616	1.00	64.06	O
ATOM	2978	O	HOH	W	302	26.044	39.676	3.125	1.00	43.54	O
ATOM	2981	O	HOH	W	303	−6.568	41.759	−7.981	1.00	71.87	O
ATOM	2984	O	HOH	W	304	15.572	55.018	−12.659	1.00	44.25	0
ATOM	2987	O	HOH	W	305	−3.057	55.505	−20.300	1.00	49.44	O
ATOM	2990	O	HOH	W	306	−4.588	64.322	6.288	1.00	58.83	O
ATOM	2993	O	HOH	W	307	8.872	46.671	−26.152	1.00	56.06	O
ATOM	2996	O	HOH	W	308	−2.200	62.584	−17.589	1.00	50.23	O
ATOM	2999	O	HOH	W	309	−8.907	52.636	4.524	1.00	43.64	O
ATOM	3002	O	HOH	W	310	22.876	62.758	−3.053	1.00	78.74	O
ATOM	3005	O	HOH	W	311	12.320	57.702	−19.442	1.00	60.73	O
ATOM	3008	O	HOH	W	312	15.945	62.355	11.697	1.00	95.98	O
ATOM	3011	O	HOH	W	313	−3.103	46.535	−20.419	1.00	45.35	O
ATOM	3014	O	HOH	W	314	14.544	59.150	−19.661	1.00	83.21	O
ATOM	3017	O	HOH	W	315	8.862	57.800	18.811	1.00	54.05	O
ATOM	3020	O	HOH	W	316	−5.884	56.012	6.102	1.00	44.15	O
ATOM	3023	O	HOH	W	317	0.618	42.638	6.364	1.00	12.34	O
ATOM	3026	O	HOH	W	318	−3.621	45.643	14.748	1.00	23.80	O
ATOM	3029	O	HOH	W	319	10.808	40.959	9.048	1.00	34.28	O
ATOM	3032	O	HOH	W	320	13.749	35.624	−1.557	1.00	21.34	O
ATOM	3035	O	HOH	W	321	16.705	41.684	11.439	1.00	40.11	O
ATOM	3038	O	HOH	W	322	−7.042	55.809	15.702	1.00	31.50	O
ATOM	3041	O	HOH	W	323	18.119	45.894	8.089	1.00	34.40	O
ATOM	3044	O	HOH	W	324	14.176	40.925	14.833	1.00	47.15	O
ATOM	3047	O	HOH	W	325	23.049	43.544	−3.659	1.00	35.82	O
ATOM	3050	O	HOH	W	326	−4.753	72.155	−3.471	1.00	86.45	O
ATOM	3053	O	HOH	W	327	21.409	37.406	−3.751	1.00	48.20	O
ATOM	3056	O	HOH	W	330	4.456	52.657	−25.335	1.00	57.68	O
ATOM	3059	O	HOH	W	331	0.006	37.015	−0.748	1.00	47.52	O
ATOM	3062	O	HOH	W	332	3.193	44.608	24.469	1.00	50.08	O
ATOM	3065	O	HOH	W	333	17.846	56.301	−10.993	1.00	46.91	O
ATOM	3068	O	HOH	W	334	16.361	59.352	14.018	1.00	64.25	O
ATOM	3071	O	HOH	W	335	12.379	50.117	20.902	1.00	52.42	O
ATOM	3074	O	HOH	W	338	2.541	62.540	3.321	1.00	58.90	O
ATOM	3077	O	HOH	W	342	19.236	57.736	4.679	1.00	58.41	O
ATOM	3080	O	HOH	W	343	14.983	60.861	2.743	1.00	39.17	O
ATOM	3083	O	HOH	W	344	−5.241	69.539	−0.010	1.00	64.14	O
ATOM	3086	O	HOH	W	345	21.804	41.918	−7.545	1.00	43.77	O
ATOM	3089	O	HOH	W	346	−3.716	43.989	−19.298	1.00	46.30	O
ATOM	3092	O	HOH	W	347	4.625	69.987	13.138	1.00	63.10	O
ATOM	3095	O	HOH	W	348	7.248	30.740	8.558	1.00	77.44	O
ATOM	3098	O	HOH	W	349	16.581	61.842	−13.261	1.00	56.65	O
ATOM	3101	O	HOH	W	350	23.989	46.986	16.869	1.00	70.85	O
ATOM	3104	O	HOH	W	353	16.199	61.207	−1.785	1.00	47.65	O
ATOM	3107	O	HOH	W	356	−3.863	60.937	14.090	1.00	53.74	O
ATOM	3110	O	HOH	W	357	12.301	43.901	0.579	1.00	13.48	O
ATOM	3113	O	HOH	W	358	0.802	53.510	−5.359	1.00	12.61	O
ATOM	3116	O	HOH	W	359	8.150	43.338	−14.133	1.00	13.98	O
ATOM	3119	O	HOH	W	360	0.324	43.474	13.169	1.00	14.56	O
ATOM	3122	O	HOH	W	367	15.014	59.022	−2.014	1.00	29.05	O
ATOM	3125	O	HOH	W	368	7.758	58.379	−16.399	1.00	34.59	O
ATOM	3128	O	HOH	W	411	1.766	58.029	22.864	1.00	31.86	O
ATOM	3131	O	HOH	W	413	20.096	46.863	8.617	1.00	40.83	O
ATOM	3134	O	HOH	W	415	8.692	59.349	15.091	1.00	28.12	O
ATOM	3137	O	HOH	W	420	16.735	56.070	3.791	1.00	41.20	O
ATOM	3140	O	HOH	W	421	6.718	44.005	−24.075	1.00	31.26	O
ATOM	3143	O	HOH	W	422	3.982	44.239	26.463	1.00	51.23	O
ATOM	3146	O	HOH	W	425	4.101	36.325	12.237	1.00	51.25	O
ATOM	3149	O	HOH	W	427	5.836	53.907	−23.829	1.00	36.87	O
ATOM	3152	O	HOH	W	428	0.815	62.667	0.840	1.00	41.62	O
ATOM	3155	O	HOH	W	429	−4.430	57.682	4.200	1.00	40.20	O
ATOM	3158	O	HOH	W	430	−0.075	39.402	10.982	1.00	37.90	O
ATOM	3161	O	HOH	W	431	12.525	60.939	−5.748	1.00	49.35	O
ATOM	3164	O	HOH	W	433	24.502	50.238	−7.371	1.00	50.44	O
ATOM	3167	O	HOH	W	434	12.218	42.640	10.614	1.00	48.43	O
ATOM	3170	O	HOH	W	437	0.408	59.563	20.080	1.00	45.61	O
ATOM	3173	O	HOH	W	438	5.015	43.535	17.595	1.00	43.03	O
ATOM	3176	O	HOH	W	439	3.707	65.537	8.611	1.00	58.11	O
ATOM	3179	O	HOH	W	440	15.448	41.840	−21.554	1.00	51.86	O
ATOM	3182	O	HOH	W	443	0.656	39.927	−11.904	1.00	59.54	O

