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- PDB-5knl: Crystal structure of S. pombe ubiquitin E1 (Uba1) in complex with... -

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Basic information

Entry
Database: PDB / ID: 5knl
TitleCrystal structure of S. pombe ubiquitin E1 (Uba1) in complex with Ubc15 and ubiquitin
Components
  • Ubiquitin
  • Ubiquitin-activating enzyme E1 1
  • Ubiquitin-conjugating enzyme E2 15
KeywordsLIGASE / UBIQUITIN / E1 / E2 / UBA1 / UBC15 / CONFORMATIONAL CHANGE / THIOESTER / ADENYLATION / THIOESTER TRANSFER (TRANSTHIOESTERIFICATION) / ATP-Binding / UBIQUITIN E2 BINDING / UBIQUITINATION
Function / homology
Function and homology information


Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Antigen processing: Ubiquitination & Proteasome degradation / E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / modification-dependent protein catabolic process / protein polyubiquitination / protein tag activity / ubiquitin-dependent protein catabolic process ...Synthesis of active ubiquitin: roles of E1 and E2 enzymes / Antigen processing: Ubiquitination & Proteasome degradation / E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / E2 ubiquitin-conjugating enzyme / ubiquitin conjugating enzyme activity / modification-dependent protein catabolic process / protein polyubiquitination / protein tag activity / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / ribosome / protein ubiquitination / structural constituent of ribosome / translation / ribonucleoprotein complex / ubiquitin protein ligase binding / DNA damage response / magnesium ion binding / ATP hydrolysis activity / ATP binding / nucleus / cytosol / cytoplasm
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 / 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, 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 / 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. / Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A / ThiF/MoeB/HesA family / THIF-type NAD/FAD binding fold / ThiF family / Ubiquitin-activating enzyme / : / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / Ubiquitin-conjugating enzyme, active site / Ubiquitin-conjugating (UBC) active site signature. / Ubiquitin-conjugating enzyme E2 / Ubiquitin-conjugating enzyme / Ubiquitin-conjugating (UBC) core domain profile. / Ubiquitin-conjugating enzyme E2, catalytic domain homologues / Ubiquitin-conjugating enzyme/RWD-like / Ribosomal L40e family / Ribosomal_L40e / Ribosomal protein L40e / Ribosomal protein L40e superfamily / Elongation Factor Tu (Ef-tu); domain 3 / FAD/NAD(P)-binding domain / 3-Layer(bba) Sandwich / : / Ubiquitin domain signature. / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Arc Repressor Mutant, subunit A / NAD(P)-binding Rossmann-like Domain / Ubiquitin-like domain superfamily / Roll / Beta Barrel / Rossmann fold / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Probable RPL40A - Ubiquitin / Ubiquitin / Ubiquitin-activating enzyme E1 1 / Ubiquitin-conjugating enzyme E2 15
Similarity search - Component
Biological speciesSchizosaccharomyces pombe (fission yeast)
Pseudozyma antarctica (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsOlsen, S.K. / Lv, Z. / Yuan, L. / Williams, K.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM115568 United States
CitationJournal: Mol. Cell / Year: 2017
Title: S. pombe Uba1-Ubc15 Structure Reveals a Novel Regulatory Mechanism of Ubiquitin E2 Activity.
Authors: Lv, Z. / Rickman, K.A. / Yuan, L. / Williams, K. / Selvam, S.P. / Woosley, A.N. / Howe, P.H. / Ogretmen, B. / Smogorzewska, A. / Olsen, S.K.
History
DepositionJun 28, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 15, 2017Provider: repository / Type: Initial release
Revision 1.1Mar 1, 2017Group: Database references
Revision 1.2Sep 20, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.4Sep 27, 2023Group: 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
Revision 1.5Nov 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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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
C: Ubiquitin-conjugating enzyme E2 15
D: Ubiquitin-activating enzyme E1 1
E: Ubiquitin
F: Ubiquitin-conjugating enzyme E2 15
hetero molecules


Theoretical massNumber of molelcules
Total (without water)286,60115
Polymers285,7366
Non-polymers8659
Water1,69394
1
A: Ubiquitin-activating enzyme E1 1
B: Ubiquitin
C: Ubiquitin-conjugating enzyme E2 15
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,3498
Polymers142,8683
Non-polymers4805
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9290 Å2
ΔGint-109 kcal/mol
Surface area51260 Å2
MethodPISA
2
D: Ubiquitin-activating enzyme E1 1
E: Ubiquitin
F: Ubiquitin-conjugating enzyme E2 15
hetero molecules


