PDB-2x9m: Hendra virus attachment glycoprotein

ID or keywords:

Entry

Database: PDB / ID: 2x9m

Title

Hendra virus attachment glycoprotein

Components

GLYCOPROTEIN G

Keywords

VIRAL PROTEIN / PARAMYXOVIRUS / VIRAL SURFACE / NIPAH VIRUS / HENIPAVIRUS / VIRUS ENVELOPE / VIRAL ATTACHMENT / HNV / NIV-G / EFNB3 / EFNB2 / EPHRINB2 / EPHRINB3

Function / homology

Function and homology information

exo-alpha-sialidase activity / host cell surface / host cell surface receptor binding / viral envelope / symbiont entry into host cell / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane
Similarity search - Function

Biological species

HENDRA VIRUS

Method

X-RAY DIFFRACTION /

SYNCHROTRON /

MOLECULAR REPLACEMENT / Resolution: 2.9 Å

Authors

Bowden, T.A. / Crispin, M. / Harvey, D. / Jones, E.Y. / Stuart, D.I.

Citation

Journal: J.Virol. / Year: 2010
Title: Dimeric Architecture of the Hendra Virus Attachment Glycoprotein: Evidence for a Conserved Mode of Assembly.
Authors: Bowden, T.A. / Crispin, M. / Harvey, D.J. / Jones, E.Y. / Stuart, D.I.

History

Deposition	Mar 23, 2010	Deposition site: PDBE / Processing site: PDBE
Revision 1.0	Apr 21, 2010	Provider: repository / Type: Initial release
Revision 1.1	May 8, 2011	Group: Version format compliance
Revision 1.2	Jul 13, 2011	Group: Version format compliance
Revision 1.3	Jul 29, 2020	Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Structure summary Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.4	Dec 20, 2023	Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.5	Nov 6, 2024	Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

Structure viewer	Molecule: MolmilJmol/JSmol

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PDBx/mmCIF format	2x9m.cif.gz	659.2 KB	Display	PDBx/mmCIF format
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Validation report

Summary document	2x9m_validation.pdf.gz	481.2 KB	Display	wwPDB validaton report
Full document	2x9m_full_validation.pdf.gz	500.7 KB	Display
Data in XML	2x9m_validation.xml.gz	59.3 KB	Display
Data in CIF	2x9m_validation.cif.gz	80.7 KB	Display
Arichive directory	https://data.pdbj.org/pub/pdb/validation_reports/x9/2x9m ftp://data.pdbj.org/pub/pdb/validation_reports/x9/2x9m	HTTPS FTP

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Related structure data

Related structure data	2vwdS 2vsk S: Starting model for refinement
Similar structure data	3vii-2 4fgl-d 6klk-d 2zb6-1 5yz5-1 4h00-2 3q8x-d 5e5c-d 3bdz-d 1mzf-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) 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	#231 - Mar 2019 Measles Virus Proteins similarity (3) #113 - May 2009 Influenza Neuraminidase similarity (1)

Deposited unit

A: GLYCOPROTEIN G

B: GLYCOPROTEIN G

C: GLYCOPROTEIN G

D: GLYCOPROTEIN G

hetero molecules

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

1

B: GLYCOPROTEIN G

D: GLYCOPROTEIN G

hetero molecules

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

2

A: GLYCOPROTEIN G

C: GLYCOPROTEIN G

hetero molecules

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

Unit cell

Length a, b, c (Å)	65.883, 84.775, 91.548
Angle α, β, γ (deg.)	103.39, 99.63, 108.62
Int Tables number	1
Space group name H-M	P1

Noncrystallographic symmetry (NCS)

NCS domain:

ID	Ens-ID	Details
1	1	A
2	1	B
3	1	C
4	1	D

NCS domain segments:

Ens-ID: 1 / Refine code: 3

Dom-ID	Component-ID	Beg auth comp-ID	Beg label comp-ID	End auth comp-ID	End label comp-ID	Auth asym-ID	Label asym-ID	Auth seq-ID	Label seq-ID
1	1	GLN	GLN	LYS	LYS	A	A	187 - 192	3 - 8
2	1	GLN	GLN	LYS	LYS	B	B	187 - 192	3 - 8
3	1	GLN	GLN	LYS	LYS	C	C	187 - 192	3 - 8
4	1	GLN	GLN	LYS	LYS	D	D	187 - 192	3 - 8
1	2	THR	THR	PRO	PRO	A	A	196 - 208	12 - 24
2	2	THR	THR	PRO	PRO	B	B	196 - 208	12 - 24
3	2	THR	THR	PRO	PRO	C	C	196 - 208	12 - 24
4	2	THR	THR	PRO	PRO	D	D	196 - 208	12 - 24
1	3	GLY	GLY	GLY	GLY	A	A	214 - 238	30 - 54
2	3	GLY	GLY	GLY	GLY	B	B	214 - 238	30 - 54
3	3	GLY	GLY	GLY	GLY	C	C	214 - 238	30 - 54
4	3	GLY	GLY	GLY	GLY	D	D	214 - 238	30 - 54
1	4	ALA	ALA	THR	THR	A	A	245 - 285	61 - 101
2	4	ALA	ALA	THR	THR	B	B	245 - 285	61 - 101
3	4	ALA	ALA	THR	THR	C	C	245 - 285	61 - 101
4	4	ALA	ALA	THR	THR	D	D	245 - 285	61 - 101
1	5	VAL	VAL	SER	SER	A	A	300 - 403	116 - 219
2	5	VAL	VAL	SER	SER	B	B	300 - 403	116 - 219
3	5	VAL	VAL	SER	SER	C	C	300 - 403	116 - 219
4	5	VAL	VAL	SER	SER	D	D	300 - 403	116 - 219
1	6	SER	SER	LEU	LEU	A	A	405 - 420	221 - 236
2	6	SER	SER	LEU	LEU	B	B	405 - 420	221 - 236
3	6	SER	SER	LEU	LEU	C	C	405 - 420	221 - 236
4	6	SER	SER	LEU	LEU	D	D	405 - 420	221 - 236
1	7	LEU	LEU	LEU	LEU	A	A	426 - 567	242 - 383
2	7	LEU	LEU	LEU	LEU	B	B	426 - 567	242 - 383
3	7	LEU	LEU	LEU	LEU	C	C	426 - 567	242 - 383
4	7	LEU	LEU	LEU	LEU	D	D	426 - 567	242 - 383
1	8	VAL	VAL	ILE	ILE	A	A	571 - 580	387 - 396
2	8	VAL	VAL	ILE	ILE	B	B	571 - 580	387 - 396
3	8	VAL	VAL	ILE	ILE	C	C	571 - 580	387 - 396
4	8	VAL	VAL	ILE	ILE	D	D	571 - 580	387 - 396
1	9	VAL	VAL	SER	SER	A	A	587 - 602	403 - 418
2	9	VAL	VAL	SER	SER	B	B	587 - 602	403 - 418
3	9	VAL	VAL	SER	SER	C	C	587 - 602	403 - 418
4	9	VAL	VAL	SER	SER	D	D	587 - 602	403 - 418

NCS oper:

ID	Code	Matrix	Vector
1	given	(-0.7904, -0.6126, -0.0008), (-0.6126, 0.7904, 0.0053), (-0.0026, 0.0046, -1)	62.3459, -23.8757, 107.3583
2	given	(-0.9073, -0.4114, -0.0869), (-0.4126, 0.9109, -0.0048), (0.0811, 0.0315, -0.9962)	50.0494, 10.14, 103.4933
3	given	(0.9692, 0.2355, 0.0717), (-0.2365, 0.9716, 0.0071), (-0.068, -0.0238, 0.9974)	-5.7316, -37.5107, 0.3894

#1: Protein

GLYCOPROTEIN G / HEV-G

Mass: 47206.543 Da / Num. of mol.: 4 / Fragment: RECEPTOR-BINDING DOMAIN, RESIDUES 185-604
Source method: isolated from a genetically manipulated source
Details: N-ACETYLGLUCOSAMINE LINKAGES OBSERVED IN STRUCTURE ASN306, ASN378, ASN417, ASN481, AND ASN529
Source: (gene. exp.)

