PDB-5y9c: Crystal structure of HPV58 pentamer in complex with the Fab fragm...

ID or keywords:

Entry

Database: PDB / ID: 5y9c

Title

Crystal structure of HPV58 pentamer in complex with the Fab fragment of antibody A12A3

Components

Major capsid protein L1
heavy chain of Fab fragment of antibody A12A3
light chain of Fab fragment of antibody A12A3

Keywords

STRUCTURAL PROTEIN/IMMUNE SYSTEM /

capsid protein /

STRUCTURAL PROTEIN-IMMUNE SYSTEM complex

Function / homology

Function and homology information

T=7 icosahedral viral capsid / endocytosis involved in viral entry into host cell / host cell nucleus / structural molecule activity / virion attachment to host cell
Similarity search - Function

Biological species

Human papillomavirus type 58

Mus musculus (house mouse)

Method

X-RAY DIFFRACTION /

SYNCHROTRON / Resolution: 3.443 Å

Authors

Li, S.W. / Li, Z.H.

Funding support

China, 4items

Organization	Grant number	Country
National Natural Science Foundation of China	31670935	China
National Natural Science Foundation of China	81671645	China
National Natural Science Foundation of China	81571996	China
Natural Science Foundation of Fujian Province	2015YZ0002	China

Citation

Journal: mBio / Year: 2017
Title: Crystal Structures of Two Immune Complexes Identify Determinants for Viral Infectivity and Type-Specific Neutralization of Human Papillomavirus.
Authors: Zhihai Li / Daning Wang / Ying Gu / Shuo Song / Maozhou He / Jingjie Shi / Xinlin Liu / Shuangping Wei / Jinjin Li / Hai Yu / Qingbing Zheng / Xiaodong Yan / Timothy S Baker / Jun Zhang / ...
Abstract: Persistent, high-risk human papillomavirus (HPV) infection is the primary cause of cervical cancer. Neutralizing antibodies elicited by L1-only virus-like particles (VLPs) can block HPV infection; ...Persistent, high-risk human papillomavirus (HPV) infection is the primary cause of cervical cancer. Neutralizing antibodies elicited by L1-only virus-like particles (VLPs) can block HPV infection; however, the lack of high-resolution structures has limited our understanding of the mode of virus infection and the requirement for type specificity at the molecular level. Here, we describe two antibodies, A12A3 and 28F10, that specifically bind to and neutralize HPV58 and HPV59, respectively, through two distinct binding stoichiometries. We show that the epitopes of A12A3 are clustered in the DE loops of two adjacent HPV58 L1 monomers, whereas 28F10 recognizes the HPV59 FG loop of a single monomer. Via structure-based mutagenesis and analysis of antibody binding, we further identified the residues HPV58 D154, S168, and N170 and HPV59 M267, Q270, E273, Y276, K278, and R283, which play critical roles in virus infection. By substituting these strategic epitope residues into other HPV genotypes, we could then redirect the type-specific binding of the antibodies to these genotypes, thus highlighting the importance of these specific residues, HPV58 R161, S168, and N308 and HPV59 Q270, E273, and D281. Overall, our findings provide molecular insights into potential structural determinants of HPV required for infectivity and type specificity. High-risk human papillomaviruses (HPVs) are considered the major causative pathogens of cancers that affect epithelial mucosa, such as cervical cancer. However, because of the lack of high-resolution structural information on the sites of neutralization, we have yet to determine the precise mode of HPV infection and how different types of HPV cause infection. Our crystal structures in this study have uncovered discrete binding stoichiometries for two different antibodies. We show that one A12A3 Fab binds to the center of one HPV58 pentamer, whereas five 28F10 Fabs bind along the top fringe of one HPV59 pentamer. Furthermore, through targeted epitope analysis, we show that 6 to 7 discontinuous residues of the L1 major capsid protein of HPV are determinants, at least in part, for virus infection and type specificity. This knowledge will help us to unravel the process of HPV infection and can potentially be used to drive the development of therapeutics that target neutralization-sensitive sites.

