PDB-4e4s: Crystal structure of Pika GITRL

ID or keywords:

Entry

Database: PDB / ID: 4e4s

Title

Crystal structure of Pika GITRL

Components

Tumor necrosis factor ligand superfamily member 18

Keywords

IMMUNE SYSTEM / GITRL / GLUCOCORTICOID-INDUCED TNF RECEPTOR LIGAND /

TNFRSF18 /

Structural genomics / PSI-Biology / New York Structural Genomics Research Consortium / NYSGRC / IFN / Atoms-to-Animals: The Immune Function Network

Function / homology

Jelly Rolls - #40 / Jelly Rolls /

Sandwich / Mainly Beta

Function and homology information

Biological species

Ochotona princeps (American pika)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.95 Å

Authors

Kumar, P.R. / Bhosle, R. / Bonanno, J. / Chowdhury, S. / Gizzi, A. / Glen, S. / Hillerich, B. / Hammonds, J. / Seidel, R. / Toro, R. ...

Citation

Journal: to be published
Title: Crystal structure of GITRL from Ochotona princeps
Authors: Kumar, P.R. / Bhosle, R. / Bonanno, J. / Chowdhury, S. / Gizzi, A. / Glen, S. / Hillerich, B. / Hammonds, J. / Seidel, R. / Toro, R. / Nathenson, S.G. / Almo, S.C.

History

Deposition	Mar 13, 2012	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Mar 21, 2012	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4e4s.cif.gz	284.6 KB	Display	PDBx/mmCIF format
PDB format	pdb4e4s.ent.gz	244.6 KB	Display	PDB format
PDBx/mmJSON format	4e4s.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/e4/4e4s ftp://data.pdbj.org/pub/pdb/validation_reports/e4/4e4s	HTTPS FTP

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Related structure data

Similar structure data	2q1m-1 2r30-1 1vbi-d 3i0p-d 4z8u-d 4db5-1 5rai-1 2rgq-d Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Search similar-shape structures by Omokage search (details) Similarity search - Function & homologyF&H Search Similarity search - HomologyF&H Search
Other databases	TargetTrack: NYSGRC-011119

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Tumor necrosis factor ligand superfamily member 18

B: Tumor necrosis factor ligand superfamily member 18

C: Tumor necrosis factor ligand superfamily member 18

D: Tumor necrosis factor ligand superfamily member 18

E: Tumor necrosis factor ligand superfamily member 18

F: Tumor necrosis factor ligand superfamily member 18

hetero molecules

84.6 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Tumor necrosis factor ligand superfamily member 18

B: Tumor necrosis factor ligand superfamily member 18

F: Tumor necrosis factor ligand superfamily member 18

hetero molecules

defined by author
42.2 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Tumor necrosis factor ligand superfamily member 18

D: Tumor necrosis factor ligand superfamily member 18

E: Tumor necrosis factor ligand superfamily member 18

hetero molecules

defined by author
42.4 kDa, 3 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	49.371, 164.588, 54.103
Angle α, β, γ (deg.)	90.000, 117.160, 90.000
Int Tables number	4
Space group name H-M	P12₁1

Details

The biological assembly is a trimer. Two such trimers are present in the asymmetric unit (Chains A-C and chains D-F)

#1: Protein	Tumor necrosis factor ligand superfamily member 18 Mass: 13979.791 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Details: synthesized gene / Source: (gene. exp.) Ochotona princeps (American pika) / Strain: synthetic geneArtificial gene synthesis / Gene: GITRL / Plasmid: modified pET28b with N-terminal Smt3 tag / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
#2: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol Mass: 92.094 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₃H₈O₃
#3: Chemical	ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#4: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 241 / Source method: isolated from a natural source / Formula: H₂O

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Experiment

Experiment	Method: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal	Density Matthews: 2.33 Å³/Da / Density % sol: 47.25 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: Protein (20 mM Hepes, pH 7.5, 150 mM NaCl, 10% glycerol; Reservoir (0.2 M Calcium Chloride, 0.1 M HEPES:NaOH pH 7.5, 30% (w/v) PEG 4000); Cryoprotection (30% glycerol), Sitting Drop Vapor ...Details: Protein (20 mM Hepes, pH 7.5, 150 mM NaCl, 10% glycerol; Reservoir (0.2 M Calcium Chloride, 0.1 M HEPES:NaOH pH 7.5, 30% (w/v) PEG 4000); Cryoprotection (30% glycerol), Sitting Drop Vapor Diffusion, temperature 298K, VAPOR DIFFUSION, SITTING DROP

