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

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Basic information

Entry
Database: PDB / ID: 6bkm
TitleCrystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin E190D mutant apo form
Components(Hemagglutinin) x 2
KeywordsVIRAL PROTEIN / Influenza / Hemagglutinin / Receptor
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
Hemagglutinin / Hemagglutinin
Similarity search - Component
Biological speciesInfluenza A virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsWu, N.C. / Wilson, I.A.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R56 AI117675 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R56 AI127371 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI114730 United States
CitationJournal: Nat Commun / Year: 2018
Title: A complex epistatic network limits the mutational reversibility in the influenza hemagglutinin receptor-binding site.
Authors: Wu, N.C. / Thompson, A.J. / Xie, J. / Lin, C.W. / Nycholat, C.M. / Zhu, X. / Lerner, R.A. / Paulson, J.C. / Wilson, I.A.
History
DepositionNov 9, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 28, 2018Provider: repository / Type: Initial release
Revision 1.1Apr 11, 2018Group: Data collection / Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._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 1.2Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / 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_nonpoly_scheme / pdbx_struct_assembly_gen / 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 / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 4, 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

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


Theoretical massNumber of molelcules
Total (without water)171,61219
Polymers166,6026
Non-polymers5,01013
Water12,574698
1
A: Hemagglutinin
C: Hemagglutinin
E: Hemagglutinin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,26715
Polymers106,4793
Non-polymers4,78912
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Hemagglutinin
D: Hemagglutinin
F: Hemagglutinin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)60,3454
Polymers60,1233
Non-polymers2211
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area38070 Å2
ΔGint-71 kcal/mol
Surface area57870 Å2
MethodPISA
Unit cell
Length a, b, c (Å)209.273, 131.447, 71.921
Angle α, β, γ (deg.)90.00, 97.88, 90.00
Int Tables number5
Space group name H-MC121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21C
12A
22E
13B
23D
14B
24F
15C
25E
16D
26F

NCS domain segments:

Component-ID: _ / Refine code: _

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11PROPROPROPROAA9 - 3243 - 318
21PROPROPROPROCC9 - 3243 - 318
12PROPROPROPROAA9 - 3243 - 318
22PROPROPROPROEE9 - 3243 - 318
13GLYGLYARGARGBB1 - 1701 - 170
23GLYGLYARGARGDD1 - 1701 - 170
14GLYGLYARGARGBB1 - 1701 - 170
24GLYGLYARGARGFF1 - 1701 - 170
15PROPROGLUGLUCC9 - 3253 - 319
25PROPROGLUGLUEE9 - 3253 - 319
16GLYGLYPHEPHEDD1 - 1711 - 171
26GLYGLYPHEPHEFF1 - 1711 - 171

NCS ensembles :
ID
1
2
3
4
5
6

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Components

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Protein , 2 types, 6 molecules ACEBDF

#1: Protein Hemagglutinin


Mass: 35492.922 Da / Num. of mol.: 3 / Mutation: E190D
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


Mass: 20041.131 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus (strain A/Northern Territory/60/1968 H3N2)
Strain: A/Northern Territory/60/1968 H3N2 / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P03436

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Sugars , 5 types, 12 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.: 2
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.: 2
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 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
#6: 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
#7: 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.: 6
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
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 , 2 types, 699 molecules

#8: Chemical ChemComp-TAM / TRIS(HYDROXYETHYL)AMINOMETHANE


Mass: 163.215 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C7H17NO3 / Comment: pH buffer*YM
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 698 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.94 Å3/Da / Density % sol: 58.17 %
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
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0332 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Nov 29, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 2.2→50 Å / Num. obs: 96961 / % possible obs: 99.4 % / Redundancy: 4.5 % / CC1/2: 1 / Rpim(I) all: 0.05 / Rsym value: 0.1 / Net I/σ(I): 16.3
Reflection shellResolution: 2.2→2.28 Å / Redundancy: 3.2 % / Mean I/σ(I) obs: 1.2 / Num. unique obs: 9442 / CC1/2: 0.71 / Rpim(I) all: 0.44 / Rsym value: 0.71 / % possible all: 97.2

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
HKL-2000712data processing
HKL-2000712data scaling
PHASER2.5.6phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4FNK

