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- PDB-6zqh: Yeast Uba1 in complex with ubiquitin -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6zqh
TitleYeast Uba1 in complex with ubiquitin
Components
  • Ubiquitin-40S ribosomal protein S31
  • Ubiquitin-activating enzyme E1 1
KeywordsLIGASE / Ubiquitin / E1
Function / homology
Function and homology information


Synthesis of active ubiquitin: roles of E1 and E2 enzymes / E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) / Formation of the ternary complex, and subsequently, the 43S complex / Translation initiation complex formation / Ribosomal scanning and start codon recognition / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) ...Synthesis of active ubiquitin: roles of E1 and E2 enzymes / E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) / Formation of the ternary complex, and subsequently, the 43S complex / Translation initiation complex formation / Ribosomal scanning and start codon recognition / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Antigen processing: Ubiquitination & Proteasome degradation / Formation of a pool of free 40S subunits / L13a-mediated translational silencing of Ceruloplasmin expression / maintenance of translational fidelity / modification-dependent protein catabolic process / protein tag activity / ribosome biogenesis / ribosomal small subunit assembly / ubiquitin-dependent protein catabolic process / cytosolic small ribosomal subunit / cytoplasmic translation / protein ubiquitination / structural constituent of ribosome / ubiquitin protein ligase binding / DNA damage response / ATP binding / nucleus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
Ubiquitin-activating enzyme E1, UFD 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, UFD 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 / THIF-type NAD/FAD binding fold / ThiF family / Ubiquitin-activating enzyme / 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 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Zinc-binding ribosomal protein / Ubiquitin-like domain superfamily / Roll / Beta Barrel / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
BETA-MERCAPTOETHANOL / Ubiquitin-ribosomal protein eS31 fusion protein / Ubiquitin-activating enzyme E1 1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.032 Å
AuthorsMisra, M. / Schindelin, H.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)GRK 2243 Germany
CitationJournal: Chemistry / Year: 2021
Title: Development of ADPribosyl Ubiquitin Analogues to Study Enzymes Involved in Legionella Infection.
Authors: Kim, R.Q. / Misra, M. / Gonzalez, A. / Tomaskovic, I. / Shin, D. / Schindelin, H. / Filippov, D.V. / Ovaa, H. / Dikic, I. / van der Heden van Noort, G.J.
History
DepositionJul 9, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 4, 2020Provider: repository / Type: Initial release
Revision 1.1Jan 13, 2021Group: Database references / Category: citation / citation_author
Item: _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Mar 3, 2021Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year / _citation_author.identifier_ORCID
Revision 1.3Jan 31, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquitin-activating enzyme E1 1
B: Ubiquitin-40S ribosomal protein S31
C: Ubiquitin-activating enzyme E1 1
D: Ubiquitin-40S ribosomal protein S31
hetero molecules


Theoretical massNumber of molelcules
Total (without water)246,80013
Polymers245,9254
Non-polymers8759
Water27,6711536
1
A: Ubiquitin-activating enzyme E1 1
B: Ubiquitin-40S ribosomal protein S31
hetero molecules


Theoretical massNumber of molelcules
Total (without water)123,3957
Polymers122,9632
Non-polymers4335
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4080 Å2
ΔGint-4 kcal/mol
Surface area46200 Å2
MethodPISA
2
C: Ubiquitin-activating enzyme E1 1
D: Ubiquitin-40S ribosomal protein S31
hetero molecules


