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

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Basic information

Entry
Database: PDB / ID: 6nhr
TitleCrystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin HA2 I45F mutant
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 / apical plasma membrane / 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: 2.1 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 2.2Nov 20, 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)171,72419
Polymers166,6566
Non-polymers5,06813
Water15,241846
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area38290 Å2
ΔGint-59 kcal/mol
Surface area57320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)208.378, 131.409, 72.280
Angle α, β, γ (deg.)90.00, 98.07, 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
#2: Protein Hemagglutinin HA2 chain


Mass: 20231.330 Da / Num. of mol.: 3 / Fragment: residues 346-521 / Mutation: I45F
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, 846 molecules

#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 846 / 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: 58.16 %
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: 2.1→50 Å / Num. obs: 110282 / % possible obs: 97.4 % / Redundancy: 5.6 % / CC1/2: 1 / Rpim(I) all: 0.05 / Rsym value: 0.1 / Net I/σ(I): 20
Reflection shellResolution: 2.1→2.2 Å / Redundancy: 5.2 % / Mean I/σ(I) obs: 1.7 / Num. unique obs: 13871 / CC1/2: 0.77 / Rpim(I) all: 0.4 / Rsym value: 0.83 / % possible all: 98.1

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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: 2.1→50 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.949 / SU B: 9.6 / SU ML: 0.129 / Cross valid method: THROUGHOUT / ESU R: 0.195 / ESU R Free: 0.163 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21614 5420 5 %RANDOM
Rwork0.18432 ---
obs0.18588 103850 97.38 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 48.81 Å2
Baniso -1Baniso -2Baniso -3
1-1.09 Å2-0 Å20.87 Å2
2--0.32 Å20 Å2
3----1.59 Å2
Refinement stepCycle: 1 / Resolution: 2.1→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11529 0 332 846 12707
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.01912170
X-RAY DIFFRACTIONr_bond_other_d0.0020.0210756
X-RAY DIFFRACTIONr_angle_refined_deg1.4971.96916553
X-RAY DIFFRACTIONr_angle_other_deg0.941325114
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.95151467
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.28424.724580
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.553151976
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.4141570
X-RAY DIFFRACTIONr_chiral_restr0.0860.21857
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0213451
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022418
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_it0.9942.675877
X-RAY DIFFRACTIONr_mcbond_other0.9942.675876
X-RAY DIFFRACTIONr_mcangle_it1.6143.9997338
X-RAY DIFFRACTIONr_mcangle_other1.61347339
X-RAY DIFFRACTIONr_scbond_it1.6183.0556292
X-RAY DIFFRACTIONr_scbond_other1.6183.0556293
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.754.5229215
X-RAY DIFFRACTIONr_long_range_B_refined5.42352.40149508
X-RAY DIFFRACTIONr_long_range_B_other5.32652.14849025
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)
11A202240.05
12C202240.05
21A200180.07
22E200180.07
31B107200.06
32D107200.06
41B107160.06
42F107160.06
51C200620.07
52E200620.07
61D109120.05
62F109120.05
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.289 404 -
Rwork0.267 7726 -
obs--98.19 %
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)
