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- PDB-4fjv: Crystal Structure of Human Otubain2 and Ubiquitin Complex -

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Basic information

Entry
Database: PDB / ID: 4fjv
TitleCrystal Structure of Human Otubain2 and Ubiquitin Complex
Components
  • Polyubiquitin-C
  • Ubiquitin thioesterase OTUB2
KeywordsHYDROLASE / Ubiquitin / otubain / NEDD8 / cleavage specificity / deubiquitylation / cysteine protease
Function / homology
Function and homology information


negative regulation of double-strand break repair / protein K11-linked deubiquitination / protein K48-linked deubiquitination / protein K63-linked deubiquitination / protein deubiquitination / Maturation of protein E / Maturation of protein E / ER Quality Control Compartment (ERQC) / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants ...negative regulation of double-strand break repair / protein K11-linked deubiquitination / protein K48-linked deubiquitination / protein K63-linked deubiquitination / protein deubiquitination / 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 / Constitutive Signaling by NOTCH1 HD Domain Mutants / Endosomal Sorting Complex Required For Transport (ESCRT) / NOTCH2 Activation and Transmission of Signal to the Nucleus / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / Regulation of FZD by ubiquitination / TICAM1,TRAF6-dependent induction of TAK1 complex / TICAM1-dependent activation of IRF3/IRF7 / APC/C:Cdc20 mediated degradation of Cyclin B / Downregulation of ERBB4 signaling / p75NTR recruits signalling complexes / TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling / APC-Cdc20 mediated degradation of Nek2A / PINK1-PRKN Mediated Mitophagy / TRAF6-mediated induction of TAK1 complex within TLR4 complex / InlA-mediated entry of Listeria monocytogenes into host cells / Pexophagy / Regulation of innate immune responses to cytosolic DNA / VLDLR internalisation and degradation / Downregulation of ERBB2:ERBB3 signaling / NRIF signals cell death from the nucleus / Activated NOTCH1 Transmits Signal to the Nucleus / Translesion synthesis by REV1 / NF-kB is activated and signals survival / Regulation of PTEN localization / Translesion synthesis by POLK / Regulation of BACH1 activity / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Translesion synthesis by POLI / Gap-filling DNA repair synthesis and ligation in GG-NER / MAP3K8 (TPL2)-dependent MAPK1/3 activation / TICAM1, RIP1-mediated IKK complex recruitment / Downregulation of TGF-beta receptor signaling / Josephin domain DUBs / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / Regulation of activated PAK-2p34 by proteasome mediated degradation / InlB-mediated entry of Listeria monocytogenes into host cell / IKK complex recruitment mediated by RIP1 / JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1 / TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition) / N-glycan trimming in the ER and Calnexin/Calreticulin cycle / Autodegradation of Cdh1 by Cdh1:APC/C / TNFR1-induced NF-kappa-B signaling pathway / ubiquitin binding / APC/C:Cdc20 mediated degradation of Securin / Asymmetric localization of PCP proteins / TCF dependent signaling in response to WNT / SCF-beta-TrCP mediated degradation of Emi1 / Regulation of NF-kappa B signaling / NIK-->noncanonical NF-kB signaling / Ubiquitin-dependent degradation of Cyclin D / AUF1 (hnRNP D0) binds and destabilizes mRNA / Negative regulators of DDX58/IFIH1 signaling / TNFR2 non-canonical NF-kB pathway / NOTCH3 Activation and Transmission of Signal to the Nucleus / activated TAK1 mediates p38 MAPK activation / Assembly of the pre-replicative complex / Vpu mediated degradation of CD4 / Deactivation of the beta-catenin transactivating complex / Degradation of DVL / Ubiquitin Mediated Degradation of Phosphorylated Cdc25A / Recognition