PDB-5d5o: HcgC from Methanocaldococcus jannaschii

ID or keywords:

Entry

Database: PDB / ID: 5d5o

Title

HcgC from Methanocaldococcus jannaschii

Components

Uncharacterized protein MJ0489

Keywords

UNKNOWN FUNCTION / Rossmann-like fold

Function / homology

FeGP cofactor biosynthesis protein, methyltransferase HcgC / FeGP cofactor biosynthesis protein, methyltransferase HcgC / Uncharacterized protein MJ0489

Function and homology information

Biological species

Methanocaldococcus jannaschii (archaea)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 2.7 Å

Authors

Fujishiro, T. / Ermler, U. / Shima, S.

Funding support

Japan,

Germany, 2items

Citation

Journal: Angew.Chem.Int.Ed.Engl. / Year: 2016
Title: Identification of HcgC as a SAM-Dependent Pyridinol Methyltransferase in [Fe]-Hydrogenase Cofactor Biosynthesis.
Authors: Fujishiro, T. / Bai, L. / Xu, T. / Xie, X. / Schick, M. / Kahnt, J. / Rother, M. / Hu, X. / Ermler, U. / Shima, S.

History

Deposition	Aug 11, 2015	Deposition site: RCSB / Processing site: PDBE
Revision 1.0	Jul 20, 2016	Provider: repository / Type: Initial release
Revision 1.1	Aug 10, 2016	Group: Database references
Revision 1.2	May 8, 2024	Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	5d5o.cif.gz	797.5 KB	Display	PDBx/mmCIF format
PDB format	pdb5d5o.ent.gz	669.2 KB	Display	PDB format
PDBx/mmJSON format	5d5o.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/d5/5d5o ftp://data.pdbj.org/pub/pdb/validation_reports/d5/5d5o	HTTPS FTP

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Related structure data

Related structure data	5d4tC 5d4uC 5d4vC 5d5tC C: citing same article (ref.)
Similar structure data	5d4t-3 5d5t-2 5d4t-4 5d4u-2 5d4t-2 5a9s-d 5d5t-1 5fwn-d 5y8j-d 1gy7-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) 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

Related structure data

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI

Deposited unit

A: Uncharacterized protein MJ0489

B: Uncharacterized protein MJ0489

C: Uncharacterized protein MJ0489

D: Uncharacterized protein MJ0489

E: Uncharacterized protein MJ0489

F: Uncharacterized protein MJ0489

G: Uncharacterized protein MJ0489

H: Uncharacterized protein MJ0489

hetero molecules

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

1

A: Uncharacterized protein MJ0489

B: Uncharacterized protein MJ0489

hetero molecules

defined by author&software
61.2 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

C: Uncharacterized protein MJ0489

D: Uncharacterized protein MJ0489

defined by author&software
61.1 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

3

E: Uncharacterized protein MJ0489

F: Uncharacterized protein MJ0489

defined by author&software
61.1 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

4

G: Uncharacterized protein MJ0489

H: Uncharacterized protein MJ0489

defined by author&software
61.1 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	142.250, 143.280, 148.330
Angle α, β, γ (deg.)	90.000, 90.000, 90.000
Int Tables number	19
Space group name H-M	P2₁2₁2₁

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	chain A and segid A
2	1	chain B and segid B
3	1	chain C and segid C
4	1	chain D and segid D
5	1	chain E and segid E
6	1	chain F and segid F
7	1	chain G and segid G
8	1	chain H and segid H

NCS domain segments:

Dom-ID	Component-ID	Ens-ID	Selection details	Auth asym-ID
1	1	1	chain A and segid A	A
2	1	1	chain B and segid B	B
3	1	1	chain C and segid C	C
4	1	1	chain D and segid D	D
5	1	1	chain E and segid E	E
6	1	1	chain F and segid F	F
7	1	1	chain G and segid G	G
8	1	1	chain H and segid H	H

