PDB-4n0c: 42F3 TCR pCPE3/H-2Ld complex

ID or keywords:

Entry

Database: PDB / ID: 4n0c

Title

42F3 TCR pCPE3/H-2Ld complex

Components

42F3 VmCh alpha
42F3 VmCh beta
H-2 class I histocompatibility antigen, L-D alpha chain
pCPE3

Keywords

IMMUNE SYSTEM / Ig / TCR / MHC / antigen

Function / homology

Function and homology information

MHC class Ib protein complex / natural killer cell lectin-like receptor binding / TAP2 binding / TAP1 binding / cis-Golgi network membrane / T cell receptor complex / TAP complex binding / Golgi medial cisterna / CD8 receptor binding / beta-2-microglobulin binding ...
Similarity search - Function

Biological species

Mus musculus (house mouse)

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.9 Å

Authors

Birnbaum, M.E. / Adams, J.J. / Garcia, K.C.

Citation

Journal: Nat. Immunol. / Year: 2016
Title: Structural interplay between germline interactions and adaptive recognition determines the bandwidth of TCR-peptide-MHC cross-reactivity.
Authors: Adams, J.J. / Narayanan, S. / Birnbaum, M.E. / Sidhu, S.S. / Blevins, S.J. / Gee, M.H. / Sibener, L.V. / Baker, B.M. / Kranz, D.M. / Garcia, K.C.

History

Deposition	Oct 1, 2013	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Aug 19, 2015	Provider: repository / Type: Initial release
Revision 1.1	Sep 26, 2018	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2	Nov 27, 2024	Group: Data collection / Database references / Structure summary Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_ref_seq_dif Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4n0c.cif.gz	505.1 KB	Display	PDBx/mmCIF format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/n0/4n0c ftp://data.pdbj.org/pub/pdb/validation_reports/n0/4n0c	HTTPS FTP

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Related structure data

Related structure data	4ms8C 4mvbC 4mxqC 4n5eC 3tf7 3tfk 3tjh 3tpu C: citing same article (ref.)
Similar structure data	3tfk-d 3cxn-d 3tpu-1 4n5e-d 6l9l-1 3tpu-4 3tpu-2 4mvb-d 3tjh-d 6l9l-2 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 - FunctionF&H Search Similarity search - HomologyF&H Search

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#63 - Mar 2005 T-Cell Receptor similarity (4) #62 - Feb 2005 Major Histocompatibility Complex similarity (3) #21 - Sep 2001 Antibodies similarity (1) #256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1) #209 - May 2017 Tissue Transglutaminase and Celiac Disease similarity (1)

Deposited unit

A: H-2 class I histocompatibility antigen, L-D alpha chain

B: pCPE3

C: 42F3 VmCh alpha

D: 42F3 VmCh beta

E: H-2 class I histocompatibility antigen, L-D alpha chain

F: pCPE3

G: 42F3 VmCh alpha

H: 42F3 VmCh beta

146 kDa, 8 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: H-2 class I histocompatibility antigen, L-D alpha chain

B: pCPE3

C: 42F3 VmCh alpha

D: 42F3 VmCh beta

defined by author
72.8 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

E: H-2 class I histocompatibility antigen, L-D alpha chain

F: pCPE3

G: 42F3 VmCh alpha

H: 42F3 VmCh beta

defined by author
72.8 kDa, 4 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	102.450, 102.450, 325.660
Angle α, β, γ (deg.)	90.00, 90.00, 120.00
Int Tables number	152
Space group name H-M	P3₁21

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID
1	1
2	2
3	3
4	4

/ NCS ensembles :

