PDB-4pc1: Elongation Factor Tu:Ts complex with a bound phosphate

ID or keywords:

Entry

Database: PDB / ID: 4pc1

Title

Elongation Factor Tu:Ts complex with a bound phosphate

Components

(Elongation factor ...) x 2

Keywords

TRANSLATION / G:GEF complex / elongation factor / Protein synthesis

Function / homology

Function and homology information

guanosine tetraphosphate binding / translation elongation factor activity / GTPase activity / GTP binding / cytoplasm / cytosol
Similarity search - Function

GTP Cyclohydrolase I; Chain A, domain 1 - #20 / Elongation factor Ts, dimerisation domain / Translation elongation factor EFTs/EF1B / Translation elongation factor EFTs/EF1B, dimerisation / Translation elongation factor Ts, conserved site / Elongation factor Ts, dimerisation domain superfamily / Elongation factor TS / Elongation factor Ts signature 1. / Elongation factor Ts signature 2. / GTP Cyclohydrolase I; Chain A, domain 1 ...
Similarity search - Domain/homology

Biological species

Escherichia coli (E. coli)

Method

X-RAY DIFFRACTION /

SYNCHROTRON / Resolution: 1.95 Å

Authors

Thirup, S.S.

Citation

Journal: J.Struct.Biol. / Year: 2015
Title: Structural outline of the detailed mechanism for elongation factor Ts-mediated guanine nucleotide exchange on elongation factor Tu.
Authors: Thirup, S.S. / Van, L.B. / Nielsen, T.K. / Knudsen, C.R.

History

Deposition	Apr 14, 2014	Deposition site: RCSB / Processing site: RCSB
Revision 1.0	May 6, 2015	Provider: repository / Type: Initial release
Revision 1.1	Jul 1, 2015	Group: Database references
Revision 1.2	Jul 15, 2015	Group: Database references
Revision 1.3	Sep 27, 2023	Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description / Source and taxonomy Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / database_2 / entity_src_gen / pdbx_initial_refinement_model / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn Item: _citation.journal_id_CSD / _database_2.pdbx_DOI ..._citation.journal_id_CSD / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity_src_gen.pdbx_alt_source_flag / _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.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.value / _pdbx_struct_oper_list.symmetry_operation / _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.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

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	4pc1.cif.gz	745.7 KB	Display	PDBx/mmCIF format
PDB format	pdb4pc1.ent.gz	632.2 KB	Display	PDB format
PDBx/mmJSON format	4pc1.json.gz		Tree view	PDBx/mmJSON format
Others	Other downloads

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Validation report

Summary document	4pc1_validation.pdf.gz	485.3 KB	Display	wwPDB validaton report
Full document	4pc1_full_validation.pdf.gz	493.1 KB	Display
Data in XML	4pc1_validation.xml.gz	59.5 KB	Display
Data in CIF	4pc1_validation.cif.gz	92 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/pc/4pc1 ftp://data.pdbj.org/pub/pdb/validation_reports/pc/4pc1	HTTPS FTP

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Related structure data

Related structure data	4pc2C 4pc3C 4pc6C 4pc7C 1tuiS S: Starting model for refinement C: citing same article (ref.)
Similar structure data	4pc6-1 4pc3-2 4pc3-1 4pc2-2 4pc6-2 4pc2-1 1iye-d 1iyd-d 2ej3-d 1xmx-2 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	#81 - Sep 2006 Elongation Factors similarity (22) #196 - Apr 2016 Lead Poisoning similarity (1) #121 - Jan 2010 70S Ribosomes similarity (13) #157 - Jan 2013 Transfer-Messenger RNA similarity (13) #214 - Oct 2017 Chimeric Antigen Receptors similarity (1) #48 - Dec 2003 Catabolite Activator Protein similarity (1) #56 - Aug 2004 Caspases similarity (1) #104 - Aug 2008 Selenocysteine Synthase similarity (6) #245 - May 2020 Spliceosomes similarity (5) #60 - Dec 2004 Ubiquitin similarity (1)

