PDB-6wif: Class C beta-lactamase from Acinetobacter baumannii in complex wi...

ID or keywords:

Entry

Database: PDB / ID: 6wif

Title

Class C beta-lactamase from Acinetobacter baumannii in complex with 4-(Ethyl(methyl)carbamoyl)phenyl boronic acid

Components

Beta-lactamase

Keywords

HYDROLASE/HYDROLASE INHIBITOR / class C beta-lactamase / structural genomics / CSGID / Center for Structural Genomics of Infectious Diseases / HYDROLASE / HYDROLASE-INHIBITOR complex / HYDROLASE-HYDROLASE INHIBITOR complex

Function / homology

Function and homology information

antibiotic catabolic process / beta-lactamase activity / beta-lactamase / outer membrane-bounded periplasmic space / response to antibiotic
Similarity search - Function

Biological species

Acinetobacter baumannii (bacteria)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.15 Å

Authors

Chang, C. / Maltseva, N. / Endres, M. / Joachimiak, A. / Center for Structural Genomics of Infectious Diseases (CSGID)

Citation

Journal: To Be Published
Title: class C beta-lactamase from Acinetobacter baumannii in complex with 4-(Ethyl(methyl)carbamoyl)phenyl boronic acid
Authors: Chang, C. / Maltseva, N. / Endres, M. / Joachimiak, A. / Center for Structural Genomics of Infectious Diseases (CSGID)

History

Deposition	Apr 9, 2020	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Apr 22, 2020	Provider: repository / Type: Initial release
Revision 1.1	Oct 18, 2023	Group: Data collection / Database references / Refinement description Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2	Oct 23, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	6wif.cif.gz	591.2 KB	Display	PDBx/mmCIF format
PDB format	pdb6wif.ent.gz	488.2 KB	Display	PDB format
PDBx/mmJSON format	6wif.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	6wif_validation.pdf.gz	1.5 MB	Display	wwPDB validaton report
Full document	6wif_full_validation.pdf.gz	1.5 MB	Display
Data in XML	6wif_validation.xml.gz	58.8 KB	Display
Data in CIF	6wif_validation.cif.gz	82 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/wi/6wif ftp://data.pdbj.org/pub/pdb/validation_reports/wi/6wif	HTTPS FTP

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Related structure data

Related structure data	4qd4S S: Starting model for refinement
Similar structure data	6pwl-1 6pwm-2 4x2j-d 4x2k-d 5w12-1 6tzg-3 4u0x-3 3gw0-d 5chm-d 6r5h-d 4qd4-1 5wae-3 6tzi-4 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
Other databases	TargetTrack: CSGID-IDP97236

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#29 - May 2002 Penicillin-binding Proteins similarity (2)

Deposited unit

A: Beta-lactamase

B: Beta-lactamase

C: Beta-lactamase

D: Beta-lactamase

hetero molecules

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

1

A: Beta-lactamase

hetero molecules

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

2

B: Beta-lactamase

hetero molecules

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

3

C: Beta-lactamase

hetero molecules

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

4

D: Beta-lactamase

hetero molecules

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

Unit cell

Length a, b, c (Å)	93.244, 80.925, 104.377
Angle α, β, γ (deg.)	90.000, 113.340, 90.000
Int Tables number	4
Space group name H-M	P12₁1

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Protein , 1 types, 4 molecules ABCD

#1: Protein	Beta-lactamase Mass: 40521.180 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Acinetobacter baumannii (bacteria) Gene: ampC, A7M79_07980, A7M90_05015, BGC29_02775, E5294_06010, FJU36_01670, LV38_01949 Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: D6NSN2, beta-lactamase

#1: Protein

Beta-lactamase

Mass: 40521.180 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Acinetobacter baumannii (bacteria)
Gene: ampC, A7M79_07980, A7M90_05015, BGC29_02775, E5294_06010, FJU36_01670, LV38_01949
Production host:

Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: D6NSN2, beta-lactamase

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Non-polymers , 5 types, 688 molecules

#2: Chemical	ChemComp-U2Y / {4-[ethyl(methyl)carbamoyl]phenyl}boronic acid Mass: 207.034 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₁₀H₁₄BNO₃ / Feature type: SUBJECT OF INVESTIGATION
#3: Chemical	ChemComp-CL / CHLORIDE ION Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#4: Chemical	ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL Mass: 62.068 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C₂H₆O₂
#5: Chemical	ChemComp-EPE / 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID / HEPES Mass: 238.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C₈H₁₈N₂O₄S / Comment: pH buffer*YM
#6: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 666 / Source method: isolated from a natural source / Formula: H₂O