History

Deposition	Aug 24, 2017	Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0	Oct 25, 2017	Provider: repository / Type: Initial release

Structure viewer	Molecule: MolmilJmol/JSmol

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Download

PDBx/mmCIF format	5y9c.cif.gz	998.5 KB	Display	PDBx/mmCIF format
PDB format	pdb5y9c.ent.gz	861.6 KB	Display	PDB format
PDBx/mmJSON format	5y9c.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/y9/5y9c ftp://data.pdbj.org/pub/pdb/validation_reports/y9/5y9c	HTTPS FTP

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Related structure data

Related structure data	6809C 6814C 5y9eC 5y9fC C: citing same article (ref.)
Similar structure data	6wsl-d 3x0y-d 6dvc-d 6a70-d 3x0x-d 6vtt-d 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	#221 - May 2018 Human Papillomavirus and Vaccines similarity (4) #21 - Sep 2001 Antibodies similarity (1) #256 - Apr 2021 SARS-CoV-2 Spike and Antibodies similarity (1) #47 - Nov 2003 Simian Virus 40 similarity (1) #200 - Aug 2016 Quasisymmetry in Icosahedral Viruses similarity (2)

Deposited unit

A: Major capsid protein L1

B: Major capsid protein L1

C: Major capsid protein L1

D: Major capsid protein L1

E: Major capsid protein L1

H: heavy chain of Fab fragment of antibody A12A3

L: light chain of Fab fragment of antibody A12A3

323 kDa, 7 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author

Unit cell

Length a, b, c (Å)	121.571, 102.600, 138.032
Angle α, β, γ (deg.)	90.00, 114.52, 90.00
Int Tables number	4
Space group name H-M	P12₁1

#1: Protein	Major capsid protein L1 Mass: 55250.492 Da / Num. of mol.: 5 / Fragment: UNP RESIDUES 36-524 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Human papillomavirus type 58 / Gene: L1 / Production host: Escherichia coli (E. coli) / References: UniProt: P26535
#2: Antibody	heavy chain of Fab fragment of antibody A12A3 Mass: 23374.998 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)
#3: Antibody	light chain of Fab fragment of antibody A12A3 Mass: 23729.375 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Mus musculus (house mouse)

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.42 Å³/Da / Density % sol: 49.2 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 8 Details: 0.2 M lithium chloride, 0.1 M Tris pH 8.0, 14% (w/v) PEG 3350

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Data collection

Diffraction	Mean temperature: 80 K
Diffraction source	Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.9795 Å
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 10, 2012
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9795 Å / Relative weight: 1
Reflection	Resolution: 3.45→50 Å / Num. obs: 41030 / % possible obs: 99.9 % / Redundancy: 6.2 % / Net I/σ(I): 10.4

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Processing

Software

Name	Version	Classification
PHENIX	(1.11.1_2575)	refinement
HKL-2000		data scaling
PHASER		phasing

Refinement

Resolution: 3.443→47.861 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.37 / Phase error: 26.58 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.2492	2024	4.94 %
R_work	0.2023	-	-
obs	0.2046	40995	99.51 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 3.443→47.861 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	19789	0	0	0	19789

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.002	20307
X-RAY DIFFRACTION	f_angle_d	0.507	27566
X-RAY DIFFRACTION	f_dihedral_angle_d	11.589	12022
X-RAY DIFFRACTION	f_chiral_restr	0.042	2956
X-RAY DIFFRACTION	f_plane_restr	0.004	3585

