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- PDB-5e6s: Structures of leukocyte integrin aLB2: The aI domain, the headpie... -

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Basic information

Entry
Database: PDB / ID: 5e6s
TitleStructures of leukocyte integrin aLB2: The aI domain, the headpiece, and the pocket for the internal ligand
Components
  • Integrin alpha-L
  • Integrin beta-2
KeywordsCELL ADHESION / lymphocyte function-associated antigen-1
Function / homology
Function and homology information


integrin alphaX-beta2 complex / memory T cell extravasation / positive regulation of neutrophil degranulation / cellular extravasation / integrin alphaM-beta2 complex / integrin alphaL-beta2 complex / ICAM-3 receptor activity / T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell / cell-cell adhesion via plasma-membrane adhesion molecules / complement component C3b binding ...integrin alphaX-beta2 complex / memory T cell extravasation / positive regulation of neutrophil degranulation / cellular extravasation / integrin alphaM-beta2 complex / integrin alphaL-beta2 complex / ICAM-3 receptor activity / T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell / cell-cell adhesion via plasma-membrane adhesion molecules / complement component C3b binding / Toll Like Receptor 4 (TLR4) Cascade / leukocyte migration involved in inflammatory response / neutrophil migration / RUNX3 Regulates Immune Response and Cell Migration / heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules / integrin complex / positive regulation of leukocyte adhesion to vascular endothelial cell / heterotypic cell-cell adhesion / regulation of peptidyl-tyrosine phosphorylation / leukocyte cell-cell adhesion / phagocytosis, engulfment / negative regulation of dopamine metabolic process / cell adhesion mediated by integrin / receptor clustering / endodermal cell differentiation / amyloid-beta clearance / tertiary granule membrane / cellular response to low-density lipoprotein particle stimulus / ficolin-1-rich granule membrane / plasma membrane raft / positive regulation of protein targeting to membrane / Integrin cell surface interactions / phagocytosis / endothelial cell migration / specific granule membrane / cell adhesion molecule binding / positive regulation of superoxide anion generation / heat shock protein binding / neutrophil chemotaxis / receptor-mediated endocytosis / cell-matrix adhesion / integrin-mediated signaling pathway / Cell surface interactions at the vascular wall / microglial cell activation / cell-cell adhesion / receptor internalization / integrin binding / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / positive regulation of nitric oxide biosynthetic process / cell-cell signaling / extracellular vesicle / regulation of cell shape / amyloid-beta binding / Interleukin-4 and Interleukin-13 signaling / receptor complex / cell adhesion / inflammatory response / external side of plasma membrane / focal adhesion / apoptotic process / Neutrophil degranulation / protein kinase binding / cell surface / signal transduction / extracellular exosome / metal ion binding / membrane / plasma membrane
Similarity search - Function
Integrin beta-2 subunit / ligand-binding face of the semaphorins, domain 2 / ntegrin, alpha v. Chain A, domain 3 / ligand-binding face of the semaphorins, domain 2 / Integrin alpha, N-terminal / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / Integrin beta tail domain / Integrin EGF domain ...Integrin beta-2 subunit / ligand-binding face of the semaphorins, domain 2 / ntegrin, alpha v. Chain A, domain 3 / ligand-binding face of the semaphorins, domain 2 / Integrin alpha, N-terminal / Integrin beta subunit, cytoplasmic domain / Integrin beta cytoplasmic domain / Integrin_b_cyt / Integrin beta tail domain / Integrin EGF domain / Integrin beta subunit, tail / Integrin beta tail domain superfamily / Integrin_B_tail / Integrin alpha cytoplasmic region / Integrins beta chain EGF (I-EGF) domain profile. / Integrin beta subunit, VWA domain / Integrin beta subunit / Integrin beta N-terminal / Integrin beta chain VWA domain / Integrin plexin domain / Integrins beta chain EGF (I-EGF) domain signature. / Integrin beta subunits (N-terminal portion of extracellular region) / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / von Willebrand factor, type A domain / Integrin alpha chain / Integrin alpha beta-propellor / Integrin alpha chain, C-terminal cytoplasmic region, conserved site / : / Integrin alpha Ig-like domain 2 / 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 / von Willebrand factor type A domain / PSI domain / domain found in Plexins, Semaphorins and Integrins / VWFA domain profile. / von Willebrand factor (vWF) type A domain / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily / EGF-like domain signature 1. / EGF-like domain signature 2. / 7 Propeller / Methylamine Dehydrogenase; Chain H / Immunoglobulin-like / Sandwich / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Integrin beta-2 / Integrin alpha-L
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.15 Å
AuthorsSpringer, T.A. / Sen, M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)NCI CA031798 United States
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2016
Title: Leukocyte integrin alpha L beta 2 headpiece structures: The alpha I domain, the pocket for the internal ligand, and concerted movements of its loops.
Authors: Sen, M. / Springer, T.A.
History
DepositionOct 10, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 2, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 16, 2016Group: Database references
Revision 1.2May 11, 2016Group: Database references
Revision 1.3Jul 20, 2016Group: Data collection
Revision 1.4Sep 27, 2017Group: Author supporting evidence / Data collection / Derived calculations
Category: diffrn_detector / pdbx_audit_support / pdbx_struct_oper_list
Item: _diffrn_detector.detector / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.5Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / pdbx_struct_conn_angle / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.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_atom_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.7Nov 6, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
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: Integrin alpha-L
B: Integrin beta-2
C: Integrin alpha-L
D: Integrin beta-2
E: Integrin alpha-L
F: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)436,88833
Polymers434,2236
Non-polymers2,66527
Water36,9672052
1
A: Integrin alpha-L
B: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,62911
Polymers144,7412
Non-polymers8889
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Integrin alpha-L
D: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,62911
Polymers144,7412
Non-polymers8889
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Integrin alpha-L
F: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,62911
Polymers144,7412
Non-polymers8889
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
A: Integrin alpha-L
B: Integrin beta-2
hetero molecules