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Details

Has ligand of interest	Y
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: 2.23 Å³/Da / Density % sol: 44.86 %
Crystal grow	Temperature: 289 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 0.2M Sodium Chloride, 0.1M HEPES, 25% PEG3350

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Data collection

Diffraction

Mean temperature: 100 K / Serial crystal experiment: N

Diffraction source

Source:

SYNCHROTRON / Site:

APS

/ Beamline: 19-BM / Wavelength: 0.97935 Å

Detector

Type: ADSC QUANTUM 315r / Detector: CCD / Date: Feb 14, 2019

Radiation

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

Radiation wavelength

Wavelength: 0.97935 Å / Relative weight: 1

Reflection

Resolution: 2.15→50 Å / Num. obs: 76937 / % possible obs: 99.2 % / Redundancy: 4.7 % / R_merge(I) obs: 0.056 / R_pim(I) all: 0.028 / R_rim(I) all: 0.062 / Χ²: 0.937 / Net I/σ(I): 10.5 / Num. measured all: 363992

Reflection shell

Diffraction-ID: 1

Resolution (Å)	Redundancy (%)	R_merge(I) obs	Num. unique obs	CC_1/2	R_pim(I) all	R_rim(I) all	Χ²	% possible all
2.15-2.19	3.2	0.579	3456	0.733	0.358	0.687	0.913	89
2.19-2.23	3.4	0.545	3665	0.783	0.328	0.642	0.925	95.5
2.23-2.27	3.8	0.482	3857	0.841	0.276	0.558	0.9	99.8
2.27-2.32	4.1	0.458	3858	0.869	0.251	0.524	0.933	100
2.32-2.37	4.4	0.403	3874	0.913	0.214	0.458	0.939	100
2.37-2.42	4.8	0.35	3852	0.932	0.176	0.393	0.929	100
2.42-2.48	5	0.301	3844	0.954	0.149	0.336	0.942	100
2.48-2.55	5	0.255	3846	0.967	0.126	0.285	0.961	100
2.55-2.62	5	0.211	3873	0.976	0.104	0.235	0.955	100
2.62-2.71	5.1	0.191	3863	0.978	0.094	0.214	0.957	100
2.71-2.81	5.1	0.148	3880	0.988	0.072	0.165	0.996	100
2.81-2.92	5.1	0.121	3850	0.991	0.059	0.134	0.994	100
2.92-3.05	5.1	0.096	3879	0.993	0.047	0.107	1.017	100
3.05-3.21	5.1	0.072	3894	0.996	0.035	0.081	1.02	100
3.21-3.41	5.1	0.052	3852	0.997	0.025	0.058	1.004	100
3.41-3.68	5.1	0.041	3897	0.998	0.019	0.045	0.988	100
3.68-4.05	5.1	0.032	3901	0.998	0.016	0.036	0.914	100
4.05-4.63	5.1	0.027	3873	0.999	0.013	0.03	0.788	100
4.63-5.83	5	0.025	3945	0.999	0.012	0.028	0.691	100
5.83-50	4.8	0.03	3978	0.998	0.015	0.034	0.938	99.3

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Processing

Software

Name	Version	Classification
SCALEPACK		data scaling
SBC-Collect		data collection
PHENIX	1.17.1_3660	refinement
PDB_EXTRACT	3.25	data extraction
HKL-3000		data reduction
HKL-3000		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 4QD4

4qd4

Resolution: 2.15→43.38 Å / SU ML: 0.26 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 25.41

	R_factor	Num. reflection	% reflection
R_free	0.2396	3532	4.88 %
R_work	0.1927	-	-
obs	0.1949	72421	93.26 %

Solvent computation

Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å

Displacement parameters

B_iso max: 165.92 Å² / B_iso mean: 35.1827 Å² / B_iso min: 5.54 Å²

Refinement step

Cycle: final / Resolution: 2.15→43.38 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	11320	0	167	666	12153
B_iso mean	-	-	50.14	35.14	-
Num. residues	-	-	-	-	1428

LS refinement shell

Refine-ID: X-RAY DIFFRACTION / R_factor R_free error: 0 / Total num. of bins used: 25

