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- PDB-5ibk: Skp1-F-box in complex with a ubiquitin variant -

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Basic information

Entry
Database: PDB / ID: 5ibk
TitleSkp1-F-box in complex with a ubiquitin variant
Components
  • F-box/WD repeat-containing protein 7
  • Polyubiquitin-B
  • S-phase kinase-associated protein 1,S-phase kinase-associated protein 1
KeywordsPROTEIN BINDING / phage display / SCF inhibitors / Fbxw7 / Fbxw11 / ?-Trcp / ubiquitin
Function / homology
Function and homology information


negative regulation of SREBP signaling pathway / negative regulation of triglyceride biosynthetic process / regulation of cell migration involved in sprouting angiogenesis / positive regulation of epidermal growth factor-activated receptor activity / negative regulation of hepatocyte proliferation / regulation of lipid storage / Parkin-FBXW7-Cul1 ubiquitin ligase complex / ubiquitin recycling / ubiquitin-protein transferase activator activity / F-box domain binding ...negative regulation of SREBP signaling pathway / negative regulation of triglyceride biosynthetic process / regulation of cell migration involved in sprouting angiogenesis / positive regulation of epidermal growth factor-activated receptor activity / negative regulation of hepatocyte proliferation / regulation of lipid storage / Parkin-FBXW7-Cul1 ubiquitin ligase complex / ubiquitin recycling / ubiquitin-protein transferase activator activity / F-box domain binding / regulation of mitophagy / phosphothreonine residue binding / regulation of cell cycle G1/S phase transition / negative regulation of osteoclast development / PcG protein complex / positive regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway / positive regulation of ubiquitin protein ligase activity / Cul7-RING ubiquitin ligase complex / maintenance of protein location in nucleus / Loss of Function of FBXW7 in Cancer and NOTCH1 Signaling / positive regulation of proteasomal protein catabolic process / vasculature development / positive regulation of ubiquitin-dependent protein catabolic process / hypothalamus gonadotrophin-releasing hormone neuron development / female meiosis I / positive regulation of protein targeting to mitochondrion / sister chromatid cohesion / positive regulation of protein monoubiquitination / SCF ubiquitin ligase complex / positive regulation of ubiquitin-protein transferase activity / fat pad development / mitochondrion transport along microtubule / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / ubiquitin ligase complex scaffold activity / female gonad development / seminiferous tubule development / Prolactin receptor signaling / lipid homeostasis / Association of TriC/CCT with target proteins during biosynthesis / male meiosis I / cullin family protein binding / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / negative regulation of Notch signaling pathway / protein monoubiquitination / ubiquitin-like ligase-substrate adaptor activity / vasculogenesis / protein K48-linked ubiquitination / Nuclear events stimulated by ALK signaling in cancer / energy homeostasis / regulation of neuron apoptotic process / Notch signaling pathway / regulation of proteasomal protein catabolic process / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Endosomal Sorting Complex Required For Transport (ESCRT) / Regulation of TBK1, IKKε (IKBKE)-mediated activation of IRF3, IRF7 / Negative regulation of FLT3 / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Regulation of TBK1, IKKε-mediated activation of IRF3, IRF7 upon TLR3 ligation / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / NOTCH2 Activation and Transmission of Signal to the Nucleus / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Regulation of FZD by ubiquitination / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / APC-Cdc20 mediated degradation of Nek2A / InlA-mediated entry of Listeria monocytogenes into host cells / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / Regulation of innate immune responses to cytosolic DNA / NF-kB is activated and signals survival / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / cyclin binding / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / neuron projection morphogenesis / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / regulation of mitochondrial membrane potential / TICAM1, RIP1-mediated IKK complex recruitment / molecular function activator activity / Translesion synthesis by REV1
Similarity search - Function
Monooxygenase - #50 / A Receptor for Ubiquitination Targets / F-box domain profile. / F-box-like domain superfamily / F-box-like / SKP1 component, dimerisation / S-phase kinase-associated protein 1 / SKP1-like, dimerisation domain superfamily / Skp1 family, dimerisation domain / F-box domain ...Monooxygenase - #50 / A Receptor for Ubiquitination Targets / F-box domain profile. / F-box-like domain superfamily / F-box-like / SKP1 component, dimerisation / S-phase kinase-associated protein 1 / SKP1-like, dimerisation domain superfamily / Skp1 family, dimerisation domain / F-box domain / Monooxygenase / Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / SKP1/BTB/POZ domain superfamily / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-B / S-phase kinase-associated protein 1 / F-box/WD repeat-containing protein 7
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.503 Å
AuthorsOrlicky, S. / Sicheri, F.
Funding support Canada, United States, 3items
OrganizationGrant numberCountry
Canadian Institutes of Health Research (CIHR)MOP-126129 Canada
Canadian Institutes of Health Research (CIHR)(MOP-136956 Canada
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM103403 United States
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2016
Title: Inhibition of SCF ubiquitin ligases by engineered ubiquitin variants that target the Cul1 binding site on the Skp1-F-box interface.
Authors: Gorelik, M. / Orlicky, S. / Sartori, M.A. / Tang, X. / Marcon, E. / Kurinov, I. / Greenblatt, J.F. / Tyers, M. / Moffat, J. / Sicheri, F. / Sidhu, S.S.
History
DepositionFeb 22, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 30, 2016Provider: repository / Type: Initial release
Revision 1.1Apr 13, 2016Group: Data collection
Revision 1.2Sep 13, 2017Group: Advisory / Author supporting evidence / Derived calculations
Category: pdbx_audit_support / pdbx_struct_oper_list / pdbx_unobs_or_zero_occ_atoms
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Sep 27, 2023Group: Advisory / Data collection ...Advisory / 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 / pdbx_unobs_or_zero_occ_atoms / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: S-phase kinase-associated protein 1,S-phase kinase-associated protein 1
B: F-box/WD repeat-containing protein 7
F: Polyubiquitin-B
C: Polyubiquitin-B
D: S-phase kinase-associated protein 1,S-phase kinase-associated protein 1
E: F-box/WD repeat-containing protein 7