E: Integrin alpha-L
F: Integrin beta-2
hetero molecules

C: Integrin alpha-L
D: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)436,88833
Polymers434,2236
Non-polymers2,66527
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_454x-1,y,z-11
crystal symmetry operation2_455-x-1,y+1/2,-z1
Buried area16860 Å2
ΔGint-163 kcal/mol
Surface area127090 Å2
MethodPISA
Unit cell
Length a, b, c (Å)151.900, 118.877, 150.967
Angle α, β, γ (deg.)90.00, 118.52, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 2 types, 6 molecules ACEBDF

#1: Protein Integrin alpha-L / CD11 antigen-like family member A / Leukocyte adhesion glycoprotein LFA-1 alpha chain / LFA-1A / ...CD11 antigen-like family member A / Leukocyte adhesion glycoprotein LFA-1 alpha chain / LFA-1A / Leukocyte function-associated molecule 1 alpha chain


Mass: 87841.086 Da / Num. of mol.: 3 / Fragment: UNP residues 26-770
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGAL, CD11A / Production host: Homo sapiens (human) / References: UniProt: P20701
#2: Protein Integrin beta-2 / Cell surface adhesion glycoproteins LFA-1/CR3/p150 / 95 subunit beta / Complement receptor C3 subunit beta


Mass: 56899.809 Da / Num. of mol.: 3 / Fragment: UNP residues 23-482
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ITGB2, CD18, MFI7 / Production host: Homo sapiens (human) / References: UniProt: P05107

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Sugars , 1 types, 9 molecules

#5: 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.: 9 / 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 , 3 types, 2070 molecules

#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#4: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 15
Source method: isolated from a genetically manipulated source
Formula: Ca
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2052 / 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

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Sample preparation

CrystalDensity Matthews: 2.88 Å3/Da / Density % sol: 57.36 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4
Details: 0.1 M Tris, pH 8, 0.1 M NaCl, and 8% polyethylene glycol (PEG) 20,000
Temp details: cold room

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.03321 Å
DetectorType: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Apr 7, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03321 Å / Relative weight: 1
ReflectionResolution: 2.15→50 Å / Num. obs: 180557 / % possible obs: 70.5 % / Redundancy: 2.8 % / Net I/σ(I): 5.2