#1: Protein	Uncharacterized protein MJ0489 / HcgC Mass: 30566.113 Da / Num. of mol.: 8 / Fragment: Rossmann-like domain, residues 1-268 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Methanocaldococcus jannaschii (archaea) Gene: MJ0489 / Plasmid: pET24b / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q57913
#2: Chemical	ChemComp-SO4 / SULFATE ION / Sulfate Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO₄
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 38 / 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: 3.09 Å³/Da / Density % sol: 60.21 %
Crystal grow	Temperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 27 % (v/v) PEG400, 45 mM Tris-HCl, 45 mM sodium sulfate, 45 mM lithium sulfate and 0.2 M 2,2,2-trifuloroethanol

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Data collection

Diffraction

Mean temperature: 100 K

Diffraction source

Source:

SYNCHROTRON / Site:

SLS

/ Beamline: X10SA / Wavelength: 1 Å

Detector

Type: PSI PILATUS 6M / Detector: PIXEL / Date: Aug 13, 2012

Radiation

Monochromator: A double-crystal Si(111) monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray

Radiation wavelength

Wavelength: 1 Å / Relative weight: 1

Reflection

Resolution: 2.7→50 Å / Num. obs: 149108 / % possible obs: 92.7 % / Observed criterion σ(I): -3 / Redundancy: 2.7 % / B_iso Wilson estimate: 52.85 Å² / R_merge F obs: 0.33 / R_merge(I) obs: 0.125 / R_rim(I) all: 0.156 / Χ²: 1.107 / Net I/σ(I): 7.72 / Num. measured all: 405877

Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)	Highest resolution (Å)	R_merge F obs	R_merge(I) obs	Mean I/σ(I) obs	Num. measured obs	Num. possible	Num. unique obs	R_rim(I) all	% possible all
2.7-2.8		1.462	0.818	1.59	43622	16599	15878	1.008	95.7
2.8-3		1.043	0.58	2.35	70551	26949	25779	0.718	95.7
3-3.4		0.616	0.322	4.09	90942	36722	34649	0.404	94.4
3.4-4.1		0.254	0.136	8.79	87225	34670	31809	0.17	91.7
4.1-5.9		0.122	0.071	13.88	75298	30517	27620	0.088	90.5
5.9-8		0.098	0.056	16.45	23404	9244	8117	0.069	87.8
8-12		0.044	0.035	23.12	10046	4365	3721	0.043	85.2
	12	0.037	0.036	26.34	4789	1847	1535	0.043	83.1

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
XSCALE		data scaling
MOLREP		phasing
PHENIX		refinement
PDB_EXTRACT	3.15	data extraction
XDS		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT / Resolution: 2.7→48.326 Å / SU ML: 0.37 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 33.01 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2628	4163	5.26 %
R_work	0.2166	74978	-
obs	0.2191	79141	94.52 %

Solvent computation

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

Displacement parameters

B_iso max: 213.09 Å² / B_iso mean: 61.3534 Å² / B_iso min: 24.37 Å²

Refinement step

Cycle: final / Resolution: 2.7→48.326 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	15862	0	5	38	15905
B_iso mean	-	-	164.27	39.49	-
Num. residues	-	-	-	-	1966

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.008	16155
X-RAY DIFFRACTION	f_angle_d	1.254	21867
X-RAY DIFFRACTION	f_chiral_restr	0.053	2558
X-RAY DIFFRACTION	f_plane_restr	0.006	2757
X-RAY DIFFRACTION	f_dihedral_angle_d	13.235	5987

