PDB-6g32: Crystal structure of human geranylgeranyl diphosphate synthase mu...

ID or keywords:

Entry

Database: PDB / ID: 6g32

Title

Crystal structure of human geranylgeranyl diphosphate synthase mutant D188Y

Components

Geranylgeranyl pyrophosphate synthase

Keywords

TRANSFERASE / geranylgeranyl diphosphate synthase /

mevalonate pathway /

prenyltransferase / GGPPS

Function / homology

Function and homology information

isoprenoid metabolic process / geranylgeranyl diphosphate biosynthetic process / geranylgeranyl diphosphate synthase /

farnesyltranstransferase activity /

Transferases; Transferring alkyl or aryl groups, other than methyl groups / geranyl diphosphate biosynthetic process /

dimethylallyltranstransferase / farnesyl diphosphate biosynthetic process / (2E,6E)-farnesyl diphosphate synthase /

geranyltranstransferase activity ...
Similarity search - Function

Biological species

Homo sapiens (human)

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 3.281 Å

Authors

Lisnyansky, M. / Kapelushnik, N. / Ben-Bassat, A. / Marom, M. / Loewenstein, A. / Khananshvili, D. / Giladi, M. / Haitin, Y.

Funding support

Israel, 4items

Organization	Grant number	Country
Other government	Israel Science Foundation (ISF) grant 1721/16	Israel
Other government	Israel Science Foundation (ISF) grant 1775/12	Israel
Other government	Israel Cancer Research Foundation (ICRF) grant 01214	Israel
German Research Foundation	I-2425-418.13/2016	Israel

Citation

Journal: Mol. Pharmacol. / Year: 2018
Title: Reduced Activity of Geranylgeranyl Diphosphate Synthase Mutant Is Involved in Bisphosphonate-Induced Atypical Fractures.
Authors: Lisnyansky, M. / Kapelushnik, N. / Ben-Bassat, A. / Marom, M. / Loewenstein, A. / Khananshvili, D. / Giladi, M. / Haitin, Y.

History

Deposition	Mar 24, 2018	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Oct 17, 2018	Provider: repository / Type: Initial release
Revision 1.1	Oct 24, 2018	Group: Data collection / Database references / Category: citation Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2	Nov 7, 2018	Group: Data collection / Database references / Category: citation Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title
Revision 1.3	Jan 17, 2024	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	6g32.cif.gz	658.2 KB	Display	PDBx/mmCIF format
PDB format	pdb6g32.ent.gz	546.7 KB	Display	PDB format
PDBx/mmJSON format	6g32.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/g3/6g32 ftp://data.pdbj.org/pub/pdb/validation_reports/g3/6g32	HTTPS FTP

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Related structure data

Related structure data	6g31C 2q80S S: Starting model for refinement C: citing same article (ref.)
Similar structure data	6g31-2 2oby-d 6g31-1 5mvj-d 4kc5-1 4hmy-d 6n8d-d 5mp5-d 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	#201 - Sep 2016 Isoprene Synthase similarity (8) #96 - Dec 2007 Oxidosqualene Cyclase similarity (1)

Deposited unit

A: Geranylgeranyl pyrophosphate synthase

B: Geranylgeranyl pyrophosphate synthase

C: Geranylgeranyl pyrophosphate synthase

D: Geranylgeranyl pyrophosphate synthase

E: Geranylgeranyl pyrophosphate synthase

F: Geranylgeranyl pyrophosphate synthase

hetero molecules

213 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

C: Geranylgeranyl pyrophosphate synthase

D: Geranylgeranyl pyrophosphate synthase

E: Geranylgeranyl pyrophosphate synthase

F: Geranylgeranyl pyrophosphate synthase

hetero molecules

A: Geranylgeranyl pyrophosphate synthase

B: Geranylgeranyl pyrophosphate synthase

hetero molecules

defined by author&software
Evidence: SAXS
213 kDa, 6 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	148.540, 148.540, 268.230
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	96
Space group name H-M	P4₃2₁2

