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- PDB-3c0r: Structure of Ovarian Tumor (OTU) domain in complex with Ubiquitin -

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Basic information

Entry
Database: PDB / ID: 3c0r
TitleStructure of Ovarian Tumor (OTU) domain in complex with Ubiquitin
Components
  • Ubiquitin
  • Ubiquitin thioesterase OTU1
KeywordsCELL CYCLE / HYDROLASE / ubiquitin hydrolase / deubiquitinase
Function / homology
Function and homology information


Ovarian tumor domain proteases / : / : / protein modification process => GO:0036211 / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane ...Ovarian tumor domain proteases / : / : / protein modification process => GO:0036211 / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / Viral mRNA Translation / protein deubiquitination / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / endoplasmic reticulum unfolded protein response / ERAD pathway / Maturation of protein E / Maturation of protein E / cytosolic ribosome / 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 / Regulation of innate immune responses to cytosolic DNA / TRAF6-mediated induction of TAK1 complex within TLR4 complex / Regulation of pyruvate metabolism / NF-kB is activated and signals survival / Downregulation of ERBB2:ERBB3 signaling / Pexophagy / NRIF signals cell death from the nucleus / Regulation of PTEN localization / VLDLR internalisation and degradation / Activated NOTCH1 Transmits Signal to the Nucleus / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Regulation of BACH1 activity / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Translesion synthesis by REV1 / Translesion synthesis by POLK / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / InlB-mediated entry of Listeria monocytogenes into host cell / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / Translesion synthesis by POLI / Regulation of activated PAK-2p34 by proteasome mediated degradation / IKK complex recruitment mediated by RIP1 / Gap-filling DNA repair synthesis and ligation in GG-NER / PINK1-PRKN Mediated Mitophagy / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / TNFR1-induced NF-kappa-B signaling pathway / Autodegradation of Cdh1 by Cdh1:APC/C / APC/C:Cdc20 mediated degradation of Securin / TCF dependent signaling in response to WNT / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Regulation of NF-kappa B signaling / Asymmetric localization of PCP proteins / Ubiquitin-dependent degradation of Cyclin D / SCF-beta-TrCP mediated degradation of Emi1 / NIK-->noncanonical NF-kB signaling / activated TAK1 mediates p38 MAPK activation / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / AUF1 (hnRNP D0) binds and destabilizes mRNA / Regulation of signaling by CBL / NOTCH3 Activation and Transmission of Signal to the Nucleus / Vpu mediated degradation of CD4 / Assembly of the pre-replicative complex / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Degradation of DVL / Deactivation of the beta-catenin transactivating complex / Negative regulation of FGFR3 signaling / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Dectin-1 mediated noncanonical NF-kB signaling
Similarity search - Function
Ubiquitin thioesterase OTU1, C-terminal C2H2-type zinc finger / : / OTU1, UBXL domain / Cathepsin B; Chain A - #80 / OTU-like cysteine protease / OTU domain / OTU domain profile. / Cathepsin B; Chain A / Ribosomal L40e family / Ribosomal_L40e ...Ubiquitin thioesterase OTU1, C-terminal C2H2-type zinc finger / : / OTU1, UBXL domain / Cathepsin B; Chain A - #80 / OTU-like cysteine protease / OTU domain / OTU domain profile. / Cathepsin B; Chain A / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Zinc finger C2H2 type domain signature. / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Zinc finger C2H2-type / Papain-like cysteine peptidase superfamily / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
3-AMINOPROPANE / Polyubiquitin-C / Ubiquitin thioesterase OTU1 / Ubiquitin-60S ribosomal protein L40
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2.315 Å
AuthorsMessick, T.E. / Marmorstein, R.
CitationJournal: J.Biol.Chem. / Year: 2008
Title: Structural basis for ubiquitin recognition by the Otu1 ovarian tumor domain protein
Authors: Messick, T.E. / Russell, N.S. / Iwata, A.J. / Sarachan, K.L. / Shiekhattar, R. / Shanks, J.R. / Reyes-Turcu, F.E. / Wilkinson, K.D. / Marmorstein, R.
History
DepositionJan 21, 2008Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 19, 2008Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 16, 2011Group: Atomic model
Revision 1.3Oct 25, 2017Group: Refinement description / Category: software
Revision 1.4Mar 26, 2025Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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_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_conn.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin thioesterase OTU1
B: Ubiquitin
C: Ubiquitin thioesterase OTU1
D: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,4596
Polymers65,3404
Non-polymers1182
Water5,873326
1
C: Ubiquitin thioesterase OTU1
D: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,7293
Polymers32,6702
Non-polymers591
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2430 Å2
ΔGint-14 kcal/mol
Surface area11660 Å2
MethodPISA
2
A: Ubiquitin thioesterase OTU1
B: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,7293
Polymers32,6702
Non-polymers591
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2390 Å2
ΔGint-14 kcal/mol
Surface area11550 Å2
MethodPISA
Unit cell
Length a, b, c (Å)107.311, 107.311, 100.239
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number172
Space group name H-MP64
Components on special symmetry positions
IDModelComponents
11A-313-

