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- PDB-2jkt: AP2 CLATHRIN ADAPTOR CORE with CD4 Dileucine peptide RM(phosphoS)... -

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Basic information

Entry
Database: PDB / ID: 2jkt
TitleAP2 CLATHRIN ADAPTOR CORE with CD4 Dileucine peptide RM(phosphoS) EIKRLLSE Q to E mutant
Components
  • (AP-2 COMPLEX SUBUNIT ...) x 4
  • CD4 PEPTIDE
KeywordsENDOCYTOSIS / ALTERNATIVE SPLICING / PHOSPHOPROTEIN / PHOSPHORYLATION / PROTEIN TRANSPORT / ADAPTOR / MEMBRANE / TRANSPORT / COATED PIT / CELL MEMBRANE / LIPID-BINDING
Function / homology
Function and homology information


Gap junction degradation / Formation of annular gap junctions / LDL clearance / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / LDL clearance / WNT5A-dependent internalization of FZD4 / Retrograde neurotrophin signalling / VLDLR internalisation and degradation / Nef Mediated CD8 Down-regulation ...Gap junction degradation / Formation of annular gap junctions / LDL clearance / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / LDL clearance / WNT5A-dependent internalization of FZD4 / Retrograde neurotrophin signalling / VLDLR internalisation and degradation / Nef Mediated CD8 Down-regulation / Trafficking of GluR2-containing AMPA receptors / Retrograde neurotrophin signalling / clathrin adaptor complex / WNT5A-dependent internalization of FZD4 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / Trafficking of GluR2-containing AMPA receptors / extrinsic component of presynaptic endocytic zone membrane / VLDLR internalisation and degradation / WNT5A-dependent internalization of FZD4 / MHC class II antigen presentation / Recycling pathway of L1 / AP-2 adaptor complex / helper T cell enhancement of adaptive immune response / interleukin-16 binding / interleukin-16 receptor activity / regulation of vesicle size / postsynaptic neurotransmitter receptor internalization / Recycling pathway of L1 / LDL clearance / maintenance of protein location in cell / Cargo recognition for clathrin-mediated endocytosis / T cell selection / Retrograde neurotrophin signalling / Cargo recognition for clathrin-mediated endocytosis / clathrin-coated endocytic vesicle / Clathrin-mediated endocytosis / clathrin adaptor activity / Clathrin-mediated endocytosis / positive regulation of synaptic vesicle endocytosis / MHC class II protein binding / membrane coat / vesicle budding from membrane / clathrin-dependent endocytosis / coronary vasculature development / MHC class II antigen presentation / endolysosome membrane / interleukin-15-mediated signaling pathway / regulation of T cell activation / cellular response to granulocyte macrophage colony-stimulating factor stimulus / signal sequence binding / positive regulation of monocyte differentiation / positive regulation of kinase activity / regulation of hematopoietic stem cell differentiation / Nef Mediated CD4 Down-regulation / Alpha-defensins / aorta development / ventricular septum development / low-density lipoprotein particle receptor binding / extracellular matrix structural constituent / T cell receptor complex / Other interleukin signaling / clathrin binding / enzyme-linked receptor protein signaling pathway / Translocation of ZAP-70 to Immunological synapse / Phosphorylation of CD3 and TCR zeta chains / positive regulation of receptor internalization / Trafficking of GluR2-containing AMPA receptors / Recycling pathway of L1 / regulation of calcium ion transport / macrophage differentiation / Generation of second messenger molecules / synaptic vesicle endocytosis / T cell differentiation / EPH-ephrin mediated repulsion of cells / PD-1 signaling / positive regulation of protein kinase activity / Binding and entry of HIV virion / negative regulation of protein localization to plasma membrane / coreceptor activity / cell surface receptor protein tyrosine kinase signaling pathway / protein serine/threonine kinase binding / clathrin-coated pit / vesicle-mediated transport / MHC class II antigen presentation / positive regulation of interleukin-2 production / VLDLR internalisation and degradation / positive regulation of calcium-mediated signaling / Neutrophil degranulation / protein tyrosine kinase binding / phosphatidylinositol binding / T cell activation / kidney development / secretory granule / Vpu mediated degradation of CD4 / intracellular protein transport / calcium-mediated signaling / clathrin-coated endocytic vesicle membrane / kinase binding / terminal bouton / receptor internalization
Similarity search - Function