Theoretical massNumber of molelcules
Total (without water)143,2527
Polymers142,8683
Non-polymers3844
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8120 Å2
ΔGint-75 kcal/mol
Surface area51280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)77.111, 82.238, 135.376
Angle α, β, γ (deg.)102.10, 95.78, 90.86
Int Tables number1
Space group name H-MP1

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Components

#1: Protein Ubiquitin-activating enzyme E1 1 / Poly(A)+ RNA transport protein 3


Mass: 111764.047 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (yeast)
Strain: 972 / ATCC 24843 / Gene: ptr3, SPBC1604.21c, SPBC211.09 / Plasmid: pSMT3 / Details (production host): pSMT3 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) codon plus / References: UniProt: O94609, E1 ubiquitin-activating enzyme
#2: Protein Ubiquitin


Mass: 10904.229 Da / Num. of mol.: 2
Mutation: K6R, K11R, K27R, S28A, K29R, K33R, K48R, S57A, K63R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Pseudozyma antarctica (fungus) / Gene: PAN0_008c3613 / Plasmid: pET-28 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) Codon Plus / References: UniProt: A0A081CFF0, UniProt: A0A081CEG8*PLUS
#3: Protein Ubiquitin-conjugating enzyme E2 15 / E2 ubiquitin-conjugating enzyme 15 / Ubiquitin carrier protein 15 / Ubiquitin-protein ligase 15


Mass: 20199.912 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Schizosaccharomyces pombe (strain 972 / ATCC 24843) (yeast)
Strain: 972 / ATCC 24843 / Gene: ubc15, SPBC1105.09 / Plasmid: pET-29 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) codon plus
References: UniProt: Q9Y818, E2 ubiquitin-conjugating enzyme
#4: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 9 / Source method: obtained synthetically / Formula: SO4
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 94 / Source method: isolated from a natural source / Formula: H2O
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.92 Å3/Da / Density % sol: 57.89 %
Crystal growTemperature: 291.15 K / Method: vapor diffusion, hanging drop
Details: 0.1 M Tris-HCl pH 8.0-8.5, 0.3-0.4 M lithium sulfate, 15-18% w/v polyethylene glycol 8000
PH range: 8.0-8.5

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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: Jul 31, 2014
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.5→29.7 Å / Num. obs: 108289 / % possible obs: 96.9 % / Redundancy: 3.5 % / CC1/2: 0.97 / Rmerge(I) obs: 0.051 / Net I/σ(I): 10.2
Reflection shellResolution: 2.5→2.55 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.289 / Mean I/σ(I) obs: 3.1 / CC1/2: 0.34 / % possible all: 93.2