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Processing

Software
NameVersionClassification
PHENIX(1.10_2155: ???)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementResolution: 2.15→49.45 Å / SU ML: 0.31 / Cross valid method: FREE R-VALUE / σ(F): 1.99 / Phase error: 25.52 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.234 9078 5.03 %Random selection
Rwork0.1937 ---
obs0.1958 180539 70.53 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.15→49.45 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23883 0 144 2052 26079
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00424847
X-RAY DIFFRACTIONf_angle_d0.833733
X-RAY DIFFRACTIONf_dihedral_angle_d15.53315059
X-RAY DIFFRACTIONf_chiral_restr0.0533725
X-RAY DIFFRACTIONf_plane_restr0.0044462
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1495-2.1740.38381480.34792595X-RAY DIFFRACTION32
2.174-2.19950.36571540.34582878X-RAY DIFFRACTION36
2.1995-2.22640.38151730.33283046X-RAY DIFFRACTION38
2.2264-2.25450.34511890.32343305X-RAY DIFFRACTION41
2.2545-2.28420.34711790.31443538X-RAY DIFFRACTION44
2.2842-2.31550.3981770.30173811X-RAY DIFFRACTION47
2.3155-2.34860.34751960.30274068X-RAY DIFFRACTION50
2.3486-2.38360.33632090.30754366X-RAY DIFFRACTION54
2.3836-2.42090.31042540.29794689X-RAY DIFFRACTION58
2.4209-2.46060.34822720.28775141X-RAY DIFFRACTION64
2.4606-2.5030.3223310.27845584X-RAY DIFFRACTION69
2.503-2.54850.34373280.25566145X-RAY DIFFRACTION76
2.5485-2.59750.33563650.24726935X-RAY DIFFRACTION85
2.5975-2.65050.30573830.24017018X-RAY DIFFRACTION87
2.6505-2.70820.26183740.22787044X-RAY DIFFRACTION87
2.7082-2.77110.27063400.22126983X-RAY DIFFRACTION86
2.7711-2.84040.28123590.22037020X-RAY DIFFRACTION86
2.8404-2.91720.25213820.21126944X-RAY DIFFRACTION86
2.9172-3.00310.2643460.20856937X-RAY DIFFRACTION86
3.0031-3.10.23873580.20086939X-RAY DIFFRACTION85
3.1-3.21080.24583550.18786853X-RAY DIFFRACTION85
3.2108-3.33930.22213810.17416772X-RAY DIFFRACTION84
3.3393-3.49120.20643720.16386846X-RAY DIFFRACTION84
3.4912-3.67520.20093370.15466736X-RAY DIFFRACTION83
3.6752-3.90540.17013900.14656690X-RAY DIFFRACTION83
3.9054-4.20680.16893520.13766676X-RAY DIFFRACTION82
4.2068-4.62990.15323290.12426611X-RAY DIFFRACTION81
4.6299-5.29920.16853530.13026513X-RAY DIFFRACTION80
5.2992-6.67380.19253330.16576490X-RAY DIFFRACTION79
6.6738-49.46350.19373590.17576288X-RAY DIFFRACTION76
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)
10.01380.00340.00640.00460.00270.0045-0.05390.014-0.0278-0.0206-0.0133-0.00450.0968-0.0188-0.02790.1326-0.07730.08290.1671-0.06070.0626-54.3465-43.6097-34.2099
20.1017-0.0384-0.04850.0569-0.00680.1019-0.05760.04730.0457-0.0297-0.03070.0048-0.0421-0.038-0.06320.1303-0.0023-0.01320.09620.00010.0779-60.7362-23.2137-32.0221
30.06940.02130.02220.02590.01930.1031-0.0330.05230.04960.07160.0489-0.0718-0.1721-0.0132-00.10390.02670.02250.07520.0050.1105-73.21156.0539-31.3088
40.0008-0.0068-0.00370.00660.00110.0020.0506-0.00390.02460.08780.0355-0.0092-0.1106-0.0450.0130.17780.03220.04950.11060.01740.1495-71.7769-8.3149-21.2609
50.014-0.0063-0.00290.02230.02450.0301-0.02510.0167-0.0095-0.0419-0.0080.0212-0.044-0.0929-0.010.0782-0.0085-0.01640.1442-0.03360.0256-71.2741-26.5844-19.5433
60.04030.01520.01980.02350.01250.01490.0251-0.0278-0.02880.06280.0374-0.01940.0248-0.0770.0743-0.1711-0.05040.03840.0697-0.00740.0513-69.4659-40.2561-11.9852