#1: Protein	Geranylgeranyl pyrophosphate synthase / GGPPSase / (2E / 6E)-farnesyl diphosphate synthase / Dimethylallyltranstransferase / Farnesyl ...GGPPSase / (2E / 6E)-farnesyl diphosphate synthase / Dimethylallyltranstransferase / Farnesyl diphosphate synthase / Farnesyltranstransferase / Geranylgeranyl diphosphate synthase / Geranyltranstransferase Mass: 35484.367 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: GGPS1 / Variant: Asp188Tyr / Production host: Escherichia coli (E. coli) References: UniProt: O95749, Transferases; Transferring alkyl or aryl groups, other than methyl groups, dimethylallyltranstransferase, geranylgeranyl diphosphate synthase, (2E,6E)-farnesyl diphosphate synthase
#2: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C₃H₈O₃
#3: Water	ChemComp-HOH / water / Water Mass: 18.015 Da / Num. of mol.: 1 / 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: 3.47 Å³/Da / Density % sol: 64.6 %
Crystal grow	Temperature: 292 K / Method: vapor diffusion, sitting drop Details: 3.6M Sodium formate, 0.01% w/v aspartame, 0.01% w/v gly-gly-gly, 0.01% w/v pentaglycine, 0.01% w/v tyr-ala, 0.01% w/v tyr-phe, 0.0018M HEPES sodium pH 6.8

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID30B / Wavelength: 0.968 Å
Detector	Type: DECTRIS EIGER X 4M / Detector: PIXEL / Date: Dec 8, 2017
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.968 Å / Relative weight: 1
Reflection	Resolution: 3.19→48.901 Å / Num. obs: 50043 / % possible obs: 98.4 % / Redundancy: 4.54 % / R_merge(I) obs: 0.205 / Net I/σ(I): 7.76
Reflection shell	Resolution: 3.19→3.206 Å

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Processing

Software

Name	Version	Classification
PHENIX	(1.11.1_2575: ???)	refinement
XDS		data reduction
XDS		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: 2Q80

2q80

Resolution: 3.281→48.901 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 25.89

	R_factor	Num. reflection	% reflection
R_free	0.2575	1978	5.03 %
R_work	0.2059	-	-
obs	0.2085	39361	84.34 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 3.281→48.901 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	12962	0	36	1	12999

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.007	13306
X-RAY DIFFRACTION	f_angle_d	0.893	18179
X-RAY DIFFRACTION	f_dihedral_angle_d	14.635	7740
X-RAY DIFFRACTION	f_chiral_restr	0.047	2116
X-RAY DIFFRACTION	f_plane_restr	0.006	2326