Theoretical massNumber of molelcules
Total (without water)66,6126
Polymers66,6126
Non-polymers00
Water68538
1
A: S-phase kinase-associated protein 1,S-phase kinase-associated protein 1
B: F-box/WD repeat-containing protein 7
C: Polyubiquitin-B


Theoretical massNumber of molelcules
Total (without water)33,3063
Polymers33,3063
Non-polymers00
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4440 Å2
ΔGint-32 kcal/mol
Surface area13620 Å2
MethodPISA
2
F: Polyubiquitin-B
D: S-phase kinase-associated protein 1,S-phase kinase-associated protein 1
E: F-box/WD repeat-containing protein 7


Theoretical massNumber of molelcules
Total (without water)33,3063
Polymers33,3063
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4600 Å2
ΔGint-35 kcal/mol
Surface area13430 Å2
MethodPISA
Unit cell
Length a, b, c (Å)63.368, 98.015, 107.704
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain D
12chain B
22chain E
13chain C
23chain F

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11GLYGLYGLUGLUchain AAA-1 - 1561 - 144
21METMETCYSCYSchain DDE1 - 1603 - 148
12GLNGLNARGARGchain BBB277 - 32217 - 62
22GLNGLNARGARGchain EEF275 - 32215 - 62
13GLYGLYARGARGchain CCD-1 - 743 - 78
23SERSERARGARGchain FFC0 - 744 - 78

NCS ensembles :
ID
1
2
3

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Components

#1: Protein S-phase kinase-associated protein 1,S-phase kinase-associated protein 1 / Cyclin-A/CDK2-associated protein p19 / p19A / Organ of Corti protein 2 / OCP-2 / Organ of Corti ...Cyclin-A/CDK2-associated protein p19 / p19A / Organ of Corti protein 2 / OCP-2 / Organ of Corti protein II / OCP-II / RNA polymerase II elongation factor-like protein / SIII / Transcription elongation factor B polypeptide 1-like / p19skp1


Mass: 16981.295 Da / Num. of mol.: 2
Fragment: UNP resdiues 1-61(deletion 37-42) and 70-163 linked by LINKER GGSG,UNP resdiues 1-61(deletion 37-42) and 70-163 linked by LINKER GGSG
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SKP1, EMC19, OCP2, SKP1A, TCEB1L / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P63208
#2: Protein F-box/WD repeat-containing protein 7 / Archipelago homolog / hAgo / F-box and WD-40 domain-containing protein 7 / F-box protein FBX30 / ...Archipelago homolog / hAgo / F-box and WD-40 domain-containing protein 7 / F-box protein FBX30 / SEL-10 / hCdc4


Mass: 7513.756 Da / Num. of mol.: 2 / Fragment: UNP residues 263-323
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FBXW7, FBW7, FBX30, SEL10 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: Q969H0
#3: Protein Polyubiquitin-B