Refine LS restraints NCS

Ens-ID	Dom-ID	Auth asym-ID	Number	Refine-ID	Rms	Type
1	1	A	9511	X-RAY DIFFRACTION	12.24	TORSIONAL
1	2	B	9511	X-RAY DIFFRACTION	12.24	TORSIONAL
1	3	C	9511	X-RAY DIFFRACTION	12.24	TORSIONAL
1	4	D	9511	X-RAY DIFFRACTION	12.24	TORSIONAL
1	5	E	9511	X-RAY DIFFRACTION	12.24	TORSIONAL
1	6	F	9511	X-RAY DIFFRACTION	12.24	TORSIONAL
1	7	G	9511	X-RAY DIFFRACTION	12.24	TORSIONAL
1	8	H	9511	X-RAY DIFFRACTION	12.24	TORSIONAL

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 30

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.7-2.7307	0.3988	139	0.3387	2522	2661	98
2.7307-2.7628	0.3815	114	0.3123	2580	2694	97
2.7628-2.7965	0.3549	130	0.3095	2563	2693	98
2.7965-2.8319	0.3942	109	0.3103	2537	2646	97
2.8319-2.8691	0.3318	109	0.3	2593	2702	97
2.8691-2.9084	0.363	162	0.2929	2530	2692	97
2.9084-2.95	0.3404	155	0.2759	2482	2637	97
2.95-2.994	0.3214	170	0.283	2503	2673	96
2.994-3.0408	0.3748	147	0.2849	2542	2689	97
3.0408-3.0906	0.3044	140	0.2851	2555	2695	97
3.0906-3.1439	0.3336	132	0.2828	2492	2624	96
3.1439-3.2011	0.2998	130	0.2697	2548	2678	96
3.2011-3.2626	0.3104	150	0.2544	2524	2674	96
3.2626-3.3292	0.3084	138	0.2477	2503	2641	96
3.3292-3.4016	0.306	171	0.2285	2476	2647	96
3.4016-3.4807	0.2622	118	0.2374	2552	2670	95
3.4807-3.5677	0.2425	118	0.2114	2516	2634	96
3.5677-3.6641	0.2816	111	0.211	2536	2647	95
3.6641-3.7719	0.2477	125	0.2183	2481	2606	94
3.7719-3.8936	0.2551	142	0.2241	2502	2644	94
3.8936-4.0327	0.2252	142	0.2081	2493	2635	94
4.0327-4.1941	0.236	162	0.1836	2459	2621	94
4.1941-4.3848	0.2319	118	0.1674	2503	2621	94
4.3848-4.6159	0.2367	126	0.1558	2457	2583	93
4.6159-4.9048	0.2114	141	0.1615	2485	2626	93
4.9048-5.2831	0.2095	138	0.1697	2455	2593	92
5.2831-5.8139	0.2344	179	0.1915	2415	2594	92
5.8139-6.6534	0.237	193	0.1969	2378	2571	90
6.6534-8.3754	0.2229	114	0.1879	2435	2549	88
8.3754-48.3337	0.2228	140	0.1933	2361	2501	83