of DNA damage by PCNA-containing replication complex / Regulation of signaling by CBL / Dectin-1 mediated noncanonical NF-kB signaling / Hh mutants are degraded by ERAD / Cdc20:Phospho-APC/C mediated degradation of Cyclin A / Fanconi Anemia Pathway / Negative regulation of FGFR3 signaling / Termination of translesion DNA synthesis / Peroxisomal protein import / Degradation of AXIN / Downregulation of SMAD2/3:SMAD4 transcriptional activity / Regulation of TNFR1 signaling / Defective CFTR causes cystic fibrosis / Degradation of GLI1 by the proteasome / Activation of NF-kappaB in B cells / Hedgehog ligand biogenesis / Negative regulation of FGFR2 signaling / Negative regulation of FGFR4 signaling / Stabilization of p53 / EGFR downregulation / Negative regulation of FGFR1 signaling
Similarity search - Function
Ubiquitin thioesterase Otubain / Peptidase C65 Otubain, subdomain 2 / Peptidase C65 Otubain, subdomain 1 / Peptidase C65, otubain / Peptidase C65, otubain, subdomain 2 / Peptidase C65, otubain, subdomain 1 / Peptidase C65 Otubain / 3 helical TM bundles of succinate and fumarate reductases / OTU domain / OTU domain profile. ...Ubiquitin thioesterase Otubain / Peptidase C65 Otubain, subdomain 2 / Peptidase C65 Otubain, subdomain 1 / Peptidase C65, otubain / Peptidase C65, otubain, subdomain 2 / Peptidase C65, otubain, subdomain 1 / Peptidase C65 Otubain / 3 helical TM bundles of succinate and fumarate reductases / OTU domain / OTU domain profile. / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Papain-like cysteine peptidase superfamily / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin domain signature. / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Ubiquitin-like domain superfamily / Phosphorylase Kinase; domain 1 / Roll / Up-down Bundle / 2-Layer Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
ETHANAMINE / Polyubiquitin-C / Ubiquitin thioesterase OTUB2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.047 Å
AuthorsAltun, M. / Walter, T.S. / Kramer, H.B. / Iphofer, A. / David, Y. / Komsany, A. / Ternette, N. / Nicholson, B. / Navon, A. / Stuart, D.I. ...Altun, M. / Walter, T.S. / Kramer, H.B. / Iphofer, A. / David, Y. / Komsany, A. / Ternette, N. / Nicholson, B. / Navon, A. / Stuart, D.I. / Ren, J. / Kessler, B.M.
CitationJournal: Plos One / Year: 2015
Title: The human otubain2-ubiquitin structure provides insights into the cleavage specificity of poly-ubiquitin-linkages.
Authors: Altun, M. / Walter, T.S. / Kramer, H.B. / Herr, P. / Iphofer, A. / Bostrom, J. / David, Y. / Komsany, A. / Ternette, N. / Navon, A. / Stuart, D.I. / Ren, J. / Kessler, B.M.
History
DepositionJun 12, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 12, 2013Provider: repository / Type: Initial release
Revision 1.1Feb 25, 2015Group: Database references
Revision 1.2Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_conn / struct_ref_seq_dif / 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_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_ref_seq_dif.details / _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 OTUB2
B: Polyubiquitin-C
C: Ubiquitin thioesterase OTUB2
D: Polyubiquitin-C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,30712
Polymers74,6654
Non-polymers6438
Water10,088560
1
A: Ubiquitin thioesterase OTUB2
B: Polyubiquitin-C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,6546
Polymers37,3322
Non-polymers3214
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2810 Å2
ΔGint-11 kcal/mol
Surface area15140 Å2
MethodPISA
2
C: Ubiquitin thioesterase OTUB2
D: Polyubiquitin-C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)37,6546
Polymers37,3322
Non-polymers3214
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3010 Å2
ΔGint-9 kcal/mol
Surface area15360 Å2
MethodPISA
3
A: Ubiquitin thioesterase OTUB2
B: Polyubiquitin-C
hetero molecules

