PDB-4bp0: Crystal structure of the closed form of Pseudomonas aeruginosa SPM-1

ID or keywords:

Entry

Database: PDB / ID: 4bp0

Title

Crystal structure of the closed form of Pseudomonas aeruginosa SPM-1

Components

METALLO-B-LACTAMASE

Keywords

HYDROLASE / METALLO BETA LACTAMASE

Function / homology

Function and homology information

antibiotic catabolic process / beta-lactamase activity / beta-lactamase / periplasmic space / response to antibiotic / zinc ion binding
Similarity search - Function

Biological species

PSEUDOMONAS AERUGINOSA (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.24 Å

Authors

McDonough, M.A. / Brem, J. / Schofield, C.J.

Citation

Journal: Chem Sci / Year: 2015
Title: Studying the active-site loop movement of the Sao Paolo metallo-beta-lactamase-1
Authors: Brem, J. / Struwe, W.B. / Rydzik, A.M. / Tarhonskaya, H. / Pfeffer, I. / Flashman, E. / van Berkel, S.S. / Spencer, J. / Claridge, T.D. / McDonough, M.A. / Benesch, J.L. / Schofield, C.J.

History

Deposition	May 22, 2013	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Jun 18, 2014	Provider: repository / Type: Initial release
Revision 1.1	Jun 24, 2015	Group: Database references
Revision 1.2	Mar 28, 2018	Group: Database references / Category: citation / citation_author Item: _citation.journal_abbrev / _citation.page_last ..._citation.journal_abbrev / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.title / _citation_author.name
Revision 1.3	Jan 30, 2019	Group: Data collection / Experimental preparation / Category: exptl_crystal_grow / Item: _exptl_crystal_grow.method
Revision 1.4	Dec 20, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr1_symmetry / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.ptnr3_symmetry / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _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	4bp0.cif.gz	411.4 KB	Display	PDBx/mmCIF format
PDB format	pdb4bp0.ent.gz	339.4 KB	Display	PDB format
PDBx/mmJSON format	4bp0.json.gz		Tree view	PDBx/mmJSON format
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Validation report

Summary document	4bp0_validation.pdf.gz	468.8 KB	Display	wwPDB validaton report
Full document	4bp0_full_validation.pdf.gz	477.7 KB	Display
Data in XML	4bp0_validation.xml.gz	41.1 KB	Display
Data in CIF	4bp0_validation.cif.gz	57.8 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/bp/4bp0 ftp://data.pdbj.org/pub/pdb/validation_reports/bp/4bp0	HTTPS FTP

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Related structure data

Related structure data	2fhxS S: Starting model for refinement
Similar structure data	1n55-d 6m1s-2 2y62-d 5fou-d 4asb-d 4wje-d 5fov-1 3som-8 6vvq-4 5wxx-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 - FunctionF&H Search Similarity search - HomologyF&H Search

Related structure data

2fhxS

S: Starting model for refinement

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#187 - Jul 2015 New Delhi Metallo-β-Lactamase similarity (3) #105 - Sep 2008 Ribonuclease A similarity (2)

Deposited unit

A: METALLO-B-LACTAMASE

B: METALLO-B-LACTAMASE

C: METALLO-B-LACTAMASE

D: METALLO-B-LACTAMASE

hetero molecules

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

1

A: METALLO-B-LACTAMASE

hetero molecules

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

2

B: METALLO-B-LACTAMASE

hetero molecules

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

3

C: METALLO-B-LACTAMASE

hetero molecules

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

4

D: METALLO-B-LACTAMASE

hetero molecules

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

Unit cell

Length a, b, c (Å)	45.650, 83.550, 282.410
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

