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- PDB-6dc6: Crystal structure of human ubiquitin activating enzyme E1 (Uba1) ... -

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Basic information

Entry
Database: PDB / ID: 6dc6
TitleCrystal structure of human ubiquitin activating enzyme E1 (Uba1) in complex with ubiquitin
Components
  • Ubiquitin-like modifier-activating enzyme 1
  • Ubiquitin
KeywordsSIGNALING PROTEIN/LIGASE / Ubiquitin / E1 / adenylation / thioester bond / E2 / transthiolation / SIGNALING PROTEIN / SIGNALING PROTEIN-LIGASE complex
Function / homology
Function and homology information


E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Translation initiation complex formation / SARS-CoV-1 modulates host translation machinery / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination ...E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Translation initiation complex formation / SARS-CoV-1 modulates host translation machinery / 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 / 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) / 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 / small-subunit processome / 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 / cytosolic ribosome / 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 / 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
Similarity search - Function
Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2 / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / Ubiquitin-activating enzyme E1, UFD domain / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, conserved site / Ubiquitin-activating enzyme signature 1. / Ubiquitin-activating enzyme E1 / Ubiquitin-activating enzyme E1, C-terminal / Ubiquitin-activating enzyme E1, FCCH domain ...Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 2 / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / Ubiquitin-activating enzyme E1, UFD domain / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, conserved site / Ubiquitin-activating enzyme signature 1. / Ubiquitin-activating enzyme E1 / Ubiquitin-activating enzyme E1, C-terminal / Ubiquitin-activating enzyme E1, FCCH domain / Ubiquitin-activating enzyme E1, four-helix bundle / Ubiquitin-activating enzyme E1, C-terminal domain superfamily / Ubiquitin-activating enzyme E1, SCCH domain / Ubiquitin-activating enzyme E1, FCCH domain superfamily / Ubiquitin fold domain / Ubiquitin-activating enzyme E1 FCCH domain / Ubiquitin-activating enzyme E1 four-helix bundle / Ubiquitin-activating enzyme e1 C-terminal domain / Ubiquitin-activating enzyme, SCCH domain / Ubiquitin-activating enzyme, SCCH domain / Ubiquitin/SUMO-activating enzyme E1-like / Ubiquitin-activating enzyme E1, inactive adenylation domain, subdomain 1 / Ubiquitin-activating enzyme E1, Cys active site / Ubiquitin-activating enzyme active site. / ThiF/MoeB/HesA family / Ubiquitin-activating enzyme / THIF-type NAD/FAD binding fold / ThiF family / Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A / S27a-like superfamily / Ribosomal protein S27a / Ribosomal protein S27a / Ribosomal protein S27a / Elongation Factor Tu (Ef-tu); domain 3 / FAD/NAD(P)-binding domain / Ubiquitin conserved site / Ubiquitin domain / 3-Layer(bba) Sandwich / Ubiquitin domain signature. / Ubiquitin family / Ubiquitin homologues / Ubiquitin-like domain / Ubiquitin domain profile. / Zinc-binding ribosomal protein / Arc Repressor Mutant, subunit A / Ubiquitin-like domain superfamily / NAD(P)-binding Rossmann-like Domain / Roll / Beta Barrel / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PYROPHOSPHATE 2- / Ubiquitin-like modifier-activating enzyme 1 / Ubiquitin-ribosomal protein eS31 fusion protein
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.14 Å
AuthorsLv, Z. / Yuan, L. / Williams, K.M. / Atkison, J.H. / Olsen, S.K.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM115568 United States
CitationJournal: J. Biol. Chem. / Year: 2018
Title: Crystal structure of a human ubiquitin E1-ubiquitin complex reveals conserved functional elements essential for activity.
Authors: Lv, Z. / Williams, K.M. / Yuan, L. / Atkison, J.H. / Olsen, S.K.
History
DepositionMay 4, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 10, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 17, 2018Group: Data collection / Database references / Structure summary
Category: citation / citation_author / entity
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name / _entity.formula_weight
Revision 1.2Dec 5, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Oct 11, 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
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.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_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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin-like modifier-activating enzyme 1
B: Ubiquitin
C: Ubiquitin-like modifier-activating enzyme 1
D: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)245,27310
Polymers244,8244
Non-polymers4496
Water0
1
A: Ubiquitin-like modifier-activating enzyme 1
B: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)122,6365
Polymers122,4122
Non-polymers2253
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3790 Å2
ΔGint-27 kcal/mol
Surface area46670 Å2
MethodPISA
2
C: Ubiquitin-like modifier-activating enzyme 1
D: Ubiquitin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)122,6365
Polymers122,4122
Non-polymers2253
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3800 Å2
ΔGint-26 kcal/mol
Surface area47650 Å2
MethodPISA
Unit cell
Length a, b, c (Å)104.999, 70.438, 188.851
Angle α, β, γ (deg.)90.000, 95.190, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resseq 49:108 or (resid 109 and (name...
21(chain C and (resseq 49:108 or (resid 109 and (name...
12(chain B and ((resid 1 and (name N or name...
22(chain D and ((resid 1 and (name N or name...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resseq 49:108 or (resid 109 and (name...A0
211(chain C and (resseq 49:108 or (resid 109 and (name...C0
112(chain B and ((resid 1 and (name N or name...B1
122(chain B and ((resid 1 and (name N or name...B1 - 76
132(chain B and ((resid 1 and (name N or name...B1 - 76
142(chain B and ((resid 1 and (name N or name...B1 - 76
152(chain B and ((resid 1 and (name N or name...B1 - 76
162(chain B and ((resid 1 and (name N or name...B1 - 76
212(chain D and ((resid 1 and (name N or name...D1
222(chain D and ((resid 1 and (name N or name...D1 - 76
232(chain D and ((resid 1 and (name N or name...D1 - 76
242(chain D and ((resid 1 and (name N or name...D1 - 76
252(chain D and ((resid 1 and (name N or name...D1 - 76
262(chain D and ((resid 1 and (name N or name...D1 - 76