PDB pages

PDBj /

wwPDB /

NCBI

Related items in Molecule of the Month

#81 - Sep 2006
Elongation Factors
similarity (22)
#196 - Apr 2016
Lead Poisoning
similarity (1)
#121 - Jan 2010
70S Ribosomes
similarity (13)
#157 - Jan 2013
Transfer-Messenger RNA
similarity (13)
#214 - Oct 2017
Chimeric Antigen Receptors
similarity (1)
#48 - Dec 2003
Catabolite Activator Protein
similarity (1)
#56 - Aug 2004
Caspases
similarity (1)
#104 - Aug 2008
Selenocysteine Synthase
similarity (6)
#245 - May 2020
Spliceosomes
similarity (5)
#60 - Dec 2004
Ubiquitin
similarity (1)

Deposited unit

A: Elongation factor Tu

B: Elongation factor Tu

C: Elongation factor Ts

D: Elongation factor Ts

hetero molecules

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

1

A: Elongation factor Tu

C: Elongation factor Ts

hetero molecules

defined by author&software
74.5 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

2

B: Elongation factor Tu

D: Elongation factor Ts

hetero molecules

defined by author&software
73.9 kDa, 2 polymers
Search similar-shape structures of this assembly by Omokage search (details)

Unit cell

Length a, b, c (Å)	73.510, 109.770, 195.030
Angle α, β, γ (deg.)	90.00, 90.00, 90.00
Int Tables number	19
Space group name H-M	P2₁2₁2₁

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Elongation factor ... , 2 types, 4 molecules ABCD

#1: Protein	Elongation factor Tu / EF-Tu Mass: 43340.465 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Strain: K12 / DH10B / Gene: tufA, tuf, ECDH10B_3514 / Production host: Escherichia coli (E. coli) / References: UniProt: B1X6I9, UniProt: A0A0M3KKV1*PLUS
#2: Protein	Elongation factor Ts / EF-Ts Mass: 30332.795 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Gene: tsf, BN17_45931, ECs0172, LF82_2325 / Production host: Escherichia coli (E. coli) / References: UniProt: C3TPM7

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Non-polymers , 5 types, 1410 molecules

#3: Chemical	ChemComp-PO4 / PHOSPHATE ION Mass: 94.971 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: PO₄
#4: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C₃H₈O₃
#5: Chemical	ChemComp-PB / LEAD (II) ION Mass: 207.200 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Pb
#6: Chemical	ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER Mass: 122.143 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C₄H₁₂NO₃ / Comment: pH buffer*YM
#7: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1402 / 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: 2.67 Å³/Da / Density % sol: 53.85 %
Crystal grow	Temperature: 292 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 100 mM Hepes,22% PEG 6000, 150mM NaCl, 10% glycerol

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: SRS / Beamline: PX9.5 / Wavelength: 0.9215 Å
Detector	Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE / Date: Aug 10, 1995
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9215 Å / Relative weight: 1
Reflection	Resolution: 1.95→68.8 Å / Num. obs: 118029 / % possible obs: 96.8 % / Redundancy: 2.7 % / R_sym value: 0.091 / Net I/σ(I): 11.6
Reflection shell	Resolution: 1.95→2 Å / Redundancy: 2.6 % / R_merge(I) obs: 0.658 / Mean I/σ(I) obs: 1.8 / % possible all: 97.2

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Processing

Software

Name: PHENIX / Version: (phenix.refine: dev_1593) / Classification: refinement

Refinement

Starting model: PDB ENTRY 1TUI

1tui

Resolution: 1.95→68.786 Å / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 20.52 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.2077	4526	3.99 %	Random
R_work	0.1743	-	-	-
obs	0.1757	113382	98.08 %	-

Solvent computation

Shrinkage radii: 1 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL

Refinement step

Cycle: LAST / Resolution: 1.95→68.786 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	9788	0	38	1402	11228

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.013	10073
X-RAY DIFFRACTION	f_angle_d	1.35	13601
X-RAY DIFFRACTION	f_dihedral_angle_d	13.888	3799
X-RAY DIFFRACTION	f_chiral_restr	0.054	1559
X-RAY DIFFRACTION	f_plane_restr	0.007	1775

