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- PDB-4fnk: Crystal structure of the A/Hong Kong/1/1968 (H3N2) influenza viru... -

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Basic information

Entry
Database: PDB / ID: 4fnk
TitleCrystal structure of the A/Hong Kong/1/1968 (H3N2) influenza virus hemagglutinin
Components(Hemagglutinin ...) x 2
KeywordsVIRAL PROTEIN / viral fusion protein / virus attachment and entry
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: 1.901 Å
AuthorsEkiert, D.C. / Wilson, I.A.
CitationJournal: Nature / Year: 2012
Title: Cross-neutralization of influenza A viruses mediated by a single antibody loop.
Authors: Damian C Ekiert / Arun K Kashyap / John Steel / Adam Rubrum / Gira Bhabha / Reza Khayat / Jeong Hyun Lee / Michael A Dillon / Ryann E O'Neil / Aleksandr M Faynboym / Michael Horowitz / ...Authors: Damian C Ekiert / Arun K Kashyap / John Steel / Adam Rubrum / Gira Bhabha / Reza Khayat / Jeong Hyun Lee / Michael A Dillon / Ryann E O'Neil / Aleksandr M Faynboym / Michael Horowitz / Lawrence Horowitz / Andrew B Ward / Peter Palese / Richard Webby / Richard A Lerner / Ramesh R Bhatt / Ian A Wilson /
Abstract: Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the size and shape of protein surfaces that ...Immune recognition of protein antigens relies on the combined interaction of multiple antibody loops, which provide a fairly large footprint and constrain the size and shape of protein surfaces that can be targeted. Single protein loops can mediate extremely high-affinity binding, but it is unclear whether such a mechanism is available to antibodies. Here we report the isolation and characterization of an antibody called C05, which neutralizes strains from multiple subtypes of influenza A virus, including H1, H2 and H3. X-ray and electron microscopy structures show that C05 recognizes conserved elements of the receptor-binding site on the haemagglutinin surface glycoprotein. Recognition of the haemagglutinin receptor-binding site is dominated by a single heavy-chain complementarity-determining region 3 loop, with minor contacts from heavy-chain complementarity-determining region 1, and is sufficient to achieve nanomolar binding with a minimal footprint. Thus, binding predominantly with a single loop can allow antibodies to target small, conserved functional sites on otherwise hypervariable antigens.
History
DepositionJun 19, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 19, 2012Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2012Group: Database references
Revision 1.2Oct 10, 2012Group: Database references
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / 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 / pdbx_struct_special_symmetry / struct_asym / struct_conn / struct_ref_seq_dif / 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.occupancy / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_special_symmetry.label_asym_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 13, 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
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Nov 6, 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 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)173,74630
Polymers166,6446
Non-polymers7,10124
Water30,7521707
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area41460 Å2
ΔGint-137 kcal/mol
Surface area57230 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.149, 151.458, 347.751
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11D-515-

HOH

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Components

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Hemagglutinin ... , 2 types, 6 molecules ACEBDF

#1: Protein Hemagglutinin HA1 chain / Hemagglutinin receptor binding subunit HA1


Mass: 35506.949 Da / Num. of mol.: 3 / Fragment: UNP residues 27-345
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Hong Kong/1/1968 H3N2 / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): High Five / References: UniProt: Q91MA7
#2: Protein Hemagglutinin HA2 chain / Hemagglutinin fusion subunit HA2


Mass: 20041.131 Da / Num. of mol.: 3 / Fragment: UNP residues 346-519
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Hong Kong/1/1968 H3N2 / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / Strain (production host): High Five / References: UniProt: Q91MA7

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Sugars , 5 types, 16 molecules

#3: 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
#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.: 6
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 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
#6: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[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: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+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 , 3 types, 1715 molecules

#8: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: SO4
#9: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1707 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY
Sequence detailsHEMAGGLUTININ HA2 RESIDUE GLY 468 IS CORRECT (ALSO PRESENT IN PDB ENTRIES 3SDY AND 4FQL).

