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- PDB-3v4p: crystal structure of a4b7 headpiece complexed with Fab ACT-1 -

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Basic information

Entry
Database: PDB / ID: 3v4p
Titlecrystal structure of a4b7 headpiece complexed with Fab ACT-1
Components
  • (MONOCLONAL ANTIBODY Act-1 ...) x 2
  • Integrin alpha-4
  • Integrin beta-7
KeywordsCELL ADHESION / MAdCAM-1 / Membrane
Function / homology
Function and homology information


clathrin-dependent extracellular exosome endocytosis / immune response in gut-associated lymphoid tissue / negative regulation of protein homodimerization activity / cell-matrix adhesion involved in ameboidal cell migration / integrin alpha4-beta7 complex / cell-cell adhesion in response to extracellular stimulus / diapedesis / integrin alpha4-beta1 complex / cell-cell adhesion mediated by integrin / T cell migration ...clathrin-dependent extracellular exosome endocytosis / immune response in gut-associated lymphoid tissue / negative regulation of protein homodimerization activity / cell-matrix adhesion involved in ameboidal cell migration / integrin alpha4-beta7 complex / cell-cell adhesion in response to extracellular stimulus / diapedesis / integrin alpha4-beta1 complex / cell-cell adhesion mediated by integrin / T cell migration / positive regulation of leukocyte tethering or rolling / axonogenesis involved in innervation / protein antigen binding / leukocyte tethering or rolling / positive regulation of endothelial cell apoptotic process / RUNX3 Regulates Immune Response and Cell Migration / heterotypic cell-cell adhesion / integrin complex / positive regulation of vascular endothelial cell proliferation / neuron projection extension / cell adhesion mediated by integrin / negative regulation of vasoconstriction / leukocyte cell-cell adhesion / leukocyte migration / endodermal cell differentiation / receptor clustering / cellular response to cytokine stimulus / fibronectin binding / positive regulation of T cell migration / Integrin cell surface interactions / coreceptor activity / cell adhesion molecule binding / B cell differentiation / substrate adhesion-dependent cell spreading / cell-matrix adhesion / integrin-mediated signaling pathway / Cell surface interactions at the vascular wall / cell-cell adhesion / cellular response to amyloid-beta / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / integrin binding / virus receptor activity / growth cone / Potential therapeutics for SARS / receptor complex / cell adhesion / external side of plasma membrane / focal adhesion / neuronal cell body / cell surface / extracellular exosome / membrane / metal ion binding / plasma membrane
Similarity search - Function
Integrin domains. Chain A, domain 2 / ntegrin, alpha v. Chain A, domain 3 / Integrin alpha, N-terminal / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / : / Integrin alpha Ig-like domain 3 / Integrin beta subunit, tail / Integrin beta tail domain superfamily ...Integrin domains. Chain A, domain 2 / ntegrin, alpha v. Chain A, domain 3 / Integrin alpha, N-terminal / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / : / Integrin alpha Ig-like domain 3 / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain cysteine-rich domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / EGF-like domain, extracellular / EGF-like domain / von Willebrand factor, type A domain / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / : / Integrin alpha Ig-like domain 2 / Integrin alpha chain / Integrin alpha beta-propellor / Integrin alpha chain, C-terminal cytoplasmic region, conserved site / Integrins alpha chain signature. / FG-GAP repeat profile. / Integrin alpha (beta-propellor repeats). / FG-GAP repeat / FG-GAP repeat / Integrin alpha, N-terminal / Integrin domain superfamily / PSI domain / domain found in Plexins, Semaphorins and Integrins / 7 Propeller / Methylamine Dehydrogenase; Chain H / von Willebrand factor A-like domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / Immunoglobulins / Immunoglobulin-like / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Integrin alpha-4 / Integrin beta-7
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 3.15 Å
AuthorsYu, Y. / Zhu, J. / Springer, T.A.
CitationJournal: J.Cell Biol. / Year: 2012
Title: Structural specializations of a4b7, an Integrin that Mediates Rolling Adhesion
Authors: Yu, Y. / Zhu, J. / Mi, L.Z. / Walz, T. / Sun, H. / Chen, J. / Springer, T.A.
History
DepositionDec 15, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 11, 2012Provider: repository / Type: Initial release
Revision 1.1Mar 28, 2012Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Source and taxonomy / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_src_gen / 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_conn_angle / pdbx_unobs_or_zero_occ_atoms / 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.type_symbol / _chem_comp.name / _chem_comp.type / _entity_src_gen.entity_id / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_alt_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_alt_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _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_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Integrin alpha-4
B: Integrin beta-7
C: Integrin alpha-4
D: Integrin beta-7
H: MONOCLONAL ANTIBODY Act-1 HEAVY CHAIN
L: MONOCLONAL ANTIBODY Act-1 LIGHT CHAIN
M: MONOCLONAL ANTIBODY Act-1 HEAVY CHAIN
N: MONOCLONAL ANTIBODY Act-1 LIGHT CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)342,66733
Polymers337,0778
Non-polymers5,59025
Water37821
1
A: Integrin alpha-4
B: Integrin beta-7
H: MONOCLONAL ANTIBODY Act-1 HEAVY CHAIN
L: MONOCLONAL ANTIBODY Act-1 LIGHT CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)172,14817
Polymers168,5394
Non-polymers3,60913
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Integrin alpha-4
D: Integrin beta-7
M: MONOCLONAL ANTIBODY Act-1 HEAVY CHAIN
N: MONOCLONAL ANTIBODY Act-1 LIGHT CHAIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)170,51916
Polymers168,5394
Non-polymers1,98012
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)137.780, 122.740, 158.140
Angle α, β, γ (deg.)90.00, 115.38, 90.00
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23
14
24
15
25
16
26
17
27