Resolution (Å)	R_factor R_free	Num. reflection R_free	R_factor R_work	Num. reflection R_work	Num. reflection all	% reflection obs (%)
2.15-2.18	0.2519	85	0.2371	1400	1485	48
2.18-2.21	0.2963	81	0.2517	1701	1782	58
2.21-2.24	0.2817	115	0.2439	2107	2222	72
2.24-2.28	0.3066	122	0.2367	2347	2469	80
2.28-2.32	0.2901	143	0.2493	2531	2674	87
2.32-2.36	0.2576	138	0.2425	2700	2838	92
2.36-2.4	0.3136	135	0.2478	2889	3024	98
2.4-2.45	0.2887	141	0.242	2950	3091	99
2.45-2.5	0.2965	150	0.2374	2883	3033	100
2.5-2.55	0.284	162	0.2399	2961	3123	100
2.55-2.61	0.3153	146	0.2258	2950	3096	100
2.61-2.67	0.2799	145	0.2292	2960	3105	100
2.67-2.75	0.2593	146	0.2282	2956	3102	100
2.75-2.83	0.2703	187	0.2176	2909	3096	100
2.83-2.92	0.247	171	0.2275	2895	3066	100
2.92-3.02	0.2733	150	0.2194	2957	3107	100
3.02-3.14	0.2589	155	0.2221	2936	3091	100
3.14-3.29	0.2542	163	0.1993	2947	3110	100
3.29-3.46	0.2428	147	0.1972	2954	3101	100
3.46-3.68	0.2235	135	0.1769	2993	3128	100
3.68-3.96	0.2355	139	0.1615	2951	3090	100
3.96-4.36	0.1704	143	0.1492	2995	3138	100
4.36-4.99	0.1697	130	0.1398	2994	3124	100
4.99-6.28	0.2003	154	0.1549	2994	3148	100
6.28-43.38	0.1851	149	0.1482	3029	3178	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	0.4127	-0.2162	0.0346	0.7365	-0.2763	0.2688	0.129	0.1103	0.2235	-0.1542	-0.1208	-0.2399	0.0109	0.1021	0.0167	0.6574	0.1297	0.3017	0.179	0.129	0.4103	18.6631	6.0293	-5.2557
2	0.5603	0.3974	-0.0987	0.7833	-0.1732	0.3134	0.116	-0.0324	0.0714	0.0367	-0.0735	-0.1292	-0.0046	0.0399	0.3071	0.3663	-0.0069	0.2477	0.113	0.0583	0.4382	25.6371	3.227	2.922
3	0.8644	-0.3056	0.0464	1.333	-0.1328	0.1976	0.2375	-0.287	0.2125	0.1059	-0.1145	-0.1514	0.0841	0.0511	-0.0327	0.4446	-0.0881	0.1058	0.1762	-0.0374	0.2215	15.7833	-0.5106	13.9301
4	1.7528	-0.0029	0.5507	0.5346	0.4134	0.4949	0.2098	-0.4573	-0.1221	0.2092	-0.0215	0.1128	0.0215	-0.0122	-0.1194	0.7098	-0.1369	0.0182	0.4854	0.2317	0.3699	9.9942	-26.6588	25.6041
5	1.1962	-0.2889	-0.0619	0.9652	0.2662	0.5435	0.1141	-0.451	-0.2584	0.399	-0.0281	0.3339	0.0726	-0.1396	-0.102	0.4409	-0.141	0.0671	0.3023	0.0676	0.2925	5.0452	-18.3395	19.5091
6	0.8133	-0.5056	-0.212	0.6378	-0.0638	0.2039	0.2142	-0.3428	0.2673	0.1546	-0.0897	-0.0123	0.0235	0.1093	-0.0906	0.4397	-0.1272	0.1343	0.2524	-0.088	0.2405	14.3052	0.3621	16.0442
7	1.5371	0.5275	0.2086	0.862	0.5174	1.0169	0.2491	-0.2352	-0.1103	0.0315	-0.0525	-0.1436	0.0092	0.1967	-0.1743	0.4176	0.0008	0.0018	0.2082	0.0258	0.1994	22.6057	-18.5045	8.9736
8	0.6231	-0.0632	0.1395	1.0843	0.0102	0.3176	0.284	-0.0469	-0.1054	-0.1219	-0.215	0.194	-0.0422	0.0388	-0.1136	0.4325	0.0111	0.0412	0.1097	-0.0001	0.1888	13.7445	-15.2006	0.4918
9	0.8511	-0.6128	0.2037	1.6734	-0.3725	0.765	0.1802	0.0894	0.0506	-0.226	-0.1578	-0.1307	0.2026	0.1122	-0.003	0.535	0.0511	0.1641	0.109	0.0294	0.2132	18.3702	-4.285	-1.8587
10	0.9998	-0.18	0.0686	1.3749	0.2904	0.9405	0.104	-0.0719	0.2436	-0.2108	0.0423	-0.3274	-0.1535	0.1063	-0.0642	0.158	-0.0158	-0.0111	0.1446	-0.1279	0.2459	67.6892	5.4014	0.577
11	0.8318	0.4276	-0.45	1.0109	-0.0733	0.638	-0.0763	-0.4446	-0.3348	0.4565	-0.076	-0.1174	0.3438	0.1113	-0.0835	0.3612	0.0182	-0.0482	0.3222	0.0798	0.2382	58.7574	-23.2929	21.3489
12	1.0374	0.0148	-0.1858	1.0529	-0.0714	0.825	-0.0036	-0.3561	-0.1911	0.4185	0.0641	0.1911	0.2365	-0.0994	-0.0091	0.2418	-0.0239	-0.0063	0.3055	0.0369	0.2257	51.1793	-18.4214	18.9924