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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: 4.15 Å3/Da / Density % sol: 70.39 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 2.0 M ammonium sulfate, 100 mM sodium cacodylate, pH 6.5, 200 mM sodium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL11-1 / Wavelength: 1.066 Å
DetectorType: MARMOSAIC 325 mm CCD / Detector: CCD / Date: Jul 17, 2009
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.066 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 215875 / % possible obs: 99.6 % / Observed criterion σ(I): -3 / Redundancy: 6.3 % / Rsym value: 0.15 / Net I/σ(I): 14.1
Reflection shellResolution: 1.9→1.97 Å / Redundancy: 3.6 % / Mean I/σ(I) obs: 1.8 / Rsym value: 0.65 / % possible all: 97.3

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Processing

Software
NameVersionClassification
Blu-Icedata collection
PHASERphasing
PHENIX(phenix.refine: 1.7.2_869)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2VIU

2viu


Resolution: 1.901→43.064 Å / SU ML: 0.5 / σ(F): 1.33 / Phase error: 16.81 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1885 10817 5.02 %
Rwork0.1616 --
obs0.1629 215391 99.42 %
Solvent computationShrinkage radii: 0.73 Å / VDW probe radii: 1 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 60.124 Å2 / ksol: 0.4 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1-2.5338 Å2-0 Å20 Å2
2---4.5309 Å20 Å2
3---1.9971 Å2
Refinement stepCycle: LAST / Resolution: 1.901→43.064 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11502 0 458 1707 13667
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01412805
X-RAY DIFFRACTIONf_angle_d1.42217463
X-RAY DIFFRACTIONf_dihedral_angle_d19.7794849
X-RAY DIFFRACTIONf_chiral_restr0.0881967
X-RAY DIFFRACTIONf_plane_restr0.0072252
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.9012-1.92280.2943550.27696431X-RAY DIFFRACTION94
1.9228-1.94540.2743540.25786601X-RAY DIFFRACTION97
1.9454-1.96920.2553490.23726700X-RAY DIFFRACTION99
1.9692-1.99410.24043880.21646723X-RAY DIFFRACTION99
1.9941-2.02030.22563360.20476763X-RAY DIFFRACTION99
2.0203-2.0480.20413760.19046774X-RAY DIFFRACTION100
2.048-2.07730.21133870.18436718X-RAY DIFFRACTION100
2.0773-2.10830.22583360.1776831X-RAY DIFFRACTION100
2.1083-2.14120.19233380.16816819X-RAY DIFFRACTION100
2.1412-2.17630.19553400.16376770X-RAY DIFFRACTION100
2.1763-2.21380.19973730.16216782X-RAY DIFFRACTION100
2.2138-2.25410.19273580.15876797X-RAY DIFFRACTION100
2.2541-2.29740.19033490.15436833X-RAY DIFFRACTION100
2.2974-2.34430.18693430.14936772X-RAY DIFFRACTION100
2.3443-2.39530.18943790.14776809X-RAY DIFFRACTION100
2.3953-2.4510.18363590.15466791X-RAY DIFFRACTION100
2.451-2.51230.18753970.14776787X-RAY DIFFRACTION100
2.5123-2.58020.18293400.14546829X-RAY DIFFRACTION100
2.5802-2.65610.18733610.14556852X-RAY DIFFRACTION100
2.6561-2.74190.17273840.14556797X-RAY DIFFRACTION100
2.7419-2.83980.18933380.14796862X-RAY DIFFRACTION100
2.8398-2.95350.1853850.14596845X-RAY DIFFRACTION100
2.9535-3.08790.16183570.14176902X-RAY DIFFRACTION100
3.0879-3.25060.17913680.14536847X-RAY DIFFRACTION100
3.2506-3.45420.17713670.14636884X-RAY DIFFRACTION100
3.4542-3.72080.17193510.15126930X-RAY DIFFRACTION100
3.7208-4.0950.1653550.14326934X-RAY DIFFRACTION100
4.095-4.68690.14753570.13256948X-RAY DIFFRACTION100
