PDB-5y9e: Crystal structure of HPV58 pentamer

ID or keywords:

Entry

Database: PDB / ID: 5y9e

Title

Crystal structure of HPV58 pentamer

Components

Major capsid protein L1

Keywords

STRUCTURAL PROTEIN / capsid protein / pentamer

Function / homology

Function and homology information

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

Biological species

Human papillomavirus type 58

Method

X-RAY DIFFRACTION /

SYNCHROTRON / Resolution: 2.042 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
Revision 1.1	Mar 27, 2024	Group: Data collection / Database references / Derived calculations Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_struct_conn_angle / struct_conn Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_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 / _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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Validation report

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Data in XML	5y9e_validation.xml.gz	82.8 KB	Display
Data in CIF	5y9e_validation.cif.gz	116.2 KB	Display
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Related structure data

Related structure data	6809C 6814C 5y9cC 5y9fC C: citing same article (ref.)
Similar structure data	6igc-8 6igc-4 6igc-1 6igc-7 6igc-2 6igc-6 6ige-2 6igd-2 6ige-1 6igf-2 6igc-3 6igd-1 2r5j-1 6igf-1 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) #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

hetero molecules

279 kDa, 5 polymers
Search similar-shape structures of this assembly by Omokage search (details)

1

Idetical with deposited unit
defined by author&software

Unit cell

Length a, b, c (Å)	187.213, 101.804, 136.195
Angle α, β, γ (deg.)	90.00, 95.68, 90.00
Int Tables number	5
Space group name H-M	C121

#1: Protein	Major capsid protein L1 Mass: 55250.492 Da / Num. of mol.: 5 / Fragment: UNP RESIDUES 36-524 / Mutation: C202S 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: Chemical	ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL Mass: 92.094 Da / Num. of mol.: 20 / Source method: obtained synthetically / Formula: C₃H₈O₃
#3: Chemical	... ChemComp-MG / MAGNESIUM ION Mass: 24.305 Da / Num. of mol.: 29 / Source method: obtained synthetically / Formula: Mg
#4: Water	ChemComp-HOH / water Mass: 18.015 Da / Num. of mol.: 1101 / 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: 2.34 Å³/Da / Density % sol: 47.38 %
Crystal grow	Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: 0.2 M magnesium formate, 14.5% (w/v) PEG 3350

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Data collection

Diffraction	Mean temperature: 80 K
Diffraction source	Source: SYNCHROTRON / Site: SSRF / Beamline: BL17U1 / Wavelength: 0.9792 Å
Detector	Type: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 10, 2014
Radiation	Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.9792 Å / Relative weight: 1
Reflection	Resolution: 2.04→30 Å / Num. obs: 159674 / % possible obs: 99.2 % / Redundancy: 7 % / Net I/σ(I): 19.6

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Processing

Software

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

Refinement

Resolution: 2.042→29.781 Å / SU ML: 0.2 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 24.24 / Stereochemistry target values: ML

	R_factor	Num. reflection	% reflection
R_free	0.1983	12229	7.67 %
R_work	0.1684	-	-
obs	0.1707	159523	98.92 %

Solvent computation

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

Refinement step

Cycle: LAST / Resolution: 2.042→29.781 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	16623	0	149	1101	17873

Refine LS restraints

Refine-ID	Type	Dev ideal	Number
X-RAY DIFFRACTION	f_bond_d	0.002	17174
X-RAY DIFFRACTION	f_angle_d	0.525	23269
X-RAY DIFFRACTION	f_dihedral_angle_d	12.654	10161
X-RAY DIFFRACTION	f_chiral_restr	0.044	2468
X-RAY DIFFRACTION	f_plane_restr	0.003	3031