13	0.1305	-0.009	0.0024	0.3755	-0.2298	0.1445	0.0466	-0.2717	0.046	0.286	-0.0475	-0.1071	-0.0434	0.0102	0.0879	0.1602	-0.0135	-0.1022	0.3317	-0.1693	0.2432	62.1391	-0.8801	15.3023
14	1.5279	0.2929	0.3799	0.3783	-0.0715	1.1279	0.0256	-0.1522	-0.3445	0.0237	-0.0864	-0.4307	0.2194	0.1155	-0.2386	0.1528	0.054	-0.1106	0.2054	-0.0071	0.3643	67.7649	-20.1395	7.0705
15	0.8069	0.6082	0.1359	0.4661	0.1134	0.7877	-0.0564	0.017	-0.1891	-0.1116	-0.0029	0.0496	0.128	-0.0266	-0.4675	0.0379	-0.043	-0.1019	0.2052	-0.1337	0.2022	58.7228	-15.7666	-0.5783
16	0.8056	0.5933	0.2057	0.9558	0.009	0.619	-0.0928	0.0621	-0.1287	-0.0345	-0.0243	-0.0947	-0.0129	-0.0122	-0.3519	0.0816	-0.0117	-0.0221	0.2001	-0.1125	0.1921	64.7688	-4.3171	0.8666
17	1.1086	0.5996	0.4795	1.0239	0.5385	0.8665	-0.0703	0.1517	-0.1031	-0.1161	0.0797	-0.1095	-0.02	0.0611	-0.1631	0.1813	-0.0894	-0.0204	0.1818	-0.157	0.1373	63.9316	-5.7157	-7.0627
18	1.1695	0.0025	-0.0882	0.8555	0.04	0.866	0.1746	-0.3767	-0.1552	0.1917	0.0723	-0.1694	0.396	0.0688	-0.0111	0.1756	0.0368	-0.0889	0.1837	0.0305	0.174	46.6419	14.6935	28.4904
19	1.4464	0.3405	-0.6512	0.523	-0.0894	0.6204	0.1615	-0.2587	0.4115	0.0618	0.0962	0.0748	-0.3074	-0.3174	-0.0788	0.6862	0.1827	0.1879	0.8825	-0.3188	0.739	32.3911	45.3944	44.0289
20	0.4422	-0.0377	0.0876	0.196	-0.2777	0.4007	0.1138	-0.1887	0.4425	-0.0026	-0.0404	0.1052	-0.2256	-0.1964	-0.1322	0.3957	0.2557	0.0477	0.6836	-0.121	0.5861	26.3334	37.9389	33.7723
21	1.5019	-0.4433	-0.0659	1.221	0.1582	0.7303	0.0506	-0.4181	0.3485	0.191	0.0082	0.1686	-0.2078	-0.3399	-0.1496	0.2999	0.1696	0.0539	0.7064	-0.2253	0.5048	28.159	36.2958	39.8921
22	1.4447	0.3559	0.5471	0.6143	0.6882	1.8381	0.0069	-0.1539	0.4165	-0.179	0.0517	0.0761	-0.447	-0.0345	0.0461	0.1555	0.0029	-0.0158	0.1433	0.0451	0.2585	43.7624	30.5367	25.025
23	1.0869	0.1497	0.5106	1.2826	0.0047	1.9406	0.1275	-0.6574	0.1078	0.4425	-0.1898	-0.1714	-0.0568	0.0027	-0.1311	0.1792	-0.0321	-0.0645	0.4096	-0.0432	0.1808	50.618	25.0498	41.4085
24	0.3651	0.338	-0.3885	0.3098	-0.3539	0.4007	0.2386	-0.8155	0.0063	0.3505	-0.1083	0.2557	0.0947	-0.5635	-0.0064	0.2232	-0.2109	0.0697	0.821	0.0585	0.1755	33.1079	18.6733	43.5443
25	0.4814	0.4602	-0.4997	0.871	0.1799	1.5342	0.186	-0.4793	-0.3093	0.3151	-0.025	-0.0646	0.316	-0.3266	-0.1931	0.3313	-0.126	-0.1065	0.3094	0.1621	0.2274	40.5435	10.6187	34.9275
26	1.0348	0.1541	-0.1508	2.0634	-0.2039	1.77	-0.1121	0.3447	-0.3568	-0.0939	0.1467	0.2535	0.44	-0.3458	-0.1797	0.2685	-0.0387	-0.0278	0.2773	-0.0608	0.2808	55.376	-34.0156	67.7427
27	0.7868	0.1456	-0.3151	1.1112	-0.4749	0.9897	0.0489	0.3285	0.1377	0.0996	0.1499	0.1378	-0.3385	-0.1136	-0.1317	0.2244	0.02	0.0329	0.2611	0.0515	0.1539	64.0137	-5.7844	62.5508
28	0.7497	0.3296	-0.2598	0.929	-0.2708	1.0202	-0.029	0.421	-0.0049	-0.0162	0.1886	0.1964	-0.2318	-0.1717	-0.0975	0.2233	0.019	-0.0066	0.2925	0.0194	0.1297	59.2819	-14.7646	62.4278
29	0.5308	0.0978	-0.4697	0.7083	-0.1883	0.5786	-0.2039	0.4178	-0.1551	-0.3	0.1857	-0.1808	0.1263	-0.0426	-0.1016	0.2593	-0.042	0.039	0.3612	-0.0897	0.1947	68.6927	-21.7757	54.8884
30	1.0596	-0.6613	-0.0608	1.583	-0.5649	2.1478	-0.1249	0.4456	-0.242	-0.3232	0.1692	0.1006	0.2526	0.0297	-0.1819	0.2049	-0.0624	-0.0051	0.2731	-0.0966	0.1854	60.7931	-28.9899	61.2047