Beta-Lactamase - #60 / Mu homology domain, subdomain B / AP-2 complex subunit sigma / Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain / Adaptor protein complex AP-2, alpha subunit / Alpha adaptin AP2, C-terminal domain / Mu2, C-terminal domain / AP-2 complex subunit mu, N-terminal / Adaptor protein complex, sigma subunit / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain ...Beta-Lactamase - #60 / Mu homology domain, subdomain B / AP-2 complex subunit sigma / Clathrin adaptor, alpha-adaptin, appendage, C-terminal subdomain / Adaptor protein complex AP-2, alpha subunit / Alpha adaptin AP2, C-terminal domain / Mu2, C-terminal domain / AP-2 complex subunit mu, N-terminal / Adaptor protein complex, sigma subunit / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta-adaptin appendage, C-terminal subdomain / AP-1/2/4 complex subunit beta / Beta2-adaptin appendage, C-terminal sub-domain / Beta2-adaptin appendage, C-terminal sub-domain / AP complex subunit beta / : / CD4, extracellular / T cell CD4 receptor C-terminal region / CD4, extracellular / T cell CD4 receptor C terminal region / T-cell surface antigen CD4 / Clathrin adaptor complex, small chain / Clathrin adaptor complexes small chain signature. / Clathrin adaptor complexes medium chain signature 1. / Clathrin adaptor, mu subunit / Clathrin adaptor, mu subunit, conserved site / Clathrin adaptor complexes medium chain signature 2. / : / Immunoglobulin C2-set / Immunoglobulin C2-set domain / Coatomer/calthrin adaptor appendage, C-terminal subdomain / Adaptor complexes medium subunit family / AP complex, mu/sigma subunit / Clathrin adaptor complex small chain / AP-2 complex subunit mu, C-terminal superfamily / Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain / Mu homology domain / Adaptin C-terminal domain / Mu homology domain (MHD) profile. / Adaptin C-terminal domain / Clathrin/coatomer adaptor, adaptin-like, N-terminal / Adaptin N terminal region / Clathrin adaptor, appendage, Ig-like subdomain superfamily / Longin-like domain superfamily / TBP domain superfamily / Leucine-rich Repeat Variant / Armadillo/beta-catenin-like repeats / Armadillo / Leucine-rich Repeat Variant / Immunoglobulin / Immunoglobulin domain / Beta-Lactamase / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-Type / Immunoglobulin V-set domain / Armadillo-like helical / Alpha Horseshoe / Immunoglobulin subtype / Immunoglobulin / Armadillo-type fold / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
cDNA, FLJ79547, highly similar to T-cell surface glycoprotein CD4 / T-cell surface glycoprotein CD4 / AP-2 complex subunit alpha-2 / AP-2 complex subunit sigma / AP-2 complex subunit beta / AP-2 complex subunit mu
Similarity search - Component
Biological speciesMUS MUSCULUS (house mouse)
HOMO SAPIENS (human)
RATTUS NORVEGICUS (Norway rat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
AuthorsOwen, D.J. / McCoy, A.J. / Kelly, B.T. / Evans, P.R.
CitationJournal: Nature / Year: 2008
Title: A Structural Explanation for the Binding of Endocytic Dileucine Motifs by the Ap2 Complex.
Authors: Kelly, B.T. / Mccoy, A.J. / Spaete, K. / Miller, S.E. / Evans, P.R. / Hoening, S. / Owen, D.J.
History
DepositionAug 29, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 28, 2008Provider: repository / Type: Initial release
Revision 1.1Jun 20, 2012Group: Database references / Derived calculations ...Database references / Derived calculations / Non-polymer description / Other / Refinement description / Version format compliance
Revision 1.2Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_conn.pdbx_leaving_atom_flag / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: AP-2 COMPLEX SUBUNIT ALPHA-2
B: AP-2 COMPLEX SUBUNIT BETA-1
E: AP-2 COMPLEX SUBUNIT BETA-1
I: AP-2 COMPLEX SUBUNIT SIGMA-1
L: AP-2 COMPLEX SUBUNIT ALPHA-2
M: AP-2 COMPLEX SUBUNIT MU-1
P: CD4 PEPTIDE
Q: CD4 PEPTIDE
S: AP-2 COMPLEX SUBUNIT SIGMA-1
U: AP-2 COMPLEX SUBUNIT MU-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)412,87741
Polymers409,89910
Non-polymers2,97831
Water34219
1
A: AP-2 COMPLEX SUBUNIT ALPHA-2
B: AP-2 COMPLEX SUBUNIT BETA-1
M: AP-2 COMPLEX SUBUNIT MU-1
P: CD4 PEPTIDE
S: AP-2 COMPLEX SUBUNIT SIGMA-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,39020
Polymers204,9505
Non-polymers1,44115
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23120 Å2
ΔGint-261.3 kcal/mol
Surface area69470 Å2
MethodPISA
2
E: AP-2 COMPLEX SUBUNIT BETA-1
I: AP-2 COMPLEX SUBUNIT SIGMA-1
L: AP-2 COMPLEX SUBUNIT ALPHA-2
Q: CD4 PEPTIDE
U: AP-2 COMPLEX SUBUNIT MU-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,48721
Polymers204,9505
Non-polymers1,53716
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area23800 Å2
ΔGint-302.3 kcal/mol
Surface area69330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)171.200, 171.200, 324.270
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22
13
23
14
24
15
25