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and (resseq 1:430 ) and (not element H)
211chain C and (resseq 1:430 ) and (not element H)
112chain B and (resseq 133:371 ) and (not element H)
212chain D and (resseq 133:371 ) and (not element H)
113chain B and (resseq 81:126 or resseq 373:454 ) and (not element H)
213chain D and (resseq 81:126 or resseq 373:454 ) and (not element H)
114chain M and (resseq 1:120 ) and (not element H)
214chain H and (resseq 1:120 ) and (not element H)
115chain M and (resseq 121:134 or resseq 142:218 ) and (not element H)
215chain H and (resseq 121:134 or resseq 142:218 ) and (not element H)
116chain N and (resseq 1:111 ) and (not element H)
216chain L and (resseq 1:111 ) and (not element H)
117chain N and (resseq 112:215 ) and (not element H)
217chain L and (resseq 112:215 ) and (not element H)

NCS ensembles :
ID
1
2
3
4
5
6
7

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein Integrin alpha-4 / CD49 antigen-like family member D / Integrin alpha-IV / VLA-4 subunit alpha


Mass: 65644.656 Da / Num. of mol.: 2 / Fragment: unp residues 34-620 / Mutation: R558A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGA4, CD49D / References: UniProt: P13612
#2: Protein Integrin beta-7 / Gut homing receptor beta subunit


Mass: 55426.227 Da / Num. of mol.: 2 / Fragment: unp residues 20-512
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGB7 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P26010

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Antibody , 2 types, 4 molecules HMLN

#3: Antibody MONOCLONAL ANTIBODY Act-1 HEAVY CHAIN


Mass: 23570.227 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Cell line (production host): HYBRIDOMA / Production host: Mus musculus (house mouse)
#4: Antibody MONOCLONAL ANTIBODY Act-1 LIGHT CHAIN


Mass: 23897.439 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Cell line (production host): HYBRIDOMA / Production host: Mus musculus (house mouse)

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Sugars , 2 types, 11 molecules

#5: 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.: 2
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


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 9
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 , 5 types, 35 molecules

#6: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 10 / Source method: obtained synthetically / Formula: Ca
#8: Chemical ChemComp-15P / POLYETHYLENE GLYCOL (N=34) / PEG 1500


Mass: 1529.829 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C69H140O35 / Comment: precipitant*YM
#9: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#10: Chemical ChemComp-TRS / 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / TRIS BUFFER


Mass: 122.143 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C4H12NO3 / Comment: pH buffer*YM
#11: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 21 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 3

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Sample preparation

CrystalDensity Matthews: 3.58 Å3/Da / Density % sol: 65.68 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: 0.1 M Tris, 0.1 M NaCl, 8-10% PEG 20,000, VAPOR DIFFUSION, HANGING DROP, temperature 277K, pH 8.5