ID
1
2
3
4

#1: Protein	H-2 class I histocompatibility antigen, L-D alpha chain Mass: 21115.303 Da / Num. of mol.: 2 / Fragment: UNP residues 25-203 / Mutation: F8Y, V12T, P15R, I23T, N30D, A49V, K131R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: H2-L / Production host: Escherichia coli (E. coli) / References: UniProt: P01897
#2: Protein/peptide	pCPE3 Mass: 1043.219 Da / Num. of mol.: 2 / Source method: obtained synthetically / Details: synthetic peptide
#3: Antibody	42F3 VmCh alpha Mass: 23383.928 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus, Homo sapiens / Production host: Escherichia coli (E. coli) / References: UniProt: P01738*PLUS
#4: Protein	42F3 VmCh beta Mass: 27248.180 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus, Homo sapiens / Production host: Escherichia coli (E. coli) / References: UniProt: A0A075B5I3*PLUS
Has protein modification	Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 3.39 Å³/Da / Density % sol: 63.71 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.6 Details: 17% PEG 3350 and 100mM BiS-TRIS, pH 6.6 and 200mM magnesium nitrate, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9795 Å
Detector	Type: PSI PILATUS 6M / Detector: PIXEL / Date: Feb 24, 2011
Radiation	Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9795 Å / Relative weight: 1
Reflection	Resolution: 2.68→88.72 Å / Num. all: 56842 / Num. obs: 56729 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0
Reflection shell	Resolution: 2.68→2.76 Å / % possible all: 99.9

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Processing

Software

Name	Version	Classification
Blu-Ice		data collection
PHASER		phasing
PHENIX	(phenix.refine: 1.8.2_1309)	refinement
MOSFLM		data reduction
SCALA		data scaling

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.9→59.987 Å / σ(F): 1.91 / Phase error: 24.63 / Stereochemistry target values: TWIN_LSQ_F

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2472	4231	5.02 %	random
R_work	0.1915	-	-	-
obs	0.1954	44888	99.37 %	-

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 2.9→59.987 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9790	0	0	0	9790

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.006	10057
X-RAY DIFFRACTION	f_angle_d	0.967	13651
X-RAY DIFFRACTION	f_dihedral_angle_d	14.513	3586
X-RAY DIFFRACTION	f_chiral_restr	0.039	1419
X-RAY DIFFRACTION	f_plane_restr	0.005	1788