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 3:623 )
211CHAIN L AND (RESSEQ 3:623 )
112CHAIN B AND (RESSEQ 12:582 )
212CHAIN E AND (RESSEQ 12:582 )
113CHAIN M AND (RESSEQ 1:141 OR RESSEQ 159:222 OR RESSEQ 232:435 )
213CHAIN U AND (RESSEQ 1:141 OR RESSEQ 159:222 OR RESSEQ 232:435 )
114CHAIN S AND (RESSEQ 1:142 )
214CHAIN I AND (RESSEQ 1:142 )
115CHAIN P AND (RESSEQ 2:10 )
215CHAIN Q AND (RESSEQ 2:10 )

NCS ensembles :
ID
1
2
3
4
5

NCS oper: (Code: given
Matrix: (0.005, 0.998, 0.062), (0.998, -0.009, 0.056), (0.057, 0.062, -0.996)
Vector: 6.985, 2.861, -160.492)

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Components

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AP-2 COMPLEX SUBUNIT ... , 4 types, 8 molecules ALBEISMU

#1: Protein AP-2 COMPLEX SUBUNIT ALPHA-2 / AP2 / ADAPTER-RELATED PROTEIN COMPLEX 2 ALPHA-2 SUBUNIT / ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT ...AP2 / ADAPTER-RELATED PROTEIN COMPLEX 2 ALPHA-2 SUBUNIT / ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT ALPHA-2 / ALPHA2-ADAPTIN / PLASMA MEMBRANE ADAPTOR HA2/AP2 ADAPTIN ALPHA C SUBUNIT / ALPHA-ADAPTIN C / CLATHRIN ASSEMBLY PROTEIN COMPLEX 2 ALPHA-C LARGE CHAIN / 100 KDA COATED VESICLE PROTEIN C


Mass: 69786.406 Da / Num. of mol.: 2 / Fragment: ALPHA CHAIN, RESIDUES 1-620
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PMW172K / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P17427
#2: Protein AP-2 COMPLEX SUBUNIT BETA-1 / AP2 / ADAPTER-RELATED PROTEIN COMPLEX 2 BETA-1 SUBUNIT / BETA2-ADAPTIN / BETA-ADAPTIN / PLASMA ...AP2 / ADAPTER-RELATED PROTEIN COMPLEX 2 BETA-1 SUBUNIT / BETA2-ADAPTIN / BETA-ADAPTIN / PLASMA MEMBRANE ADAPTOR HA2/AP2 ADAPTIN BETA SUBUNIT / CLATHRIN ASSEMBLY PROTEIN COMPLEX 2 BETA LARGE CHAIN / AP105B