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 (%)
1.95-1.9722	0.3215	132	0.2779	3625	X-RAY DIFFRACTION	98
1.9722-1.9954	0.2914	139	0.258	3581	X-RAY DIFFRACTION	98
1.9954-2.0197	0.295	162	0.2515	3555	X-RAY DIFFRACTION	98
2.0197-2.0453	0.2848	152	0.2404	3571	X-RAY DIFFRACTION	97
2.0453-2.0722	0.2393	131	0.2325	3597	X-RAY DIFFRACTION	98
2.0722-2.1006	0.2814	135	0.2174	3610	X-RAY DIFFRACTION	97
2.1006-2.1306	0.2737	169	0.2175	3557	X-RAY DIFFRACTION	98
2.1306-2.1624	0.2293	151	0.2051	3608	X-RAY DIFFRACTION	97
2.1624-2.1962	0.2191	164	0.2022	3573	X-RAY DIFFRACTION	99
2.1962-2.2322	0.2288	156	0.1917	3556	X-RAY DIFFRACTION	98
2.2322-2.2707	0.2114	141	0.186	3612	X-RAY DIFFRACTION	99
2.2707-2.312	0.2282	155	0.1855	3605	X-RAY DIFFRACTION	98
2.312-2.3564	0.2414	158	0.1787	3605	X-RAY DIFFRACTION	98
2.3564-2.4045	0.204	143	0.1769	3574	X-RAY DIFFRACTION	98
2.4045-2.4568	0.2345	161	0.1771	3587	X-RAY DIFFRACTION	97
2.4568-2.514	0.2461	153	0.1717	3607	X-RAY DIFFRACTION	98
2.514-2.5769	0.2041	166	0.1695	3582	X-RAY DIFFRACTION	98
2.5769-2.6465	0.2381	158	0.1737	3588	X-RAY DIFFRACTION	97
2.6465-2.7244	0.2083	138	0.1688	3593	X-RAY DIFFRACTION	97
2.7244-2.8123	0.2063	135	0.1722	3647	X-RAY DIFFRACTION	98
2.8123-2.9129	0.2169	165	0.1737	3587	X-RAY DIFFRACTION	98
2.9129-3.0295	0.1988	152	0.1653	3594	X-RAY DIFFRACTION	98
3.0295-3.1674	0.1956	140	0.172	3640	X-RAY DIFFRACTION	97
3.1674-3.3344	0.1797	159	0.163	3588	X-RAY DIFFRACTION	97
3.3344-3.5433	0.1754	160	0.1649	3622	X-RAY DIFFRACTION	98
3.5433-3.8168	0.2111	131	0.1574	3725	X-RAY DIFFRACTION	99
3.8168-4.2009	0.1754	149	0.1421	3731	X-RAY DIFFRACTION	99
4.2009-4.8086	0.1543	145	0.1325	3774	X-RAY DIFFRACTION	100
4.8086-6.0578	0.1848	153	0.1559	3825	X-RAY DIFFRACTION	100
6.0578-68.8289	0.1827	173	0.1737	3937	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	1.8933	0.6728	0.3582	2.3966	0.6148	2.2887	0.0625	-0.1607	0.1156	0.1803	0.0282	-0.1942	-0.1579	0.0587	-0.0245	0.1844	0.0121	-0.0124	0.1224	-0.028	0.1474	14.4001	61.427	73.3049
2	3.9769	-1.7767	2.5207	3.2745	-2.8862	3.6289	-0.1916	-0.1062	0.0751	0.3904	0.1319	-0.5235	-0.3497	0.3286	0.1151	0.3962	0.1516	-0.1184	0.5264	-0.184	0.3041	33.118	45.4271	101.8355
3	0.1976	0.0971	0.007	0.9223	0.6417	1.8738	-0.1685	-0.4047	0.1591	0.1999	0.0057	0.0445	-0.1401	-0.3043	-0.0632	0.2599	0.1264	-0.0527	0.4402	-0.1788	0.2312	26.9789	35.9256	93.1835
4	2.4492	0.6765	-0.8811	2.0915	-0.2492	1.5017	0.1649	-0.3336	-0.2874	0.2398	-0.1801	0.0603	0.1918	-0.0487	-0.025	0.3166	-0.1129	-0.0323	0.2189	0.052	0.1707	48.1919	-16.6827	79.5634
5	0.0797	0.011	0.1644	0.9855	-0.3564	0.4094	0.0989	-0.0835	-0.2095	0.4313	0.1915	0.2847	-0.0166	-0.2173	0.3835	0.5918	-0.3954	0.33	1.1395	0.1606	-0.0233	23.9194	-2.0001	99.2845
6	0.4288	-0.2423	-0.0373	0.2329	0.0744	0.0451	0.1159	-0.635	-0.3753	0.372	0.1037	0.3237	0.0035	-0.0864	0.1484	0.8629	-0.5519	0.3038	1.312	0.1458	-0.0509	20.4838	3.5433	105.7804
