PDB-3md9: Structure of apo form of a periplasmic heme binding protein

ID or keywords:

Entry

Database: PDB / ID: 3md9

Title

Structure of apo form of a periplasmic heme binding protein

Components

Hemin-binding periplasmic protein hmuT

Keywords

TRANSPORT PROTEIN / alpha beta protein / rigid helical backbone / substrate-free / heme transport / Iron transport

Function / homology

Function and homology information

: / monoatomic ion transport /

periplasmic space
Similarity search - Function

Biological species

Yersinia pestis (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 1.5 Å

Authors

Mattle, D. / Goetz, B.A. / Locher, K.P.

Citation

Journal: J.Mol.Biol. / Year: 2010
Title: Two stacked heme molecules in the binding pocket of the periplasmic heme-binding protein HmuT from Yersinia pestis.
Authors: Mattle, D. / Zeltina, A. / Woo, J.S. / Goetz, B.A. / Locher, K.P.

History

Deposition	Mar 30, 2010	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Sep 15, 2010	Provider: repository / Type: Initial release
Revision 1.1	Jul 13, 2011	Group: Version format compliance
Revision 1.2	Sep 6, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	3md9.cif.gz	211.8 KB	Display	PDBx/mmCIF format
PDB format	pdb3md9.ent.gz	169.6 KB	Display	PDB format
PDBx/mmJSON format	3md9.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/md/3md9 ftp://data.pdbj.org/pub/pdb/validation_reports/md/3md9	HTTPS FTP

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Related structure data

Related structure data	3nu1C 3md8 PDB Unreleased entryS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	5y8b-d 3nu1-2 6cfv-d 5khl-d 5vqh-2 2phz-d 4pup-1 4wep-1 4n4i-d 5c6c-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 - 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	#122 - Feb 2010 Enhanceosome similarity (1) #220 - Apr 2018 Dehalogenases similarity (1)

Deposited unit

A: Hemin-binding periplasmic protein hmuT

B: Hemin-binding periplasmic protein hmuT

hetero molecules

54.7 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

A: Hemin-binding periplasmic protein hmuT

hetero molecules

defined by author&software
27.3 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Hemin-binding periplasmic protein hmuT

hetero molecules

defined by author&software
27.4 kDa, 1 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	61.710, 66.740, 62.270
Angle α, β, γ (deg.)	90.00, 110.70, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Hemin-binding periplasmic protein hmuT Mass: 26967.174 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Yersinia pestis (bacteria) / Gene: hmuT, YPO0281, y0541, YP_0436 / Production host: Escherichia coli (E. coli) / References: UniProt: Q56991
#2: Chemical	ChemComp-BR / BROMIDE ION / Bromide Mass: 79.904 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Br
#3: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₃H₈O₃
#4: Chemical	ChemComp-SO4 / SULFATE ION / Sulfate Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO₄
#5: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 537 / 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: 2.22 Å³/Da / Density % sol: 44.69 %
Crystal grow	Temperature: 283 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 29% (w/v) PEG 5K MME, 0.1 M Magnesium acetate, 0.1 MES, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 283K

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Data collection

Diffraction source	Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.9191 Å
Detector	Type: PSI PILATUS 6M / Detector: PIXEL / Date: Oct 11, 2009
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9191 Å / Relative weight: 1
Reflection	Resolution: 1.48→29.13 Å / Num. all: 78325 / Num. obs: 78325 / R_merge(I) obs: 0.089 / R_sym value: 0.089 / Net I/σ(I): 14.24
Reflection shell	Resolution: 1.48→1.52 Å / R_merge(I) obs: 0.528 / Mean I/σ(I) obs: 4.31 / % possible all: 97

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Processing

Software

Name	Version	Classification
XDS		data scaling
PHENIX	(phenix.refine)	refinement
XDS		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3MD8

3md8
PDB Unreleased entry

Resolution: 1.5→29.125 Å / SU ML: 0.17 / σ(F): 1.8 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.1812	5289	7.05 %	Random
R_work	0.1521	-	-	-
obs	0.1541	75064	99.2 %	-

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / B_sol: 62.718 Å² / k_sol: 0.38 e/Å³