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 (%)
3.2814-3.3635	0.329	16	0.3476	272	X-RAY DIFFRACTION	9
3.3635-3.4544	0.3637	34	0.3045	832	X-RAY DIFFRACTION	26
3.4544-3.556	0.3367	80	0.2962	1721	X-RAY DIFFRACTION	55
3.556-3.6708	0.3419	176	0.2933	3046	X-RAY DIFFRACTION	99
3.6708-3.8019	0.3215	157	0.2486	3135	X-RAY DIFFRACTION	100
3.8019-3.9541	0.2978	164	0.2348	3128	X-RAY DIFFRACTION	100
3.9541-4.1339	0.2652	172	0.2178	3123	X-RAY DIFFRACTION	100
4.1339-4.3518	0.2493	172	0.2063	3135	X-RAY DIFFRACTION	100
4.3518-4.6242	0.2363	175	0.1852	3125	X-RAY DIFFRACTION	100
4.6242-4.9809	0.2339	157	0.1745	2952	X-RAY DIFFRACTION	93
4.9809-5.4816	0.2505	159	0.1999	3090	X-RAY DIFFRACTION	97
5.4816-6.2734	0.3295	178	0.2416	3184	X-RAY DIFFRACTION	100
6.2734-7.8984	0.2617	169	0.211	3247	X-RAY DIFFRACTION	100
7.8984-48.9067	0.1881	169	0.157	3393	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	5.1508	-1.095	0.5337	7.767	0.702	6.5269	-0.2316	0.0019	-1.0472	0.4542	-0.0497	1.3226	0.1066	-1.0288	0.8884	0.4696	-0.1085	0.1425	0.8109	-0.03	0.5368	40.4144	10.8716	24.1929
2	1.1913	-2.7949	-2.2511	6.8413	5.3153	4.1673	0.2369	-0.2378	-0.694	0.6275	-0.6858	1.1629	0.4511	-0.2857	0.4325	0.7799	0.1406	-0.1709	1.0693	-0.1572	0.8034	34.922	32.3574	36.0645
3	0.4913	0.5673	-0.5408	3.5757	0.7081	0.9795	-0.0672	-0.3533	0.2475	0.3898	-0.0104	0.1752	-0.1776	-0.1305	0.1187	0.5398	0.1408	-0.0535	0.7282	-0.0576	0.3991	47.9464	27.8587	27.7304
4	4.6743	-3.675	0.5808	4.4781	0.5634	0.6526	0.0601	0.0894	-0.4749	0.6836	0.2197	0.0039	0.4842	-0.2166	-0.4017	0.7346	0.0167	-0.1267	0.5566	-0.0297	0.5579	54.0201	29.5067	43.13
5	6.0083	-1.0124	1.1278	8.7449	-2.244	6.9326	-0.1319	-0.3402	-0.0554	0.7202	0.2871	-1.2252	0.6706	1.3981	-0.2914	0.5672	0.0813	-0.0442	0.7734	-0.1024	0.4583	68.5514	26.9201	48.1319
6	8.6357	-2.5793	0.5458	2.0451	0.1898	2.503	-0.563	-1.2385	-0.442	0.4585	0.4507	0.3598	-0.4486	-0.1983	0.2257	0.7706	0.1911	-0.0408	0.5827	-0.011	0.5754	45.8558	39.6472	47.7995
7	6.0895	-1.4429	3.1892	0.3928	-0.425	7.4091	0.1096	0.2087	0.0549	-0.4046	-0.0455	-0.008	0.1522	0.2683	-0.0074	0.6516	0.0164	-0.098	0.5186	0.0178	0.3933	60.3537	22.7426	7.954
8	0.9832	1.2353	0.0296	3.1623	1.6316	1.3569	0.1254	0.2223	-0.0602	-0.2577	0.0204	-0.0388	-0.108	-0.2426	-0.1288	0.4698	0.0266	0.025	0.519	0.02	0.376	50.1812	12.8529	6.8668
9	1.4168	-2.3566	2.5662	7.6362	-5.2406	9.5529	0.0601	0.1787	-0.1513	-0.3978	0.0198	0.0185	0.7197	0.1122	-0.1153	0.3047	-0.023	0.0374	0.4788	-0.1185	0.3837	56.8447	-1.586	-0.4606
10	2.175	-1.7737	0.994	8.8085	-3.2853	3.0094	-0.0662	0.659	0.5564	-0.5113	-0.4794	-0.5491	-0.68	0.8852	0.5637	0.8864	-0.0755	0.0783	0.7082	0.1056	0.614	85.2114	41.8501	-38.1013
11	5.1707	-1.3513	0.4061	0.7651	-0.9434	1.3089	-0.0853	0.5579	0.222	0.0573	-0.0194	-0.0094	-0.2919	0.2551	0.1216	0.7505	-0.0292	0.0452	0.6454	-0.0047	0.4254	73.8883	35.6744	-35.4879
12	2.9769	2.0735	2.783	2.1609	0.5193	4.372	0.103	0.1044	0.4811	-0.1213	0.1023	-0.365	-0.9306	0.8408	-0.2156	0.7621	-0.0453	0.1279	0.5846	-0.0984	0.5675	69.5918	42.3107	-45.6476
13	3.5386	1.4632	1.5821	8.976	1.2644	2.4061	-0.0886	0.4955	0.1881	-1.1392	-0.0773	-0.1221	-0.1421	0.1707	0.0979	0.6376	0.0752	0.1513	0.5884	-0.0052	0.4258	63.3225	35.2393	-55.6999
14	1.5876	1.4534	1.651	3.2825	3.1098	4.1671	0.1787	-0.2413	0.0359	0.3058	-0.0586	-0.0803	-0.1554	-0.4862	-0.124	0.7293	-0.0359	0.1091	0.6268	-0.0206	0.57	68.86	26.0623	-15.6579