#1: Protein	METALLO-B-LACTAMASE / SPM-1 / METALLO-BETA-LACTAMASE BLASPM-1 Mass: 27927.178 Da / Num. of mol.: 4 / Fragment: RESIDUES 29-276 Source method: isolated from a genetically manipulated source Source: (gene. exp.) PSEUDOMONAS AERUGINOSA (bacteria) / Strain: 48-1997A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: Q8G9Q0, beta-lactamase
#2: Chemical	ChemComp-ZN / ZINC ION Mass: 65.409 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Zn
#3: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C₃H₈O₃
#4: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: Cl
#5: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 418 / Source method: isolated from a natural source / Formula: H₂O
Nonpolymer details	CHLORIDE ION (CL): CHLORIDE WAS MODELED AS PUTATIVE ION DUE TO LACK OF BETTER ALTERNATIVE BASED ON ...CHLORIDE ION (CL): CHLORIDE WAS MODELED AS PUTATIVE ION DUE TO LACK OF BETTER ALTERNATIVE BASED ON CRYSTALLISATION CONDITION CONTENTS.
Sequence details	THE TWO N-TERMINAL RESIDUES 'GP' FROM THE 3C PROTEASE CLEAVAGE SITE REMAIN PART OF THE PROTEIN ...THE TWO N-TERMINAL RESIDUES 'GP' FROM THE 3C PROTEASE CLEAVAGE SITE REMAIN PART OF THE PROTEIN AFTER CLEAVAGE OF THE HIS-TAG

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.32 Å³/Da / Density % sol: 47.01 % / Description: NONE
Crystal grow	Method: vapor diffusion, sitting drop / pH: 7.5 Details: PROTEIN WAS CRYTALLISED FROM 10% W/V POLYETHYLENE GLYCOL 8000, 0.1M HEPES, PH7.5, VAPOR DIFFUSION SITTING DROP, ROOM TEMPERATURE

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 1.0081
Detector	Type: DECTRIS PILATUS / Detector: PIXEL / Date: Dec 11, 2012 Details: KIRKPATRICK BAEZ BIMORPH MIRROR PAIR FOR HORIZONTAL AND VERTICAL FOCUSSING
Radiation	Monochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.0081 Å / Relative weight: 1
Reflection	Resolution: 2.24→71.91 Å / Num. obs: 53352 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 6.4 % / B_iso Wilson estimate: 40.96 Å² / R_merge(I) obs: 0.08 / Net I/σ(I): 15.7
Reflection shell	Resolution: 2.24→2.3 Å / Redundancy: 6.4 % / R_merge(I) obs: 0.76 / Mean I/σ(I) obs: 3 / % possible all: 100

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Processing

Software

Name	Version	Classification
PHENIX	(PHENIX.REFINE)	refinement
XDS		data reduction
XDS		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2FHX

2fhx

Resolution: 2.24→71.9428 Å / SU ML: 0.23 / σ(F): 1.34 / Phase error: 20.34 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1981	3779	3.8 %
R_work	0.1516	-	-
obs	0.1533	53254	99.48 %

Solvent computation

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

Displacement parameters

B_iso mean: 49.51 Å²

Refinement step

Cycle: LAST / Resolution: 2.24→71.9428 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	7707	0	65	418	8190

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.014	7967
X-RAY DIFFRACTION	f_angle_d	1.174	10766
X-RAY DIFFRACTION	f_dihedral_angle_d	14.499	2968
X-RAY DIFFRACTION	f_chiral_restr	0.065	1176
X-RAY DIFFRACTION	f_plane_restr	0.005	1358

