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

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Basic information

Entry
Database: PDB / ID: 6nhp
TitleCrystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin HA2 I45T mutant
Components(Hemagglutinin ...) x 2
KeywordsVIRAL PROTEIN / influenza virus / hemagglutinin
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: 2.25 Å
AuthorsWu, N.C. / Wilson, I.A.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R56 AI127371 United States
CitationJournal: Science / Year: 2020
Title: Different genetic barriers for resistance to HA stem antibodies in influenza H3 and H1 viruses.
Authors: Wu, N.C. / Thompson, A.J. / Lee, J.M. / Su, W. / Arlian, B.M. / Xie, J. / Lerner, R.A. / Yen, H.L. / Bloom, J.D. / Wilson, I.A.
History
DepositionDec 23, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 15, 2020Provider: repository / Type: Initial release
Revision 1.1Jun 17, 2020Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Jul 1, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
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 / _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 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 2.2Oct 23, 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 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)171,58619
Polymers166,5186
Non-polymers5,06813
Water11,998666
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area38340 Å2
ΔGint-60 kcal/mol
Surface area57320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)209.212, 131.146, 72.176
Angle α, β, γ (deg.)90.00, 98.15, 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 - 3241 - 316
21PROPROPROPROCC9 - 3241 - 316
12PROPROPROPROAA9 - 3241 - 316
22PROPROPROPROEE9 - 3241 - 316
13GLYGLYARGARGBB1 - 1701 - 170
23GLYGLYARGARGDD1 - 1701 - 170
14GLYGLYARGARGBB1 - 1701 - 170
24GLYGLYARGARGFF1 - 1701 - 170
15PROPROGLUGLUCC9 - 3251 - 317
25PROPROGLUGLUEE9 - 3251 - 317
16GLYGLYPHEPHEDD1 - 1711 - 171
26GLYGLYPHEPHEFF1 - 1711 - 171

NCS ensembles :
ID
1
2
3
4
5
6

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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: H9XC94, UniProt: Q91MA7*PLUS
#2: Protein Hemagglutinin HA2 chain


Mass: 20185.260 Da / Num. of mol.: 3 / Fragment: residues 346-521 / Mutation: I45T
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

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Sugars , 5 types, 13 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.: 7
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 , 1 types, 666 molecules

#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 666 / 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: 58.21 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1 M sodium cacodylate pH 6.5, 5% PEG 8000, and 38% 2-methyl-2,4-pentanediol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Mar 2, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.25→50 Å / Num. obs: 89621 / % possible obs: 97.4 % / Redundancy: 5 % / Biso Wilson estimate: 38 Å2 / CC1/2: 1 / Rpim(I) all: 0.04 / Rsym value: 0.09 / Net I/σ(I): 16.2
Reflection shellResolution: 2.25→2.35 Å / Redundancy: 4.7 % / Mean I/σ(I) obs: 1.3 / Num. unique obs: 10991 / CC1/2: 0.68 / Rpim(I) all: 0.49 / Rsym value: 0.94 / % possible all: 95.7

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Processing

Software
NameVersionClassification
REFMAC5.8.0155refinement
HKL-2000712data scaling
PHASER2.5.6phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4FNK