NCS ensembles :
ID
1
2

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Components

#1: Protein Ubiquitin-like modifier-activating enzyme 1 / Protein A1S9 / Ubiquitin-activating enzyme E1


Mass: 113504.680 Da / Num. of mol.: 2 / Mutation: C632A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: UBA1, A1S9T, UBE1 / Plasmid: pFastbac-HTB / Production host: Escherichia coli (E. coli) / References: UniProt: P22314, E1 ubiquitin-activating enzyme
#2: Protein Ubiquitin /


Mass: 8907.232 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pET29-NTEV / Production host: Escherichia coli (E. coli) / References: UniProt: P62979
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-POP / PYROPHOSPHATE 2- / Pyrophosphate


Mass: 175.959 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: H2O7P2

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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: 2.86 Å3/Da / Density % sol: 56.95 %
Crystal growTemperature: 285 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: 0.1 M MgCl2, 0.2 M Tris HCl pH 8.0, 20% PEG 4000

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Data collection

DiffractionMean temperature: 108 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Dec 16, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.15→50 Å / Num. obs: 46012 / % possible obs: 94.6 % / Redundancy: 2.9 % / Biso Wilson estimate: 70.5 Å2 / Rmerge(I) obs: 0.139 / Rpim(I) all: 0.088 / Rrim(I) all: 0.165 / Χ2: 0.946 / Net I/σ(I): 5.7 / Num. measured all: 133897
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) allΧ2% possible all
3.15-3.262.50.45945030.5920.3270.5660.49593.5
3.26-3.392.60.38245460.7460.2620.4660.56394.2
3.39-3.552.70.32845760.810.2230.3990.72694.8
3.55-3.732.80.25845900.8920.170.310.87694.9
3.73-3.972.80.21445980.9180.140.2571.01195.2
3.97-4.2730.15645890.9710.0980.1850.99295.6
4.27-4.73.10.14647110.9630.090.1711.14496.1
4.7-5.383.10.12746220.9750.0780.1491.28795.3
5.38-6.783.20.09846400.9830.0610.1161.05994.7
6.78-503.30.0846370.9860.0490.0951.00691.7

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Processing

Software
NameVersionClassification
PHENIX1.10.1_2155refinement
HKL-2000data reduction
HKL-2000data scaling
PDB_EXTRACT3.24data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3CMM

3cmm


Resolution: 3.14→41.702 Å / SU ML: 0.5 / Cross valid method: THROUGHOUT / σ(F): 1.41 / Phase error: 27.94 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.25 1997 4.35 %
Rwork0.2125 43931 -
obs0.2142 45928 94.51 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 200.06 Å2 / Biso mean: 90.0623 Å2 / Biso min: 3.78 Å2
Refinement stepCycle: final / Resolution: 3.14→41.702 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16866 0 22 0 16888
Biso mean--54.06 --
Num. residues----2140
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00317244
X-RAY DIFFRACTIONf_angle_d0.55423385
X-RAY DIFFRACTIONf_chiral_restr0.0412590
X-RAY DIFFRACTIONf_plane_restr0.0043077
X-RAY DIFFRACTIONf_dihedral_angle_d12.98410415
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A8103X-RAY DIFFRACTION10.741TORSIONAL
12C8103X-RAY DIFFRACTION10.741TORSIONAL
21B752X-RAY DIFFRACTION10.741TORSIONAL
22D752X-RAY DIFFRACTION10.741TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 14

