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- PDB-6twh: Crystal structure of the haemagglutinin mutant (Gln226Leu, Gly228... -

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Basic information

Entry
Database: PDB / ID: 6twh
TitleCrystal structure of the haemagglutinin mutant (Gln226Leu, Gly228Ser) from an H10N7 seal influenza virus isolated in Germany
Components
  • Hemagglutinin
  • Hemagglutinin HA2
KeywordsVIRAL PROTEIN / Host Cell Surface Receptor Binding / Fusion of Virus Membrane with Host Plasma Membrane / Viral Envelope
Function / homology
Function and homology information


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 / metal ion binding / membrane
Similarity search - Function
Hemagglutinin Ectodomain; Chain B - #10 / Hemagglutinin Ectodomain; Chain B / 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: 2.68 Å
AuthorsZhang, J. / Xiong, X. / Purkiss, A. / Walker, P. / Gamblin, S. / Skehel, J.J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
The Francis Crick Institute United Kingdom
CitationJournal: Cell Host Microbe / Year: 2020
Title: Hemagglutinin Traits Determine Transmission of Avian A/H10N7 Influenza Virus between Mammals.
Authors: Herfst, S. / Zhang, J. / Richard, M. / McBride, R. / Lexmond, P. / Bestebroer, T.M. / Spronken, M.I.J. / de Meulder, D. / van den Brand, J.M. / Rosu, M.E. / Martin, S.R. / Gamblin, S.J. / ...Authors: Herfst, S. / Zhang, J. / Richard, M. / McBride, R. / Lexmond, P. / Bestebroer, T.M. / Spronken, M.I.J. / de Meulder, D. / van den Brand, J.M. / Rosu, M.E. / Martin, S.R. / Gamblin, S.J. / Xiong, X. / Peng, W. / Bodewes, R. / van der Vries, E. / Osterhaus, A.D.M.E. / Paulson, J.C. / Skehel, J.J. / Fouchier, R.A.M.
History
DepositionJan 13, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 21, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2Nov 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
B: Hemagglutinin HA2
C: Hemagglutinin
D: Hemagglutinin HA2
E: Hemagglutinin
F: Hemagglutinin HA2
L: Hemagglutinin
M: Hemagglutinin HA2
N: Hemagglutinin
O: Hemagglutinin HA2
P: Hemagglutinin
Q: Hemagglutinin HA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)337,70425
Polymers334,96512
Non-polymers2,73913
Water1,45981
1
A: Hemagglutinin
B: Hemagglutinin HA2
C: Hemagglutinin
D: Hemagglutinin HA2
E: Hemagglutinin
F: Hemagglutinin HA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)169,03512
Polymers167,4836
Non-polymers1,5536
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area33680 Å2
ΔGint-157 kcal/mol
Surface area59170 Å2
MethodPISA
2
L: Hemagglutinin
M: Hemagglutinin HA2
N: Hemagglutinin
O: Hemagglutinin HA2
P: Hemagglutinin
Q: Hemagglutinin HA2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)168,66913
Polymers167,4836
Non-polymers1,1867
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area33860 Å2
ΔGint-172 kcal/mol
Surface area57680 Å2
MethodPISA
Unit cell
Length a, b, c (Å)69.310, 213.610, 156.800
Angle α, β, γ (deg.)90.000, 102.290, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 2 types, 12 molecules ACELNPBDFMOQ

#1: Protein
Hemagglutinin


Mass: 35514.137 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus (A/harbour seal/Germany/1/2014(H10N7))
Gene: HA / Cell line (production host): Sf9 / Production host: unidentified baculovirus / References: UniProt: A0A0A7HR51
#2: Protein
Hemagglutinin HA2


Mass: 20313.389 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus (A/harbour seal/Germany/1/2014(H10N7))
Gene: HA / Cell line (production host): Sf9 / Production host: unidentified baculovirus / References: UniProt: A0A0A7HR51

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Sugars , 2 types, 10 molecules

#3: 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 natural 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
#4: 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.: 8 / Source method: isolated from a natural 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, 84 molecules

#5: Chemical ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Formula: Ca
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 81 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
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: 3.5 Å3/Da / Density % sol: 64.4 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / Details: 6% PEG3350, 0.1 M MES pH6.5

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jan 29, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.68→72.11 Å / Num. obs: 124460 / % possible obs: 99.9 % / Redundancy: 7 % / CC1/2: 0.998 / Net I/σ(I): 8.9
Reflection shellResolution: 2.68→2.75 Å / Num. unique obs: 9164 / CC1/2: 0.627

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
PDB_EXTRACT3.1data extraction
xia2data reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4D00

4d00


Resolution: 2.68→72.11 Å / Cor.coef. Fo:Fc: 0.905 / Cor.coef. Fo:Fc free: 0.907 / Occupancy max: 1 / Occupancy min: 1 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.696 / ESU R Free: 0.364 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
RfactorNum. reflection% reflectionSelection details
Rfree0.3017 6188 5 %RANDOM
Rwork0.269 118236 --
obs0.2706 124424 99.91 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso max: 267.58 Å2 / Biso mean: 91.6135 Å2 / Biso min: 28.08 Å2
Baniso -1Baniso -2Baniso -3
1-0.07 Å20 Å2-0.43 Å2
2--0.48 Å20 Å2
3----0.33 Å2
Refinement stepCycle: LAST / Resolution: 2.68→72.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms22886 0 171 81 23138
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0130.01923546
X-RAY DIFFRACTIONr_bond_other_d00.0220860
X-RAY DIFFRACTIONr_angle_refined_deg1.8181.9431890
X-RAY DIFFRACTIONr_angle_other_deg4.21348651
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.27352928
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.82724.961129
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.76154002
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.3815127
X-RAY DIFFRACTIONr_chiral_restr0.0890.23495
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0226442
X-RAY DIFFRACTIONr_gen_planes_other0.0070.024632
X-RAY DIFFRACTIONr_mcbond_it5.8829.01811757
X-RAY DIFFRACTIONr_mcbond_other5.8829.01811756
X-RAY DIFFRACTIONr_mcangle_it9.15413.52514670
LS refinement shellResolution: 2.68→2.75 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.557 427 -
Rwork0.562 8728 -
all-9155 -
obs--99.91 %

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