11.03250.06770.01111.63520.31190.5126-0.0418-0.2316-0.30890.0798-0.0398-0.01250.2116-0.13980.08160.1486-0.0640.02710.23190.08350.123-26.36650.730125.8376
216.7845-1.9963-0.34911.36270.56022.24330.03610.2109-0.2809-0.1919-0.14540.05760.09-0.34170.10930.2998-0.0806-0.01310.16010.0270.1646-29.0783-11.87579.7288
30.85170.38810.12131.48580.19110.3416-0.0313-0.20770.02670.0996-0.02670.03010.0591-0.17430.0580.0618-0.0211-0.00460.26040.020.0319-25.546115.017929.1594
42.64420.70420.67051.02521.30076.4055-0.0638-0.28680.37730.25490.0264-0.1903-0.2698-0.04460.03730.18860.0706-0.15430.2088-0.20420.2672-16.488260.730448.1441
54.52425.72673.276212.67849.10169.78460.1243-0.2625-0.03980.8348-0.0771-0.14490.4245-0.2117-0.04720.13970.0939-0.06680.2759-0.05710.1066-28.13244.412243.9112
68.1409-1.2937-6.37122.67992.078911.2102-0.0692-0.27790.06940.16340.0760.02760.1315-0.0223-0.00680.0677-0.0133-0.03970.15390.0420.0726-25.423614.074321.6652
70.4059-0.1777-0.01753.32312.212.0918-0.1095-0.23510.26430.13220.1333-0.1324-0.1822-0.0427-0.02370.14950.1044-0.09720.2565-0.16250.2123-25.077557.728540.3109
80.42740.48130.2962.05091.4291.4536-0.0783-0.12710.0332-0.0285-0.08180.37330.0225-0.36730.16010.04320.0212-0.04210.33530.0140.1933-52.053225.484813.922
91.1499-0.07670.62922.8066-1.36173.74620.03780.04890.0578-0.3696-0.3422-0.13870.58610.33660.30440.1553-0.02050.01310.21870.06130.1152-47.0424-2.365-9.3551
100.54160.31950.4271.81341.28371.1578-0.0863-0.14750.0652-0.0614-0.05040.3498-0.0969-0.23870.13670.07950.0348-0.02410.30270.01380.1984-49.7831.541817.6086
111.5634-0.3528-0.82553.24251.89663.6713-0.0569-0.33980.3155-0.0327-0.13080.3001-0.4205-0.5210.18760.16490.2252-0.0780.3618-0.1560.2842-46.582462.811633.5589
120.01110.10870.036339.158323.146213.97350.04580.0745-0.0088-1.32750.0777-0.4989-0.6182-0.4965-0.12350.6755-0.20390.03141.1418-0.11360.5049-44.031640.524513.2359
130.4746-0.16870.03622.29180.82150.8743-0.1375-0.21620.24850.09190.07970.1944-0.2273-0.24680.05770.14330.1583-0.05580.2758-0.10910.2322-39.286955.414529.5769
140.5314-0.3905-0.27281.3810.86741.01580.02350.11840.0772-0.14460.0024-0.0651-0.037-0.0851-0.0260.0308-0.0186-0.01310.13220.04270.0589-16.950522.9821-4.4738
151.76440.07550.34830.65630.15061.7707-0.03160.0329-0.30420.0205-0.00990.07710.317-0.13520.04140.1228-0.07050.01980.08560.00110.0776-17.9791-4.4868-4.911
160.7996-0.8689-0.41582.14361.25571.22460.01010.05090.2313-0.18160.0851-0.1162-0.2347-0.0187-0.09520.08040.008-0.01020.10060.03860.1353-21.023739.24253.0336
170.939-0.6019-0.05914.0492-0.01511.21430.0382-0.04960.4405-0.41240.0433-0.3835-0.52070.0349-0.08150.28890.00730.0020.04-0.0860.345-20.476268.124419.6001
185.25753.12641.04454.05761.76732.0232-0.1147-0.12950.0954-0.19420.0639-0.038-0.27490.0320.05070.1133-0.01750.00110.18650.00990.0499-21.684926.49235.2466
190.60960.64330.38033.70281.68121.3381-0.0689-0.06940.3465-0.03250.1233-0.1098-0.3507-0.0911-0.05450.23920.0888-0.03470.1119-0.08290.3297-24.554763.132924.9105
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A9 - 200
2X-RAY DIFFRACTION2A201 - 231
3X-RAY DIFFRACTION3A232 - 329
4X-RAY DIFFRACTION4B1 - 35
5X-RAY DIFFRACTION5B36 - 58
6X-RAY DIFFRACTION6B59 - 75
7X-RAY DIFFRACTION7B76 - 172
8X-RAY DIFFRACTION8C9 - 119
9X-RAY DIFFRACTION9C120 - 258
10X-RAY DIFFRACTION10C259 - 325
11X-RAY DIFFRACTION11D1 - 55
12X-RAY DIFFRACTION12D56 - 60
13X-RAY DIFFRACTION13D61 - 171
14X-RAY DIFFRACTION14E9 - 155
15X-RAY DIFFRACTION15E156 - 263
16X-RAY DIFFRACTION16E264 - 325
17X-RAY DIFFRACTION17F1 - 56
18X-RAY DIFFRACTION18F57 - 72
19X-RAY DIFFRACTION19F73 - 171

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