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- PDB-4o5i: Crystal structure of broadly neutralizing antibody F045-092 in co... -

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Basic information

Entry
Database: PDB / ID: 4o5i
TitleCrystal structure of broadly neutralizing antibody F045-092 in complex with A/Victoria/361/2011 (H3N2) influenza hemagglutinin
Components
  • (Fab F045-092 ...) x 2
  • (Hemagglutinin ...) x 2
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / immunoglobulin / virus attachment and entry / immune recognition / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


IgD immunoglobulin complex / IgM immunoglobulin complex / IgA immunoglobulin complex / IgE immunoglobulin complex / positive regulation of B cell activation / phagocytosis, recognition / CD22 mediated BCR regulation / immunoglobulin complex / IgG immunoglobulin complex / Fc epsilon receptor (FCERI) signaling ...IgD immunoglobulin complex / IgM immunoglobulin complex / IgA immunoglobulin complex / IgE immunoglobulin complex / positive regulation of B cell activation / phagocytosis, recognition / CD22 mediated BCR regulation / immunoglobulin complex / IgG immunoglobulin complex / Fc epsilon receptor (FCERI) signaling / Classical antibody-mediated complement activation / phagocytosis, engulfment / Initial triggering of complement / FCGR activation / immunoglobulin mediated immune response / Role of phospholipids in phagocytosis / Role of LAT2/NTAL/LAB on calcium mobilization / Scavenging of heme from plasma / immunoglobulin complex, circulating / immunoglobulin receptor binding / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / viral budding from plasma membrane / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / complement activation, classical pathway / Regulation of Complement cascade / Cell surface interactions at the vascular wall / FCERI mediated MAPK activation / FCGR3A-mediated phagocytosis / antigen binding / B cell receptor signaling pathway / Regulation of actin dynamics for phagocytic cup formation / FCERI mediated NF-kB activation / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / clathrin-dependent endocytosis of virus by host cell / adaptive immune response / blood microparticle / host cell surface receptor binding / defense response to bacterium / apical plasma membrane / fusion of virus membrane with host plasma membrane / external side of plasma membrane / innate immune response / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. ...Haemagglutinin, influenzavirus A / Haemagglutinin, HA1 chain, alpha/beta domain superfamily / Haemagglutinin / Haemagglutinin, influenzavirus A/B / Viral capsid/haemagglutinin protein / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Immunoglobulin lambda constant 2 / Hemagglutinin / IgG H chain
Similarity search - Component
Biological speciesInfluenza A virus
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 6.501 Å
AuthorsLee, P.S. / Wilson, I.A.
CitationJournal: Nat Commun / Year: 2014
Title: Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus.
Authors: Lee, P.S. / Ohshima, N. / Stanfield, R.L. / Yu, W. / Iba, Y. / Okuno, Y. / Kurosawa, Y. / Wilson, I.A.
History
DepositionDec 19, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 16, 2014Provider: repository / Type: Initial release
Revision 1.1May 14, 2014Group: Database references
Revision 1.2Aug 2, 2017Group: Refinement description / Source and taxonomy / Category: entity_src_gen / software
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / 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_validate_close_contact / struct_asym / struct_conn / struct_ref_seq / 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.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _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.db_align_end / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Apr 3, 2024Group: 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

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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
G: Hemagglutinin HA1 chain
H: Hemagglutinin HA2 chain
I: Hemagglutinin HA1 chain
J: Hemagglutinin HA2 chain
K: Hemagglutinin HA1 chain
L: Hemagglutinin HA2 chain
M: Fab F045-092 heavy chain
N: Fab F045-092 light chain
O: Fab F045-092 heavy chain
P: Fab F045-092 light chain
Q: Fab F045-092 heavy chain
R: Fab F045-092 light chain
S: Fab F045-092 heavy chain
T: Fab F045-092 light chain
U: Fab F045-092 heavy chain
V: Fab F045-092 light chain
W: Fab F045-092 heavy chain
X: Fab F045-092 light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)649,14271
Polymers626,60724
Non-polymers22,53547
Water00
1
A: Hemagglutinin HA1 chain
B: Hemagglutinin HA2 chain
C: Hemagglutinin HA1 chain
D: Hemagglutinin HA2 chain
E: Hemagglutinin HA1 chain
F: Hemagglutinin HA2 chain
M: Fab F045-092 heavy chain
N: Fab F045-092 light chain
O: Fab F045-092 heavy chain
P: Fab F045-092 light chain
Q: Fab F045-092 heavy chain
R: Fab F045-092 light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)325,77835
Polymers313,30312
Non-polymers12,47423
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area59070 Å2
ΔGint-42 kcal/mol
Surface area120380 Å2
MethodPISA
2
G: Hemagglutinin HA1 chain
H: Hemagglutinin HA2 chain
I: Hemagglutinin HA1 chain
J: Hemagglutinin HA2 chain
K: Hemagglutinin HA1 chain
L: Hemagglutinin HA2 chain
S: Fab F045-092 heavy chain
T: Fab F045-092 light chain
U: Fab F045-092 heavy chain
V: Fab F045-092 light chain
W: Fab F045-092 heavy chain
X: Fab F045-092 light chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)323,36436
Polymers313,30312
Non-polymers10,06024
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area57290 Å2
ΔGint-78 kcal/mol
Surface area117960 Å2
MethodPISA
Unit cell
Length a, b, c (Å)318.123, 187.167, 353.636
Angle α, β, γ (deg.)90.00, 90.47, 90.00
Int Tables number5
Space group name H-MC121
DetailsAsymmetric contains two copies of the biological assembly.