Mass: 66953.195 Da / Num. of mol.: 2 / Fragment: BETA2 CHAIN, RESIDUES 1-591
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PMW172H6 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P63010
#3: Protein AP-2 COMPLEX SUBUNIT SIGMA-1 / AP2 / ADAPTER-RELATED PROTEIN COMPLEX 2 SIGMA-1 SUBUNIT / SIGMA2-ADAPTIN / SIGMA-ADAPTIN 3B / ...AP2 / ADAPTER-RELATED PROTEIN COMPLEX 2 SIGMA-1 SUBUNIT / SIGMA2-ADAPTIN / SIGMA-ADAPTIN 3B / PLASMA MEMBRANE ADAPTOR AP-2 17 KDA PROTEIN / CLATHRIN ASSEMBLY PROTEIN 2 SMALL CHAIN / CLATHRIN COAT ASSEMBLY PROTEIN AP17 / CLATHRIN COAT-ASSOCIATED PROTEIN AP17


Mass: 17038.688 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) MUS MUSCULUS (house mouse) / Plasmid: PMW172K / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62743
#4: Protein AP-2 COMPLEX SUBUNIT MU-1 / AP2 / MU2-ADAPTIN / AP-2 MU-2 CHAIN / PLASMA MEMBRANE ADAPTOR AP-2 50 KDA PROTEIN / CLATHRIN ...AP2 / MU2-ADAPTIN / AP-2 MU-2 CHAIN / PLASMA MEMBRANE ADAPTOR AP-2 50 KDA PROTEIN / CLATHRIN ASSEMBLY PROTEIN COMPLEX 2 MEDIUM CHAIN / CLATHRIN COAT ASSEMBLY PROTEIN AP50 / CLATHRIN COAT-ASSOCIATED PROTEIN AP50


Mass: 49726.641 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Plasmid: PMW172H6 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P84092

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Protein/peptide , 1 types, 2 molecules PQ

#5: Protein/peptide CD4 PEPTIDE / CDNA / FLJ79547 / HIGHLY SIMILAR TO T-CELL SURFACE GLYCOPROTEIN CD4


Mass: 1444.614 Da / Num. of mol.: 2 / Fragment: RESIDUES 252-262 / Mutation: YES / Source method: obtained synthetically
Details: RMS(P)EIKRLLSE. Q4 TO E MUTANT RESIDUE 3 IS PHOSPHOSERINE THOUGH NO PHOSPHORYL GROUP WAS VISIBLE IN THE STRUCTURE
Source: (synth.) HOMO SAPIENS (human) / References: UniProt: B0AZV7, UniProt: P01730*PLUS

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Non-polymers , 2 types, 50 molecules

#6: Chemical...
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 31 / Source method: obtained synthetically / Formula: SO4
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 19 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN P, GLN 255 TO GLU ENGINEERED RESIDUE IN CHAIN Q, GLN 255 TO GLU
Sequence detailsQ4 TO E MUTANT IN CHAINS P AND Q SEQUENCE OF CHAINS A AND L IS FROM MOUSE BUT HAS GLU INSERTED AT POSITION 272

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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: 2.95 Å3/Da / Density % sol: 57.96 % / Description: ISOMORPHOUS TO 2JKR
Crystal growpH: 6.5
Details: 1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE ...Details: 1.7-2.2M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH6 .5 AND 5MM DTT FROM A MIXTURE OF 10MG/ML AP2 CORE AND 7MG/ML PEPTIDE. CRYOPROTECTED WITH 1.8-2.3M AMMONIUM SULPHATE, 100MM SODIUM CITRATE PH 6.5, 17% GLYCEROL AND 7MG/ ML CD4 DILEUCINE PEPTIDE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.976
DetectorType: ADSC CCD / Detector: CCD / Date: May 23, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.976 Å / Relative weight: 1
ReflectionResolution: 3.4→47 Å / Num. obs: 64153 / % possible obs: 85.8 % / Observed criterion σ(I): -9 / Redundancy: 6.4 % / Rmerge(I) obs: 0.2 / Net I/σ(I): 7.8
Reflection shellResolution: 3.4→3.58 Å / Redundancy: 5 % / Rmerge(I) obs: 0.96 / Mean I/σ(I) obs: 1.9 / % possible all: 89.1

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
MOSFLMdata reduction
SCALAdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2JKR

