PDB-5kkf: Crystal structure of TEM1 beta-lactamase mutant I263L

ID or keywords:

Entry

Database: PDB / ID: 5kkf

Title

Crystal structure of TEM1 beta-lactamase mutant I263L

Components

Beta-lactamase TEM

Keywords

HYDROLASE

Function / homology

Function and homology information

beta-lactam antibiotic catabolic process /

beta-lactamase activity /

beta-lactamase / response to antibiotic
Similarity search - Function

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT /

molecular replacement / Resolution: 1.82 Å

Authors

Roose, B.W. / Dmochowski, I.J.

Funding support

United States, 2items

Organization	Grant number	Country
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)	R01-GM097478	United States
Department of Defense Lung Cancer Research Program	W81XWH-14-1-0424	United States

Citation

Journal: Chemphyschem / Year: 2018
Title: A Structural Basis for129Xe Hyper-CEST Signal in TEM-1 beta-Lactamase.
Authors: Roose, B.W. / Zemerov, S.D. / Wang, Y. / Kasimova, M.A. / Carnevale, V. / Dmochowski, I.J.

History

Deposition	Jun 21, 2016	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	Jun 28, 2017	Provider: repository / Type: Initial release
Revision 1.1	Sep 20, 2017	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2	Jan 16, 2019	Group: Data collection / Database references / Category: citation / citation_author Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.3	Dec 25, 2019	Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4	Sep 27, 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

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5kkf.cif.gz	401.8 KB	Display	PDBx/mmCIF format
PDB format	pdb5kkf.ent.gz	328.9 KB	Display	PDB format
PDBx/mmJSON format	5kkf.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/kk/5kkf ftp://data.pdbj.org/pub/pdb/validation_reports/kk/5kkf	HTTPS FTP

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Related structure data

Related structure data	5hviSC 5hw1C 5i52C 5i63C 5kpuC 6apaC 6aykC S: Starting model for refinement C: citing same article (ref.)
Similar structure data	5kpu-4 5hvi-3 5i52-2 4oqg-6 3jyi-3 5hw1-4 5i63-1 5hw1-1 6ayk-3 5iq8-2 5iq8-4 5hw5-4 6ayk-4 4rx2-3 1erq-d 5hw5-2 6b2n-3 1htz-5 3p98-1 4oqg-1 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

5hviSC

S: Starting model for refinement

C: citing same article (ref.)

Similar structure data

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Links

PDB pages	PDBj / wwPDB / NCBI
Related items in Molecule of the Month	#164 - Aug 2013 Serotonin Receptor similarity (6) #29 - May 2002 Penicillin-binding Proteins similarity (3) #187 - Jul 2015 New Delhi Metallo-β-Lactamase similarity (2)

Deposited unit

A: Beta-lactamase TEM

B: Beta-lactamase TEM

C: Beta-lactamase TEM

D: Beta-lactamase TEM

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

1

A: Beta-lactamase TEM

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

2

B: Beta-lactamase TEM

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

3

C: Beta-lactamase TEM

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

4

D: Beta-lactamase TEM

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

Unit cell

Length a, b, c (Å)	60.500, 84.030, 94.920
Angle α, β, γ (deg.)	90.00, 90.42, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Beta-lactamase TEM / IRT-4 / Penicillinase / TEM-1 / TEM-16/CAZ-7 / TEM-2 / TEM-24/CAZ-6 / TEM-3 / TEM-4 / TEM-5 / TEM-6 ...IRT-4 / Penicillinase / TEM-1 / TEM-16/CAZ-7 / TEM-2 / TEM-24/CAZ-6 / TEM-3 / TEM-4 / TEM-5 / TEM-6 / TEM-8/CAZ-2 Mass: 28911.904 Da / Num. of mol.: 4 / Mutation: M180T, I259L Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: bla, blaT-3, blaT-4, blaT-5, blaT-6 / Plasmid: pJ411 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62593, beta-lactamase
#2: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 557 / Source method: isolated from a natural source / Formula: H₂O

#1: Protein

Beta-lactamase TEM / IRT-4 / Penicillinase / TEM-1 / TEM-16/CAZ-7 / TEM-2 / TEM-24/CAZ-6 / TEM-3 / TEM-4 / TEM-5 / TEM-6 ...

Mass: 28911.904 Da / Num. of mol.: 4 / Mutation: M180T, I259L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.)