Theoretical massNumber of molelcules
Total (without water)123,4056
Polymers122,9632
Non-polymers4434
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4510 Å2
ΔGint-4 kcal/mol
Surface area46260 Å2
MethodPISA
Unit cell
Length a, b, c (Å)76.868, 173.172, 214.805
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP22121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 12 through 15 or resid 17...
21(chain C and (resid 12 through 15 or resid 17...
12(chain B and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))
22(chain D and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 12 through 15 or resid 17...A12 - 15
121(chain A and (resid 12 through 15 or resid 17...A17 - 88
131(chain A and (resid 12 through 15 or resid 17...A90 - 100
141(chain A and (resid 12 through 15 or resid 17...A102 - 120
151(chain A and (resid 12 through 15 or resid 17...A284 - 368
161(chain A and (resid 12 through 15 or resid 17...A370 - 388
171(chain A and (resid 12 through 15 or resid 17...A390 - 4508
181(chain A and (resid 12 through 15 or resid 17...A510508
191(chain A and (resid 12 through 15 or resid 17...A510 - 545
1101(chain A and (resid 12 through 15 or resid 17...A547 - 57747
1111(chain A and (resid 12 through 15 or resid 17...A74983
1121(chain A and (resid 12 through 15 or resid 17...A585 - 747
1131(chain A and (resid 12 through 15 or resid 17...A749 - 851
1141(chain A and (resid 12 through 15 or resid 17...A934932
1151(chain A and (resid 12 through 15 or resid 17...A934 - 99
1161(chain A and (resid 12 through 15 or resid 17...A994 - 1003
1171(chain A and (resid 12 through 15 or resid 17...A1005 - 1021
1181(chain A and (resid 12 through 15 or resid 17...A1023 - 1024
211(chain C and (resid 12 through 15 or resid 17...C12 - 15
221(chain C and (resid 12 through 15 or resid 17...C17 - 88
231(chain C and (resid 12 through 15 or resid 17...C90 - 100
241(chain C and (resid 12 through 15 or resid 17...C264 - 282
251(chain C and (resid 12 through 15 or resid 17...C284 - 368
261(chain C and (resid 12 through 15 or resid 17...C370 - 388
271(chain C and (resid 12 through 15 or resid 17...C390 - 4508
281(chain C and (resid 12 through 15 or resid 17...C510508
291(chain C and (resid 12 through 15 or resid 17...C510 - 545
2101(chain C and (resid 12 through 15 or resid 17...C547 - 57747
2111(chain C and (resid 12 through 15 or resid 17...C74983
2121(chain C and (resid 12 through 15 or resid 17...C585 - 747
2131(chain C and (resid 12 through 15 or resid 17...C749 - 786
2141(chain C and (resid 12 through 15 or resid 17...C872870
2151(chain C and (resid 12 through 15 or resid 17...C872 - 93
2161(chain C and (resid 12 through 15 or resid 17...C934 - 992
2171(chain C and (resid 12 through 15 or resid 17...C994 - 1003
2181(chain C and (resid 12 through 15 or resid 17...C1005 - 1021
2191(chain C and (resid 12 through 15 or resid 17...C1023 - 1024
112(chain B and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))B1 - 38
122(chain B and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))B40 - 73
132(chain B and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))B75 - 76
142(chain B and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))B101
212(chain D and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))D1 - 38
222(chain D and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))D40 - 73
232(chain D and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))D75 - 76
242(chain D and (resid 1 through 38 or resid 40 through 73 or resid 75 through 76 or resid 101))D101

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein Ubiquitin-activating enzyme E1 1


Mass: 114393.844 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: UBA1, YKL210W / Production host: Escherichia coli (E. coli) / References: UniProt: P22515, E1 ubiquitin-activating enzyme
#2: Protein Ubiquitin-40S ribosomal protein S31


Mass: 8568.769 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (brewer's yeast)
Gene: RPS31, RPS37, UBI3, YLR167W, L9470.14 / Production host: Escherichia coli (E. coli) / References: UniProt: P05759

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Non-polymers , 4 types, 1545 molecules

#3: Chemical
ChemComp-BME / BETA-MERCAPTOETHANOL


Mass: 78.133 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C2H6OS
#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical ChemComp-PG4 / TETRAETHYLENE GLYCOL


Mass: 194.226 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C8H18O5 / Comment: precipitant*YM
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1536 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 2.91 Å3/Da / Density % sol: 57.68 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: ammonium formate, PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.1 / Wavelength: 0.9184 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jun 12, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9184 Å / Relative weight: 1
ReflectionResolution: 2.026→46.16 Å / Num. obs: 131321 / % possible obs: 70.4 % / Redundancy: 5.6 % / CC1/2: 0.99 / Net I/σ(I): 6.5
Reflection shellResolution: 2.026→2.105 Å / Num. unique obs: 6564 / CC1/2: 0.357

