Murine IL-18 crystal structure

Abstract

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

Description

FIELD OF THE INVENTION

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

BACKGROUND OF THE INVENTION

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.

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

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

In another aspect, the present invention provides a novel crystalline form of the murine IL-18 molecule.

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

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

DETAILED DESCRIPTION OF THE INVENTION

The present invention provides a novel murine 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 mIL-18 without compromising its biological activity and methods to use this crystalline form in identifying, improving or antagonizing the biological activity of mIL-18.

The Novel Murine IL-18 Crystalline Three-Dimensional Structure

The crystal structure of the murine IL-18 in its native form has been determined by molecular replacement and refined to 1.55 Å resolution. The novel murine 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) 10-46, (ii)103-152, 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 murine 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 the IL-18-receptor complex, the mIL-18 structure and that of the IL1β-IL1β receptor complex (PDB:11TB, G. P. Vigers et al. (1997) Nature 386, 190) are used as models for interactions between IL-18 and its receptor and provide rational guidance as to where to place potential agents in the IL18 molecule (see FIG. 3). IL1β and IL-18 have similar overall folds 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 Ca atoms of IL1β onto the Cα atoms of IL-18 to achieve an overall root mean square (r.m.s.) deviation of 7 Å. Based on this superposition, IL-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: 15-18, 22-27, 31-36, 128-131, and 145-148. On another proposed surface located on the other side of the molecule, the interface is lined by IL-18 residues: 3-8, 50-58 and 89-92. A third proposed surface is located between the previous two and includes residues 103-109 of the IL-18 molecule. This leaves residues 38-41, 67-70, 76-88, 117-120 and 140-142 in mIL-18 free from interactions with the receptor, and these residues are mostly solvent exposed and are potentially positions to attach a derivatization agent, such as a polyethyleneglycol molecule, whereas said agent does not compromise IL-18's binding to its receptor.

In a preferred embodiment, this invention relates to the crystal of murine IL-18, wherein said crystal effectively diffracts x-rays for the determination of the atomic coordinates of said murine IL-18 to a resolution of between about 1.3 Å and 5.0 Å. In a most particularly preferred embodiment, the resolution is between about 1.3 Å and 3.0 Å. In a most particularly preferred embodiment, the resolution of between about 1.3 Å and 2.5 Å.

Table I provides the atomic coordinates of the native murine IL-18. These coordinates were obtained using a model encompassing residues 1 to 152 in the crystallographic asymmetric unit. The amino acid sequence of the native murine IL-18 is provided in SEQ ID NO: 1. Residues 153-157 are not visible in the x-ray determined structure of the wild type molecule.

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, 392400. 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.

DESCRIPTION OF THE FIGURES

FIG. 1 provides a ribbon diagram of native murine IL-18 of this invention with the view taken perpendicular to 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-terminus and the color red at the C-terminus.

FIG. 2 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.

FIG. 3 provides a diagram where the mIL-18 model is superimposed on the IL1β-IL1 receptor complex. Murine IL-18 is drawn in a green line and the IL1β-IL1 complex is drawn in a yellow line as the cytokine and a red line as the receptor. This diagram suggests the manner in which mIL-18 binds its receptor and the amino acid interactions between the cytokine and the receptor.

MUTANTS AND DERIVATIVES

The invention further provides homologues, co-complexes, mutants and derivatives of the murine IL-18 crystal structure of the invention.

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

The term “homolog”, as used herein, means a protein having at least 30% amino acid sequence identity with a functional domain of murine 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.

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

The term “mutant”, as used herein, means the murine IL-18 polypeptide, i.e., a polypeptide displaying the biological activity of wild-type murine 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 murine IL-18 cDNA previously altered in its coding sequence by oligonucleotide-directed mutagenesis.

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

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.

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

Murine IL-18 mutants may also be generated by site-specific incorporation of unnatural amino acids into the murine 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 murine 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 murine IL-18 enzyme with the site-specific incorporated unnatural amino acid.

Selenocysteine or selenomethionine may be incorporated into wild-type or mutant cytokine by expression of murine 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.

The term “heavy atom derivative” refers to derivatives of murine IL-18 produced by chemically modifying a crystal of murine 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).

Methods of Identifying Agonist or Antagonists of the Novel Murine IL-18 Crystalline Structure

Another aspect of this invention involves a method for identifying agonists or antagonists of a murine IL-18 through the crystal structure described herein. The novel murine 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 murine IL-18; or non-competitive and bind to and inhibit IL-18 activity whether or not it is bound to the receptor.

One embodiment probes the murine 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 mIL-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 murine IL-18 agonist/antagonist activities.

Another embodiment screens small molecule databases computationally for chemical entities or compounds that can bind in whole, or in part, to murine IL-18 or murine IL-18 receptor, or both. This screening method and its utility are 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.

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.

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 Murine IL-18 Mutant C7S-Q37C from Escherichia coli

Murine proIL-18 was overexpressed in E. coli as a soluble protein with an N-terminal hexa His tag. ProIL-18 was purified with a Ni-NTA affinity column, followed by a DEAE-650M column. This purified proIL-18 was then cleaved to become mature IL-18 using caspase 1. The cleavage product was applied to a second Ni-NTA column and only the mature form of murine IL-18 flows through while the uncleaved proIL-18 is bound to the column. The mature IL-18 was further purified using a Superdex 75 column, from which it was eluted in the form of a monomer. This was followed by a high-resolution monoQ column so that the mature murine IL-18 was sufficiently pure for crystallography studies.

E. coli cells were suspended at 3 ml/g in 50 mM Tris (pH 8), 0.5M NaCl, 10 mM β-mercaptoethanol, 5% glycerol, 1 μg/ml pepstatin A, 1 μg/ml leupeptin, 0.4mM AEBSF. Cells were homogenized and then lysed at 12,000 psi with a microfluidizer (M110-Y, Microfluidics, Inc.). The cell lysate was then centrifuged at 30,000×g for 20 minutes. HexaHis tagged proIL-18 from the supernatant was applied to a Ni-NTA column (Qiagen, Inc.) in the presence of 5 mM imidazole. The Ni-NTA was extensively washed (more than 5 column volumes) with 50 mM Tris (pH 8), 0.5M NaCl, 10 mM β-mercaptoethanol and 5 mM imidazole. ProIL-18 was eluted from the column with 30 mM imidazole. The HexaHis proIL-18 in the Ni-NTA eluate was dialyzed against a buffer of 50 mM Tris (pH 8) and 10 mM β-mercaptoethanol. The dialyzed solution was then centrifuged at 30,000×g for 10 minutes and applied to a Toyopearl DEAE 650M column. HexaHis proIL-18 was eluted with a linear salt gradient of 0 to 0.5M NaCl in 25 mM HEPES (pH 8) and 10 mM β-Mercaptoethanol.

ProIL-18 was cleaved using caspase 1 to generate mature L-18 for 5.5 hours at room temperature at a weight ratio of ProIL 8:caspase 1=1:500. The cleaved mixture containing the pro-domain and uncleaved HexaHis proIL-18 were applied to a second Ni-NTA column, whereby the pro-domain and the uncleaved proIL-18 was captured. The flow through fractions containing mature IL-18 was concentrated and treated with 40 mM DTT at pH 8 for 2 hours. Thereafter, the mature L-18 solution was adjusted to pH 6 using 1M phosphoric acid. This solution was centrifuged at 30,000×g before it was applied to a Superdex 75 column equilibrated with 10 mM NaPi (pH 6) and 0.1M NaCl. The monomer peak from the Superdex 75 column eluate was pooled and further fractioned by a MonoQ HR 10/10 column. Mature L-18 was eluted with a linear salt gradient of 0 to 0.25M NaCl in 25 mM Tris (pH 7.5) and 5 mM β-Mercaptoethanol. Mature IL-18 was then pooled and dialyzed against a buffer of 25mM Tris (pH 7.5), 50 mM NaCl, 0.1 mM EDTA and 5 mM β-Mercaptoethanol and concentrated to 11 mg/ml.

The invention described herein provides a method for defining ligand interactions with L-18 and its receptor:

1.A. Effects of ligand binding upon enzyme intrinsic fluorescence 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 Murine IL-18

2.A. Crystallization

The murine IL-18 native crystals grew from sitting or hanging drops equilibrated through the vapor phase at room temperature with a reservoir of 500 μL reservoir solution containing 23-30% polyethylene glycol (PEG) 1500 in 1-6 weeks. The drops contained 2 μL of protein at 10-30 mg/ml in 50 mM NaCl, 25 mM Tris (pH 7.4), 0.1 mM EDTA and 2 μL reservoir solution. Form I crystals belong to the space group P2₁2₁2 with unit cell dimensions of a=71.3 Å, b=96.5 Å, c=50.8 Å with two molecules per asymmetric unit. Form II crystals belong to the space group P2₁2₁2₁ with unit cell dimensions a=36.0 Å, b=61.2 Å, c=65.3 Å and one molecule in the asymmetric unit.

The mutant murine IL-18 (C7S, Q37C) crystals grew from sitting or hanging drops equilibrated through the vapor phase at room temperature against a reservoir of 500 μL reservoir solution containing 18-30% polyethylene glycol (PEG) 1500 with 0 or 2-5 mM Tris (pH 8) in seven days. The drops contained 2 μL of protein at 10 mg/ml in 50 mM NaCl, 25 mM Tris (pH 7.5), 0.1 mM EDTA, 5 mM β-Mercaptoethanol and 2 μL reservoir solution. The crystals belong to the space group P2₁2₁2₁ with unit cell dimensions of a=36.0 Å, b=61.3 Å, c=65.3 Å and one copy of the murine IL-18 C7S, Q37C mutant protein in the asymmetric unit.

2.B. Heavy Atom Derivatization

Form I native crystal was used to form heavy atom derivatives. These heavy atoms provided weak derivatization and the data collected from them were used to resolve the native murine IL-18 structure. A saturated solution of MeHgCl was used to soak a crystal for 2 hours in the first derivative. A saturated solution of PCMB was used to soak a second crystal for 5 hrs in the second derivative. A saturated solution of Baker's dimercurial was used to soak a third crystal for 4 hrs in the third derivative.

2.C. X-ray Diffraction Data Collection

We collected data from the Form I native murine IL-18 crystal and the heavy atom derivative crystals (MeHgCl, pCMB and Baker's dimercurial) at room temperature on an R-axis image plate using x-rays generated by a Rigaku RU200 rotating anode. The data were then processed with an HKL program as described by Otwinowski, et al. in the Methods in Enzymology, 276:307-326, Carter, Jr. and Sweet, eds., Academic Press, New York.

The C7S-Q37C mutant crystals were soaked in a cryo-solution containing 80% reservoir solution and 20% ethylene glycol. A Form II mutant crystal was then suspended in a nylon loop and frozen under a nitrogen gas stream. Likewise, the Form II native crystal was suspended in a nylon loop, dipped in paratone-N oil and frozen under a nitrogen gas stream.

Data from the Form II native crystal and the mutant crystal were collected with a MAR CCD detector on beamline 17ID, the Advanced Photon Source at Argonne National Laboratory. The data were processed with HKL2000 as described by Otwinowski, in the Proceedings of the CCP4 Study Weekend: “Data Collection and Processing”, Daresbury, England (1993).

2.D. Structure Determination and Refinement

The crystal structure of murine IL-18 was determined by the heavy atom method using a computer program named SOLVE as described by Terwilliger, et al. in Acta Crystallogr. D 55:849-861 (1999). The structure of each derivative was determined individually and then in combination with the heavy atom information using phase combination. The resulting map was solvent flattened using a program named DM (CCP4, 1993). The backbone of the molecule was then incorporated into this electron density map using a program named XTALVIEW. McRee, Practical Protein Crystallography, Academic Press, San Diego (1993). This backbone provided a structural model for the murine protein in the deter. Using this model and molecular replacement program AmoRe (Navaza, Acta Cryst. A 50:157-163 (1994)), we determined that the Form II mutant IL-18 contains one monomer in the asymmetric unit. This structure was refined using ARP/wARP as described by Perrakis, et al. in Acta Cryst. D53, 448455 (1997) and further refined with a program named CNX (by Accelrys) to final R-factors of R=18.88% and R_free=21.37% for 29188 reflections at 1.35 Å resolution. The mutant murine IL-18 (C7S-Q37C) contains residues 1-157 and 243 water molecules.

Using the mutant structure as a search model, the structure of the Form II native crystal was determined by molecular replacement AmoRe. Like the Form II mutant crystals, the native Form II crystal coordinates were built using ARP/wARP and further refined using CNX to final R-factors of R=20.21% and R_free=23.96% for 20885 reflections at a resolution of 1.55 Å. The native murine IL-18 contain residues 1-152 and 230 water molecules. Table I lists the final coordinates of the native murine IL-18.