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 (%)
2.0416-2.0648	0.3203	343	0.2849	4062	X-RAY DIFFRACTION	83
2.0648-2.089	0.29	405	0.2631	4773	X-RAY DIFFRACTION	97
2.089-2.1145	0.3026	410	0.2537	4801	X-RAY DIFFRACTION	98
2.1145-2.1413	0.2667	375	0.2366	4838	X-RAY DIFFRACTION	98
2.1413-2.1694	0.2614	404	0.2257	4955	X-RAY DIFFRACTION	99
2.1694-2.1991	0.2442	410	0.2158	4840	X-RAY DIFFRACTION	99
2.1991-2.2306	0.2645	398	0.2116	4902	X-RAY DIFFRACTION	99
2.2306-2.2638	0.263	395	0.2041	4972	X-RAY DIFFRACTION	99
2.2638-2.2992	0.2383	383	0.1965	4877	X-RAY DIFFRACTION	100
2.2992-2.3369	0.2229	411	0.1861	4917	X-RAY DIFFRACTION	100
2.3369-2.3772	0.2387	394	0.1906	4982	X-RAY DIFFRACTION	100
2.3772-2.4204	0.2429	446	0.1883	4921	X-RAY DIFFRACTION	100
2.4204-2.4669	0.2585	406	0.1868	4950	X-RAY DIFFRACTION	100
2.4669-2.5172	0.217	413	0.1733	4881	X-RAY DIFFRACTION	100
2.5172-2.5719	0.2108	407	0.169	4984	X-RAY DIFFRACTION	100
2.5719-2.6317	0.2261	427	0.1708	4940	X-RAY DIFFRACTION	100
2.6317-2.6975	0.2145	380	0.1683	4963	X-RAY DIFFRACTION	100
2.6975-2.7704	0.2077	387	0.1698	5001	X-RAY DIFFRACTION	100
2.7704-2.8518	0.2193	398	0.1689	4987	X-RAY DIFFRACTION	100
2.8518-2.9438	0.2166	402	0.1772	4939	X-RAY DIFFRACTION	100
2.9438-3.0489	0.2106	427	0.165	4950	X-RAY DIFFRACTION	100
3.0489-3.1709	0.2018	429	0.1598	4948	X-RAY DIFFRACTION	100
3.1709-3.315	0.1781	435	0.1638	4960	X-RAY DIFFRACTION	100
3.315-3.4895	0.1881	384	0.1586	4963	X-RAY DIFFRACTION	100
3.4895-3.7078	0.1741	410	0.1532	4991	X-RAY DIFFRACTION	100
3.7078-3.9934	0.159	465	0.1467	4925	X-RAY DIFFRACTION	100
3.9934-4.3942	0.1523	403	0.1381	5008	X-RAY DIFFRACTION	100
4.3942-5.0274	0.1488	447	0.1212	4969	X-RAY DIFFRACTION	100
5.0274-6.324	0.1706	416	0.1501	5006	X-RAY DIFFRACTION	100
6.324-29.7842	0.2107	419	0.1916	5089	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	1.7559	0.9132	0.1873	0.8041	0.3275	0.6436	0.0824	0.0709	-0.254	0.0553	-0.0736	0.0288	0.1866	-0.2673	-0.0628	0.329	-0.0982	-0.0054	0.4717	-0.0332	0.3518	35.6332	-3.1961	44.6189
2	0.6695	0.2868	-0.3683	0.1533	0.0866	0.6174	0.1175	-0.1317	-0.0708	-0.009	-0.0811	-0.0587	0.0828	0.2293	-0.0184	0.273	-0.0139	-0.0092	0.4002	0.0196	0.2993	74.9851	8.9329	57.4867
3	1.2525	0.0541	0.0591	0.0831	0.0633	0.6005	0.0722	0.0997	-0.2917	-0.0257	-0.0148	-0.0309	0.1855	-0.0523	-0.0682	0.3318	-0.0391	-0.0408	0.3321	-0.0237	0.3466	61.7888	-2.0037	45.3512
4	1.668	-0.1133	0.019	0.0812	-0.2864	0.536	0.0572	0.2075	-0.0758	-0.0334	-0.0119	-0.0051	0.0694	-0.0657	-0.0397	0.3061	-0.0175	-0.0196	0.3682	-0.0647	0.3206	70.6432	8.6936	44.7825
5	1.6239	1.4436	0.7698	2.2208	1.5535	1.4666	-0.0595	0.5203	-0.0345	-0.0223	0.1043	0.0574	-0.1342	-0.2154	-0.0539	0.2701	-0.074	-0.0284	0.5066	-0.0349	0.3219	41.1899	-0.6663	36.6154
6	1.2336	0.493	0.6189	0.7411	0.578	1.4713	-0.0407	-0.1131	0.0243	0.0369	-0.0471	0.0746	-0.0871	-0.1398	0.0729	0.2749	-0.0421	0.0134	0.4866	-0.0003	0.2913	47.1834	10.3807	61.1385