Escherichia coli (E. coli) / Gene: bla, blaT-3, blaT-4, blaT-5, blaT-6 / Plasmid: pJ411 / Production host:

Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62593,

beta-lactamase

#2: Water

ChemComp-HOH / water /

Water

Mass: 18.015 Da / Num. of mol.: 557 / 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: 2.09 Å³/Da / Density % sol: 41.04 %
Crystal grow	Temperature: 294 K / Method: vapor diffusion, hanging drop Details: 2% (v/v) tacsimate (pH 6.0), 0.1 M BIS-TRIS (pH 6.5), 20% (w/v) PEG 3350 PH range: 6.0 - 7.4

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SSRL / Beamline: BL14-1 / Wavelength: 1.181 Å
Detector	Type: MARMOSAIC 325 mm CCD / Detector: CCD / Date: May 18, 2016
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 1.181 Å / Relative weight: 1
Reflection twin	Operator: h,-k,-l / Fraction: 0.35
Reflection	Resolution: 1.82→62.92 Å / Num. obs: 82018 / % possible obs: 96.5 % / Redundancy: 3.8 % / R_merge(I) obs: 0.13 / Net I/σ(I): 6.3
Reflection shell	Resolution: 1.82→1.85 Å / Redundancy: 3.8 % / R_merge(I) obs: 0.444 / % possible all: 94.8

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Phasing

Phasing	Method: molecular replacement

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Processing

Software

Name	Version	Classification
PHENIX	1.9_1692	refinement
Aimless	0.5.17	data scaling
PHASER		phasing
PDB_EXTRACT	3.2	data extraction
iMOSFLM		data reduction

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 5HVI

5hvi

Resolution: 1.82→51.19 Å / Cross valid method: FREE R-VALUE / σ(F): 0.1 / Phase error: 36.97

	R_factor	Num. reflection	% reflection
R_free	0.227	8375	5.18 %
R_work	0.182	-	-
obs	0.185	81991	96.5 %

Solvent computation

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

Displacement parameters

B_iso mean: 11.32 Å²

Refinement step

Cycle: LAST / Resolution: 1.82→51.19 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	8037	0	0	557	8594

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.011	8200
X-RAY DIFFRACTION	f_angle_d	1.135	11129
X-RAY DIFFRACTION	f_dihedral_angle_d	13.613	3053
X-RAY DIFFRACTION	f_chiral_restr	0.048	1292
X-RAY DIFFRACTION	f_plane_restr	0.006	1453

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 (%)
1.8202-1.8516	0.289	384	0.2557	7501	X-RAY DIFFRACTION	90
1.8516-1.8853	0.3397	393	0.2423	7522	X-RAY DIFFRACTION	90
1.8853-1.9215	0.2523	344	0.2338	7674	X-RAY DIFFRACTION	91
1.9215-1.9608	0.2553	393	0.2179	7533	X-RAY DIFFRACTION	90
1.9608-2.0034	0.2507	336	0.2131	7655	X-RAY DIFFRACTION	91
2.0034-2.05	0.241	395	0.208	7612	X-RAY DIFFRACTION	91
2.05-2.1012	0.2446	367	0.2006	7686	X-RAY DIFFRACTION	91
2.1012-2.158	0.2428	417	0.1953	7605	X-RAY DIFFRACTION	90
2.158-2.2215	0.2241	447	0.1912	7603	X-RAY DIFFRACTION	91
2.2215-2.2932	0.2156	476	0.1943	7561	X-RAY DIFFRACTION	91
2.2932-2.3752	0.2474	346	0.1824	7775	X-RAY DIFFRACTION	92
2.3752-2.4702	0.2582	411	0.1891	7684	X-RAY DIFFRACTION	92
2.4702-2.5826	0.2115	458	0.179	7641	X-RAY DIFFRACTION	91
2.5826-2.7187	0.2441	393	0.188	7743	X-RAY DIFFRACTION	92
2.7187-2.889	0.2196	422	0.1827	7790	X-RAY DIFFRACTION	92
2.889-3.1119	0.2364	403	0.1762	7744	X-RAY DIFFRACTION	93
3.1119-3.4248	0.2231	369	0.1607	7840	X-RAY DIFFRACTION	93
3.4248-3.9198	0.2075	417	0.1446	7764	X-RAY DIFFRACTION	93
3.9198-4.9362	0.1907	502	0.1392	7811	X-RAY DIFFRACTION	93
4.9362-34.231	0.1882	457	0.1806	7801	X-RAY DIFFRACTION	93