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 (%)
3.4425-3.5286	0.3149	127	0.287	2662	X-RAY DIFFRACTION	95
3.5286-3.6239	0.3601	129	0.2702	2777	X-RAY DIFFRACTION	100
3.6239-3.7305	0.3137	144	0.26	2767	X-RAY DIFFRACTION	100
3.7305-3.8509	0.2795	144	0.2454	2781	X-RAY DIFFRACTION	100
3.8509-3.9885	0.2853	138	0.2386	2780	X-RAY DIFFRACTION	100
3.9885-4.1481	0.2771	153	0.2343	2774	X-RAY DIFFRACTION	100
4.1481-4.3367	0.2571	169	0.2007	2772	X-RAY DIFFRACTION	100
4.3367-4.5652	0.2316	160	0.1907	2760	X-RAY DIFFRACTION	100
4.5652-4.851	0.1921	148	0.1667	2794	X-RAY DIFFRACTION	100
4.851-5.2251	0.2017	145	0.1702	2783	X-RAY DIFFRACTION	100
5.2251-5.7502	0.2222	136	0.1835	2817	X-RAY DIFFRACTION	100
5.7502-6.5804	0.2496	149	0.2073	2787	X-RAY DIFFRACTION	100
6.5804-8.2836	0.2633	152	0.1948	2818	X-RAY DIFFRACTION	100
8.2836-47.8653	0.2169	130	0.1609	2899	X-RAY DIFFRACTION	100