Displacement parameters

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.757 Å²	-0 Å²	0.567 Å²
2-	-	-1.166 Å²	-0 Å²
3-	-	-	0.408 Å²

Refinement step

Cycle: LAST / Resolution: 1.5→29.125 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	3730	0	18	537	4285

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.009	3791
X-RAY DIFFRACTION	f_angle_d	1.195	5145
X-RAY DIFFRACTION	f_dihedral_angle_d	14.651	1412
X-RAY DIFFRACTION	f_chiral_restr	0.073	622
X-RAY DIFFRACTION	f_plane_restr	0.005	668

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 (%)
1.5-1.517	0.2177	208	0.1809	2313	X-RAY DIFFRACTION	100
1.517-1.5349	0.2035	186	0.1694	2271	X-RAY DIFFRACTION	99
1.5349-1.5536	0.2261	187	0.1675	2306	X-RAY DIFFRACTION	100
1.5536-1.5733	0.19	206	0.1645	2322	X-RAY DIFFRACTION	99
1.5733-1.594	0.1961	163	0.155	2327	X-RAY DIFFRACTION	99
1.594-1.6158	0.1873	164	0.1506	2308	X-RAY DIFFRACTION	99
1.6158-1.6389	0.1815	173	0.1511	2339	X-RAY DIFFRACTION	99
1.6389-1.6633	0.1739	173	0.1473	2315	X-RAY DIFFRACTION	99
1.6633-1.6893	0.1903	191	0.1457	2301	X-RAY DIFFRACTION	99
1.6893-1.717	0.1818	163	0.1514	2349	X-RAY DIFFRACTION	99
1.717-1.7466	0.1815	188	0.1414	2279	X-RAY DIFFRACTION	99
1.7466-1.7784	0.1822	195	0.143	2273	X-RAY DIFFRACTION	98
1.7784-1.8126	0.1832	185	0.1479	2300	X-RAY DIFFRACTION	99
1.8126-1.8496	0.1766	186	0.1434	2246	X-RAY DIFFRACTION	98
1.8496-1.8898	0.1681	153	0.1396	2374	X-RAY DIFFRACTION	99
1.8898-1.9337	0.1726	179	0.1333	2352	X-RAY DIFFRACTION	100
1.9337-1.9821	0.1583	157	0.1385	2337	X-RAY DIFFRACTION	100
1.9821-2.0357	0.1352	191	0.1377	2322	X-RAY DIFFRACTION	100
2.0357-2.0956	0.1546	190	0.1277	2317	X-RAY DIFFRACTION	100
2.0956-2.1632	0.1527	174	0.1355	2357	X-RAY DIFFRACTION	100
2.1632-2.2405	0.1584	148	0.1335	2338	X-RAY DIFFRACTION	99
2.2405-2.3301	0.1845	192	0.1384	2318	X-RAY DIFFRACTION	99
2.3301-2.4361	0.1881	140	0.1513	2348	X-RAY DIFFRACTION	99
2.4361-2.5645	0.1798	153	0.1537	2329	X-RAY DIFFRACTION	98
2.5645-2.7251	0.1925	159	0.1573	2303	X-RAY DIFFRACTION	98
2.7251-2.9353	0.1806	182	0.1565	2369	X-RAY DIFFRACTION	100
2.9353-3.2303	0.1738	173	0.1558	2342	X-RAY DIFFRACTION	100
3.2303-3.697	0.167	176	0.1432	2365	X-RAY DIFFRACTION	100
3.697-4.6547	0.1682	153	0.1435	2371	X-RAY DIFFRACTION	99
4.6547-29.1305	0.21	201	0.1845	2384	X-RAY DIFFRACTION	99