HOH

21B-100-

HOH

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Components

#1: Protein Ubiquitin thioesterase OTU1 / E.C.3.4.19.12 / Otu1 / OTU domain-containing protein 1


Mass: 24150.406 Da / Num. of mol.: 2 / Fragment: Otu domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: Otu1 / Plasmid: pTYB2 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P43558, ubiquitinyl hydrolase 1
#2: Protein Ubiquitin / Ubiquitin B


Mass: 8519.778 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Description: propylamine added by intein-mediated ligation / Gene: ubiquitin B / Plasmid: pTYB2 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P62988, UniProt: P0CG48*PLUS
#3: Chemical ChemComp-3CN / 3-AMINOPROPANE


Mass: 59.110 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H9N
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 326 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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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: 2.55 Å3/Da / Density % sol: 51.76 %
Crystal growTemperature: 277 K / Method: hanging drop / pH: 6.5
Details: MES, ammonium acetate, PEG3350, pH 6.5, hanging drop, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.9793, 0.9795, 0.9566
DetectorType: MARRESEARCH / Detector: CCD / Date: Mar 25, 2005
RadiationProtocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
10.97931
20.97951
30.95661
ReflectionRedundancy: 18.1 % / Av σ(I) over netI: 15.8 / Number: 517121 / Rmerge(I) obs: 0.091 / Χ2: 1.07 / D res high: 2.31 Å / D res low: 50 Å / Num. obs: 28554 / % possible obs: 99.8
Diffraction reflection shell
Highest resolution (Å)Lowest resolution (Å)% possible obs (%)IDRmerge(I) obsChi squaredRedundancy
4.985099.810.0711.03217.9
3.954.9810010.071.00918.3
3.453.9510010.0711.08418.5
3.133.4510010.0871.08318.6
2.913.1310010.1131.03818.6
2.742.9110010.1611.08718.6
2.62.7410010.2021.08418.6
2.492.699.910.2721.08918.4
2.392.4910010.3531.07517.7
2.312.3998.210.4081.0715.6
ReflectionResolution: 2.315→36.626 Å / Num. obs: 28554 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 18.1 % / Biso Wilson estimate: 50.66 Å2 / Rsym value: 0.08 / Net I/σ(I): 30.2
Reflection shellResolution: 2.315→2.39 Å / Rmerge(I) obs: 0.357 / Mean I/σ(I) obs: 3.29 / Num. unique all: 2785 / Rsym value: 0.529