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	2.1461	0.1189	-0.3645	0.8686	0.1954	0.565	-0.0252	-0.1298	-0.0915	0.0163	0.084	-0.0055	0.0189	-0.0345	0.0201	0.0391	0.0184	0.0328	0.1502	0.0592	0.1029	22.6283	-23.4251	108.1826
2	0.7884	-0.0675	-0.3348	0.2668	-0.2891	1.102	0.0191	-0.0574	-0.1095	-0.0033	0.0931	0.0777	0.0567	-0.1116	-0.0372	0.031	-0.0024	0.0012	0.1288	-0.0037	0.1257	13.3591	-19.9061	104.906
3	0.3325	-0.0881	0.012	0.1799	-0.0432	0.5643	0.0004	0.0674	0.0629	-0.0029	0.0083	-0.0255	-0.0751	0.0418	-0.0122	0.0419	-0.0052	0.0408	0.0864	0.0032	0.0936	16.5456	-5.2077	80.44
4	2.5763	-0.2308	-0.6576	1.4221	-0.1744	1.1793	-0.0367	-0.0502	-0.158	0.0159	-0.0879	0.0451	0.138	0.0604	0.0618	0.0445	-0.0018	0.0368	0.0659	-0.0117	0.0668	19.7136	-10.4821	80.9917
5	1.0532	0.2203	-0.4889	0.3702	-0.0971	0.2273	0.0481	-0.1428	0.0471	0.0477	-0.0333	-0.0143	-0.0286	0.0238	0.022	0.0173	-0.007	0.0205	0.0934	0.0014	0.083	12.4679	-3.5647	94.859
6	0.3683	-0.4495	-0.5733	0.6626	0.4715	1.3507	0.0333	0.0283	0.0242	0.0085	-0.0672	0.1431	0.0507	-0.1726	0.0373	0.0276	-0.0014	0.0157	0.1088	0.0194	0.0762	9.4767	-17.8994	96.7647
7	0.3439	-0.0258	0.0739	0.0681	0.0008	0.0794	0.0002	0.0094	-0.0422	-0.0056	0.0263	0.003	0.0158	0.021	0.0141	0.0125	0.0107	0.0366	0.106	0.0132	0.1158	19.9216	-20.4514	92.1141
8	2.332	0.7094	-0.2365	1.5443	0.1838	0.6279	-0.0716	-0.2133	-0.1936	0.0728	0.0172	-0.1489	0.0649	-0.0266	0.0604	0.0408	0.038	0.0216	0.1197	0.0142	0.0761	28.3702	-24.7196	101.2181
9	0.6255	-0.1261	-0.4074	0.7925	-0.1253	0.6411	0.0007	0.089	-0.0205	-0.035	-0.0112	-0.0189	0.0213	0.0176	0.0174	0.0254	-0.0016	0.0345	0.1137	-0.0226	0.09	-9.3393	-23.3459	103.8917
10	0.2415	0.0908	-0.1237	0.1654	0.06	0.1494	0.0008	-0.0116	-0.0333	-0.0096	0.0443	-0.0754	-0.0037	0.0709	0.162	0.0285	0.0023	0.0336	0.1261	-0.0005	0.1108	0.0083	-20.0755	107.63
11	1.2049	0.2806	0.004	0.3336	0.0056	1.3747	-0.0045	-0.0655	0.084	0.0205	-0.0396	0.0313	-0.0823	-0.0827	-0.0009	0.0406	-0.0071	0.0364	0.0544	-0.0003	0.0908	-4.1614	-5.9625	131.6327
12	1.3277	-0.0448	-0.4454	0.5101	0.2733	0.4384	0.0119	0.072	0.1061	-0.0792	0.0055	-0.0287	-0.0655	0.065	-0.0157	0.0372	-0.0177	0.0186	0.0703	0.0123	0.0697	0.9487	-3.4857	117.3182
13	0.772	0.1044	-0.0195	0.195	0.0751	0.1383	-0.001	0.005	-0.03	0.0165	0.0252	0.0025	0.0098	-0.0187	0.0225	0.0071	0.0092	0.0217	0.0841	0.0139	0.0853	-6.8497	-20.8426	117.7154
14	1.6662	0.6027	-0.0286	1.135	-0.2267	0.2879	0.0302	-0.0405	0.1027	0.057	-0.0451	0.0109	-0.066	0.0064	-0.0357	0.0539	0.0007	0.0405	0.1197	-0.004	0.0975	20.7423	-9.7227	155.9016
15	0.7198	-0.5005	0.547	0.9442	0.1604	1.3786	-0.0685	0.0814	0.1412	-0.059	0.021	-0.1749	-0.1912	0.1545	-0.0133	0.075	-0.0059	0.0459	0.0975	0.0048	0.1268	30.4557	-12.9344	152.0497
