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- PDB-3k72: Structure of integrin alphaX beta2 -

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Basic information

Entry
Database: PDB / ID: 3k72
TitleStructure of integrin alphaX beta2
Components
  • Integrin alpha-X
  • Integrin beta-2
KeywordsCELL ADHESION / integrin / cell receptor / Pyrrolidone carboxylic acid
Function / homology
Function and homology information


positive regulation of endothelial tube morphogenesis / integrin alphaX-beta2 complex / positive regulation of prostaglandin-E synthase activity / positive regulation of neutrophil degranulation / integrin alphaM-beta2 complex / integrin alphaL-beta2 complex / ICAM-3 receptor activity / complement component C3b binding / positive regulation of myelination / neutrophil migration ...positive regulation of endothelial tube morphogenesis / integrin alphaX-beta2 complex / positive regulation of prostaglandin-E synthase activity / positive regulation of neutrophil degranulation / integrin alphaM-beta2 complex / integrin alphaL-beta2 complex / ICAM-3 receptor activity / complement component C3b binding / positive regulation of myelination / neutrophil migration / Toll Like Receptor 4 (TLR4) Cascade / negative regulation of dopamine metabolic process / cell-cell adhesion via plasma-membrane adhesion molecules / integrin complex / heterotypic cell-cell adhesion / positive regulation of leukocyte adhesion to vascular endothelial cell / cell adhesion mediated by integrin / leukocyte cell-cell adhesion / phagocytosis, engulfment / receptor clustering / endodermal cell differentiation / plasma membrane raft / amyloid-beta clearance / tertiary granule membrane / ficolin-1-rich granule membrane / cellular response to low-density lipoprotein particle stimulus / positive regulation of protein targeting to membrane / ECM proteoglycans / Integrin cell surface interactions / specific granule membrane / regulation of peptidyl-tyrosine phosphorylation / cell adhesion molecule binding / heat shock protein binding / neutrophil chemotaxis / receptor-mediated endocytosis / cell-matrix adhesion / secretory granule membrane / positive regulation of superoxide anion generation / integrin-mediated signaling pathway / Cell surface interactions at the vascular wall / animal organ morphogenesis / microglial cell activation / receptor internalization / receptor tyrosine kinase binding / cell-cell adhesion / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / extracellular vesicle / integrin binding / cell-cell signaling / signaling receptor activity / amyloid-beta binding / regulation of cell shape / Interleukin-4 and Interleukin-13 signaling / defense response to virus / receptor complex / cell adhesion / positive regulation of cell migration / inflammatory response / external side of plasma membrane / focal adhesion / positive regulation of cell population proliferation / Neutrophil degranulation / positive regulation of gene expression / protein kinase binding / apoptotic process / cell surface / extracellular exosome / membrane / metal ion binding / plasma membrane
Similarity search - Function
ntegrin, alpha v. Chain A, domain 4 / Integrin beta-2 subunit / : / Integrin alpha-X-like, Ig-like domain 3 / 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 ...ntegrin, alpha v. Chain A, domain 4 / Integrin beta-2 subunit / : / Integrin alpha-X-like, Ig-like domain 3 / 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 beta tail domain / 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) / Integrin alpha cytoplasmic region / von Willebrand factor, type A domain / Integrin alpha-2 / Integrin alpha Ig-like domain 1 / 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 domain superfamily / Integrin alpha, N-terminal / von Willebrand factor type A domain / PSI domain / domain found in Plexins, Semaphorins and Integrins / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / 7 Propeller / Methylamine Dehydrogenase; Chain H / von Willebrand factor A-like domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / Immunoglobulin-like / Sandwich / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
alpha-D-mannopyranose / Integrin beta-2 / Integrin alpha-X
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 3.7 Å
AuthorsXie, C. / Zhu, J. / Chen, X. / Mi, L. / Nishida, N. / Springer, T.A.
CitationJournal: Embo J. / Year: 2010
Title: Structure of an integrin with an alphaI domain, complement receptor type 4.
Authors: Xie, C. / Zhu, J. / Chen, X. / Mi, L. / Nishida, N. / Springer, T.A.
History
DepositionOct 11, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 12, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
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 / database_PDB_caveat / 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_conn_angle / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_chiral / pdbx_validate_close_contact / 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 / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_unobs_or_zero_occ_atoms.label_asym_id / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _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 / _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-X
B: Integrin beta-2
C: Integrin alpha-X
D: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)399,78227
Polymers393,3024
Non-polymers6,47923
Water00
1
A: Integrin alpha-X
B: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)199,98313
Polymers196,6512
Non-polymers3,33211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6380 Å2
ΔGint-27 kcal/mol
Surface area75600 Å2
MethodPISA
2
C: Integrin alpha-X
D: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)199,79814
Polymers196,6512
Non-polymers3,14712
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area6330 Å2
ΔGint-26 kcal/mol
Surface area75320 Å2
MethodPISA
3
A: Integrin alpha-X
B: Integrin beta-2
C: Integrin alpha-X
D: Integrin beta-2
hetero molecules