2jkr


Resolution: 3.4→45.7 Å / SU ML: 0.47 / σ(F): 1.22 / Phase error: 25.78 / Stereochemistry target values: ML
Details: 28 TLS GROUPS THE PHOSPHATE OF THE PHOSPHOSERINE RESIDUES P3 AND Q3 WERE NOT VISIBLE, SO THE RESIDUE WAS MODELLED AS SERINE
RfactorNum. reflection% reflection
Rfree0.256 5902 5.1 %
Rwork0.202 --
obs0.205 116095 91.7 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 53.7 Å2 / ksol: 0.32 e/Å3
Refinement stepCycle: LAST / Resolution: 3.4→45.7 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms27946 0 155 19 28120
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00928556
X-RAY DIFFRACTIONf_angle_d1.2438646
X-RAY DIFFRACTIONf_dihedral_angle_d23.26917614
X-RAY DIFFRACTIONf_chiral_restr0.0844472
X-RAY DIFFRACTIONf_plane_restr0.0054892
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A4885X-RAY DIFFRACTIONPOSITIONAL
12L4885X-RAY DIFFRACTIONPOSITIONAL0.045
21B4527X-RAY DIFFRACTIONPOSITIONAL
22E4527X-RAY DIFFRACTIONPOSITIONAL0.041
31M3288X-RAY DIFFRACTIONPOSITIONAL
32U3288X-RAY DIFFRACTIONPOSITIONAL0.04
41S1200X-RAY DIFFRACTIONPOSITIONAL
42I1200X-RAY DIFFRACTIONPOSITIONAL0.041
51P73X-RAY DIFFRACTIONPOSITIONAL
52Q73X-RAY DIFFRACTIONPOSITIONAL0.031
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.4-3.43860.39921670.32623308X-RAY DIFFRACTION82
3.4386-3.47910.38051710.33713229X-RAY DIFFRACTION81
3.4791-3.52150.37221970.32253297X-RAY DIFFRACTION82
3.5215-3.56610.37772050.30173229X-RAY DIFFRACTION81
3.5661-3.6130.33441450.28683242X-RAY DIFFRACTION81
3.613-3.66240.31361970.29873254X-RAY DIFFRACTION82
3.6624-3.71470.36791870.30083242X-RAY DIFFRACTION81
3.7147-3.77020.33181740.27783240X-RAY DIFFRACTION82
3.7702-3.8290.31381660.26793332X-RAY DIFFRACTION82
3.829-3.89180.30651510.24573333X-RAY DIFFRACTION82
3.8918-3.95890.32471860.23513338X-RAY DIFFRACTION84
3.9589-4.03080.27131750.22663495X-RAY DIFFRACTION87
4.0308-4.10830.26861640.21113597X-RAY DIFFRACTION89
4.1083-4.19210.26552100.20643652X-RAY DIFFRACTION92
4.1921-4.28320.2822010.19383824X-RAY DIFFRACTION94
4.2832-4.38270.24112150.17443823X-RAY DIFFRACTION96
4.3827-4.49220.23311930.15653912X-RAY DIFFRACTION97
4.4922-4.61360.1822370.1543895X-RAY DIFFRACTION98
4.6136-4.74920.19151800.1594019X-RAY DIFFRACTION99
4.7492-4.90230.23522060.16123972X-RAY DIFFRACTION99
4.9023-5.07730.24071820.15784000X-RAY DIFFRACTION100
5.0773-5.28030.23642320.15573979X-RAY DIFFRACTION100
5.2803-5.52030.24672100.15944026X-RAY DIFFRACTION100
5.5203-5.81080.24232520.17043949X-RAY DIFFRACTION100
5.8108-6.1740.25072350.17873987X-RAY DIFFRACTION100
6.174-6.64940.28721970.17494022X-RAY DIFFRACTION100
6.6494-7.31610.22222110.15164009X-RAY DIFFRACTION100
7.3161-8.36910.19122450.12933982X-RAY DIFFRACTION100
8.3691-10.52290.11912390.09873973X-RAY DIFFRACTION100
10.5229-45.70290.21431720.20874033X-RAY DIFFRACTION99
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)