Mass: 8811.088 Da / Num. of mol.: 2 / Fragment: UNP residues 75-150
Mutation: L8G, T9A, G10R, K11T, T12A, R42I, A46S, G47R, Q49L, Q62H, K63R, H68R, R72I, L73F
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBB / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P0CG47
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 38 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.51 Å3/Da / Density % sol: 51.01 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 4.5 / Details: 100 mM Acetate pH 4.5, 12% PEG 4000, 15% glyerol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9795 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Aug 7, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 2.5→47.709 Å / Num. obs: 23666 / % possible obs: 99.4 % / Redundancy: 4.4 % / Biso Wilson estimate: 64.87 Å2 / Rmerge(I) obs: 0.046 / Rpim(I) all: 0.024 / Rrim(I) all: 0.052 / Χ2: 0.43 / Net I/av σ(I): 19.63 / Net I/σ(I): 5.6 / Num. measured all: 103319
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsDiffraction-ID% possible all
2.5-2.563.90.657199.1
2.56-2.624.50.557199.8
2.62-2.694.60.4631100
2.69-2.774.50.3691100
2.77-2.864.50.263199.6
2.86-2.964.50.2199.3
2.96-3.084.20.161199.6
3.08-3.224.20.119199
3.22-3.394.60.082199.8
3.39-3.614.50.064199.8
3.61-3.884.40.05199.1
3.88-4.274.20.037198.5
4.27-4.894.50.029199.8
4.89-6.164.20.03198.5
6.16-504.20.021198.8

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Processing

Software
NameVersionClassification
SCALEPACKdata scaling
PHENIX1.8.2_1309refinement
PDB_EXTRACT3.2data extraction
HKL-2000data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2OVR, 1UBQ

2ovr

1ubq


Resolution: 2.503→47.709 Å / SU ML: 0.41 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 25.53
RfactorNum. reflection% reflection
Rfree0.2399 1210 5.12 %
Rwork0.1997 --
obs0.2016 23612 99.25 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 218.53 Å2 / Biso mean: 80.85 Å2 / Biso min: 22.36 Å2
Refinement stepCycle: final / Resolution: 2.503→47.709 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4246 0 0 38 4284
Biso mean---51.21 -
Num. residues----526
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0044314
X-RAY DIFFRACTIONf_angle_d0.8795830
X-RAY DIFFRACTIONf_chiral_restr0.035680
X-RAY DIFFRACTIONf_plane_restr0.003742
X-RAY DIFFRACTIONf_dihedral_angle_d13.2771649
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1206X-RAY DIFFRACTION8.694TORSIONAL
12D1206X-RAY DIFFRACTION8.694TORSIONAL
21B434X-RAY DIFFRACTION8.694TORSIONAL
22E434X-RAY DIFFRACTION8.694TORSIONAL
31C680X-RAY DIFFRACTION8.694TORSIONAL
32F680X-RAY DIFFRACTION8.694TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 9