A: Integrin alpha-X
B: Integrin beta-2
C: Integrin alpha-X
D: Integrin beta-2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)799,56354
Polymers786,6058
Non-polymers12,95946
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation6_555-x,-y+1/2,z1
Buried area40540 Å2
ΔGint-135 kcal/mol
Surface area286720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)160.962, 165.549, 536.178
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number24
Space group name H-MI212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23
14
24
15
25
16
26
17
27
18
28
19
29
110
210
111
211
112
212
113
213
114
214

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain A and (resseq 1:126 or resseq 330:595 or resseq 2005-2007)
211chain C and (resseq 1:126 or resseq 330:595 or resseq 2005-2007)
112chain A and (resseq 600:617 or resseq 627:750 )
212chain C and (resseq 600:617 or resseq 627:750 )
113chain A and (resseq 760:902 )
213chain C and (resseq 760:902 )
114chain A and (resseq 903:986 or resseq 995:1081 )
214chain C and (resseq 903:986 or resseq 995:1081 )
115chain B and (resseq 1:56 )
215chain D and (resseq 1:56 )
116chain B and (resseq 60:67 or resseq 73:99 or resseq 348:423 )
216chain D and (resseq 60:67 or resseq 73:99 or resseq 348:423 )
117chain B and (resseq 436:461 )
217chain D and (resseq 436:461 )
118chain B and (resseq 102:342 or resid 2002 )
218chain D and (resseq 102:342 or resid 2002 )
119chain B and (resseq 463:473 )
219chain D and (resseq 463:473 )
1110chain B and (resseq 475:512 )
2110chain D and (resseq 475:512 )
1111chain B and (resseq 516:550 )
2111chain D and (resseq 516:550 )
1112chain B and (resseq 555:592 )
2112chain D and (resseq 555:592 )
1113chain B and (resseq 593:597 )
2113chain D and (resseq 593:597 )
1114chain B and (resseq 600:673 )
2114chain D and (resseq 600:673 )

NCS ensembles :
ID
1
2
3
4
5
6
7
8
9
10
11
12
13
14

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein Integrin alpha-X / Leukocyte adhesion glycoprotein p150 / 95 alpha chain / Leukocyte adhesion receptor p150 / 95 / Leu ...Leukocyte adhesion glycoprotein p150 / 95 alpha chain / Leukocyte adhesion receptor p150 / 95 / Leu M5 / CD11 antigen-like family member C


Mass: 120708.203 Da / Num. of mol.: 2 / Fragment: residues 20-1103
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CD11C, ITGAX / Plasmid: pcDNA3.1 / Production host: Cricetulus griseus (Chinese hamster) / Strain (production host): CHO Lec 3.2.8.1 / References: UniProt: P20702
#2: Protein Integrin beta-2 / Cell surface adhesion glycoproteins LFA-1/CR3/p150 / 95 subunit beta / Complement receptor C3 subunit beta


Mass: 75942.992 Da / Num. of mol.: 2 / Fragment: residues 23-700
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CD18, ITGB2, MFI7 / Plasmid: pEF1/puro / Production host: Cricetulus griseus (Chinese hamster) / Strain (production host): CHO Lec 3.2.8.1 / References: UniProt: P05107

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Sugars , 5 types, 15 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 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
#4: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-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.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2-2-2/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
#5: Polysaccharide alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...alpha-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.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_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: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose


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
#8: Sugar ChemComp-MAN / alpha-D-mannopyranose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Non-polymers , 1 types, 8 molecules

#7: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Ca

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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: 4.54 Å3/Da / Density % sol: 72.91 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 7.2
Details: 0.915M sodium/potassium phosphate, pH 7.2, VAPOR DIFFUSION, HANGING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 0.97928 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD
RadiationMonochromator: double crystal monochromator and K-B pair of biomorph mirrors for vertical and horizontal focusing
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97928 Å / Relative weight: 1
ReflectionResolution: 3.7→50 Å / Num. all: 76217 / Num. obs: 76217 / % possible obs: 99.4 % / Redundancy: 7.5 % / Biso Wilson estimate: 124.3 Å2 / Rmerge(I) obs: 0.104 / Rsym value: 0.104 / Net I/σ(I): 12.6
Reflection shellResolution: 3.7→3.86 Å / Redundancy: 7.6 % / Rmerge(I) obs: 1.355 / Mean I/σ(I) obs: 1.9 / Num. unique all: 8974 / Rsym value: 1.355 / % possible all: 99.4