16	0.6003	0.2248	-0.0458	0.3158	-0.4203	0.7058	0.0026	0.0735	-0.0866	-0.0557	-0.0184	-0.048	0.0957	-0.0083	0	0.0383	-0.0011	0.0132	0.0408	-0.0212	0.1023	32.1876	-25.3479	128.958
17	2.6722	-0.083	0.573	1.9045	-0.2136	0.6811	0.0023	0.1308	-0.1767	0.0613	0.0626	0.2147	0.1322	-0.2507	-0.0246	0.063	-0.033	0.0308	0.1356	-0.0191	0.1009	18.6155	-31.7167	125.8014
18	0.4812	0.1825	0.2247	0.2343	-0.0672	0.3607	-0.0015	0.0046	0.0381	-0.013	-0.0124	-0.0381	0.0063	0.068	0.0195	0.0134	-0.0039	0.0332	0.0675	-0.0115	0.0855	30.3766	-26.6233	133.5447
19	1.671	0.3298	-0.2257	1.125	0.0864	1.2528	-0.0412	-0.0432	-0.0814	0.0759	0.0699	0.0423	0.146	-0.1671	-0.0017	0.0553	-0.0017	0.0286	0.1057	0.0071	0.0972	28.1386	-30.3632	147.0156
20	0.9748	0.2571	-1.0164	1.1163	-1.5468	3.7236	0.0326	0.0275	0.066	-0.0501	-0.0174	-0.0967	-0.1249	0.0848	-0.0057	0.0409	-0.0123	0.0316	0.0949	0.0024	0.0548	33.6752	-15.3571	144.2362
21	0.7074	0.0593	-0.3652	0.2994	0.0115	0.7089	0.0209	-0.0145	0.0433	0.0104	-0.0099	0.0178	-0.0451	-0.06	-0.0661	0.0309	-0.0022	0.0397	0.0643	0.0161	0.0811	23.4257	-12.5984	139.5831
22	0.8206	0.3546	-0.4971	1.7557	0.2756	0.8301	0.0621	-0.0655	0.1198	0.1151	-0.0232	0.1549	-0.0345	0.0084	-0.0814	0.0554	0.0217	0.0375	0.1562	-0.0005	0.0789	14.9669	-8.4475	148.7778
23	1.0567	0.0011	-0.1459	1.2261	-0.2387	1.3029	0.0093	-0.0594	0.0621	0.0868	-0.0349	-0.0143	-0.2327	0.1159	-0.0025	0.0702	-0.0125	0.0165	0.0905	-0.0066	0.087	10.4854	30.8924	131.8002
24	0.5852	-0.1612	-0.3812	0.0798	0.0803	0.6274	-0.0475	0.0541	-0.0739	-0.0221	-0.0251	-0.0014	0.0714	-0.0031	0.0016	0.0329	-0.0205	0.0379	0.0752	-0.0037	0.0829	17.519	16.5743	106.6047
25	0.8043	-0.1359	-0.1593	0.3106	-0.0257	0.5204	-0.0283	0.007	-0.0274	-0.0038	0.0054	0.0227	0.0464	-0.0339	0.006	0.0164	-0.0035	0.0389	0.086	0.007	0.0818	11.3371	13.6573	108.2137
26	1.3902	0.8852	-0.2955	0.7877	-0.2722	0.0947	0.0297	-0.1208	-0.065	0.0394	-0.0145	-0.0064	0.0118	-0.0384	0.0396	0.0354	-0.0071	0.034	0.1201	-0.014	0.1031	13.4372	11.6437	124.731
27	1.2368	0.6315	-0.8825	0.7679	-1.3973	2.8145	0.0817	-0.1494	0.0531	-0.0503	-0.0949	-0.1621	-0.1267	0.2448	0.0538	0.0619	-0.0167	0.0363	0.0945	-0.005	0.0696	19.239	26.596	121.9284
28	1.1001	0.067	-0.6477	0.5217	0.1626	1.0361	0.0139	-0.0568	0.1004	0.0079	0.0094	-0.0205	-0.0672	-0.0631	-0.0214	0.0333	0.0049	0.0165	0.0598	0.0064	0.0761	11.331	31.4048	111.8512
29	0.4697	-0.1168	-0.0002	0.3693	0.08	0.4579	0.0227	-0.0459	-0.0293	0.0349	-0	0.0296	0.0411	-0.0628	-0.0279	0.0453	-0.0244	0.0318	0.0528	0.02	0.0721	6.2009	25.4804	120.5899
30	1.821	0.312	-0.2194	1.545	-0.0433	1.0962	0.0031	-0.0564	0.1116	0.0666	0.0436	0.0459	-0.1702	-0.0789	-0.0323	0.061	-0.0023	0.0237	0.0806	-0.0119	0.0547	3.6555	32.0822	125.2706