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 (%)
2.24-2.2684	0.2908	146	0.2542	3662	X-RAY DIFFRACTION	100
2.2684-2.2982	0.299	139	0.2404	3553	X-RAY DIFFRACTION	100
2.2982-2.3297	0.2688	137	0.2269	3532	X-RAY DIFFRACTION	100
2.3297-2.363	0.2462	136	0.2183	3568	X-RAY DIFFRACTION	100
2.363-2.3983	0.2554	141	0.2145	3622	X-RAY DIFFRACTION	100
2.3983-2.4357	0.2657	137	0.2022	3543	X-RAY DIFFRACTION	100
2.4357-2.4757	0.2674	137	0.201	3525	X-RAY DIFFRACTION	100
2.4757-2.5184	0.2261	139	0.1956	3642	X-RAY DIFFRACTION	100
2.5184-2.5642	0.2354	139	0.1826	3516	X-RAY DIFFRACTION	100
2.5642-2.6135	0.2181	138	0.1724	3532	X-RAY DIFFRACTION	99
2.6135-2.6668	0.2097	146	0.1729	3598	X-RAY DIFFRACTION	100
2.6668-2.7248	0.2398	140	0.1683	3543	X-RAY DIFFRACTION	99
2.7248-2.7882	0.1987	134	0.1625	3524	X-RAY DIFFRACTION	99
2.7882-2.8579	0.2337	144	0.1641	3635	X-RAY DIFFRACTION	99
2.8579-2.9352	0.2035	137	0.1577	3480	X-RAY DIFFRACTION	100
2.9352-3.0216	0.2251	145	0.1626	3597	X-RAY DIFFRACTION	99
3.0216-3.1191	0.2688	141	0.1605	3512	X-RAY DIFFRACTION	100
3.1191-3.2306	0.2452	143	0.159	3594	X-RAY DIFFRACTION	100
3.2306-3.3599	0.1961	135	0.1508	3521	X-RAY DIFFRACTION	99
3.3599-3.5128	0.1975	141	0.1483	3610	X-RAY DIFFRACTION	99
3.5128-3.698	0.1686	139	0.1371	3473	X-RAY DIFFRACTION	99
3.698-3.9297	0.202	141	0.1385	3582	X-RAY DIFFRACTION	100
3.9297-4.2331	0.1618	140	0.1267	3580	X-RAY DIFFRACTION	100
4.2331-4.659	0.1432	143	0.105	3551	X-RAY DIFFRACTION	100
4.659-5.333	0.1471	137	0.1159	3553	X-RAY DIFFRACTION	99
5.333-6.7183	0.1693	141	0.1444	3549	X-RAY DIFFRACTION	99
6.7183-71.9428	0.1878	143	0.1518	3520	X-RAY DIFFRACTION	98