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.5027-2.60290.39411390.30912420255998
2.6029-2.72140.34611400.269624432583100
2.7214-2.86480.29551370.246724592596100
2.8648-3.04430.30621290.25382465259499
3.0443-3.27930.29191140.24362489260399
3.2793-3.60920.24471360.211524752611100
3.6092-4.13120.19391540.18322467262199
4.1312-5.20390.19311240.159725562680100
5.2039-47.7180.24151370.18812628276599
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)
12.76741.7679-7.18472.6011-7.86713.5245-0.1291-0.2657-1.6375-0.7919-0.8509-2.12360.78140.13040.930.5178-0.13290.0340.65720.00070.5718-18.5207-23.2401-9.4032
22.2055-3.4806-0.10585.94893.18869.74270.28060.192-0.68470.0158-0.10710.45570.9406-0.9298-0.19820.2415-0.020.00960.39470.01880.5446-19.3166-25.8332-3.9125
32.54141.35120.33327.37-2.53896.59070.16030.0368-0.159-0.0177-0.09990.3035-0.1622-0.3501-0.05630.20160.02440.0250.3537-0.0590.3025-18.2198-18.7314-3.4546
45.72432.05580.27917.35821.29995.20851.6733-2.90480.29212.1959-1.48821.5121.9161-1.74910.01690.756-0.17820.04291.28090.25460.838-11.8041-26.736512.9617
53.5203-1.09971.82765.44541.93816.8485-0.1542-0.30150.16580.3240.4142-0.7392-0.57830.6309-0.27570.3347-0.03030.02790.43190.00460.383-3.2181-13.27158.3286
67.9435-2.2734-1.42734.8575-0.35034.0449-0.32710.61360.5919-0.8112-0.34-1.3032-2.37131.0701-0.9981.403-0.6553-0.00731.3895-0.08750.88475.39625.747310.9589
72.6965-1.1668-2.74690.54610.86026.14450.6861-0.3092-0.3943-0.36010.50790.16891.89980.038-1.24111.9027-0.6016-0.08241.6242-0.18811.05654.80868.590823.5847
82.12463.5857-2.22961.0788-0.52580.5480.78220.53080.9440.37810.0251-0.6764-0.58950.8067-0.32220.5016-0.05060.03890.6716-0.12860.5082-3.4418-0.68594.9192
99.18040.3457-0.25367.81841.1965.90610.1504-0.98530.52931.5228-0.2499-0.4425-1.04630.6006-0.12630.7826-0.0614-0.01140.6627-0.12670.4404-4.863-5.292617.9778
109.2698-2.10451.86472.16430.51042.05530.6815-0.74120.26940.5331-0.73020.312-1.9295-0.28120.0820.9719-0.20920.08440.9034-0.21760.5884-5.92421.585518.4712
118.0618-5.46431.45159.24791.01212.7948-0.21771.69431.3351-0.8982-0.45180.3996-1.5637-0.38430.5011.32860.1364-0.03450.73290.38820.875-11.820910.9606-23.3172
122.84450.7038-0.66915.3699-4.68014.05070.87180.4785-0.655-1.8578-1.74062.47192.4543-0.31660.7572.52940.53860.46880.82250.1691.8484-16.736423.3933-16.9762
136.1957-1.12133.40862.1068-8.03952.17910.1414-0.10770.7729-0.21190.17890.4118-2.1598-0.5793-0.40061.25330.08480.24560.5660.00710.8412-13.444211.1387-11.3807
146.5338-6.1828-3.89486.05222.98252.14220.53110.4032.4409-1.07061.0428-1.24710.6986-0.9505-0.99021.457-0.0750.27450.83610.42641.0889-4.380820.6942-13.5861
155.38081.0482-0.69998.29184.08842.337-0.38280.6840.7099-0.35340.57470.3041-0.1896-0.6302-0.49731.909-0.06230.28921.00820.43831.4626-8.535622.5996-22.4471
167.3745-3.17944.60027.6244-1.98372.05630.10360.19420.5521-0.24130.23120.1523-1.8226-0.5162-0.81880.8488-0.07540.0480.375-0.01250.5436-5.94188.1909-11.2675
177.77642.23183.24970.65210.15395.1187-1.1293-0.96921.04541.32390.46751.1776-1.6762-1.32820.27650.87270.33770.28340.8316-0.1280.943-28.84651.44796.2669
182.08575.18-4.98185.32682.78859.27890.43680.49161.3716-1.0689-1.04831.4004-2.0859-0.0162-0.17370.74940.34620.02910.55560.01641.1105-26.19944.2677-2.5588
192.36192.0235-1.23512.7001-2.84213.160.03490.04590.70280.06110.41731.8198-0.6134-0.7354-0.15220.55540.23420.05120.74910.09691.0507-31.5143-4.1894-4.1275
203.0958-1.4931-1.94077.20912.8316.81080.93340.0681.8050.42940.04290.7175-0.7328-0.7529-0.91930.59760.15880.09740.73280.04810.8114-31.0788-4.19191.0572
212.15343.4552-5.78252.53271.94543.91971.1665-3.1994-1.4380.6288-1.7732-1.742-0.23351.8560.29780.6148-0.14860.05221.2580.21170.7037.5559-0.6227-4.9595
229.6008-0.3048-0.05092.87830.86177.11320.2726-0.25120.3049-0.0469-0.2992-1.1763-0.91861.5862-0.03280.6131-0.18120.09910.78130.11460.59436.5692-0.0893-11.8322