15	3.0247	1.1147	-0.1354	1.4925	0.645	0.3166	-0.2493	-0.4113	0.2002	0.4692	0.2026	-0.034	-0.4124	0.2086	-0.0014	0.8691	0.0641	0.0205	0.5412	-0.0435	0.4341	81.1718	31.7656	-16.2941
16	1.3232	-1.8146	-1.8923	5.5747	0.8059	5.01	0.2886	0.1741	-0.2733	-0.7272	-0.588	0.8291	-0.2281	-0.958	0.282	0.3993	-0.093	-0.1054	0.624	0.0108	0.4737	86.4904	14.3491	-11.0974
17	1.2914	-1.3898	0.9759	7.2272	4.8016	7.0572	0.1191	0.0538	0.0655	0.6354	0.0997	-0.2738	0.9965	0.2026	-0.1992	0.4747	-0.1414	-0.0239	0.5404	-0.0223	0.4036	88.0654	11.1548	-7.2706
18	4.3229	1.339	-0.4273	4.3055	-0.6901	0.116	0.108	0.1494	-0.189	1.0215	0.2393	-0.8814	-0.4149	-0.4191	-0.1482	0.7844	0.1554	-0.1444	1.0147	-0.1612	0.6659	106.2678	-3.7007	-24.4291
19	0.6582	-0.6818	0.8849	7.3535	1.2006	1.8094	-0.6441	-1.1725	-1.1866	0.6142	2.0551	0.342	-0.419	-0.8169	-0.8358	0.6753	0.2025	0.06	1.4129	0.0549	1.2729	108.8688	-27.4281	-16.3979
20	3.4879	-0.33	-0.1745	1.5307	0.4952	1.9875	0.5039	-0.371	-1.3984	-0.1758	0.2411	-0.7971	0.4753	0.4865	-0.7123	0.5397	0.1449	-0.1371	0.8493	-0.0662	0.8703	106.7217	-17.92	-24.9191
21	3.5371	-1.8558	-0.8845	1.9634	-0.1016	2.4968	0.1433	-0.1736	-0.288	0.1237	0.1449	-0.5841	0.5188	0.2448	-0.4167	0.4999	0.0773	-0.1497	0.9418	-0.0467	0.7522	103.1338	-11.2547	-28.8418
22	1.9343	1.5845	-2.5473	3.6026	-1.1276	4.2046	-0.0995	-0.399	-0.1514	0.0099	0.2176	-0.6323	0.3816	0.1836	0.0243	0.5741	0.1001	-0.0522	0.8215	-0.1593	0.7242	103.1124	-28.638	-33.7071
23	5.7341	-1.1878	-0.0473	1.5229	-1.4823	1.7841	0.1982	-0.3658	0.2388	0.3064	0.4024	-0.4242	0.3498	0.2881	-0.3499	0.7565	0.181	-0.1042	0.7141	-0.2129	0.8305	88.1917	-30.434	-26.924
24	9.4587	0.6824	1.311	2.0477	0.0138	4.7048	-0.1477	-0.2811	-0.6894	0.0197	0.2921	0.6994	0.2154	0.6074	-0.1601	0.5476	0.2096	-0.0029	0.663	-0.0052	0.6805	74.14	-27.4246	-31.2396
25	6.7576	-2.8204	4.042	4.8783	0.2262	6.5539	-0.8963	-2.2695	-2.7755	0.1808	1.2043	-0.2894	-0.1875	-0.547	-0.3251	0.6143	0.0669	-0.1158	0.7301	0.0521	1.2572	93.2039	-41.6621	-21.4166
26	6.7909	0.1117	-0.6626	4.3351	0.9021	1.8365	-1.6006	-1.5883	-0.5109	0.8266	1.6915	0.6904	0.7052	-0.2089	-0.2619	1.3748	0.3663	-0.1072	1.0159	0.1847	0.916	99.927	-36.7521	-13.588
27	2.8435	-0.299	-1.2127	4.4158	-1.3235	1.1354	-0.2788	0.459	-1.2189	-1.0245	0.1507	0.0844	0.1089	0.1239	-0.2606	0.7741	-0.1213	-0.0281	0.9346	-0.0578	0.8605	99.3046	-20.7619	-50.2485
28	3.9706	2.9965	1.8544	2.226	1.3849	0.8626	-0.4098	-0.1541	-0.1276	-0.5977	0.4494	-0.8267	-0.3366	-0.354	-0.2165	0.9987	0.3025	0.2376	1.384	0.3339	1.2637	118.1922	-5.7967	-57.7456
29	5.7889	-2.2295	0.8684	0.8389	-0.1816	0.8672	-0.11	0.1755	-0.1526	-0.385	0.4112	-0.9106	-0.0344	0.8413	-0.0967	0.5311	0.1327	0.1303	0.9552	-0.2327	0.9127	105.0676	-12.1933	-46.9763
30	1.2224	0.711	0.9976	3.2082	-1.8245	2.8435	0.0949	0.5422	-0.0429	-0.4174	-0.0049	-0.6603	0.2453	0.2724	-0.0688	0.5971	-0.0091	0.1425	0.9013	-0.1424	0.8042	114.2843	1.3457	-43.2557
31	0.5486	0.0421	1.124	3.1212	-0.4454	2.3735	-0.7158	0.4566	-0.1803	-1.5155	0.1943	0.4544	0.576	0.5818	-0.4856	0.7037	-0.1307	0.0556	1.1586	0.0133	1.0201	96.2798	9.2934	-47.5785
32	9.3516	-2.962	0.5457	6.9614	4.721	4.3086	0.0316	-0.2699	0.941	-0.1789	0.1172	-0.6869	-0.1937	0.3746	-0.2844	0.5455	-0.0561	0.1513	0.9264	0.1198	0.7244	96.6087	19.1239	-43.0459
33	7.4869	-2.8584	-0.5764	1.9127	1.3251	1.7317	0.3337	2.0156	1.0865	-0.4659	-0.1228	-0.9244	-0.2352	0.3064	-0.1684	0.8665	-0.1037	0.3791	1.2266	0.0825	1.1628	117.9148	11.8963	-56.2146