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Phasing

PhasingMethod: MAD
Phasing MAD set
IDHighest resolution (Å)Lowest resolution (Å)Power acentricPower centricReflection acentricReflection centric
ISO_12.3136.630027555972
ISO_22.3136.630.0590.05127159971
ANO_12.3136.632.220274720
ANO_22.3136.631.5470268490
Phasing MAD set shell
IDResolution (Å)Power acentricPower centricReflection acentricReflection centric
ISO_19.98-36.630031849
ISO_17.19-9.980056847
ISO_15.91-7.190071553
ISO_15.14-5.910087546
ISO_14.6-5.140098449
ISO_14.21-4.600107549
ISO_13.9-4.2100119248
ISO_13.65-3.900126447
ISO_13.44-3.6500133850
ISO_13.27-3.4400143545
ISO_13.12-3.2700149554
ISO_12.98-3.1200157244
ISO_12.87-2.9800163750
ISO_12.76-2.8700170848
ISO_12.67-2.7600175252
ISO_12.59-2.6700184745
ISO_12.51-2.5900188449
ISO_12.44-2.5100194247
ISO_12.37-2.4400197952
ISO_12.31-2.3700197548
ANO_19.98-36.633.49703180
ANO_17.19-9.984.13205680
ANO_15.91-7.194.74407150
ANO_15.14-5.914.25108740
ANO_14.6-5.143.30409840
ANO_14.21-4.62.808010750
ANO_13.9-4.212.881011920
ANO_13.65-3.92.861012640
ANO_13.44-3.652.682013380
ANO_13.27-3.442.606014350
ANO_13.12-3.272.542014950
ANO_12.98-3.122.347015720
ANO_12.87-2.982.085016370
ANO_12.76-2.871.816017080
ANO_12.67-2.761.729017520
ANO_12.59-2.671.497018470
ANO_12.51-2.591.247018840
ANO_12.44-2.511.087019390
ANO_12.37-2.440.897019630
ANO_12.31-2.370.834019120
ISO_29.98-36.630.1070.08131349
ISO_27.19-9.980.0950.06156347
ISO_25.91-7.190.10.05771153
ISO_25.14-5.910.0890.05587146
ISO_24.6-5.140.0720.05198149
ISO_24.21-4.60.0570.048107349
ISO_23.9-4.210.0570.044118948
ISO_23.65-3.90.0550.052126147
ISO_23.44-3.650.0510.044133750
ISO_23.27-3.440.0540.043143445
ISO_23.12-3.270.0560.044149554
ISO_22.98-3.120.0570.037157144
ISO_22.87-2.980.0540.049163750
ISO_22.76-2.870.0530.035170648
ISO_22.67-2.760.0520.055175252
ISO_22.59-2.670.050.043184045
ISO_22.51-2.590.0450.036186549
ISO_22.44-2.510.0410.031189747
ISO_22.37-2.440.0370.024187052
ISO_22.31-2.370.0310.029179347
ANO_29.98-36.633.3503130
ANO_27.19-9.984.23605630
ANO_25.91-7.194.68907110
ANO_25.14-5.913.84208710
ANO_24.6-5.142.98809810
ANO_24.21-4.62.464010710
ANO_23.9-4.212.306011870
ANO_23.65-3.92.096012590
ANO_23.44-3.652.002013350
ANO_23.27-3.441.823014320
ANO_23.12-3.271.763014940
ANO_22.98-3.121.491015710
ANO_22.87-2.981.266016360
ANO_22.76-2.871.14017050
ANO_22.67-2.761017500
ANO_22.59-2.670.878018330
ANO_22.51-2.590.781018370
ANO_22.44-2.510.681018520
ANO_22.37-2.440.63018090
ANO_22.31-2.370.565016390