TABLE I
Atomic coordinates of the native murine IL-18 structure
1	CB	ASN	A	1	−9.865	20.729	−8.348	1.00	22.11
2	CG	ASN	A	1	−10.876	19.626	−8.175	1.00	25.16
3	OD1	ASN	A	1	−12.086	19.881	−8.154	1.00	26.62
4	ND2	ASN	A	1	−10.398	18.389	−8.061	1.00	24.23
5	C	ASN	A	1	−9.275	20.938	−5.896	1.00	18.24
6	O	ASN	A	1	−9.498	20.013	−5.125	1.00	17.59
7	N	ASN	A	1	−8.019	19.368	−7.404	1.00	20.53
8	CA	ASN	A	1	−8.739	20.674	−7.308	1.00	19.06
9	N	PHE	A	2	−9.460	22.217	−5.564	1.00	17.55
10	CA	PHE	A	2	−9.910	22.648	−4.242	1.00	16.07
11	CB	PHE	A	2	−8.914	23.651	−3.661	1.00	17.36
12	CG	PHE	A	2	−7.540	23.107	−3.461	1.00	13.98
13	CD1	PHE	A	2	−7.213	22.388	−2.295	1.00	14.03
14	CD2	PHE	A	2	−6.555	23.345	−4.405	1.00	14.18
15	CE1	PHE	A	2	−5.903	21.921	−2.083	1.00	11.11
16	CE2	PHE	A	2	−5.239	22.883	−4.206	1.00	12.74
17	CZ	PHE	A	2	−4.915	22.172	−3.040	1.00	12.98
18	C	PHE	A	2	−11.244	23.371	−4.332	1.00	17.48
19	O	PHE	A	2	−11.463	24.128	−5.275	1.00	20.98
20	N	GLY	A	3	−12.104	23.160	−3.346	1.00	16.12
21	CA	GLY	A	3	−13.402	23.824	−3.332	1.00	17.13
22	C	GLY	A	3	−13.526	24.559	−2.015	1.00	16.98
23	O	GLY	A	3	−13.316	23.967	−0.955	1.00	17.79
24	N	ARG	A	4	−13.889	25.836	−2.065	1.00	18.57
25	CA	ARG	A	4	−13.968	26.618	−0.840	1.00	17.15
26	CB	ARG	A	4	−14.078	28.099	−1.187	1.00	16.30
27	CG	ARG	A	4	−13.691	28.996	−0.022	1.00	17.00
28	CD	ARG	A	4	−13.838	30.429	−0.369	1.00	19.79
29	NE	ARG	A	4	−15.240	30.838	−0.372	1.00	21.81
30	CZ	ARG	A	4	−15.633	32.073	−0.650	1.00	25.07
31	NH1	ARG	A	4	−14.740	32.999	−0.954	1.00	23.73
32	NH2	ARG	A	4	−16.914	32.394	−0.572	1.00	27.29
33	C	ARG	A	4	−15.121	26.190	0.060	1.00	19.88
34	O	ARG	A	4	−16.243	25.991	−0.408	1.00	21.53
35	N	LEU	A	5	−14.828	26.027	1.346	1.00	19.15
36	CA	LEU	A	5	−15.816	25.620	2.340	1.00	20.48
37	CB	LEU	A	5	−15.292	24.429	3.165	1.00	22.10
38	CG	LEU	A	5	−14.905	23.191	2.324	1.00	24.19
39	CD1	LEU	A	5	−14.284	22.118	3.173	1.00	25.88
40	CD2	LEU	A	5	−16.135	22.654	1.632	1.00	25.55
41	C	LEU	A	5	−16.063	26.851	3.219	1.00	19.93
42	O	LEU	A	5	−16.131	27.964	2.698	1.00	24.40
43	N	HIS	A	6	−16.184	26.684	4.527	1.00	21.35
44	CA	HIS	A	6	−16.447	27.860	5.350	1.00	21.14
45	CB	HIS	A	6	−17.412	27.526	6.503	1.00	23.05
46	CG	HIS	A	6	−16.775	26.810	7.657	1.00	27.34
47	CD2	HIS	A	6	−16.361	27.264	8.866	1.00	27.83
48	ND1	HIS	A	6	−16.509	25.459	7.644	1.00	28.07
49	CE1	HIS	A	6	−15.962	25.108	8.796	1.00	30.59
50	NE2	HIS	A	6	−15.860	26.186	9.555	1.00	29.47
51	C	HIS	A	6	−15.194	28.505	5.908	1.00	21.75
52	O	HIS	A	6	−14.094	27.957	5.803	1.00	20.28
53	N	CYS	A	7	−15.361	29.693	6.480	1.00	20.13
54	CA	CYS	A	7	−14.221	30.384	7.067	1.00	19.41
55	CB	CYS	A	7	−13.979	31.755	6.406	1.00	20.20
56	SG	CYS	A	7	−15.383	32.948	6.489	1.00	22.66
57	C	CYS	A	7	−14.443	30.594	8.541	1.00	21.66
58	O	CYS	A	7	−15.559	30.503	9.037	1.00	21.74
59	N	THR	A	8	−13.335	30.827	9.232	1.00	18.67
60	CA	THR	A	8	−13.316	31.143	10.652	1.00	18.54
61	CB	THR	A	8	−12.817	29.988	11.513	1.00	18.35
62	OG1	THR	A	8	−11.560	29.526	11.015	1.00	22.80
63	CG2	THR	A	8	−13.831	28.849	11.509	1.00	21.68
64	C	THR	A	8	−12.302	32.266	10.719	1.00	17.98
65	O	THR	A	8	−11.605	32.542	9.741	1.00	17.69
66	N	THR	A	9	−12.223	32.943	11.849	1.00	18.04
67	CA	THR	A	9	−11.251	34.001	11.947	1.00	18.97
68	CB	THR	A	9	−11.883	35.369	12.261	1.00	21.56
69	OG1	THR	A	9	−12.507	35.334	13.547	1.00	23.78
70	CG2	THR	A	9	−12.907	35.739	11.199	1.00	22.25
71	C	THR	A	9	−10.303	33.622	13.055	1.00	19.38
72	O	THR	A	9	−10.655	32.881	13.976	1.00	19.63
73	N	ALA	A	10	−9.079	34.114	12.943	1.00	16.88
74	CA	ALA	A	10	−8.079	33.831	13.963	1.00	15.66
75	CB	ALA	A	10	−7.407	32.482	13.715	1.00	17.32
76	C	ALA	A	10	−7.024	34.893	13.962	1.00	14.99
77	O	ALA	A	10	−6.767	35.540	12.959	1.00	13.33
78	N	VAL	A	11	−6.410	35.065	15.118	1.00	14.32
79	CA	VAL	A	11	−5.290	35.971	15.264	1.00	14.19
80	CB	VAL	A	11	−5.375	36.764	16.559	1.00	14.11
81	CG1	VAL	A	11	−4.050	37.503	16.813	1.00	14.59
82	CG2	VAL	A	11	−6.525	37.758	16.456	1.00	14.05
83	C	VAL	A	11	−4.119	34.978	15.295	1.00	13.53
84	O	VAL	A	11	−4.154	33.954	16.005	1.00	15.49
85	N	ILE	A	12	−3.090	35.261	14.510	1.00	13.01
86	CA	ILE	A	12	−1.955	34.388	14.383	1.00	12.82
87	CB	ILE	A	12	−1.592	34.216	12.898	1.00	14.30
88	CG2	ILE	A	12	−0.335	33.410	12.746	1.00	14.56
89	CG1	ILE	A	12	−2.758	33.552	12.173	1.00	16.31
90	CD1	ILE	A	12	−2.482	33.278	10.719	1.00	16.85
91	C	ILE	A	12	−0.764	34.947	15.124	1.00	11.30
92	O	ILE	A	12	−0.408	36.118	14.952	1.00	12.05
93	N	ARG	A	13	−0.175	34.111	15.970	1.00	12.36
94	CA	ARG	A	13	1.005	34.540	16.709	1.00	10.15
95	CB	ARG	A	13	0.736	34.519	18.204	1.00	11.19
96	CG	ARG	A	13	−0.109	35.692	18.633	1.00	10.74
97	CD	ARG	A	13	−0.550	35.548	20.075	1.00	12.36
98	NE	ARG	A	13	−1.301	36.718	20.510	1.00	12.86
99	CZ	ARG	A	13	−2.614	36.859	20.390	1.00	13.50
100	NH1	ARG	A	13	−3.363	35.896	19.853	1.00	15.13
101	NH2	ARG	A	13	−3.177	37.988	20.821	1.00	14.39
102	C	ARG	A	13	2.190	33.651	16.383	1.00	12.82
103	O	ARG	A	13	2.052	32.431	16.208	1.00	11.19
104	N	ASN	A	14	3.353	34.264	16.270	1.00	11.57
105	CA	ASN	A	14	4.546	33.500	15.961	1.00	11.48
106	CB	ASN	A	14	5.595	34.334	15.210	1.00	12.45
107	CG	ASN	A	14	6.194	35.434	16.051	1.00	13.41
108	OD1	ASN	A	14	6.051	35.444	17.270	1.00	13.43
109	ND2	ASN	A	14	6.893	36.360	15.399	1.00	14.05
110	C	ASN	A	14	5.131	32.866	17.200	1.00	13.19
111	O	ASN	A	14	4.574	32.987	18.287	1.00	13.86
112	N	ILE	A	15	6.245	32.172	17.031	1.00	15.08
113	CA	ILE	A	15	6.867	31.464	18.145	1.00	17.72
114	CB	ILE	A	15	8.140	30.720	17.669	1.00	18.28
115	CG2	ILE	A	15	9.172	31.725	17.170	1.00	20.74
116	CG1	ILE	A	15	8.684	29.838	18.789	1.00	23.00
117	CD1	ILE	A	15	7.772	28.699	19.133	1.00	21.89
118	C	ILE	A	15	7.209	32.352	19.326	1.00	19.15
119	O	ILE	A	15	7.269	31.868	20.459	1.00	21.65
120	N	ASN	A	16	7.415	33.640	19.067	1.00	18.32
121	CA	ASN	A	16	7.758	34.584	20.130	1.00	18.96
122	CB	ASN	A	16	8.870	35.496	19.645	1.00	20.26
123	CG	ASN	A	16	10.149	34.725	19.382	1.00	23.71
124	OD1	ASN	A	16	10.899	35.029	18.464	1.00	25.03
125	ND2	ASN	A	16	10.393	33.703	20.200	1.00	24.94
126	C	ASN	A	16	6.557	35.372	20.620	1.00	18.55
127	O	ASN	A	16	6.696	36.409	21.267	1.00	20.18
128	N	ASP	A	17	5.374	34.864	20.285	1.00	15.80
129	CA	ASP	A	17	4.098	35.423	20.714	1.00	14.14
130	CB	ASP	A	17	4.084	35.544	22.247	1.00	19.26
131	CG	AASP	A	17	4.336	34.218	22.934	0.50	21.08
132	CG	BASP	A	17	2.745	35.196	22.839	0.50	19.49
133	OD1	AASP	A	17	3.690	33.226	22.557	0.50	21.91
134	OD1	BASP	A	17	1.982	34.434	22.201	0.50	22.80
135	OD2	AASP	A	17	5.174	34.168	23.855	0.50	23.89
136	OD2	BASP	A	17	2.469	35.663	23.966	0.50	24.36
137	C	ASP	A	17	3.715	36.761	20.086	1.00	14.47
138	O	ASP	A	17	2.844	37.477	20.585	1.00	16.52
139	N	GLN	A	18	4.380	37.086	18.992	1.00	13.41
140	CA	GLN	A	18	4.098	38.321	18.279	1.00	12.27
141	CB	GLN	A	18	5.314	38.749	17.483	1.00	12.96
142	CG	GLN	A	18	6.512	39.055	18.361	1.00	14.89
143	CD	GLN	A	18	7.732	39.329	17.565	1.00	16.33
144	OE1	GLN	A	18	8.081	38.567	16.673	1.00	16.77
145	NE2	GLN	A	18	8.413	40.438	17.880	1.00	19.49
146	C	GLN	A	18	2.917	38.095	17.358	1.00	13.10
147	O	GLN	A	18	2.763	37.027	16.772	1.00	12.70
148	N	VAL	A	19	2.096	39.126	17.220	1.00	12.22
149	CA	VAL	A	19	0.877	39.040	16.421	1.00	12.52
150	CB	AVAL	A	19	−0.166	40.030	17.019	0.50	11.54
151	CB	BVAL	A	19	−0.216	39.956	17.005	0.50	13.33
152	CG1	AVAL	A	19	−1.337	40.222	16.080	0.50	12.35
153	CG1	BVAL	A	19	0.270	41.372	17.005	0.50	14.39
154	CG2	AVAL	A	19	−0.616	39.541	18.387	0.50	9.67
155	CG2	BVAL	A	19	−1.501	39.832	16.203	0.50	16.45
156	C	VAL	A	19	1.121	39.406	14.953	1.00	12.96
157	O	VAL	A	19	1.803	40.396	14.664	1.00	12.90
158	N	LEU	A	20	0.578	38.596	14.040	1.00	11.20
159	CA	LEU	A	20	0.674	38.894	12.607	1.00	9.98
160	CB	LEU	A	20	0.178	37.689	11.789	1.00	11.57
161	CG	LEU	A	20	0.179	37.923	10.290	1.00	11.32
162	CD1	LEU	A	20	1.585	38.347	9.781	1.00	13.05
163	CD2	LEU	A	20	−0.234	36.609	9.671	1.00	12.15
164	C	LEU	A	20	−0.237	40.119	12.397	1.00	12.64
165	O	LEU	A	20	−1.417	40.097	12.714	1.00	11.62
166	N	PHE	A	21	0.340	41.177	11.845	1.00	13.85
167	CA	PHE	A	21	−0.349	42.452	11.631	1.00	12.63
168	CB	PHE	A	21	0.342	43.505	12.500	1.00	13.71
169	CG	PHE	A	21	−0.409	44.797	12.664	1.00	15.44
170	CD1	PHE	A	21	−0.460	45.735	11.632	1.00	18.36
171	CD2	PHE	A	21	−0.992	45.109	13.894	1.00	16.04
172	CE1	PHE	A	21	−1.078	46.976	11.824	1.00	19.58
173	CE2	PHE	A	21	−1.619	46.347	14.102	1.00	18.12
174	CZ	PHE	A	21	−1.664	47.284	13.068	1.00	16.49
175	C	PHE	A	21	−0.167	42.772	10.160	1.00	12.86
176	O	PHE	A	21	0.949	43.059	9.732	1.00	15.40
177	N	VAL	A	22	−1.254	42.720	9.388	1.00	12.83
178	CA	VAL	A	22	−1.175	42.969	7.945	1.00	13.23
179	CB	VAL	A	22	−1.914	41.861	7.160	1.00	11.71
180	CG1	VAL	A	22	−1.639	42.007	5.668	1.00	11.83
181	CG2	VAL	A	22	−1.501	40.470	7.664	1.00	12.72
182	C	VAL	A	22	−1.825	44.310	7.648	1.00	13.64
183	O	VAL	A	22	−3.051	44.409	7.588	1.00	13.52
184	N	ASP	A	23	−1.003	45.339	7.463	1.00	15.46
185	CA	ASP	A	23	−1.508	46.684	7.216	1.00	15.25
186	CB	ASP	A	23	−0.786	47.654	8.163	1.00	16.03
187	CG	ASP	A	23	−1.477	48.994	8.286	1.00	21.45
188	OD1	ASP	A	23	−2.623	49.149	7.822	1.00	20.42
189	OD2	ASP	A	23	−0.849	49.898	8.876	1.00	23.14
190	C	ASP	A	23	−1.242	47.044	5.758	1.00	16.45
191	O	ASP	A	23	−0.096	47.019	5.312	1.00	16.34
192	N	LYS	A	24	−2.313	47.372	5.045	1.00	18.40
193	CA	LYS	A	24	−2.237	47.711	3.624	1.00	20.51
194	CB	LYS	A	24	−1.612	49.091	3.417	1.00	23.94
195	CG	LYS	A	24	−2.485	50.255	3.888	1.00	27.86
196	CD	ALYS	A	24	−2.967	50.108	5.314	0.50	27.38
197	CD	BLYS	A	24	−1.724	51.580	3.810	0.50	28.39
198	CE	ALYS	A	24	−3.823	51.299	5.739	0.50	27.92
199	CE	BLYS	A	24	−2.476	52.710	4.509	0.50	28.38
200	NZ	ALYS	A	24	−4.368	51.137	7.117	0.50	24.39
201	NZ	BLYS	A	24	−1.702	53.988	4.536	0.50	30.10
202	C	LYS	A	24	−1.418	46.629	2.935	1.00	20.07
203	O	LYS	A	24	−0.419	46.891	2.246	1.00	21.56
204	N	ARG	A	25	−1.845	45.397	3.195	1.00	19.53
205	CA	ARG	A	25	−1.271	44.185	2.620	1.00	17.88
206	CB	ARG	A	25	−1.501	44.223	1.103	1.00	20.64
207	CG	ARG	A	25	−2.965	44.456	0.781	1.00	21.58
208	CD	ARG	A	25	−3.298	44.248	−0.692	1.00	26.78
209	NE	ARG	A	25	−2.751	45.280	−1.560	1.00	31.19
210	CZ	ARG	A	25	−1.867	45.053	−2.530	1.00	35.33
211	NH1	ARG	A	25	−1.417	43.826	−2.753	1.00	34.83
212	NH2	ARG	A	25	−1.452	46.054	−3.299	1.00	35.49
213	C	ARG	A	25	0.183	43.858	2.951	1.00	17.97
214	O	ARG	A	25	0.772	42.946	2.369	1.00	17.05
215	N	GLN	A	26	0.766	44.577	3.905	1.00	16.87
216	CA	GLN	A	26	2.148	44.318	4.287	1.00	16.96
217	CB	GLN	A	26	2.912	45.631	4.485	1.00	20.86
218	CG	GLN	A	26	2.983	46.507	3.247	1.00	23.99
219	CD	GLN	A	26	3.629	45.794	2.089	1.00	25.42
220	OE1	GLN	A	26	4.611	45.067	2.264	1.00	29.88
221	NE2	GLN	A	26	3.092	45.998	0.905	1.00	27.56
222	C	GLN	A	26	2.119	43.567	5.610	1.00	17.72
223	O	GLN	A	26	1.723	44.128	6.629	1.00	18.68
224	N	PRO	A	27	2.528	42.296	5.606	1.00	16.31
225	CD	PRO	A	27	2.886	41.451	4.455	1.00	16.37
226	CA	PRO	A	27	2.519	41.519	6.845	1.00	17.06
227	CB	PRO	A	27	2.374	40.104	6.343	1.00	16.90
228	CG	PRO	A	27	3.228	40.131	5.106	1.00	17.58
229	C	PRO	A	27	3.786	41.694	7.652	1.00	18.72
230	O	PRO	A	27	4.884	41.746	7.096	1.00	22.96
231	N	VAL	A	28	3.629	41.832	8.962	1.00	15.03
232	CA	VAL	A	28	4.761	41.927	9.860	1.00	14.94
233	CB	VAL	A	28	5.211	43.383	10.078	1.00	16.40
234	CG1	VAL	A	28	5.445	44.053	8.721	1.00	20.59
235	CG2	VAL	A	28	4.202	44.144	10.876	1.00	18.71
236	C	VAL	A	28	4.267	41.355	11.182	1.00	14.92
237	O	VAL	A	28	3.059	41.221	11.390	1.00	15.52
238	N	PHE	A	29	5.188	40.971	12.056	1.00	13.35
239	CA	PHE	A	29	4.786	40.494	13.369	1.00	13.87
240	CB	PHE	A	29	5.525	39.216	13.717	1.00	13.00
241	CG	PHE	A	29	5.075	38.042	12.917	1.00	11.79
242	CD1	PHE	A	29	3.991	37.260	13.347	1.00	13.09
243	CD2	PHE	A	29	5.711	37.729	11.719	1.00	12.43
244	CE1	PHE	A	29	3.545	36.178	12.583	1.00	12.68
245	CE2	PHE	A	29	5.273	36.647	10.956	1.00	13.02
246	CZ	PHE	A	29	4.183	35.869	11.388	1.00	12.83
247	C	PHE	A	29	5.115	41.589	14.369	1.00	12.75
248	O	PHE	A	29	6.179	42.215	14.275	1.00	15.29
249	N	GLU	A	30	4.203	41.817	15.309	1.00	13.51
250	CA	GLU	A	30	4.351	42.861	16.327	1.00	14.32
251	CB	GLU	A	30	3.262	43.907	16.152	1.00	18.01
252	CG	GLU	A	30	3.320	44.616	14.859	1.00	20.70
253	CD	GLU	A	30	4.230	45.806	14.942	1.00	23.57
254	OE1	GLU	A	30	5.034	45.885	15.906	1.00	26.17
255	OE2	GLU	A	30	4.148	46.662	14.050	1.00	26.38