HENDRA VIRUS / Description: SYNTHETICALLY OPTIMIZED CDNA (GENEART) / Plasmid: PHLSEC / Cell line (production host): 293T / Organ (production host): EMBRYONIC KIDNEY / Production host:

HOMO SAPIENS (human) / References: UniProt: O89343

#2: Sugar

ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE

Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 10
Source method: isolated from a genetically manipulated source
Formula: C₈H₁₅NO₆

Identifier	Type	Program
DGlcpNAcb	CONDENSED IUPAC CARBOHYDRATE SYMBOL	GMML 1.0
N-acetyl-b-D-glucopyranosamine	COMMON NAME	GMML 1.0
b-D-GlcpNAc	IUPAC CARBOHYDRATE SYMBOL	PDB-CARE 1.0
GlcNAc	SNFG CARBOHYDRATE SYMBOL	GMML 1.0

#3: Water

ChemComp-HOH / water

Mass: 18.015 Da / Num. of mol.: 117 / Source method: isolated from a natural source / Formula: H₂O

Has protein modification

Y

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Experiment

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

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Sample preparation

Crystal	Density Matthews: 2.4 Å³/Da / Density % sol: 48 % / Description: NONE
Crystal grow	pH: 6.5 Details: 30% PEG 8000, 0.2 M AMMONIUM SULPHATE, 0.1 M SODIUM CACODYLATE BUFFER PH 6.5

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Data collection

Diffraction	Mean temperature: 100 K
Diffraction source	Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.8726
Detector	Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: May 16, 2009 / Details: MIRRORS
Radiation	Monochromator: SI (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength	Wavelength: 0.8726 Å / Relative weight: 1
Reflection	Resolution: 2.9→50 Å / Num. obs: 38664 / % possible obs: 99.2 % / Observed criterion σ(I): -3 / Redundancy: 3 % / B_iso Wilson estimate: 37.8 Å² / R_merge(I) obs: 0.17 / Net I/σ(I): 6.1
Reflection shell	Resolution: 2.9→2.95 Å / Redundancy: 2.9 % / R_merge(I) obs: 0.45 / Mean I/σ(I) obs: 2.9 / % possible all: 98

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Processing

Software

Name	Version	Classification
REFMAC	5.5.0109	refinement
DENZO		data reduction
SCALEPACK		data scaling
PHASER		phasing

Refinement

Method to determine structure:

MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2VWD

2vwd

Resolution: 2.9→44.2 Å / Cor.coef. F_o:F_c: 0.876 / Cor.coef. F_o:F_c free: 0.819 / SU B: 42.258 / SU ML: 0.38 / Cross valid method: THROUGHOUT / ESU R Free: 0.489 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. B VALUES HAVE TLS CONTRIBUTION.

	R_factor	Num. reflection	% reflection	Selection details
R_free	0.27273	1926	5 %	RANDOM
R_work	0.23306	-	-	-
obs	0.23507	36735	98.92 %	-

Solvent computation

Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK

Displacement parameters

B_iso mean: 23.765 Å²

	B_aniso -1	B_aniso -2	B_aniso -3
1-	0.97 Å²	0.11 Å²	-0.34 Å²
2-	-	-0.25 Å²	-0.09 Å²
3-	-	-	-0.81 Å²