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
SHARPphasing
SOLOMONphasing
PHENIXrefinement
PDB_EXTRACT3.004data extraction
HKL-2000data collection
RefinementMethod to determine structure: MAD / Resolution: 2.315→36.626 Å / Cross valid method: THROUGHOUT / Stereochemistry target values: MLHL
RfactorNum. reflection% reflectionSelection details
Rfree0.243 1438 5.04 %random
Rwork0.196 ---
obs0.198 28527 99.64 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 16.46 Å2 / Biso mean: 54.26 Å2 / Biso min: 174.56 Å2
Baniso -1Baniso -2Baniso -3
1-0.065 Å20 Å20 Å2
2--0.065 Å2-0 Å2
3----0.131 Å2
Refinement stepCycle: LAST / Resolution: 2.315→36.626 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3962 0 8 326 4296
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.014036
X-RAY DIFFRACTIONf_angle_d1.235444
X-RAY DIFFRACTIONf_chiral_restr0.079628
X-RAY DIFFRACTIONf_plane_restr0.004700
X-RAY DIFFRACTIONf_dihedral_angle_d18.3341490
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 10

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.315-2.3970.3251350.2452613274897
2.397-2.4930.2691700.24426942864100
2.493-2.6070.2681480.2326732821100
2.607-2.7440.291260.22127422868100
2.744-2.9160.2831280.22927252853100
2.916-3.1410.2821500.20826972847100
3.141-3.4570.221420.19427352877100
3.457-3.9570.2181270.1727322859100
3.957-4.9830.2051710.14826932864100
4.983-36.6310.2061410.1727852926100
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)
1-0.0298-0.070.01040.08520.05390.14910.66850.3437-0.07280.04520.3191-1.53090.01220.95910.00030.26570.10670.02450.3722-0.18050.728840.415136.380241.0376
20.75610.81870.13490.8867-0.66121.6681-0.3387-0.0072-0.34920.04360.1168-0.06460.22740.2504-0.00110.2492-0.0018-0.05390.14910.03460.222125.332638.359442.695
30.06430.19750.02790.3957-0.62240.9850.22910.41230.865-0.32740.69660.9135-0.4895-0.58810.02980.30510.0294-0.09790.26920.00360.465310.473945.168642.6828
45.95854.8351.07399.98993.23871.35220.28172.1628-0.5233-2.24080.6322-1.2987-0.28180.46561.4255-0.16620.1446-0.44050.31110.23970.6330.060738.148648.8024
50.11330.07350.09360.1251-0.09610.2678-0.1972-0.02570.10470.04280.91441.7055-0.0967-0.7596-0.00130.19950.08830.09060.94730.24810.9090.148835.374158.5727
6-0.56632.52175.18439.24654.81915.1741-0.26790.40221.954-1.4782-0.3814-1.1919-1.24730.58730.43070.20530.3645-0.16590.5437-0.13040.7247.444346.331255.0128
70.50220.85750.30457.86470.63250.6783-0.5335-0.83790.1051-1.14410.2522.5681-0.4564-0.9397-0.0360.03830.13890.11330.38720.01180.210811.136638.454653.8085
80.8036-0.4522-0.53461.36040.07390.4850.0016-0.4902-0.1534-0.0550.18120.29540.1901-0.31030.00010.1533-0.0315-0.07620.20640.11760.265218.344630.653746.8019
91.09735.08311.53722.02960.6101-0.3675-0.23590.7507-0.4707-1.18320.2724-1.12870.31540.83770.03120.30790.0343-0.1250.32520.11130.227424.814433.924434.4479
