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- PDB-5vtu: Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza viru... -

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Basic information

Entry
Database: PDB / ID: 5vtu
TitleCrystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin G225L/L226S mutant apo form
Components(Hemagglutinin ...) x 2
KeywordsVIRAL PROTEIN / Influenza A virus / hemagglutinin / mutant / receptor binding
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
Biological speciesInfluenza A virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.45 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 AI117675 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01 AI114730 United States
CitationJournal: Cell Host Microbe / Year: 2017
Title: Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin.
Authors: Wu, N.C. / Xie, J. / Zheng, T. / Nycholat, C.M. / Grande, G. / Paulson, J.C. / Lerner, R.A. / Wilson, I.A.
History
DepositionMay 18, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 28, 2017Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
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 2.2Oct 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)171,62218
Polymers166,7346
Non-polymers4,88812
Water4,936274
1
A: Hemagglutinin HA1 chain
B: Hemagglutinin HA2 chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,0316
Polymers55,5782
Non-polymers1,4534
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7230 Å2
ΔGint-15 kcal/mol
Surface area24290 Å2
MethodPISA
2
C: Hemagglutinin HA1 chain
D: Hemagglutinin HA2 chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)56,9725
Polymers55,5782
Non-polymers1,3943
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6970 Å2
ΔGint-16 kcal/mol
Surface area24210 Å2
MethodPISA
3
E: Hemagglutinin HA1 chain
F: Hemagglutinin HA2 chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,6187
Polymers55,5782
Non-polymers2,0405
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7860 Å2
ΔGint-8 kcal/mol
Surface area24680 Å2
MethodPISA
4


  • Idetical with deposited unit
  • defined by software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area37760 Å2
ΔGint-71 kcal/mol
Surface area57480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)205.554, 129.392, 72.894
Angle α, β, γ (deg.)90.00, 102.66, 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
11GLYGLYPROPROAA10 - 3244 - 318
21GLYGLYPROPROCC10 - 3244 - 318
12PROPROGLUGLUAA9 - 3253 - 319
22PROPROGLUGLUEE9 - 3253 - 319
13GLYGLYARGARGBB1 - 1701 - 170
23GLYGLYARGARGDD1 - 1701 - 170
14GLYGLYARGARGBB1 - 1701 - 170
24GLYGLYARGARGFF1 - 1701 - 170
15GLYGLYPROPROCC10 - 3244 - 318
25GLYGLYPROPROEE10 - 3244 - 318
16GLYGLYPHEPHEDD1 - 1711 - 171
26GLYGLYPHEPHEFF1 - 1711 - 171

NCS ensembles :
ID
6
1
2
3
4
5

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Components

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Hemagglutinin ... , 2 types, 6 molecules ACEBDF

#1: Protein Hemagglutinin HA1 chain


Mass: 35536.973 Da / Num. of mol.: 3
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: 20041.131 Da / Num. of mol.: 3
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, 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.: 1
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.: 4
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.: 5
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, 274 molecules

#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 274 / 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: 2.84 Å3/Da / Density % sol: 56.63 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.2 M potassium nitrate and 20% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.0331 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 15, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0331 Å / Relative weight: 1
ReflectionResolution: 2.45→50 Å / Num. obs: 66821 / % possible obs: 98 % / Redundancy: 6.3 % / CC1/2: 1 / Rpim(I) all: 0.04 / Rsym value: 0.1 / Net I/σ(I): 18.2
Reflection shellResolution: 2.45→2.53 Å / Redundancy: 4.4 % / Mean I/σ(I) obs: 1.6 / Num. unique obs: 5155 / CC1/2: 0.81 / Rpim(I) all: 0.26 / Rsym value: 0.52 / % possible all: 83.3