4fnk


Resolution: 2.2→50 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.947 / SU B: 11.397 / SU ML: 0.146 / Cross valid method: THROUGHOUT / ESU R: 0.222 / ESU R Free: 0.173 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20934 4791 4.9 %RANDOM
Rwork0.1811 ---
obs0.18247 92139 99.05 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 49.69 Å2
Baniso -1Baniso -2Baniso -3
1--0.12 Å2-0 Å2-0.73 Å2
2--1.66 Å20 Å2
3----1.28 Å2
Refinement stepCycle: 1 / Resolution: 2.2→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11517 0 329 698 12544
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.01912137
X-RAY DIFFRACTIONr_bond_other_d0.0010.0210749
X-RAY DIFFRACTIONr_angle_refined_deg1.4611.96916506
X-RAY DIFFRACTIONr_angle_other_deg0.94325097
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.03951465
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.56624.757576
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.381151975
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.0211570
X-RAY DIFFRACTIONr_chiral_restr0.0830.21856
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213399
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022395
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.9872.7125873
X-RAY DIFFRACTIONr_mcbond_other0.9872.7115871
X-RAY DIFFRACTIONr_mcangle_it1.6584.0627330
X-RAY DIFFRACTIONr_mcangle_other1.6584.0627331
X-RAY DIFFRACTIONr_scbond_it1.613.1036263
X-RAY DIFFRACTIONr_scbond_other1.6083.1036263
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.7824.5919176
X-RAY DIFFRACTIONr_long_range_B_refined5.34453.04448645
X-RAY DIFFRACTIONr_long_range_B_other5.26452.77248175
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION / Type: interatomic distance / Weight position: 0.05

