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- PDB-4uqi: AP2 controls clathrin polymerization with a membrane-activated switch -

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Basic information

Entry
Database: PDB / ID: 4uqi
TitleAP2 controls clathrin polymerization with a membrane-activated switch
Components(AP-2 COMPLEX SUBUNIT ...) x 4
KeywordsENDOCYTOSIS / PROTEIN TRANSPORT / LIPID BINDING
Function / homology
Function and homology information


LDL clearance / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / Gap junction degradation / Formation of annular gap junctions / WNT5A-dependent internalization of FZD4 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / Nef Mediated CD8 Down-regulation / Trafficking of GluR2-containing AMPA receptors / LDL clearance / Retrograde neurotrophin signalling ...LDL clearance / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / Gap junction degradation / Formation of annular gap junctions / WNT5A-dependent internalization of FZD4 / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / Nef Mediated CD8 Down-regulation / Trafficking of GluR2-containing AMPA receptors / LDL clearance / Retrograde neurotrophin signalling / Retrograde neurotrophin signalling / VLDLR internalisation and degradation / WNT5A-dependent internalization of FZD2, FZD5 and ROR2 / WNT5A-dependent internalization of FZD4 / Trafficking of GluR2-containing AMPA receptors / clathrin adaptor complex / VLDLR internalisation and degradation / WNT5A-dependent internalization of FZD4 / Recycling pathway of L1 / extrinsic component of presynaptic endocytic zone membrane / MHC class II antigen presentation / regulation of vesicle size / postsynaptic endocytic zone / AP-2 adaptor complex / postsynaptic neurotransmitter receptor internalization / Cargo recognition for clathrin-mediated endocytosis / Recycling pathway of L1 / Retrograde neurotrophin signalling / clathrin-coated endocytic vesicle / membrane coat / Clathrin-mediated endocytosis / clathrin coat assembly / positive regulation of synaptic vesicle endocytosis / Cargo recognition for clathrin-mediated endocytosis / clathrin adaptor activity / Clathrin-mediated endocytosis / LDL clearance / vesicle budding from membrane / clathrin-dependent endocytosis / MHC class II antigen presentation / signal sequence binding / coronary vasculature development / Nef Mediated CD4 Down-regulation / positive regulation of protein localization to membrane / neurotransmitter secretion / endolysosome membrane / aorta development / Neutrophil degranulation / ventricular septum development / low-density lipoprotein particle receptor binding / clathrin binding / Trafficking of GluR2-containing AMPA receptors / Recycling pathway of L1 / positive regulation of receptor internalization / positive regulation of endocytosis / EPH-ephrin mediated repulsion of cells / synaptic vesicle endocytosis / negative regulation of protein localization to plasma membrane / vesicle-mediated transport / clathrin-coated pit / phosphatidylinositol binding / MHC class II antigen presentation / protein serine/threonine kinase binding / VLDLR internalisation and degradation / intracellular protein transport / kidney development / clathrin-coated endocytic vesicle membrane / receptor internalization / kinase binding / cytoplasmic side of plasma membrane / terminal bouton / disordered domain specific binding / synaptic vesicle / endocytic vesicle membrane / Cargo recognition for clathrin-mediated endocytosis / presynapse / Clathrin-mediated endocytosis / protein-containing complex assembly / cytoplasmic vesicle / Potential therapeutics for SARS / transmembrane transporter binding / postsynapse / protein domain specific binding / synapse / lipid binding / protein kinase binding / protein-containing complex binding / glutamatergic synapse / membrane / plasma membrane / cytosol
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 / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta2-adaptin appendage, C-terminal sub-domain ...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 / Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain / Beta2-adaptin appendage, C-terminal sub-domain / AP-1/2/4 complex subunit beta / Adaptor protein complex, sigma subunit / : / Beta-adaptin appendage, C-terminal subdomain / Beta2-adaptin appendage, C-terminal sub-domain / AP complex subunit beta / 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. / : / Coatomer/calthrin adaptor appendage, C-terminal subdomain / Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain / Adaptin C-terminal domain / Adaptin C-terminal domain / AP complex, mu/sigma subunit / Adaptor complexes medium subunit family / Clathrin adaptor complex small chain / Clathrin/coatomer adaptor, adaptin-like, N-terminal / Adaptin N terminal region / AP-2 complex subunit mu, C-terminal superfamily / Mu homology domain / Mu homology domain (MHD) profile. / Clathrin adaptor, appendage, Ig-like subdomain superfamily / Longin-like domain superfamily / TBP domain superfamily / Armadillo/beta-catenin-like repeats / Armadillo / Leucine-rich Repeat Variant / Leucine-rich Repeat Variant / Beta-Lactamase / Armadillo-like helical / Alpha Horseshoe / Armadillo-type fold / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
INOSITOL HEXAKISPHOSPHATE / 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 speciesRATTUS NORVEGICUS (Norway rat)
HOMO SAPIENS (human)
MUS MUSCULUS (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.79 Å
AuthorsKelly, B.T. / Graham, S.C. / Liska, N. / Dannhauser, P.N. / Hoening, S. / Ungewickell, E.J. / Owen, D.J.
CitationJournal: Science / Year: 2014
Title: Clathrin Adaptors. Ap2 Controls Clathrin Polymerization with a Membrane-Activated Switch.
Authors: Kelly, B.T. / Graham, S.C. / Liska, N. / Dannhauser, P.N. / Honing, S. / Ungewickell, E.J. / Owen, D.J.
History
DepositionJun 23, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 30, 2014Provider: repository / Type: Initial release
Revision 1.1Aug 6, 2014Group: Database references
Revision 1.2Oct 7, 2020Group: Derived calculations / Other / Structure summary / Category: chem_comp / pdbx_database_status / struct_site
Item: _chem_comp.pdbx_synonyms / _pdbx_database_status.status_code_sf ..._chem_comp.pdbx_synonyms / _pdbx_database_status.status_code_sf / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.3Jan 10, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _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: AP-2 COMPLEX SUBUNIT ALPHA-2
B: AP-2 COMPLEX SUBUNIT BETA
M: AP-2 COMPLEX SUBUNIT MU
S: AP-2 COMPLEX SUBUNIT SIGMA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)213,0246
Polymers212,3294
Non-polymers6952
Water543
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21000 Å2
ΔGint-98.2 kcal/mol
Surface area71240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)121.300, 121.300, 259.370
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number152
Space group name H-MP3121