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	0.0225	-0.0357	0.0516	0.0441	-0.0097	0.0324	0.1724	-0.1858	-0.2248	0.0688	-0.0698	0.2812	0.1363	0.07	-0	0.1175	-0.0271	-0.0407	0.148	0.004	0.2309	-32.0673	-19.6372	-14.2192
2	0.2482	-0.4102	0.2372	0.2599	-0.1026	0.172	0.0274	-0.0131	-0.0731	-0.0582	-0.0289	0.0426	0.0651	0.0761	-0	0.1249	-0.0094	-0.0105	0.1245	-0.0042	0.139	-24.1668	-22.4689	-13.1353
3	0.0159	0.0033	0.0042	0.0028	0.0329	0.0271	-0.1311	0.1857	-0.2965	-0.4422	-0.3157	-0.5789	0.1945	0.2807	-0	0.2874	0.0476	0.0376	0.2193	-0.0591	0.3033	-18.342	-26.0539	-18.3275
4	0.0536	0.1199	-0.023	0.0784	0.0804	-0.0798	0.181	0.4347	-0.0004	-0.152	-0.1038	-0.4577	0.1198	0.4011	-0	0.2316	0.0391	-0.0244	0.254	0.017	0.1882	-22.1527	-13.3643	-20.3336
5	0.2308	-0.0786	-0.1068	0.2373	0.1719	0.2782	0.1148	0.0272	0.0418	-0.2358	0.1332	0.3089	0.0829	-0.4042	0.0259	0.1553	0.0123	-0.0624	0.2142	0.0334	0.1628	-33.8045	-13.4685	-19.2627
6	0.0848	-0.0945	0.0882	0.043	-0.3275	0.1894	-0.0951	-0.2678	0.1049	0.073	0.0519	-0.0325	-0.1374	-0.0689	-0	0.1255	0.0264	-0.0304	0.1435	0.0104	0.1579	-29.2313	-8.0833	-11.2796
7	0.0053	-0.139	-0.1466	0.6038	-0.2845	0.1934	0.048	-0.2998	0.081	0.0794	-0.053	-0.2271	-0.1483	0.0152	-0	0.0906	-0.0062	0.0022	0.1374	0.0109	0.1157	-20.4241	-16.7792	-0.3988
8	0.0263	-0.0052	-0.0123	-0.0029	-0.0163	0.0301	0.0529	-0.4407	-0.6607	0.0273	0.2416	0.2275	0.2579	-0.5132	0	0.1555	-0.0665	-0.0595	0.3359	0.0702	0.2288	-31.6062	-26.1789	-0.3111
9	0.2009	-0.2222	-0.0119	0.0821	0.074	0.2836	0.0225	-0.449	-0.2933	0.1015	-0.0697	-0.0468	0.1089	-0.0861	-0.0001	0.1371	-0.0097	0.0009	0.1465	0.072	0.1811	-15.1601	-27.4241	3.3325
10	0.6172	0.4714	0.3391	0.5181	-0.0179	1.3459	0.0081	-0.1804	0.0242	0.1359	-0.1237	-0.0307	-0.1731	-0.0927	-0.6446	0.0747	-0.0198	-0.0047	0.1078	0.0094	0.0661	3.2607	-14.3713	-3.0676
11	0.1805	0.1217	0.2672	0.2471	0.1043	0.496	0.0371	0.2767	0.0689	-0.2081	-0.4707	0.2497	-0.1258	-0.0736	-0.0384	0.1846	0.0997	-0.0237	0.1812	-0.0197	0.1321	-2.4295	-4.7963	-17.5866
12	1.0448	0.0938	0.2179	0.1879	0.0087	0.138	0.219	-0.2934	0.0784	0.1656	-0.1766	0.1049	-0.0834	-0.0344	0.0345	0.133	-0.024	0.0307	0.1163	-0.0183	0.0963	-1.326	-9.2944	-2.0845
13	0.0345	-0.128	0.1606	0.1075	-0.0886	0.2249	0.2285	0.1104	0.3128	-0.1254	-0.1061	0.1278	-0.1043	-0.1101	-0	0.1268	-0.0061	0.0239	0.1076	-0.0186	0.1516	2.5275	-1.0388	-11.5799