Crystal

Density Matthews: 2.33 Å³/Da / Density % sol: 47.25 %

Crystal grow

Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: Protein (20 mM Hepes, pH 7.5, 150 mM NaCl, 10% glycerol; Reservoir (0.2 M Calcium Chloride, 0.1 M HEPES:NaOH pH 7.5, 30% (w/v) PEG 4000); Cryoprotection (30% glycerol), Sitting Drop Vapor ...

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

NSLS

/ Beamline: X29A / Wavelength: 1.075 Å

Detector

Type: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 27, 2011 / Details: MIRRORS

Radiation

Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1.075 Å / Relative weight: 1

Reflection twin

Operator: h,-k,-h-l / Fraction: 0.441

Reflection

Resolution: 1.95→50 Å / Num. obs: 55662 / % possible obs: 100 % / Redundancy: 7.5 % / R_merge(I) obs: 0.094 / Χ²: 0.962 / Net I/σ(I): 8.9

Reflection shell

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique all	Χ²	Diffraction-ID	% possible all
1.95-1.98	7.4	0.755	2745	0.887	1	100
1.98-2.02	7.5	0.629	2771	0.902	1	100
2.02-2.06	7.5	0.551	2828	0.94	1	100
2.06-2.1	7.5	0.465	2748	0.959	1	100
2.1-2.15	7.6	0.392	2802	0.955	1	100
2.15-2.2	7.6	0.358	2746	0.963	1	100
2.2-2.25	7.6	0.294	2830	0.956	1	100
2.25-2.31	7.6	0.278	2710	0.987	1	100
2.31-2.38	7.6	0.24	2794	0.997	1	100
2.38-2.46	7.6	0.216	2849	0.987	1	100
2.46-2.54	7.6	0.181	2719	0.969	1	100
2.54-2.65	7.6	0.164	2752	0.993	1	100
2.65-2.77	7.6	0.136	2788	0.998	1	100
2.77-2.91	7.6	0.11	2786	0.99	1	100
2.91-3.1	7.6	0.095	2779	1.055	1	100
3.1-3.33	7.5	0.077	2803	1.097	1	100
3.33-3.67	7.4	0.062	2788	1.053	1	100
3.67-4.2	7.3	0.053	2797	0.949	1	100
4.2-5.29	7.2	0.047	2791	0.83	1	100
5.29-50	7.4	0.046	2836	0.757	1	99.9

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Processing

Software

Name	Version	Classification
DENZO		data reduction
SCALEPACK		data scaling
PHENIX	1.7.3_928	refinement
PDB_EXTRACT	3.1	data extraction
CBASS		data collection
PHENIX	1.7.3_928	phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 1.95→46.203 Å / Occupancy max: 1 / Occupancy min: 0.41 / FOM work R set: 0.7765 / σ(F): 1.36 / Phase error: 29.85 / Stereochemistry target values: TWIN_LSQ_F

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.1777	2616	5.14 %	RANDOM
R_work	0.1467	-	-	-
obs	0.1483	50869	91.35 %	-

Solvent computation

Shrinkage radii: 0.86 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL / B_sol: 40.01 Å² / k_sol: 0.377 e/Å³

Displacement parameters

B_iso max: 119.17 Å² / B_iso mean: 26.2909 Å² / B_iso min: 6.17 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	-2.2223 Å²	0 Å²	0.1262 Å²
2-	-	0.8726 Å²	-0 Å²
3-	-	-	1.3496 Å²

Refinement step

Cycle: LAST / Resolution: 1.95→46.203 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	5442	0	49	241	5732

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.006	5625
X-RAY DIFFRACTION	f_angle_d	1.094	7597
X-RAY DIFFRACTION	f_chiral_restr	0.072	827
X-RAY DIFFRACTION	f_plane_restr	0.004	975
X-RAY DIFFRACTION	f_dihedral_angle_d	13.936	2077