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Components

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AP-2 COMPLEX SUBUNIT ... , 4 types, 4 molecules ABMS

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


Mass: 70310.062 Da / Num. of mol.: 1 / Fragment: ALPHA SUBUNIT TRUNK DOMAIN, RESIDUES 1-620
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Plasmid: PMW172K / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P18484
#2: Protein AP-2 COMPLEX SUBUNIT BETA / AP105B / ADAPTER-RELATED PROTEIN COMPLEX 2 SUBUNIT BETA / ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT BETA ...AP105B / ADAPTER-RELATED PROTEIN COMPLEX 2 SUBUNIT BETA / ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT BETA / BETA-2-ADAPTIN / BETA-ADAPTIN / CLATHRIN ASSEMBLY PROTEIN COMPLEX 2 BETA LARGE CHAIN / PLASMA MEMBRANE ADAPTOR HA2/AP2 ADAPTIN BETA SUBUNIT


Mass: 73935.914 Da / Num. of mol.: 1
Fragment: BETA 2 SUBUNIT EXTENDED TRUNK DOMAIN, RESIDUES 1-651
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PMW172 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P63010
#3: Protein AP-2 COMPLEX SUBUNIT MU / AP-2 MU CHAIN / ADAPTER-RELATED PROTEIN COMPLEX 2 SUBUNIT MU / ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT ...AP-2 MU CHAIN / ADAPTER-RELATED PROTEIN COMPLEX 2 SUBUNIT MU / ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT MU / CLATHRIN ASSEMBLY PROTEIN COMPLEX 2 MU MEDIUM CHAIN / CLATHRIN COAT ASSEMBLY PROTEIN AP50 / CLATHRIN COAT-ASSOCIATED PROTEIN AP50 / MU2-ADAPTIN / PLASMA MEMBRANE ADAPTOR AP-2 50 KDA PROTEIN


Mass: 51044.113 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) RATTUS NORVEGICUS (Norway rat) / Plasmid: PMW172 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): PLYSS / References: UniProt: P84092
#4: Protein AP-2 COMPLEX SUBUNIT SIGMA / ADAPTER-RELATED PROTEIN COMPLEX 2 SUBUNIT SIGMA / ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT SIGMA / ...ADAPTER-RELATED PROTEIN COMPLEX 2 SUBUNIT SIGMA / ADAPTOR PROTEIN COMPLEX AP-2 SUBUNIT SIGMA / CLATHRIN ASSEMBLY PROTEIN 2 SIGMA SMALL CHAIN / CLATHRIN COAT ASSEMBLY PROTEIN AP17 / CLATHRIN COAT-ASSOCIATED PROTEIN AP17 / PLASMA MEMBRANE ADAPTOR AP-2 17 KDA PROTEIN / SIGMA-ADAPTIN 3B / SIGMA2-ADAPTIN


Mass: 17038.688 Da / Num. of mol.: 1
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) / Variant (production host): PLYSS / References: UniProt: P62743

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Non-polymers , 3 types, 5 molecules

