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- PDB-4auq: Structure of BIRC7-UbcH5b-Ub complex. -

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Basic information

Entry
Database: PDB / ID: 4auq
TitleStructure of BIRC7-UbcH5b-Ub complex.
Components
  • BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 7
  • POLYUBIQUITIN-C
  • UBIQUITIN-CONJUGATING ENZYME E2 D2
KeywordsLIGASE/LIGASE/SIGNALLING PROTEIN / LIGASE-LIGASE-SIGNALLING PROTEIN COMPLEX
Function / homology
Function and homology information


regulation of natural killer cell apoptotic process / (E3-independent) E2 ubiquitin-conjugating enzyme / lens development in camera-type eye / E2 ubiquitin-conjugating enzyme / cysteine-type endopeptidase inhibitor activity / ubiquitin conjugating enzyme activity / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / negative regulation of tumor necrosis factor-mediated signaling pathway / protein K48-linked ubiquitination / protein autoubiquitination ...regulation of natural killer cell apoptotic process / (E3-independent) E2 ubiquitin-conjugating enzyme / lens development in camera-type eye / E2 ubiquitin-conjugating enzyme / cysteine-type endopeptidase inhibitor activity / ubiquitin conjugating enzyme activity / cysteine-type endopeptidase inhibitor activity involved in apoptotic process / negative regulation of tumor necrosis factor-mediated signaling pathway / protein K48-linked ubiquitination / protein autoubiquitination / ubiquitin ligase complex / 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 / NOTCH2 Activation and Transmission of Signal to the Nucleus / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of FZD by ubiquitination / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3 / 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 / APC/C:Cdc20 mediated degradation of Securin / positive regulation of protein ubiquitination / 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 / NOTCH3 Activation and Transmission of Signal to the Nucleus / TNFR2 non-canonical NF-kB pathway / 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 / Peroxisomal protein import / Termination of translesion DNA synthesis / 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
Similarity search - Function
BIR repeat. / BIR repeat / Inhibitor of Apoptosis domain / BIR repeat profile. / Baculoviral inhibition of apoptosis protein repeat / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Zinc finger, C3HC4 type (RING finger) / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. ...BIR repeat. / BIR repeat / Inhibitor of Apoptosis domain / BIR repeat profile. / Baculoviral inhibition of apoptosis protein repeat / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Zinc finger, C3HC4 type (RING finger) / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme/RWD-like / Zinc/RING finger domain, C3HC4 (zinc finger) / Herpes Virus-1 / Zinc finger, RING-type, conserved site / Zinc finger RING-type signature. / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ring finger / Ubiquitin conserved site / Ubiquitin domain / Zinc finger RING-type profile. / Zinc finger, RING-type / Ubiquitin domain signature. / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Ubiquitin-like domain superfamily / Zinc finger, RING/FYVE/PHD-type / Roll / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Polyubiquitin-C / Ubiquitin-conjugating enzyme E2 D2 / Baculoviral IAP repeat-containing protein 7
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.176 Å
AuthorsDou, H. / Buetow, L. / Sibbet, G.J. / Cameron, K. / Huang, D.T.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2012
Title: Birc7-E2 Ubiquitin Conjugate Structure Reveals the Mechanism of Ubiquitin Transfer by a Ring Dimer.
Authors: Dou, H. / Buetow, L. / Sibbet, G.J. / Cameron, K. / Huang, D.T.
History
DepositionMay 21, 2012Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 15, 2012Provider: repository / Type: Initial release
Revision 1.1Sep 26, 2012Group: Database references
Revision 1.2Jul 31, 2019Group: Advisory / Data collection / Derived calculations
Category: pdbx_struct_conn_angle / pdbx_validate_close_contact ...pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_conn / struct_conn_type
Item: _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id ..._pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value
Revision 1.3Dec 20, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _struct_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-CONJUGATING ENZYME E2 D2
B: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 7
C: POLYUBIQUITIN-C
D: UBIQUITIN-CONJUGATING ENZYME E2 D2
E: BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 7
F: POLYUBIQUITIN-C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)65,34310
Polymers65,0816
Non-polymers2624
Water2,756153
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8710 Å2
ΔGint-42.5 kcal/mol
Surface area25040 Å2
MethodPISA
Unit cell
Length a, b, c (Å)100.640, 100.640, 123.899
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein UBIQUITIN-CONJUGATING ENZYME E2 D2 / UBIQUITIN CARRIER PROTEIN D2 / UBIQUITIN-CONJUGATING ENZYME E2(17)KB 2 / UBIQUITIN-CONJUGATING ...UBIQUITIN CARRIER PROTEIN D2 / UBIQUITIN-CONJUGATING ENZYME E2(17)KB 2 / UBIQUITIN-CONJUGATING ENZYME E2-17 KDA 2 / UBIQUITIN-PROTEIN LIGASE D2