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	0.1847	-0.5067	0.0273	0.7755	0.0707	-0.119	0.215	-0.1062	-0.0797	0.2725	-0.0816	-0.0618	-0.0305	0.0871	0	0.5822	0.0095	-0.0634	0.4531	0.0563	0.5365	11.978	-4.1941	64.5621
2	0.2406	0.1117	0.2922	0.0865	0.1167	0.2541	0.0365	-0.1627	-0.1883	0.7496	-0.3861	-0.2502	-0.0749	-0.2009	-0.0017	0.7467	-0.251	0.0426	0.6128	0.0659	0.5927	-2.2106	-4.87	79.4069
3	0.4837	0.1967	0.5517	0.5252	0.4527	0.4961	-0.0159	-0.0449	-0.1817	-0.006	-0.0101	0.0325	0.1349	0.277	-0	0.5447	0.0474	0.0197	0.449	-0.0089	0.623	13.5914	-1.205	41.923
4	0.4219	0.5951	-0.2704	0.5612	0.6055	0.8803	0.0805	-0.3058	0.1493	0.1397	-0.2203	0.0966	0.3005	0.2997	-0.0007	0.4884	-0.0447	0.033	0.6095	0.1549	0.6753	6.4067	-3.5636	69.2207
5	0.4059	0.0014	0.4056	-0.2521	0.138	0.5697	0.0112	-0.1582	-0.1375	0.0514	-0.0061	-0.1098	-0.3055	-0.0483	0.0118	0.7223	-0.1199	0.0424	0.4549	-0.1118	0.5094	17.588	36.8239	68.2463
6	0.589	0.209	0.3343	1.0786	-0.1055	0.5615	-0.2764	-0.3264	-0.2922	0.4377	0.0408	0.2977	-0.7382	0.5081	0.3746	0.51	-0.1446	-0.0609	0.406	-0.234	0.372	11.0873	36.6158	69.3663
7	0.1755	-0.0565	0.0799	0.0111	0.003	-0.036	0.0768	-0.2147	0.1545	-0.3169	-0.0754	-0.1804	-0.1336	0.4964	0	0.6072	-0.0222	0.0733	0.7797	-0.0269	0.6751	27.7628	17.9253	41.1908
8	0.0669	0.0968	-0.1212	0.2173	-0.0073	0.0464	-0.4904	0.1891	-0.1062	-0.4559	-0.0957	0.0311	0.342	0.5868	-0.0009	0.7506	0.136	0.0477	0.9391	0.1111	0.7623	31.3815	10.4821	64.6555
9	-0.0808	0.5695	-0.7653	0.3833	-0.5186	0.6518	0.0397	-0.2602	-0.1752	0.024	-0.0598	0.1048	-0.111	0.4156	-0	0.443	0.0049	-0.0237	0.6922	-0.0323	0.5605	25.15	15.3544	53.3459
10	0.0173	-0.0099	0.0572	0.1105	0.0801	0.0432	0.033	-0.0492	0.2893	-0.0656	0.0932	-0.1932	0.3619	-0.4672	0	0.6834	-0.0638	0.0575	0.5446	-0.0419	0.7469	3.5983	29.0329	62.694
11	0.1024	-0.4926	-0.3805	0.6476	0.0087	-0.0984	0.0345	-0.0482	0.0027	0.1721	-0.2176	-0.0539	-0.2734	0.382	-0.0311	0.6752	-0.1935	0.0582	0.6803	-0.0951	0.4936	20.1513	40.1717	54.1637
12	0.2535	-0.1919	-0.3937	0.041	0.0214	0.5544	0.2035	-0.4224	0.0099	0.1798	0.0085	0.2686	-0.6691	0.3786	0.0186	0.7725	-0.0745	0.1127	0.63	-0.1818	0.6429	9.3106	36.5379	78.9926
13	0.4073	0.0204	0.1774	0.0908	-0.0089	0.2563	0.1216	-0.0148	-0.4493	-0.4968	-0.1241	0.2013	0.0103	-0.1261	-0.1565	0.6822	-0.2968	-0.0377	0.5125	-0.177	1.0245	-13.1512	-11.1278	31.7606
14	0.4689	0.1231	0.2005	0.0331	0.0668	0.2098	-0.0043	-0.2375	-0.3526	-0.1256	0.2099	0.4463	0.4401	-0.2628	0.3174	0.7554	-0.5053	-0.074	0.9472	0.0496	1.3738	-29.7964	-13.6987	43.4128
15	0.2	0.3417	0.1626	0.7993	0.2671	0.1657	-0.0874	0.8086	-0.2349	-0.5574	-0.413	-0.1821	0.0311	-0.3752	-0.2664	0.4281	-0.1897	-0.1721	0.4797	-0.3494	0.628	4.8824	6.8316	19.1711
16	0.2162	-0.1187	-0.0618	0.2432	0.0286	-0.009	-0.0188	0.6317	-0.548	-0.1364	-0.2692	-0.0324	0.3397	-0.383	-0.4645	0.4535	-0.4546	-0.1721	0.6246	-0.5756	0.5219	-8.6741	3.2987	12.8567