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
31001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONAPS 23-ID-D11.00695
SYNCHROTRONAPS 23-ID-D20.97945
SYNCHROTRONAPS 23-ID-D30.97945,0.97960,0.94957
Detector
TypeIDDetectorDate
MARMOSAIC 300 mm CCD1CCDDec 6, 2008
2
3
Radiation
IDMonochromatorProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1double silicon crystalSINGLE WAVELENGTHMx-ray1
2double silicon crystalSINGLE WAVELENGTHMx-ray1
3double silicon crystalMADMx-ray1
Radiation wavelength
IDWavelength (Å)Relative weight
11.006951
20.979451
30.97961
40.949571
ReflectionResolution: 3.15→50 Å / Num. obs: 82079 / % possible obs: 99.3 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 3.78 % / Rmerge(I) obs: 0.089 / Rsym value: 0.089 / Net I/σ(I): 10.3
Reflection shellResolution: 3.15→3.299 Å / Rmerge(I) obs: 0.915 / Mean I/σ(I) obs: 1.9 / Rsym value: 0.915 / % possible all: 100

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Processing

Software
NameVersionClassification
HKL-2000data collection
SHARPphasing
PHENIX(phenix.refine: 1.7.1_743)refinement
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: SAD / Resolution: 3.15→46.13 Å / SU ML: 0.82 / σ(F): 1.99 / Phase error: 27.1 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2514 1067 1.3 %
Rwork0.2199 --
obs0.2204 82057 99.46 %
Solvent computationShrinkage radii: 0.04 Å / VDW probe radii: 0.4 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 94.27 Å2 / ksol: 0.35 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--32.8093 Å2-0 Å23.9672 Å2
2---16.651 Å2-0 Å2
3----11.7665 Å2
Refinement stepCycle: LAST / Resolution: 3.15→46.13 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21380 0 298 21 21699
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00322230
X-RAY DIFFRACTIONf_angle_d0.68930152
X-RAY DIFFRACTIONf_dihedral_angle_d11.6518170
X-RAY DIFFRACTIONf_chiral_restr0.0473346
X-RAY DIFFRACTIONf_plane_restr0.0033902
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A3288X-RAY DIFFRACTIONPOSITIONAL
12C3288X-RAY DIFFRACTIONPOSITIONAL0.008
21B1843X-RAY DIFFRACTIONPOSITIONAL
22D1843X-RAY DIFFRACTIONPOSITIONAL0.007
31B1006X-RAY DIFFRACTIONPOSITIONAL
32D1006X-RAY DIFFRACTIONPOSITIONAL0.004
41M941X-RAY DIFFRACTIONPOSITIONAL
42H941X-RAY DIFFRACTIONPOSITIONAL0.006
51M666X-RAY DIFFRACTIONPOSITIONAL
52H666X-RAY DIFFRACTIONPOSITIONAL0.008
61N851X-RAY DIFFRACTIONPOSITIONAL
62L851X-RAY DIFFRACTIONPOSITIONAL0.007
71N811X-RAY DIFFRACTIONPOSITIONAL
72L811X-RAY DIFFRACTIONPOSITIONAL0.007
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.15-3.29330.37741250.339310117X-RAY DIFFRACTION100
3.2933-3.46690.33761540.300510063X-RAY DIFFRACTION100
3.4669-3.6840.31411210.264810105X-RAY DIFFRACTION100
3.684-3.96830.26121420.225410100X-RAY DIFFRACTION100
3.9683-4.36740.22741190.184710130X-RAY DIFFRACTION100
4.3674-4.99870.19491440.158910106X-RAY DIFFRACTION100
4.9987-6.29530.20781150.180110190X-RAY DIFFRACTION99
6.2953-46.13460.22181470.208810179X-RAY DIFFRACTION98
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)
11.29390.11530.13881.72210.31381.96830.0114-0.0794-0.18930.3130.0744-0.21610.35170.2732-0.0670.41940.163-0.08850.3614-0.08580.29599.737227.62743.4492
