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- PDB-6tzb: Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza viru... -

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Basic information

Entry
Database: PDB / ID: 6tzb
TitleCrystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin in complex with 6'-SLNLN
Components(Hemagglutinin ...) x 2
KeywordsVIRAL PROTEIN
Function / homology
Function and homology information


viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / host cell surface receptor binding / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / membrane
Similarity search - Function
Hemagglutinin Ectodomain; Chain B - #10 / Hemagglutinin Ectodomain; Chain B / Hemagglutinin (Ha1 Chain); Chain: A; domain 1 / Haemagglutinin, alpha/beta domain, HA1 chain / Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
6'-sialyl-N-acetyllactosamine / Hemagglutinin / Hemagglutinin
Similarity search - Component
Biological speciesInfluenza A virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.243 Å
AuthorsWu, N.C. / Wilson, I.A.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R56 AI127371 United States
Bill & Melinda Gates FoundationOPP1170236 United States
CitationJournal: Nat Commun / Year: 2020
Title: Major antigenic site B of human influenza H3N2 viruses has an evolving local fitness landscape.
Authors: Wu, N.C. / Otwinowski, J. / Thompson, A.J. / Nycholat, C.M. / Nourmohammad, A. / Wilson, I.A.
History
DepositionAug 12, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 30, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Mar 25, 2020Group: Data collection / Database references / Category: chem_comp / citation / citation_author
Item: _chem_comp.type / _citation.country ..._chem_comp.type / _citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_comp_id_1 / _pdbx_validate_close_contact.auth_comp_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _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.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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 11, 2023Group: 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 2.2Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Hemagglutinin HA1 chain
B: Hemagglutinin HA2 chain
C: Hemagglutinin HA1 chain
D: Hemagglutinin HA2 chain
E: Hemagglutinin HA1 chain
F: Hemagglutinin HA2 chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)174,94522
Polymers166,5546
Non-polymers8,39116
Water16,556919
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area42880 Å2
ΔGint-23 kcal/mol
Surface area58110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)210.401, 132.173, 72.468
Angle α, β, γ (deg.)90.000, 97.930, 90.000
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain B and resid 1 through 171)
21chain D
31chain F
12(chain A and resid 9 through 325)
22chain C
32chain E

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLYGLYPHEPHE(chain B and resid 1 through 171)BB1 - 1711 - 171
21GLYGLYPHEPHEchain DDD1 - 1711 - 171
31GLYGLYPHEPHEchain FFF1 - 1711 - 171
12PROPROGLUGLU(chain A and resid 9 through 325)AA9 - 3251 - 317
22PROPROGLUGLUchain CCC9 - 3251 - 317
32PROPROGLUGLUchain EEE9 - 3251 - 317

NCS ensembles :
ID
1
2

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Components

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Hemagglutinin ... , 2 types, 6 molecules ACEBDF

#1: Protein Hemagglutinin HA1 chain


Mass: 35320.781 Da / Num. of mol.: 3 / Fragment: residues 27-345
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus (strain A/Hong Kong/1/1968 H3N2)
Strain: A/Hong Kong/1/1968 H3N2 / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: Q91MA7
#2: Protein Hemagglutinin HA2 chain


Mass: 20197.312 Da / Num. of mol.: 3 / Fragment: residues 346-521
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus (strain A/Hong Kong/1/1968 H3N2)
Strain: A/Hong Kong/1/1968 H3N2 / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: H9XC94

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Sugars , 7 types, 16 molecules

#3: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#4: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: Polysaccharide N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D- ...N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-3)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1039.937 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DNeup5Aca2-6DGalpb1-4DGlcpNAcb1-3DGalpb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a2112h-1b_1-5][Aad21122h-2a_2-6_5*NCC/3=O]/1-2-1-2-3/a4-b1_b3-c1_c4-d1_d6-e2WURCSPDB2Glycan 1.1.0
[][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{[(3+1)][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{[(6+2)][a-D-Neup5Ac]{}}}}}LINUCSPDB-CARE
#6: Polysaccharide alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-6DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c6-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#7: Polysaccharide N-acetyl-alpha-neuraminic acid-(2-6)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / 6'-sialyl-N-acetyllactosamine


Type: oligosaccharide, Oligosaccharide / Class: Glycan component / Mass: 674.604 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: 6'-sialyl-N-acetyllactosamine
DescriptorTypeProgram
DNeup5Aca2-6DGalpb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/3,3,2/[a2122h-1b_1-5_2*NCC/3=O][a2112h-1b_1-5][Aad21122h-2a_2-6_5*NCC/3=O]/1-2-3/a4-b1_b6-c2WURCSPDB2Glycan 1.1.0
[][b-D-GlcpNAc]{[(4+1)][b-D-Galp]{[(6+2)][a-D-Neup5Ac]{}}}LINUCSPDB-CARE
#8: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#9: 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.: 5
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6 / Feature type: SUBJECT OF INVESTIGATION
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 1 types, 919 molecules