17	0.3541	-0.4738	0.1227	0.4785	-0.1022	0.0352	-0.1078	0.191	-0.2417	-0.1393	0.2391	0.1261	0.1945	-0.0925	0	0.6609	-0.1491	-0.0402	0.8523	-0.159	0.6971	-5.4685	6.6857	19.412
18	0.6766	-0.4941	0.3745	0.48	0.1023	0.4206	-0.0272	0.219	-0.4102	-0.2251	-0.0697	0.0943	0.1818	-0.3756	-0	0.5472	-0.1717	-0.0805	0.6395	-0.1102	0.5849	-6.5076	8.2503	26.7183
19	0.1501	-0.0967	-0.2354	0.2589	-0.4952	0.93	0.2909	0.3337	0.095	-0.14	-0.0889	0.0166	0.3451	-0.3362	0.0001	0.599	-0.1425	0.0192	0.6863	-0.1794	0.9283	-9.9167	-11.0075	31.186
20	0.0077	0.0209	0.0219	0.1751	-0.0526	0.0732	0.1502	-0.0909	-0.2688	-0.0995	0.13	0.2024	-0.0151	-0.3926	0.0001	0.8137	-0.1527	0.1123	0.8343	-0.0712	1.05	-17.3427	-10.9974	45.3008
21	0.0421	-0.338	0.2473	0.0396	-0.2855	0.4389	0.0443	0.1573	0.0854	0.0396	0.1311	0.1526	0.3592	-0.228	0.188	0.5116	-0.0463	-0.2311	1.0367	0.0403	0.664	-23.0691	26.008	15.1368
22	0.036	0.3645	0.1235	0.3753	0.2424	0.3982	0.1286	0.4772	-0.0928	-0.3234	-0.0563	0.162	-0.2562	-0.2882	-0.0184	0.503	0.1058	-0.1957	0.8557	0.0584	0.7163	-10.1131	27.6025	19.1322
23	0.3436	0.0015	0.1737	0.4022	-0.0079	0.225	0.1373	0.2329	-0.1853	-0.2368	-0.0419	0.0709	-0.1577	-0.0486	0	0.6861	0.0674	-0.0756	0.876	0.0604	0.5662	-0.2452	37.4202	19.2565
24	0.114	0.0573	0.0363	0.1806	-0.281	0.5221	0.0472	-0.063	-0.1023	0.2302	-0.1464	0.0885	0.0078	-1.1991	-0.0656	0.6293	-0.0033	-0.1529	0.8347	-0.0151	0.7222	-19.7858	25.5482	31.8412
25	0.0196	0.11	-0.0517	0.1636	0.0884	-0.0855	-0.3038	0.4398	0.2749	-0.0611	0.3605	-0.1728	0.2585	-0.221	0	0.6512	0.0221	-0.0986	1.0814	-0.0948	0.7267	-11.8283	16.6618	13.7781
26	0.5047	0.491	-0.348	0.2368	-0.3077	0.348	0.1564	0.2354	-0.0324	-0.4041	-0.1601	0.3914	0.0438	-0.9298	-0.1343	0.6421	0.1307	-0.2315	1.4243	0.0321	1.0085	-34.7247	29.6658	21.2957
27	-0.0012	0.0051	-0.1469	0.4374	0.0497	0.2916	0.1066	0.0472	0.095	-0.0656	-0.0774	-0.0709	-0.2297	0.1897	-0	0.9446	0.2676	0.0231	0.523	0.0642	0.7178	-4.076	55.6738	37.7782
28	0.0534	0.0151	0.4059	0.4204	-0.2732	0.8405	-0.2985	-0.3596	-0.1733	0.1343	0.1782	0.1698	-0.3513	0.229	-0.0004	0.8532	0.1341	0.0404	0.5245	-0.008	0.6979	4.8843	45.3767	37.5662
29	0.7288	0.2715	0.5595	0.2392	0.3054	0.7829	0.1194	0.2277	0.0345	0.0104	0.2434	0.3435	-0.711	0.6174	0.0864	0.9681	-0.0031	0.1499	0.4042	-0.0004	0.6272	13.5279	47.4461	42.8863
30	0.1251	0.0585	-0.315	0.4184	-0.1445	0.7793	-0.0687	-0.1753	-0.2005	-0.0635	0.0544	0.086	-0.5612	0.3743	0.0009	0.6243	-0.1318	-0.0025	0.5252	-0.0383	0.6515	20.0233	39.6102	42.3731
31	0.1097	0.1015	0.1744	0.112	0.0239	0.2021	-0.2405	0.0071	0.0259	0.5152	0.2723	0.1339	-0.0351	-0.3594	0.0058	0.8398	0.1746	0.0465	0.6626	-0.1315	0.8664	-8.3117	41.2293	45.8168
32	0.5647	0.0945	0.1034	-0.1988	-0.0363	0.2634	0.1991	0.28	0.1624	-0.2551	-0.1184	0.1265	-0.937	-0.1937	-0.003	0.8768	0.2148	0.1289	0.4607	0.0019	0.7334	-6.8199	53.238	37.0707