Refinement step

Cycle: LAST / Resolution: 2.9→44.2 Å

	Protein	Nucleic acid	Ligand	Solvent	Total
Num. atoms	13207	0	140	117	13464

Refine LS restraints

Refine-ID	Type	Dev ideal	Dev ideal target	Number
X-RAY DIFFRACTION	r_bond_refined_d	0.008	0.022	13706
X-RAY DIFFRACTION	r_bond_other_d	0.003	0.02	9182
X-RAY DIFFRACTION	r_angle_refined_deg	1.124	1.968	18687
X-RAY DIFFRACTION	r_angle_other_deg	0.904	3	22407
X-RAY DIFFRACTION	r_dihedral_angle_1_deg	6.324	5	1667
X-RAY DIFFRACTION	r_dihedral_angle_2_deg	31.702	24.286	602
X-RAY DIFFRACTION	r_dihedral_angle_3_deg	15.165	15	2246
X-RAY DIFFRACTION	r_dihedral_angle_4_deg	16.829	15	72
X-RAY DIFFRACTION	r_chiral_restr	0.087	0.2	2107
X-RAY DIFFRACTION	r_gen_planes_refined	0.004	0.021	15115
X-RAY DIFFRACTION	r_gen_planes_other	0.001	0.02	2691
X-RAY DIFFRACTION	r_nbd_refined
X-RAY DIFFRACTION	r_nbd_other
X-RAY DIFFRACTION	r_nbtor_refined
X-RAY DIFFRACTION	r_nbtor_other
X-RAY DIFFRACTION	r_xyhbond_nbd_refined
X-RAY DIFFRACTION	r_xyhbond_nbd_other
X-RAY DIFFRACTION	r_metal_ion_refined
X-RAY DIFFRACTION	r_metal_ion_other
X-RAY DIFFRACTION	r_symmetry_vdw_refined
X-RAY DIFFRACTION	r_symmetry_vdw_other
X-RAY DIFFRACTION	r_symmetry_hbond_refined
X-RAY DIFFRACTION	r_symmetry_hbond_other
X-RAY DIFFRACTION	r_symmetry_metal_ion_refined
X-RAY DIFFRACTION	r_symmetry_metal_ion_other
X-RAY DIFFRACTION	r_mcbond_it	0.705	1.5	8348
X-RAY DIFFRACTION	r_mcbond_other	0.131	1.5	3344
X-RAY DIFFRACTION	r_mcangle_it	1.306	2	13630
X-RAY DIFFRACTION	r_mcangle_other
X-RAY DIFFRACTION	r_scbond_it	0.986	3	5358
X-RAY DIFFRACTION	r_scbond_other
X-RAY DIFFRACTION	r_scangle_it	1.701	4.5	5057
X-RAY DIFFRACTION	r_scangle_other
X-RAY DIFFRACTION	r_long_range_B_refined
X-RAY DIFFRACTION	r_long_range_B_other
X-RAY DIFFRACTION	r_rigid_bond_restr
X-RAY DIFFRACTION	r_sphericity_free
X-RAY DIFFRACTION	r_sphericity_bonded

Refine LS restraints NCS

Ens-ID: 1 / Refine-ID: X-RAY DIFFRACTION

Dom-ID	Auth asym-ID	Number	Type	Rms dev position (Å)	Weight position
1	A	2192	tight positional	0.02	0.05
2	B	2192	tight positional	0.02	0.05
3	C	2192	tight positional	0.02	0.05
4	D	2192	tight positional	0.02	0.05
1	A	2801	loose positional	0.05	5
2	B	2801	loose positional	0.03	5
3	C	2801	loose positional	0.04	5
4	D	2801	loose positional	0.05	5
1	A	2192	tight thermal	0.04	0.5
2	B	2192	tight thermal	0.04	0.5
3	C	2192	tight thermal	0.06	0.5
4	D	2192	tight thermal	0.04	0.5
1	A	2801	loose thermal	0.03	10
2	B	2801	loose thermal	0.03	10
3	C	2801	loose thermal	0.04	10
4	D	2801	loose thermal	0.03	10

LS refinement shell

Resolution: 2.899→2.974 Å / Total num. of bins used: 20

	R_factor	Num. reflection	% reflection
R_free	0.364	142	-
R_work	0.301	2541	-
obs	-	-	93.75 %