10.0608-0.0943-0.03840.01230.03520.0260.07280.2439-0.1171-0.0643-0.04670.11940.19670.180.00010.54590.2363-0.24811.07620.01350.97481.5372-24.6574-98.12
20.58230.11850.00650.07850.22510.46660.4202-0.3316-0.1559-0.1380.3017-0.37790.0001-0.09370.06120.29270.03690.08640.15390.01540.525473.4708-4.1731-108.3043
30.13450.061-0.0419-0.1716-0.21210.17240.44830.58940.1142-0.0372-0.1725-0.1591-0.3139-0.1584-0.0050.1260.18150.25110.58040.18480.397648.9791.7329-119.3737
40.9827-0.5193-0.4150.34030.30410.26260.10090.3347-0.25830.2111-0.3484-0.0378-0.0853-0.03750.01610.2099-0.0948-0.00470.319-0.03270.197229.6-8.1417-98.7284
50.99550.1239-0.6130.32190.20680.6297-0.43510.2703-0.26060.23430.15550.04220.0060.0385-0.96880.37760.1888-0.11430.28360.0871-0.029415.1758-0.4681-55.3119
60.0006-0.0058-0.00240.003-0.0023-0.01370.21460.0679-0.0072-0.1226-0.147-0.0430.0264-0.079-0.00270.59540.1074-0.14920.38660.14080.37330.421925.546-89.1977
7-0.00590.0155-0.0063-0.00720.0056-0.00960.14180.18520.01130.0711-0.21620.0299-0.0647-0.11570.00010.6943-0.3254-0.10020.9588-0.10061.025968.1066-46.5241-83.6373
8-0.0770.0518-0.1378-0.00120.03450.1481-0.36250.1417-0.50930.1252-0.01320.1086-0.1921-0.0112-0.00050.5763-0.1275-0.06040.4302-0.08260.545855.651-52.2353-58.7327
90.0624-0.05070.46370.47120.29240.4264-0.1816-0.13640.06260.10050.5076-0.44930.0845-0.22990.3230.34680.2754-0.2998-0.85560.22940.334453.3283-16.2579-37.8214
100.2629-0.0634-0.392-0.00120.36140.1242-0.0421-0.05040.18220.28590.1753-0.24630.0675-0.3760.00270.4546-0.0604-0.22080.26960.05550.242129.368316.6715-48.9778
110.0201-0.04580.0432-0.00340.00260.02940.43430.02290.04470.02280.15540.1715-0.08060.0615-0.00040.2945-0.1858-0.02250.26140.04020.451641.1391-22.4707-43.8601
120.4367-0.0513-0.39020.0659-0.19870.85620.20690.2438-0.07650.20230.0285-0.22-0.3167-0.10120.13430.29130.0274-0.31370.3320.01650.583560.9809-29.3665-62.512
13-0.0823-0.1890.3028-0.0391-0.1357-0.1377-0.04440.23730.19820.2288-0.0626-0.07420.02880.1713-00.4614-0.0528-0.14860.55720.12140.559754.04074.9406-71.4299
140.35550.05540.0392-0.10630.19970.19430.1412-0.5051-0.4494-0.25630.005-0.2180.24180.07050.00970.39410.0282-0.04340.36530.00660.373757.4102-17.4278-102.046
150.12510.1574-0.19480.09010.06110.08280.11150.3947-0.05180.4627-0.05560.118-0.0461-0.17550.00020.45370.1570.11190.33160.29390.4905-23.526178.5966-60.3461
160.1858-0.0506-0.18260.6136-0.00630.84760.0002-0.01580.2295-0.23650.4592-0.1263-0.0502-0.22670.060.221-0.0180.04240.2469-0.0080.6647-3.811269.649-49.402
170.2688-0.0548-0.09320.9169-0.42031.0589-0.0549-0.25140.22130.4480.5729-0.08830.3195-0.01630.18470.38180.0777-0.2315-0.0033-0.08610.20371.178744.419-39.6211
180.66120.0138-0.14510.46580.2271.0084-0.50460.19090.14710.2408-0.05350.18050.1562-0.0788-0.94060.3694-0.1070.11930.09320.0425-0.2308-7.448226.5405-62.0997
190.4566-0.4388-0.60240.33850.41620.18160.25150.2792-0.1432-0.0098-0.45220.2089-0.109-0.2243-0.09380.31780.13230.08130.44510.0704-0.00432.930414.8672-105.7844