C: Ubiquitin thioesterase OTUB2
D: Polyubiquitin-C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)75,30712
Polymers74,6654
Non-polymers6438
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_545-x,y-1/2,-z+1/21
Buried area7710 Å2
ΔGint-21 kcal/mol
Surface area28620 Å2
MethodPISA
Unit cell
Length a, b, c (Å)54.063, 76.825, 198.847
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111chain 'A' and (resseq 4:231 ) and backbone
211chain 'C' and (resseq 4:231 ) and backbone
112chain 'B' and (resseq -5:75 ) and backbone
212chain 'D' and (resseq -5:75 ) and backbone

NCS ensembles :
ID
1
2

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Components

#1: Protein Ubiquitin thioesterase OTUB2 / Deubiquitinating enzyme OTUB2 / OTU domain-containing ubiquitin aldehyde-binding protein 2 / ...Deubiquitinating enzyme OTUB2 / OTU domain-containing ubiquitin aldehyde-binding protein 2 / Otubain-2 / Ubiquitin-specific-processing protease OTUB2


Mass: 27533.207 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: OTUB2, C14orf137, OTB2, OTU2 / Plasmid: pET28a-LIC / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q96DC9, ubiquitinyl hydrolase 1
#2: Protein Polyubiquitin-C / Ubiquitin


Mass: 9799.111 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBC / Production host: Escherichia coli (E. coli) / References: UniProt: P0CG48
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-NEH / ETHANAMINE / Ethylamine


Mass: 45.084 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C2H7N
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 560 / 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: 2

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Sample preparation

CrystalDensity Matthews: 2.77 Å3/Da / Density % sol: 55.52 %
Crystal growTemperature: 279 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 15 % (w/v) Polyethylene Glycol 3350, 0.1 M Magnesium Formate , pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 279K

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Data collection

Diffraction
IDMean temperature (K)Crystal-ID
11001
21001
Diffraction source
SourceSiteBeamlineIDWavelength (Å)
SYNCHROTRONDiamond I04-110.9173
SYNCHROTRONDiamond I04-120.9173
Detector
TypeIDDetectorDate
DECTRIS PILATUS 2M1PIXELMay 12, 2011
DECTRIS PILATUS 2M2PIXELMay 12, 2011
Radiation
IDProtocolMonochromatic (M) / Laue (L)Scattering typeWavelength-ID
1SINGLE WAVELENGTHMx-ray1
2SINGLE WAVELENGTHMx-ray1
Radiation wavelengthWavelength: 0.9173 Å / Relative weight: 1
ReflectionResolution: 2.047→50 Å / Num. obs: 52092 / % possible obs: 99.1 % / Observed criterion σ(I): -1 / Redundancy: 9 % / Rmerge(I) obs: 0.168 / Net I/σ(I): 11
Reflection shellResolution: 2.05→2.12 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.627 / Mean I/σ(I) obs: 2.5 / Num. unique all: 4955 / % possible all: 96.1

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Processing

Software
NameVersionClassification
MOLREPphasing
PHENIX(phenix.refine: 1.7.3_928)refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1TFF and 3N32