#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 919 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3 Å3/Da / Density % sol: 58.95 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1 M sodium cacodylate pH 6.5, 6% PEG 8000, and 39% 2-methyl-2,4-pentanediol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.0332 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jun 12, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.243→50 Å / Num. obs: 93371 / % possible obs: 100 % / Redundancy: 6.5 % / Biso Wilson estimate: 37.03 Å2 / Rmerge(I) obs: 0.099 / Rpim(I) all: 0.042 / Rrim(I) all: 0.108 / Χ2: 1.111 / Net I/σ(I): 6.3
Reflection shell

Diffraction-ID: 1 / % possible all: 100

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2
2.25-2.3460.895103550.6060.3970.9811.123
2.34-2.456.90.628103360.8460.260.6810.446
2.45-2.586.80.486103280.7630.2030.5270.674
2.58-2.746.70.318103270.9530.1340.3460.51
2.74-2.956.40.194103490.980.0830.2110.502
2.95-3.245.80.115103640.9810.0520.1260.66
3.24-3.716.70.078103770.9970.0330.0840.824
3.71-4.6870.049104110.9980.020.0531.018
4.68-506.30.039105240.9850.0170.0434.327

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Processing

Software
NameVersionClassification
HKL-2000712data scaling
PHENIX1.12_2829refinement
PDB_EXTRACT3.25data extraction
PHASER2.5.6phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4FNK