4.6869-5.90260.17383540.16267037X-RAY DIFFRACTION100
5.9026-43.07490.23373830.22317206X-RAY DIFFRACTION100
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)
11.49251.70920.93842.02711.21941.9481-0.09620.09560.0851-0.30010.08330.0402-0.29610.05710.05530.0995-0.0207-0.00210.09390.00420.14224.39165.2908-35.854
20.2331-0.6743-0.08382.16470.34510.08480.0044-0.01750.0840.16460.0785-0.54430.04350.0996-0.06420.12870.0317-0.04880.1468-0.02350.217334.8287-38.6047-41.1062
30.96980.03080.01261.7610.0491.07940.03130.0519-0.19050.0098-0.0358-0.07160.1946-0.16410.0140.09580.0238-0.03670.1401-0.0430.143926.5232-61.268-46.5073
40.4456-0.13350.02084.82842.08140.99440.01340.01870.0212-0.09840.0666-0.3218-0.04430.1274-0.02750.07150.00520.00830.1143-0.00570.142625.9189-15.128-39.6419
50.91580.83930.70691.92620.44791.63090.0518-0.09530.26790.0339-0.0041-0.1272-0.1730.13490.03370.1074-0.04490.01630.1559-0.03960.22327.436212.6868-27.5147
63.00253.94540.89126.65851.52331.35550.0178-0.0216-0.03580.25530.1352-0.35740.02740.1487-0.09610.0913-0.0051-0.01170.1383-0.01070.149926.5531-1.1361-23.0078
72.90090.80790.64662.2543-0.38321.14510.1312-0.17980.07310.36940.0671-0.2409-0.07720.1202-0.15220.18490.0521-0.03420.1772-0.02270.172622.0559-35.1309-42.4556
80.23110.19190.12142.44811.30011.0406-0.015-0.02610.0937-0.04840.0492-0.0405-0.11050.0764-0.03360.0739-0.00830.00090.124-0.01170.129319.04740.7889-28.4141
91.92152.56590.36733.4792-0.12257.18630.0445-0.36280.72050.4306-0.02280.3792-0.9332-0.05060.06310.2711-0.0012-0.00190.2514-0.17310.416718.464430.1032-10.6423
101.2803-0.3881-0.58821.94781.06522.2987-0.0936-0.12860.04310.17770.1135-0.15240.08110.1306-0.03660.0808-0.002-0.02820.1411-0.02510.05769.3294-3.8887-11.8272
110.16130.56640.15672.05520.63740.25860.0995-0.10610.0380.316-0.2050.29660.1441-0.16610.09690.1577-0.06590.03490.1722-0.03610.1742-6.4879-44.7026-27.2103
121.62260.29630.27321.5270.59410.97010.05340.1998-0.10510.0027-0.120.1930.2674-0.16330.05340.2028-0.0694-0.01410.1857-0.03420.1692-9.2557-64.8352-44.5074
132.9815-0.20260.3921.82811.0721.89430.17240.3521-0.5139-0.0036-0.0059-0.14980.46680.2995-0.15630.2573-0.0036-0.01380.235-0.08970.1988-1.2472-72.1214-48.6703
142.0522-0.14590.23212.85170.09191.5140.17690.53840.0422-0.2676-0.1905-0.07810.10060.2301-0.02420.1244-0.00220.01440.287-0.00140.1271-1.4378-65.2577-51.961
150.59720.9040.19381.70220.21950.07610.046-0.00210.17740.1644-0.11640.35690.0513-0.10060.07610.1197-0.03280.01590.1571-0.0310.1717-5.7884-43.6674-31.9724
160.3583-0.1834-0.26924.10051.84951.6665-0.0212-0.0930.00110.29840.0584-0.01770.1650.0612-0.09780.1204-0.0064-0.00540.1145-0.00120.07856.0459-20.2931-20.8098
172.32080.4558-1.2354.65521.94595.39350.0237-0.00450.132-0.0371-0.0903-0.1984-0.03350.19080.06590.1275-0.0030.01390.1402-0.00570.149711.70663.2345-16.9182
185.635-0.89171.76283.83720.91316.0261-0.0088-0.48310.05380.3898-0.00730.0735-0.1175-0.0720.04030.20060.00450.00890.1526-0.03090.0642.2683-0.715-7.0781
190.84130.12570.42684.55254.36325.6462-0.0532-0.13590.10680.1079-0.20360.3325-0.0511-0.28390.21570.10630.00140.01790.1744-0.02440.1048-3.06210.6178-13.4761
201.50760.6264-0.27821.59950.79333.364-0.0426-0.08760.08710.1752-0.1070.4883-0.1207-0.30650.12460.1479-0.0230.00020.1461-0.03330.20422.1107-38.3613-35.1197