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4II2

4ii2


Resolution: 2.5→28.314 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 2.53 / Phase error: 26.78
RfactorNum. reflection% reflectionSelection details
Rfree0.2513 10828 10 %random selection
Rwork0.216 ---
obs0.2196 108284 96.88 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.5→28.314 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19279 0 45 94 19418
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00319751
X-RAY DIFFRACTIONf_angle_d0.69926745
X-RAY DIFFRACTIONf_dihedral_angle_d11.9947409
X-RAY DIFFRACTIONf_chiral_restr0.0272965
X-RAY DIFFRACTIONf_plane_restr0.0033482
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5001-2.52840.37813410.35463067X-RAY DIFFRACTION93
2.5284-2.55820.38593520.35423175X-RAY DIFFRACTION93
2.5582-2.58930.38583530.34183176X-RAY DIFFRACTION95
2.5893-2.62210.35173500.3263145X-RAY DIFFRACTION95
2.6221-2.65660.35513660.32743295X-RAY DIFFRACTION95
2.6566-2.69290.33873460.3113118X-RAY DIFFRACTION95
2.6929-2.73140.33193570.31173215X-RAY DIFFRACTION96
2.7314-2.77210.34393590.29953220X-RAY DIFFRACTION96
2.7721-2.81540.3493570.29283217X-RAY DIFFRACTION96
2.8154-2.86150.32143590.28933229X-RAY DIFFRACTION96
2.8615-2.91080.32883540.29243194X-RAY DIFFRACTION96
2.9108-2.96370.32323610.29243239X-RAY DIFFRACTION96
2.9637-3.02060.32483590.28463238X-RAY DIFFRACTION97
3.0206-3.08220.29713650.26573277X-RAY DIFFRACTION97
3.0822-3.14910.29373630.26453279X-RAY DIFFRACTION97
3.1491-3.22230.30433600.25513233X-RAY DIFFRACTION97
3.2223-3.30280.26393650.24523292X-RAY DIFFRACTION98
3.3028-3.39190.26853690.23043314X-RAY DIFFRACTION98
3.3919-3.49160.26593630.21823269X-RAY DIFFRACTION98
3.4916-3.6040.23743660.19953300X-RAY DIFFRACTION98
3.604-3.73260.25273680.19553303X-RAY DIFFRACTION99
3.7326-3.88170.22333660.19023292X-RAY DIFFRACTION98
3.8817-4.05790.20043680.1683328X-RAY DIFFRACTION99
4.0579-4.27110.19533660.16073287X-RAY DIFFRACTION99
4.2711-4.53770.18013690.15233321X-RAY DIFFRACTION99
4.5377-4.88640.17873680.1413307X-RAY DIFFRACTION99
4.8864-5.37510.18543620.14763273X-RAY DIFFRACTION98
5.3751-6.1460.21043660.16473288X-RAY DIFFRACTION98
6.146-7.71720.1983680.15623311X-RAY DIFFRACTION98
7.7172-28.31620.16293620.14373254X-RAY DIFFRACTION97
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)
10.23550.0016-0.02060.07110.10960.20710.1853-0.1692-0.39040.1198-0.0142-0.21450.12280.18220.71790.11190.0229-0.07410.17470.00930.346428.1116-95.73381.2257
20.0187-0.00390.00540.00240.00140.00290.0606-0.03-0.0318-0.0247-0.0595-0.0645-0.0076-0.084400.29620.0648-0.07090.8976-0.04360.5949-14.5963-96.97140.739
30.0644-0.03620.12520.1329-0.03340.44940.1383-0.0474-0.23660.0038-0.01670.02470.2701-0.19210.1250.28310.0447-0.16820.18240.11440.591815.8735-112.407-3.6621
40.26980.05420.30720.1998-0.07330.43320.11890.1092-0.2884-0.19040.0879-0.18980.18710.36021.25610.08280.04530.04740.1952-0.09240.265230.1154-95.0603-19.693
50.2699-0.1950.03660.2131-0.01570.1135-0.071-0.00690.16210.02190.0433-0.1832-0.1874-0.1419-0.17050.23820.20230.05970.0361-0.19390.0176-0.4906-67.0306-16.9409
60.0457-0.00750.050.2616-0.0410.07-0.1696-0.09530.2169-0.04020.001-0.2519-0.1802-0.0775-0.17760.29360.0813-0.050.1431-0.03640.2714-0.1755-61.5856-14.0224
70.24780.0426-0.00230.0508-0.01920.02840.1480.3134-0.1439-0.1566-0.0101-0.10540.1178-0.00210.3920.44340.0837-0.03120.2907-0.10280.157712.4136-92.0513-44.8619
80.01430.02550.00350.0524-00.0125-0.05670.0017-0.02480.0261-0.0326-0.0020.00890.0124-0.04130.315-0.1668-0.05640.14360.05420.3964-0.3831-106.941-13.2167