#5: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#6: Chemical ChemComp-IHP / INOSITOL HEXAKISPHOSPHATE / MYO-INOSITOL HEXAKISPHOSPHATE / INOSITOL 1,2,3,4,5,6-HEXAKISPHOSPHATE


Mass: 660.035 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H18O24P6
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsCHAIN A: GLU INSERTED BETWEEN RESIDUES 271 AND 272 CHAIN M: MYC TAG INSERTED BETWEEN RESIDUES 236 AND 237

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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: 2.75 Å3/Da / Density % sol: 55.37 %
Description: SOLVED BY MOLECULAR REPLACEMENT FROM AN ISOMORPHOUS MODEL
Crystal growpH: 6.2
Details: 18% PEG1000, 10MM NA/K PHOSPHATE PH 6.2, 200MM NACL, 4MM DTT, IP6

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9393
DetectorType: ADSC CCD / Detector: CCD / Date: Oct 20, 2010 / Details: MIRRORS
RadiationMonochromator: DOUBLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9393 Å / Relative weight: 1
ReflectionResolution: 2.79→97.37 Å / Num. obs: 55666 / % possible obs: 99.9 % / Observed criterion σ(I): -3 / Redundancy: 10.9 % / Biso Wilson estimate: 74.2 Å2 / Rmerge(I) obs: 0.07 / Net I/σ(I): 21.9
Reflection shellResolution: 2.79→2.86 Å / Redundancy: 11.2 % / Rmerge(I) obs: 0.86 / Mean I/σ(I) obs: 3.2 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.8.0049refinement
XDSdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2VGL