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Components

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Hemagglutinin ... , 2 types, 12 molecules ACEGIKBDFHJL

#1: Protein
Hemagglutinin HA1 chain


Mass: 35934.473 Da / Num. of mol.: 6 / Fragment: Hemagglutinin HA1 chain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Singapore/H2011.447/2011(H3N2) / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: R9U684
#2: Protein
Hemagglutinin HA2 chain


Mass: 20153.393 Da / Num. of mol.: 6 / Fragment: Hemagglutinin HA2 chain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Influenza A virus / Strain: A/Singapore/H2011.447/2011(H3N2) / Gene: HA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: R9U684

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Antibody , 2 types, 12 molecules MOQSUWNPRTVX

#3: Antibody
Fab F045-092 heavy chain


Mass: 25719.725 Da / Num. of mol.: 6 / Fragment: Fab F045-092 heavy chain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: S6C4S0
#4: Antibody
Fab F045-092 light chain


Mass: 22626.895 Da / Num. of mol.: 6 / Fragment: Fab F045-092 light chain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGL@, IGLC2 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P0CG05

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Sugars , 5 types, 47 molecules

#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.: 13
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
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.: 15
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
#7: 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.: 4
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
#8: 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.: 3
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
#9: 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.: 12
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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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 20% PEG 400, 30% 1,2-propanediol, 0.1 M HEPES pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.03318 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Feb 23, 2013
RadiationMonochromator: Double crystal cryo-cooled Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03318 Å / Relative weight: 1
ReflectionResolution: 6.5→50 Å / Num. all: 38102 / Num. obs: 38102 / % possible obs: 92.8 % / Observed criterion σ(I): -3 / Redundancy: 2 % / Rmerge(I) obs: 0.07 / Rsym value: 0.07 / Net I/σ(I): 10.8
Reflection shellResolution: 6.5→6.89 Å / Redundancy: 2 % / Rmerge(I) obs: 0.5 / Mean I/σ(I) obs: 2.1 / Rsym value: 0.5 / % possible all: 91.7

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Processing

Software
NameVersionClassification
Blu-Icedata collection
PHASERphasing
PHENIX(phenix.refine: 1.8.1_1168)refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: apo F045-092 structure, apo A/Victoria/361/2011 (H3N2) HA structure