210.4053-0.8511-0.40264.67482.28351.32610.0208-0.03670.07230.04260.0115-0.0987-0.0294-0.0044-0.03030.0811-0.0056-0.00230.1203-0.0070.08568.0118-9.2006-25.6661
220.9689-0.3699-0.53864.332-0.06561.82210.0555-0.1810.49970.1474-0.00150.2707-0.2845-0.0679-0.04870.19740.0587-0.03120.1825-0.09380.2832-1.603523.0029-7.9579
230.17750.03130.00710.38350.22490.33830.01020.11990.0427-0.1552-0.02650.04120.0038-0.01360.040.17560.0475-0.04590.182-0.0210.03371.9755-31.727-65.3631
241.96080.4891-0.43281.34210.15181.6999-0.0505-0.0162-0.27910.03530.02-0.18880.37670.15350.01090.2720.0726-0.0190.2245-0.03020.12212.2348-58.9297-70.099
250.4808-0.1997-0.21161.39890.84611.37940.07820.10890.0858-0.2743-0.0387-0.0099-0.26570.0335-0.03640.20340.0266-0.02840.20730.0030.09895.9626-32.7372-68.2631
260.1816-0.3742-0.01714.13831.75331.13650.01380.04720.0309-0.1618-0.11470.2849-0.1126-0.11940.09070.08660.0257-0.03210.1276-0.01860.1179-1.4797-11.7932-47.4562
270.53-0.0451-0.52223.5809-0.40580.7187-0.1055-0.020.2624-0.0322-0.10290.004-0.2692-0.13220.1040.1480.0468-0.06930.1449-0.01060.2059-2.538616.4334-36.1025
282.0086-2.9726-0.54727.23381.07710.86640.08960.0380.1744-0.5555-0.0636-0.0364-0.2535-0.0484-0.02140.1240.0139-0.01430.11160.01920.12386.41158.5916-44.3144
291.7735-1.0451-0.03451.5904-0.15872.2780.02370.12750.2463-0.521-0.03270.0465-0.16130.02150.04180.2070.0065-0.02560.1589-0.00620.12584.812-30.4507-54.5205
300.13480.17580.05436.0161.46040.49950.0095-0.00080.07330.0405-0.04590.0789-0.0248-0.04570.03080.08920.0127-0.01790.1149-0.00010.11995.3924-6.2707-36.8074
311.79620.2921-1.00183.33680.05061.6282-0.0132-0.06020.47650.00450.00430.0779-0.51270.0414-0.01620.2834-0.0021-0.08010.1339-0.01660.31566.168131.3372-29.8129
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resseq 9:33)
2X-RAY DIFFRACTION2chain 'A' and (resseq 34:89)
3X-RAY DIFFRACTION3chain 'A' and (resseq 90:288)
4X-RAY DIFFRACTION4chain 'A' and (resseq 289:326)
5X-RAY DIFFRACTION5chain 'B' and (resseq 1:30)
6X-RAY DIFFRACTION6chain 'B' and (resseq 31:55)
7X-RAY DIFFRACTION7chain 'B' and (resseq 56:75)
8X-RAY DIFFRACTION8chain 'B' and (resseq 76:158)
9X-RAY DIFFRACTION9chain 'B' and (resseq 159:172)
10X-RAY DIFFRACTION10chain 'C' and (resseq 9:33)
11X-RAY DIFFRACTION11chain 'C' and (resseq 34:89)
12X-RAY DIFFRACTION12chain 'C' and (resseq 90:175)
13X-RAY DIFFRACTION13chain 'C' and (resseq 176:195)
14X-RAY DIFFRACTION14chain 'C' and (resseq 196:249)
15X-RAY DIFFRACTION15chain 'C' and (resseq 250:300)
16X-RAY DIFFRACTION16chain 'C' and (resseq 301:325)
17X-RAY DIFFRACTION17chain 'D' and (resseq 1:10)
18X-RAY DIFFRACTION18chain 'D' and (resseq 11:22)
19X-RAY DIFFRACTION19chain 'D' and (resseq 23:55)
20X-RAY DIFFRACTION20chain 'D' and (resseq 56:75)
21X-RAY DIFFRACTION21chain 'D' and (resseq 76:137)
22X-RAY DIFFRACTION22chain 'D' and (resseq 138:171)
23X-RAY DIFFRACTION23chain 'E' and (resseq 10:153)
24X-RAY DIFFRACTION24chain 'E' and (resseq 154:249)
25X-RAY DIFFRACTION25chain 'E' and (resseq 250:288)
26X-RAY DIFFRACTION26chain 'E' and (resseq 289:326)
27X-RAY DIFFRACTION27chain 'F' and (resseq 1:30)
28X-RAY DIFFRACTION28chain 'F' and (resseq 31:55)
29X-RAY DIFFRACTION29chain 'F' and (resseq 56:75)
30X-RAY DIFFRACTION30chain 'F' and (resseq 76:132)
31X-RAY DIFFRACTION31chain 'F' and (resseq 133:171)

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