[0050]

Claims

1. A composition comprising a human IL-18 in crystalline form.

2. The composition of claim 1 wherein said human IL-18 is an essentially pure native form or a homolog thereof.

3. The composition according to claim 1, wherein said composition has one or more patches of its surface in contact with its receptor; wherein said patches are lined by two groups of amino acid residues; wherein said first group comprises Lys4-Gln18, Phe 30-Asp37, Pro107-Lys112, Lys128-Leu 135 and Aspl45-Ile148; wherein said second group comprises Lys1-Lys8, Ser50-Ser55, Pro89-Lys93, Gln103-Ser105, and Glu155-Asp156.

4. A heavy atom derivative of the composition in claim 1 wherein said derivative comprises a protein having the coordinates in Table I and in FIGS. 1-4.

5. The composition according to claim 1 wherein said human IL-18 is characterized by a β-trefoil fold.

6. A process of identifying an agonist or an antagonist molecule comprising an entity selected from the group consisting of: a peptide, a non-peptide molecule and a chemical compound; wherein said molecule is capable of enhancing, eliciting or blocking the biological activity resulting from interaction with the human IL-18 and its receptor; wherein said process comprises: introducing into a suitable computer program parameters defining an interacting surface based on the conformation of human IL-18 corresponding to the coordinates of FIGS. 1-4 and Table I; wherein said program displays the three-dimensional structure thereof; creating a three-dimensional structure of a test compound in said computer program; displaying an superimposing the model of said test compound on the model. assessing whether said test compound model fits spatially into the binding site; incorporating said test compound in a biological cytokine activity assay; and determining whether said test compound inhibits or enhances the biological activity of human IL-18.

7. A process of identifying an agonist or an antagonist capable of modifying the biological activity of the composition of claim 1, wherein said process comprises: carrying out an in vitro assay by introducing said compound into a biological cytokine activity assay mixture; and determining whether said test compound inhibits or enhances the biological activity of human IL-18 receptor.

8. A molecule identified by the method of claims 6 or 7 wherein said molecule is selected from a group consisting of: a peptide, a peptidomimetic and a synthetic compound.

9. The molecule of claim 8 that is selected from a group consisting of: an antagonist and an agonist.

10. A method of determining a crystal structure comprising using the structural coordinates of a human IL-18 crystal or portions thereof and determining the structure coordinates of a mutant, homologue or co-complex of said human IL-18 by molecular replacement.

11. A method of drug design comprising the use of the atomic coordinates of a human IL-18 crystal to computationally evaluate a chemical entity for association with the receptor binding site of human IL-18.

12. The method according to claim 11 wherein said entity is an agonist or an antagonist of human IL-18.

13. The method of drug design according to claim 11 comprising the steps of using the structure coordinates of human IL-18 to identify an intermediate in a chemical reaction between human IL-18 and a compound which is a ligand of said human IL-18.

14. The method according to one of claims 11-13, wherein said structure coordinates comprises the coordinates of FIGS. 1-4 and Table I.