256	C	GLU	A	30	4.200	42.356	17.731	1.00	15.20
257	O	GLU	A	30	3.391	41.479	17.980	1.00	15.87
258	N	ASP	A	31	4.946	42.931	18.667	1.00	16.69
259	CA	ASP	A	31	4.777	42.540	20.049	1.00	17.47
260	CB	ASP	A	31	5.833	43.182	20.954	1.00	20.86
261	CG	ASP	A	31	7.232	42.715	20.636	1.00	25.47
262	OD1	ASP	A	31	7.419	41.517	20.337	1.00	26.85
263	OD2	ASP	A	31	8.159	43.546	20.704	1.00	33.31
264	C	ASP	A	31	3.423	43.079	20.427	1.00	15.46
265	O	ASP	A	31	3.058	44.197	20.041	1.00	15.35
266	N	MET	A	32	2.674	42.296	21.181	1.00	14.56
267	CA	MET	A	32	1.345	42.681	21.610	1.00	15.04
268	CB	MET	A	32	0.755	41.574	22.466	1.00	19.75
269	CG	MET	A	32	0.302	40.406	21.633	1.00	22.06
270	SD	MET	A	32	−0.501	39.183	22.659	1.00	29.43
271	CE	MET	A	32	0.859	38.149	22.940	1.00	27.59
272	C	MET	A	32	1.331	43.988	22.384	1.00	15.28
273	O	MET	A	32	0.398	44.758	22.276	1.00	19.59
274	N	THR	A	33	2.377	44.221	23.162	1.00	16.47
275	CA	THR	A	33	2.437	45.443	23.960	1.00	16.94
276	CB	THR	A	33	3.638	45.450	24.942	1.00	14.34
277	OG1	THR	A	33	4.846	45.277	24.207	1.00	17.85
278	CG2	THR	A	33	3.518	44.350	25.983	1.00	19.59
279	C	THR	A	33	2.574	46.696	23.115	1.00	17.33
280	O	THR	A	33	2.253	47.797	23.592	1.00	18.77
281	N	ASP	A	34	3.034	46.532	21.874	1.00	16.12
282	CA	ASP	A	34	3.284	47.667	20.993	1.00	16.46
283	CB	ASP	A	34	4.489	47.386	20.107	1.00	18.70
284	CG	ASP	A	34	5.755	47.178	20.907	1.00	21.90
285	OD1	ASP	A	34	5.709	47.403	22.134	1.00	26.20
286	OD2	ASP	A	34	6.782	46.800	20.307	1.00	26.01
287	C	ASP	A	34	2.154	48.106	20.115	1.00	16.97
288	O	ASP	A	34	2.267	49.132	19.458	1.00	17.02
289	N	ILE	A	35	1.077	47.342	20.097	1.00	15.54
290	CA	ILE	A	35	−0.065	47.694	19.264	1.00	14.41
291	CB	ILE	A	35	−0.300	46.627	18.156	1.00	17.77
292	CG2	ILE	A	35	0.908	46.541	17.234	1.00	18.36
293	CG1	ILE	A	35	−0.623	45.273	18.806	1.00	17.07
294	CD1	ILE	A	35	−1.004	44.179	17.795	1.00	19.32
295	C	ILE	A	35	−1.340	47.745	20.084	1.00	16.21
296	O	ILE	A	35	−1.392	47.254	21.214	1.00	15.80
297	N	ASP	A	36	−2.373	48.350	19.520	1.00	14.90
298	CA	ASP	A	36	−3.677	48.332	20.151	1.00	16.77
299	CB	ASP	A	36	−4.351	49.700	20.103	1.00	16.16
300	CG	ASP	A	36	−5.771	49.647	20.617	1.00	19.51
301	OD1	ASP	A	36	−6.328	48.531	20.692	1.00	20.01
302	OD2	ASP	A	36	−6.347	50.704	20.934	1.00	18.76
303	C	ASP	A	36	−4.428	47.351	19.247	1.00	16.91
304	O	ASP	A	36	−4.926	47.720	18.172	1.00	17.46
305	N	GLN	A	37	−4.503	46.095	19.663	1.00	20.31
306	CA	GLN	A	37	−5.158	45.105	18.831	1.00	19.91
307	CB	GLN	A	37	−5.006	43.721	19.445	1.00	21.24
308	CG	GLN	A	37	−5.470	42.599	18.543	1.00	24.10
309	CD	GLN	A	37	−5.389	41.265	19.256	1.00	24.17
310	OE1	GLN	A	37	−4.324	40.874	19.741	1.00	26.60
311	NE2	GLN	A	37	−6.514	40.567	19.332	1.00	25.48
312	C	GLN	A	37	−6.625	45.386	18.567	1.00	19.67
313	O	GLN	A	37	−7.129	45.130	17.465	1.00	20.86
314	N	SER	A	38	−7.326	45.924	19.559	1.00	19.52
315	CA	SER	A	38	−8.738	46.210	19.359	1.00	20.61
316	CB	SER	A	38	−9.375	46.654	20.679	1.00	23.23
317	OG	SER	A	38	−8.960	47.968	21.022	1.00	26.19
318	C	SER	A	38	−8.967	47.266	18.281	1.00	19.57
319	O	SER	A	38	−10.029	47.308	17.665	1.00	21.18
320	N	ALA	A	39	−7.961	48.107	18.031	1.00	18.48
321	CA	ALA	A	39	−8.094	49.155	17.023	1.00	17.27
322	CB	ALA	A	39	−7.388	50.428	17.488	1.00	16.51
323	C	ALA	A	39	−7.499	48.704	15.702	1.00	18.81
324	O	ALA	A	39	−7.425	49.471	14.753	1.00	19.79
325	N	SER	A	40	−7.072	47.450	15.668	1.00	18.59
326	CA	SER	A	40	−6.424	46.887	14.499	1.00	18.28
327	CB	SER	A	40	−4.967	46.623	14.839	1.00	20.22
328	OG	SER	A	40	−4.368	47.772	15.419	1.00	18.89
329	C	SER	A	40	−7.060	45.585	14.042	1.00	18.60
330	O	SER	A	40	−6.343	44.686	13.614	1.00	16.43
331	N	GLU	A	41	−8.383	45.490	14.127	1.00	18.44
332	CA	GLU	A	41	−9.087	44.268	13.735	1.00	19.57
333	CB	GLU	A	41	−10.594	44.442	13.990	1.00	21.67
334	CG	GLU	A	41	−11.469	43.215	13.708	1.00	26.29
335	CD	GLU	A	41	−11.811	43.001	12.219	1.00	29.17
336	OE1	GLU	A	41	−11.880	43.974	11.420	1.00	30.03
337	OE2	GLU	A	41	−12.037	41.831	11.850	1.00	31.07
338	C	GLU	A	41	−8.856	43.812	12.299	1.00	18.24
339	O	GLU	A	41	−8.517	42.641	12.064	1.00	16.26
340	N	PRO	A	42	−9.022	44.709	11.313	1.00	18.25
341	CD	PRO	A	42	−9.497	46.104	11.388	1.00	19.11
342	CA	PRO	A	42	−8.815	44.313	9.915	1.00	18.20
343	CB	PRO	A	42	−9.054	45.612	9.145	1.00	20.60
344	CG	PRO	A	42	−10.075	46.308	9.984	1.00	19.63
345	C	PRO	A	42	−7.418	43.783	9.649	1.00	18.52
346	O	PRO	A	42	−7.215	42.941	8.771	1.00	20.18
347	N	GLN	A	43	−6.459	44.278	10.421	1.00	16.41
348	CA	GLN	A	43	−5.061	43.911	10.243	1.00	14.34
349	CB	GLN	A	43	−4.150	45.062	10.682	1.00	15.38
350	CG	GLN	A	43	−4.308	46.351	9.895	1.00	15.32
351	CD	GLN	A	43	−5.633	47.029	10.107	1.00	16.71
352	OE1	GLN	A	43	−6.227	46.916	11.172	1.00	17.99
353	NE2	GLN	A	43	−6.096	47.764	9.107	1.00	18.35
354	C	GLN	A	43	−4.609	42.673	10.996	1.00	13.64
355	O	GLN	A	43	−3.582	42.110	10.671	1.00	13.77
356	N	THR	A	44	−5.362	42.278	12.015	1.00	11.95
357	CA	THR	A	44	−4.967	41.137	12.836	1.00	12.27
358	CB	THR	A	44	−4.718	41.558	14.305	1.00	13.41
359	OG1	THR	A	44	−5.899	42.144	14.865	1.00	15.65
360	CG2	THR	A	44	−3.568	42.546	14.366	1.00	14.79
361	C	THR	A	44	−5.922	39.964	12.848	1.00	12.84
362	O	THR	A	44	−5.547	38.861	13.248	1.00	12.74
363	N	ARG	A	45	−7.160	40.189	12.425	1.00	13.15
364	CA	ARG	A	45	−8.113	39.098	12.416	1.00	16.60
365	CB	ARG	A	45	−9.502	39.629	12.739	1.00	18.42
366	CG	ARG	A	45	−10.545	38.550	12.897	1.00	24.87
367	CD	ARG	A	45	−11.814	39.145	13.480	1.00	26.48
368	NE	ARG	A	45	−11.617	39.596	14.855	1.00	29.29
369	CZ	ARG	A	45	−12.495	40.327	15.545	1.00	29.33
370	NH1	ARG	A	45	−13.637	40.705	14.983	1.00	29.91
371	NH2	ARG	A	45	−12.247	40.651	16.811	1.00	27.73
372	C	ARG	A	45	−8.066	38.458	11.042	1.00	16.09
373	O	ARG	A	45	−8.691	38.932	10.097	1.00	18.98
374	N	LEU	A	46	−7.294	37.395	10.926	1.00	13.35
375	CA	LEU	A	46	−7.138	36.694	9.659	1.00	15.38
376	CB	LEU	A	46	−5.919	35.765	9.726	1.00	16.55
377	CG	LEU	A	46	−4.529	36.358	9.438	1.00	18.84
378	CD1	LEU	A	46	−4.313	36.464	7.954	1.00	19.37
379	CD2	LEU	A	46	−4.381	37.731	10.076	1.00	16.64
380	C	LEU	A	46	−8.381	35.875	9.389	1.00	15.61
381	O	LEU	A	46	−8.950	35.272	10.292	1.00	16.43
382	N	ILE	A	47	−8.803	35.869	8.128	1.00	14.86
383	CA	ILE	A	47	−9.958	35.101	7.706	1.00	14.41
384	CB	ILE	A	47	−10.788	35.897	6.685	1.00	15.54
385	CG2	ILE	A	47	−11.880	35.029	6.102	1.00	15.91
386	CG1	ILE	A	47	−11.376	37.130	7.398	1.00	18.38
387	CD1	ILE	A	47	−11.678	38.302	6.515	1.00	22.09
388	C	ILE	A	47	−9.392	33.828	7.084	1.00	14.94
389	O	ILE	A	47	−8.687	33.874	6.073	1.00	16.17
390	N	ILE	A	48	−9.687	32.699	7.705	1.00	13.61
391	CA	ILE	A	48	−9.159	31.440	7.226	1.00	12.55
392	CB	ILE	A	48	−8.475	30.699	8.373	1.00	14.43
393	CG2	ILE	A	48	−7.960	29.350	7.893	1.00	16.30
394	CG1	ILE	A	48	−7.367	31.606	8.953	1.00	17.50
395	CD1	ILE	A	48	−6.592	30.997	10.062	1.00	22.06
396	C	ILE	A	48	−10.241	30.571	6.628	1.00	13.80
397	O	ILE	A	48	−11.134	30.099	7.338	1.00	15.75
398	N	TYR	A	49	−10.178	30.393	5.317	1.00	13.63
399	CA	TYR	A	49	−11.151	29.537	4.653	1.00	13.80
400	CB	TYR	A	49	−11.479	30.033	3.235	1.00	15.93
401	CG	TYR	A	49	−12.604	31.032	3.180	1.00	16.52
402	CD1	TYR	A	49	−13.934	30.610	3.114	1.00	18.44
403	CE1	TYR	A	49	−14.972	31.533	3.031	1.00	19.03
404	CD2	TYR	A	49	−12.335	32.397	3.172	1.00	16.27
405	CE2	TYR	A	49	−13.377	33.339	3.092	1.00	19.45
406	CZ	TYR	A	49	−14.688	32.891	3.019	1.00	20.98
407	OH	TYR	A	49	−15.716	33.813	2.935	1.00	21.87
408	C	TYR	A	49	−10.604	28.134	4.513	1.00	14.64
409	O	TYR	A	49	−9.444	27.935	4.116	1.00	13.90
410	N	MET	A	50	−11.443	27.170	4.855	1.00	15.66
411	CA	MET	A	50	−11.123	25.765	4.698	1.00	15.50
412	CB	MET	A	50	−11.975	24.921	5.636	1.00	18.56
413	CG	MET	A	50	−11.541	24.956	7.077	1.00	21.58
414	SD	MET	A	50	−12.663	23.992	8.081	1.00	27.12
415	CE	MET	A	50	−12.298	22.355	7.561	1.00	22.95
416	C	MET	A	50	−11.508	25.400	3.266	1.00	17.81
417	O	MET	A	50	−12.481	25.931	2.721	1.00	18.06
418	N	TYR	A	51	−10.750	24.502	2.658	1.00	15.81
419	CA	TYR	A	51	−11.045	24.035	1.303	1.00	15.35
420	CB	TYR	A	51	−9.964	24.465	0.295	1.00	14.24
421	CG	TYR	A	51	−10.075	25.894	−0.177	1.00	14.38
422	CD1	TYR	A	51	−9.771	26.957	0.665	1.00	14.26
423	CE1	TYR	A	51	−9.907	28.274	0.242	1.00	15.84
424	CD2	TYR	A	51	−10.517	26.189	−1.473	1.00	13.13
425	CE2	TYR	A	51	−10.655	27.505	−1.917	1.00	14.07
426	CZ	TYR	A	51	−10.347	28.553	−1.044	1.00	14.00
427	OH	TYR	A	51	−10.464	29.843	−1.493	1.00	15.60
428	C	TYR	A	51	−11.065	22.519	1.300	1.00	18.24
429	O	TYR	A	51	−10.354	21.878	2.080	1.00	18.55
430	N	LYS	A	52	−11.896	21.964	0.425	1.00	18.07
431	CA	LYS	A	52	−11.943	20.534	0.220	1.00	18.12
432	CB	LYS	A	52	−13.300	20.099	−0.359	1.00	20.55
433	CG	LYS	A	52	−13.261	18.680	−0.935	1.00	23.64
434	CD	LYS	A	52	−14.592	18.298	−1.534	1.00	24.82
435	CE	LYS	A	52	−14.548	16.879	−2.067	1.00	28.40
436	NZ	LYS	A	52	−13.634	16.776	−3.222	1.00	31.95
437	C	LYS	A	52	−10.848	20.302	−0.825	1.00	18.51
438	O	LYS	A	52	−10.754	21.023	−1.818	1.00	19.93
439	N	ASP	A	53	−10.010	19.300	−0.588	1.00	17.99
440	CA	ASP	A	53	−8.912	18.963	−1.490	1.00	14.95
441	CB	ASP	A	53	−7.618	18.868	−0.677	1.00	15.86
442	CG	ASP	A	53	−6.429	18.361	−1.477	1.00	13.89
443	OD1	ASP	A	53	−6.400	18.411	−2.730	1.00	14.82
444	OD2	ASP	A	53	−5.459	17.912	−0.838	1.00	15.61
445	C	ASP	A	53	−9.214	17.623	−2.143	1.00	16.55
446	O	ASP	A	53	−9.422	16.638	−1.446	1.00	18.70
447	N	SER	A	54	−9.244	17.589	−3.473	1.00	17.52
448	CA	SER	A	54	−9.535	16.342	−4.163	1.00	18.31
449	CB	SER	A	54	−9.570	16.561	−5.678	1.00	14.96
450	OG	SER	A	54	−8.297	16.938	−6.182	1.00	19.31
451	C	SER	A	54	−8.518	15.273	−3.810	1.00	18.78
452	O	SER	A	54	−8.845	14.080	−3.816	1.00	21.77
453	N	GLU	A	55	−7.302	15.692	−3.481	1.00	17.60
454	CA	GLU	A	55	−6.253	14.752	−3.130	1.00	18.32
455	CB	GLU	A	55	−4.880	15.300	−3.523	1.00	22.79
456	CG	GLU	A	55	−4.596	15.218	−5.008	1.00	28.65
457	CD	GLU	A	55	−4.652	13.784	−5.491	1.00	32.26
458	OE1	GLU	A	55	−5.548	13.478	−6.307	1.00	34.10
459	OE2	GLU	A	55	−3.812	12.964	−5.034	1.00	35.46
460	C	GLU	A	55	−6.256	14.403	−1.656	1.00	17.26
461	O	GLU	A	55	−5.428	13.619	−1.237	1.00	19.07
462	N	VAL	A	56	−7.187	14.973	−0.882	1.00	17.06
463	CA	VAL	A	56	−7.297	14.696	0.553	1.00	16.58
464	CB	AVAL	A	56	−7.984	13.341	0.804	0.50	17.64
465	CB	BVAL	A	56	−7.962	13.322	0.796	0.50	15.94
466	CG1	AVAL	A	56	−9.322	13.290	0.088	0.50	17.39
467	CG1	BVAL	A	56	−8.523	13.266	2.213	0.50	14.65
468	CG2	AVAL	A	56	−7.111	12.237	0.336	0.50	19.35
469	CG2	BVAL	A	56	−9.067	13.083	−0.231	0.50	14.51
470	C	VAL	A	56	−5.926	14.712	1.249	1.00	17.26
471	O	VAL	A	56	−5.538	13.771	1.957	1.00	18.42
472	N	ARG	A	57	−5.178	15.791	1.041	1.00	15.87
473	CA	ARG	A	57	−3.853	15.911	1.646	1.00	15.65
474	CB	ARG	A	57	−2.925	16.717	0.748	1.00	17.60
475	CG	ARG	A	57	−2.380	15.940	−0.414	1.00	19.60
476	CD	ARG	A	57	−1.780	16.874	−1.422	1.00	19.85
477	NE	ARG	A	57	−2.848	17.626	−2.066	1.00	23.12
478	CZ	ARG	A	57	−2.672	18.496	−3.049	1.00	26.23
479	NH1	ARG	A	57	−1.456	18.749	−3.511	1.00	23.53
480	NH2	ARG	A	57	−3.730	19.077	−3.599	1.00	22.31
481	C	ARG	A	57	−3.886	16.541	3.020	1.00	16.15
482	O	ARG	A	57	−2.849	16.649	3.673	1.00	18.57
483	N	GLY	A	58	−5.068	16.951	3.460	1.00	14.70
484	CA	GLY	A	58	−5.183	17.544	4.779	1.00	17.17
485	C	GLY	A	58	−6.057	18.784	4.898	1.00	17.08
486	O	GLY	A	58	−7.023	18.997	4.143	1.00	17.15
487	N	LEU	A	59	−5.712	19.617	5.873	1.00	15.26
488	CA	LEU	A	59	−6.477	20.816	6.153	1.00	16.29
489	CB	LEU	A	59	−6.341	21.198	7.629	1.00	21.79
490	CG	LEU	A	59	−6.681	20.100	8.634	1.00	25.86
491	CD1	LEU	A	59	−6.255	20.536	10.043	1.00	28.61
492	CD2	LEU	A	59	−8.165	19.799	8.572	1.00	29.27
493	C	LEU	A	59	−6.014	21.943	5.278	1.00	16.23
494	O	LEU	A	59	−5.156	22.737	5.653	1.00	15.43
495	N	ALA	A	60	−6.583	21.999	4.086	1.00	13.19
496	CA	ALA	A	60	−6.239	23.024	3.120	1.00	13.34
497	CB	ALA	A	60	−6.709	22.585	1.734	1.00	13.93
498	C	ALA	A	60	−6.921	24.318	3.490	1.00	14.71
499	O	ALA	A	60	−8.139	24.348	3.708	1.00	13.73
500	N	VAL	A	61	−6.149	25.401	3.543	1.00	12.02
501	CA	VAL	A	61	−6.706	26.690	3.868	1.00	11.97
502	CB	VAL	A	61	−6.482	27.058	5.390	1.00	11.44
503	CG1	VAL	A	61	−7.091	26.025	6.307	1.00	13.57
504	CG2	VAL	A	61	−4.945	27.222	5.686	1.00	13.14
505	C	VAL	A	61	−6.094	27.827	3.074	1.00	11.99
506	O	VAL	A	61	−5.007	27.698	2.474	1.00	10.58