7	1.1993	-0.0734	-0.0971	1.7153	-0.0578	1.3403	0.1976	-0.6799	-0.1486	0.6319	-0.2928	0.0064	0.1532	-0.2328	-0.0343	0.3173	-0.1628	0.0294	0.5001	-0.0171	0.1077	32.4748	11.137	91.551
8	4.4766	-0.2896	1.1941	2.0215	-0.4424	3.1691	-0.086	-0.4345	-0.0643	0.1074	0.2631	0.2533	-0.1426	-0.5394	-0.1577	0.1873	0.0871	-0.0082	0.2528	0.0409	0.1844	-6.9979	62.9639	57.9131
9	3.5689	-3.7578	-0.7184	4.5264	0.5004	1.7543	0.1379	-0.0496	-0.2282	-0.0937	0.0496	0.2771	-0.0526	-0.2207	-0.0962	0.1556	-0.0076	-0.0229	0.132	0.0471	0.1408	-1.0718	56.4193	49.0393
10	0.2533	0.2664	0.0412	2.9856	-0.0643	0.2992	-0.01	-0.0045	0.0243	0.0985	0.0236	0.0625	0.0188	-0.0756	-0.0204	0.0945	0.0032	-0.0122	0.1247	0.0003	0.1365	6.9823	35.5423	56.0536
11	0.5438	-0.7121	0.3277	4.0864	-0.6731	0.7032	-0.0326	-0.0205	0.0199	-0.1135	0.0749	0.0059	-0.0153	-0.024	-0.0551	0.0709	-0.0174	0.0089	0.1179	-0.0021	0.102	8.343	32.9565	54.4032
12	3.0426	0.7927	-1.7741	2.8062	-0.2309	5.0614	0.0339	0.1411	-0.1881	0.0832	0.0267	0.0055	0.1009	-0.0693	-0.0219	0.0881	0.0107	-0.0454	0.1037	-0.0153	0.145	19.3468	17.1311	59.5392
13	4.0447	4.093	4.3651	5.5222	4.4262	5.8272	-0.2108	0.3835	0.1922	-0.2758	-0.1235	0.1813	-0.2415	-0.0793	0.2561	0.157	0.043	0.0056	0.2114	0.017	0.1368	42.4539	18.8514	47.5774
14	6.0295	1.1947	-0.2297	3.5716	-2.1145	1.5828	0.0835	0.31	-0.3951	-0.1887	-0.1028	-0.0705	0.1986	0.0369	0.0686	0.1827	0.0228	-0.0344	0.1798	-0.0635	0.1517	43.2455	13.2246	53.4875
15	2.0867	0.166	0.6353	2.3725	-0.2967	2.0207	0.0917	-0.0392	-0.2783	0.0306	-0.102	-0.1344	0.2562	0.0661	-0.0071	0.0934	-0.0045	-0.0213	0.1101	-0.0107	0.1529	20.3126	13.5779	61.9598
16	0.932	0.9192	1.0458	1.4508	1.9382	2.5262	-0.067	0.1146	0.0098	-0.4582	0.4524	-0.9411	-0.3041	0.4725	-0.2924	0.2626	-0.0141	0.131	0.255	-0.0823	0.4802	26.2427	52.9458	60.4766
17	3.0343	-2.2462	0.3881	3.4502	0.2515	3.5769	0.0247	-0.184	-0.6404	0.1256	-0.0698	-0.6385	0.7032	0.5185	-0.0476	0.3714	0.0661	-0.0585	0.2587	0.0946	0.5252	72.9692	-21.0003	71.8312
18	1.1381	0.2458	-0.126	1.8857	-0.0276	0.9023	-0.0309	-0.0883	-0.036	0.1438	-0.001	-0.0996	0.1311	0.0547	0.0042	0.1559	0.0004	0.0009	0.1395	-0.0052	0.1179	65.2048	2.9548	65.7232
19	1.085	-0.4642	-0.2983	2.5587	0.735	1.0928	-0.0881	-0.0995	0.0996	0.024	0.0978	-0.1385	0.0577	0.0131	-0.0099	0.1029	-0.0154	-0.0321	0.1225	-0.0178	0.1089	62.4349	11.5934	64.6273
20	3.6065	0.4161	2.0427	0.3905	0.1856	2.0601	-0.1429	0.2191	0.5488	-0.0501	-0.1188	-0.0575	-0.1348	0.0851	0.2103	0.1716	0.0272	0.0039	0.1182	0.0129	0.2665	43.3279	27.3044	56.9689
21	2.8414	0.7133	3.3712	3.5751	1.5422	5.0663	0.0339	0.3315	0.6379	-0.2758	-0.1849	-0.1847	-0.1939	0.2512	0.1442	0.1643	0.0258	0.0392	0.1612	0.0207	0.2482	30.2957	32.0139	51.1531
22	0.4089	0.3563	-0.4315	1.238	0.0232	1.7805	0.0635	-0.0659	0.4817	0.0197	-0.0726	0.1571	-0.2938	-0.1169	0.049	0.1558	0.0023	-0.0222	0.1433	-0.0522	0.3286	49.1626	31.0412	67.3208
23	3.2849	2.1697	-1.9151	1.6027	-1.6605	1.814	-0.4401	0.2522	-0.1131	-1.0118	0.5168	0.3515	0.3868	-0.428	-0.133	0.3624	-0.0725	-0.1462	0.2813	0.0537	0.2722	42.5393	-5.532	63.9357