1tff

3n32


Resolution: 2.047→49.712 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 0 / Phase error: 27.61 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2672 2641 5.08 %RANDOM
Rwork0.2057 ---
obs0.2088 52002 97.65 %-
Solvent computationShrinkage radii: 1.11 Å / VDW probe radii: 1.3 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 34.348 Å2 / ksol: 0.316 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--1.9217 Å20 Å2-0 Å2
2--3.726 Å2-0 Å2
3----1.8043 Å2
Refinement stepCycle: LAST / Resolution: 2.047→49.712 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5086 0 42 560 5688
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0075224
X-RAY DIFFRACTIONf_angle_d1.0357030
X-RAY DIFFRACTIONf_dihedral_angle_d13.9121952
X-RAY DIFFRACTIONf_chiral_restr0.075783
X-RAY DIFFRACTIONf_plane_restr0.005905
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A912X-RAY DIFFRACTIONPOSITIONAL
12C912X-RAY DIFFRACTIONPOSITIONAL0.045
21B324X-RAY DIFFRACTIONPOSITIONAL
22D324X-RAY DIFFRACTIONPOSITIONAL0.05
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.0465-2.08370.4131830.38231768X-RAY DIFFRACTION66
2.0837-2.12380.39051320.34532589X-RAY DIFFRACTION100
2.1238-2.16710.38151390.32252641X-RAY DIFFRACTION100
2.1671-2.21430.3561410.29852604X-RAY DIFFRACTION100
2.2143-2.26580.37321300.28662648X-RAY DIFFRACTION100
2.2658-2.32240.28771280.25132629X-RAY DIFFRACTION100
2.3224-2.38520.33741580.23942574X-RAY DIFFRACTION100
2.3852-2.45540.30661520.23522656X-RAY DIFFRACTION100
2.4554-2.53470.3061480.23342587X-RAY DIFFRACTION100
2.5347-2.62530.29951430.23182567X-RAY DIFFRACTION97
2.6253-2.73040.29851510.21462584X-RAY DIFFRACTION98
2.7304-2.85460.30191370.20752660X-RAY DIFFRACTION100
2.8546-3.00510.24511360.18832643X-RAY DIFFRACTION100
3.0051-3.19330.26571360.18752669X-RAY DIFFRACTION100
3.1933-3.43980.2521570.19082635X-RAY DIFFRACTION100
3.4398-3.78590.23631250.17282685X-RAY DIFFRACTION99
3.7859-4.33350.22571190.15642689X-RAY DIFFRACTION99
4.3335-5.45860.20221660.14072720X-RAY DIFFRACTION99
5.4586-49.72640.18431600.1642813X-RAY DIFFRACTION98
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)
12.82180.91030.19672.9048-0.16223.33590.1175-0.20710.07420.2884-0.0841-0.1886-0.17990.3192-0.05110.1523-0.0639-0.00880.55170.03840.10169.03278.699939.4444
22.52091.77240.18822.1363-0.10364.81940.03570.07610.2372-0.01230.01640.2373-0.3257-0.6224-0.15670.16680.04470.04320.68320.05160.1795-10.345510.856629.446
30.56830.0771-0.59180.1368-0.27850.9222-0.0497-0.0767-0.04830.04350.03930.04910.09250.00770.05310.108-0.05270.0450.47020.09510.06758.17992.698128.9175
45.03375.1145-5.23646.2393-5.86065.8108-0.4045-0.0408-0.1995-0.37440.32390.01850.5457-0.18450.12450.24650.14370.02250.55930.11850.164721.9401-9.099321.7321
50.64250.0271-0.00010.0434-0.01060.396-0.0412-0.0465-0.0275-0.0083-0.0235-0.05290.0430.26780.00030.07910.01460.07170.67920.09010.026921.49852.413122.5967