507	N	THR	A	62	−6.829	28.944	3.054	1.00	11.02
508	CA	THR	A	62	−6.320	30.185	2.499	1.00	10.68
509	CB	THR	A	62	−7.176	30.812	1.375	1.00	11.49
510	OG1	THR	A	62	−8.524	30.963	1.817	1.00	13.86
511	CG2	THR	A	62	−7.110	29.954	0.099	1.00	13.14
512	C	THR	A	62	−6.369	31.133	3.688	1.00	11.80
513	O	THR	A	62	−7.126	30.916	4.635	1.00	13.19
514	N	LEU	A	63	−5.550	32.166	3.629	1.00	11.94
515	CA	LEU	A	63	−5.485	33.166	4.687	1.00	11.08
516	CB	LEU	A	63	−4.094	33.159	5.355	1.00	13.09
517	CG	LEU	A	63	−3.809	32.100	6.426	1.00	17.87
518	CD1	LEU	A	63	−3.856	30.734	5.857	1.00	20.69
519	CD2	LEU	A	63	−2.453	32.365	7.057	1.00	17.94
520	C	LEU	A	63	−5.718	34.521	4.041	1.00	11.67
521	O	LEU	A	63	−5.040	34.866	3.078	1.00	11.40
522	N	SER	A	64	−6.686	35.282	4.553	1.00	11.74
523	CA	SER	A	64	−6.971	36.604	4.008	1.00	10.59
524	CB	SER	A	64	−8.279	36.589	3.214	1.00	13.51
525	OG	SER	A	64	−8.268	35.614	2.202	1.00	13.18
526	C	SER	A	64	−7.168	37.639	5.109	1.00	12.92
527	O	SER	A	64	−7.307	37.289	6.256	1.00	12.84
528	N	VAL	A	65	−7.150	38.908	4.724	1.00	14.38
529	CA	VAL	A	65	−7.456	39.992	5.662	1.00	15.02
530	CB	VAL	A	65	−6.258	40.886	6.016	1.00	17.78
531	CG1	VAL	A	65	−5.343	40.128	6.952	1.00	17.73
532	CG2	VAL	A	65	−5.544	41.350	4.780	1.00	18.38
533	C	VAL	A	65	−8.490	40.814	4.918	1.00	16.31
534	O	VAL	A	65	−8.463	40.911	3.692	1.00	17.00
535	N	LYS	A	66	−9.408	41.401	5.662	1.00	17.79
536	CA	LYS	A	66	−10.451	42.184	5.051	1.00	18.90
537	CB	LYS	A	66	−11.802	41.576	5.435	1.00	20.44
538	CG	LYS	A	66	−13.039	42.410	5.113	1.00	23.51
539	CD	LYS	A	66	−13.148	42.708	3.642	1.00	28.98
540	CE	LYS	A	66	−14.414	43.512	3.375	1.00	30.87
541	NZ	LYS	A	66	−15.582	42.846	4.020	1.00	35.82
542	C	LYS	A	66	−10.341	43.628	5.506	1.00	21.57
543	O	LYS	A	66	−10.506	43.928	6.681	1.00	21.71
544	N	ASP	A	67	−9.996	44.504	4.574	1.00	24.49
545	CA	ASP	A	67	−9.925	45.933	4.855	1.00	28.29
546	CB	ASP	A	67	−8.745	46.569	4.113	1.00	33.32
547	CG	ASP	A	67	−8.227	47.848	4.797	1.00	38.19
548	OD1	ASP	A	67	−7.180	48.360	4.327	1.00	40.49
549	OD2	ASP	A	67	−8.846	48.341	5.789	1.00	38.08
550	C	ASP	A	67	−11.256	46.338	4.229	1.00	30.38
551	O	ASP	A	67	−12.322	45.957	4.730	1.00	33.54
552	N	SER	A	68	−11.223	47.075	3.131	1.00	29.94
553	CA	SER	A	68	−12.482	47.428	2.478	1.00	29.05
554	CB	SER	A	68	−12.290	48.614	1.533	1.00	30.55
555	OG	SER	A	68	−13.521	48.968	0.924	1.00	31.57
556	C	SER	A	68	−12.837	46.175	1.689	1.00	28.80
557	O	SER	A	68	−13.994	45.766	1.586	1.00	28.69
558	N	LYS	A	69	−11.815	45.571	1.111	1.00	27.30
559	CA	LYS	A	69	−12.024	44.354	0.374	1.00	27.76
560	CB	LYS	A	69	−11.838	44.582	−1.129	1.00	29.95
561	CG	LYS	A	69	−10.524	45.197	−1.551	1.00	31.83
562	CD	LYS	A	69	−10.740	46.148	−2.748	1.00	34.15
563	CE	LYS	A	69	−11.716	45.593	−3.800	1.00	35.45
564	NZ	LYS	A	69	−11.122	44.605	−4.752	1.00	37.07
565	C	LYS	A	69	−11.018	43.366	0.923	1.00	25.25
566	O	LYS	A	69	−10.234	43.694	1.812	1.00	26.87
567	N	MET	A	70	−11.068	42.151	0.412	1.00	23.69
568	CA	MET	A	70	−10.175	41.116	0.881	1.00	21.35
569	CB	MET	A	70	−10.850	39.751	0.703	1.00	23.05
570	CG	AMET	A	70	−12.146	39.571	1.446	0.50	23.06
571	CG	BMET	A	70	−12.095	39.633	1.548	0.50	24.64
572	SD	AMET	A	70	−11.838	38.805	3.017	0.50	24.93
573	SD	BMET	A	70	−12.835	38.037	1.426	0.50	27.70
574	CE	AMET	A	70	−12.150	37.121	2.609	0.50	21.42
575	CE	BMET	A	70	−11.893	37.163	2.620	0.50	23.38
576	C	MET	A	70	−8.859	41.123	0.133	1.00	19.52
577	O	MET	A	70	−8.781	41.541	−1.020	1.00	19.18
578	N	SER	A	71	−7.817	40.677	0.825	1.00	15.82
579	CA	SER	A	71	−6.494	40.496	0.238	1.00	16.42
580	CB	ASER	A	71	−5.477	41.489	0.799	0.50	18.42
581	CB	BSER	A	71	−5.459	41.515	0.725	0.50	18.71
582	OG	ASER	A	71	−5.721	42.787	0.281	0.50	16.45
583	OG	BSER	A	71	−5.184	41.396	2.094	0.50	18.52
584	C	SER	A	71	−6.212	39.068	0.724	1.00	16.36
585	O	SER	A	71	−6.598	38.691	1.839	1.00	16.21
586	N	THR	A	72	−5.599	38.260	−0.124	1.00	13.02
587	CA	THR	A	72	−5.342	36.877	0.234	1.00	12.17
588	CB	THR	A	72	−6.174	35.967	−0.681	1.00	14.46
589	OG1	THR	A	72	−7.567	36.233	−0.447	1.00	14.61
590	CG2	THR	A	72	−5.895	34.510	−0.426	1.00	15.94
591	C	THR	A	72	−3.853	36.580	0.124	1.00	12.63
592	O	THR	A	72	−3.179	37.045	−0.786	1.00	13.57
593	N	LEU	A	73	−3.353	35.812	1.084	1.00	11.63
594	CA	LEU	A	73	−1.956	35.450	1.120	1.00	11.94
595	CB	LEU	A	73	−1.670	34.720	2.433	1.00	12.27
596	CG	LEU	A	73	−0.246	34.154	2.583	1.00	11.98
597	CD1	LEU	A	73	0.785	35.251	2.517	1.00	15.22
598	CD2	LEU	A	73	−0.158	33.380	3.924	1.00	14.43
599	C	LEU	A	73	−1.584	34.537	−0.053	1.00	12.95
600	O	LEU	A	73	−2.272	33.558	−0.333	1.00	12.53
601	N	SER	A	74	−0.498	34.899	−0.726	1.00	12.08
602	CA	SER	A	74	0.063	34.120	−1.825	1.00	13.43
603	CB	SER	A	74	−0.071	34.870	−3.147	1.00	15.37
604	OG	SER	A	74	0.785	34.281	−4.139	1.00	19.98
605	C	SER	A	74	1.548	33.926	−1.541	1.00	11.44
606	O	SER	A	74	2.184	34.790	−0.954	1.00	13.15
607	N	CYS	A	75	2.095	32.788	−1.959	1.00	12.82
608	CA	CYS	A	75	3.527	32.543	−1.805	1.00	12.41
609	CB	CYS	A	75	3.803	31.345	−0.889	1.00	15.03
610	SG	CYS	A	75	3.246	29.737	−1.493	1.00	14.95
611	C	CYS	A	75	4.123	32.288	−3.198	1.00	15.39
612	O	CYS	A	75	5.152	31.626	−3.340	1.00	15.73
613	N	LYS	A	76	3.471	32.846	−4.213	1.00	17.25
614	CA	LYS	A	76	3.931	32.685	−5.592	1.00	17.87
615	CB	LYS	A	76	3.117	33.580	−6.516	1.00	19.69
616	CG	LYS	A	76	3.336	33.258	−7.994	1.00	24.67
617	CD	LYS	A	76	2.275	33.908	−8.863	1.00	27.85
618	CE	LYS	A	76	2.408	35.430	−8.875	1.00	31.65
619	NZ	LYS	A	76	1.558	36.045	−9.931	1.00	34.74
620	C	LYS	A	76	5.424	33.018	−5.715	1.00	17.82
621	O	LYS	A	76	5.892	34.025	−5.190	1.00	18.79
622	N	ASN	A	77	6.160	32.143	−6.399	1.00	20.58
623	CA	ASN	A	77	7.600	32.310	−6.607	1.00	21.23
624	CB	ASN	A	77	7.864	33.596	−7.405	1.00	23.75
625	CG	ASN	A	77	7.086	33.645	−8.710	1.00	27.51
626	OD1	ASN	A	77	6.388	34.630	−8.992	1.00	32.76
627	ND2	ASN	A	77	7.197	32.584	−9.516	1.00	27.56
628	C	ASN	A	77	8.370	32.359	−5.288	1.00	20.98
629	O	ASN	A	77	9.431	32.979	−5.197	1.00	21.46
630	N	LYS	A	78	7.812	31.697	−4.270	1.00	19.95
631	CA	LYS	A	78	8.385	31.628	−2.928	1.00	18.97
632	CB	LYS	A	78	9.746	30.922	−2.955	1.00	21.56
633	CG	LYS	A	78	9.657	29.544	−3.583	1.00	22.77
634	CD	LYS	A	78	10.903	28.709	−3.308	1.00	23.94
635	CE	LYS	A	78	10.804	27.355	−3.959	1.00	26.35
636	NZ	LYS	A	78	11.078	27.439	−5.425	1.00	33.16
637	C	LYS	A	78	8.501	32.977	−2.264	1.00	18.94
638	O	LYS	A	78	9.322	33.175	−1.360	1.00	19.31
639	N	ILE	A	79	7.675	33.913	−2.721	1.00	16.05
640	CA	ILE	A	79	7.657	35.255	−2.150	1.00	16.85
641	CB	ILE	A	79	7.897	36.343	−3.228	1.00	19.97
642	CG2	ILE	A	79	7.801	37.725	−2.600	1.00	21.54
643	CG1	ILE	A	79	9.267	36.121	−3.871	1.00	22.28
644	CD1	ILE	A	79	10.432	36.146	−2.884	1.00	24.28
645	C	ILE	A	79	6.283	35.472	−1.515	1.00	14.59
646	O	ILE	A	79	5.266	35.197	−2.123	1.00	16.80
647	N	ILE	A	80	6.267	35.981	−0.290	1.00	15.26
648	CA	ILE	A	80	5.008	36.217	0.396	1.00	15.28
649	CB	ILE	A	80	5.213	36.214	1.916	1.00	15.42
650	CG2	ILE	A	80	3.950	36.775	2.617	1.00	12.93
651	CG1	ILE	A	80	5.629	34.819	2.387	1.00	15.28
652	CD1	ILE	A	80	4.619	33.723	2.130	1.00	13.88
653	C	ILE	A	80	4.391	37.562	0.021	1.00	16.46
654	O	ILE	A	80	5.064	38.578	0.004	1.00	18.29
655	N	SER	A	81	3.099	37.553	−0.278	1.00	15.80
656	CA	SER	A	81	2.382	38.787	−0.573	1.00	16.94
657	CB	SER	A	81	2.521	39.172	−2.049	1.00	19.27
658	OG	SER	A	81	1.613	38.442	−2.839	1.00	23.09
659	C	SER	A	81	0.912	38.565	−0.283	1.00	17.78
660	O	SER	A	81	0.429	37.436	−0.261	1.00	18.89
661	N	PHE	A	82	0.207	39.651	−0.024	1.00	15.45
662	CA	PHE	A	82	−1.226	39.564	0.151	1.00	14.77
663	CB	PHE	A	82	−1.703	40.282	1.413	1.00	15.41
664	CG	PHE	A	82	−1.671	39.404	2.626	1.00	12.72
665	CD1	PHE	A	82	−0.467	39.124	3.263	1.00	13.82
666	CD2	PHE	A	82	−2.839	38.832	3.113	1.00	14.26
667	CE1	PHE	A	82	−0.439	38.288	4.376	1.00	14.72
668	CE2	PHE	A	82	−2.811	37.992	4.230	1.00	13.40
669	CZ	PHE	A	82	−1.603	37.728	4.855	1.00	13.52
670	C	PHE	A	82	−1.706	40.253	−1.104	1.00	17.25
671	O	PHE	A	82	−1.470	41.450	−1.298	1.00	18.41
672	N	GLU	A	83	−2.327	39.462	−1.971	1.00	19.38
673	CA	GLU	A	83	−2.837	39.940	−3.248	1.00	19.61
674	CB	GLU	A	83	−2.856	38.808	−4.274	1.00	21.27
675	CG	AGLU	A	83	−1.507	38.161	−4.521	0.50	24.59
676	CG	BGLU	A	83	−1.487	38.192	−4.581	0.50	24.80
677	CD	AGLU	A	83	−1.571	37.088	−5.587	0.50	25.84
678	CD	BGLU	A	83	−0.565	39.119	−5.358	0.50	26.64
679	OE1	AGLU	A	83	−2.478	36.237	−5.517	0.50	26.32
680	OE1	BGLU	A	83	−0.959	39.570	−6.455	0.50	28.76
681	OE2	AGLU	A	83	−0.711	37.094	−6.493	0.50	29.51
682	OE2	BGLU	A	83	0.558	39.391	−4.882	0.50	28.12
683	C	GLU	A	83	−4.246	40.455	−3.087	1.00	19.90
684	O	GLU	A	83	−5.044	39.892	−2.358	1.00	17.94
685	N	GLU	A	84	−4.557	41.525	−3.808	1.00	22.59
686	CA	GLU	A	84	−5.884	42.101	−3.742	1.00	24.32
687	CB	GLU	A	84	−5.868	43.477	−4.415	1.00	25.42
688	CG	AGLU	A	84	−4.854	44.427	−3.817	0.50	27.52
689	CG	BGLU	A	84	−6.481	44.542	−3.554	0.50	28.22
690	CD	AGLU	A	84	−4.657	45.666	−4.663	0.50	29.00
691	CD	BGLU	A	84	−7.722	44.044	−2.866	0.50	28.45
692	OE1	AGLU	A	84	−3.624	45.751	−5.360	0.50	28.85
693	OE1	BGLU	A	84	−8.694	43.722	−3.573	0.50	31.66
694	OE2	AGLU	A	84	−5.541	46.545	−4.635	0.50	29.98
695	OE2	BGLU	A	84	−7.717	43.961	−1.624	0.50	29.55
696	C	GLU	A	84	−6.865	41.176	−4.461	1.00	24.42
697	O	GLU	A	84	−7.124	41.341	−5.658	1.00	27.68
698	N	MET	A	85	−7.418	40.214	−3.735	1.00	22.01
699	CA	MET	A	85	−8.362	39.274	−4.322	1.00	22.67
700	CB	MET	A	85	−7.618	38.303	−5.238	1.00	24.97
701	CG	MET	A	85	−6.720	37.352	−4.459	1.00	26.77
702	SD	MET	A	85	−5.752	36.259	−5.486	1.00	33.90
703	CE	MET	A	85	−6.974	35.128	−6.021	1.00	30.61
704	C	MET	A	85	−9.057	38.473	−3.236	1.00	21.35
705	O	MET	A	85	−8.514	38.300	−2.141	1.00	19.24
706	N	ASP	A	86	−10.257	37.989	−3.522	1.00	18.17
707	CA	ASP	A	86	−10.980	37.175	−2.553	1.00	20.10
708	CB	ASP	A	86	−12.477	37.123	−2.854	1.00	21.34
709	CG	ASP	A	86	−13.167	38.446	−2.698	1.00	22.68
710	OD1	ASP	A	86	−12.578	39.395	−2.158	1.00	22.70
711	OD2	ASP	A	86	−14.336	38.514	−3.125	1.00	27.94
712	C	ASP	A	86	−10.472	35.745	−2.692	1.00	18.80
713	O	ASP	A	86	−9.958	35.372	−3.735	1.00	20.14
714	N	PRO	A	87	−10.610	34.930	−1.639	1.00	18.18
715	CD	PRO	A	87	−10.995	35.279	−0.263	1.00	16.11
716	CA	PRO	A	87	−10.155	33.533	−1.732	1.00	17.40
717	CB	PRO	A	87	−10.450	32.972	−0.345	1.00	18.66
718	CG	PRO	A	87	−10.432	34.147	0.526	1.00	20.76
719	C	PRO	A	87	−11.096	32.915	−2.767	1.00	18.53
720	O	PRO	A	87	−12.299	33.016	−2.626	1.00	20.16
721	N	PRO	A	88	−10.558	32.250	−3.795	1.00	18.80
722	CD	PRO	A	88	−9.136	31.980	−4.073	1.00	18.15
723	CA	PRO	A	88	−11.424	31.651	−4.819	1.00	17.32
724	CB	PRO	A	88	−10.416	31.134	−5.854	1.00	18.71
725	CG	PRO	A	88	−9.211	30.806	−5.034	1.00	21.64
726	C	PRO	A	88	−12.415	30.576	−4.363	1.00	18.89
727	O	PRO	A	88	−12.139	29.787	−3.467	1.00	18.86
728	N	GLU	A	89	−13.590	30.567	−4.989	1.00	18.05
729	CA	GLU	A	89	−14.609	29.574	−4.682	1.00	18.83
730	CB	GLU	A	89	−15.853	29.812	−5.531	1.00	22.49
731	CG	GLU	A	89	−16.405	31.187	−5.413	1.00	29.78
732	CD	GLU	A	89	−16.970	31.418	−4.049	1.00	35.11
733	OE1	GLU	A	89	−17.382	30.413	−3.431	1.00	35.91
734	OE2	GLU	A	89	−17.013	32.595	−3.605	1.00	36.99
735	C	GLU	A	89	−14.059	28.208	−5.056	1.00	15.39
736	O	GLU	A	89	−14.313	27.216	−4.392	1.00	17.46
737	N	ASN	A	90	−13.324	28.186	−6.158	1.00	16.43
738	CA	ASN	A	90	−12.747	26.967	−6.682	1.00	17.28
739	CB	ASN	A	90	−13.619	26.442	−7.815	1.00	15.51
740	CG	ASN	A	90	−14.992	26.112	−7.362	1.00	14.75
741	OD1	ASN	A	90	−15.188	25.128	−6.678	1.00	17.59
742	ND2	ASN	A	90	−15.973	26.954	−7.725	1.00	16.75
743	C	ASN	A	90	−11.364	27.197	−7.235	1.00	16.58
744	O	ASN	A	90	−11.081	28.238	−7.820	1.00	18.55
745	N	ILE	A	91	−10.492	26.211	−7.035	1.00	18.81
746	CA	ILE	A	91	−9.134	26.252	−7.557	1.00	18.68
747	CB	ILE	A	91	−8.080	26.301	−6.443	1.00	19.32
748	CG2	ILE	A	91	−6.708	26.363	−7.058	1.00	17.89
749	CG1	ILE	A	91	−8.320	27.511	−5.546	1.00	17.34
750	CD1	ILE	A	91	−7.370	27.577	−4.335	1.00	17.37
751	C	ILE	A	91	−9.047	24.939	−8.301	1.00	21.82
752	O	ILE	A	91	−9.069	23.867	−7.699	1.00	20.95
753	N	ASP	A	92	−8.959	25.032	−9.614	1.00	20.54
754	CA	ASP	A	92	−8.972	23.837	−10.433	1.00	25.57
755	CB	ASP	A	92	−9.876	24.113	−11.646	1.00	24.59
756	CG	ASP	A	92	−11.160	24.911	−11.271	1.00	24.09
757	OD1	ASP	A	92	−12.057	24.413	−10.612	1.00	15.45
758	OD2	ASP	A	92	−11.272	26.088	−11.648	1.00	30.89