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	2.0739	-0.7145	-0.2488	9.8826	7.3684	6.4258	-0.1999	0.525	0.3004	-1.039	-0.1523	0.5247	-0.9362	-0.0229	0.4201	0.4423	0.0495	-0.104	0.5417	0.1333	0.3492	-28.4614	40.3046	-21.9332
2	2.3955	1.9743	5.3511	5.4015	2.6897	8.6251	-0.1159	0.4007	0.5748	-0.4358	-0.0464	0.5119	-0.1975	-0.2356	0.0485	0.4383	0.0161	-0.0984	0.7282	0.0018	0.5212	-34.8985	24.9264	-31.0771
3	7.5943	3.564	0.411	8.9542	-0.1039	8.1203	-0.0822	0.0491	0.4412	0.0859	-0.3256	1.1523	-0.0102	-1.2901	0.2593	0.3328	0.0494	-0.0168	0.7675	-0.0853	0.3632	-41.5071	16.3347	-27.4979
4	2.6203	1.8948	2.5352	3.0364	4.1154	4.2864	0.0886	0.0988	-0.332	0.0667	0.0011	-0.1761	0.2636	-0.0917	-0.0921	0.3064	0.0281	0.0126	0.4958	-0.0089	0.3069	-23.2826	17.5846	-20.9576
5	0.8731	1.0368	0.0489	5.455	3.3856	3.2154	-0.0782	0.1177	0.2541	-0.2077	-0.0511	0.6834	-0.019	-0.1607	0.1466	0.3323	0.097	-0.1049	0.3952	0.0625	0.4118	-27.8136	41.3798	-13.1066
6	3.1746	3.7463	1.6418	3.1025	5.6893	8.4845	0.5476	-0.8398	0.5402	1.8077	-1.1317	0.9738	1.2721	-0.2169	0.6283	0.4949	-0.0222	0.1044	0.7088	-0.0721	0.4638	-27.5306	41.3836	12.12
7	6.2425	-0.6025	0.6854	3.2896	-1.0168	2.0866	0.0701	-1.037	0.5602	0.8056	-0.5189	1.4339	0.0046	-1.4759	0.3929	0.6186	-0.1015	0.2538	1.3299	-0.5467	1.171	-33.9579	58.6438	20.7103
8	3.1667	-1.057	-2.4472	4.7211	2.5739	7.7822	0.1048	-0.8616	1.3203	-0.5035	0.2904	1.2091	-1.62	-0.401	-0.192	0.7275	-0.0274	0.1512	1.0661	-0.4958	1.1555	-31.074	69.6449	16.7408
9	3.2965	-1.8805	-4.0748	4.801	4.6555	9.8136	0.6245	-1.064	1.2618	0.4647	0.5472	-0.5004	-1.2702	0.6986	-0.9912	0.6795	-0.0922	0.0999	0.61	-0.2047	0.7658	-16.9143	65.6584	8.8426
10	1.3742	1.6198	-0.1353	5.2023	2.3818	2.525	-0.0853	-0.0897	0.5658	0.1109	0.0206	0.4988	-0.1035	-0.1006	0.0291	0.2222	0.0314	0.0323	0.3717	-0.0124	0.4586	-23.6674	44.5249	2.6589
11	2.2509	0.8492	0.1508	3.6456	2.7566	4.2535	0.0216	-0.2173	0.4078	0.1446	-0.1749	0.3579	-0.1249	-0.0942	0.1468	0.3261	-0.0602	0.0761	0.5719	0.06	0.3532	-27.8641	40.1977	6.2035
12	0.8941	1.6183	1.5071	6.9986	5.7885	4.5815	-0.2433	0.1482	0.3516	-1.534	0.3514	-0.0865	-1.4388	0.3579	-0.0518	0.7148	-0.1397	0.044	0.4476	0.0983	0.4978	7.723	61.0334	-5.5382
13	8.6286	2.2689	3.3822	5.6404	1.2843	7.4312	-0.2965	0.5498	0.4236	-0.5638	0.2	-1.0241	-0.5612	0.9233	0.175	0.4984	-0.0887	0.0501	0.4286	-0.0356	0.5977	17.9568	65.6482	6.6385
14	6.0871	5.3531	3.2489	9.8618	2.8722	3.1964	-0.0981	-0.5931	0.4907	0.1671	-0.2592	0.5731	-0.2269	0.1499	0.3085	0.3491	0.0624	0.0685	0.4207	-0.0281	0.3033	2.8159	63.1118	11.9282
15	0.5716	1.6108	0.9292	4.4148	4.0955	3.5122	-0.1114	0.1768	-0.034	-0.3865	0.0844	-0.0463	-0.556	0.2899	-0.0059	0.4129	-0.0511	0.0561	0.3571	0.1295	0.3253	5.3558	47.197	-8.888
16	-0.2292	-0.6073	-1.3693	7.4646	4.4535	4.0869	-0.3065	-0.3436	-0.2582	0.6728	0.5664	-0.2584	0.7145	0.6363	-0.2702	0.3197	0.1383	-0.0505	0.4645	0.095	0.4249	7.1593	16.6209	-7.9308
17	5.6096	-1.211	-2.2502	7.6531	2.1455	7.0235	0.2118	-0.4136	0.194	-0.1506	-0.1657	-0.7641	0.1572	1.1706	-0.0404	0.3032	0.1	0.0567	0.4816	0.0778	0.3194	15.0979	10.3176	-24.1589