238.03223.73482.64268.21084.34971.9886-1.1262.50960.4458-1.04020.00380.64451.19932.9235-0.41220.82780.14470.16261.250.06720.727711.594-9.0473-26.662
249.6712-5.01311.97427.84895.77152.0289-0.34461.1565-0.0357-0.0610.4632-1.88412.46911.56650.35751.09550.43840.22131.05780.04040.8385.2944-17.6928-21.0058
257.72830.70840.38676.131.84668.4097-0.07370.78320.1204-0.15160.3767-0.2438-0.42130.8069-0.16330.46130.08850.11680.62740.1280.3127-3.0963-6.8138-17.4739
269.40662.97890.5575.54381.55436.9939-0.11951.074-0.0713-1.67270.1147-0.06780.23941.4424-0.22780.90060.14710.13820.68290.08910.4177-1.4189-11.5163-26.7313
272.10112.75344.8065.83290.05761.614-0.56361.3318-0.7866-1.20920.47950.63171.188-0.906-0.17531.3544-0.2174-0.26970.8807-0.11350.7446-17.1776-21.8716-28.0148
287.96830.143.00754.87490.76596.63470.67670.83480.6249-0.3992-0.66170.25091.38960.3986-0.19261.62580.0006-0.5411.24380.07451.1999-24.6211-15.7542-39.8797
292.01823.663-5.64760.8745-1.31012.14760.47451.5538-0.8951-0.45810.1851.02430.5492-1.8659-0.87981.0818-0.221-0.2521.14890.10760.7419-22.855-13.7652-19.3535
306.40254.4061-6.17248.2936-2.34537.0242-0.62651.17940.4015-0.77510.1244-0.05720.3147-0.19280.40880.75030.0634-0.06960.59210.09540.335-10.3261-7.6383-26.1106
310.5673-0.26662.346.2688-2.25529.7194-1.10522.6613-1.9273-1.29940.5366-0.2232.55120.46870.84011.4427-0.0331-0.01961.4689-0.38730.5301-12.906-16.3022-37.4411
327.4424-4.5387.63917.7653-8.73892.4030.1870.39650.5145-0.1933-0.9186-0.3678-0.57360.09481.00061.08360.0064-0.14150.7224-0.14120.5942-17.8719-8.6143-33.4293
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid -1 through 12 )A-1 - 12
2X-RAY DIFFRACTION2chain 'A' and (resid 13 through 23 )A13 - 23
3X-RAY DIFFRACTION3chain 'A' and (resid 24 through 64 )A24 - 64
4X-RAY DIFFRACTION4chain 'A' and (resid 65 through 86 )A65 - 86
5X-RAY DIFFRACTION5chain 'A' and (resid 87 through 139 )A87 - 139
6X-RAY DIFFRACTION6chain 'A' and (resid 140 through 146 )A140 - 146
7X-RAY DIFFRACTION7chain 'A' and (resid 147 through 156 )A147 - 156
8X-RAY DIFFRACTION8chain 'B' and (resid 277 through 285 )B277 - 285
9X-RAY DIFFRACTION9chain 'B' and (resid 286 through 306 )B286 - 306
10X-RAY DIFFRACTION10chain 'B' and (resid 307 through 322 )B307 - 322
11X-RAY DIFFRACTION11chain 'F' and (resid 0 through 17 )F0 - 17
12X-RAY DIFFRACTION12chain 'F' and (resid 18 through 22 )F18 - 22
13X-RAY DIFFRACTION13chain 'F' and (resid 23 through 44 )F23 - 44
14X-RAY DIFFRACTION14chain 'F' and (resid 45 through 56 )F45 - 56
15X-RAY DIFFRACTION15chain 'F' and (resid 57 through 65 )F57 - 65
16X-RAY DIFFRACTION16chain 'F' and (resid 66 through 74 )F66 - 74
17X-RAY DIFFRACTION17chain 'C' and (resid -1 through 22 )C-1 - 22
18X-RAY DIFFRACTION18chain 'C' and (resid 23 through 34 )C23 - 34
19X-RAY DIFFRACTION19chain 'C' and (resid 35 through 56 )C35 - 56
20X-RAY DIFFRACTION20chain 'C' and (resid 57 through 74 )C57 - 74
21X-RAY DIFFRACTION21chain 'D' and (resid 1 through 12 )D1 - 12
22X-RAY DIFFRACTION22chain 'D' and (resid 13 through 64 )D13 - 64
23X-RAY DIFFRACTION23chain 'D' and (resid 65 through 86 )D65 - 86
24X-RAY DIFFRACTION24chain 'D' and (resid 87 through 96 )D87 - 96
25X-RAY DIFFRACTION25chain 'D' and (resid 97 through 112 )D97 - 112
26X-RAY DIFFRACTION26chain 'D' and (resid 113 through 127 )D113 - 127
27X-RAY DIFFRACTION27chain 'D' and (resid 128 through 146 )D128 - 146
28X-RAY DIFFRACTION28chain 'D' and (resid 147 through 160 )D147 - 160
29X-RAY DIFFRACTION29chain 'E' and (resid 275 through 279 )E275 - 279
30X-RAY DIFFRACTION30chain 'E' and (resid 280 through 295 )E280 - 295
31X-RAY DIFFRACTION31chain 'E' and (resid 296 through 306 )E296 - 306
32X-RAY DIFFRACTION32chain 'E' and (resid 307 through 322 )E307 - 322

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