759	C	ASP	A	92	−7.566	23.354	−10.801	1.00	24.67
760	O	ASP	A	92	−7.163	23.286	−11.968	1.00	28.38
761	N	ASP	A	93	−6.809	23.028	−9.760	1.00	22.69
762	CA	ASP	A	93	−5.449	22.529	−9.903	1.00	23.13
763	CB	ASP	A	93	−4.449	23.678	−10.104	1.00	26.05
764	CG	ASP	A	93	−3.147	23.215	−10.734	1.00	29.72
765	OD1	ASP	A	93	−2.382	22.463	−10.090	1.00	29.89
766	OD2	ASP	A	93	−2.892	23.592	−11.903	1.00	34.67
767	C	ASP	A	93	−5.140	21.803	−8.604	1.00	21.08
768	O	ASP	A	93	−5.848	21.983	−7.617	1.00	20.24
769	N	ILE	A	94	−4.097	20.977	−8.591	1.00	20.15
770	CA	ILE	A	94	−3.769	20.261	−7.367	1.00	20.98
771	CB	ILE	A	94	−3.184	18.856	−7.635	1.00	23.61
772	CG2	ILE	A	94	−4.311	17.914	−8.043	1.00	23.40
773	CG1	ILE	A	94	−2.089	18.920	−8.701	1.00	24.17
774	CD1	ILE	A	94	−1.342	17.583	−8.869	1.00	28.22
775	C	ILE	A	94	−2.792	21.047	−6.510	1.00	21.87
776	O	ILE	A	94	−2.474	20.658	−5.396	1.00	21.96
777	N	GLN	A	95	−2.318	22.162	−7.037	1.00	19.02
778	CA	GLN	A	95	−1.398	23.004	−6.299	1.00	19.98
779	CB	GLN	A	95	0.034	22.847	−6.818	1.00	23.97
780	CG	GLN	A	95	0.527	21.415	−6.759	1.00	28.41
781	CD	GLN	A	95	1.969	21.269	−7.173	1.00	32.45
782	OE1	GLN	A	95	2.346	21.637	−8.286	1.00	34.02
783	NE2	GLN	A	95	2.794	20.730	−6.272	1.00	34.91
784	C	GLN	A	95	−1.829	24.432	−6.468	1.00	17.22
785	O	GLN	A	95	−2.364	24.814	−7.503	1.00	19.35
786	N	SER	A	96	−1.585	25.237	−5.451	1.00	15.97
787	CA	SER	A	96	−1.931	26.638	−5.530	1.00	16.16
788	CB	SER	A	96	−3.374	26.856	−5.109	1.00	15.85
789	OG	SER	A	96	−3.654	28.241	−4.954	1.00	14.88
790	C	SER	A	96	−1.037	27.439	−4.619	1.00	14.50
791	O	SER	A	96	−0.720	27.001	−3.513	1.00	16.46
792	N	ASP	A	97	−0.654	28.618	−5.081	1.00	15.93
793	CA	ASP	A	97	0.161	29.517	−4.294	1.00	15.84
794	CB	ASP	A	97	0.701	30.645	−5.169	1.00	17.89
795	CG	ASP	A	97	−0.405	31.445	−5.841	1.00	15.35
796	OD1	ASP	A	97	−1.282	30.833	−6.460	1.00	23.15
797	OD2	ASP	A	97	−0.400	32.690	−5.766	1.00	22.26
798	C	ASP	A	97	−0.662	30.128	−3.154	1.00	13.09
799	O	ASP	A	97	−0.104	30.825	−2.319	1.00	12.86
800	N	LEU	A	98	−1.971	29.864	−3.135	1.00	13.02
801	CA	LEU	A	98	−2.877	30.407	−2.110	1.00	12.02
802	CB	LEU	A	98	−4.195	30.859	−2.758	1.00	13.29
803	CG	LEU	A	98	−4.103	31.759	−3.983	1.00	13.93
804	CD1	LEU	A	98	−5.525	32.047	−4.475	1.00	17.40
805	CD2	LEU	A	98	−3.359	33.034	−3.657	1.00	14.69
806	C	LEU	A	98	−3.213	29.381	−1.049	1.00	11.66
807	O	LEU	A	98	−3.682	29.721	0.035	1.00	11.48
808	N	ILE	A	99	−3.015	28.112	−1.368	1.00	11.13
809	CA	ILE	A	99	−3.363	27.070	−0.428	1.00	11.30
810	CB	ILE	A	99	−3.955	25.869	−1.160	1.00	11.91
811	CG2	ILE	A	99	−4.089	24.703	−0.208	1.00	13.29
812	CG1	ILE	A	99	−5.301	26.260	−1.800	1.00	13.89
813	CD1	ILE	A	99	−6.453	26.451	−0.813	1.00	14.88
814	C	ILE	A	99	−2.230	26.559	0.443	1.00	12.54
815	O	ILE	A	99	−1.161	26.216	−0.049	1.00	12.28
816	N	PHE	A	100	−2.487	26.512	1.743	1.00	11.42
817	CA	PHE	A	100	−1.515	25.978	2.684	1.00	12.45
818	CB	PHE	A	100	−1.068	27.063	3.664	1.00	11.81
819	CG	PHE	A	100	−0.371	28.186	2.999	1.00	13.04
820	CD1	PHE	A	100	−1.092	29.202	2.373	1.00	12.97
821	CD2	PHE	A	100	1.016	28.189	2.897	1.00	11.78
822	CE1	PHE	A	100	−0.432	30.207	1.647	1.00	12.11
823	CE2	PHE	A	100	1.668	29.191	2.172	1.00	14.15
824	CZ	PHE	A	100	0.954	30.195	1.547	1.00	13.64
825	C	PHE	A	100	−2.195	24.862	3.434	1.00	13.20
826	O	PHE	A	100	−3.410	24.879	3.617	1.00	13.09
827	N	PHE	A	101	−1.429	23.880	3.871	1.00	10.67
828	CA	PHE	A	101	−2.025	22.814	4.642	1.00	12.08
829	CB	PHE	A	101	−1.497	21.469	4.157	1.00	13.01
830	CG	PHE	A	101	−2.049	21.069	2.813	1.00	12.10
831	CD1	PHE	A	101	−3.361	20.617	2.706	1.00	14.27
832	CD2	PHE	A	101	−1.263	21.164	1.673	1.00	13.60
833	CE1	PHE	A	101	−3.894	20.258	1.453	1.00	13.74
834	CE2	PHE	A	101	−1.795	20.803	0.422	1.00	13.76
835	CZ	PHE	A	101	−3.101	20.357	0.335	1.00	13.40
836	C	PHE	A	101	−1.627	23.036	6.085	1.00	11.97
837	O	PHE	A	101	−0.443	23.136	6.378	1.00	13.44
838	N	GLN	A	102	−2.610	23.140	6.971	1.00	12.46
839	CA	GLN	A	102	−2.347	23.322	8.403	1.00	14.12
840	CB	GLN	A	102	−3.602	23.739	9.149	1.00	17.33
841	CG	GLN	A	102	−4.239	24.988	8.661	1.00	16.36
842	CD	GLN	A	102	−5.422	25.364	9.526	1.00	17.78
843	OE1	GLN	A	102	−6.255	24.521	9.850	1.00	22.15
844	NE2	GLN	A	102	−5.496	26.620	9.908	1.00	16.96
845	C	GLN	A	102	−1.904	22.015	8.989	1.00	16.30
846	O	GLN	A	102	−2.579	20.995	8.827	1.00	19.92
847	N	LYS	A	103	−0.784	22.030	9.694	1.00	15.11
848	CA	LYS	A	103	−0.243	20.804	10.293	1.00	14.68
849	CB	LYS	A	103	1.128	20.486	9.704	1.00	15.14
850	CG	LYS	A	103	1.151	20.364	8.209	1.00	16.52
851	CD	LYS	A	103	0.473	19.102	7.782	1.00	20.19
852	CE	LYS	A	103	0.539	18.973	6.275	1.00	18.98
853	NZ	LYS	A	103	−0.055	17.656	5.865	1.00	25.28
854	C	LYS	A	103	−0.063	21.012	11.768	1.00	16.97
855	O	LYS	A	103	0.692	21.896	12.178	1.00	17.65
856	N	ARG	A	104	−0.729	20.197	12.573	1.00	15.77
857	CA	ARG	A	104	−0.594	20.314	14.014	1.00	16.61
858	CB	ARG	A	104	−1.596	19.401	14.727	1.00	19.43
859	CG	ARG	A	104	−1.319	19.323	16.240	1.00	22.08
860	CD	ARG	A	104	−2.071	18.220	17.000	1.00	24.56
861	NE	ARG	A	104	−1.669	18.268	18.403	1.00	25.94
862	CZ	ARG	A	104	−1.959	17.344	19.317	1.00	26.63
863	NH1	ARG	A	104	−2.663	16.263	18.993	1.00	25.41
864	NH2	ARG	A	104	−1.546	17.517	20.571	1.00	27.03
865	C	ARG	A	104	0.819	19.925	14.445	1.00	16.10
866	O	ARG	A	104	1.430	18.999	13.904	1.00	16.54
867	N	VAL	A	105	1.366	20.656	15.408	1.00	15.36
868	CA	VAL	A	105	2.664	20.319	15.945	1.00	15.62
869	CB	VAL	A	105	3.777	21.274	15.456	1.00	15.43
870	CG1	VAL	A	105	3.919	21.113	13.935	1.00	18.41
871	CG2	VAL	A	105	3.468	22.718	15.822	1.00	18.06
872	C	VAL	A	105	2.456	20.380	17.449	1.00	13.59
873	O	VAL	A	105	1.448	20.879	17.907	1.00	16.69
874	N	PRO	A	106	3.403	19.857	18.232	1.00	18.80
875	CD	PRO	A	106	4.722	19.326	17.864	1.00	18.82
876	CA	PRO	A	106	3.237	19.878	19.690	1.00	19.55
877	CB	PRO	A	106	4.566	19.315	20.199	1.00	19.56
878	CG	PRO	A	106	5.054	18.494	19.075	1.00	20.35
879	C	PRO	A	106	2.935	21.230	20.301	1.00	19.68
880	O	PRO	A	106	3.425	22.249	19.832	1.00	21.59
881	N	GLY	A	107	2.128	21.233	21.354	1.00	20.66
882	CA	GLY	A	107	1.824	22.493	22.005	1.00	22.99
883	C	GLY	A	107	0.370	22.891	21.988	1.00	22.95
884	O	GLY	A	107	−0.479	22.213	21.413	1.00	26.62
885	N	HIS	A	108	0.070	24.011	22.633	1.00	23.86
886	CA	HIS	A	108	−1.300	24.476	22.700	1.00	23.63
887	CB	HIS	A	108	−1.487	25.307	23.972	1.00	26.13
888	CG	HIS	A	108	−2.908	25.687	24.242	1.00	30.80
889	CD2	HIS	A	108	−4.069	25.041	23.979	1.00	32.61
890	ND1	HIS	A	108	−3.260	26.883	24.834	1.00	34.25
891	CE1	HIS	A	108	−4.578	26.960	24.910	1.00	33.96
892	NE2	HIS	A	108	−5.091	25.856	24.398	1.00	34.63
893	C	HIS	A	108	−1.648	25.310	21.470	1.00	23.33
894	O	HIS	A	108	−1.026	26.348	21.245	1.00	20.80
895	N	ASN	A	109	−2.622	24.853	20.677	1.00	20.80
896	CA	ASN	A	109	−3.054	25.580	19.477	1.00	21.61
897	CB	ASN	A	109	−3.682	26.932	19.864	1.00	24.97
898	CG	ASN	A	109	−5.098	26.811	20.432	1.00	29.39
899	OD1	ASN	A	109	−5.503	25.764	20.923	1.00	30.70
900	ND2	ASN	A	109	−5.846	27.911	20.380	1.00	30.97
901	C	ASN	A	109	−1.883	25.858	18.521	1.00	20.37
902	O	ASN	A	109	−1.882	26.890	17.835	1.00	19.86
903	N	LYS	A	110	−0.898	24.965	18.467	1.00	18.56
904	CA	LYS	A	110	0.254	25.178	17.592	1.00	16.64
905	CB	LYS	A	110	1.553	24.723	18.265	1.00	16.98
906	CG	LYS	A	110	2.094	25.644	19.356	1.00	24.91
907	CD	LYS	A	110	3.613	25.527	19.414	1.00	27.43
908	CE	LYS	A	110	4.203	26.319	20.567	1.00	30.69
909	NZ	LYS	A	110	4.255	27.769	20.304	1.00	33.04
910	C	LYS	A	110	0.143	24.464	16.267	1.00	15.55
911	O	LYS	A	110	−0.298	23.306	16.196	1.00	15.29
912	N	MET	A	111	0.534	25.160	15.205	1.00	14.18
913	CA	MET	A	111	0.507	24.538	13.896	1.00	14.57
914	CB	MET	A	111	−0.891	24.618	13.321	1.00	16.69
915	CG	MET	A	111	−1.287	26.045	13.036	1.00	15.81
916	SD	MET	A	111	−2.929	26.118	12.289	1.00	21.78
917	CE	MET	A	111	−3.925	25.783	13.747	1.00	21.24
918	C	MET	A	111	1.467	25.206	12.929	1.00	14.54
919	O	MET	A	111	1.996	26.286	13.192	1.00	14.18
920	N	GLU	A	112	1.690	24.531	11.819	1.00	12.42
921	CA	GLU	A	112	2.517	25.055	10.750	1.00	12.11
922	CB	GLU	A	112	3.669	24.110	10.393	1.00	12.57
923	CG	GLU	A	112	4.665	23.835	11.525	1.00	14.68
924	CD	GLU	A	112	5.526	22.602	11.248	1.00	17.35
925	OE1	GLU	A	112	5.104	21.746	10.444	1.00	17.25
926	OE2	GLU	A	112	6.614	22.487	11.846	1.00	19.59
927	C	GLU	A	112	1.602	25.147	9.551	1.00	12.78
928	O	GLU	A	112	0.516	24.552	9.540	1.00	13.84
929	N	PHE	A	113	2.051	25.898	8.554	1.00	11.10
930	CA	PHE	A	113	1.302	26.052	7.308	1.00	11.96
931	CB	PHE	A	113	0.874	27.502	7.098	1.00	11.23
932	CG	PHE	A	113	−0.127	27.972	8.088	1.00	11.83
933	CD1	PHE	A	113	0.272	28.473	9.311	1.00	12.39
934	CD2	PHE	A	113	−1.480	27.906	7.801	1.00	13.91
935	CE1	PHE	A	113	−0.657	28.910	10.238	1.00	14.18
936	CE2	PHE	A	113	−2.413	28.338	8.719	1.00	15.19
937	CZ	PHE	A	113	−2.002	28.843	9.938	1.00	16.27
938	C	PHE	A	113	2.234	25.649	6.198	1.00	10.30
939	O	PHE	A	113	3.173	26.380	5.872	1.00	12.19
940	N	GLU	A	114	1.981	24.484	5.613	1.00	10.85
941	CA	GLU	A	114	2.830	24.000	4.536	1.00	11.42
942	CB	GLU	A	114	2.960	22.483	4.616	1.00	14.13
943	CG	GLU	A	114	4.017	21.966	3.647	1.00	14.86
944	CD	GLU	A	114	4.349	20.505	3.830	1.00	18.25
945	OE1	GLU	A	114	3.732	19.820	4.686	1.00	19.69
946	OE2	GLU	A	114	5.256	20.043	3.096	1.00	19.74
947	C	GLU	A	114	2.256	24.382	3.174	1.00	11.11
948	O	GLU	A	114	1.082	24.170	2.899	1.00	12.56
949	N	SER	A	115	3.101	24.954	2.335	1.00	11.88
950	CA	SER	A	115	2.655	25.349	1.008	1.00	12.18
951	CB	SER	A	115	3.779	26.089	0.303	1.00	13.90
952	OG	SER	A	115	3.415	26.376	−1.036	1.00	14.01
953	C	SER	A	115	2.208	24.163	0.144	1.00	14.22
954	O	SER	A	115	2.892	23.141	0.080	1.00	14.80
955	N	SER	A	116	1.057	24.286	−0.520	1.00	12.54
956	CA	SER	A	116	0.607	23.207	−1.395	1.00	13.95
957	CB	SER	A	116	−0.889	23.335	−1.709	1.00	15.49
958	OG	SER	A	116	−1.114	24.396	−2.605	1.00	21.00
959	C	SER	A	116	1.410	23.256	−2.689	1.00	14.78
960	O	SER	A	116	1.620	22.222	−3.323	1.00	20.48
961	N	LEU	A	117	1.871	24.443	−3.068	1.00	15.76
962	CA	LEU	A	117	2.665	24.610	−4.296	1.00	14.89
963	CB	LEU	A	117	2.527	26.054	−4.778	1.00	17.05
964	CG	LEU	A	117	3.259	26.411	−6.073	1.00	18.25
965	CD1	LEU	A	117	2.711	25.548	−7.205	1.00	20.93
966	CD2	LEU	A	117	3.075	27.907	−6.367	1.00	19.17
967	C	LEU	A	117	4.148	24.232	−4.108	1.00	16.33
968	O	LEU	A	117	4.785	23.640	−5.000	1.00	19.22
969	N	TYR	A	118	4.698	24.568	−2.951	1.00	15.94
970	CA	TYR	A	118	6.089	24.258	−2.632	1.00	16.21
971	CB	TYR	A	118	6.843	25.549	−2.311	1.00	17.11
972	CG	TYR	A	118	6.753	26.539	−3.451	1.00	17.91
973	CD1	TYR	A	118	7.274	26.224	−4.706	1.00	20.29
974	CE1	TYR	A	118	7.122	27.096	−5.790	1.00	19.88
975	CD2	TYR	A	118	6.082	27.749	−3.301	1.00	18.50
976	CE2	TYR	A	118	5.924	28.629	−4.374	1.00	20.19
977	CZ	TYR	A	118	6.445	28.293	−5.617	1.00	20.90
978	OH	TYR	A	118	6.260	29.144	−6.684	1.00	20.87
979	C	TYR	A	118	6.141	23.316	−1.445	1.00	16.88
980	O	TYR	A	118	6.317	23.742	−0.302	1.00	15.27
981	N	GLU	A	119	6.006	22.023	−1.714	1.00	16.33
982	CA	GLU	A	119	6.028	21.036	−0.648	1.00	18.42
983	CB	GLU	A	119	5.941	19.621	−1.231	1.00	21.75
984	CG	GLU	A	119	4.638	19.358	−1.976	1.00	30.12
985	CD	GLU	A	119	4.572	17.950	−2.549	1.00	34.08
986	OE1	GLU	A	119	4.853	17.007	−1.781	1.00	37.54
987	OE2	GLU	A	119	4.237	17.794	−3.754	1.00	38.83
988	C	GLU	A	119	7.319	21.204	0.125	1.00	15.05
989	O	GLU	A	119	8.367	21.498	−0.451	1.00	17.32
990	N	GLY	A	120	7.244	21.047	1.440	1.00	16.26
991	CA	GLY	A	120	8.446	21.183	2.236	1.00	17.41
992	C	GLY	A	120	8.806	22.617	2.581	1.00	15.81
993	O	GLY	A	120	9.816	22.868	3.237	1.00	17.99
994	N	HIS	A	121	7.998	23.570	2.116	1.00	15.30
995	CA	HIS	A	121	8.227	24.976	2.422	1.00	13.61
996	CB	HIS	A	121	8.247	25.828	1.160	1.00	17.73
997	CG	HIS	A	121	9.401	25.528	0.257	1.00	17.99
998	CD2	HIS	A	121	9.784	24.378	−0.346	1.00	18.39
999	ND1	HIS	A	121	10.340	26.474	−0.087	1.00	21.46
1000	CE1	HIS	A	121	11.255	25.921	−0.865	1.00	19.82
1001	NE2	HIS	A	121	10.941	24.650	−1.038	1.00	19.41
1002	C	HIS	A	121	7.058	25.379	3.294	1.00	14.70
1003	O	HIS	A	121	5.921	24.954	3.055	1.00	14.66
1004	N	PHE	A	122	7.345	26.213	4.285	1.00	12.51
1005	CA	PHE	A	122	6.329	26.597	5.247	1.00	12.15
1006	CB	PHE	A	122	6.619	25.953	6.607	1.00	13.26
1007	CG	PHE	A	122	6.663	24.467	6.577	1.00	14.18
1008	CD1	PHE	A	122	7.765	23.792	6.050	1.00	13.89