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Processing

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

4fnk


Resolution: 2.45→50 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.935 / SU B: 19.057 / SU ML: 0.206 / Cross valid method: THROUGHOUT / ESU R: 0.444 / ESU R Free: 0.241 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21956 3348 5 %RANDOM
Rwork0.19799 ---
obs0.19913 63464 97.89 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 61.35 Å2
Baniso -1Baniso -2Baniso -3
1-2.03 Å20 Å22.88 Å2
2---2.03 Å20 Å2
3----1.17 Å2
Refinement stepCycle: 1 / Resolution: 2.45→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11483 0 321 274 12078
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0090.01912088
X-RAY DIFFRACTIONr_bond_other_d0.0010.0211090
X-RAY DIFFRACTIONr_angle_refined_deg1.4331.96816430
X-RAY DIFFRACTIONr_angle_other_deg0.917325587
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.9451458
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.9624.774574
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.982151967
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.4281569
X-RAY DIFFRACTIONr_chiral_restr0.080.21851
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0213673
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022784
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_it1.0813.5365848
X-RAY DIFFRACTIONr_mcbond_other1.0813.5365847
X-RAY DIFFRACTIONr_mcangle_it1.7925.3017301
X-RAY DIFFRACTIONr_mcangle_other1.7925.3017302
X-RAY DIFFRACTIONr_scbond_it1.6733.9026238
X-RAY DIFFRACTIONr_scbond_other1.6733.9036239
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.7555.8039129
X-RAY DIFFRACTIONr_long_range_B_refined5.43268.59947735
X-RAY DIFFRACTIONr_long_range_B_other5.42468.57547673
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)
11A198740.05
12C198740.05
21A199260.06
22E199260.06
31B106120.04
32D106120.04
41B106040.04
42F106040.04
51C199420.05
52E199420.05
61D107020.05
62F107020.05
LS refinement shellResolution: 2.451→2.515 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.324 172 -
Rwork0.29 3927 -
obs--80.94 %
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)
10.44280.344-0.21282.1084-0.09620.72970.0555-0.07180.08060.1272-0.07580.2565-0.2061-0.17240.02030.130.02050.06250.3134-0.0660.0918-3.7337-14.647190.3641
22.36550.12290.64591.855-0.37982.6420.02810.07270.4269-0.0035-0.1588-0.0968-0.51250.27350.13070.3868-0.07790.10830.1512-0.04330.14814.360415.173579.1454
30.29260.1195-0.4742.7449-0.17830.9471-0.0026-0.0349-0.06220.0105-0.07250.2041-0.0871-0.15710.07510.11880.02430.03180.3645-0.02610.1615-4.4967-22.360191.5479
410.4217-1.063-4.17283.02051.01317.22070.05410.3476-0.29110.08170.00010.33480.6-0.5274-0.05420.2646-0.07890.05030.3147-0.00940.2288-13.7751-59.369696.0231
50.4195-1.6556-0.78466.55813.13221.6176-0.07460.0551-0.11030.4205-0.22870.47260.3368-0.35040.30340.4726-0.18590.13420.567-0.02620.3295-16.5654-57.3359107.3963
66.55267.3671-2.427810.3765-3.10582.73940.2493-0.4321-0.1020.6725-0.41110.11240.0862-0.13420.16180.2672-0.01610.07020.2932-0.02450.1787-8.3664-50.6421106.435
71.08691.03420.10831.1956-0.89585.3578-0.0285-0.2796-0.08470.0233-0.1223-0.11790.0397-0.38040.15080.28120.0720.06980.4639-0.00180.25433.898-17.583487.2359
80.90821.4051-0.84874.4487-2.52192.48190.0049-0.1557-0.15540.2768-0.06510.04770.1466-0.19830.06010.1535-0.0330.06740.287-0.01220.1539-3.4646-48.322292.2757
94.8943-2.64220.93056.1918-0.57591.0052-0.22-0.4617-0.1770.7680.0285-0.18610.3007-0.04320.19140.6951-0.25390.13460.46440.20780.2643-10.386-75.3539115.0349