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	2.6136	0.0466	2.5698	2.0977	0.3456	3.3622	-0.0795	-0.2506	-0.2044	0.3624	0.2232	0.2126	-0.0844	-0.4949	-0.1438	0.1448	0.0352	0.0609	0.2327	0.0331	0.0447	0.5211	27.1387	44.3179
2	1.1527	-0.0453	0.9178	0.0801	-0.3611	2.1049	-0.1385	0.0436	0.0617	0.0517	0.0289	-0.0336	-0.2417	-0.1683	0.1095	0.2005	0.0492	-0.1235	0.0672	-0.0288	0.1488	17.6267	32.682	41.4327
3	1.8431	-0.0437	0.237	1.6313	-0.0174	1.7316	-0.1661	-0.1565	0.064	0.2347	0.1054	-0.2688	0.0066	-0.0845	0.0607	0.1612	0.0402	-0.0506	0.075	-0.0011	0.059	19.9741	27.1807	42.3214
4	1.3007	-0.3354	0.6229	1.2205	-0.4206	1.4064	-0.0043	0.088	0.0349	-0.1061	-0.0135	-0.061	0.0754	0.0001	0.0178	0.1342	0.0072	0.0016	0.033	-0.0122	0.0165	12.4802	29.2265	24.0805
5	2.3467	-0.7906	1.208	0.3839	0.0124	2.12	-0.1391	-0.5404	-0.1659	0.1106	0.109	0.0937	0.2076	-0.4544	0.0301	0.1761	-0.0037	0.0521	0.1654	0.0314	0.0497	3.4432	23.8166	42.1041
6	2.6377	2.7932	1.7318	4.6285	1.0907	1.9405	-0.1378	-0.3496	0.3618	0.3105	0.1126	0.4453	-0.1927	-0.5733	0.0252	0.1979	0.0917	-0.0042	0.2438	-0.0022	0.1371	2.6743	33.4259	44.1082
7	2.3413	0.0302	1.8994	1.543	1.2155	3.4893	0.077	0.2719	-0.0463	-0.4544	0.0941	-0.2145	-0.4145	0.425	-0.1711	0.2546	-0.0824	0.0705	0.1511	0.0256	0.061	18.053	77.9615	63.4415
8	1.9202	0.1382	-0.6342	0.4648	0.911	2.2415	0.0492	-0.0769	-0.0707	-0.1807	-0.0948	0.0333	-0.366	-0.1158	0.0457	0.2573	0.0469	-0.1135	0.0434	-0.0274	0.1167	0.8623	71.7858	66.2924
9	1.4024	0.3115	0.1345	1.0101	0.4358	2.1207	-0.0626	0.1394	-0.114	-0.2607	-0.0519	0.1907	-0.0599	-0.0301	0.1145	0.2035	0.0307	-0.0591	0.0555	-0.0197	0.0641	2.1942	66.2529	65.4876
10	0.9157	-0.3087	0.1775	1.4915	1.1073	2.2458	-0.0417	-0.089	-0.1241	0.2072	-0.0836	0.2065	0.2544	-0.1243	0.1252	0.1862	-0.008	0.0055	0.0398	0.0211	0.0655	0.1469	66.2113	85.5358
11	1.0778	0.0788	-0.1759	1.3724	0.78	1.6179	-0.0138	-0.0158	0.0228	-0.0816	0.09	-0.0695	-0.1213	0.2055	-0.0762	0.1617	0.0088	-0.0276	0.0706	0.0083	0.0253	13.5644	77.0937	80.6426
12	10.1911	-2.0119	1.8523	1.4106	-0.0302	1.202	0.0849	-0.1781	0.4995	-0.5117	0.0394	-0.0366	-0.4864	0.2569	-0.1243	0.4542	-0.0877	0.0711	0.1782	-0.0778	0.1149	12.2948	81.4981	63.5896
13	1.8306	-0.639	0.0063	0.5605	0.4602	2.6398	0.2443	0.591	0.1153	-0.3247	-0.1201	-0.1885	-0.2224	0.5512	-0.1242	0.2969	-0.0305	0.0385	0.3589	0.082	0.1581	30.5537	35.4583	62.4739
14	0.9798	-0.1014	0.427	1.1836	0.2661	2.2998	-0.0116	-0.0086	-0.0433	0.0039	0.023	0.1451	0.0603	-0.2139	-0.0114	0.1465	0.0129	0.0041	0.0507	0.0378	0.0587	12.8952	26.6212	76.6175
15	2.6385	-0.4067	-10.567	0.0635	1.6337	42.3537	-0.6436	0.0797	-0.266	0.0497	-0.2313	0.0452	1.6668	-0.4431	0.8749	0.508	0.1856	-0.068	0.5655	0.0095	0.4958	7.0793	8.2826	79.6619
16	1.4206	0.0603	0.1372	1.4171	0.2344	1.8129	-0.0687	-0.0263	0.1367	0.0738	0.0739	-0.1637	-0.2082	0.2	-0.0051	0.1704	0.0038	-0.0356	0.0688	0.0135	0.0542	27.9543	34.3629	80.2465
17	15.5294	-11.6246	15.3836	8.7914	-11.5172	15.2394	-0.273	-0.5562	-0.3166	0.2045	0.6052	0.3412	-0.2622	-0.5544	-0.3321	0.7223	0.0119	-0.1324	0.5016	0.259	0.1606	17.9184	46.4217	62.2929
18	10.2096	-2.0851	1.6117	0.7788	-0.2637	3.5966	0.2539	0.3103	0.3209	-0.4485	-0.0729	-0.1906	-0.1714	0.4896	-0.181	0.476	-0.0594	0.1216	0.1609	0.0529	0.1185	32.805	35.7998	63.4348
19	2.4239	0.4014	1.9643	1.0608	0.554	3.2786	-0.0862	-0.3569	-0.0617	0.367	0.0916	0.2963	0.1568	-0.6656	-0.0054	0.2033	-0.0275	0.1303	0.2724	0.0428	0.1004	-13.9226	62.2653	44.0183
20	0.659	1.0555	-0.1478	1.9334	0.3319	2.4174	0.0568	-0.0309	-0.0207	0.1528	-0.0161	-0.1303	-0.332	-0.0783	-0.0407	0.2351	0.0591	-0.0717	0.0868	-0.0571	0.105	3.4795	75.6412	43.1724
21	0.7961	0.0945	0.5698	1.0898	-0.2005	2.3269	-0.0555	0.0524	0.0323	0.0269	0.0357	-0.1018	-0.0828	0.2362	0.0198	0.1377	0.0097	0.0085	0.066	-0.0088	0.0503	8.721	69.4049	29.2684
22	1.261	0.2157	0.3877	0.9852	-0.0441	2.151	-0.068	-0.064	0.027	-0.0391	0.0774	0.1483	-0.0498	-0.3262	-0.0094	0.1365	0.0249	-0.0067	0.0885	0.0002	0.0597	-8.0474	66.6169	27.6934
23	41.2799	-5.2494	9.0486	3.7079	-1.6731	2.0766	-0.8135	-0.907	-0.7848	0.4272	1.0244	0.4149	-0.2305	-0.386	-0.2108	0.367	0.1415	0.0673	0.5517	-0.1262	0.3234	-8.5585	83.5771	46.1736
24	4.7608	3.7067	1.3025	3.6858	1.5568	2.9853	0.139	-0.3014	-0.0163	0.5269	-0.026	0.1682	0.1178	-0.6154	-0.1129	0.2613	0.1276	0.1243	0.3324	0.1014	0.0689	-12.6057	65.1751	44.3909