1009	CD2	PHE	A	122	5.597	23.745	7.074	1.00	14.29
1010	CE1	PHE	A	122	7.790	22.388	6.020	1.00	14.70
1011	CE2	PHE	A	122	5.610	22.344	7.055	1.00	13.73
1012	CZ	PHE	A	122	6.709	21.674	6.524	1.00	14.90
1013	C	PHE	A	122	6.323	28.084	5.486	1.00	12.57
1014	O	PHE	A	122	7.314	28.756	5.254	1.00	13.14
1015	N	LEU	A	123	5.186	28.600	5.952	1.00	10.71
1016	CA	LEU	A	123	5.152	29.996	6.358	1.00	11.63
1017	CB	LEU	A	123	3.748	30.388	6.791	1.00	9.10
1018	CG	LEU	A	123	2.795	30.423	5.609	1.00	10.54
1019	CD1	LEU	A	123	1.429	30.905	6.117	1.00	11.15
1020	CD2	LEU	A	123	3.318	31.377	4.527	1.00	11.37
1021	C	LEU	A	123	6.081	30.076	7.577	1.00	11.96
1022	O	LEU	A	123	6.198	29.125	8.366	1.00	12.05
1023	N	ALA	A	124	6.720	31.225	7.753	1.00	12.85
1024	CA	ALA	A	124	7.622	31.365	8.884	1.00	11.53
1025	CB	ALA	A	124	8.980	30.738	8.550	1.00	13.24
1026	C	ALA	A	124	7.818	32.820	9.198	1.00	12.94
1027	O	ALA	A	124	7.524	33.691	8.380	1.00	13.23
1028	N	CYS	A	125	8.322	33.067	10.402	1.00	13.26
1029	CA	CYS	A	125	8.644	34.415	10.812	1.00	13.48
1030	CB	CYS	A	125	8.251	34.667	12.265	1.00	13.20
1031	SG	CYS	A	125	8.781	36.300	12.818	1.00	19.51
1032	C	CYS	A	125	10.157	34.519	10.681	1.00	15.89
1033	O	CYS	A	125	10.887	33.580	11.020	1.00	18.43
1034	N	GLN	A	126	10.630	35.640	10.151	1.00	16.06
1035	CA	GLN	A	126	12.069	35.842	10.012	1.00	17.60
1036	CB	GLN	A	126	12.539	35.509	8.593	1.00	20.69
1037	CG	GLN	A	126	14.052	35.634	8.399	1.00	24.00
1038	CD	AGLN	A	126	14.759	34.337	8.674	0.50	22.65
1039	CD	BGLN	A	126	14.514	35.169	7.021	0.50	23.59
1040	OE1	AGLN	A	126	14.583	33.359	7.948	0.50	26.30
1041	OE1	BGLN	A	126	14.245	35.819	6.009	0.50	25.95
1042	NE2	AGLN	A	126	15.564	34.313	9.725	0.50	27.75
1043	NE2	BGLN	A	126	15.200	34.033	6.976	0.50	24.53
1044	C	GLN	A	126	12.382	37.289	10.304	1.00	18.81
1045	O	GLN	A	126	11.760	38.186	9.752	1.00	19.93
1046	N	LYS	A	127	13.362	37.515	11.173	1.00	20.55
1047	CA	LYS	A	127	13.748	38.879	11.491	1.00	23.77
1048	CB	LYS	A	127	14.567	38.925	12.779	1.00	24.21
1049	CG	LYS	A	127	14.802	40.337	13.301	1.00	27.87
1050	CD	LYS	A	127	15.675	40.321	14.540	1.00	29.02
1051	CE	LYS	A	127	15.836	41.713	15.144	1.00	31.54
1052	NZ	LYS	A	127	16.437	41.644	16.509	1.00	33.62
1053	C	LYS	A	127	14.582	39.402	10.334	1.00	25.42
1054	O	LYS	A	127	15.509	38.743	9.887	1.00	25.74
1055	N	GLU	A	128	14.220	40.571	9.826	1.00	25.95
1056	CA	GLU	A	128	14.966	41.192	8.747	1.00	29.30
1057	CB	GLU	A	128	14.130	41.291	7.480	1.00	31.49
1058	CG	GLU	A	128	14.964	41.545	6.227	1.00	35.73
1059	CD	GLU	A	128	14.170	42.212	5.126	1.00	38.50
1060	OE1	GLU	A	128	13.862	43.417	5.264	1.00	41.50
1061	OE2	GLU	A	128	13.843	41.542	4.122	1.00	41.96
1062	C	GLU	A	128	15.254	42.576	9.288	1.00	31.50
1063	O	GLU	A	128	14.342	43.397	9.426	1.00	32.21
1064	N	ASP	A	129	16.518	42.829	9.613	1.00	32.76
1065	CA	ASP	A	129	16.913	44.106	10.181	1.00	35.20
1066	CB	ASP	A	129	16.624	45.235	9.190	1.00	37.54
1067	CG	ASP	A	129	17.578	45.205	7.997	1.00	39.65
1068	OD1	ASP	A	129	18.813	45.254	8.207	1.00	40.49
1069	OD2	ASP	A	129	17.105	45.111	6.846	1.00	43.03
1070	C	ASP	A	129	16.165	44.273	11.499	1.00	34.76
1071	O	ASP	A	129	16.418	43.520	12.436	1.00	36.76
1072	N	ASP	A	130	15.253	45.222	11.623	1.00	34.20
1073	CA	ASP	A	130	14.577	45.313	12.911	1.00	32.98
1074	CB	ASP	A	130	14.775	46.705	13.522	1.00	36.86
1075	CG	ASP	A	130	16.115	46.829	14.264	1.00	38.69
1076	OD1	ASP	A	130	16.259	46.203	15.340	1.00	39.67
1077	OD2	ASP	A	130	17.037	47.534	13.774	1.00	41.31
1078	C	ASP	A	130	13.102	44.921	12.852	1.00	31.57
1079	O	ASP	A	130	12.378	45.027	13.845	1.00	32.43
1080	N	ALA	A	131	12.679	44.430	11.692	1.00	27.42
1081	CA	ALA	A	131	11.302	44.006	11.488	1.00	23.99
1082	CB	ALA	A	131	10.819	44.445	10.117	1.00	24.71
1083	C	ALA	A	131	11.203	42.492	11.586	1.00	22.78
1084	O	ALA	A	131	12.187	41.785	11.419	1.00	24.27
1085	N	PHE	A	132	10.008	41.996	11.869	1.00	19.22
1086	CA	PHE	A	132	9.791	40.551	11.934	1.00	17.56
1087	CB	PHE	A	132	9.230	40.191	13.297	1.00	18.03
1088	CG	PHE	A	132	10.232	40.373	14.391	1.00	22.00
1089	CD1	PHE	A	132	11.237	39.434	14.584	1.00	23.59
1090	CD2	PHE	A	132	10.232	41.526	15.163	1.00	22.92
1091	CE1	PHE	A	132	12.245	39.642	15.539	1.00	25.47
1092	CE2	PHE	A	132	11.232	41.742	16.115	1.00	23.24
1093	CZ	PHE	A	132	12.233	40.798	16.298	1.00	24.74
1094	C	PHE	A	132	8.826	40.277	10.796	1.00	16.02
1095	O	PHE	A	132	7.675	40.683	10.842	1.00	17.63
1096	N	LYS	A	133	9.315	39.592	9.775	1.00	15.51
1097	CA	LYS	A	133	8.522	39.370	8.577	1.00	15.56
1098	CB	LYS	A	133	9.380	39.726	7.358	1.00	21.68
1099	CG	LYS	A	133	10.022	41.103	7.414	1.00	23.79
1100	CD	LYS	A	133	8.984	42.198	7.316	1.00	28.93
1101	CE	LYS	A	133	9.579	43.556	6.912	1.00	32.70
1102	NZ	LYS	A	133	10.002	43.637	5.476	1.00	33.12
1103	C	LYS	A	133	7.956	37.980	8.383	1.00	13.95
1104	O	LYS	A	133	8.446	37.008	8.956	1.00	14.81
1105	N	LEU	A	134	6.899	37.898	7.576	1.00	13.83
1106	CA	LEU	A	134	6.293	36.614	7.240	1.00	13.03
1107	CB	LEU	A	134	4.805	36.787	7.019	1.00	13.18
1108	CG	LEU	A	134	4.051	35.543	6.569	1.00	12.67
1109	CD1	LEU	A	134	4.055	34.488	7.705	1.00	13.20
1110	CD2	LEU	A	134	2.625	35.935	6.232	1.00	12.70
1111	C	LEU	A	134	6.956	36.197	5.943	1.00	13.54
1112	O	LEU	A	134	6.921	36.940	4.963	1.00	14.23
1113	N	ILE	A	135	7.570	35.023	5.932	1.00	12.99
1114	CA	ILE	A	135	8.240	34.523	4.724	1.00	13.65
1115	CB	ILE	A	135	9.786	34.572	4.863	1.00	14.46
1116	CG2	ILE	A	135	10.251	36.027	4.996	1.00	17.46
1117	CG1	ILE	A	135	10.214	33.705	6.053	1.00	15.82
1118	CD1	ILE	A	135	11.691	33.339	6.042	1.00	18.39
1119	C	ILE	A	135	7.863	33.064	4.479	1.00	13.24
1120	O	ILE	A	135	7.119	32.475	5.265	1.00	13.19
1121	N	LEU	A	136	8.359	32.496	3.382	1.00	12.56
1122	CA	LEU	A	136	8.147	31.094	3.088	1.00	12.33
1123	CB	LEU	A	136	7.558	30.874	1.687	1.00	14.97
1124	CG	LEU	A	136	7.235	29.400	1.401	1.00	14.23
1125	CD1	LEU	A	136	5.865	29.098	2.028	1.00	13.48
1126	CD2	LEU	A	136	7.214	29.112	−0.133	1.00	13.37
1127	C	LEU	A	136	9.557	30.511	3.104	1.00	14.28
1128	O	LEU	A	136	10.451	31.056	2.467	1.00	16.88
1129	N	LYS	A	137	9.750	29.402	3.802	1.00	13.54
1130	CA	LYS	A	137	11.071	28.794	3.858	1.00	14.56
1131	CB	LYS	A	137	11.890	29.414	4.996	1.00	15.95
1132	CG	LYS	A	137	11.371	29.062	6.381	1.00	18.25
1133	CD	LYS	A	137	12.186	29.691	7.486	1.00	22.46
1134	CE	LYS	A	137	13.067	28.690	8.193	1.00	21.75
1135	NZ	LYS	A	137	13.728	29.370	9.346	1.00	17.93
1136	C	LYS	A	137	11.001	27.314	4.132	1.00	14.87
1137	O	LYS	A	137	9.989	26.798	4.593	1.00	14.80
1138	N	LYS	A	138	12.101	26.630	3.838	1.00	16.07
1139	CA	LYS	A	138	12.216	25.231	4.200	1.00	16.43
1140	CB	LYS	A	138	13.358	24.556	3.454	1.00	18.90
1141	CG	LYS	A	138	13.110	24.365	1.987	1.00	20.88
1142	CD	LYS	A	138	14.012	23.255	1.485	1.00	25.69
1143	CE	LYS	A	138	13.894	23.048	0.008	1.00	26.71
1144	NZ	LYS	A	138	14.451	21.707	−0.367	1.00	28.61
1145	C	LYS	A	138	12.628	25.336	5.670	1.00	15.78
1146	O	LYS	A	138	13.155	26.367	6.100	1.00	18.59
1147	N	LYS	A	139	12.389	24.286	6.444	1.00	17.51
1148	CA	LYS	A	139	12.795	24.285	7.848	1.00	16.96
1149	CB	LYS	A	139	12.307	23.004	8.527	1.00	18.35
1150	CG	LYS	A	139	10.804	22.911	8.742	1.00	19.71
1151	CD	LYS	A	139	10.527	21.512	9.258	1.00	23.58
1152	CE	LYS	A	139	9.066	21.209	9.534	1.00	26.29
1153	NZ	LYS	A	139	8.954	19.737	9.843	1.00	25.65
1154	C	LYS	A	139	14.330	24.333	7.881	1.00	17.92
1155	O	LYS	A	139	14.973	23.710	7.033	1.00	19.75
1156	N	ASP	A	140	14.911	25.091	8.811	1.00	19.30
1157	CA	ASP	A	140	16.381	25.156	8.910	1.00	20.30
1158	CB	ASP	A	140	16.866	26.140	9.973	1.00	20.83
1159	CG	ASP	A	140	16.617	27.566	9.612	1.00	20.94
1160	OD1	ASP	A	140	16.334	27.861	8.432	1.00	22.64
1161	OD2	ASP	A	140	16.724	28.403	10.532	1.00	25.18
1162	C	ASP	A	140	16.853	23.797	9.344	1.00	22.77
1163	O	ASP	A	140	17.929	23.341	8.964	1.00	23.14
1164	N	GLU	A	141	16.056	23.179	10.198	1.00	22.47
1165	CA	GLU	A	141	16.372	21.859	10.676	1.00	26.83
1166	CB	GLU	A	141	17.531	21.903	11.676	1.00	28.35
1167	CG	GLU	A	141	17.193	22.548	13.013	1.00	29.02
1168	CD	GLU	A	141	17.240	24.067	12.973	1.00	32.41
1169	OE1	GLU	A	141	18.244	24.623	12.472	1.00	32.00
1170	OE2	GLU	A	141	16.277	24.703	13.453	1.00	33.91
1171	C	GLU	A	141	15.143	21.326	11.352	1.00	28.16
1172	O	GLU	A	141	14.141	22.025	11.514	1.00	26.16
1173	N	ASN	A	142	15.215	20.057	11.718	1.00	30.27
1174	CA	ASN	A	142	14.126	19.423	12.413	1.00	31.97
1175	CB	ASN	A	142	14.482	17.962	12.675	1.00	35.33
1176	CG	ASN	A	142	13.436	17.248	13.490	1.00	37.20
1177	OD1	ASN	A	142	12.591	16.534	12.948	1.00	39.29
1178	ND2	ASN	A	142	13.478	17.441	14.808	1.00	39.62
1179	C	ASN	A	142	14.096	20.186	13.726	1.00	33.28
1180	O	ASN	A	142	15.108	20.247	14.434	1.00	34.62
1181	N	GLY	A	143	12.965	20.787	14.057	1.00	33.41
1182	CA	GLY	A	143	12.915	21.521	15.310	1.00	31.70
1183	C	GLY	A	143	12.959	23.022	15.122	1.00	29.85
1184	O	GLY	A	143	13.018	23.775	16.091	1.00	30.77
1185	N	ASP	A	144	12.944	23.454	13.867	1.00	25.57
1186	CA	ASP	A	144	12.944	24.868	13.544	1.00	23.35
1187	CB	ASP	A	144	13.083	25.060	12.041	1.00	22.25
1188	CG	ASP	A	144	13.166	26.507	11.655	1.00	21.13
1189	OD1	ASP	A	144	12.927	27.377	12.526	1.00	18.37
1190	OD2	ASP	A	144	13.473	26.771	10.480	1.00	17.30
1191	C	ASP	A	144	11.590	25.381	13.991	1.00	20.88
1192	O	ASP	A	144	10.559	25.071	13.397	1.00	22.99
1193	N	LYS	A	145	11.581	26.174	15.040	1.00	19.51
1194	CA	LYS	A	145	10.322	26.671	15.546	1.00	18.75
1195	CB	LYS	A	145	10.439	26.922	17.050	1.00	21.90
1196	CG	LYS	A	145	10.687	25.648	17.872	1.00	24.52
1197	CD	LYS	A	145	10.549	25.948	19.366	1.00	26.57
1198	CE	LYS	A	145	10.796	24.710	20.217	1.00	30.11
1199	NZ	LYS	A	145	9.742	23.680	20.087	1.00	31.97
1200	C	LYS	A	145	9.810	27.929	14.862	1.00	16.66
1201	O	LYS	A	145	8.688	28.369	15.151	1.00	16.06
1202	N	SER	A	146	10.596	28.498	13.952	1.00	15.88
1203	CA	SER	A	146	10.181	29.728	13.280	1.00	14.67
1204	CB	SER	A	146	11.328	30.307	12.437	1.00	14.91
1205	OG	SER	A	146	11.585	29.472	11.323	1.00	15.64
1206	C	SER	A	146	8.959	29.514	12.384	1.00	14.13
1207	O	SER	A	146	8.330	30.482	11.945	1.00	12.98
1208	N	VAL	A	147	8.653	28.252	12.087	1.00	13.49
1209	CA	VAL	A	147	7.501	27.921	11.250	1.00	13.71
1210	CB	VAL	A	147	7.787	26.739	10.317	1.00	11.55
1211	CG1	VAL	A	147	8.866	27.099	9.304	1.00	14.25
1212	CG2	VAL	A	147	8.163	25.536	11.133	1.00	15.65
1213	C	VAL	A	147	6.298	27.535	12.112	1.00	11.71
1214	O	VAL	A	147	5.258	27.152	11.590	1.00	10.63
1215	N	MET	A	148	6.424	27.634	13.435	1.00	12.60
1216	CA	MET	A	148	5.321	27.281	14.303	1.00	14.00
1217	CB	MET	A	148	5.830	26.516	15.512	1.00	14.92
1218	CG	MET	A	148	6.469	25.231	15.076	1.00	18.15
1219	SD	MET	A	148	7.076	24.375	16.500	1.00	24.45
1220	CE	MET	A	148	7.997	23.101	15.708	1.00	24.28
1221	C	MET	A	148	4.572	28.500	14.740	1.00	13.74
1222	O	MET	A	148	5.162	29.498	15.171	1.00	14.34
1223	N	PHE	A	149	3.260	28.418	14.625	1.00	12.40
1224	CA	PHE	A	149	2.380	29.523	14.980	1.00	14.24
1225	CB	PHE	A	149	1.690	30.066	13.730	1.00	13.47
1226	CG	PHE	A	149	2.630	30.602	12.727	1.00	15.00
1227	CD1	PHE	A	149	3.129	31.887	12.863	1.00	13.31
1228	CD2	PHE	A	149	3.063	29.806	11.673	1.00	11.42
1229	CE1	PHE	A	149	4.058	32.386	11.964	1.00	13.16
1230	CE2	PHE	A	149	3.989	30.288	10.769	1.00	12.94
1231	CZ	PHE	A	149	4.494	31.594	10.917	1.00	13.99
1232	C	PHE	A	149	1.282	29.044	15.888	1.00	15.18
1233	O	PHE	A	149	0.952	27.852	15.917	1.00	14.60
1234	N	THR	A	150	0.716	29.968	16.641	1.00	14.14
1235	CA	THR	A	150	−0.423	29.612	17.459	1.00	16.16
1236	CB A	THR	A	150	−0.225	29.966	18.939	0.50	15.90
1237	CB B	THR	A	150	−0.238	30.083	18.927	0.50	17.48
1238	OG1A	THR	A	150	−0.014	31.369	19.073	0.50	13.73
1239	OG1B	THR	A	150	0.849	29.375	19.533	0.50	20.99
1240	CG2A	THR	A	150	0.970	29.224	19.493	0.50	18.22
1241	CG2B	THR	A	150	−1.499	29.845	19.729	0.50	19.08
1242	C	THR	A	150	−1.610	30.374	16.884	1.00	16.42
1243	O	THR	A	150	−1.509	31.572	16.582	1.00	16.83
1244	N	LEU	A	151	−2.738	29.695	16.706	1.00	16.47
1245	CA	LEU	A	151	−3.934	30.355	16.194	1.00	20.02
1246	CB	LEU	A	151	−4.471	29.667	14.932	1.00	20.88
1247	CG	LEU	A	151	−4.037	30.322	13.618	1.00	21.54
1248	CD1	LEU	A	151	−2.549	30.059	13.465	1.00	21.65
1249	CD2	LEU	A	151	−4.795	29.758	12.423	1.00	23.25
1250	C	LEU	A	151	−5.016	30.333	17.251	1.00	24.42
1251	O	LEU	A	151	−5.211	29.307	17.896	1.00	25.23
1252	N	THR	A	152	−5.709	31.452	17.444	1.00	23.97