4fnk


Resolution: 2.25→50 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.952 / SU B: 11.97 / SU ML: 0.149 / Cross valid method: THROUGHOUT / ESU R: 0.253 / ESU R Free: 0.184 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.20759 4390 4.9 %RANDOM
Rwork0.18186 ---
obs0.18313 84488 97.36 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 50.917 Å2
Baniso -1Baniso -2Baniso -3
1-1.33 Å20 Å20.56 Å2
2---0.7 Å20 Å2
3----0.76 Å2
Refinement stepCycle: 1 / Resolution: 2.25→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11517 0 332 666 12515
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01912135
X-RAY DIFFRACTIONr_bond_other_d0.0020.0210726
X-RAY DIFFRACTIONr_angle_refined_deg1.5451.96916506
X-RAY DIFFRACTIONr_angle_other_deg0.958325045
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.10151463
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.59824.757576
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.503151971
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.1341570
X-RAY DIFFRACTIONr_chiral_restr0.0850.21858
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0213402
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_it1.1182.9165870
X-RAY DIFFRACTIONr_mcbond_other1.1182.9155869
X-RAY DIFFRACTIONr_mcangle_it1.8454.3687327
X-RAY DIFFRACTIONr_mcangle_other1.8454.3687328
X-RAY DIFFRACTIONr_scbond_it1.7933.3446264
X-RAY DIFFRACTIONr_scbond_other1.7933.3456265
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other3.0774.959180
X-RAY DIFFRACTIONr_long_range_B_refined5.5457.07149061
X-RAY DIFFRACTIONr_long_range_B_other5.49256.92748697
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)
11A201060.06
12C201060.06
21A198420.08
22E198420.08
31B106540.05
32D106540.05
41B106520.06
42F106520.06
51C200000.06
52E200000.06
61D108240.05
62F108240.05
LS refinement shellResolution: 2.25→2.308 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.349 293 -
Rwork0.327 6024 -
obs--94.5 %
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)
10.6495-0.01650.01762.98120.06170.0211-0.0507-0.31120.25670.42970.0684-0.33690.0394-0.0541-0.01770.164-0.0055-0.12930.2957-0.10370.1758-16.431740.799338.8261
22.9102-0.4928-1.02341.25440.60031.8008-0.13080.0294-0.80860.0641-0.14130.17830.371-0.32250.27210.1765-0.1319-0.02430.1440.0610.2897-30.8802-11.394919.2838
30.53190.28410.18411.59610.17510.274-0.0063-0.31150.12350.2153-0.0647-0.03930.0276-0.12270.0710.0906-0.0196-0.06590.2717-0.02330.0997-20.255525.03533.8455
41.99070.90880.61162.63971.1041.5274-0.0443-0.33770.30240.50830.1076-0.26510.07610.0038-0.06330.20420.1202-0.19110.3278-0.22820.2568-21.266154.202446.2495
58.0741-1.5187-6.71662.79072.923910.1631-0.0402-0.46750.04490.06930.12030.06590.02210.1491-0.08010.1071-0.0212-0.07370.13230.07210.0885-25.530814.073921.6775
60.3733-0.2357-0.10713.61842.34432.1038-0.1061-0.25890.26670.20550.1059-0.1049-0.0895-0.00770.00010.14290.0734-0.12910.2551-0.17230.255-25.075957.713740.233
73.2746-1.6891-0.61987.18530.20551.7669-0.0789-0.4135-0.12640.40080.17060.40790.0562-0.2775-0.09180.13190.1086-0.02690.3747-0.06630.0745-44.725354.570838.732
80.15290.39240.18771.99411.19151.5075-0.0739-0.0380.0429-0.1467-0.1220.31060.0389-0.2340.1960.1001-0.0731-0.10780.28830.02470.2607-54.68019.0335-0.4054
91.0715-0.25930.68152.4379-0.64573.19210.00030.09820.032-0.0489-0.311-0.25110.14250.42630.31070.0549-0.0523-0.03730.23940.09310.1666-44.259-1.9731-8.3398
100.39670.17180.13221.97011.11450.9386-0.098-0.09990.0632-0.0743-0.05020.4228-0.0508-0.2470.14820.08040.0048-0.07760.24830.01180.2168-49.783631.581717.4777
111.9284-0.2345-0.06911.65171.08882.2517-0.0639-0.38660.38730.0378-0.0764-0.0154-0.2565-0.24320.14030.14130.1494-0.07910.2385-0.1360.2083-46.506363.444433.6177
120.38163.3092.757629.013324.179920.1536-0.10520.0205-0.0153-1.25360.1753-0.0849-1.04570.1176-0.07010.403-0.00020.01990.43120.03790.3095-43.920539.809312.8356
130.5139-0.32440.00922.63720.9320.732-0.1248-0.22070.23160.11540.10510.1541-0.1088-0.15350.01970.1170.1004-0.0680.2138-0.10270.2352-39.099455.726229.6327
140.5462-0.3813-0.30531.56850.88310.88770.02250.11040.0917-0.13970.036-0.093-0.021-0.0693-0.05860.0682-0.0268-0.04780.1370.0540.0883-16.954222.8206-4.4765
151.85670.23680.30090.8540.01731.7178-0.04960.032-0.20190.04920.03120.10240.3271-0.12640.01840.1416-0.0618-0.02780.08110.01340.0868-17.8918-4.3821-4.6398
160.6069-0.6615-0.42291.84691.18070.93090.03450.10680.2351-0.19670.0361-0.0995-0.1754-0.066-0.07060.08150.0028-0.03780.09520.05840.1519-21.243339.41892.8932
171.19350.2554-0.07742.77040.9121.7862-0.0555-0.03920.6178-0.33980.2628-0.4698-0.43530.0777-0.20720.1728-0.0269-0.00760.0343-0.08360.4873-19.950165.912219.0796
180.48170.00270.02251.24170.71410.7373-0.0499-0.01870.3015-0.11710.09610.0214-0.1716-0.0855-0.04620.12160.0346-0.05680.1151-0.01390.2612-26.796650.085218.452
191.493-0.1703-2.05522.62541.01949.87470.1341-0.29490.4738-0.08620.1503-0.3724-0.79240.5814-0.28440.4453-0.0734-0.08110.098-0.20480.692-16.0585.281634.5263
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A9 - 56
2X-RAY DIFFRACTION2A57 - 258
3X-RAY DIFFRACTION3A259 - 329
4X-RAY DIFFRACTION4B1 - 58
5X-RAY DIFFRACTION5B59 - 75
6X-RAY DIFFRACTION6B76 - 172
7X-RAY DIFFRACTION7C9 - 37
8X-RAY DIFFRACTION8C38 - 163
9X-RAY DIFFRACTION9C164 - 258
10X-RAY DIFFRACTION10C259 - 325
11X-RAY DIFFRACTION11D1 - 54
12X-RAY DIFFRACTION12D55 - 61
13X-RAY DIFFRACTION13D62 - 171
14X-RAY DIFFRACTION14E9 - 155
15X-RAY DIFFRACTION15E156 - 264
16X-RAY DIFFRACTION16E265 - 325
17X-RAY DIFFRACTION17F1 - 60
18X-RAY DIFFRACTION18F61 - 145
19X-RAY DIFFRACTION19F146 - 171

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