Refinement TLS group

ID	Refine-ID	Refine TLS-ID	Auth asym-ID	Auth seq-ID
1	X-RAY DIFFRACTION	1	A	185 - 212
2	X-RAY DIFFRACTION	2	A	213 - 239
3	X-RAY DIFFRACTION	3	A	240 - 289
4	X-RAY DIFFRACTION	4	A	290 - 567
5	X-RAY DIFFRACTION	5	A	568 - 580
6	X-RAY DIFFRACTION	6	A	581 - 603
7	X-RAY DIFFRACTION	7	B	185 - 212
8	X-RAY DIFFRACTION	8	B	213 - 239
9	X-RAY DIFFRACTION	9	B	240 - 289
10	X-RAY DIFFRACTION	10	B	290 - 419
11	X-RAY DIFFRACTION	11	B	421 - 580
12	X-RAY DIFFRACTION	12	B	581 - 603
13	X-RAY DIFFRACTION	13	C	186 - 215
14	X-RAY DIFFRACTION	14	C	216 - 419
15	X-RAY DIFFRACTION	15	C	420 - 425
16	X-RAY DIFFRACTION	16	C	426 - 579
17	X-RAY DIFFRACTION	17	C	580 - 586
18	X-RAY DIFFRACTION	18	C	587 - 603
19	X-RAY DIFFRACTION	19	D	186 - 210
20	X-RAY DIFFRACTION	20	D	211 - 244
21	X-RAY DIFFRACTION	21	D	245 - 419
22	X-RAY DIFFRACTION	22	D	420 - 580
23	X-RAY DIFFRACTION	23	D	581 - 586
24	X-RAY DIFFRACTION	24	D	587 - 603

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