90.00090.0002-0.00120.0002-0.00020.00380.0001-0.00520.0034-0.009-0.00420.00250.00080.000700.713-0.0812-0.10720.7509-0.0410.7321-6.1274-115.2908-24.5958
100.00110.0002-0.00130.0031-0.00040.00130.0483-0.0012-0.01870.01480.0252-0.0014-0.0146-0.0092-00.4143-0.01990.030.41230.05380.706-5.651-104.0922-22.9983
110.00240.001-0.00080.0006-0.0005-0.00010.01850.0223-0.01030.0212-0.01480.0041-0.0352-0.039500.33020.0474-0.08020.1775-0.02220.43311.008-98.7682-23.6359
120.00180.00070.00050.0025-0.00350.0034-0.01940.0011-0.0334-0.0389-0.0177-0.03750.02490.0005-00.44080.0392-0.13280.2603-0.07610.44255.1845-110.6601-27.4678
130.00690.0083-0.01540.0488-0.0330.03770.0403-0.0079-0.04560.0082-0.00630.0175-0.0036-0.0116-0.00630.58250.0121-0.17130.1303-0.02580.48972.51-117.8618-21.0536
140.0108-0.00330.00810.0036-0.00320.00390.0343-0.02050.01190.03450.0579-0.01490.0464-0.0200.23120.0029-0.10230.26620.02120.36398.4862-98.5564-18.9881
150.0049-0.0037-0.00150.00930.01050.00740.0097-0.024-0.011-0.03020.02240.020.02510.093100.5073-0.0372-0.02040.3490.03220.35111.2656-87.7243-43.0175
160.0034-0.0015-0.00470.00210.00180.0064-0.03690.00010.0115-0.0245-0.0393-0.0695-0.062-0.0144-00.4284-0.0442-0.02750.34660.05330.3293-7.7831-80.2019-46.4155
170.0044-0.0234-0.00410.41660.09150.01910.1185-0.0305-0.082-0.08630.0387-0.1227-0.044-0.22670.05260.207-0.0118-0.0180.4030.06890.185-13.3075-75.5568-34.0142
180.00090.0010.00020.00090.00040.0072-0.00490.01070.00210.03320.0176-0.015-0.00890.00201.0040.12470.12930.8538-0.07490.8534-12.2189-87.7669-14.9433
190.00520.0058-0.00310.00730.00020.01060.0047-0.03040.00280.00210.0210.03610.05970.042100.4034-0.0621-0.06420.50110.02650.3271-14.3026-84.6867-33.291
200.02270.01120.03210.00960.01180.04990.0193-0.01770.01090.06250.02730.0165-0.03410.00610.00470.2454-0.04890.00670.51610.06980.1323-24.7435-70.4846-22.3641
210.00410.00280.00150.0016-0.00050.0021-0.0047-0.02070.013-0.0579-0.01310.0234-0.0423-0.0241-00.3560.0062-0.09070.60890.07240.3156-25.2569-62.9477-39.1769
220.3246-0.16980.16310.34030.08480.41390.0080.09750.00280.0065-0.01620.0205-0.08540.1362-0.07840.1379-0.05290.02260.15620.04350.10335.9818-65.793921.7614
230.11460.11190.0270.3387-0.00930.30160.0901-0.0654-0.13950.00550.03940.0430.1669-0.01210.61860.2322-0.0916-0.08790.17280.08460.238229.1227-97.558545.6358
240.11530.03530.00140.14180.03480.21890.0271-0.0102-0.06450.08480.09090.0660.0270.0480.33490.2498-0.124-0.02790.10930.06350.181233.6186-87.367738.4328
250.4266-0.2332-0.21240.14180.12910.1181-0.2059-0.28190.04270.25290.0081-0.0157-0.11650.1594-0.13280.3817-0.1172-0.11510.61110.06920.278262.9891-76.596361.2158
260.01950.02570.02270.03440.03180.0305-0.0093-0.00520.013-0.00210.00180.0059-0.0098-0.02930.0130.2624-0.0072-0.07150.2515-0.22710.269725.7592-54.490643.8018
270.00250.0027-0.00290.0034-0.00340.0027-0.0208-0.04010.0303-0.0108-0.00280.02720.0321-0.0398-0.00250.27480.0027-0.01230.3568-0.19390.285224.2561-60.436843.5742
280.0376-0.00190.0060.0001-0.00050.00280.0017-0.0038-0.0030.0103-0.00910.00920.0049-0.0075-0.00030.9612-0.00930.0830.9698-0.21150.909730.0251-49.247255.4067
290.0008-0.0003-0.00070.0005-00.00230.0095-0.0148-0.0250.01450.00940.0213-0.0123-0.0368-00.726900.15580.8561-0.04990.630529.2412-60.412754.189
300.00380.0009-0.00120.0005-0.00150.00140.0392-0.03190.0059-0.00750.00940.0287-0.0044-0.0354-00.3738-0.19740.11530.414-0.08010.228833.9651-65.732949.2372
310.0042-0.00720.00080.0123-0.00090.00030.0008-0.00180.019-0.00230.0052-0.0068-0.0120.00330.02390.33510.017-0.00720.0952-0.12920.263339.2474-53.962548.1197