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 18

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
1.9505-1.988	0.2431	73	0.1844	1570	1643	51
1.988-2.0286	0.2289	94	0.176	1836	1930	60
2.0286-2.0727	0.2176	105	0.178	2080	2185	67
2.0727-2.1209	0.1677	137	0.1804	2265	2402	74
2.1209-2.1739	0.213	117	0.1617	2554	2671	82
2.1739-2.2327	0.2207	146	0.1681	2740	2886	89
2.2327-2.2984	0.2189	134	0.1729	2895	3029	94
2.2984-2.3726	0.197	164	0.1603	2969	3133	95
2.3726-2.4574	0.195	155	0.1654	2989	3144	95
2.4574-2.5558	0.2125	134	0.164	2903	3037	96
2.5558-2.6721	0.1782	148	0.1614	2922	3070	95
2.6721-2.8129	0.1992	159	0.1694	2940	3099	95
2.8129-2.9891	0.1725	173	0.1509	2928	3101	94
2.9891-3.2199	0.1986	166	0.1515	2928	3094	95
3.2199-3.5438	0.1622	170	0.1278	2928	3098	95
3.5438-4.0562	0.147	167	0.1156	2943	3110	95
4.0562-5.1092	0.1405	166	0.1042	2929	3095	95
5.1092-43.9398	0.1801	179	0.1633	2961	3140	94

Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

ID	L11 (°²)	L12 (°²)	L13 (°²)	L22 (°²)	L23 (°²)	L33 (°²)	S11 (Å °)	S12 (Å °)	S13 (Å °)	S21 (Å °)	S22 (Å °)	S23 (Å °)	S31 (Å °)	S32 (Å °)	S33 (Å °)	T11 (Å²)	T12 (Å²)	T13 (Å²)	T22 (Å²)	T23 (Å²)	T33 (Å²)	Origin x (Å)	Origin y (Å)	Origin z (Å)
1	0.4494	0.2347	-0.1385	0.4198	-0.2625	1.6257	-0.0849	0.0175	-0.0242	0.2197	0.121	0.1835	-0.009	-0.1289	-0.2367	0.2721	0.0296	0.1831	0.077	0.1093	0.0714	-25.0904	-22.3628	66.0495
2	1.3182	0.6635	-0.6592	1.61	-1.1349	1.4646	-0.1519	0.0592	-0.1287	0.1008	0.0901	0.1319	0.2148	-0.1231	-0.0001	0.2039	0.0042	0.137	0.0524	0.0075	0.1047	-20.6357	-32.0605	63.888
3	1.8357	-0.3192	2.6503	2.4452	0.2563	6.7227	-0.0957	-0.0211	0.1035	0.189	0.0642	-0.207	-0.4228	0.4943	0.0331	0.1594	-0.0685	-0.0414	0.1467	0.0092	0.0253	-3.9074	-16.7138	53.2278
4	3.6009	0.2624	-2.4159	0.0191	-0.1759	1.6209	-0.0064	-0.5575	0.0696	0.5324	0.0086	0.1309	-0.4117	0.371	0.0147	0.3284	-0.0008	0.0396	0.155	0.029	0.0864	-9.7442	-27.0467	67.5762
5	1.0474	0.403	-0.4328	1.0324	-0.6841	2.4104	-0.0537	-0.0747	-0.034	0.2101	-0.0915	0.0004	-0.1031	0.1778	-0.0168	0.2751	0.0148	0.0824	0.0902	0.0236	0.0406	-13.3551	-29.3019	63.8766
6	0.1446	-0.2853	0.2866	0.7908	-0.8519	1.1816	-0.0426	0.0329	0.0695	0.2426	0.1083	0.1728	-0.1818	-0.1218	-0.1311	0.2408	-0.0182	0.0767	0.0901	0.0375	0.045	-17.4465	-24.1837	60.4066
7	1.6252	0.278	0.8816	3.5241	1.6544	3.3829	0.1212	-0.3291	-0.2197	0.2771	-0.0679	0.1493	0.193	-0.1695	-0.0254	0.1282	0.0004	0.029	0.1007	0.0349	0.0816	-20.6902	-52.3632	74.7374
8	4.4898	0.88	1.7873	2.3576	0.7218	3.4505	0.1117	0.2219	-0.2207	-0.0193	-0.0049	-0.6579	-0.0448	0.7812	-0.0412	0.1867	-0.0204	0.0894	0.2507	0.0722	0.2344	-6.5101	-47.9908	68.5415
9	0.1135	0.0769	0.2164	0.2	0.2896	0.551	-0.0271	0.1268	0.1395	-0.1707	-0.0921	-0.5192	-0.1978	0.5672	-0.11	0.2296	-0.0524	0.0985	0.3582	0.1643	0.4258	-3.0895	-40.2893	67.589
10	2.4859	2.6277	1.1504	3.9559	-0.2047	3.0432	-0.0389	0.3036	-0.1546	-0.247	0.1512	-0.052	0.2661	0.3142	-0.0614	0.1655	0.0438	0.0879	0.1188	0.0185	0.0895	-16.0822	-52.595	63.6095
11	5.5414	1.5865	3.0204	1.7241	1.1198	5.0083	0.317	-0.296	-0.3622	0.0785	-0.1462	-0.3703	-0.0059	0.2074	-0.1151	0.1683	-0.0174	0.0421	0.1309	0.0883	0.1572	-11.793	-47.0612	72.3125
12	1.2631	0.4533	-0.2839	1.3102	-1.1238	0.9953	0.106	-0.3701	0.2326	0.2959	-0.1756	-0.0073	-0.2372	0.2629	0.0428	0.2184	0.0047	-0.073	0.1809	-0.067	0.1251	-29.8994	-70.8603	77.8941
13	1.2648	0.1212	0.1031	2.1883	-0.4392	1.4234	-0.0055	-0.1191	-0.0472	0.0826	0.0525	0.579	0.029	-0.5619	-0.019	0.118	-0.0003	-0.0318	0.2495	-0.064	0.191	-43.7585	-77.6198	74.2871
14	2.8438	3.5902	-0.996	4.5472	-1.034	3.661	-0.1113	0.1599	0.3876	-0.2439	0.1011	0.5484	-0.1908	-0.4857	0.065	0.1941	0.0311	-0.136	0.1744	-0.0464	0.2015	-41.6075	-70.4814	66.36
15	4.0135	0.5504	1.1965	3.5813	0.1173	3.6727	-0.1663	0.2865	-0.6413	-0.1792	-0.0247	0.9642	0.747	-0.8967	0.1883	0.3555	-0.1098	-0.0543	0.2925	-0.0576	0.3703	-46.2154	-83.2239	70.6955
16	3.3397	2.3293	-1.4771	3.8526	-0.7974	3.5829	0.1786	0.0828	0.2087	-0.1953	-0.231	0.0439	-0.3531	-0.1271	0.0129	0.1585	0.0332	-0.0848	0.0657	-0.0086	0.073	-33.2945	-70.6169	66.5198