10-0.04690.04090.0510.09990.11540.1537-0.533-0.4485-1.66040.0676-0.0895-0.38320.34250.4246-0.00110.48890.0594-0.05030.2664-0.01930.346524.056422.204135.4324
11-0.1357-0.1252-0.45920.2486-0.42850.12630.1608-0.29590.23110.1454-0.39810.00060.3331-0.0519-0.00230.23260.0045-0.04560.18080.06490.238332.566630.86649.149
120.02670.20290.1062-0.0048-0.0029-0.1941-0.35110.02790.12070.7617-0.16280.65460.4581-0.18070.00360.65630.05680.16110.618-0.1480.41225.276635.512462.1601
13-0.12120.00730.00160.0851-0.2495-0.0318-0.0325-0.0428-1.4024-0.3518-0.54330.45260.9019-0.3301-0.00490.7846-0.4095-0.11810.85890.70521.23426.913711.099760.39
14-0.0094-0.0148-0.0147-0.07230.1347-0.01580.57080.6227-0.696-1.11590.42170.37450.1477-1.01290.00420.4626-0.198-0.2350.57830.1650.66246.794121.513852.0347
150.02460.0372-0.01730.0485-0.02480.1916-0.43320.6627-0.9470.47450.02060.27960.35490.3836-0.00190.6714-0.1421-0.31960.68450.40661.411211.26210.28561.2599
160.0818-0.0270.07230.0793-0.0610.0203-0.2379-0.69050.21120.41220.411-0.33440.6492-0.56470.0020.5435-0.2039-0.10251.19290.53220.577713.81815.190870.4803
170.05690.00150.01780.0605-0.02140.0679-0.2861-0.4713-1.00190.0489-0.77840.27670.07140.1240.0010.2978-0.10360.03480.69660.37950.573516.43117.274663.6346
18-0.0294-0.0148-0.0596-0.07240.07790.03450.50450.1096-0.9039-0.3806-0.14720.33650.72450.5025-0.00050.34270.11410.07630.47170.20360.735819.315318.975156.5483
19-0.02170.01330.03980.0294-0.03390.08760.0969-0.5935-0.1132-0.29910.3227-0.0003-0.6210.01390.00040.18950.02660.06630.73070.29270.403715.133626.579762.1558
20-0.062-0.0651-0.08920.15750.11930.1301-1.0294-0.21750.09680.1195-0.33151.2196-0.0037-0.5551-0.0010.3320.10280.10181.04260.45360.68064.761224.42668.1383
210.01070.0593-0.07140.0350.00450.028-0.5341-0.6314-0.18421.02750.13710.4264-0.2745-0.3013-0.00210.5886-0.06580.06551.72630.81960.988910.53318.472873.2792
22-0.0050.07040.0726-0.02450.01810.00890.2655-0.3492-0.40310.19040.37840.93830.4098-0.89080.00631.04510.23210.3432.42871.60081.65293.89813.268469.1931
230.08890.12690.08321.23521.18462.41160.15670.6233-0.9711-0.647-0.25350.0426-1.0063-0.6918-0.00270.226-0.3292-0.12780.78380.42151.15043.058416.460160.7555
240.1075-0.2396-0.163-0.05330.00590.08180.2734-0.98510.09350.35990.03050.3539-0.3914-0.5009-0.00050.18380.0592-0.02380.56630.09360.305813.835632.242257.984
250.1032-0.3476-0.16460.3489-0.12060.58330.34150.444-0.10540.0165-0.42991.2062-0.1097-1.0338-0.0060.35310.0316-0.06640.289-0.00380.41740.487652.911825.3598
260.29780.23730.04070.2145-0.13460.0409-0.2565-0.06160.229-0.07120.2230.56420.2532-0.98480.00550.22520.0310.02470.39010.00240.1279-2.282245.790731.9137
270.03860.3820.5540.26970.2152-0.25320.04250.4532-0.30680.2808-0.15670.0822-0.05660.245-0.00020.21160.0475-0.03960.33890.02940.180318.006543.239821.0894
280.3355-1.5579-0.27482.02271.25880.9883-0.230.2642-0.45841.05420.4775-0.12361.129-0.0377-0.00510.25040.064-0.10610.54140.01460.400526.124937.177623.1365