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	1.3899	1.5876	0.1568	3.3723	2.9309	4.8378	-0.278	0.336	-0.3954	-0.5137	0.2155	0.3527	0.4594	-0.1852	-0.013	0.248	-0.0578	-0.0343	0.3653	-0.0363	0.343	34.5912	-0.0995	42.6985
2	3.1685	0.4802	0.6641	3.9304	0.6677	5.6951	0.0366	0.1743	-0.2106	-0.1525	0.0483	0.2246	0.3181	-0.0944	-0.0795	0.1099	-0.0352	-0.0043	0.2104	-0.0109	0.2577	37.9977	3.3288	51.3454
3	3.3547	-0.0777	0.2094	7.9087	0.7553	5.1617	-0.0143	0.077	-0.2081	-0.143	-0.0603	0.3314	0.4403	-0.5446	0.1071	0.2015	-0.0776	-0.0349	0.3887	0.0054	0.3863	28.7138	3.3498	51.7407
4	2.7059	0.7469	0.402	3.6809	0.5709	4.433	-0.0627	-0.0537	0.1177	0.1151	0.0666	0.3176	-0.0591	-0.3412	0.0557	0.1106	0.0192	0.0098	0.2215	0.0191	0.2676	37.5826	13.0121	60.2853
5	8.5665	6.9941	4.7773	2.3794	8.3173	6.3629	-0.784	1.0497	0.9621	-1.598	0.2386	0.3128	-1.528	0.4211	0.5845	0.6073	-0.0262	-0.1162	0.4281	0.2108	0.6232	33.7673	24.8334	45.1097
6	5.264	-0.9435	-0.9644	4.2781	-0.8775	5.0212	-0.0417	-0.6126	0.4012	0.3804	0.0441	-0.286	-0.1409	0.0729	-0.0986	0.2009	-0.0551	-0.0172	0.1823	-0.0477	0.222	41.5251	14.4682	64.8197
7	3.1504	-0.2762	-0.7554	1.6253	0.4054	3.1079	-0.0863	-0.2648	-0.3323	0.1177	-0.0067	-0.2402	0.3001	0.2813	0.0944	0.1605	0.0017	-0.0624	0.2393	0.0147	0.2975	49.0078	3.4619	59.7382
8	6.2253	-0.6326	-0.3151	5.2188	-0.1468	4.7509	0.0116	-0.0666	0.1698	-0.0469	0.1136	-0.6255	-0.2523	0.4957	-0.1184	0.1647	-0.0766	-0.0078	0.3043	-0.0177	0.3232	57.306	13.466	50.5488
9	2.381	2.1704	-1.1622	2.324	-2.3982	9.7647	0.1735	0.6154	-0.8327	-0.3133	-0.2028	-0.0623	0.8957	-0.0268	-0.0896	0.2782	-0.0378	-0.0332	0.2906	-0.0727	0.3871	50.4307	0.7719	48.3772
10	3.0767	4.0438	-1.4382	2.1915	-3.5648	8.952	0.1167	0.2934	0.4987	-0.5905	-0.2704	-0.3528	-0.4798	0.5501	0.1466	0.2381	0.046	0.0916	0.4819	0.0281	0.6284	61.9018	12.7871	45.1649
11	0.2815	-1.2351	0.525	7.0902	-3.5253	1.9266	-0.3717	-1.3308	-0.5033	1.1387	0.1153	0.3124	0.6271	-0.0149	-0.005	0.7601	0.2655	0.1154	0.6671	0.0586	0.3765	37.9631	-2.4559	99.5583
12	5.6587	2.5952	2.7169	7.2426	4.3639	8.7529	-0.0502	-0.8003	-0.2337	1.0469	0.1393	0.2242	0.5214	-0.1733	-0.0914	0.454	0.1986	0.0814	0.3858	0.1113	0.3166	37.7324	2.7503	91.1347
13	6.2933	5.4138	3.8137	7.2135	5.983	9.7676	0.2096	-0.491	-0.4916	1.0022	0.123	-0.13	0.7035	-0.0778	-0.2856	0.5257	0.1969	0.0329	0.4189	0.0629	0.3664	44.9324	-3.0231	90.7346
14	3.4867	1.6005	0.1933	4.3885	-0.6641	4.1107	-0.2725	-0.2423	-0.0192	0.3863	0.191	-0.2472	-0.1353	0.0625	0.0628	0.2787	0.1042	-0.0206	0.2763	-0.0255	0.2138	44.3602	10.2691	82.5151
15	8.7792	2.1252	-0.1831	2.0856	-8.4688	6.9407	-0.1852	-2.077	1.1909	2.0362	-0.0304	-0.1011	-1.5636	0.6491	0.2418	1.1271	0.1637	-0.2353	0.8446	-0.2424	0.69	54.8795	16.372	97.9705
16	3.8767	0.9032	0.2233	3.6935	0.2226	3.476	-0.132	-0.1984	0.115	0.32	0.1804	0.4951	-0.21	-0.4406	-0.0277	0.3343	0.1386	0.0122	0.3458	0.0646	0.2948	32.9304	11.1181	81.5248
17	4.9024	0.7648	-0.9313	5.4207	-0.6754	4.4889	-0.22	-0.528	0.1212	0.7238	0.3363	0.7644	-0.4958	-0.4917	-0.1089	0.617	0.32	0.115	0.5784	0.0191	0.4053	28.2581	17.9539	92.9026
18	6.0273	5.7276	-0.0554	9.8862	1.6625	5.3993	0.2738	-0.7727	0.7251	0.8937	-0.0657	0.6766	-0.5482	-0.1701	-0.1428	0.7848	0.3919	0.1631	0.8987	-0.0195	0.5395	24.6444	24.5057	97.8708
19	4.1229	-0.1483	-1.9338	2.4193	-0.3579	5.9502	-0.019	-0.0525	-0.0527	0.0605	-0.0706	0.2277	0.295	-0.6407	0.071	0.3712	-0.0788	-0.0222	0.2815	-0.0154	0.2312	39.4932	-1.2412	17.6123
20	2.3231	-1.7827	-7.6296	9.2251	3.2397	5.8602	0.0447	-1.1525	-0.1679	1.3824	-0.0939	-0.2873	0.7575	1.1208	0.1447	0.7927	0.0708	-0.1057	0.5113	0.0658	0.4909	54.1051	-12.2626	26.2487
21	3.2762	0.2124	1.3361	5.1825	-0.0329	5.548	0.0158	0.0056	0.4021	0.0381	-0.1254	-0.2661	-0.759	0.0595	0.1372	0.3899	-0.0453	0.0669	0.2572	0.0216	0.2653	48.2801	9.7472	13.3643
22	8.5606	2.4532	2.1912	8.3685	1.2564	8.5694	-0.0745	-0.525	1.0185	0.6833	-0.1194	-0.1453	-1.0614	-0.0538	0.211	0.7586	-0.0575	0.0202	0.3252	-0.0795	0.4393	49.6013	17.1237	23.7646
23	4.4271	0.7626	-0.9405	2.6001	0.111	4.6788	-0.1068	-0.1199	-0.2611	0.2944	-0.1465	0.1697	0.5805	-0.371	0.2664	0.47	-0.0859	0.0011	0.2868	0.009	0.2817	61.1761	38.3451	17.4125
24	2.2937	1.5673	-6.0193	7.2696	-6.624	2.1834	0.2483	-2.09	-0.19	1.7105	-0.4334	-0.6879	0.4789	1.4277	-0.0329	0.9798	0.0653	-0.169	0.9896	0.2132	0.7239	77.5945	32.3924	27.9487
25	3.2183	0.2426	0.3946	3.9684	0.2249	6.9796	-0.0907	0.0202	0.2152	-0.0036	-0.0987	-0.1291	-0.5727	0.0827	0.213	0.3598	-0.0505	0.0183	0.2274	0.0453	0.2424	66.1569	49.1774	12.9065
26	8.5375	2.0521	0.5112	7.8478	1.0108	4.7916	0.0756	-0.067	1.0378	0.6018	-0.2119	0.1541	-1.6211	0.1363	0.1551	0.8078	-0.0957	-0.0313	0.298	-0.0052	0.3616	67.3457	59.4515	21.9667