14	0.2024	-0.1168	-0.2157	0.1616	-0.0444	0.1964	0.0708	-0.045	0.0434	0.0786	-0.0685	0.0058	-0.0183	0.0018	-0.0039	0.0831	-0.0082	-0.0008	0.0669	0.0006	0.0697	7.0807	-10.9119	-9.8294
15	0.026	-0.08	-0.1111	0.3321	0.1671	0.4845	0.0449	0.2164	0.0473	-0.1743	-0.0126	0.3734	-0.0542	-0.4259	-0.0192	0.1344	0.0225	-0.0167	0.1277	0.0021	0.1179	-2.755	-14.2325	-22.3993
16	0.1025	0.1108	0.0463	-0.0202	-0.0362	0.0666	0.0043	-0.0137	0.0445	-0.0556	-0.0569	-0.0705	0.0053	0.0032	-0	0.1138	0.0019	0.0095	0.0924	-0.0043	0.094	10.0626	-11.4536	-18.0125
17	0.2961	0.0027	-0.0081	0.052	0.0441	0.033	-0.143	-0.4286	-0.0784	0.0272	0.0419	-0.1493	0.0895	0.1487	-0.0014	0.0847	0.0038	0.0004	0.1111	-0.0055	0.1243	11.4346	-18.4969	-13.0752
18	0.3001	-0.1211	-0.2234	0.1263	0.186	0.1885	0.082	0.2667	0.0313	-0.1071	0.0451	0.0289	-0.053	-0.1847	0.008	0.0795	-0.0032	-0.0077	0.1275	0.0122	0.1148	-9.317	-18.721	-10.3987
19	0.0645	-0.0198	-0.0626	0.0237	0.0394	0.0508	0.0082	0.2381	-0.3661	-0.1537	-0.0446	0.1227	0.069	0.0777	-0	0.1245	0.0045	-0.0088	0.1283	0.0082	0.1427	-5.6884	-24.2691	-4.9357
20	0.0459	0.0115	-0.0097	0.0082	0.3528	0.2583	0.0385	0.035	-0.0893	0.0299	0.1648	-0.4317	-0.0584	1.1032	0.1473	0.1162	0.0178	-0.0037	0.3265	-0.0113	0.1265	6.3289	-24.1578	-3.4081
21	0.0289	0.1419	0.0222	0.1528	0.2308	0.2883	0.2877	-0.4534	0.5959	0.0657	-0.127	0.3422	0.0922	0.0261	0.0033	0.1233	0.026	0.0599	0.2788	-0.0882	0.3732	-14.9826	-9.9032	-41.7093
22	0.3285	0.1151	-0.0075	0.0981	-0.0382	0.0559	0.2552	-0.5824	0.5063	0.1868	-0.2752	0.3461	-0.1025	-0.0116	0.0473	0.1681	0.0148	0.0654	0.272	-0.1421	0.3983	-13.0227	-7.4432	-39.3176
23	0.0089	0.0064	-0.0036	0.0053	0.0078	0.0196	0.0936	-0.4596	0.2109	0.2806	-0.1582	-0.0298	-0.2369	-0.068	0	0.36	-0.0483	0.0749	0.6787	-0.3828	0.4709	-9.4165	-7.2561	-31.2733
24	0.2292	-0.0728	0.7563	0.0776	0.2479	1.5279	0.1055	-0.8002	0.0162	0.1795	-0.0678	-0.2735	0.5823	-0.172	0.0488	0.1474	-0.0388	0.1399	0.6305	-0.2182	0.3879	-18.2163	-13.2322	-32.5095
25	-0.016	-0.0205	-0.0103	0.0016	-0.0365	0.0689	0.1921	-0.8991	-0.0416	0.5053	-0.3113	0.3412	0.0279	-0.2743	-0	0.2402	-0.0343	0.0982	0.519	0.0272	0.4604	-24.9577	-17.2589	-37.4656
26	0.1175	0.0246	0.016	0.0179	0.0218	0.1271	0.009	-0.0366	-0.0446	-0.1025	0.082	0.1593	0.105	-0.3278	0.0023	0.0931	0.017	0.0071	0.2557	0.0061	0.2904	-18.3581	-14.9819	-44.4709
27	0.0645	-0.0298	-0.0684	0.1047	0.0916	0.0898	0.0276	0.5467	-0.3025	-0.1016	-0.4105	0.4191	0.244	-0.0286	-0.0007	0.1641	-0.0122	-0.017	0.4084	-0.0342	0.4415	-24.9143	-20.1635	-46.1924