291.16721.0152-0.29721.15160.56910.0851.57160.4362-1.20150.6468-0.9849-0.55130.72361.01350.01490.12070.6149-0.18050.5431-0.35070.440125.519823.476410.6843
300.3363-0.0197-0.16411.2743-5.1123.09280.20210.10660.85760.285-0.5184-0.937-0.67661.11760.00820.23780.251-0.1040.8548-0.09170.398829.186835.483111.4413
312.28960.18980.33861.2282-0.16621.21630.37890.3833-0.13690.0883-0.12680.07890.27010.1024-00.21150.0556-0.12380.1879-0.06840.17811.510134.44718.8468
321.24966.1087-1.7372.0396-4.83293.36940.3374-0.03090.68871.5273-0.13342.5117-0.6154-1.46450.5150.3145-0.0639-0.1610.2479-0.07770.19087.526441.211632.4897
33-0.06270.0387-0.02640.1273-0.01090.0540.3769-0.1994-0.37730.5444-0.59461.1211-0.493-0.662-0.00080.4057-0.0824-0.12530.39080.0740.45110.006632.413231.7674
340.1242-0.10270.06870.12660.10910.05520.2704-0.05160.07390.0876-0.26960.1028-0.21190.18690.0010.2119-0.0376-0.05930.2472-0.02180.2047-1.070842.444421.0887
350.06760.0677-0.0695-0.01230.05560.0380.03890.09420.8716-0.6985-0.791-0.3655-0.7223-0.34190.00050.299-0.0029-0.07080.26590.11670.39861.428449.862611.2575
36-0.0401-0.0149-0.02660.00080.09190.03790.06270.19020.4663-0.40950.1438-0.1120.2115-0.0709-0.00190.44330.0457-0.12440.8225-0.03070.73488.534942.594.7683
370.08970.00920.01610.0199-0.01810.0821-0.12320.0431-0.42371.08710.1850.34880.8859-0.7087-0.00440.72150.09-0.31260.482-0.44421.21372.162412.35767.2764
380.04190.0493-0.0056-0.02870.0391-0.09250.9168-0.5734-0.42940.4427-0.43120.41070.00460.1663-00.73150.031-0.23760.4516-0.27050.625811.411520.400215.5093
390.07440.05160.02740.082-0.00710.15470.33660.2173-1.3985-0.2186-0.68570.85010.0979-0.88130.00250.75550.2232-0.55550.7605-0.40091.1093-0.383415.04555.3228
40-0.0232-0.07430.0542-0.0891-0.0256-0.01430.25360.393-0.01120.13340.1660.5872-0.05470.07880.00230.520.3658-0.29910.8028-0.47950.53181.013922.1572-2.0387
41-0.15820.14540.03791.79491.04550.28750.67190.0361-0.57040.105-0.23061.29811.3979-0.0916-0.00060.49270.2286-0.39580.4558-0.29940.62540.696724.59315.3644
42-0.1059-0.0143-0.02990.0085-0.04330.06430.13510.6370.0055-1.02470.40780.85460.2715-0.12040.00380.32250.113-0.14550.4491-0.20320.51620.566426.766911.0938
430.0760.084-0.09790.1158-0.08560.19980.61191.361-0.7429-0.3331-0.33040.5485-0.24020.43910.00090.55770.421-0.30630.5843-0.30660.46769.654325.52974.2466
440.07580.08790.10150.0349-0.09630.131-0.18140.58230.2146-0.7784-0.0608-0.31170.3740.80820.00090.63830.4165-0.34711.0032-0.50260.608311.968421.1339-2.4633
450.0146-0.18140.0574-0.00620.0813-0.0096-0.19510.95550.0978-0.9394-0.351-0.8733-0.33820.504-0.00120.9830.3268-0.45641.1584-0.62440.77656.540916.4691-5.8841
46-0.0074-0.07980.08140.06770.0496-0.0481-0.3278-0.4128-1.05160.85790.23630.39840.6488-0.76290.00061.2410.5918-0.87671.1687-0.77871.59844.76038.21541.6609
470.67270.4137-1.3602-0.0006-1.40570.92250.5911-0.0586-0.67610.7081-0.23030.1490.19970.74450.01230.56820.3296-0.3630.4431-0.28220.699910.39317.65797.3728