LS refinement shell

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Refine-ID	% reflection obs (%)
2.9005-2.9505	0.424	217	0.3867	3969	X-RAY DIFFRACTION	94
2.9505-3.0041	0.3849	208	0.3547	4060	X-RAY DIFFRACTION	94
3.0041-3.0619	0.3451	202	0.3243	3888	X-RAY DIFFRACTION	94
3.0619-3.1243	0.3427	214	0.3104	3991	X-RAY DIFFRACTION	93
3.1243-3.1923	0.3427	204	0.2978	4037	X-RAY DIFFRACTION	95
3.1923-3.2665	0.2637	207	0.2686	3966	X-RAY DIFFRACTION	94
3.2665-3.3481	0.3828	210	0.2483	4022	X-RAY DIFFRACTION	94
3.3481-3.4386	0.2989	217	0.2343	3976	X-RAY DIFFRACTION	94
3.4386-3.5398	0.2825	203	0.2193	4010	X-RAY DIFFRACTION	95
3.5398-3.654	0.2366	218	0.2172	4014	X-RAY DIFFRACTION	95
3.654-3.7845	0.2651	216	0.201	4000	X-RAY DIFFRACTION	94
3.7845-3.9359	0.2597	207	0.1882	3989	X-RAY DIFFRACTION	94
3.9359-4.1149	0.2446	210	0.1801	4028	X-RAY DIFFRACTION	95
4.1149-4.3317	0.2289	206	0.1574	3980	X-RAY DIFFRACTION	95
4.3317-4.6028	0.1777	207	0.145	4042	X-RAY DIFFRACTION	95
4.6028-4.9577	0.2101	194	0.1425	3975	X-RAY DIFFRACTION	95
4.9577-5.4557	0.2139	202	0.1492	4037	X-RAY DIFFRACTION	95
5.4557-6.243	0.2138	216	0.1621	4007	X-RAY DIFFRACTION	95
6.243-7.8576	0.2403	223	0.1609	4019	X-RAY DIFFRACTION	94
7.8576-42.8067	0.2179	229	0.1517	3961	X-RAY DIFFRACTION	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	1.5021	-0.0655	0.3356	0.2684	-0.3312	0.3398	-0.3276	0.8047	-0.4041	-0.0112	-0.1458	-0.5601	0.3737	0.1051	0.1568	0.8337	-0.4641	0.1009	0.8118	-0.0515	0.5685	4.0151	77.0148	312.2081
2	1.1036	-0.2121	0.031	1.6295	-0.7096	1.2033	-0.1447	0.2828	-0.0752	-0.4755	0.1149	-0.0991	0.0013	0.2159	0.1004	0.5815	-0.1397	0.0129	0.445	-0.1336	0.5853	5.4865	79.9822	313.6549
3	0.5781	-0.3616	-1.0136	0.2755	0.4992	2.1735	-0.1471	0.5295	-0.165	-0.0775	0.1658	-0.2238	-0.4206	-0.8307	-0.0239	0.5723	-0.2854	-0.1649	0.6245	0.2062	0.9052	-7.7682	94.2268	317.8013
4	0.5826	-0.6328	0.3532	0.9909	-0.1223	0.4195	-0.6146	-0.128	-0.2492	-0.2846	0.2578	-0.0507	-0.0836	0.3654	0.233	0.3852	-0.1758	0.072	0.5778	0.0121	0.4933	4.3964	92.0508	316.0651
5	0.1023	-0.0037	-0.2114	2.5966	0.0791	1.7574	0.2093	0.1123	0.0595	0.2705	0.0946	-0.4086	-0.3517	0.1111	0.4814	0.429	-0.0858	-0.0579	0.0681	0.1849	1.0875	6.25	85.3984	321.7397
6	2.9985	0.8067	0.6873	0.7061	-0.9828	2.9691	0.3878	-0.4058	0.2257	0.3943	-0.6668	0.0029	0.5448	0.9278	0.0044	0.5778	-0.0782	-0.0607	0.5868	0.0574	0.5799	20.4328	108.9333	339.2671
7	1.3154	0.0837	-1.5094	0.6836	0.544	2.3272	-0.5848	0.1112	0.0241	-0.3388	0.1726	0.1482	0.7314	0.0953	0.4142	0.4489	0.0381	-0.0851	0.3514	0.0429	0.6599	17.4012	99.9718	330.9188
8	1.6801	0.6121	0.3455	0.7937	0.0524	1.0946	0.1478	-0.2574	0.2132	-0.0855	-0.2395	-0.1024	0.1413	-0.7383	0.0617	0.3568	-0.0851	-0.0623	0.2861	0.0684	0.4074	11.4238	105.2797	335.2254
9	1.5018	-0.0607	0.3563	0.7295	0.3574	1.2879	0.2573	0.0832	-0.1335	0.226	-0.1677	0.0077	-0.4216	0.086	-0.358	0.4492	0.0508	0.0606	0.5441	0.4224	0.4669	17.8508	92.4256	332.8181
10	0.2569	-0.1842	-0.034	0.7275	1.0455	1.7809	0.2022	-0.476	0.0553	-0.4285	0.4789	-0.3484	-0.9535	-0.2494	-0.4495	0.5953	-0.1299	0.2699	0.9071	0.1901	0.8767	20.6315	116.436	365.1125
11	1.9626	-0.4039	0.5762	0.6051	-0.2561	1.5084	-0.1881	0.4487	0.1716	-0.6282	0.2221	-0.8268	-0.9741	0.6838	0.0009	0.9861	-0.3494	0.0977	0.5408	-0.1277	1.0644	15.1826	112.496	362.3776
12	0.8965	-0.5659	1.4014	1.1092	-0.318	2.6303	-0.2167	-0.5737	-0.0852	-0.194	-0.3959	-0.4354	-0.4683	0.2165	0.3786	1.3313	-0.2497	0.371	0.6963	0.1827	0.6948	15.5236	114.7184	363.5778
13	2.2372	0.511	-0.2031	5.379	1.1507	2.9109	-0.3373	0.0471	-0.4731	1.1848	0.5711	-0.8593	0.197	-0.679	-0.703	0.6805	-0.2154	-0.0865	0.9486	0.2509	0.6853	29.7275	118.7639	370.5362