20-0.0050.00710.0018-0.0089-0.0175-0.0063-0.10660.0254-0.22190.1965-0.04040.1692-0.0471-0.053-0.00010.56290.0748-0.10090.34150.1770.481426.802527.6039-69.3759
210.01460.01420.01930.01750.01010.0055-0.47630.016-0.11620.0813-0.00260.1015-0.04440.05130.00041.1379-0.28140.15870.7103-0.08381.2301-44.376166.3771-76.6919
220.06330.0237-0.1128-0.07430.14210.0496-0.1512-0.03270.15930.0039-0.27540.80350.08070.0642-0.00080.48930.05550.10.62990.04350.5577-48.973255.3297-102.4741
230.8219-0.0166-0.2771-0.111-0.30880.47050.5723-0.38980.4686-0.12750.0986-0.34630.2205-0.04520.05420.09520.07570.03530.01920.658-0.0388-12.063753.8883-121.7826
240.2224-0.2503-0.27330.21690.22610.15270.22930.35850.3204-0.0496-0.1742-0.47970.0985-0.0130.12710.3145-0.0343-0.02790.29160.16240.225520.219929.1327-110.4277
25-0.0115-0.04630.01940.013-0.07030.02920.0281-0.0963-0.4343-0.0080.5395-0.1807-0.1271-0.1101-0.00040.2912-0.18550.0640.652-0.06740.6776-18.608941.4364-116.7088
260.2495-0.10240.29130.20330.21260.54220.05990.48040.30230.45660.03510.127-0.02030.16120.09140.35580.0580.09210.2590.26070.3243-26.167160.4547-97.3684
270.1809-0.16110.0568-0.1582-0.2439-0.0329-0.03150.23130.00330.2770.0423-0.1639-0.23310.06740.00170.4519-0.0034-0.07040.38680.15620.28937.569452.4395-87.2323
28-0.0073-0.2706-0.30990.9077-0.05680.07660.2228-0.07540.1054-0.43730.0120.2885-0.2213-0.15520.02310.37-0.02580.09570.4040.07540.2328-16.67354.3462-57.5909
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND RESID 1:50)
2X-RAY DIFFRACTION2CHAIN A AND RESID 51:186)
3X-RAY DIFFRACTION3CHAIN A AND RESID 187:245)
4X-RAY DIFFRACTION4CHAIN A AND RESID 246:457)
5X-RAY DIFFRACTION5CHAIN A AND RESID 458:610)
6X-RAY DIFFRACTION6CHAIN A AND RESID 611:999)
7X-RAY DIFFRACTION7CHAIN B AND RESID 10:51)
8X-RAY DIFFRACTION8CHAIN B AND RESID 52:206)
9X-RAY DIFFRACTION9CHAIN B AND RESID 207:414)
10X-RAY DIFFRACTION10CHAIN B AND RESID 415:549)
11X-RAY DIFFRACTION11CHAIN B AND RESID 550:582)
12X-RAY DIFFRACTION12CHAIN M AND RESID 1:159)
13X-RAY DIFFRACTION13CHAIN M AND RESID 160:435)
14X-RAY DIFFRACTION14CHAIN S AND RESID 1:142) OR CHAIN P
15X-RAY DIFFRACTION15CHAIN L AND RESID 1:50)
16X-RAY DIFFRACTION16CHAIN L AND RESID 51:186)
17X-RAY DIFFRACTION17CHAIN L AND RESID 187:245)
18X-RAY DIFFRACTION18CHAIN L AND RESID 246:457)
19X-RAY DIFFRACTION19CHAIN L AND RESID 458:610)
20X-RAY DIFFRACTION20CHAIN L AND RESID 611:999)
21X-RAY DIFFRACTION21CHAIN E AND RESID 10:51)
22X-RAY DIFFRACTION22CHAIN E AND RESID 52:206)
23X-RAY DIFFRACTION23CHAIN E AND RESID 207:414)
24X-RAY DIFFRACTION24CHAIN E AND RESID 415:549)
25X-RAY DIFFRACTION25CHAIN E AND RESID 550:582)
26X-RAY DIFFRACTION26CHAIN U AND RESID 1:159)
27X-RAY DIFFRACTION27CHAIN U AND RESID 160:435)
28X-RAY DIFFRACTION28CHAIN I AND RESID 1:142) OR CHAIN Q

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