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.1401-3.21860.39111380.3413053319193
3.2186-3.30560.34771410.31213096323794
3.3056-3.40280.36671420.28683102324495
3.4028-3.51260.31861430.27653151329495
3.5126-3.63810.30251400.25273092323295
3.6381-3.78370.29661420.25083120326295
3.7837-3.95570.31571440.23593161330595
3.9557-4.16410.24311430.21183152329595
4.1641-4.42470.24171450.18643173331896
4.4247-4.76590.19651440.18063162330696
4.7659-5.24470.21921440.17783187333195
5.2447-6.00170.25751440.20363172331695
6.0017-7.55420.21381440.18973161330594
7.5542-41.70550.16691430.1583149329291
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)
11.50470.2035-0.26022.3540.92011.66520.23530.0937-0.0782-0.931-0.2634-0.2486-0.3473-0.43840.06960.74130.12590.27180.4789-0.01540.4737525.3829-79.2782378.99
23.05120.16721.08361.05520.39110.48380.2846-0.7572-0.39610.1808-0.1119-0.50240.1351-0.3785-0.17220.3375-0.00190.12040.74180.07530.7245545.6472-75.0024412.9038
31.1654-0.11060.02741.34420.55221.10020.0924-0.2430.1350.2222-0.2123-0.0485-0.3043-0.19040.08730.4822-0.04780.16660.56290.00860.4814526.1878-64.7808409.8227
48.35550.4201-4.01136.6141-1.92422.787-0.83080.2482-1.4511-0.1820.24140.06640.9545-0.30120.55130.6963-0.07350.48750.9555-0.03620.8242516.5739-95.4133395.5088
56.7896-3.8376-5.20946.60423.47214.4415-0.14440.1303-2.02720.46070.56140.69130.16550.0373-0.37810.93360.16990.62670.91660.16361.826514.9687-99.7506399.2005
67.93550.5323-2.71080.7742-2.23446.6307-0.2754-0.194-1.3710.457-0.21840.91740.8687-1.51010.48650.9164-0.25970.631.60430.20511.4731502.8395-97.061403.5763
76.80140.55374.67134.60361.89823.7139-0.2246-2.102-1.08722.1815-0.42770.29690.7629-0.22750.58630.82940.12220.19481.26230.2980.6478511.2577-91.4252406.8017
89.84932.14757.26212.74483.59247.30830.8732-1.0921-1.83851.8893-0.2865-0.02970.03120.1632-0.60920.7242-0.1685-0.00191.40780.39321.0073519.8186-92.6619407.0035
99.58380.74984.44914.3371-3.06494.80881.1-2.79820.2142.3199-0.67461.2544-0.4253-1.8821-0.41570.9585-0.33710.21390.9908-0.10390.7572515.4057-84.053402.4331
102.58140.61322.50480.23550.44612.6787-0.1767-0.5622-0.36440.31750.20730.8928-0.014-0.93620.01370.4078-0.00390.27140.7454-0.08050.8952507.3423-84.9697393.0415
113.22193.8635-5.11616.0531-7.14218.83820.7357-1.11.31632.84050.24783.1318-1.7109-1.3594-0.98210.8514-0.02920.26930.8923-0.20971.0581504.6864-83.8725402.565
128.8367-5.0652.79193.0027-1.5450.9126-0.60052.1144-0.5779-0.63411.48782.66380.3543-0.9532-0.8720.7975-0.55610.19051.58260.00121.2187500.9651-89.5109398.9283
138.12440.62271.94848.5361-6.09165.05590.14574.5474-2.9365-1.3382-1.00211.42851.013-0.49320.86020.5807-0.05920.23761.5259-0.3591.378503.9074-97.5267393.1046
146.30376.2149-6.94297.8498-8.10648.5706-0.67740.8961-2.5257-0.71580.5915-1.79031.569-0.84510.05840.9241-0.12030.31080.4064-0.05840.75514.0843-90.4094394.2322
155.79265.4603-5.66615.7536-4.3548.4082-0.1872-0.6221-1.01180.2363-0.162-2.49450.48061.44390.33850.43130.23770.00610.6224-0.12420.7305525.4077-75.9848396.3981
161.9130.45390.15240.3534-0.37152.690.2346-0.3506-0.18580.9697-0.14630.0099-0.23470.34610.37762.0666-0.17640.43380.61990.11780.4257491.968-63.6335475.4486
172.3717-3.27330.59317.25283.99758.620.43660.8315-1.9455-0.06630.38690.46351.50460.7726-0.59251.0030.1864-0.00980.7314-0.3131.5318493.4933-87.0615443.7691