480.0306-1.1362-0.80197.9245.07643.24260.47160.7025-0.3915-0.75960.3029-0.3896-0.36050.37420.21190.27180.2375-0.19750.6502-0.1360.091914.626234.33239.0266
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resseq 92:97A92 - 97
2X-RAY DIFFRACTION2chain A and resseq 98:129A98 - 129
3X-RAY DIFFRACTION3chain A and resseq 130:140A130 - 140
4X-RAY DIFFRACTION4chain A and resseq 141:148A141 - 148
5X-RAY DIFFRACTION5chain A and resseq 149:167A149 - 167
6X-RAY DIFFRACTION6chain A and resseq 168:172A168 - 172
7X-RAY DIFFRACTION7chain A and resseq 173:183A173 - 183
8X-RAY DIFFRACTION8chain A and resseq 184:226A184 - 226
9X-RAY DIFFRACTION9chain A and resseq 227:236A227 - 236
10X-RAY DIFFRACTION10chain A and resseq 237:244A237 - 244
11X-RAY DIFFRACTION11chain A and resseq 245:261A245 - 261
12X-RAY DIFFRACTION12chain A and resseq 262:266A262 - 266
13X-RAY DIFFRACTION13chain B and resseq 1:5B1 - 5
14X-RAY DIFFRACTION14chain B and resseq 6:12B6 - 12
15X-RAY DIFFRACTION15chain B and resseq 13:18B13 - 18
16X-RAY DIFFRACTION16chain B and resseq 19:24B19 - 24
17X-RAY DIFFRACTION17chain B and resseq 25:30B25 - 30
18X-RAY DIFFRACTION18chain B and resseq 31:37B31 - 37
19X-RAY DIFFRACTION19chain B and resseq 38:43B38 - 43
20X-RAY DIFFRACTION20chain B and resseq 44:51B44 - 51
21X-RAY DIFFRACTION21chain B and resseq 52:57B52 - 57
22X-RAY DIFFRACTION22chain B and resseq 58:63B58 - 63
23X-RAY DIFFRACTION23chain B and resseq 64:68B64 - 68
24X-RAY DIFFRACTION24chain B and resseq 69:76B69 - 76
25X-RAY DIFFRACTION25chain C and resseq 92:99C92 - 99
26X-RAY DIFFRACTION26chain C and resseq 100:109C100 - 109
27X-RAY DIFFRACTION27chain C and resseq 110:130C110 - 130
28X-RAY DIFFRACTION28chain C and resseq 131:141C131 - 141
29X-RAY DIFFRACTION29chain C and resseq 142:166C142 - 166
30X-RAY DIFFRACTION30chain C and resseq 167:172C167 - 172
31X-RAY DIFFRACTION31chain C and resseq 173:227C173 - 227
32X-RAY DIFFRACTION32chain C and resseq 228:236C228 - 236
33X-RAY DIFFRACTION33chain C and resseq 237:243C237 - 243
34X-RAY DIFFRACTION34chain C and resseq 244:256C244 - 256
35X-RAY DIFFRACTION35chain C and resseq 257:261C257 - 261
36X-RAY DIFFRACTION36chain C and resseq 262:266C262 - 266
37X-RAY DIFFRACTION37chain D and resseq 1:5D1 - 5
38X-RAY DIFFRACTION38chain D and resseq 6:11D6 - 11
39X-RAY DIFFRACTION39chain D and resseq 12:20D12 - 20
40X-RAY DIFFRACTION40chain D and resseq 21:25D21 - 25
41X-RAY DIFFRACTION41chain D and resseq 26:31D26 - 31
42X-RAY DIFFRACTION42chain D and resseq 32:37D32 - 37
43X-RAY DIFFRACTION43chain D and resseq 38:45D38 - 45
44X-RAY DIFFRACTION44chain D and resseq 46:53D46 - 53
45X-RAY DIFFRACTION45chain D and resseq 54:59D54 - 59
46X-RAY DIFFRACTION46chain D and resseq 60:64D60 - 64
47X-RAY DIFFRACTION47chain D and resseq 65:70D65 - 70
48X-RAY DIFFRACTION48chain D and resseq 71:76D71 - 76

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