Mass: 16766.252 Da / Num. of mol.: 2 / Fragment: UBCH5B, RESIDUES 1-147 / Mutation: YES
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P62837, ubiquitin-protein ligase
#2: Protein BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 7 / KIDNEY INHIBITOR OF APOPTOSIS PROTEIN / KIAP / LIVIN / MELANOMA INHIBITOR OF APOPTOSIS PROTEIN / ML- ...KIDNEY INHIBITOR OF APOPTOSIS PROTEIN / KIAP / LIVIN / MELANOMA INHIBITOR OF APOPTOSIS PROTEIN / ML-IAP / RING FINGER PROTEIN 50 / BACULOVIRAL IAP REPEAT-CONTAINING PROTEIN 7 30KDA SUBUNIT / TRUNCATED LIVIN / P30-LIVIN / TLIVIN


Mass: 6852.156 Da / Num. of mol.: 2 / Fragment: RESIDUES 239-298
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: Q96CA5, Ligases; Forming carbon-nitrogen bonds; Acid-amino-acid ligases (peptide synthases)
#3: Protein POLYUBIQUITIN-C / UBIQUITIN


Mass: 8922.141 Da / Num. of mol.: 2 / Fragment: UBIQUITIN, RESIDUES 1-76
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P0CG48
#4: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Zn
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 153 / Source method: isolated from a natural source / Formula: H2O
Compound detailsENGINEERED RESIDUE IN CHAIN A, SER 22 TO ARG ENGINEERED RESIDUE IN CHAIN A, ASN 77 TO ALA ...ENGINEERED RESIDUE IN CHAIN A, SER 22 TO ARG ENGINEERED RESIDUE IN CHAIN A, ASN 77 TO ALA ENGINEERED RESIDUE IN CHAIN A, CYS 85 TO SER ENGINEERED RESIDUE IN CHAIN D, SER 22 TO ARG ENGINEERED RESIDUE IN CHAIN D, ASN 77 TO ALA ENGINEERED RESIDUE IN CHAIN D, CYS 85 TO SER

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.41 Å3/Da / Density % sol: 48.96 % / Description: NONE

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9763
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 2.18→30 Å / Num. obs: 33958 / % possible obs: 99.8 % / Observed criterion σ(I): 2 / Redundancy: 6.7 % / Biso Wilson estimate: 46.81 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 16.5
Reflection shellResolution: 2.18→2.29 Å / Redundancy: 6.6 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 3.3 / % possible all: 99.2