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Processing

Software
NameVersionClassification
MAR345dtbdata collection
SOLVEphasing
PHENIX(phenix.refine)refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MAD / Resolution: 3.7→48.475 Å / SU ML: 0.69 / Isotropic thermal model: isotropic / Cross valid method: THROUGHOUT / σ(F): 1.34 / Stereochemistry target values: Engh & Huber / Details: MLHL
RfactorNum. reflection% reflectionSelection details
Rfree0.3346 843 1.11 %random
Rwork0.315 ---
obs0.3152 76217 99.38 %-
all-76217 --
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 0.8 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 150 Å2 / ksol: 0.381 e/Å3
Refine analyzeLuzzati sigma a free: 0.73 Å
Refinement stepCycle: LAST / Resolution: 3.7→48.475 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms23970 0 412 0 24382
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.09348556
X-RAY DIFFRACTIONf_angle_d1.17987257
X-RAY DIFFRACTIONf_dihedral_angle_d19.71812299
X-RAY DIFFRACTIONf_chiral_restr0.0553798
X-RAY DIFFRACTIONf_plane_restr0.0067656
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A5796X-RAY DIFFRACTIONPOSITIONAL
12C5796X-RAY DIFFRACTIONPOSITIONAL0.298
21A2275X-RAY DIFFRACTIONPOSITIONAL
22C2275X-RAY DIFFRACTIONPOSITIONAL0.053
31A2158X-RAY DIFFRACTIONPOSITIONAL
32C2158X-RAY DIFFRACTIONPOSITIONAL0.625
41A2709X-RAY DIFFRACTIONPOSITIONAL
42C2709X-RAY DIFFRACTIONPOSITIONAL0.16
51B826X-RAY DIFFRACTIONPOSITIONAL
52D826X-RAY DIFFRACTIONPOSITIONAL0.005
61B1720X-RAY DIFFRACTIONPOSITIONAL
62D1720X-RAY DIFFRACTIONPOSITIONAL0.096
71B366X-RAY DIFFRACTIONPOSITIONAL
72D366X-RAY DIFFRACTIONPOSITIONAL0.121
81B3752X-RAY DIFFRACTIONPOSITIONAL
82D3752X-RAY DIFFRACTIONPOSITIONAL0.064
91B157X-RAY DIFFRACTIONPOSITIONAL
92D157X-RAY DIFFRACTIONPOSITIONAL0.59
101B534X-RAY DIFFRACTIONPOSITIONAL
102D534X-RAY DIFFRACTIONPOSITIONAL0.301
111B479X-RAY DIFFRACTIONPOSITIONAL
112D479X-RAY DIFFRACTIONPOSITIONAL0.009
121B568X-RAY DIFFRACTIONPOSITIONAL
122D568X-RAY DIFFRACTIONPOSITIONAL0.014
131B57X-RAY DIFFRACTIONPOSITIONAL
132D57X-RAY DIFFRACTIONPOSITIONAL0.52
141B1114X-RAY DIFFRACTIONPOSITIONAL
142D1114X-RAY DIFFRACTIONPOSITIONAL0.021
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.7-3.93170.42491390.412612402X-RAY DIFFRACTION99
3.9317-4.23510.39281190.363712463X-RAY DIFFRACTION99
4.2351-4.6610.37081280.299112449X-RAY DIFFRACTION99
4.661-5.33480.24421440.264512548X-RAY DIFFRACTION99
5.3348-6.71840.36111670.29712585X-RAY DIFFRACTION100
6.7184-48.47920.28821460.27512927X-RAY DIFFRACTION99
Refinement TLS params.