14	0.441	0.5567	-0.0157	1.6945	-0.8732	1.4753	0.1169	-0.2274	-0.6245	0.166	-0.0416	-0.4152	0.4414	0.3791	0.0482	0.2897	0.0748	0.0374	0.4153	0.0144	0.639	14.8537	82.2103	344.24
15	1.5138	1.0001	0.0387	1.6529	0.5191	1.575	0.3416	-0.4243	-0.6612	0.0384	0.0471	-0.1371	0.4776	0.5897	-0.2178	0.1878	0.0536	0.0175	0.4374	-0.042	0.5378	19.3775	87.831	355.006
16	1.2018	-0.2908	-0.3528	1.27	-0.215	1.4256	0.0335	-0.1851	0.3992	-0.6403	0.0885	-0.0095	-0.6477	0.4123	-0.0983	0.6052	-0.1758	-0.116	0.603	0.1058	0.6557	14.9421	106.0246	370.9107
17	2.8359	-0.1101	-1.0737	1.5639	-0.1381	0.8784	0.3172	0.2547	0.3025	-0.2686	-0.1301	-0.2009	-0.4481	0.5771	-0.217	0.4933	-0.0729	-0.0239	0.5836	0.0085	0.3734	16.8487	104.0206	366.4266
18	1.8736	0.1095	-0.0404	1.3406	-1.529	1.7633	0.0517	0.2305	-0.3212	0.0799	-0.1048	-0.2005	-0.7443	0.6401	-0.0925	0.4078	-0.2107	-0.1281	0.639	0.137	0.3514	7.3704	101.0521	374.6484
19	1.062	0.0667	0.2643	2.3632	1.3638	1.4818	0.1497	-0.0501	0.1483	-0.3953	0.4212	-0.7372	0.0218	0.6344	-0.4914	0.322	-0.0445	0.0535	0.7337	0.148	0.6042	18.0576	88.6218	373.984
20	0.2403	0.1245	0.0923	0.3015	-0.3128	0.7464	-0.2022	-0.0624	-0.0471	0.1	0.1084	-0.0605	-0.2384	-0.1224	-0.8036	0.7878	0.2501	0.3771	0.8149	0.6046	0.5381	-4.2763	83.524	397.4842
21	0.9359	0.3175	0.6267	1.18	-0.3645	1.5958	0.309	0.0523	-0.3858	-0.1747	0.1992	-0.0223	0.5448	-0.2966	-0.0177	0.9811	-0.32	-0.1627	0.6941	0.4596	0.5291	-5.1774	70.7512	388.4058
22	1.9159	-0.4372	0.3579	1.8914	-0.2242	0.8141	-0.1931	-0.7489	-0.4735	0.3533	-0.0469	0.4546	0.0583	0.2219	0.1219	0.5495	-0.0409	0.172	0.594	0.0841	0.4574	-6.3141	79.9695	391.4089
23	0.994	-0.2909	-0.6009	1.7065	1.125	3.12	-0.1806	-0.2991	-0.0333	-0.1789	-0.1129	0.219	-0.846	0.4076	0.3078	0.6894	-0.1564	-0.0861	0.5066	0.0693	0.3397	-2.1042	92.2037	388.5116
24	0.501	0.335	0.1575	0.4961	0.4181	0.4038	-0.3031	0.3479	0.4829	-0.2049	0.4128	0.3455	-0.3291	-0.0451	0.1646	0.2317	0.0108	0.0251	0.5551	0.1977	0.7412	-7.142	85.2851	383.8901
25	0.2481	0.2566	0.3744	0.3232	-0.0316	1.5643	-0.0961	0.0702	0.0222	-0.0203	-0.1855	0.3462	-0.2623	-1.3226	0.1406	0.4021	0.1528	0.0959	0.4599	-0.1116	0.5819	-17.2888	103.6657	368.9839
26	0.7811	-0.0645	0.3271	0.185	0.5301	1.3141	0.3095	0.0656	-0.1742	-0.2724	-0.3618	-0.1396	0.303	-0.1113	-0.0044	0.5995	0.1537	0.1301	0.3627	-0.0681	0.5316	-12.6908	106.8193	368.7244
27	0.1794	0.1017	-0.7396	0.6643	0.4212	4.1731	-0.2505	-0.008	0.21	-0.0867	-0.1518	0.3348	-0.0181	-0.8509	0.0834	0.9371	0.7641	-0.1094	0.39	-0.0009	0.8102	-23.6412	113.4547	337.7168
28	1.0307	0.0699	-0.2076	0.5074	-0.3574	0.899	0.204	0.4934	0.4613	0.1279	0.0133	0.7071	-0.4587	-0.015	-0.1543	0.4684	0.0171	-0.0541	0.4367	0.1745	1.154	-20.1883	116.2858	338.2959
29	0.5359	-0.2862	0.8116	1.4788	0.0379	1.2881	-0.1321	-0.1102	-0.5396	0.2841	0.1247	0.3528	0.0015	-0.3638	-0.0149	0.5165	0.0472	0.1554	0.5229	-0.0575	0.3693	-15.6721	82.0994	361.2303
30	1.2241	-0.9273	0.4713	1.5823	-0.2502	1.1834	-0.2127	0.3321	-0.1894	-0.1243	0.0441	0.2404	-0.4096	-0.0735	0.0249	0.4399	0.0223	0.1058	0.5215	-0.2161	0.5567	-20.1544	87.9557	350.6479
31	0.8508	0.1485	-0.4994	2.0932	-0.3629	1.2483	0.4425	0.4521	0.1112	-0.2764	-0.2878	0.7707	-0.1783	-0.4173	-0.2178	0.3634	0.1415	-0.0324	0.7151	0.0083	0.4146	-15.4257	106.3647	334.6742
32	0.6447	-0.1116	0.1279	1.3489	-0.0021	1.0962	-0.0934	0.4771	0.27	0.0355	0.1172	0.7603	-0.6101	-0.4026	-0.019	0.4817	0.1838	-0.0497	0.6093	0.0046	0.5034	-17.0438	104.3709	339.0141
33	1.0439	-0.3499	-0.0376	1.9299	-0.4963	0.5862	-0.0334	0.1623	0.0928	-0.3455	0.2912	0.9613	0.019	0.2215	-0.1059	0.3664	-0.0677	-0.1053	0.7888	-0.1933	0.5129	-15.3893	92.8281	331.1709