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 28 through 50 )	A	28 - 50
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 51 through 68 )	A	51 - 68
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 69 through 103 )	A	69 - 103
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 104 through 129 )	A	104 - 129
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 130 through 200 )	A	130 - 200
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 201 through 263 )	A	201 - 263
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 264 through 299 )	A	264 - 299
8	X-RAY DIFFRACTION	8	chain 'A' and (resid 300 through 350 )	A	300 - 350
9	X-RAY DIFFRACTION	9	chain 'A' and (resid 351 through 382 )	A	351 - 382
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 24 through 86 )	B	24 - 86
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 87 through 129 )	B	87 - 129
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 130 through 200 )	B	130 - 200
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 201 through 263 )	B	201 - 263
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 264 through 299 )	B	264 - 299
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 300 through 350 )	B	300 - 350
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 351 through 366 )	B	351 - 366
17	X-RAY DIFFRACTION	17	chain 'B' and (resid 367 through 382 )	B	367 - 382
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 26 through 103 )	C	26 - 103
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 104 through 129 )	C	104 - 129
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 130 through 160 )	C	130 - 160
21	X-RAY DIFFRACTION	21	chain 'C' and (resid 161 through 190 )	C	161 - 190
22	X-RAY DIFFRACTION	22	chain 'C' and (resid 191 through 248 )	C	191 - 248
23	X-RAY DIFFRACTION	23	chain 'C' and (resid 249 through 279 )	C	249 - 279
24	X-RAY DIFFRACTION	24	chain 'C' and (resid 280 through 350 )	C	280 - 350
25	X-RAY DIFFRACTION	25	chain 'C' and (resid 351 through 382 )	C	351 - 382
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 26 through 58 )	D	26 - 58
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 59 through 216 )	D	59 - 216
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 217 through 299 )	D	217 - 299
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 300 through 350 )	D	300 - 350
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 351 through 382 )	D	351 - 382

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