Ens-IDDom-IDAuth asym-IDNumberRms dev position (Å)
11A199940.05
12C199940.05
21A199040.05
22E199040.05
31B105720.05
32D105720.05
41B106120.06
42F106120.06
51C198960.06
52E198960.06
61D107800.05
62F107800.05
LS refinement shellResolution: 2.198→2.255 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.294 312 -
Rwork0.273 6434 -
obs--93.1 %
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)
10.61310.2061-0.02632.48280.31830.2776-0.0152-0.3721-0.00690.2849-0.0096-0.25020.1142-0.07180.02480.065-0.0207-0.02720.31050.00720.0877-20.052622.123635.522
23.2485-0.4011-1.31921.38320.59262.2866-0.28910.1562-0.80510.1118-0.13140.20540.5505-0.49280.42050.2014-0.18620.07330.23740.02650.2967-32.1709-13.292216.9964
30.41850.1544-0.03462.47690.06910.1479-0.0045-0.26960.09990.2314-0.0483-0.05580.0333-0.10720.05280.0675-0.0121-0.02150.3913-0.02730.1494-20.142925.114333.7509
41.75570.56860.57392.59431.39672.1746-0.0189-0.49240.32060.44880.1007-0.17170.0703-0.0243-0.08180.12390.111-0.1060.4013-0.24020.2522-20.860355.014146.321
58.1884-1.4021-5.93192.77272.448412.62390.0405-0.48620.08750.14160.04070.0866-0.2399-0.1289-0.08120.1017-0.0283-0.05160.15330.08520.1283-25.961214.895823.0835
60.39430.01280.02825.24753.69663.0015-0.0753-0.2690.24440.02960.0845-0.0338-0.1009-0.0169-0.00920.05610.0772-0.07380.3039-0.16790.2646-24.951757.766939.9178
73.4533-2.4055-0.70248.66430.64631.0875-0.1038-0.4084-0.15760.61010.06110.38790.0734-0.16350.04260.09650.0966-0.00930.3682-0.07510.0549-44.697154.779738.8193
80.24070.24920.27411.35141.25171.4723-0.0707-0.00410.0689-0.0006-0.11230.28770.0781-0.2370.1830.0575-0.0688-0.05150.30030.01390.2354-54.01188.9633-1.6612
91.77950.16970.33992.2128-0.03852.03670.03640.05440.04130.0822-0.089-0.03190.23850.12980.05260.059-0.0491-0.03080.24030.01750.0935-44.5003-1.9994-6.9274
101.31790.50880.19971.41760.78212.5168-0.0899-0.09870.2055-0.09-0.15850.4928-0.2258-0.26970.24840.03030.0141-0.05080.261-0.02010.2381-52.285827.58912.7559
111.759-0.70580.146812.82667.25394.5715-0.0974-0.26570.10260.65490.03970.30240.2861-0.14050.05760.05530.03090.0320.25830.00380.1356-44.940742.558531.5989
121.462-0.1407-0.00162.6611.56892.3843-0.0439-0.30870.322-0.089-0.14290.2155-0.3287-0.28330.18670.09840.1538-0.04530.3563-0.14550.3234-46.61663.605633.7014
130.38053.18372.638226.655922.086718.3013-0.12740.0215-0.0107-1.13970.2023-0.0745-0.93710.164-0.07490.46460.02370.00760.45760.03270.3374-44.174239.970512.7331
140.4976-0.4052-0.08523.14241.14540.7077-0.1089-0.22520.20810.08170.1210.1276-0.077-0.1582-0.0120.05580.1015-0.01920.2801-0.10680.2537-39.213455.917929.6088
150.4806-0.3754-0.31921.77721.12621.0180.01380.10390.0765-0.17020.0439-0.0847-0.0361-0.0707-0.05770.0423-0.0289-0.01950.18550.05240.0979-17.010922.7613-4.5292
161.75190.26260.62890.72130.18912.1138-0.03430.0113-0.23690.01450.0080.04860.3575-0.15820.02630.1233-0.08830.01550.12980.01360.0985-18.03-4.8487-4.8755
170.8386-0.9939-0.50942.66251.62571.08940.02350.06340.2641-0.18070.1001-0.2074-0.1624-0.0274-0.12360.09920.0224-0.00780.20090.06110.1937-21.065539.14132.9055
181.4054-1.4246-0.03014.91880.35461.22240.0693-0.12720.5156-0.35240.1665-0.4955-0.3758-0.0043-0.23580.13360.00210.06180.0375-0.09450.3757-20.386168.366319.2679
196.91761.39163.35721.06050.56424.4512-0.1419-0.33380.3554-0.0814-0.0229-0.1257-0.42630.11380.16470.1112-0.0317-0.01220.19370.01790.1708-20.971527.03165.9888
201.12211.68030.68827.57693.11831.4978-0.0215-0.0460.20010.00240.09270.0388-0.0713-0.0751-0.07120.08640.04180.00040.20080.01970.1841-29.011844.030616.8922
219.17561.7021.32911.01481.59764.6858-0.10130.06430.8217-0.27920.3001-0.1749-1.00390.1675-0.19880.40950.03070.0420.198-0.1920.595-23.42884.184631.5267
220.8283-0.88011.91574.8323-0.56247.47280.0433-0.11730.1438-0.19330.2728-0.3223-0.6590.7297-0.31610.4836-0.1778-0.01370.4151-0.28640.8406-16.137185.796734.1892
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A9 - 89
2X-RAY DIFFRACTION2A90 - 258
3X-RAY DIFFRACTION3A259 - 329
4X-RAY DIFFRACTION4B1 - 57
5X-RAY DIFFRACTION5B58 - 74
6X-RAY DIFFRACTION6B75 - 172
7X-RAY DIFFRACTION7C9 - 37
8X-RAY DIFFRACTION8C38 - 172
9X-RAY DIFFRACTION9C173 - 260
10X-RAY DIFFRACTION10C261 - 306
11X-RAY DIFFRACTION11C307 - 325
12X-RAY DIFFRACTION12D1 - 54
13X-RAY DIFFRACTION13D55 - 61
14X-RAY DIFFRACTION14D62 - 171
15X-RAY DIFFRACTION15E9 - 155
16X-RAY DIFFRACTION16E156 - 263
17X-RAY DIFFRACTION17E264 - 325
18X-RAY DIFFRACTION18F1 - 56
19X-RAY DIFFRACTION19F57 - 71
20X-RAY DIFFRACTION20F72 - 125
21X-RAY DIFFRACTION21F126 - 145
22X-RAY DIFFRACTION22F146 - 171

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