70.0169-0.0008-0.00690.01260.00030.0143-0.01380.023-0.0504-0.008-0.00450.03590.0336-0.0535-0.00350.1162-0.06860.04510.0374-0.12320.0717-61.3557-52.9025-24.9471
80.00230.0029-0.00120.0034-0.00020.0031-0.02280.01780.0076-0.01920.02530.0077-0.0138-0.02700.3071-0.04730.0560.29430.10460.4045-56.1837-86.22713.0589
90.017-0.02320.03650.045-0.05750.0758-0.0634-0.0147-0.05360.0499-0.0349-0.0347-0.0039-0.0266-0.06570.1643-0.04230.03790.18810.02240.2392-48.9596-74.476612.3008
100.0359-0.0031-0.00970.03020.02630.0304-0.03540.02270.0297-0.017-0.0006-0.0181-0.1040.1146-0.00890.0967-0.0455-0.03040.1095-0.0120.1013-39.7401-26.0819-2.9067
110.02980.00620.00520.0143-0.02450.04630.0143-0.0038-0.0204-0.0216-0.02620.03410.0558-0.0332-0.00530.2125-0.0996-0.03230.0915-0.0490.0533-50.2663-44.739411.3997
120.0047-0.00310.00050.00130.0008-0.00070.0173-0.0262-0.0399-0.01630.01790.00690.0299-0.0339-0.00020.2155-0.01770.03760.06280.0120.1804-42.1284-68.14837.6487
130.00140.0007-0.00170.0009-0.00010.00120.01470.00460.003-0.00870.02010.00310.0112-0.011100.7584-0.00110.10130.7716-0.03490.8154-43.8828-100.0121.0503
140.00880.0014-0.00510.00790.00390.01610.0114-0.024-0.004-0.03980.00470.03780.0163-0.04930.00280.1468-0.0688-0.0180.1527-0.0050.0936-52.5946-24.433927.9748
150.02110.0088-0.02130.0317-0.01450.0467-0.04010.04180.0266-0.0340.01680.0115-0.0443-0.0917-0.03340.0863-0.0117-0.01010.11720.01510.0856-55.0792-4.474135.1645
160.039-0.040.01950.0327-0.00720.0515-0.0644-0.01650.07440.0099-0.0254-0.0574-0.04740.0326-0.11420.05960.1235-0.0205-0.0154-0.01780.0927-61.691524.549346.1379
170.0120.00610.02060.01060.02510.0601-0.02480.01510.03550.03810.0481-0.0188-0.153-0.0464-0.00210.1480.02150.00250.1782-0.01660.1024-53.55584.385750.513
180.0776-0.00050.00190.22-0.02690.1458-0.0184-0.0961-0.04290.14410.0795-0.029-0.0109-0.1390.12630.0786-0.03450.00620.109-0.00190.0092-46.4286-18.493352.7355
190.0106-0.02380.01040.0564-0.01340.04060.0474-0.0304-0.04490.02770.0030.07410.1128-0.0680.05550.1887-0.1461-0.06610.0183-0.05650.0372-48.5734-33.801537.7436
200.00270.00230.0010.0044-0.00260.0038-0.0291-0.0160.00180.01920.0120.0234-0.0068-0.053800.4262-0.05250.06850.31750.04280.3087-20.6278-67.412852.9023
210.0980.00920.0390.051-0.0420.1035-0.04790.01330.07540.0162-0.0178-0.0020.14950.0182-0.05470.1491-0.01710.08550.09930.01830.1101-9.3443-35.27246.9012
220.0375-0.0220.01490.1824-0.09280.07910.04830.07130.0946-0.1128-0.0514-0.06240.0521-0.0031-0.00550.0325-0.0002-0.01070.09080.00830.1214-21.7172-7.973137.0433
230.0057-0.0036-0.00160.0212-0.00730.0059-0.0046-0.0195-0.0282-0.0081-0.04060.0270.0631-0.0067-0.00460.1524-0.0461-0.01350.15210.06030.1861-10.7895-32.029552.3759
240.008-0.0026-0.00120.00140.00270.0057-0.032-0.00810.0016-0.0059-0.0139-0.00270.0296-0.0254-0.00780.324-0.01210.04990.1550.05540.1782-10.209-49.122243.1756
25-0.00010.0005-00.00070-0.00010.00180.0092-0.0010.00260.00880.0006-0.0029-0.002100.7604-0.0283-0.01350.6539-0.01060.7148-14.5233-81.651440.8545
260.0091-0.0091-0.010.03160.0130.0161-0.0152-0.0033-0.04370.042-0.04160.0430.0506-0.0181-0.03310.0646-0.0998-0.00590.14630.04360.1153-1.0649-4.770864.0275
270.0061-0.00480.0070.00050.00030.0220.0104-0.0230.0273-0.0035-0.0285-0.0106-0.025-0.0622-0.06640.0314-0.03930.11110.01630.04840.01363.749715.452269.1295
280.08920.0190.03720.04560.0010.0910.0344-0.05530.1015-0.00440.0113-0.0103-0.1618-0.02690.01620.08620.00130.01140.0616-0.02580.106310.008144.9979.9444