1253	CA	THR	A	152	−6.790	31.478	18.433	1.00	27.51
1254	CB	THR	A	152	−7.303	32.893	18.682	1.00	28.24
1255	OG1	THR	A	152	−7.707	33.487	17.435	1.00	23.89
1256	CG2	THR	A	152	−6.222	33.722	19.345	1.00	26.78
1257	C	THR	A	152	−7.968	30.646	17.913	1.00	29.17
1258	O	THR	A	152	−8.012	30.408	16.700	1.00	32.76
1259	OXT	THR	A	152	−8.837	30.240	18.715	1.00	32.55
1261	OH2	WAT	W	201	−3.900	32.052	1.360	1.00	12.31
1262	OH2	WAT	W	202	0.952	27.488	−1.480	1.00	11.96
1263	OH2	WAT	W	203	4.419	27.262	8.986	1.00	12.37
1264	OH2	WAT	W	204	−8.954	33.221	3.352	1.00	14.41
1265	OH2	WAT	W	205	−2.685	33.405	18.409	1.00	15.70
1266	OH2	WAT	W	206	−3.050	37.896	13.444	1.00	15.52
1267	OH2	WAT	W	207	−6.432	19.889	−5.125	1.00	16.05
1268	OH2	WAT	W	208	6.860	31.415	14.235	1.00	17.33
1269	OH2	WAT	W	209	−9.099	41.023	8.402	1.00	17.16
1270	OH2	WAT	W	210	−3.026	19.195	6.916	1.00	17.06
1271	OH2	WAT	W	211	−10.571	41.368	−3.019	1.00	19.89
1272	OH2	WAT	W	212	8.803	36.869	0.960	1.00	19.27
1273	OH2	WAT	W	213	6.589	45.066	17.945	1.00	20.95
1274	OH2	WAT	W	214	4.237	29.236	17.984	1.00	20.13
1275	OH2	WAT	W	215	3.776	39.679	21.941	1.00	20.24
1276	OH2	WAT	W	216	1.779	45.769	8.893	1.00	21.79
1277	OH2	WAT	W	217	11.361	21.895	5.097	1.00	22.74
1278	OH2	WAT	W	218	−8.886	22.794	6.297	1.00	22.52
1279	OH2	WAT	W	219	−4.294	29.092	−7.341	1.00	21.52
1280	OH2	WAT	W	220	−8.112	16.957	2.679	1.00	22.94
1281	OH2	WAT	W	221	4.278	18.802	7.412	1.00	23.11
1282	OH2	WAT	W	222	7.997	43.792	13.015	1.00	23.72
1283	OH2	WAT	W	223	−11.530	27.956	9.056	1.00	22.04
1284	OH2	WAT	W	224	−8.653	23.818	8.764	1.00	21.43
1285	OH2	WAT	W	225	2.146	20.373	0.340	1.00	23.56
1286	OH2	WAT	W	226	8.334	38.402	3.039	1.00	22.17
1287	OH2	WAT	W	227	1.941	42.076	0.257	1.00	22.36
1288	OH2	WAT	W	228	−10.479	17.579	1.652	1.00	22.96
1289	OH2	WAT	W	229	−7.988	27.707	−10.764	1.00	24.24
1290	OH2	WAT	W	230	−6.714	30.341	−7.632	1.00	23.93
1291	OH2	WAT	W	231	−14.300	22.760	−6.864	1.00	22.46
1292	OH2	WAT	W	232	−16.801	24.026	−2.339	1.00	24.15
1293	OH2	WAT	W	233	9.661	34.190	1.228	1.00	23.84
1294	OH2	WAT	W	234	−12.267	19.457	−4.246	1.00	24.11
1295	OH2	WAT	W	235	11.147	29.355	0.425	1.00	23.09
1296	OH2	WAT	W	236	2.851	31.305	19.366	1.00	23.61
1297	OH2	WAT	W	237	−14.428	20.889	−4.675	1.00	24.21
1298	OH2	WAT	W	238	−8.739	29.567	−9.042	1.00	23.83
1299	OH2	WAT	W	239	−9.534	43.654	16.866	1.00	26.13
1300	OH2	WAT	W	240	15.821	27.151	5.814	1.00	23.94
1301	OH2	WAT	W	241	−15.060	29.317	−9.580	1.00	26.94
1302	OH2	WAT	W	242	−10.219	47.657	14.755	1.00	24.37
1303	OH2	WAT	W	243	5.801	21.033	−4.404	1.00	26.11
1304	OH2	WAT	W	244	14.946	31.902	5.121	1.00	25.96
1305	OH2	WAT	W	245	−17.189	29.249	0.593	1.00	27.88
1306	OH2	WAT	W	246	−4.185	44.762	4.335	1.00	25.86
1307	OH2	WAT	W	247	−7.887	27.244	11.439	1.00	24.83
1308	OH2	WAT	W	248	−9.807	26.190	9.790	1.00	24.32
1309	OH2	WAT	W	249	6.211	44.171	5.246	1.00	28.83
1310	OH2	WAT	W	250	6.220	17.732	3.474	1.00	26.28
1311	OH2	WAT	W	251	−10.816	35.197	−6.225	1.00	27.93
1312	OH2	WAT	W	252	−4.857	47.448	6.218	1.00	27.36
1313	OH2	WAT	W	253	14.206	27.972	2.351	1.00	26.84
1314	OH2	WAT	W	254	−13.160	31.030	−8.452	1.00	26.95
1315	OH2	WAT	W	255	3.076	16.943	3.868	1.00	28.38
1316	OH2	WAT	W	256	−6.468	46.023	22.407	1.00	26.15
1317	OH2	WAT	W	257	−7.406	14.793	−7.421	1.00	26.97
1318	OH2	WAT	W	258	−10.375	31.766	−9.434	1.00	26.85
1319	OH2	WAT	W	259	−12.198	22.930	−8.047	1.00	27.42
1320	OH2	WAT	W	260	−11.329	38.500	−6.075	1.00	27.37
1321	OH2	WAT	W	261	−6.736	19.384	−9.944	1.00	28.38
1322	OH2	WAT	W	262	−5.492	44.706	6.464	1.00	29.70
1323	OH2	WAT	W	263	−8.997	29.569	12.161	1.00	27.88
1324	OH2	WAT	W	264	−13.481	41.577	−0.850	1.00	27.89
1325	OH2	WAT	W	265	−19.259	26.016	2.977	1.00	28.97
1326	OH2	WAT	W	266	−6.571	33.032	−8.254	1.00	28.20
1327	OH2	WAT	W	267	−6.775	48.685	23.870	1.00	27.71
1328	OH2	WAT	W	268	−14.337	32.281	13.760	1.00	28.87
1329	OH2	WAT	W	269	3.746	36.474	−3.957	1.00	28.98
1330	OH2	WAT	W	270	−3.030	47.364	24.055	1.00	28.80
1331	OH2	WAT	W	271	−12.038	46.877	−6.546	1.00	29.27
1332	OH2	WAT	W	272	16.897	23.821	4.967	1.00	27.76
1333	OH2	WAT	W	273	−6.102	11.280	3.008	1.00	29.68
1334	OH2	WAT	W	274	−3.325	26.939	−8.814	1.00	26.87
1335	OH2	WAT	W	275	−18.075	31.088	5.751	1.00	30.31
1336	OH2	WAT	W	276	16.410	21.627	3.627	1.00	32.17
1337	OH2	WAT	W	277	−14.397	33.979	−3.997	1.00	30.43
1338	OH2	WAT	W	278	13.763	20.490	4.110	1.00	30.05
1339	OH2	WAT	W	279	14.009	27.171	16.485	1.00	30.86
1340	OH2	WAT	W	280	−10.386	33.699	17.348	1.00	29.78
1341	OH2	WAT	W	281	12.225	20.181	1.984	1.00	29.82
1342	OH2	WAT	W	282	1.311	43.820	29.305	1.00	29.14
1343	OH2	WAT	W	283	14.625	35.318	12.464	1.00	32.75
1344	OH2	WAT	W	284	9.241	22.510	12.673	1.00	27.48
1345	OH2	WAT	W	285	−2.507	41.407	21.101	1.00	29.36
1346	OH2	WAT	W	286	−11.878	44.585	17.206	1.00	33.36
1347	OH2	WAT	W	287	10.382	37.173	17.161	1.00	30.66
1348	OH2	WAT	W	288	4.222	41.816	24.115	1.00	28.13
1349	OH2	WAT	W	289	11.224	21.434	21.871	1.00	30.72
1350	OH2	WAT	W	290	−9.949	38.432	16.612	1.00	31.21
1351	OH2	WAT	W	291	17.088	21.905	0.723	1.00	31.76
1352	OH2	WAT	W	292	−10.054	42.132	19.115	1.00	32.79
1353	OH2	WAT	W	293	5.848	28.024	−9.058	1.00	32.96
1354	OH2	WAT	W	294	7.449	46.288	11.558	1.00	32.64
1355	OH2	WAT	W	295	−3.819	45.211	22.206	1.00	31.93
1356	OH2	WAT	W	296	−2.550	31.348	−8.532	1.00	29.42
1357	OH2	WAT	W	297	8.083	46.403	8.637	1.00	31.26
1358	OH2	WAT	W	298	−6.277	23.034	12.180	1.00	31.59
1359	OH2	WAT	W	299	−9.865	34.305	−8.499	1.00	33.74
1360	OH2	WAT	W	300	−11.753	15.406	−1.471	1.00	31.99
1361	OH2	WAT	W	301	1.231	50.941	7.449	1.00	33.26
1362	OH2	WAT	W	302	4.884	40.349	1.873	1.00	30.36
1363	OH2	WAT	W	303	−0.290	17.509	3.266	1.00	33.60
1364	OH2	WAT	W	304	−8.306	49.520	8.996	1.00	32.12
1365	OH2	WAT	W	305	−16.179	21.404	−2.841	1.00	34.47
1366	OH2	WAT	W	306	−9.767	22.287	10.819	1.00	33.82
1367	OH2	WAT	W	307	2.605	25.493	23.695	1.00	32.70
1368	OH2	WAT	W	308	−1.233	29.153	22.803	1.00	31.89
1369	OH2	WAT	W	309	3.294	43.277	31.535	1.00	30.01
1370	OH2	WAT	W	310	−18.145	32.995	3.738	1.00	31.44
1371	OH2	WAT	W	311	3.862	47.222	7.780	1.00	34.38
1372	OH2	WAT	W	312	1.401	19.720	3.009	1.00	32.88
1373	OH2	WAT	W	313	2.362	48.671	6.269	1.00	29.57
1374	OH2	WAT	W	314	−8.726	15.367	4.938	1.00	31.71
1375	OH2	WAT	W	315	−17.604	30.244	−9.311	1.00	31.67
1376	OH2	WAT	W	316	6.049	23.620	−7.356	1.00	30.98
1377	OH2	WAT	W	317	−17.887	17.323	−5.165	1.00	29.81
1378	OH2	WAT	W	318	0.756	45.919	28.072	1.00	34.09
1379	OH2	WAT	W	319	4.224	50.319	18.097	1.00	36.06
1380	OH2	WAT	W	320	−1.807	34.389	−7.302	1.00	32.63
1381	OH2	WAT	W	321	−5.641	26.448	16.631	1.00	34.55
1382	OH2	WAT	W	322	−8.023	11.775	−5.519	1.00	37.17
1383	OH2	WAT	W	323	0.906	27.929	21.790	1.00	31.90
1384	OH2	WAT	W	324	16.865	27.638	12.993	1.00	39.01
1385	OH2	WAT	W	325	13.149	32.235	10.074	1.00	30.65
1386	OH2	WAT	W	326	0.881	52.908	5.493	1.00	36.21
1387	OH2	WAT	W	327	−11.094	35.858	15.788	1.00	35.61
1388	OH2	WAT	W	328	9.464	44.941	14.828	1.00	35.35
1389	OH2	WAT	W	329	11.956	33.216	−1.753	1.00	35.31
1390	OH2	WAT	W	330	−15.633	35.904	−1.678	1.00	34.57
1391	OH2	WAT	W	331	0.433	18.388	−5.721	1.00	33.25
1392	OH2	WAT	W	332	−3.090	22.685	15.873	1.00	36.98
1393	OH2	WAT	W	333	−17.189	23.616	6.052	1.00	32.38
1394	OH2	WAT	W	334	17.579	18.631	10.887	1.00	35.84
1395	OH2	WAT	W	335	−0.520	28.452	−8.229	1.00	35.62
1396	OH2	WAT	W	336	5.589	22.680	18.766	1.00	35.02
1397	OH2	WAT	W	337	−5.195	11.581	−7.734	1.00	38.68
1398	OH2	WAT	W	338	14.660	30.377	1.229	1.00	35.10
1399	OH2	WAT	W	339	−17.723	20.205	−0.873	1.00	34.14
1400	OH2	WAT	W	340	12.282	40.815	19.756	1.00	39.51
1401	OH2	WAT	W	341	−16.095	49.517	2.071	1.00	37.48
1402	OH2	WAT	W	342	16.962	24.111	−1.316	1.00	37.77
1403	OH2	WAT	W	343	8.916	39.469	21.199	1.00	34.40
1404	OH2	WAT	W	344	−20.253	29.440	4.304	1.00	37.94
1405	OH2	WAT	W	345	−3.441	21.151	18.584	1.00	33.63
1406	OH2	WAT	W	346	11.274	39.429	3.812	1.00	39.15
1407	OH2	WAT	W	347	5.930	40.904	−1.475	1.00	35.58
1408	OH2	WAT	W	348	−15.467	35.778	5.107	1.00	36.50
1409	OH2	WAT	W	349	1.737	30.364	−8.724	1.00	37.24
1410	OH2	WAT	W	350	−4.187	22.695	21.115	1.00	35.40
1411	OH2	WAT	W	351	−11.792	25.223	11.653	1.00	34.67
1412	OH2	WAT	W	352	13.323	31.807	2.854	1.00	34.62
1413	OH2	WAT	W	353	1.228	19.080	−2.076	1.00	36.49
1414	OH2	WAT	W	354	−18.253	20.118	−5.099	1.00	39.85
1415	OH2	WAT	W	355	−15.224	37.809	6.369	1.00	38.11
1416	OH2	WAT	W	356	−15.750	43.843	6.998	1.00	38.78
1417	OH2	WAT	W	357	8.688	23.641	−7.129	1.00	40.34
1418	OH2	WAT	W	358	6.766	40.676	3.480	1.00	37.27
1419	OH2	WAT	W	359	10.089	26.035	−7.559	1.00	37.40
1420	OH2	WAT	W	360	−1.653	34.642	−10.325	1.00	41.05
1421	OH2	WAT	W	361	11.902	35.717	14.116	1.00	38.61
1422	OH2	WAT	W	362	5.278	13.387	6.098	1.00	38.64
1423	OH2	WAT	W	363	1.897	18.206	−8.382	1.00	39.07
1424	OH2	WAT	W	364	−4.846	26.666	−10.725	1.00	38.17
1425	OH2	WAT	W	365	9.544	22.055	−3.166	1.00	37.03
1426	OH2	WAT	W	366	−13.428	31.452	19.752	1.00	40.02
1427	OH2	WAT	W	367	−3.675	19.985	−11.673	1.00	39.56
1428	OH2	WAT	W	368	5.940	48.016	13.223	1.00	36.94
1429	OH2	WAT	W	369	−15.068	43.053	−2.748	1.00	38.98
1430	OH2	WAT	W	370	17.423	44.152	4.412	1.00	41.67
1431	OH2	WAT	W	371	−9.559	20.801	4.372	1.00	38.63
1432	OH2	WAT	W	372	−17.485	40.033	−1.895	1.00	42.67
1433	OH2	WAT	W	373	10.911	38.587	20.026	1.00	41.59
1434	OH2	WAT	W	374	5.617	16.185	5.471	1.00	38.51
1435	OH2	WAT	W	375	5.058	38.594	−5.007	1.00	37.41
1436	OH2	WAT	W	376	7.267	44.085	25.369	1.00	41.82
1437	OH2	WAT	W	377	17.288	38.270	7.853	1.00	37.77
1438	OH2	WAT	W	378	10.919	19.053	11.527	1.00	39.48
1439	OH2	WAT	W	379	18.280	39.031	10.623	1.00	37.56
1440	OH2	WAT	W	380	8.958	43.761	17.287	1.00	39.15
1441	OH2	WAT	W	381	−11.761	40.530	9.983	1.00	40.41
1442	OH2	WAT	W	382	8.645	25.729	21.957	1.00	41.15
1443	OH2	WAT	W	383	12.776	23.515	−3.174	1.00	39.26
1444	OH2	WAT	W	384	1.500	48.497	0.811	1.00	42.98
1445	OH2	WAT	W	385	6.410	25.470	−8.821	1.00	42.34
1446	OH2	WAT	W	386	18.547	41.167	9.409	1.00	38.96
1447	OH2	WAT	W	387	−18.337	35.945	7.027	1.00	41.21
1448	OH2	WAT	W	388	−17.146	19.303	1.205	1.00	41.48
1449	OH2	WAT	W	389	−8.236	20.789	12.609	1.00	42.25
1450	OH2	WAT	W	390	−14.693	18.506	2.086	1.00	43.16
1451	OH2	WAT	W	391	10.531	22.385	17.929	1.00	38.36
1452	OH2	WAT	W	392	5.923	36.758	−6.984	1.00	43.87
1453	OH2	WAT	W	393	−4.095	47.470	−0.042	1.00	41.94
1454	OH2	WAT	W	394	2.227	24.121	−10.040	1.00	42.58
1455	OH2	WAT	W	395	0.739	16.533	−3.072	1.00	43.06
1456	OH2	WAT	W	396	8.462	45.631	21.908	1.00	37.63
1457	OH2	WAT	W	397	3.389	38.004	−10.331	1.00	43.14
1458	OH2	WAT	W	398	−4.299	38.307	−7.880	1.00	43.62
1459	OH2	WAT	W	399	−12.240	29.023	19.389	1.00	45.17
1460	OH2	WAT	W	400	7.768	47.162	23.911	1.00	45.18
1461	OH2	WAT	W	401	−15.550	21.715	6.543	1.00	45.05
1462	OH2	WAT	W	402	−13.415	46.294	12.126	1.00	39.05
1463	OH2	WAT	W	403	−7.012	9.727	0.551	1.00	31.21
1464	OH2	WAT	W	404	−6.831	45.423	−0.004	1.00	44.32
1465	OH2	WAT	W	405	1.401	36.546	−5.582	1.00	36.83
1466	OH2	WAT	W	406	6.714	40.039	5.978	1.00	26.38
1467	OH2	WAT	W	407	1.846	26.595	−12.694	1.00	41.70
1468	OH2	WAT	W	408	15.551	16.798	9.433	1.00	39.88
1469	OH2	WAT	W	409	−13.045	36.935	17.563	1.00	38.24
1470	OH2	WAT	W	410	−15.712	34.236	10.684	1.00	35.00
1471	OH2	WAT	W	411	8.412	28.930	−8.302	1.00	34.98
1472	OH2	WAT	W	412	−9.821	38.455	−8.616	1.00	37.51
1473	OH2	WAT	W	413	6.183	39.366	22.141	1.00	33.61
1474	OH2	WAT	W	414	−8.491	25.915	18.008	1.00	39.16
1475	OH2	WAT	W	415	12.368	34.247	1.800	1.00	34.92
1476	OH2	WAT	W	416	−1.315	11.452	−6.334	1.00	38.39
1477	OH2	WAT	W	417	15.835	15.071	15.103	1.00	41.32
1478	OH2	WAT	W	418	−8.602	41.350	15.721	1.00	28.93
1479	OH2	WAT	W	419	−16.014	40.490	2.677	1.00	39.46
1480	OH2	WAT	W	420	−19.535	29.475	−2.875	1.00	40.49
1481	OH2	WAT	W	421	12.703	39.037	5.886	1.00	42.65
1482	OH2	WAT	W	422	10.637	20.682	13.781	1.00	34.75
1483	OH2	WAT	W	423	10.352	21.563	−6.884	1.00	39.85
1484	OH2	WAT	W	424	−5.568	46.943	1.853	1.00	39.37
1485	OH2	WAT	W	425	13.509	35.976	3.341	1.00	40.52
1486	OH2	WAT	W	426	7.916	20.112	−8.973	1.00	42.90
1487	OH2	WAT	W	427	9.277	41.681	1.669	1.00	43.21
1488	OH2	WAT	W	428	0.833	18.171	1.190	1.00	42.90
1489	OH2	WAT	W	429	18.908	47.454	5.692	1.00	45.51
1490	OH2	WAT	W	430	−9.037	22.244	15.522	1.00	39.57