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 3A33 AND 3EB6

3a33

3eb6


Resolution: 2.176→29.499 Å / SU ML: 0.79 / σ(F): 1.34 / Phase error: 23.89 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2495 1718 5.1 %
Rwork0.2021 --
obs0.2044 33958 99.84 %
Solvent computationShrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 57.769 Å2 / ksol: 0.342 e/Å3
Displacement parametersBiso mean: 63.4 Å2
Baniso -1Baniso -2Baniso -3
1--2.4426 Å20 Å20 Å2
2---2.4426 Å20 Å2
3---4.8852 Å2
Refinement stepCycle: LAST / Resolution: 2.176→29.499 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4199 0 4 153 4356
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0094338
X-RAY DIFFRACTIONf_angle_d1.2395929
X-RAY DIFFRACTIONf_dihedral_angle_d14.8931584
X-RAY DIFFRACTIONf_chiral_restr0.083690
X-RAY DIFFRACTIONf_plane_restr0.008769
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1764-2.24040.41481380.35022602X-RAY DIFFRACTION98
2.2404-2.31270.35021580.32072616X-RAY DIFFRACTION100
2.3127-2.39530.32881400.27492648X-RAY DIFFRACTION100
2.3953-2.49120.27461330.2572658X-RAY DIFFRACTION100
2.4912-2.60450.27821360.23172647X-RAY DIFFRACTION100
2.6045-2.74170.30961260.23972690X-RAY DIFFRACTION100
2.7417-2.91330.29151590.22122644X-RAY DIFFRACTION100
2.9133-3.1380.27761640.21112668X-RAY DIFFRACTION100
3.138-3.45340.26981410.19642690X-RAY DIFFRACTION100
3.4534-3.95210.21251440.19252715X-RAY DIFFRACTION100
3.9521-4.97530.21491500.15152745X-RAY DIFFRACTION100
4.9753-29.50190.20811290.19252917X-RAY DIFFRACTION100
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)
19.5556-0.1331-5.54217.6347-0.04512.21930.02720.5242-1.9287-0.4623-0.5105-0.46260.67090.82130.44910.43650.15860.01680.4223-0.02580.43754.877-31.98499.5367
23.9333-0.4743-2.20413.7341-1.84983.3243-1.37890.77220.1317-0.8036-0.8846-0.18391.2741-0.93610.73190.5462-0.0680.27730.50370.05510.614410.8077-27.455-0.5565
35.27711.4234-3.16474.8904-2.65635.2086-0.25550.51260.15240.00660.0206-0.73740.0460.39760.17370.2230.0004-0.09440.40770.00260.43618.0081-19.24854.4517
43.1971-0.0324-1.00366.5545-6.72338.45280.29080.23431.30670.13160.169-0.0023-1.02730.1634-0.43950.386-0.1114-0.06570.50.10450.559.643-9.76330.0527
56.19943.252-0.26077.6063-3.4944.58420.15420.57581.2035-0.2571-0.25460.3776-0.18230.20170.09560.30050.0532-0.06380.39550.10560.491-0.9818-14.0460.8252
67.80863.9181-3.9629.1974-4.97012.1282-0.38990.32550.4622-0.86161.01250.08290.8062-0.9029-0.66620.35-0.0144-0.06380.456-0.03250.40533.6334-20.0401-4.4178
79.53841.8872-6.56082.04886.02886.64631.68912.3343-1.8049-0.8002-1.31361.87680.8597-2.124-0.65520.7430.0662-0.25661.04840.17681.3569-1.6923-6.7686-8.4414
86.372-1.90131.18348.4859-1.75846.52281.76263.00860.1854-0.9820.62171.9324-1.0447-1.1209-0.69250.6291-0.2097-0.07120.45041.56471.16673.1822-0.6747-14.5519
94.2063-1.34883.03385.7611-3.65437.99730.27630.68471.2194-0.9572-0.4741-0.92810.2031.3661-0.00920.5371-0.2410.03711.07230.37170.851915.1279-6.0816-11.9135
106.9294-2.6726-0.21362.02112.47366.1656-0.942-0.5366-0.1357-2.0720.7429-2.1954-0.88321.13440.02390.73190.0917-0.15510.5871-0.25051.1424-1.8536-45.94293.7762