33	0.1979	-0.0913	0.0953	0.4391	-0.1328	0.1755	0.0445	-0.0442	0.004	-0.0386	-0.1629	-0.0713	-0.0573	0.278	0	0.9591	0.024	0.0423	0.9451	-0.0841	0.7112	38.3936	16.3269	6.5654
34	0.0595	-0.0227	-0.0531	-0.0017	-0.0003	0.0266	-0.3428	0.0562	-0.5244	0.0784	-0.0388	-0.0803	0.226	0.0672	-0	1.0297	0.1078	0.0926	1.1643	-0.1006	1.3465	32.6331	12.139	5.5967
35	0.2871	0.0547	-0.3671	0.0457	-0.0972	0.1528	-0.2757	0.2267	-0.1207	-0.014	0.1154	0.282	0.3841	0.3351	0	1.0864	0.0687	0.0404	1.2139	-0.1263	0.9673	38.2243	19.1731	4.6198
36	0.0681	0.0839	0.1012	0.0539	0.0041	0.0459	-0.3816	-0.5941	0.6884	0.2626	0.0651	-0.2489	-0.534	0.1409	0	1.2113	0.1369	-0.0226	1.4221	-0.0775	1.6043	69.8105	12.1519	-4.6088
37	0.0091	0.0271	0.0003	0.0262	0.0731	0.059	0.2791	-0.8457	-0.4924	0.0942	0.0492	0.2927	-0.144	-0.1519	0	1.7544	0.0271	0.0459	1.8077	0.2104	1.7809	67.4132	13.0173	-1.8514
38	0.0314	-0.0243	-0.0258	0.0156	0.0338	0.011	-0.3479	0.4881	0.0125	-0.3832	-0.0142	0.5448	0.9501	-0.0771	-0.0001	1.6454	0.2689	0.0717	1.7784	-0.0836	1.362	64.8016	16.1437	-6.5899
39	0.0177	0.0325	-0.0246	-0.0258	0.0011	0.0568	-0.2185	-0.4238	0.323	0.331	-0.017	0.3768	0.0393	0.467	-0	1.8291	-0.0773	-0.4886	1.6407	0.075	2.057	76.6514	19.4341	-1.5599
40	0.0147	0.0159	0.0091	-0.0054	0.008	0.047	-0.0273	0.1016	-0.3151	0.9717	0.4289	0.7613	0.5211	0.2325	0	1.0724	0.066	-0.0501	1.767	0.3182	1.1866	70.2321	9.8212	4.9123
41	0.0653	-0.0361	0.0753	-0.0218	-0.0165	0.036	0.2749	0.2349	-0.1926	-0.6441	-0.4371	-0.3464	-0.1875	-0.562	0.0001	0.8734	-0.0778	0.0423	1.1593	0.073	0.8114	41.5971	34.3826	-13.305
42	0.0599	0.0135	-0.0641	0.0238	-0.0475	0.0938	0.3001	0.264	0.0359	-0.6386	0.102	0.0866	-0.1785	-0.5582	0.0001	0.8808	-0.0412	0.0665	1.1833	-0.0021	0.729	33.0461	32.9498	-4.8848
43	0.0343	-0.0105	-0.0383	0.008	-0.0938	0.2568	-0.1414	-0.3819	0.0418	-0.2184	-0.2435	0.2614	0.0678	0.418	0	0.8596	-0.1238	-0.0479	1.1189	-0.0979	0.9115	42.4856	36.4377	1.4331
44	0.0292	0.0345	-0.0565	0.0588	-0.0417	0.0643	0.3782	0.2032	-0.1177	-0.11	0.1098	0.4681	0.2181	-0.4953	0.0002	1.3918	-0.0557	0.1452	1.279	-0.111	0.7526	36.1741	39.5847	-8.6487
45	-0.0127	0.0121	0.0092	0.3701	-0.0694	0.026	0.3775	0.6043	0.3438	0.1837	-0.033	0.3819	0.1221	0.1366	0	1.0953	-0.1349	0.0633	1.2038	-0.1132	0.6737	41.505	31.7284	-5.1276
46	0.0564	-0.0386	0.0401	0.0043	0.0147	0.0576	0.0725	0.3789	0.1526	0.3373	-0.319	0.2955	0.5908	0.1353	-0.0002	1.1468	-0.1288	0.3392	1.2846	-0.0846	1.0886	61.1865	34.6896	-14.2298
47	0.3941	-0.0178	0.061	0.1134	0.009	-0.0057	0.2701	-0.1405	0.4069	0.2	0.4774	-0.8207	0.2513	0.2784	0.0167	1.3724	0.4089	-0.2168	1.4236	-0.2831	1.1047	73.1565	15.8821	-16.5894
48	0.0797	-0.0981	0.0828	0.0774	-0.0313	-0.0343	0.2319	0.2862	-0.9787	-0.2585	-0.3598	0.7161	-0.7433	0.4002	-0.0003	1.2424	0.1818	0.098	1.7132	-0.331	1.0763	69.7057	17.1187	-14.5367
49	1.5337	1.1014	0.6399	0.7558	0.4165	0.2764	-0.6174	-0.1735	0.4409	-0.2512	-0.0482	0.4966	-0.2784	0.5353	-0.0363	0.9796	0.1328	0.1754	1.5101	-0.2151	0.723	75.3332	24.2976	-22.8277