Claims

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

2. A crystal of murine IL-18, wherein said crystal effectively diffracts x-rays for the determination of the atomic coordinates of said murine IL-18 to a resolution of between about 1.3 Å and 5.0 Å.

3. The crystal as claimed in claim 2 that effectively diffracts x-rays for the determination of the atomic coordinates of said murine IL-18 to a resolution of between about 1.3 Å and 3.0 Å.

4. The crystal as claimed in claim 3 that effectively diffracts x-rays for the determination of the atomic coordinates of said murine IL-18 to a resolution of between about 1.3 Å and 2.5 Å.

5. The composition as claimed in claim 1, wherein said murine IL-18 is an essentially pure native form or a homolog thereof.

6. The composition as claimed in claim 1, wherein said composition has one or more patches of its surface in contact with its receptor; wherein said patches are lined by three groups of amino acid residues; wherein said first group comprises Ile15-Gln18, Val22-Pro27, Asp31-Asp36, Glu128-Ala131, Lys145-Met148; wherein said second group comprises Gly3-Thr8, Met 50-Gly58, Glu89-Asp92; and wherein said third group comprises Lys103-Asn109.

7. 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. 1-3.

8. The composition as claimed in claim 2, wherein said murine IL-18 is characterized by a β-trefoil fold.

9. A process of identifying an agonist or an antagonist molecule of murine IL-18, 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 murine 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 murine IL-18 corresponding to the coordinates of FIGS. 1-3 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 murine IL-18.

10. 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 murine IL-18 receptor.

11. A molecule identified by the method of claim 9, wherein said molecule is selected from a group consisting of: a peptide, a peptidomimetic and a synthetic compound.

12. A molecule identified by the method of claim 10, wherein said molecule is selected from a group consisting of: a peptide, a peptidomimetic and a synthetic compound.

13. The molecule as claimed in claim 11, wherein said molecule is selected from a group consisting of: an antagonist and an agonist.

14. The molecule as claimed in claim 12, wherein said molecule is selected from a group consisting of: an antagonist and an agonist.

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

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

17. The method as claimed in claim 16, wherein said entity is an agonist or an antagonist of murine IL-18.

18. The method of drug design as claimed in claim 16, wherein said method comprises the step of: using the structure coordinates of murine IL-18 to identify an intermediate in a chemical reaction between murine IL-18 and a compound which is a ligand of said murine IL-18.

19. The method as claimed in claim 16, wherein said structure coordinates comprises the coordinates of FIGS. 1-3 and Table I.

20. The method as claimed in claim 17, wherein said structure coordinates comprises the coordinates of FIGS. 1-3 and Table I.

21. The method as claimed in claim 18, wherein said structure coordinates comprises the coordinates of FIGS. 1-3 and Table I.