100.55960.6368-0.39931.4399-0.62450.8050.0204-0.1978-0.1190.0114-0.126-0.2922-0.03010.25770.10560.0508-0.03320.04370.2734-0.01660.193534.3457-17.644276.0005
111.1101-0.4769-0.09873.42910.55762.19680.1102-0.0215-0.0465-0.1272-0.1810.1124-0.2273-0.15190.07080.1348-0.06110.08720.2778-0.05430.209931.70820.544261.2779
120.60960.5365-0.04242.1648-0.63291.2227-0.0271-0.2291-0.17020.1527-0.0666-0.37740.02980.28280.09370.08330.00850.0090.30760.04620.214626.9524-32.763486.771
134.6762-0.5394-0.25514.48890.95323.28910.1803-0.5817-0.89980.6452-0.2219-0.32930.5523-0.0490.04150.4083-0.02290.00650.3620.20590.263814.0824-64.0601105.4452
142.0281-0.54940.714811.4613-7.4367.4443-0.0099-0.2656-0.30580.0773-0.1029-0.2940.32850.04210.11280.22290.02590.00580.29310.01090.347419.6085-61.964794.7277
153.543-0.6827-0.51351.62071.54984.448-0.0869-0.2055-0.14370.08440.0443-0.22770.08090.33470.04260.171-0.03250.02230.28740.01780.184619.2086-19.505179.6787
160.40860.7045-0.25066.9231-2.59551.5101-0.0585-0.1705-0.21290.13490.10230.14350.2758-0.1224-0.04380.2713-0.01430.03060.30740.05540.27839.0646-55.477193.9866
170.26870.365-0.0240.5212-0.05960.04260.3575-0.3795-0.35950.5138-0.4693-0.51910.03870.01320.11181.359-0.2039-0.01560.71890.57340.871210.4251-79.6035108.1103
184.22152.7381-2.24883.679-0.14417.91840.06910.0377-0.36790.3584-0.1258-0.39750.4004-0.32310.05670.53130.0296-0.00970.13930.2280.50629.0504-86.1017102.2417
190.26040.0407-0.17371.3937-0.75861.0350.01540.0312-0.004-0.14910.02180.1119-0.0908-0.067-0.03720.12870.00430.01550.2164-0.05250.09383.3564-18.336454.4478
206.5367-2.57144.571810.85470.69244.92170.10960.2960.3798-0.0788-0.1171-0.2899-0.2120.26580.00740.3228-0.08230.03050.1920.01490.221117.334810.988947.8174
213.1095-0.2375-0.97521.63360.79991.79210.0384-0.21890.17780.0445-0.0367-0.0333-0.35150.1162-0.00170.3515-0.00360.03310.1717-0.06060.08318.84152.893255.8634
220.09070.1494-0.23353.1878-1.61131.615-0.05080.0071-0.0995-0.18110.03010.15180.141-0.08730.02070.1511-0.00150.01960.2531-0.04050.18223.1977-34.916962.0389
232.70051.5243-0.14454.4160.54122.1369-0.0230.0749-0.4879-0.1332-0.0657-0.05780.6416-0.22420.08880.3731-0.02130.11960.1622-0.0150.2242-1.4666-74.534379.1167
245.29854.8486-0.398418.0345-1.46394.6308-0.0810.08160.11770.02760.23060.37420.0464-0.1698-0.14960.20230.01940.0130.3232-0.0240.2313-6.6018-53.964476.9223
259.30612.34370.7973.1441.31272.43810.01290.1101-0.15310.0012-0.05860.10060.016-0.24110.04570.24360.0454-0.01840.2308-0.01120.16297.9138-24.3664.6825
261.26512.1943-0.66854.1928-0.87540.82240.0107-0.1139-0.14840.1856-0.1723-0.03020.3251-0.03750.16160.3204-0.03510.08530.2595-0.00220.2742-1.5917-64.303385.367
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A9 - 120
2X-RAY DIFFRACTION2A121 - 258
3X-RAY DIFFRACTION3A259 - 325
4X-RAY DIFFRACTION4B1 - 16
5X-RAY DIFFRACTION5B17 - 27
6X-RAY DIFFRACTION6B28 - 56
7X-RAY DIFFRACTION7B57 - 71
8X-RAY DIFFRACTION8B72 - 145
9X-RAY DIFFRACTION9B146 - 172
10X-RAY DIFFRACTION10C10 - 170
11X-RAY DIFFRACTION11C171 - 258
12X-RAY DIFFRACTION12C259 - 325
13X-RAY DIFFRACTION13D1 - 27
14X-RAY DIFFRACTION14D28 - 57
15X-RAY DIFFRACTION15D58 - 86
16X-RAY DIFFRACTION16D87 - 131
17X-RAY DIFFRACTION17D132 - 149
18X-RAY DIFFRACTION18D150 - 171
19X-RAY DIFFRACTION19E9 - 182
20X-RAY DIFFRACTION20E183 - 201
21X-RAY DIFFRACTION21E202 - 254
22X-RAY DIFFRACTION22E255 - 325
23X-RAY DIFFRACTION23F1 - 38
24X-RAY DIFFRACTION24F39 - 57
25X-RAY DIFFRACTION25F58 - 75
26X-RAY DIFFRACTION26F76 - 171

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