22.02220.13862.22790.67430.83766.74070.1692-0.11570.04990.5278-0.0362-0.3469-0.2610.1879-0.00151.2118-0.2026-0.43790.8969-0.03590.842439.920543.845677.5204
31.1949-0.1952-0.20580.9816-0.03041.87910.0811-0.1848-0.11920.4875-0.50660.715-0.1438-0.92050.20650.56160.00470.18660.7288-0.33580.6367-23.980629.624153.0402
43.08810.59280.69234.7551.21634.8509-0.1871-0.03220.1223-0.2032-0.1484-0.2053-0.57340.30740.19431.4903-0.14020.49131.56-0.35260.9646-16.274343.882882.2822
53.9059-1.1114-1.05341.65680.61681.77090.17640.03780.72330.41090.2961.0152-0.4888-0.4118-0.20111.0931.7208-0.15211.0469-0.23271.7373-47.129372.700131.6267
60.4752-0.1401-0.26671.46-0.21391.43050.0429-0.21290.23080.6413-0.20.1209-0.2248-0.2590.13222.62470.21540.59671.358-0.30571.7485-56.933969.959967.0002
71.981-0.5037-0.3512.0713-0.29992.2577-0.00640.2111-0.10750.5796-0.05120.3366-0.1238-0.3714-0.02410.83970.7734-0.19181.0498-0.51241.4497-42.964152.09735.7753
80.00020.0084-0.01840.0491-0.10970.2506-0.2293-0.23930.00860.33450.07270.7624-0.406-0.46250.14451.87480.18960.48691.6241-0.73882.4847-66.568856.692362.7812
90.77580.029-0.1761.3094-0.03051.41590.05140.10620.2626-0.4759-0.04720.0573-0.6807-0.03930.02521.06940.0945-0.05770.379-0.03940.37997.138562.74827.2178
101.551-0.4897-1.37691.14460.73554.5903-0.13430.4186-0.3765-0.38950.0942-0.1230.2970.15750.04711.13830.05860.22721.0237-0.12140.638138.532847.2341-27.1228
111.55190.29970.45260.7129-0.44452.0368-0.06180.1530.3445-0.34650.02690.6756-0.1441-0.9571-0.04661.25330.4437-0.41541.1165-0.15130.9116-26.565657.0181-1.3002
124.2442-0.6368-0.09944.11231.42925.1089-0.23520.0708-0.0030.11570.0609-0.04910.07330.40020.09961.3781-0.0456-0.48241.2293-0.09910.7341-17.966344.3907-31.0486
133.97091.58751.44733.15490.35332.2171-0.2520.47180.0423-0.2822-0.02160.78370.2772-0.73470.05770.4956-0.1592-0.05071.0526-0.42130.9678-42.900211.05120.5121
140.4124-0.29220.57311.17460.12491.4744-0.04890.1783-0.0269-0.46130.0174-0.05890.1053-0.05050.01341.9837-0.525-0.36011.8166-0.20951.4799-52.401812.496-15.1027
153.0850.06490.36621.8698-1.02572.7515-0.2280.42680.1745-0.46610.09150.6805-0.233-0.6666-0.00570.78320.3118-0.36621.176-0.37241.271-41.631.993216.3406
160.1132-0.05490.00640.0958-0.12890.2422-0.38190.36050.1151-0.38910.02860.73550.062-0.56080.28241.8611-0.1963-0.75212.8101-0.34911.8941-63.748524.2291-11.4057
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain A and resid 1:430
2X-RAY DIFFRACTION2chain A and resid 431:587
3X-RAY DIFFRACTION3chain B and resid 131:371
4X-RAY DIFFRACTION4chain B and (resid 80:130 or resid 372:459)
5X-RAY DIFFRACTION5chain M and resid 1:121
6X-RAY DIFFRACTION6chain M and resid 122:219
7X-RAY DIFFRACTION7chain N and resid 1:112
8X-RAY DIFFRACTION8chain N and resid 113:215
9X-RAY DIFFRACTION9chain C and resid 1:430
10X-RAY DIFFRACTION10chain C and resid 431:587
11X-RAY DIFFRACTION11chain D and resid 131:371
12X-RAY DIFFRACTION12chain D and (resid 80:130 or resid 372:459)
13X-RAY DIFFRACTION13chain H and resid 1:121
14X-RAY DIFFRACTION14chain H and resid 122:219
15X-RAY DIFFRACTION15chain L and resid 1:112
16X-RAY DIFFRACTION16chain L and resid 113:215

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