18	3.5517	-3.4932	-1.9318	8.3526	2.3024	2.8716	0.0998	0.5444	-0.4729	-0.8212	-0.3622	1.0708	-0.0679	0.1005	0.2346	0.3374	0.08	-0.1459	0.4137	-0.0316	0.4371	-1.7323	16.5524	-26.6984
19	0.4826	0.057	0.487	5.2861	3.4073	2.9896	-0.0074	0.1187	0.0162	0.1406	-0.0685	-0.0246	0.0972	0.2645	0.0763	0.2443	0.0651	0.0048	0.4117	0.1405	0.331	3.2366	30.2832	-5.0643
20	2.0533	2.964	-3.3313	5.9171	-6.6838	9.1953	-0.1673	-0.6878	0.3956	1.3008	-0.1401	-0.4343	-0.9197	0.1947	-0.0194	0.4339	0.2256	0.0875	0.7694	0.0025	0.3529	23.8374	40.243	-52.3036
21	8.2192	-1.0091	0.4285	8.3868	1.0144	6.7135	-0.0841	-0.0705	0.3058	0.2632	-0.0602	-0.7141	0.1245	0.7592	0.2665	0.3849	0.1668	0.0628	0.7346	0.1085	0.4273	33.9819	19.9779	-45.317
22	1.7332	-0.9443	0.8464	2.977	-2.075	4.2156	-0.0208	0.1333	-0.2098	-0.3076	0.0157	-0.1059	0.332	-0.0375	0.0097	0.3983	0.1163	0.1196	0.5153	0.0069	0.3502	18.3853	17.4849	-53.2128
23	1.4346	0.9837	-0.1575	6.2655	-3.4852	3.3373	-0.0091	-0.07	-0.0691	-0.1392	-0.0773	-0.5233	0.0561	0.5756	0.037	0.3285	0.0618	0.0499	0.5608	-0.1279	0.3375	23.0649	41.3009	-61.1004
24	1.6112	-0.0766	-0.5841	2.3524	-3.0612	3.821	0.2901	0.9304	0.0494	-1.3229	-0.6875	-0.7539	0.8624	0.2252	0.3127	0.8596	0.2282	0.2147	0.7907	0.0252	0.5702	22.6012	41.3745	-86.335
25	3.2699	0.4007	-2.1872	1.7757	-1.1809	7.154	0.5321	0.8646	1.0006	-0.614	-0.5673	-0.963	-0.5397	1.0301	-0.0009	0.7216	0.1644	0.321	1.0057	0.3744	0.9622	23.8178	64.576	-90.4583
26	1.7658	-0.7928	0.1534	2.8706	-0.9647	1.1354	0.0084	0.2189	0.2589	-0.207	-0.0471	-0.4093	0.0754	0.1854	0.0193	0.4708	0.1585	0.1465	0.6445	0.042	0.381	22.5476	45.093	-76.6077
27	0.9971	-0.7127	0.1856	2.7134	-2.2942	1.5596	0.3065	0.2025	0.1038	-0.9165	-0.2857	-0.1657	0.4375	0.2455	-0.1537	0.6404	0.1442	0.0516	0.6728	-0.0488	0.3023	17.3715	37.3712	-82.1144
28	1.1618	2.0335	-2.1344	8.3995	-6.4219	5.295	-0.283	-0.9642	0.7661	0.9172	0.4614	0.0455	-0.8165	-0.8166	-0.0831	0.3854	0.0067	-0.0683	0.0628	-0.2076	0.6891	-10.7853	56.031	-63.504
29	7.4483	-0.4582	3.1351	6.7668	-0.778	6.1685	0.112	-0.52	-0.0609	-0.2655	0.0016	1.0728	0.006	-0.9509	-0.1396	0.2752	0.0073	-0.0185	0.5643	0.0003	0.6522	-21.1949	67.6794	-79.8467
30	5.4634	-4.0273	1.6441	7.1959	-3.1018	3.9103	0.1307	0.4816	0.3884	-0.5695	-0.2542	0.119	-0.2245	0.1349	0.1463	0.3996	-0.0647	-0.0712	0.3044	-0.0164	0.4534	-7.7123	63.3392	-85.6422
31	0.4657	-0.5432	-0.0827	6.3829	-2.8585	3.0084	0.0696	0.058	-0.0231	-0.3579	-0.0861	0.2775	0.2894	0.0237	0.0752	0.2901	0.0393	0.0344	0.35	-0.1323	0.3152	-10.1555	47.2834	-65.0837
32	0.379	1.2247	-0.7685	3.7186	-5.8415	8.095	-0.2338	0.1102	-0.2131	-0.9719	0.3726	0.0095	0.9448	-0.3731	-0.1481	0.7407	0.0288	0.0318	0.395	-0.1092	0.5056	-13.7651	15.7794	-64.0522
33	2.3039	3.1002	-1.3051	4.3892	-2.1921	1.9707	-0.0315	-0.2084	-0.3511	-0.3595	-0.291	-0.667	0.5798	0.2736	0.3416	0.5392	0.1626	0.0584	0.308	-0.0077	0.4919	-6.8857	15.7644	-49.8022
34	0.8886	-0.2095	0.1192	4.4202	-2.2396	4.4779	0.012	0.1064	-0.2245	-0.4657	0.0052	0.1842	0.4194	-0.0171	-0.0059	0.4128	-0.0727	-0.0379	0.291	-0.0781	0.3365	-9.8913	32.0195	-70.7513