7	1.1382	0.4076	0.03	0.8055	0.6709	0.9851	-0.0005	0.2191	-0.3239	0.0263	-0.0327	0.0791	0.3094	-0.2946	0.0261	0.3517	-0.1397	-0.0153	0.5444	-0.0617	0.4265	32.0158	-6.6502	38.5085
8	1.33	0.0863	0.3485	0.6427	0.0684	0.9054	-0.1292	-0.0382	0.1744	-0.0892	0.0566	0.1568	-0.1952	-0.1985	0.0018	0.2887	0.0716	0.0068	0.5109	-0.0098	0.3922	31.659	37.4078	50.1491
9	1.0432	0.2061	0.8498	0.4311	-0.1289	0.8537	-0.0881	-0.3667	0.4031	0.0599	0.0074	0.0727	-0.155	-0.4473	0.0928	0.3256	0.0938	0.0418	0.566	-0.1018	0.4308	35.1793	39.1009	59.3238
10	0.2253	0.0305	-0.1488	0.3583	0.0595	0.2496	0.0436	0.025	0.1182	-0.0288	-0.0241	0.2134	-0.1539	-0.26	-0.0029	0.3215	0.0663	-0.0014	0.5901	-0.0286	0.4751	31.448	37.458	48.0871
11	0.3453	-0.106	-0.3312	0.5937	0.2666	0.283	0.0987	-0.3951	0.0585	0.0798	-0.0169	-0.0714	0.0583	-0.1016	-0.0635	0.2757	-0.0435	-0.0031	0.3778	0.0012	0.2883	62.2301	22.1088	61.957
12	2.096	-0.4865	0.277	1.6301	-0.0207	0.8041	0.0319	-0.3371	-0.2176	0.2051	-0.024	0.1606	0.0386	-0.2822	-0.0166	0.2927	-0.0354	0.0337	0.5555	-0.0065	0.3163	41.1656	19.9318	62.6178
13	0.8471	-0.304	0.1254	0.4346	0.0882	0.2098	0.031	-0.1441	-0.0412	0.0065	-0.0095	0.0844	0.0491	-0.1849	-0.0153	0.2861	-0.0369	0.0008	0.4768	0.0027	0.3024	51.7287	19.6768	57.2034
14	3.2299	0.4761	-0.1814	0.8047	-0.4008	0.2158	-0.0911	0.2116	-0.1912	-0.2056	0.085	0.1902	-0.0723	-0.3337	-0.0025	0.2666	0.038	0.0042	0.5914	-0.0232	0.4251	28.1502	29.7441	44.7734
15	0.7931	0.0694	0.1997	0.2937	-0.0839	0.4982	-0.0022	-0.0198	0.2168	0.0172	0.0094	0.0303	-0.1671	-0.047	-0.0076	0.3302	0.0296	0.009	0.4346	-0.0608	0.4104	50.7764	44.8856	56.6505
16	1.3746	0.538	0.2708	1.2272	-0.0768	0.1464	-0.0008	-0.2229	0.2107	0.0069	-0.0068	0.4303	-0.0284	-0.2851	0.0339	0.3049	0.1022	0.0061	0.6335	-0.0208	0.5052	21.7126	36.2382	47.0681
17	0.4838	0.0486	0.0906	0.7172	-0.0067	1.7738	0.0023	0.416	-0.2567	-0.1863	-0.0479	-0.0227	0.3068	-0.3097	0.0068	0.4237	-0.0076	-0.0018	0.6973	-0.1972	0.42	67.667	-7.7546	16.0959
18	0.4988	-0.1596	-0.3485	0.9147	-0.4649	0.5316	0.0489	0.1051	0.0431	0.1784	-0.1193	-0.1363	-0.0269	0.0885	0.0596	0.2503	-0.0021	-0.0098	0.4289	0.0273	0.263	87.6883	16.1606	46.1708
19	0.6142	0.084	0.0678	0.2839	0.0707	0.6074	0.0325	0.3097	-0.1142	-0.0564	-0.0159	-0.0413	0.0884	0.0436	-0.0146	0.2903	0.0295	-0.006	0.5216	-0.0413	0.2869	78.3808	8.1988	29.155
20	0.4115	0.3753	-0.1991	0.4362	-0.2913	1.1239	-0.0444	0.5784	-0.2267	-0.2445	-0.0249	-0.0109	0.3404	-0.2571	0.0235	0.534	0.0066	0.0069	0.8428	-0.2369	0.4816	65.6943	-7.6435	8.5202
21	1.1471	-0.0755	0.6287	0.8183	-0.1591	1.0648	0.1396	0.4058	-0.2617	-0.2442	0.0856	0.3168	-0.0373	-0.2298	-0.1268	0.4224	0.1564	0.0459	0.9772	0.1058	0.2909	71.8361	31.8836	0.7018
22	0.9546	-0.5258	0.9043	0.4644	0.1015	1.8938	0.0171	0.3509	0.1587	-0.1231	-0.0306	-0.1529	-0.3147	0.7028	0.0785	0.3766	-0.0164	0.0627	0.8171	0.1287	0.3676	91.313	31.7745	15.6935