290.0069-0.0034-0.00970.00710.00540.0058-0.0256-0.0410.1152-0.05220.0021-0.0301-0.07180.015400.1491-0.0126-0.01160.1013-0.00690.108317.305126.086574.8528
300.005-0.00580.00230.00930.01190.01210.0033-0.01830.03750.0220.0594-0.0546-0.0135-0.0031-00.0953-0.0136-0.01480.11110.00230.129620.739312.775672.1857
310.0726-0.0206-0.0010.0422-0.00510.0406-0.0058-0.1093-0.03320.05740.0131-0.10640.05050.03050.01650.00890.039-0.0930.01870.08190.021925.7507-1.376167.7182
320.0735-0.01380.01080.0460.04070.07020.0011-0.0297-0.05860.0222-0.02290.00270.06760.0196-0.05280.1245-0.0121-0.01560.11210.02240.126910.7192-14.258666.3978
330.2156-0.0546-0.06440.18220.00310.28030.2004-0.0533-0.1646-0.06650.13170.03510.0308-0.05820.38340.24830.0483-0.21210.09930.03290.200337.7351-38.041338.3898
340.08150.0004-0.0490.0257-0.04760.15670.0520.0077-0.0336-0.0467-0.016-0.0158-0.01140.01750.16210.02960.00740.06420.05320.05060.074426.46357.093738.1758
350.01070.00280.00630.0194-0.00270.00910.02530.0063-0.0112-0.00240.02190.00640.0093-0.03370.02010.1990.0557-0.14170.06480.06360.18631.4789-28.520832.5004
360-0.00010.00060.0003-0.00050.0002-0.0191-0.00120.0001-0.0015-0.0122-0.00570.0018-0.004100.9669-0.0368-0.13780.9503-0.00820.955228.0938-61.141834.3708
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 57 )
2X-RAY DIFFRACTION2chain 'A' and (resid 58 through 129 )
3X-RAY DIFFRACTION3chain 'A' and (resid 130 through 277 )
4X-RAY DIFFRACTION4chain 'A' and (resid 278 through 330 )
5X-RAY DIFFRACTION5chain 'A' and (resid 331 through 393 )
6X-RAY DIFFRACTION6chain 'A' and (resid 394 through 502 )
7X-RAY DIFFRACTION7chain 'A' and (resid 503 through 589 )
8X-RAY DIFFRACTION8chain 'B' and (resid 1 through 27 )
9X-RAY DIFFRACTION9chain 'B' and (resid 28 through 104 )
10X-RAY DIFFRACTION10chain 'B' and (resid 105 through 301 )
11X-RAY DIFFRACTION11chain 'B' and (resid 302 through 401 )
12X-RAY DIFFRACTION12chain 'B' and (resid 402 through 431 )
13X-RAY DIFFRACTION13chain 'B' and (resid 432 through 459 )
14X-RAY DIFFRACTION14chain 'C' and (resid 1 through 57 )
15X-RAY DIFFRACTION15chain 'C' and (resid 58 through 129 )
16X-RAY DIFFRACTION16chain 'C' and (resid 130 through 281 )
17X-RAY DIFFRACTION17chain 'C' and (resid 282 through 344 )
18X-RAY DIFFRACTION18chain 'C' and (resid 345 through 513 )
19X-RAY DIFFRACTION19chain 'C' and (resid 514 through 590 )
20X-RAY DIFFRACTION20chain 'D' and (resid 1 through 27 )
21X-RAY DIFFRACTION21chain 'D' and (resid 28 through 149 )
22X-RAY DIFFRACTION22chain 'D' and (resid 150 through 329 )
23X-RAY DIFFRACTION23chain 'D' and (resid 330 through 401 )
24X-RAY DIFFRACTION24chain 'D' and (resid 402 through 431 )
25X-RAY DIFFRACTION25chain 'D' and (resid 432 through 459 )
26X-RAY DIFFRACTION26chain 'E' and (resid 1 through 57 )
27X-RAY DIFFRACTION27chain 'E' and (resid 58 through 129 )
28X-RAY DIFFRACTION28chain 'E' and (resid 130 through 277 )
29X-RAY DIFFRACTION29chain 'E' and (resid 278 through 342 )
30X-RAY DIFFRACTION30chain 'E' and (resid 343 through 393 )
31X-RAY DIFFRACTION31chain 'E' and (resid 394 through 502 )
32X-RAY DIFFRACTION32chain 'E' and (resid 503 through 590 )
33X-RAY DIFFRACTION33chain 'F' and (resid 1 through 104 )
34X-RAY DIFFRACTION34chain 'F' and (resid 105 through 401 )
35X-RAY DIFFRACTION35chain 'F' and (resid 402 through 431 )
36X-RAY DIFFRACTION36chain 'F' and (resid 432 through 459 )

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