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details	Auth asym-ID
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 13 through 42 )	A
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 43 through 69 )	A
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 70 through 116 )	A
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 117 through 184 )	A
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 185 through 268 )	A
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 13 through 42 )	B
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 43 through 96 )	B
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 97 through 139 )	B
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 140 through 166 )	B
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 167 through 221 )	B
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 222 through 268 )	B
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 13 through 55 )	C
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 56 through 105 )	C
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 106 through 184 )	C
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 185 through 268 )	C
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 13 through 69 )	D
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 70 through 116 )	D
18	X-RAY DIFFRACTION	18	chain 'D' and (resid 117 through 166 )	D
19	X-RAY DIFFRACTION	19	chain 'D' and (resid 167 through 268 )	D
20	X-RAY DIFFRACTION	20	chain 'E' and (resid 13 through 42 )	E
21	X-RAY DIFFRACTION	21	chain 'E' and (resid 43 through 116 )	E
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 117 through 184 )	E
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 185 through 268 )	E
24	X-RAY DIFFRACTION	24	chain 'F' and (resid 13 through 42 )	F
25	X-RAY DIFFRACTION	25	chain 'F' and (resid 43 through 166 )	F
26	X-RAY DIFFRACTION	26	chain 'F' and (resid 167 through 233 )	F
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 234 through 268 )	F
28	X-RAY DIFFRACTION	28	chain 'G' and (resid 13 through 42 )	G
29	X-RAY DIFFRACTION	29	chain 'G' and (resid 43 through 105 )	G
30	X-RAY DIFFRACTION	30	chain 'G' and (resid 106 through 184 )	G
31	X-RAY DIFFRACTION	31	chain 'G' and (resid 185 through 268 )	G
32	X-RAY DIFFRACTION	32	chain 'H' and (resid 13 through 91 )	H
33	X-RAY DIFFRACTION	33	chain 'H' and (resid 92 through 184 )	H
34	X-RAY DIFFRACTION	34	chain 'H' and (resid 185 through 268 )	H

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