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Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
STARANISOdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3CMM

3cmm


Resolution: 2.032→46.158 Å / SU ML: 0.25 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 26.9 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2269 3250 2.5 %
Rwork0.1951 126509 -
obs0.1959 129759 70.26 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 167.18 Å2 / Biso mean: 42.8539 Å2 / Biso min: 11.5 Å2
Refinement stepCycle: final / Resolution: 2.032→46.158 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17079 0 127 1561 18767
Biso mean--53.68 37.32 -
Num. residues----2163
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A9459X-RAY DIFFRACTION6.286TORSIONAL
12C9459X-RAY DIFFRACTION6.286TORSIONAL
21B715X-RAY DIFFRACTION6.286TORSIONAL
22D715X-RAY DIFFRACTION6.286TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.0322-2.06250.573820.35841922
2.0625-2.09470.492770.32154035
2.0947-2.12910.4019100.31916608
2.1291-2.16580.3129320.2998113
2.1658-2.20520.3246450.288131617
2.2052-2.24760.2739440.2889196525
2.2476-2.29340.3111670.2849279936
2.2934-2.34330.3321910.2823376348
2.3433-2.39780.31181500.2775517367
2.3978-2.45780.30981720.2792706691
2.4578-2.52420.29132020.277774299
2.5242-2.59850.30441730.26497792100
2.5985-2.68240.30252090.25647769100
2.6824-2.77820.25231850.24487795100
2.7782-2.88940.2752090.2377757100
2.8894-3.02090.27262020.22177795100
3.0209-3.18020.25871970.21457849100
3.1802-3.37940.22952140.18277812100
3.3794-3.64020.1782090.16597863100
3.6402-4.00630.191980.14587890100
4.0063-4.58560.15292030.12637907100
4.5856-5.77560.17012140.14617969100
5.7756-46.1580.21092150.1767825199
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)
11.22230.4791-0.21970.93-0.25160.8454-0.03710.0642-0.0603-0.02030.06330.06320.14870.0034-00.22030.0158-0.02120.1633-0.04660.2139-10.883-31.077143.17
20.94930.21510.4311.00540.15131.3431-0.06950.11140.0295-0.0640.0625-0.0646-0.06580.19390.0040.09320.01020.01890.1599-0.02560.15925.9748-14.515646.0665
3-0.14330.30230.15640.9817-0.2078-0.05640.1247-0.1271-0.02140.3688-0.06260.04030.06160.02470.00160.26890.00450.00540.2058-0.00510.2323-3.8207-27.248970.2681
41.0381-0.14130.52490.604-0.53320.655-0.0571-0.64250.1670.55230.0494-0.0576-0.249-0.15650.01380.61490.0321-0.17610.49250.02880.3933-1.6745-56.630384.818
51.57030.56980.97941.8655-0.01041.88480.0066-0.0842-0.2360.27970.09250.18330.1171-0.0455-0.00150.3018-0.0441-0.04420.16770.07990.2424-16.4317-56.919272.2663
61.62880.02860.34941.5683-0.57361.11530.1199-0.3505-0.13520.31020.00620.08170.0723-0.07670.0030.3743-0.014-0.05560.26620.01780.2513-8.624-53.80875.1447
70.96390.54710.53990.43540.6322.33440.108-0.43370.0060.2117-0.10850.00380.01760.0991-0.00010.26740.01230.00780.3365-0.02040.25825.7886-9.715380.9962