2vgl


Resolution: 2.79→97.37 Å / Cor.coef. Fo:Fc: 0.949 / Cor.coef. Fo:Fc free: 0.915 / SU B: 33.604 / SU ML: 0.302 / Cross valid method: THROUGHOUT / ESU R Free: 0.378 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES WITH TLS ADDED.
RfactorNum. reflection% reflectionSelection details
Rfree0.2592 2824 5.1 %RANDOM
Rwork0.20292 ---
obs0.20573 52840 99.92 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 83.089 Å2
Baniso -1Baniso -2Baniso -3
1-0.22 Å20.11 Å20 Å2
2--0.22 Å20 Å2
3----0.7 Å2
Refinement stepCycle: LAST / Resolution: 2.79→97.37 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13849 0 37 3 13889
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0120.01914130
X-RAY DIFFRACTIONr_bond_other_d0.0010.0213921
X-RAY DIFFRACTIONr_angle_refined_deg1.5381.97619140
X-RAY DIFFRACTIONr_angle_other_deg2.152331999
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.32851727
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.54524.369634
X-RAY DIFFRACTIONr_dihedral_angle_3_deg17.55152599
X-RAY DIFFRACTIONr_dihedral_angle_4_deg16.7751592
X-RAY DIFFRACTIONr_chiral_restr0.0820.22228
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.02115693
X-RAY DIFFRACTIONr_gen_planes_other0.0040.023123
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it1.5733.9326931
X-RAY DIFFRACTIONr_mcbond_other1.5733.9326930
X-RAY DIFFRACTIONr_mcangle_it2.4195.8978650
X-RAY DIFFRACTIONr_mcangle_other2.4195.8978651
X-RAY DIFFRACTIONr_scbond_it1.824.1057197
X-RAY DIFFRACTIONr_scbond_other1.824.1057194
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other2.8176.09810488
X-RAY DIFFRACTIONr_long_range_B_refined3.90731.25616319
X-RAY DIFFRACTIONr_long_range_B_other3.90731.25716320
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.792→2.865 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.327 205 -
Rwork0.277 3869 -
obs--100 %
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)
15.1768-1.7552.27684.5335-0.68925.03210.06080.3798-0.1216-0.27430.00960.2610.0065-0.1152-0.07040.2522-0.0364-0.0340.46330.06650.026688.32445.293-15.89
21.2277-0.1569-0.17141.2265-0.12664.54860.01770.1725-0.1793-0.05740.0115-0.15060.60690.3437-0.02910.19570.0493-0.02590.2295-0.04160.0566103.52525.87912.424
37.361-1.1816-2.89550.24540.48751.4075-0.0935-0.27790.16490.15640.03140.0125-0.05460.00090.0620.46310.02260.00110.4778-0.07550.138365.42935.77544.473
44.2922-0.1116-0.32442.79370.47824.4126-0.1551-0.3278-0.24970.38580.22640.3924-0.0176-0.4808-0.07130.39330.11970.14660.7658-0.03930.328533.31734.29648.463
54.0296-3.28871.01117.6887-1.21610.3418-0.221-0.02530.35830.21990.16620.11-0.2248-0.01220.05480.51820.06780.07470.46290.10070.432383.99768.6762.553
64.88590.7291-0.96510.98860.23950.75750.2009-0.68091.0010.20860.04910.3121-0.535-0.0535-0.250.9560.17840.2790.70160.05091.119255.99781.05115.122
74.0297-0.995-0.84044.63680.35651.98430.6820.74840.3961-0.115-0.26850.6162-0.3406-0.7789-0.41350.30930.27570.12740.99240.24970.465832.556.22710.74
84.84251.2115-4.22931.9329-2.29666.6019-0.1510.3012-0.30720.14070.04670.25950.5757-0.90680.10430.3424-0.0774-0.06920.9401-0.17380.462128.92929.16519.016
95.9201-0.13062.16712.68380.5434.1367-0.0066-0.264-1.1263-0.00470.10680.29920.7031-1.0208-0.10030.6162-0.15570.14270.83540.03850.673231.26520.30839.272
1019.9609-3.76650.88150.7546-0.18368.64570.1083-1.12320.38390.1010.105-0.0728-0.1906-0.7032-0.21330.5875-0.07240.13550.57450.03550.515140.9858.68124.816
1110.3088-0.93162.42810.2792-1.38087.57780.17550.67861.6763-0.09180.0895-0.06180.5593-0.5531-0.2650.56470.0824-0.06530.5472-0.08390.495651.15746.06937.172
128.1821-2.9213-1.87591.05190.77942.26060.38771.0910.0765-0.1281-0.3331-0.0010.22120.4818-0.05460.8732-0.0035-0.13930.7786-0.09960.616950.09139.44724.623
134.49010.6194-2.46253.2524-1.4424.77730.44210.5730.46650.1615-0.0643-0.1616-0.2113-0.3267-0.37780.27210.19070.05180.51620.15420.559561.27159.047.241
148.82960.51217.29331.75790.40866.22520.0090.17910.1943-0.3534-0.06390.3753-0.12770.12230.05490.23590.03190.00230.2614-0.00120.133551.57327.1420.347
154.03860.31814.38790.79580.38975.611-0.18570.45750.3247-0.24580.01080.1035-0.40280.52270.17490.2702-0.0159-0.0160.2995-0.00560.080358.8529.9452.471
168.0226-3.69761.73447.1423-0.91865.54550.1528-0.5612-0.43260.4990.0246-0.08610.4554-0.39-0.17740.3766-0.1384-0.00150.31230.03120.04764.36116.69129.808
1716.6285-5.34332.78412.5743-4.787512.91440.21620.1069-0.06750.5138-0.2495-2.18420.88551.90840.03330.67910.0997-0.22060.4876-0.09390.665183.57911.9831.593
187.0025-1.38986.06311.7047-1.59396.49060.1548-0.30440.0067-0.09230.03420.49040.0416-0.5149-0.1890.20430.0442-0.00150.2701-0.02330.177949.78227.5366.114
195.02480.93750.96041.7574-1.24716.9296-0.1430.14830.30920.0090.1530.2099-0.2142-0.5303-0.010.10410.0451-0.02070.24770.00320.036783.54138.42110.34
201.74280.7885-0.24462.6527-1.11154.3258-0.01080.04630.2315-0.04040.0573-0.0418-0.22420.0316-0.04650.08790.0328-0.00940.2095-0.00410.044995.70742.9888.52
211.31492.65831.31647.11492.17462.22140.0465-0.0218-0.110.060.1165-0.18810.16570.3271-0.1630.12730.0655-0.03760.2881-0.01370.0196104.6835.5299.632
227.74164.40267.47865.44223.478515.1423-0.21950.3538-0.2453-0.35670.0986-0.3605-0.6245-0.04020.12080.21520.0274-0.01310.3535-0.01960.1304110.37941.84-1.904
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A9 - 76
2X-RAY DIFFRACTION2A77 - 332
3X-RAY DIFFRACTION3A333 - 538
4X-RAY DIFFRACTION4A539 - 608
5X-RAY DIFFRACTION5B4 - 78
6X-RAY DIFFRACTION6B79 - 247
7X-RAY DIFFRACTION7B248 - 364
8X-RAY DIFFRACTION8B365 - 456
9X-RAY DIFFRACTION9B457 - 552
10X-RAY DIFFRACTION10B553 - 582
11X-RAY DIFFRACTION11B618 - 623
12X-RAY DIFFRACTION12B624 - 635
13X-RAY DIFFRACTION13M1 - 141
14X-RAY DIFFRACTION14M159 - 222
15X-RAY DIFFRACTION15M240 - 292
16X-RAY DIFFRACTION16M293 - 368
17X-RAY DIFFRACTION17M369 - 384
18X-RAY DIFFRACTION18M385 - 435
19X-RAY DIFFRACTION19S1 - 61
20X-RAY DIFFRACTION20S62 - 118
21X-RAY DIFFRACTION21S119 - 132
22X-RAY DIFFRACTION22S133 - 142

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