17	3.1451	0.8866	-2.6171	1.4193	-1.401	4.2719	0.0539	-0.193	-0.054	-0.0763	-0.0888	0.3367	-0.0559	-0.0835	0.09	0.1459	0.0164	-0.0298	0.0674	-0.0788	0.2025	-36.6042	-75.8397	74.5677
18	5.3839	-2.1734	0.5627	5.7721	-0.0868	3.3769	0.0744	0.3428	0.1891	-0.1	-0.149	-0.6596	-0.162	0.6174	0.0677	0.1903	-0.0218	-0.0212	0.1998	0.0097	0.1332	-21.8096	-77.4227	47.0864
19	2.2852	-0.1069	1.5339	0.1155	-0.0366	1.8095	0.0132	0.0783	-0.0277	-0.0235	-0.0529	0.0142	0.0489	-0.0542	-0.0188	0.2496	0.0171	-0.1121	0.1016	-0.0266	0.0757	-36.2769	-81.5287	48.0289
20	6.5905	2.5805	7.1488	3.5422	2.1156	8.8139	-0.1607	-0.9824	0.1203	0.4565	-0.1231	0.3676	-0.1119	-1.0423	0.2375	0.1769	0.0261	-0.0297	0.2951	-0.0023	0.1826	-42.5188	-77.8225	53.5639
21	2.6444	-1.6367	-1.0091	4.439	0.089	2.9529	0.0882	0.0409	-0.1395	-0.2559	0.0439	-0.2767	0.3357	0.272	-0.074	0.2108	0.0284	-0.0419	0.0431	-0.0407	0.127	-27.0949	-87.2637	50.6751
22	0.6528	-0.1031	0.4565	1.6377	-0.324	1.4013	-0.1481	0.1953	0.1563	0.1174	-0.0711	-0.1096	-0.0393	0.0696	-0.0527	0.2377	0.0089	-0.1011	0.1333	-0.0534	0.0996	-31.2732	-77.2849	49.3776
23	0.1104	0.1057	-0.4258	0.275	-0.3092	1.7008	-0.0243	-0.098	0.0429	0.2942	0.0819	-0.2915	-0.0298	0.2275	-0.1759	0.3356	0.0596	-0.1821	0.0878	-0.1051	0.1704	-22.4507	-99.4954	69.2678
24	1.5223	0.6322	2.2664	1.2708	1.7597	4.6467	-0.0451	-0.1154	0.1127	0.2891	0.0724	-0.2148	0.0432	0.0395	-0.1239	0.2175	0.0255	-0.1188	0.056	-0.0289	0.1031	-26.9276	-89.6408	69.9834
25	0.2691	-0.1914	0.817	3.5868	2.9183	6.0329	0.0335	0.11	-0.1214	0.217	-0.0409	0.0895	0.4157	-0.4535	-0.0302	0.1596	-0.0152	0.0105	0.1188	-0.0418	0.0067	-43.6646	-105.0706	56.2957
26	2.0104	-0.383	1.7575	0.6718	-0.2982	1.5387	-0.0076	-0.5365	-0.0283	0.5656	-0.009	0.0082	0.0684	-0.6744	0.0339	0.3259	-0.0094	0.0425	0.1744	-0.0017	0.0529	-39.6513	-96.2868	71.2807
27	0.5179	0.2937	-0.174	0.8174	0.4751	1.0303	-0.0902	0.0004	0.0598	0.1569	-0.0002	-0.0403	-0.0241	-0.1447	-0.049	0.2943	0.0566	-0.0733	0.1164	-0.0292	0.0554	-36.4507	-91.9222	65.0346
28	3.025	-1.1277	2.6689	2.3469	2.4706	8.5891	0.1727	-0.38	-0.0665	0.5003	-0.3421	0.2446	0.76	-0.5805	0.1509	0.3556	-0.0444	-0.0278	0.1332	-0.0162	0.1019	-34.3722	-99.7104	72.3232
29	0.1944	-0.0833	0.0853	0.3858	0.5344	1.2119	-0.0476	0.0027	0.0036	0.186	0.1317	-0.1351	0.0387	0.0953	0.0359	0.2417	0.0409	-0.0747	0.0529	-0.0872	0.0665	-31.3466	-98.2251	64.3081
30	2.6972	-1.3326	-0.2372	4.3273	-0.3714	2.9658	-0.0131	0.2478	-0.5368	-0.2704	-0.0795	0.5766	0.2211	-0.5332	0.0683	0.2231	-0.0768	0.0024	0.2124	-0.0311	0.1865	-27.6116	-45.7722	44.0767
31	1.958	0.0962	-1.4264	0.0345	0.0382	1.4699	0.0383	-0.0096	0.1107	-0.0964	-0.077	-0.1114	-0.0961	0.1007	-0.04	0.2307	0.0185	0.0683	0.0961	0.0563	0.063	-13.1644	-41.7216	44.9794
32	5.2814	0.3348	-0.1495	2.52	-0.5554	0.1524	-0.2999	-0.1827	-0.1632	0.0988	0.1278	-0.2033	-0.0398	0.3175	0.1623	0.3048	-0.0122	0.0417	0.2535	0.015	0.1104	-6.8981	-45.5281	50.3956
33	4.2795	-2.1668	2.5604	4.829	-0.028	2.1098	-0.0795	0.0213	0.1348	-0.1643	-0.0095	0.0921	-0.5724	-0.2667	0.0139	0.2372	0.0355	0.0382	0.1251	0.0579	0.0921	-22.3641	-36.032	47.6577
34	2.5992	-1.9912	-1.198	4.0034	1.3306	0.7256	-0.1955	0.2315	-0.3462	0.0436	-0.0518	0.1844	0.2285	-0.2262	0.2489	0.1648	0.0271	0.0136	0.1557	0.0352	0.0827	-19.8534	-43.9489	47.6531