80.036-0.020.05520.0161-0.02390.07890.07360.3295-0.0279-0.2798-0.04860.3631-0.009-0.0748-00.17930.0434-0.04730.272-0.04540.3191-24.1466-12.216156.9411
90.18610.06460.05360.0516-0.01190.2066-0.0604-0.2586-0.09910.0494-0.07920.2220.0988-0.090200.20860.03480.02520.2781-0.05770.3751-24.3243-11.864161.2142
100.1081-0.0117-0.00880.1271-0.11490.1418-0.0821-0.0591-0.11640.61590.26990.4741-0.036-0.09970.00090.2420.01990.07270.33530.00460.3616-23.0611-13.982868.3846
113.58222.37791.30772.15530.8180.48390.2833-1.0827-0.50090.67410.0167-0.32520.37240.16580.14290.30120.09380.0480.28920.01270.2951-14.9809-16.602467.7804
121.5263-0.4740.67820.7689-0.43950.3893-0.336-0.76850.67880.39240.3063-0.362-0.4034-0.0703-0.00130.16520.032-0.03710.2728-0.09860.3286-14.0013-4.793763.9206
130.37350.0749-0.29230.0244-0.05750.2270.1770.65390.5902-0.3558-0.02020.5308-0.438-0.42330.02340.22530.0378-0.01840.3653-0.01550.4561-21.059-2.350957.7402
140.3737-0.01380.08830.10020.03160.41290.1601-0.2007-0.2088-0.0812-0.19370.22050.1409-0.30160.01890.1676-0.0313-0.0110.15630.00550.2145-9.0741-20.319160.9825
150.64350.10120.10951.182-0.20941.6576-0.04390.08830.01-0.0609-0.0401-0.30510.0460.2136-0.00030.14030.0066-0.01180.18330.00260.2808-16.9776-66.171538.4065
160.9627-0.34030.62481.787-0.36081.50710.04580.07710.0580.0887-0.00870.1438-0.287-0.1581-00.25920.0091-0.00160.27890.00410.3276-36.5754-30.992738.2519
170.84850.0368-0.00391.3396-0.2831.1729-0.02510.094-0.0584-0.20270.02770.01630.0712-0.0645-0.00040.1595-0.0122-0.02050.1429-0.02440.1933-33.0026-73.813232.4068
180.03930.2616-0.16310.3343-0.153-0.11880.01720.15630.1324-0.3864-0.02970.1536-0.0262-0.121100.3808-0.0175-0.09320.34520.01280.3138-43.2191-56.049916.1979
190.4536-0.351-0.21021.30720.24910.3982-0.02540.7936-0.1722-0.644-0.02020.3117-0.0852-0.49620.00080.534-0.1021-0.06930.7192-0.04310.3423-27.9717-35.1869-5.6555
201.32591.07190.38792.1833-0.1262.5073-0.0080.11460.2266-0.00730.1101-0.0544-0.22550.04420.00160.3183-0.0378-0.01140.2710.0270.1407-21.6122-24.70168.9525
211.35590.2-0.38532.30510.09441.7069-0.1250.4320.1194-0.31850.1290.1871-0.167-0.17950.00030.4292-0.0714-0.03870.44090.04760.2606-23.7203-29.23021.1716
220.15750.0904-0.35930.3779-0.56611.25840.02320.1359-0.0226-0.24490.02770.10570.2337-0.27930.01550.2703-0.0373-0.09050.2848-0.02580.2402-46.3681-63.824318.9832
230.5053-0.23510.34760.5404-0.46090.8381-0.15530.41910.6138-0.50020.0618-0.20190.40630.03210.00280.7276-0.2758-0.10580.89040.07860.5549-63.7079-68.8463-5.9492
240.1048-0.1392-0.09470.29560.13030.0736-0.0382-0.87440.05210.898-0.1610.4224-0.1113-0.2977-0.00790.44230.0298-0.0250.5255-0.05940.4463-51.5281-48.837840.9693
250.12470.108-0.20280.0977-0.16840.3022-0.2587-0.13040.40980.225-0.00720.4183-0.67960.1816-0.00320.32010.0487-0.09640.4448-0.03180.5551-47.5551-46.047437.7688