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 2 through 28 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 29 through 126 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 127 through 137 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 138 through 175 )
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 1 through 9 )
6	X-RAY DIFFRACTION	6	chain 'C' and (resid 0 through 20 )
7	X-RAY DIFFRACTION	7	chain 'C' and (resid 21 through 37 )
8	X-RAY DIFFRACTION	8	chain 'C' and (resid 38 through 94 )
9	X-RAY DIFFRACTION	9	chain 'C' and (resid 95 through 107 )
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 108 through 154 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 155 through 168 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 169 through 178 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 179 through 197 )
14	X-RAY DIFFRACTION	14	chain 'D' and (resid 3 through 96 )
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 97 through 120 )
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 121 through 158 )
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 159 through 199 )
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 200 through 211 )
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 212 through 241 )
20	X-RAY DIFFRACTION	20	chain 'E' and (resid 2 through 12 )
21	X-RAY DIFFRACTION	21	chain 'E' and (resid 13 through 28 )
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 29 through 126 )
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 127 through 175 )
24	X-RAY DIFFRACTION	24	chain 'F' and (resid 1 through 9 )
25	X-RAY DIFFRACTION	25	chain 'G' and (resid 0 through 43 )
26	X-RAY DIFFRACTION	26	chain 'G' and (resid 44 through 120 )
27	X-RAY DIFFRACTION	27	chain 'G' and (resid 121 through 162 )
28	X-RAY DIFFRACTION	28	chain 'G' and (resid 163 through 200 )
29	X-RAY DIFFRACTION	29	chain 'H' and (resid 3 through 96 )
30	X-RAY DIFFRACTION	30	chain 'H' and (resid 97 through 120 )
31	X-RAY DIFFRACTION	31	chain 'H' and (resid 121 through 158 )
32	X-RAY DIFFRACTION	32	chain 'H' and (resid 159 through 199 )
33	X-RAY DIFFRACTION	33	chain 'H' and (resid 200 through 241 )

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