23	0.2928	-0.3972	0.45	0.9578	-0.9746	1.3558	0.2696	0.4365	-0.0204	-0.3847	-0.0745	0.1928	0.2556	-0.0511	-0.1052	0.4919	0.1679	0.0062	1.1217	0.1189	0.3298	73.1486	31.2468	-7.9028
24	0.6833	-0.0913	-0.0765	0.7737	0.2687	0.1693	-0.0971	-0.0191	0.2203	0.0228	-0	-0.0056	0.0014	0.205	0.0935	0.2745	-0.0326	0.0156	0.4598	0.0363	0.3248	86.4907	34.5472	46.8954
25	0.4575	-0.0592	0.4146	0.51	0.069	1.1799	0.0225	0.3483	0.1374	-0.0741	-0.0381	0.0121	-0.0947	0.0522	0.0004	0.3028	-0.0107	0.0429	0.5522	0.1292	0.364	78.8676	37.5666	24.5542
26	1.8869	0.5574	1.116	0.9581	0.2288	4.3957	0.1086	0.036	0.6729	0.2245	-0.0848	-0.1712	-0.8868	0.109	-0.0379	0.6441	-0.0879	0.055	0.5434	0.1485	0.6155	84.3109	56.6756	30.8299
27	0.6498	-0.0304	-0.2153	0.1169	0.1892	0.7215	0.0287	0.2255	0.2045	-0.0769	-0.0369	0.0156	-0.1744	0.1033	0.0223	0.337	-0.013	0.0128	0.4812	0.0895	0.3615	78.2628	40.0149	32.7096
28	0.1183	-0.3465	0.2534	1.7572	-2.0151	3.1276	0.012	0.3485	0.042	-0.1284	-0.0504	0.0198	-0.05	0.0771	0.049	0.367	0.0607	0.0059	0.7739	0.095	0.3304	72.047	34.9836	8.4308
29	0.6545	-0.3389	0.6575	0.4915	-0.8008	1.756	0.0983	0.4346	0.0778	-0.0364	-0.1314	-0.0605	-0.1191	0.1779	0.0571	0.3895	0.0841	0.0444	0.7779	0.0923	0.3358	84.9511	30.8147	12.0569
30	1.0049	0.3722	-0.1529	1.8979	0.5522	2.1098	0.2131	0.3363	0.0084	-0.2066	-0.271	0.0311	0.1424	0.017	0.093	0.4222	0.1353	-0.0008	0.8665	0.0324	0.2887	73.2219	21.3841	0.8112
31	0.8463	-0.5964	0.4527	0.6922	-0.4349	0.6052	0.1093	0.2989	0.2091	-0.1254	-0.0909	-0.0008	-0.2073	-0.0303	0.0204	0.4808	0.0551	0.0215	0.4736	0.1497	0.4916	58.1988	57.8407	28.0223
32	0.7036	0.1272	-0.4599	0.8165	0.1638	0.398	0.088	-0.1608	0.1798	-0.0066	-0.0928	-0.0558	-0.0682	0.1461	-0.0032	0.3039	-0.0259	0.0287	0.3817	-0.0323	0.3618	68.691	39.029	55.7908
33	0.8481	0.0285	-0.4587	0.7791	0.3391	0.5148	-0.0116	-0.5061	0.2802	0.275	0.0705	0.1177	-0.3669	-0.439	-0.0445	0.5724	0.1338	0.0661	0.5755	-0.0817	0.6046	50.2505	55.0612	57.9094
34	0.6037	0.1178	-0.0253	0.4918	-0.0411	0.5131	0.0175	0.011	0.3197	-0.0381	-0.0467	0.0555	-0.1972	-0.1195	0.0239	0.3659	0.0462	0.012	0.3971	-0.0078	0.4516	57.3318	48.1091	48.5566
35	0.7218	-0.0137	0.1166	0.6996	-0.6026	1.6508	0.0226	-0.0415	0.1922	0.0031	-0.0216	0.0049	-0.0676	-0.2357	-0.0025	0.3	-0.0056	0.0136	0.4002	-0.0245	0.3632	61.5494	35.8214	52.4147
36	2.2438	-1.6746	0.5473	1.2607	-0.4125	0.7943	-0.0097	0.0594	-0.1087	-0.177	0.0173	0.1805	-0.1698	-0.0705	-0.0233	0.444	0.085	0.005	0.539	0.1057	0.4787	49.89	52.5769	27.6667
37	0.4727	-0.2063	-0.2106	0.2954	0.1064	0.4452	0.0688	0.3133	0.1594	-0.094	-0.0371	-0.0193	-0.1822	0.1387	-0.0453	0.3831	-0.0344	0.0038	0.4641	0.1337	0.4554	76.7866	51.1916	33.7939
38	1.6984	-0.4917	-0.1576	0.4084	-0.173	0.3077	0.1666	0.4031	0.5434	-0.1689	-0.1896	0.1114	-0.3608	-0.2048	0.0003	0.6652	0.1118	-0.0177	0.5184	0.1469	0.6323	48.9423	61.6306	21.4896