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resseq 4:39)	A	4 - 39
2	X-RAY DIFFRACTION	2	chain 'A' and (resseq 40:49)	A	40 - 49
3	X-RAY DIFFRACTION	3	chain 'A' and (resseq 50:61)	A	50 - 61
4	X-RAY DIFFRACTION	4	chain 'A' and (resseq 62:74)	A	62 - 74
5	X-RAY DIFFRACTION	5	chain 'A' and (resseq 75:99)	A	75 - 99
6	X-RAY DIFFRACTION	6	chain 'A' and (resseq 100:121)	A	100 - 121
7	X-RAY DIFFRACTION	7	chain 'B' and (resseq 4:39)	B	4 - 39
8	X-RAY DIFFRACTION	8	chain 'B' and (resseq 40:74)	B	40 - 74
9	X-RAY DIFFRACTION	9	chain 'B' and (resseq 75:84)	B	75 - 84
10	X-RAY DIFFRACTION	10	chain 'B' and (resseq 85:99)	B	85 - 99
11	X-RAY DIFFRACTION	11	chain 'B' and (resseq 100:121)	B	100 - 121
12	X-RAY DIFFRACTION	12	chain 'C' and (resseq 4:39)	C	4 - 39
13	X-RAY DIFFRACTION	13	chain 'C' and (resseq 40:61)	C	40 - 61
14	X-RAY DIFFRACTION	14	chain 'C' and (resseq 62:74)	C	62 - 74
15	X-RAY DIFFRACTION	15	chain 'C' and (resseq 75:84)	C	75 - 84
16	X-RAY DIFFRACTION	16	chain 'C' and (resseq 85:99)	C	85 - 99
17	X-RAY DIFFRACTION	17	chain 'C' and (resseq 100:123)	C	100 - 123
18	X-RAY DIFFRACTION	18	chain 'D' and (resseq 3:39)	D	3 - 39
19	X-RAY DIFFRACTION	19	chain 'D' and (resseq 40:74)	D	40 - 74
20	X-RAY DIFFRACTION	20	chain 'D' and (resseq 75:84)	D	75 - 84
21	X-RAY DIFFRACTION	21	chain 'D' and (resseq 85:99)	D	85 - 99
22	X-RAY DIFFRACTION	22	chain 'D' and (resseq 100:123)	D	100 - 123
23	X-RAY DIFFRACTION	23	chain 'E' and (resseq 3:39)	E	3 - 39
24	X-RAY DIFFRACTION	24	chain 'E' and (resseq 40:47)	E	40 - 47
25	X-RAY DIFFRACTION	25	chain 'E' and (resseq 48:61)	E	48 - 61
26	X-RAY DIFFRACTION	26	chain 'E' and (resseq 62:74)	E	62 - 74
27	X-RAY DIFFRACTION	27	chain 'E' and (resseq 75:93)	E	75 - 93
28	X-RAY DIFFRACTION	28	chain 'E' and (resseq 94:99)	E	94 - 99
29	X-RAY DIFFRACTION	29	chain 'E' and (resseq 100:123)	E	100 - 123
30	X-RAY DIFFRACTION	30	chain 'F' and (resseq 3:39)	F	3 - 39
31	X-RAY DIFFRACTION	31	chain 'F' and (resseq 40:74)	F	40 - 74
32	X-RAY DIFFRACTION	32	chain 'F' and (resseq 75:84)	F	75 - 84
33	X-RAY DIFFRACTION	33	chain 'F' and (resseq 85:99)	F	85 - 99
34	X-RAY DIFFRACTION	34	chain 'F' and (resseq 100:124)	F	100 - 124

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