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 20 through 83 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 84 through 110 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 111 through 355 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 356 through 473 )
5	X-RAY DIFFRACTION	5	chain 'B' and (resid 20 through 83 )
6	X-RAY DIFFRACTION	6	chain 'B' and (resid 84 through 126 )
7	X-RAY DIFFRACTION	7	chain 'B' and (resid 127 through 161 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 162 through 187 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 188 through 296 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 297 through 324 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 325 through 381 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 382 through 473 )
13	X-RAY DIFFRACTION	13	chain 'C' and (resid 20 through 83 )
14	X-RAY DIFFRACTION	14	chain 'C' and (resid 84 through 110 )SOU 2137 O SER
15	X-RAY DIFFRACTION	15	chain 'C' and (resid 111 through 172 )
16	X-RAY DIFFRACTION	16	chain 'C' and (resid 173 through 209 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 210 through 272 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 273 through 338 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 339 through 442 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 443 through 473 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 20 through 83 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 84 through 146 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 147 through 296 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 297 through 324 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 325 through 381 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 382 through 473 )
27	X-RAY DIFFRACTION	27	chain 'E' and (resid 20 through 83 )
28	X-RAY DIFFRACTION	28	chain 'E' and (resid 84 through 146 )
29	X-RAY DIFFRACTION	29	chain 'E' and (resid 147 through 209 )
30	X-RAY DIFFRACTION	30	chain 'E' and (resid 210 through 296 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 297 through 324 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 325 through 473 )
33	X-RAY DIFFRACTION	33	chain 'H' and (resid 1 through 60 )
34	X-RAY DIFFRACTION	34	chain 'H' and (resid 61 through 77 )
35	X-RAY DIFFRACTION	35	chain 'H' and (resid 78 through 113 )
36	X-RAY DIFFRACTION	36	chain 'H' and (resid 114 through 141 )
37	X-RAY DIFFRACTION	37	chain 'H' and (resid 142 through 160 )
38	X-RAY DIFFRACTION	38	chain 'H' and (resid 161 through 179 )
39	X-RAY DIFFRACTION	39	chain 'H' and (resid 180 through 199 )
40	X-RAY DIFFRACTION	40	chain 'H' and (resid 200 through 216 )
41	X-RAY DIFFRACTION	41	chain 'L' and (resid 1 through 25 )
42	X-RAY DIFFRACTION	42	chain 'L' and (resid 26 through 38 )
43	X-RAY DIFFRACTION	43	chain 'L' and (resid 39 through 61 )
44	X-RAY DIFFRACTION	44	chain 'L' and (resid 62 through 75 )
45	X-RAY DIFFRACTION	45	chain 'L' and (resid 76 through 101 )
46	X-RAY DIFFRACTION	46	chain 'L' and (resid 102 through 112 )
47	X-RAY DIFFRACTION	47	chain 'L' and (resid 113 through 157 )
48	X-RAY DIFFRACTION	48	chain 'L' and (resid 158 through 188 )
49	X-RAY DIFFRACTION	49	chain 'L' and (resid 193 through 209 )

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