320.0049-0.00020.00230.00530.00070.00290.02590.0041-0.01190.0496-0.0056-0.0026-0.0214-0.019400.76960.0876-0.3340.4247-0.15750.587532.2521-47.000645.9584
330.0029-0.00650.00170.0244-0.00310.004-0.0153-0.0305-0.0060.0032-0.02880.0056-0.0212-0.0109-0.00010.32620.0708-0.01630.3654-0.0460.361131.8747-58.842441.6438
340.0025-0.0173-0.00430.10590.02840.00770.0131-0.0351-0.0071-0.0114-0.0414-0.01260.00650.0047-0.0230.2834-0.06210.1150.28840.04110.170838.5557-73.95538.587
350.00840.00530.00350.00460.00090.00220.00780.0149-0.0350.0181-0.05850.01880.03580.0076-00.4484-0.1263-0.00360.56190.05930.381549.5611-76.967460.9253
360.0031-0.0032-00.0034-0.00030.00010.0343-0.0294-0.0299-0.02490.0682-0.00810.0385-0.02650.00010.3808-0.0445-0.06740.3894-0.05510.223147.069-84.929369.9861
370.0375-0.00260.00850.03430.02650.0196-0.0138-0.1892-0.0649-0.03510.0562-0.0029-0.0676-0.0530.00120.3377-0.0829-0.02240.55770.140.348635.0352-90.556167.5231
380.0044-0.0024-0.00580.00310.0010.0053-0.0843-0.13980.05420.004-0.01020.06480.0144-0.059900.35740.0266-0.00130.5004-0.01290.38528.9486-82.886965.6124
390.0049-0.0169-0.00670.07070.01950.00540.02450.0856-0.04060.1267-0.0548-0.05260.0608-0.1738-0.0030.3903-0.2242-0.02080.83320.23910.505727.8788-101.749576.5807
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 14 through 181 )
2X-RAY DIFFRACTION2chain 'A' and (resid 182 through 228 )
3X-RAY DIFFRACTION3chain 'A' and (resid 229 through 331 )
4X-RAY DIFFRACTION4chain 'A' and (resid 332 through 538 )
5X-RAY DIFFRACTION5chain 'A' and (resid 539 through 753 )
6X-RAY DIFFRACTION6chain 'A' and (resid 754 through 855 )
7X-RAY DIFFRACTION7chain 'A' and (resid 856 through 1012 )
8X-RAY DIFFRACTION8chain 'B' and (resid 1 through 16 )
9X-RAY DIFFRACTION9chain 'B' and (resid 17 through 22 )
10X-RAY DIFFRACTION10chain 'B' and (resid 23 through 33 )
11X-RAY DIFFRACTION11chain 'B' and (resid 34 through 44 )
12X-RAY DIFFRACTION12chain 'B' and (resid 45 through 56 )
13X-RAY DIFFRACTION13chain 'B' and (resid 57 through 64 )
14X-RAY DIFFRACTION14chain 'B' and (resid 65 through 76 )
15X-RAY DIFFRACTION15chain 'C' and (resid 1 through 17 )
16X-RAY DIFFRACTION16chain 'C' and (resid 18 through 36 )
17X-RAY DIFFRACTION17chain 'C' and (resid 37 through 99 )
18X-RAY DIFFRACTION18chain 'C' and (resid 100 through 109 )
19X-RAY DIFFRACTION19chain 'C' and (resid 110 through 129 )
20X-RAY DIFFRACTION20chain 'C' and (resid 130 through 148 )
21X-RAY DIFFRACTION21chain 'C' and (resid 149 through 171 )
22X-RAY DIFFRACTION22chain 'D' and (resid 14 through 538 )
23X-RAY DIFFRACTION23chain 'D' and (resid 539 through 752 )
24X-RAY DIFFRACTION24chain 'D' and (resid 753 through 904 )
25X-RAY DIFFRACTION25chain 'D' and (resid 905 through 1012 )
26X-RAY DIFFRACTION26chain 'E' and (resid 1 through 7 )
27X-RAY DIFFRACTION27chain 'E' and (resid 8 through 16 )
28X-RAY DIFFRACTION28chain 'E' and (resid 17 through 22 )
29X-RAY DIFFRACTION29chain 'E' and (resid 23 through 33 )
30X-RAY DIFFRACTION30chain 'E' and (resid 34 through 44 )
31X-RAY DIFFRACTION31chain 'E' and (resid 45 through 56 )
32X-RAY DIFFRACTION32chain 'E' and (resid 57 through 65 )
33X-RAY DIFFRACTION33chain 'E' and (resid 66 through 70 )
34X-RAY DIFFRACTION34chain 'E' and (resid 71 through 76 )
35X-RAY DIFFRACTION35chain 'F' and (resid 1 through 17 )
36X-RAY DIFFRACTION36chain 'F' and (resid 18 through 36 )
37X-RAY DIFFRACTION37chain 'F' and (resid 37 through 94 )
38X-RAY DIFFRACTION38chain 'F' and (resid 95 through 138 )
39X-RAY DIFFRACTION39chain 'F' and (resid 139 through 171 )

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