Refine-ID: X-RAY DIFFRACTION

IDMethodL11 (°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)
1refined-2.22570.8561-1.3039-0.65470.9459-2.90610.36670.3662-0.1024-0.3536-0.33670.104-0.089-0.05130.0681.5731-0.0630.08730.9883-0.18170.580919.12542.7088121.627
2-1.53911.17390.1402-2.6850.0531-3.081-0.1819-0.5528-0.27890.82220.2312-0.2872-0.0760.32660.02231.02950.0316-0.1881.69960.02740.5311
31.12610.8507-0.9358-1.9351-2.73721.7080.0508-0.0703-0.0492-0.4793-0.2154-0.23760.43240.71130.17761.1306-0.05910.22360.5213-0.12580.7563
4-2.89610.1203-3.07981.94460.42961.142-0.3139-0.2828-0.25560.03280.0685-0.14550.50890.00260.16770.4580.0113-0.23391.1430.1250.7543
5-0.0082-0.42182.37171.56260.50621.09610.74290.3761-0.73280.0625-0.87660.1888-0.8936-0.5760.03860.2815-0.18490.14250.930.03420.647
61.56470.42850.66930.06742.59210.0387-1.0197-0.4335-0.03630.650.6523-0.7567-0.6319-0.61350.14590.5781-0.30330.02360.50660.28760.793
70.5620.6991-0.655-2.1577-0.6697-2.3653-1.0245-0.4811-1.1155-0.7630.12420.12490.6698-0.19110.04391.0486-0.19180.18840.78370.1870.3511
8-0.7585-0.6574-1.5527-0.8057-0.3432-1.3729-0.0724-0.6177-0.1272-0.3335-0.5099-0.6107-0.05870.62910.11050.9168-0.21720.09251.54930.21050.4496
9-0.8299-0.38020.25310.0420.1689-0.0263-0.9135-0.0051-0.3807-1.3074-0.12731.48440.8181-1.79920.13722.87610.28280.42482.17180.01951.7515
10-0.2572-0.1116-0.128-0.1561-0.5404-0.06030.1286-1.60490.1649-0.59490.3829-0.9921-2.26952.0133-0.06122.11150.58720.04352.33570.4161.6946
11-1.0646-0.75870.5250.01610.8279-1.21720.7056-0.0594-0.02670.44320.0576-0.59841.0838-0.2667-0.21381.80760.07880.23020.6753-0.191.1357
12-0.64330.42990.3549-0.0966-0.5832-0.9341-0.87210.5666-0.2471-0.24040.27380.0775-0.16720.99310.17971.16980.3786-0.36052.12470.32051.3717
13-0.21530.13130.6329-0.25220.1643-0.11781.38460.9967-0.41591.2984-0.85880.5661.09250.46540.00012.3307-0.21870.06021.38030.44351.8631
14-0.3353-0.7879-0.2785-1.06310.9275-1.1322-2.04330.01790.35850.83951.2239-0.14531.1232-2.15650.01441.15860.30470.282.18540.33231.4397
150.06020.70651.0967-0.5268-1.1283-1.8428-1.37210.19380.7418-1.77661.86710.3516-0.7441-1.51640.52622.56340.50050.54340.8437-0.71480.0719
16-1.10091.3862-0.38060.22132.2648-1.79370.373-0.6233-0.2908-0.4436-0.58720.7447-0.70320.68050.00881.75960.6473-0.2782.41620.40310.5984
170.7249-0.9706-0.6067-0.12040.472-0.23891.56740.8049-0.2891-2.6054-0.6142-1.7370.1050.4607-0.14282.1572-0.65810.32280.43160.06311.4639
18-0.02520.0076-0.77620.404-0.98870.1129-0.1849-1.8896-0.83180.71221.1901-0.49791.39450.4018-0.120.59670.0127-0.10952.23560.02851.2618
190.2198-0.2068-0.584-0.0636-0.17750.3747-0.02081.80610.779-0.06240.1991-0.27940.7957-2.4686-0.02141.1635-0.57090.20490.4919-0.00511.0224
20-0.0998-0.2498-0.5114-0.28140.0795-0.3091.43570.74360.20080.6041-0.74460.1903-0.7512.1417-0.0290.7814-0.29360.16091.5280.10220.8311
210.3997-0.31640.4708-0.1393-0.23391.82340.9653-0.14690.80250.7176-0.31210.2189-0.80772.7221-0.09261.35070.33340.54821.36430.31111.5986
22-0.42910.10570.05650.25950.46120.1661-1.11640.5789-1.89320.299-0.0584-0.40771.3925-0.3161-0.15891.992-0.11360.06261.83420.42361.5714
23-0.21690.20710.1740.24581.3177-0.19440.15612.6344-0.6279-1.07390.0054-1.5888-0.3175-0.8239-0.13791.4058-0.13620.34021.2473-0.34371.1738
240.1576-0.08440.5588-0.4459-0.3574-0.14771.3857-0.711-0.39362.9617-0.2841-1.0957-0.15480.6921-0.30191.6955-0.3998-0.31661.23260.29030.9882
Refinement TLS groupSelection details: chain D and resseq 600-676

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