118.87222.36862.44573.66591.44539.91340.0033-0.39280.04490.0837-0.0938-0.00720.4671-0.31570.09890.34910.019-0.07020.2217-0.01350.2409-12.0591-34.91228.4664
129.46757.0765-2.69752.57990.81677.60720.15170.15770.54510.232-0.21840.4274-0.2894-0.60540.10250.33060.0154-0.05350.30910.00040.323-18.263-32.53995.4831
138.326-0.45240.73557.0701-2.28156.8746-0.18570.1315-1.25220.04050.07370.03360.90710.0084-0.0480.52560.043-0.07030.42880.00010.6669-1.2572-36.9018-11.573
146.02521.1915-3.86561.8771-1.80127.0354-0.29620.6126-0.3932-0.28420.1378-0.05140.1279-1.21150.17730.3873-0.0644-0.16910.54280.07220.4984-8.5847-30.2216-14.151
159.47543.08146.56617.40343.66376.8260.20261.8519-0.1174-1.09890.3061-0.2321-1.87580.1925-0.54030.57260.0639-0.05931.04540.01920.4789-0.3386-22.2432-16.8569
166.23033.4522-2.40752.0556-5.0758.6148-0.25412.1841-0.1062-1.4361-0.3091-2.06861.00410.3290.59980.54040.00350.1560.7956-0.03460.7913.4644-29.9384-21.3168
171.82212.98580.67785.37132.59555.62790.14580.3873-0.23531.13280.1607-1.47980.1212-0.2129-0.41230.52730.1009-0.24980.48180.06890.58-0.7495-28.3149-8.1354
188.4778-1.92241.78632.00770.78772.027-0.56990.96620.54890.79070.42450.7298-2.2092-0.29150.17380.84430.1113-0.12720.83250.3420.9575-7.1569-15.1329-6.4303
192.3957-1.04881.36142.6729-1.49046.89430.0782-0.28990.11170.39750.1055-1.51370.16320.8390.00340.3662-0.0498-0.04820.43310.02080.4632-15.8407-66.4334-2.4302
2010.11413.0207-2.43293.3541-5.08538.7215-0.1702-0.3265-0.77540.614-0.6039-0.78730.43060.7650.67490.48890.01690.02190.3066-0.00890.484-21.204-75.69870.6273
213.20652.3656-1.05186.0514-2.2031.65410.1212-0.2604-0.1920.844-0.06530.2721-0.1276-0.225-0.06710.4049-0.04970.12240.3503-0.08230.359-30.5164-74.52023.4763
224.07553.9049-1.67156.4206-2.73110.97980.2922-0.47820.71120.451-0.06721.2714-0.03890.0309-0.18230.39920.00120.1690.3456-0.05660.4893-35.7422-68.05233.1655
232.55246.1535-6.30632.3468-6.70782.26520.3513-1.26840.03840.7884-0.89130.8290.03670.36930.34340.6306-0.06870.15070.4806-0.06330.4899-29.2776-70.03649.7142
242.32492.73752.94683.67394.81216.41930.3287-1.30360.88480.49780.19091.9628-1.14-1.2118-0.45270.774-0.04420.34761.01910.23410.8659-44.2763-70.528210.5063
256.9495-2.00330.10933.4591-0.83345.1972-0.2578-1.0125-0.20541.58020.47191.3602-0.0693-0.723-0.24150.8448-0.020.37160.48980.02090.7168-42.3982-82.816615.8176
261.43471.0986-0.30430.9528-0.37440.13120.9653-1.07220.08930.793-1.19320.137-0.132-0.58320.44820.8949-0.0948-0.40790.7461-0.20071.024-7.2672-53.6697.1479
277.3093.07170.16988.36890.58845.2957-0.1099-0.0239-0.03760.1456-0.1154-0.9807-0.35250.81380.18790.2911-0.0459-0.04830.39-0.04230.418-15.9194-53.0967-1.8971
282.3995-1.9103-2.70972.39372.02498.6121-0.08530.04060.0290.1653-0.26870.37410.0046-0.29350.36360.3299-0.0656-0.01880.2914-0.04870.2533-23.6501-46.5752-0.6112
292.2536-3.937-1.31892.16546.37177.6303-0.62240.54850.23530.23410.08920.43880.3351-0.97070.51390.3364-0.08370.01570.438-0.0290.4274-30.6179-49.46042.7888
304.34043.5672-1.04922.3168-1.20932.3799-0.55420.0333-1.3243-0.94130.161-0.2378-0.09260.54110.43010.6688-0.2046-0.14970.43240.13480.6298-18.4793-39.5872-2.2582