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resseq 8:198)
2	X-RAY DIFFRACTION	2	chain 'A' and (resseq 199:230)
3	X-RAY DIFFRACTION	3	chain 'A' and (resseq 231:393)
4	X-RAY DIFFRACTION	4	chain 'B' and (resseq 8:197)
5	X-RAY DIFFRACTION	5	chain 'B' and (resseq 198:223)
6	X-RAY DIFFRACTION	6	chain 'B' and (resseq 224:260)
7	X-RAY DIFFRACTION	7	chain 'B' and (resseq 261:393)
8	X-RAY DIFFRACTION	8	chain 'C' and (resseq 1:32)
9	X-RAY DIFFRACTION	9	chain 'C' and (resseq 33:51)
10	X-RAY DIFFRACTION	10	chain 'C' and (resseq 52:106)
11	X-RAY DIFFRACTION	11	chain 'C' and (resseq 107:161)
12	X-RAY DIFFRACTION	12	chain 'C' and (resseq 162:186)
13	X-RAY DIFFRACTION	13	chain 'C' and (resseq 187:204)
14	X-RAY DIFFRACTION	14	chain 'C' and (resseq 205:225)
15	X-RAY DIFFRACTION	15	chain 'C' and (resseq 226:259)
16	X-RAY DIFFRACTION	16	chain 'C' and (resseq 260:280)
17	X-RAY DIFFRACTION	17	chain 'D' and (resseq 2:32)
18	X-RAY DIFFRACTION	18	chain 'D' and (resseq 33:106)
19	X-RAY DIFFRACTION	19	chain 'D' and (resseq 107:161)
20	X-RAY DIFFRACTION	20	chain 'D' and (resseq 162:204)
21	X-RAY DIFFRACTION	21	chain 'D' and (resseq 205:225)
22	X-RAY DIFFRACTION	22	chain 'D' and (resseq 226:259)
23	X-RAY DIFFRACTION	23	chain 'D' and (resseq 260:279)

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