28	0.2736	0.3959	0.0604	0.3361	0.1267	0.071	0.1389	0.1631	-0.0272	0.014	-0.1263	0.0841	0.1874	-0.1149	0.0007	0.1116	0.0003	-0.0065	0.1804	0.0121	0.1379	-6.1004	-16.8351	-48.1235
29	0.0575	-0.0077	0.0252	0.0903	0.0514	0.1913	0.0003	0.5161	0.6599	-0.2046	0.0364	0.27	-0.3122	-0.2057	0.01	0.1871	0.0528	-0.0407	0.2134	0.0909	0.3118	-4.1871	-4.3376	-52.9003
30	0.0692	-0.0063	0.0069	0.0046	-0.0384	0.1309	0.1252	0.0683	0.0591	-0.0261	-0.057	-0.1107	-0.1853	0.1573	0.0004	0.1512	-0.0084	-0.0113	0.1116	0.0053	0.1053	7.6346	-12.1779	-45.1663
31	0.0918	-0.191	0.102	0.5185	0.0516	0.2703	-0.147	0.1698	0.0939	-0.0511	0.0565	-0.0103	-0.0031	-0.0392	-0.0012	0.0802	-0.0015	0.0032	0.1041	0.0095	0.0892	9.2151	-28.8462	-31.8128
32	0.1539	0.1145	-0.1524	-0.4457	-0.3244	-0.0072	-0.1613	-0.2281	-0.0951	0.4016	-0.1051	0.8197	0.0539	-0.4566	-0.0698	0.1844	-0.0295	0.1471	0.2358	-0.0516	0.3094	-6.8537	-35.7183	-23.8814
33	0.7164	-0.1478	0.1022	0.6146	-0.165	0.4948	-0.0122	0.0466	0.0041	-0.0571	-0.0211	-0.0033	0.0703	-0.0411	-0.3039	0.1035	-0.0084	0.0054	0.0786	-0.0176	0.073	4.3614	-32.7135	-35.8845
34	0.1349	-0.0063	0.0599	0.04	-0.0602	0.2278	-0.0485	-0.0042	-0.0816	0.0593	0.0156	-0.0065	0.0904	-0.0145	-0.0278	0.123	0.0013	0.0082	0.0693	-0.0074	0.0969	5.7241	-36.7752	-24.723
35	0.0069	0.0465	-0.1359	-0.0126	-0.0379	0.2968	0.0362	0.1106	0.0998	0.1492	-0.0454	0.2512	-0.1711	-0.5198	0.0024	0.1154	-0.0181	0.0122	0.1426	-0.0115	0.1107	-5.239	-24.3287	-21.1441
36	0.2797	-0.6427	-0.041	1.0109	0.2732	0.3629	-0.1106	0.0112	-0.0385	0.2954	-0.0237	0.1002	0.2107	-0.0312	-0.0839	0.1709	0.0124	0.0135	0.081	-0.006	0.0941	5.7939	-32.3278	-16.5426
37	0.2875	-0.0354	-0.0444	0.1146	0.1443	0.0902	-0.2208	-0.0089	0.0727	0.1689	0.0571	-0.1703	-0.0381	-0.0056	-0.0108	0.1228	0.0138	-0.0174	0.0744	0.0034	0.1071	9.6807	-25.0331	-20.2298
38	0.0136	-0.0371	0.0225	0.0581	0.0451	0.0793	-0.1444	0.0102	0.0508	0.0316	-0.0423	0.2999	0.2283	-0.515	-0.0022	0.104	0.008	-0.0134	0.1726	0.0033	0.13	-2.4468	-19.4158	-30.7313
39	0.3381	0.0573	0.1996	0.1787	-0.2177	0.3209	-0.0579	-0.1545	0.189	-0.0044	0.01	-0.0379	-0.0558	-0.115	-0.0006	0.125	-0.0096	-0.0035	0.102	-0.0159	0.0917	4.6007	-17.4455	-35.7524
40	0.1355	0.4646	-0.2563	0.2947	-0.1777	0.4494	-0.0139	-0.1288	-0.2738	0.4625	0.1108	-0.6662	0.1739	0.8352	-0.0561	0.1963	-0.0226	-0.0913	0.2171	-0.0106	0.1813	16.0083	-21.1199	-27.8161