316.5402-0.6843-0.83695.4009-0.63790.20920.3069-0.9530.27410.84550.9542-0.50990.61280.9987-0.9881.96570.0756-0.17281.4820.05570.3402-16.2234-60.557620.0462
327.63652.14050.40542.01772.12742.018-0.23720.4073-0.18030.77631.2518-0.72861.5796-0.2713-0.88961.1026-0.18890.00921.92-0.44620.6885-17.7072-57.757813.4073
334.137-0.8218-1.90330.13310.36460.8673-0.0657-1.9107-0.79510.5881.0387-0.49730.55230.5656-0.18082.10931.14070.4123.3116-0.102-0.7163-22.6435-57.53530.5307
348.40021.45244.56662.01-6.45027.1594-0.8676-0.29890.15522.3913-0.14520.0728-0.4391-0.69140.77461.3677-0.27550.1781.0358-0.15080.7091-25.0312-52.019119.9631
357.03263.86080.64192.2114-0.09334.18980.42541.2794-0.06921.0533-0.54530.8404-0.15850.27230.01191.1897-0.03750.29590.69430.05010.8255-29.8389-56.312114.9318
365.20735.29023.97225.99632.44167.08581.70390.67440.0495-0.85860.2126-2.15410.03470.1731-1.56551.29910.6050.23851.4289-0.15571.4716-28.5867-68.732918.6713
379.18888.5444-3.36262.00564.24731.99370.3316-2.2988-0.46481.3228-1.4948-0.69180.0553-0.31381.05461.5311-0.21230.08891.39050.22551.0037-29.6351-63.280426.9559
380.50790.391-1.50865.9121-0.61615.0946-0.3316-0.30431.0750.3573-0.3753-0.28510.0684-0.49060.09450.6519-0.27780.17671.1826-0.32781.198-26.2652-63.345116.669
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A AND (RESSEQ 2:15)
2X-RAY DIFFRACTION2CHAIN A AND (RESSEQ 16:25)
3X-RAY DIFFRACTION3CHAIN A AND (RESSEQ 26:65)
4X-RAY DIFFRACTION4CHAIN A AND (RESSEQ 66:74)
5X-RAY DIFFRACTION5CHAIN A AND (RESSEQ 75:98)
6X-RAY DIFFRACTION6CHAIN A AND (RESSEQ 99:111)
7X-RAY DIFFRACTION7CHAIN A AND (RESSEQ 112:120)
8X-RAY DIFFRACTION8CHAIN A AND (RESSEQ 121:130)
9X-RAY DIFFRACTION9CHAIN A AND (RESSEQ 131:147)
10X-RAY DIFFRACTION10CHAIN B AND (RESSEQ 242:249)
11X-RAY DIFFRACTION11CHAIN B AND (RESSEQ 250:278)
12X-RAY DIFFRACTION12CHAIN B AND (RESSEQ 279:298)
13X-RAY DIFFRACTION13CHAIN C AND (RESSEQ 0:17)
14X-RAY DIFFRACTION14CHAIN C AND (RESSEQ 18:44)
15X-RAY DIFFRACTION15CHAIN C AND (RESSEQ 45:54)
16X-RAY DIFFRACTION16CHAIN C AND (RESSEQ 55:65)
17X-RAY DIFFRACTION17CHAIN C AND (RESSEQ 66:71)
18X-RAY DIFFRACTION18CHAIN C AND (RESSEQ 72:76)
19X-RAY DIFFRACTION19CHAIN D AND (RESSEQ 2:15)
20X-RAY DIFFRACTION20CHAIN D AND (RESSEQ 16:38)
21X-RAY DIFFRACTION21CHAIN D AND (RESSEQ 39:74)
22X-RAY DIFFRACTION22CHAIN D AND (RESSEQ 75:98)
23X-RAY DIFFRACTION23CHAIN D AND (RESSEQ 99:111)
24X-RAY DIFFRACTION24CHAIN D AND (RESSEQ 112:120)
25X-RAY DIFFRACTION25CHAIN D AND (RESSEQ 121:147)
26X-RAY DIFFRACTION26CHAIN E AND (RESSEQ 242:249)
27X-RAY DIFFRACTION27CHAIN E AND (RESSEQ 250:261)
28X-RAY DIFFRACTION28CHAIN E AND (RESSEQ 262:278)
29X-RAY DIFFRACTION29CHAIN E AND (RESSEQ 279:290)
30X-RAY DIFFRACTION30CHAIN E AND (RESSEQ 291:298)
31X-RAY DIFFRACTION31CHAIN F AND (RESSEQ 2:6)
32X-RAY DIFFRACTION32CHAIN F AND (RESSEQ 7:15)
33X-RAY DIFFRACTION33CHAIN F AND (RESSEQ 16:22)
34X-RAY DIFFRACTION34CHAIN F AND (RESSEQ 23:34)
35X-RAY DIFFRACTION35CHAIN F AND (RESSEQ 35:44)
36X-RAY DIFFRACTION36CHAIN F AND (RESSEQ 45:49)
37X-RAY DIFFRACTION37CHAIN F AND (RESSEQ 50:59)
38X-RAY DIFFRACTION38CHAIN F AND (RESSEQ 60:76)

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