260.0018-0.00330.0010.0063-0.00390.0166-0.1117-0.57330.40190.18470.1562-0.0767-0.4008-0.0964-00.32990.0381-0.02430.53740.01640.8075-63.8021-50.120237.9409
270.28610.0318-0.34720.0095-0.04630.42220.3193-0.28070.46230.01130.41280.2708-0.2365-0.30740.04390.38380.0567-0.11340.4440.02390.5639-55.9229-45.385830.7465
280.0341-0.0845-0.04340.31590.03470.06950.12240.22380.0858-0.5092-0.17750.1602-0.2205-0.07840.01040.36460.0452-0.11450.38070.07460.4921-51.1285-50.393725.5371
290.2315-0.0512-0.05180.3420.08770.1839-0.171-0.24140.22370.15650.04620.7417-0.0344-0.3161-0.00120.33270.0199-0.02090.41750.01510.4665-55.9214-56.962536.4425
300.0347-0.02660.00530.0420.03140.04680.01940.29540.4134-0.5428-0.1075-0.1629-0.36720.2168-0.00010.3517-0.0764-0.02590.29790.02080.309-38.382-55.872121.3838
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 12 through 264 )A12 - 264
2X-RAY DIFFRACTION2chain 'A' and (resid 265 through 545 )A265 - 545
3X-RAY DIFFRACTION3chain 'A' and (resid 546 through 624 )A546 - 624
4X-RAY DIFFRACTION4chain 'A' and (resid 625 through 684 )A625 - 684
5X-RAY DIFFRACTION5chain 'A' and (resid 685 through 754 )A685 - 754
6X-RAY DIFFRACTION6chain 'A' and (resid 755 through 866 )A755 - 866
7X-RAY DIFFRACTION7chain 'A' and (resid 867 through 1024 )A867 - 1024
8X-RAY DIFFRACTION8chain 'B' and (resid 1 through 7 )B1 - 7
9X-RAY DIFFRACTION9chain 'B' and (resid 8 through 22 )B8 - 22
10X-RAY DIFFRACTION10chain 'B' and (resid 23 through 34 )B23 - 34
11X-RAY DIFFRACTION11chain 'B' and (resid 35 through 44 )B35 - 44
12X-RAY DIFFRACTION12chain 'B' and (resid 45 through 56 )B45 - 56
13X-RAY DIFFRACTION13chain 'B' and (resid 57 through 65 )B57 - 65
14X-RAY DIFFRACTION14chain 'B' and (resid 66 through 76 )B66 - 76
15X-RAY DIFFRACTION15chain 'C' and (resid 12 through 166 )C12 - 166
16X-RAY DIFFRACTION16chain 'C' and (resid 167 through 264 )C167 - 264
17X-RAY DIFFRACTION17chain 'C' and (resid 265 through 545 )C265 - 545
18X-RAY DIFFRACTION18chain 'C' and (resid 546 through 608 )C546 - 608
19X-RAY DIFFRACTION19chain 'C' and (resid 609 through 668 )C609 - 668
20X-RAY DIFFRACTION20chain 'C' and (resid 669 through 754 )C669 - 754
21X-RAY DIFFRACTION21chain 'C' and (resid 755 through 844 )C755 - 844
22X-RAY DIFFRACTION22chain 'C' and (resid 845 through 949 )C845 - 949
23X-RAY DIFFRACTION23chain 'C' and (resid 950 through 1024 )C950 - 1024
24X-RAY DIFFRACTION24chain 'D' and (resid 1 through 7 )D1 - 7
25X-RAY DIFFRACTION25chain 'D' and (resid 8 through 16 )D8 - 16
26X-RAY DIFFRACTION26chain 'D' and (resid 17 through 22 )D17 - 22
27X-RAY DIFFRACTION27chain 'D' and (resid 23 through 34 )D23 - 34
28X-RAY DIFFRACTION28chain 'D' and (resid 35 through 44 )D35 - 44
29X-RAY DIFFRACTION29chain 'D' and (resid 45 through 70 )D45 - 70
30X-RAY DIFFRACTION30chain 'D' and (resid 71 through 76 )D71 - 76

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