Resolution: 6.501→49 Å / SU ML: 0.98 / σ(F): 2 / Phase error: 29.56 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2476 1923 5.05 %
Rwork0.2008 --
obs0.2032 38102 92.74 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 6.501→49 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms42816 0 1489 0 44305
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00645444
X-RAY DIFFRACTIONf_angle_d1.21861787
X-RAY DIFFRACTIONf_dihedral_angle_d20.22916929
X-RAY DIFFRACTIONf_chiral_restr0.0767088
X-RAY DIFFRACTIONf_plane_restr0.0057828
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
6.501-6.66320.41481390.32752437X-RAY DIFFRACTION88
6.6632-6.84290.37421470.32362612X-RAY DIFFRACTION95
6.8429-7.04370.35481380.30172596X-RAY DIFFRACTION94
7.0437-7.27040.37341310.27922633X-RAY DIFFRACTION95
7.2704-7.52930.34411380.25972598X-RAY DIFFRACTION94
7.5293-7.82960.2671450.22542622X-RAY DIFFRACTION95
7.8296-8.18440.2341520.19552600X-RAY DIFFRACTION94
8.1844-8.61370.23071340.16362615X-RAY DIFFRACTION94
8.6137-9.15010.17661240.13882612X-RAY DIFFRACTION93
9.1501-9.85130.17841420.12792560X-RAY DIFFRACTION92
9.8513-10.8330.17631270.11932609X-RAY DIFFRACTION93
10.833-12.37850.15741370.12952548X-RAY DIFFRACTION91
12.3785-15.5130.20521280.19312589X-RAY DIFFRACTION92
15.513-49.00120.31191410.27772548X-RAY DIFFRACTION89
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)
10.3112-0.08590.19750.37820.20011.8792-0.158-0.07390.04680.1301-0.05520.06850.0029-0.05890.19710.514-0.0298-0.00340.56870.03250.7574-105.6616-140.2663-13.877
20.80470.0457-0.19651.0554-0.13394.8865-0.0722-0.1147-0.08350.0545-0.0307-0.0295-0.04470.16930.15330.67550.0747-0.00980.7098-0.0250.728-54.6769-46.3577187.618
32.2001-0.09771.07293.95830.3273.63770.68360.1368-0.2930.546-0.4516-0.10250.19541.7155-0.07030.6855-0.03340.14991.1129-0.04880.4741-151.3386-142.527546.2982
42.29990.29950.05092.8174-0.33960.989-0.0834-0.5046-0.6937-0.15260.57390.0181-0.02610.1773-0.35220.7099-0.2404-0.36632.01420.21440.8222-170.275-140.878575.6724
53.0620.1945-0.79582.355-2.36212.5397-0.36930.31590.29480.55320.26230.33181.3213-1.00780.14171.3154-0.2466-0.02770.80340.11160.533-86.0491-100.00446.5058
62.0331-0.06320.29331.4504-0.38752.0811.5399-0.18190.41860.56770.31040.9071-0.0366-1.13-0.77912.2687-0.40170.4060.91810.45221.1143-74.9122-83.374975.7578
71.82990.06640.47431.4195-0.23172.79070.0147-0.84460.0339-0.36530.1617-0.2389-1.1679-0.79280.03741.09390.2677-0.00110.92260.30040.6679-82.3906-178.316446.3906
81.4352-0.81330.37252.5517-0.36190.7274-0.6176-0.58760.48771.27750.4641-0.7108-0.1655-0.2375-0.02451.44160.59670.1021.0157-0.36960.7767-74.6302-196.012875.6898
91.23870.32460.3423.869-0.5821.63920.8885-0.83050.04481.6108-0.40981.20060.2816-0.2058-0.01482.0081-0.8398-0.19870.994-0.40171.0165-71.2399-88.9997127.8527
101.12291.0407-0.19012.0083-0.53030.18420.2973-0.10931.00991.5403-0.05850.2338-0.63770.6060.12352.4391-1.6336-0.00561.73750.07931.2303-82.2438-107.03899.1835
112.1641-0.05750.59421.35830.0371.36570.3875-0.6943-0.02070.18550.3625-0.0812-0.31220.1369-0.25540.70740.34190.63422.63320.07440.9611-9.009-40.1689128.2193
120.3277-0.1309-0.29550.0116-0.18641.16860.5428-0.3672-0.21070.14530.15120.6429-0.556-0.5268-0.04530.86790.48590.57513.690.13840.924512.0511-41.037199.5167
133.4299-1.3617-0.82282.62881.16461.8665-0.085-0.65860.78130.89310.7426-1.11270.1587-0.1211-0.361.74160.8228-0.24731.36550.09170.969-81.9682-10.1203127.6921
141.8346-1.54650.69651.4814-0.20810.6950.1038-0.9835-0.44920.75740.8261-0.0960.81230.3847-0.55733.1780.9221-0.05581.6099-0.07470.8837-91.40869.427799.0775
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A or chain B or chain C or chain D or chain E or chain F
2X-RAY DIFFRACTION2chain G or chain H or chain I or chain J or chain K or chain L
3X-RAY DIFFRACTION3chain M and resid 1:113 or chain N and resid 1:108
4X-RAY DIFFRACTION4chain M and resid 114:214 or chain N and resid 109:209
5X-RAY DIFFRACTION5chain O and resid 1:113 or chain P and resid 1:108
6X-RAY DIFFRACTION6chain O and resid 114:214 or chain P and resid 109:209
7X-RAY DIFFRACTION7chain Q and resid 1:113 or chain R and resid 1:108
8X-RAY DIFFRACTION8chain Q and resid 114:214 or chain R and resid 109:209
9X-RAY DIFFRACTION9chain S and resid 1:113 or chain T and resid 1:108
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