180.6771-0.0384-0.95410.00550.0341.34720.1233-0.6553-0.31431.158-0.2628-0.6278-0.37340.83490.22642.2281-0.3454-0.26941.0270.28030.7415511.7246-61.2355480.3585
191.8015-1.0951-0.31620.9029-0.35941.45150.2381-0.0230.49240.8352-0.1451-0.1161-0.71860.3302-0.10471.8319-0.18040.25780.51330.01850.5739501.2356-40.5171460.9169
204.7353-1.44752.41051.1333-0.55311.4331-0.23380.97650.26450.2589-0.30870.0497-0.53070.43580.5730.806-0.12110.17490.78990.03890.53491.227-49.4677434.1396
212.5772-1.211.77496.2916-0.3921.984-0.0760.5207-0.24790.1907-0.0050.4186-0.0891-0.24850.11130.5309-0.05620.25560.811-0.23570.6383475.316-56.2929429.3756
221.84950.591-1.14271.8913-0.59062.72140.318-0.5339-0.0140.9717-0.4928-0.3554-0.32860.54170.18581.0338-0.1109-0.04910.45920.04250.4673510.7716-54.4142455.9561
238.2838-1.0209-3.60446.1127-0.1037.8680.21431.0840.5326-0.2182-0.3133-0.4419-0.8836-0.0580.11450.7362-0.13130.01560.74020.24670.6684523.3259-33.804433.2542
244.43483.8581-2.38888.3412-2.7656.5043-0.51140.687-1.8469-0.68050.2561-1.52480.21970.6710.23660.9259-0.3540.32041.0307-0.00981.3858516.4697-77.9078453.4169
259.4941-3.7317-0.55827.9553-0.96948.8781-0.36513.3749-1.8369-2.0029-0.3452-0.60790.8940.22470.68671.1197-0.07650.42471.4301-0.27410.9013515.8408-72.9163444.9464
266.9386-0.2317-4.15222.80353.0825.58420.454-0.2934-0.8460.1252-0.5051-0.67160.73330.91670.01780.9695-0.1129-0.01830.67570.3120.7824517.9868-67.3676454.8146
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 49 through 590 )A49 - 590
2X-RAY DIFFRACTION2chain 'A' and (resid 591 through 776 )A591 - 776
3X-RAY DIFFRACTION3chain 'A' and (resid 777 through 1057 )A777 - 1057
4X-RAY DIFFRACTION4chain 'B' and (resid 1 through 11 )B1 - 11
5X-RAY DIFFRACTION5chain 'B' and (resid 12 through 16 )B12 - 16
6X-RAY DIFFRACTION6chain 'B' and (resid 17 through 22 )B17 - 22
7X-RAY DIFFRACTION7chain 'B' and (resid 23 through 31 )B23 - 31
8X-RAY DIFFRACTION8chain 'B' and (resid 32 through 37 )B32 - 37
9X-RAY DIFFRACTION9chain 'B' and (resid 38 through 44 )B38 - 44
10X-RAY DIFFRACTION10chain 'B' and (resid 45 through 49 )B45 - 49
11X-RAY DIFFRACTION11chain 'B' and (resid 50 through 54 )B50 - 54
12X-RAY DIFFRACTION12chain 'B' and (resid 55 through 59 )B55 - 59
13X-RAY DIFFRACTION13chain 'B' and (resid 60 through 64 )B60 - 64
14X-RAY DIFFRACTION14chain 'B' and (resid 65 through 70 )B65 - 70
15X-RAY DIFFRACTION15chain 'B' and (resid 71 through 76 )B71 - 76
16X-RAY DIFFRACTION16chain 'C' and (resid 49 through 234 )C49 - 234
17X-RAY DIFFRACTION17chain 'C' and (resid 235 through 295 )C235 - 295
18X-RAY DIFFRACTION18chain 'C' and (resid 296 through 477 )C296 - 477
19X-RAY DIFFRACTION19chain 'C' and (resid 478 through 601 )C478 - 601
20X-RAY DIFFRACTION20chain 'C' and (resid 602 through 702 )C602 - 702
21X-RAY DIFFRACTION21chain 'C' and (resid 703 through 872 )C703 - 872
22X-RAY DIFFRACTION22chain 'C' and (resid 873 through 962 )C873 - 962
23X-RAY DIFFRACTION23chain 'C' and (resid 963 through 1057 )C963 - 1057
24X-RAY DIFFRACTION24chain 'D' and (resid 1 through 22 )D1 - 22
25X-RAY DIFFRACTION25chain 'D' and (resid 23 through 37 )D23 - 37
26X-RAY DIFFRACTION26chain 'D' and (resid 38 through 76 )D38 - 76

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