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 5 through 20 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 21 through 42 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 43 through 173 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 174 through 214 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 215 through 255 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 256 through 296 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 5 through 84 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 85 through 223 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 224 through 296 )
10	X-RAY DIFFRACTION	10	chain 'C' and (resid 6 through 42 )
11	X-RAY DIFFRACTION	11	chain 'C' and (resid 43 through 152 )
12	X-RAY DIFFRACTION	12	chain 'C' and (resid 153 through 214 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 215 through 296 )
14	X-RAY DIFFRACTION	14	chain 'D' and (resid 6 through 84 )
15	X-RAY DIFFRACTION	15	chain 'D' and (resid 85 through 173 )
16	X-RAY DIFFRACTION	16	chain 'D' and (resid 174 through 223 )
17	X-RAY DIFFRACTION	17	chain 'D' and (resid 224 through 296 )
18	X-RAY DIFFRACTION	18	chain 'E' and (resid 5 through 20 )
19	X-RAY DIFFRACTION	19	chain 'E' and (resid 21 through 42 )
20	X-RAY DIFFRACTION	20	chain 'E' and (resid 43 through 67 )
21	X-RAY DIFFRACTION	21	chain 'E' and (resid 68 through 108 )
22	X-RAY DIFFRACTION	22	chain 'E' and (resid 109 through 173 )
23	X-RAY DIFFRACTION	23	chain 'E' and (resid 174 through 223 )
24	X-RAY DIFFRACTION	24	chain 'E' and (resid 224 through 255 )
25	X-RAY DIFFRACTION	25	chain 'E' and (resid 256 through 277 )
26	X-RAY DIFFRACTION	26	chain 'E' and (resid 278 through 295 )
27	X-RAY DIFFRACTION	27	chain 'F' and (resid 5 through 20 )
28	X-RAY DIFFRACTION	28	chain 'F' and (resid 21 through 42 )
29	X-RAY DIFFRACTION	29	chain 'F' and (resid 43 through 108 )
30	X-RAY DIFFRACTION	30	chain 'F' and (resid 109 through 194 )
31	X-RAY DIFFRACTION	31	chain 'F' and (resid 195 through 214 )
32	X-RAY DIFFRACTION	32	chain 'F' and (resid 215 through 255 )
33	X-RAY DIFFRACTION	33	chain 'F' and (resid 256 through 295 )

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