66.36796.45492.1426.83011.3972.8178-0.13960.65530.562-0.52430.11990.2639-0.2803-0.60390.00640.2449-0.05680.07020.51090.06390.199717.076413.29745.4646
70.97240.6414-0.43220.9597-0.25781.1170.0416-0.1224-0.0211-0.0166-0.0437-0.0263-0.0542-0.02950.01040.1181-0.03280.03590.38240.01980.09113.4216.413215.583
81.4564-0.6258-0.25560.84510.41111.03220.00030.13520.0074-0.0267-0.04330.12080.0016-0.2672-0.08820.0568-0.0028-0.00130.53350.08990.0818-0.43342.871621.2484
94.01223.65522.17317.10132.69868.8778-0.6443-1.03250.47380.36240.21810.2879-1.3213-1.51430.43150.32780.044-0.11420.5699-0.12260.2536-12.65.6452-20.0313
106.7041-0.33775.32944.1201-1.51365.51810.43270.4312-0.5312-0.3672-0.01980.20490.81330.2711-0.44530.26290.0823-0.10820.4235-0.01390.1752-0.09031.284-6.1323
111.8566-0.50831.86121.8765-1.15072.1030.15640.2334-0.1696-0.45860.05150.44420.185-0.2753-0.22320.16510.0445-0.10690.2828-0.0550.105-3.33643.3405-4.4706
126.42561.21211.64732.7711-0.17513.1373-0.1106-0.4238-0.003-0.05760.04730.4-0.1007-0.5537-0.00910.10680.0672-0.06760.46860.05140.1708-5.19267.49573.2953
133.13260.37541.38980.33320.00853.5432-0.2516-0.4390.34010.3040.0739-0.1055-0.4814-0.15920.16640.26950.0674-0.10520.40110.00930.13461.487915.2771-3.7527
141.8333-2.4163-0.73163.93491.71142.50380.11990.6765-0.0459-1.0249-0.1390.4590.13040.26140.02110.36630.1167-0.07370.42850.02820.15110.84269.8982-12.0812
151.55811.061.57024.12754.66528.42850.1496-0.00620.3035-0.30530.1071-0.0353-0.710.0997-0.21440.1766-0.01550.03150.2852-0.06540.10664.1198.3056.3205
163.8109-0.33930.79614.1174-0.13864.97530.0496-0.65890.42540.4386-0.0772-0.325-0.32010.32730.04110.198-0.0581-0.01020.2553-0.04050.1469.587547.049656.9845
171.40050.33590.0671.6961.01533.5191-0.01340.07590.0714-0.0723-0.16090.2174-0.2479-0.45580.07980.05940.07070.03710.295-0.10310.075-9.103349.337247.4919
181.6254-0.4072-0.13290.2924-0.27331.32760.0032-0.17550.0003-0.0053-0.0384-0.0397-0.0663-0.18060.03140.0909-0.00730.02290.1136-0.02790.08069.464341.261846.843
195.6892.7615-5.90384.0134-4.68798.0189-0.41450.1966-0.325-0.34150.1863-0.23020.5321-0.22340.23560.1253-0.0160.09210.3656-0.02410.218323.274529.493839.438
200.50220.0903-0.25360.2334-0.07190.6340.019-0.01280.0987-0.0449-0.1202-0.18580.03440.1967-0.028-0.0217-0.01530.09240.45640.03340.078322.707841.066140.4186
216.0445.42890.86965.73241.74283.0138-0.16070.86320.9726-0.69990.090.2536-1.0505-0.07540.0770.44710.0070.10640.33080.1820.379618.184952.077723.4323
220.61440.33980.20230.9468-0.16540.4467-0.01990.02670.20590.0106-0.0347-0.0275-0.0880.0640.02230.1684-0.06930.11850.01220.0270.168714.577945.100233.5131
235.7413-3.02910.40532.6485-0.06011.84060.1030.28610.2876-0.1096-0.17050.0162-0.1452-0.39310.05870.1189-0.00280.04780.2713-0.00890.071-2.44844.206737.0247
240.9975-0.25960.1791.84590.81472.1759-0.01710.01180.014-0.0717-0.02180.11530.0727-0.0248-0.0430.1111-0.02380.0466-0.0697-0.04730.17192.500939.991240.4236