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Selection details
1	X-RAY DIFFRACTION	1	chain 'A' and (resid 20 through 110 )
2	X-RAY DIFFRACTION	2	chain 'A' and (resid 111 through 146 )
3	X-RAY DIFFRACTION	3	chain 'A' and (resid 147 through 272 )
4	X-RAY DIFFRACTION	4	chain 'A' and (resid 273 through 312 )
5	X-RAY DIFFRACTION	5	chain 'A' and (resid 313 through 338 )
6	X-RAY DIFFRACTION	6	chain 'A' and (resid 339 through 381 )
7	X-RAY DIFFRACTION	7	chain 'A' and (resid 382 through 473 )
8	X-RAY DIFFRACTION	8	chain 'B' and (resid 20 through 56 )
9	X-RAY DIFFRACTION	9	chain 'B' and (resid 57 through 83 )
10	X-RAY DIFFRACTION	10	chain 'B' and (resid 84 through 126 )
11	X-RAY DIFFRACTION	11	chain 'B' and (resid 127 through 161 )
12	X-RAY DIFFRACTION	12	chain 'B' and (resid 162 through 209 )
13	X-RAY DIFFRACTION	13	chain 'B' and (resid 210 through 312 )
14	X-RAY DIFFRACTION	14	chain 'B' and (resid 313 through 335 )
15	X-RAY DIFFRACTION	15	chain 'B' and (resid 336 through 381 )
16	X-RAY DIFFRACTION	16	chain 'B' and (resid 382 through 473 )
17	X-RAY DIFFRACTION	17	chain 'C' and (resid 20 through 110 )
18	X-RAY DIFFRACTION	18	chain 'C' and (resid 111 through 146 )
19	X-RAY DIFFRACTION	19	chain 'C' and (resid 147 through 381 )
20	X-RAY DIFFRACTION	20	chain 'C' and (resid 382 through 473 )
21	X-RAY DIFFRACTION	21	chain 'D' and (resid 20 through 46 )
22	X-RAY DIFFRACTION	22	chain 'D' and (resid 47 through 83 )
23	X-RAY DIFFRACTION	23	chain 'D' and (resid 84 through 110 )
24	X-RAY DIFFRACTION	24	chain 'D' and (resid 111 through 146 )
25	X-RAY DIFFRACTION	25	chain 'D' and (resid 147 through 172 )
26	X-RAY DIFFRACTION	26	chain 'D' and (resid 173 through 194 )
27	X-RAY DIFFRACTION	27	chain 'D' and (resid 195 through 312 )
28	X-RAY DIFFRACTION	28	chain 'D' and (resid 313 through 338 )
29	X-RAY DIFFRACTION	29	chain 'D' and (resid 339 through 445 )
30	X-RAY DIFFRACTION	30	chain 'D' and (resid 446 through 473 )
31	X-RAY DIFFRACTION	31	chain 'E' and (resid 20 through 126 )
32	X-RAY DIFFRACTION	32	chain 'E' and (resid 127 through 161 )
33	X-RAY DIFFRACTION	33	chain 'E' and (resid 162 through 187 )
34	X-RAY DIFFRACTION	34	chain 'E' and (resid 188 through 272 )
35	X-RAY DIFFRACTION	35	chain 'E' and (resid 273 through 312 )
36	X-RAY DIFFRACTION	36	chain 'E' and (resid 313 through 338 )
37	X-RAY DIFFRACTION	37	chain 'E' and (resid 339 through 381 )
38	X-RAY DIFFRACTION	38	chain 'E' and (resid 382 through 473 )

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