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	CHAIN A AND (RESID 31 THROUGH 46 )
2	X-RAY DIFFRACTION	2	CHAIN A AND (RESID 47 THROUGH 79 )
3	X-RAY DIFFRACTION	3	CHAIN A AND (RESID 80 THROUGH 96 )
4	X-RAY DIFFRACTION	4	CHAIN A AND (RESID 97 THROUGH 141 )
5	X-RAY DIFFRACTION	5	CHAIN A AND (RESID 142 THROUGH 162 )
6	X-RAY DIFFRACTION	6	CHAIN A AND (RESID 163 THROUGH 177 )
7	X-RAY DIFFRACTION	7	CHAIN A AND (RESID 178 THROUGH 216 )
8	X-RAY DIFFRACTION	8	CHAIN A AND (RESID 217 THROUGH 245 )
9	X-RAY DIFFRACTION	9	CHAIN A AND (RESID 246 THROUGH 290 )
10	X-RAY DIFFRACTION	10	CHAIN A AND (RESID 291 THROUGH 310 )
11	X-RAY DIFFRACTION	11	CHAIN B AND (RESID 31 THROUGH 46 )
12	X-RAY DIFFRACTION	12	CHAIN B AND (RESID 47 THROUGH 79 )
13	X-RAY DIFFRACTION	13	CHAIN B AND (RESID 80 THROUGH 96 )
14	X-RAY DIFFRACTION	14	CHAIN B AND (RESID 97 THROUGH 141 )
15	X-RAY DIFFRACTION	15	CHAIN B AND (RESID 142 THROUGH 162 )
16	X-RAY DIFFRACTION	16	CHAIN B AND (RESID 163 THROUGH 216 )
17	X-RAY DIFFRACTION	17	CHAIN B AND (RESID 217 THROUGH 290 )
18	X-RAY DIFFRACTION	18	CHAIN B AND (RESID 291 THROUGH 309 )
19	X-RAY DIFFRACTION	19	CHAIN C AND (RESID 31 THROUGH 141 )
20	X-RAY DIFFRACTION	20	CHAIN C AND (RESID 142 THROUGH 162 )
21	X-RAY DIFFRACTION	21	CHAIN C AND (RESID 163 THROUGH 243 )
22	X-RAY DIFFRACTION	22	CHAIN C AND (RESID 244 THROUGH 308 )
23	X-RAY DIFFRACTION	23	CHAIN D AND (RESID 31 THROUGH 141 )
24	X-RAY DIFFRACTION	24	CHAIN D AND (RESID 142 THROUGH 161 )
25	X-RAY DIFFRACTION	25	CHAIN D AND (RESID 162 THROUGH 232 )
26	X-RAY DIFFRACTION	26	CHAIN D AND (RESID 233 THROUGH 308 )

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