255.7636-0.0555-4.50822.63961.70834.57650.26080.34510.305-0.0389-0.15430.1859-0.3245-0.4409-0.11730.30130.02910.16650.65990.08780.3607-14.568344.7305-2.0094
264.784-1.78185.04683.3476-2.60785.97380.39470.6232-0.2649-0.465-0.07850.12310.80340.6365-0.31710.32490.1204-0.04770.67970.08230.19410.081440.336711.7322
272.8781-1.71023.00734.743-2.23993.19740.2250.0408-0.2332-0.67320.16210.45430.1607-0.2467-0.39650.33540.1353-0.02310.80440.01110.1756-2.998842.163513.7723
287.50782.50671.43433.0237-0.48526.9063-0.03820.01880.2847-0.1809-0.04790.3674-0.1996-0.26130.07630.19290.1077-0.04290.60730.07610.2909-4.588446.283821.6544
299.3557-3.61730.03932.54361.70125.79850.05350.12420.8983-0.26450.0986-0.4339-0.7370.2249-0.15190.41210.08080.0990.97090.29610.54541.474254.271214.1371
302.3954-1.2015-1.495.08676.18058.2190.01950.81020.1294-1.53220.02830.4112-0.35360.2026-0.03980.55020.0862-0.08740.98740.16320.31770.691848.83465.9514
310.50710.84070.95451.45781.72152.79040.22170.24430.2345-0.23680.176-0.0813-0.45970.0088-0.41310.19780.02870.12560.52540.09390.23544.919547.2724.3148
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 2:14 )A2 - 14
2X-RAY DIFFRACTION2( CHAIN A AND RESID 15:37 )A15 - 37
3X-RAY DIFFRACTION3( CHAIN A AND RESID 38:67 )A38 - 67
4X-RAY DIFFRACTION4( CHAIN A AND RESID 68:87 )A68 - 87
5X-RAY DIFFRACTION5( CHAIN A AND RESID 88:153 )A88 - 153
6X-RAY DIFFRACTION6( CHAIN A AND RESID 154:167 )A154 - 167
7X-RAY DIFFRACTION7( CHAIN A AND RESID 168:187 )A168 - 187
8X-RAY DIFFRACTION8( CHAIN A AND RESID 188:232 )A188 - 232
9X-RAY DIFFRACTION9( CHAIN B AND RESID -5:0 )B-5 - 0
10X-RAY DIFFRACTION10( CHAIN B AND RESID 1:7 )B1 - 7
11X-RAY DIFFRACTION11( CHAIN B AND RESID 8:22 )B8 - 22
12X-RAY DIFFRACTION12( CHAIN B AND RESID 23:44 )B23 - 44
13X-RAY DIFFRACTION13( CHAIN B AND RESID 45:56 )B45 - 56
14X-RAY DIFFRACTION14( CHAIN B AND RESID 57:65 )B57 - 65
15X-RAY DIFFRACTION15( CHAIN B AND RESID 66:75 )B66 - 75
16X-RAY DIFFRACTION16( CHAIN C AND RESID 3:14 )C3 - 14
17X-RAY DIFFRACTION17( CHAIN C AND RESID 15:37 )C15 - 37
18X-RAY DIFFRACTION18( CHAIN C AND RESID 38:67 )C38 - 67
19X-RAY DIFFRACTION19( CHAIN C AND RESID 68:87 )C68 - 87
20X-RAY DIFFRACTION20( CHAIN C AND RESID 88:153 )C88 - 153
21X-RAY DIFFRACTION21( CHAIN C AND RESID 154:167 )C154 - 167
22X-RAY DIFFRACTION22( CHAIN C AND RESID 168:187 )C168 - 187
23X-RAY DIFFRACTION23( CHAIN C AND RESID 188:203 )C188 - 203
24X-RAY DIFFRACTION24( CHAIN C AND RESID 204:232 )C204 - 232
25X-RAY DIFFRACTION25( CHAIN D AND RESID -6:0 )D-6 - 0
26X-RAY DIFFRACTION26( CHAIN D AND RESID 1:7 )D1 - 7
27X-RAY DIFFRACTION27( CHAIN D AND RESID 8:22 )D8 - 22
28X-RAY DIFFRACTION28( CHAIN D AND RESID 23:44 )D23 - 44
29X-RAY DIFFRACTION29( CHAIN D AND RESID 45:56 )D45 - 56
30X-RAY DIFFRACTION30( CHAIN D AND RESID 57:65 )D57 - 65
31X-RAY DIFFRACTION31( CHAIN D AND RESID 66:75 )D66 - 75

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