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	CHAIN 'A' AND (RESID 26 THROUGH 50 )
2	X-RAY DIFFRACTION	2	CHAIN 'A' AND (RESID 51 THROUGH 68 )
3	X-RAY DIFFRACTION	3	CHAIN 'A' AND (RESID 69 THROUGH 118 )
4	X-RAY DIFFRACTION	4	CHAIN 'A' AND (RESID 119 THROUGH 131 )
5	X-RAY DIFFRACTION	5	CHAIN 'A' AND (RESID 132 THROUGH 179 )
6	X-RAY DIFFRACTION	6	CHAIN 'A' AND (RESID 180 THROUGH 195 )
7	X-RAY DIFFRACTION	7	CHAIN 'A' AND (RESID 196 THROUGH 271 )
8	X-RAY DIFFRACTION	8	CHAIN 'A' AND (RESID 272 THROUGH 290 )
9	X-RAY DIFFRACTION	9	CHAIN 'B' AND (RESID 26 THROUGH 50 )
10	X-RAY DIFFRACTION	10	CHAIN 'B' AND (RESID 51 THROUGH 68 )
11	X-RAY DIFFRACTION	11	CHAIN 'B' AND (RESID 69 THROUGH 131 )
12	X-RAY DIFFRACTION	12	CHAIN 'B' AND (RESID 132 THROUGH 179 )
13	X-RAY DIFFRACTION	13	CHAIN 'B' AND (RESID 180 THROUGH 290 )
14	X-RAY DIFFRACTION	14	CHAIN 'C' AND (RESID 26 THROUGH 50 )
15	X-RAY DIFFRACTION	15	CHAIN 'C' AND (RESID 51 THROUGH 68 )
16	X-RAY DIFFRACTION	16	CHAIN 'C' AND (RESID 69 THROUGH 98 )
17	X-RAY DIFFRACTION	17	CHAIN 'C' AND (RESID 99 THROUGH 118 )
18	X-RAY DIFFRACTION	18	CHAIN 'C' AND (RESID 119 THROUGH 155 )
19	X-RAY DIFFRACTION	19	CHAIN 'C' AND (RESID 156 THROUGH 179 )
20	X-RAY DIFFRACTION	20	CHAIN 'C' AND (RESID 180 THROUGH 195 )
21	X-RAY DIFFRACTION	21	CHAIN 'C' AND (RESID 196 THROUGH 271 )
22	X-RAY DIFFRACTION	22	CHAIN 'C' AND (RESID 272 THROUGH 290 )
23	X-RAY DIFFRACTION	23	CHAIN 'D' AND (RESID 26 THROUGH 68 )
24	X-RAY DIFFRACTION	24	CHAIN 'D' AND (RESID 69 THROUGH 98 )
25	X-RAY DIFFRACTION	25	CHAIN 'D' AND (RESID 99 THROUGH 155 )
26	X-RAY DIFFRACTION	26	CHAIN 'D' AND (RESID 156 THROUGH 179 )
27	X-RAY DIFFRACTION	27	CHAIN 'D' AND (RESID 180 THROUGH 195 )
28	X-RAY DIFFRACTION	28	CHAIN 'D' AND (RESID 196 THROUGH 229 )
29	X-RAY DIFFRACTION	29	CHAIN 'D' AND (RESID 230 THROUGH 251 )
30	X-RAY DIFFRACTION	30	CHAIN 'D' AND (RESID 252 THROUGH 290 )

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