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 resid 26:32)	A	26 - 32
2	X-RAY DIFFRACTION	2	(chain A and resid 33:56)	A	33 - 56
3	X-RAY DIFFRACTION	3	(chain A and resid 57:63)	A	57 - 63
4	X-RAY DIFFRACTION	4	(chain A and resid 64:75)	A	64 - 75
5	X-RAY DIFFRACTION	5	(chain A and resid 76:86)	A	76 - 86
6	X-RAY DIFFRACTION	6	(chain A and resid 87:111)	A	87 - 111
7	X-RAY DIFFRACTION	7	(chain A and resid 112:131)	A	112 - 131
8	X-RAY DIFFRACTION	8	(chain A and resid 132:136)	A	132 - 136
9	X-RAY DIFFRACTION	9	(chain A and resid 137:153)	A	137 - 153
10	X-RAY DIFFRACTION	10	(chain A and resid 154:165)	A	154 - 165
11	X-RAY DIFFRACTION	11	(chain A and resid 166:176)	A	166 - 176
12	X-RAY DIFFRACTION	12	(chain A and resid 177:198)	A	177 - 198
13	X-RAY DIFFRACTION	13	(chain A and resid 199:206)	A	199 - 206
14	X-RAY DIFFRACTION	14	(chain A and resid 207:219)	A	207 - 219
15	X-RAY DIFFRACTION	15	(chain A and resid 220:227)	A	220 - 227
16	X-RAY DIFFRACTION	16	(chain A and resid 228:244)	A	228 - 244
17	X-RAY DIFFRACTION	17	(chain A and resid 245:250)	A	245 - 250
18	X-RAY DIFFRACTION	18	(chain A and resid 251:262)	A	251 - 262
19	X-RAY DIFFRACTION	19	(chain A and resid 263:271)	A	263 - 271
20	X-RAY DIFFRACTION	20	(chain A and resid 272:278)	A	272 - 278
21	X-RAY DIFFRACTION	21	(chain B and resid 26:38)	B	26 - 38
22	X-RAY DIFFRACTION	22	(chain B and resid 39:56)	B	39 - 56
23	X-RAY DIFFRACTION	23	(chain B and resid 57:63)	B	57 - 63
24	X-RAY DIFFRACTION	24	(chain B and resid 64:71)	B	64 - 71
25	X-RAY DIFFRACTION	25	(chain B and resid 72:82)	B	72 - 82
26	X-RAY DIFFRACTION	26	(chain B and resid 83:93)	B	83 - 93
27	X-RAY DIFFRACTION	27	(chain B and resid 94:108)	B	94 - 108
28	X-RAY DIFFRACTION	28	(chain B and resid 109:132)	B	109 - 132
29	X-RAY DIFFRACTION	29	(chain B and resid 133:140)	B	133 - 140
30	X-RAY DIFFRACTION	30	(chain B and resid 141:153)	B	141 - 153
31	X-RAY DIFFRACTION	31	(chain B and resid 154:166)	B	154 - 166
32	X-RAY DIFFRACTION	32	(chain B and resid 167:174)	B	167 - 174
33	X-RAY DIFFRACTION	33	(chain B and resid 175:200)	B	175 - 200
34	X-RAY DIFFRACTION	34	(chain B and resid 201:218)	B	201 - 218
35	X-RAY DIFFRACTION	35	(chain B and resid 219:227)	B	219 - 227
36	X-RAY DIFFRACTION	36	(chain B and resid 228:245)	B	228 - 245
37	X-RAY DIFFRACTION	37	(chain B and resid 246:251)	B	246 - 251
38	X-RAY DIFFRACTION	38	(chain B and resid 252:257)	B	252 - 257
39	X-RAY DIFFRACTION	39	(chain B and resid 258:272)	B	258 - 272
40	X-RAY DIFFRACTION	40	(chain B and resid 273:278)	B	273 - 278

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