4fnk


Resolution: 2.243→39.748 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 20.4
RfactorNum. reflection% reflection
Rfree0.2069 4625 4.96 %
Rwork0.1572 --
obs0.1597 93317 99.5 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 148.21 Å2 / Biso mean: 49.0655 Å2 / Biso min: 15.26 Å2
Refinement stepCycle: final / Resolution: 2.243→39.748 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11520 0 559 919 12998
Biso mean--89.67 46.78 -
Num. residues----1469
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00812378
X-RAY DIFFRACTIONf_angle_d0.96916855
X-RAY DIFFRACTIONf_chiral_restr0.0571951
X-RAY DIFFRACTIONf_plane_restr0.0062141
X-RAY DIFFRACTIONf_dihedral_angle_d11.7157333
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11B2551X-RAY DIFFRACTION10.55TORSIONAL
12D2551X-RAY DIFFRACTION10.55TORSIONAL
13F2551X-RAY DIFFRACTION10.55TORSIONAL
21A4558X-RAY DIFFRACTION10.55TORSIONAL
22C4558X-RAY DIFFRACTION10.55TORSIONAL
23E4558X-RAY DIFFRACTION10.55TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.243-2.26850.28971260.2837261287
2.2685-2.29520.30121460.25882923100
2.2952-2.32320.30641470.23152938100
2.3232-2.35260.27951580.22322980100
2.3526-2.38350.25841560.19562937100
2.3835-2.41620.28621420.19192984100
2.4162-2.45070.26191610.18092927100
2.4507-2.48730.23741890.18622967100
2.4873-2.52610.25141780.18212923100
2.5261-2.56760.23361480.17752948100
2.5676-2.61180.22861640.17372961100
2.6118-2.65930.22931570.16412950100
2.6593-2.71040.21581720.16442936100
2.7104-2.76570.24251500.16133009100
2.7657-2.82590.22691400.16532956100
2.8259-2.89160.22811440.16553015100
2.8916-2.96390.23371530.16342959100
2.9639-3.0440.2261540.15972970100
3.044-3.13350.19311480.16042948100
3.1335-3.23460.2341460.16172956100
3.2346-3.35020.21581710.15692999100
3.3502-3.48420.20041460.14712962100
3.4842-3.64270.20241520.14362980100
3.6427-3.83460.20261640.14352947100
3.8346-4.07460.17631620.13362985100
4.0746-4.38890.17871520.12282991100
4.3889-4.82990.17391560.12252987100
4.8299-5.52720.16911560.13662980100
5.5272-6.95760.17151430.16263018100
6.9576-39.7480.18811440.1668304499
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°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)
10.83050.78150.18721.61811.39983.0192-0.1341-0.33340.40740.40340.0886-0.3002-0.12760.2465-0.12860.3870.0612-0.17230.5246-0.1720.53-14.656553.540738.9739
21.6193-0.177-0.45151.63750.11911.018-0.1010.0275-0.64580.0709-0.13930.10680.4565-0.33230.19470.4311-0.130.08560.38590.07330.4164-29.9325-8.592721.0427
30.80860.2540.36592.5109-0.05620.57440.0049-0.2950.04840.4276-0.07380.1240.0286-0.26660.08550.2534-0.04070.05350.38820.0220.1927-23.628617.106832.2873
42.6764-0.41990.26640.0948-0.27111.3201-0.1236-0.55750.98190.3956-0.0083-0.4139-0.22110.17430.11290.41750.036-0.16660.4027-0.1680.6185-10.055752.29139.7163
51.75330.8990.26411.18971.52173.297-0.091-0.42670.34730.61370.0652-0.3578-0.1978-0.08260.00870.53530.1434-0.20890.5195-0.19240.5184-21.63253.658445.7089
60.8021-0.16470.20191.80720.50341.016-0.1776-0.38390.40740.40880.1091-0.1793-0.2094-0.11560.01220.3780.0802-0.10110.4037-0.14540.3685-25.061551.974437.495
72.0308-1.7658-1.46355.64141.02471.0351-0.3685-0.3912-0.02960.72480.31910.3187-0.1002-0.25030.08850.43510.1357-0.02210.6477-0.12520.3238-44.89255.05538.6301
80.25720.37280.35391.6941.48211.8221-0.0752-0.050.0129-0.0487-0.03750.21960.0184-0.0980.12080.2065-0.0691-0.02450.3370.06670.3118-50.386510.63871.1888
91.7086-1.501-0.58312.605-0.10591.2084-0.1279-0.29470.18570.1791-0.08220.2548-0.1831-0.46870.20440.37690.1513-0.02640.4888-0.15360.4041-46.525761.494431.4137
100.6857-0.40780.00972.68410.48580.7843-0.1742-0.260.34370.2120.1410.1694-0.2837-0.12380.07010.33470.0843-0.0420.3981-0.09150.3995-39.396855.988229.4053
110.5339-0.5133-0.1962.29271.0171.07390.02190.0970.2049-0.17290.025-0.1648-0.1302-0.0552-0.05830.1885-0.02260.01120.24020.04770.2208-19.354631.7812-1.3838
121.7407-0.1027-0.24071.4715-0.03451.5096-0.0540.1759-0.2984-0.0340.05110.09870.3848-0.13810.00570.3073-0.07230.04410.21510.00160.2468-16.3872-4.3099-7.1386
130.6703-0.756-0.4482.65911.48111.25680.01090.10460.2554-0.13110.0637-0.2804-0.1683-0.012-0.08010.2467-0.01390.00660.2360.02810.2916-20.548238.17293.0045
140.25630.78380.07793.00690.36480.9355-0.0876-0.18650.6015-0.3740.1941-0.3434-0.5610.0362-0.07430.49580.0105-0.02720.2904-0.08370.6966-20.599568.896419.3228
150.0384-0.2443-0.13171.52280.81640.43570.02940.0848-0.69090.17840.1565-0.76120.5270.389-0.1830.5894-0.0434-0.06480.637-0.12860.8423-15.529939.335113.1318
161.13870.11660.16852.03520.52161.0668-0.0747-0.20570.5192-0.05340.0785-0.333-0.4382-0.0663-0.03360.32150.0259-0.05090.2387-0.06960.4647-24.48858.801922.0456
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 9:37)A9 - 37
2X-RAY DIFFRACTION2(chain A and resid 38:257)A38 - 257
3X-RAY DIFFRACTION3(chain A and resid 258:314)A258 - 314
4X-RAY DIFFRACTION4(chain A and resid 315:329)A315 - 329
5X-RAY DIFFRACTION5(chain B and resid 1:60)B1 - 60
6X-RAY DIFFRACTION6(chain B and resid 61:172)B61 - 172
7X-RAY DIFFRACTION7(chain C and resid 9:37)C9 - 37
8X-RAY DIFFRACTION8(chain C and resid 38:325)C38 - 325
9X-RAY DIFFRACTION9(chain D and resid 1:60)D1 - 60
10X-RAY DIFFRACTION10(chain D and resid 61:171)D61 - 171
11X-RAY DIFFRACTION11(chain E and resid 9:117)E9 - 117
12X-RAY DIFFRACTION12(chain E and resid 118:260)E118 - 260
13X-RAY DIFFRACTION13(chain E and resid 261:325)E261 - 325
14X-RAY DIFFRACTION14(chain F and resid 1:55)F1 - 55
15X-RAY DIFFRACTION15(chain F and resid 56:60)F56 - 60
16X-RAY DIFFRACTION16(chain F and resid 61:171)F61 - 171

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