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- PDB-6nya: Crystal Structure of ubiquitin E1 (Uba1) in complex with Ubc3 (Cd... -

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Basic information

Entry
Database: PDB / ID: 6nya
TitleCrystal Structure of ubiquitin E1 (Uba1) in complex with Ubc3 (Cdc34) and ubiquitin
Components
  • Ubiquitin-activating enzyme E1 1
  • Ubiquitin-conjugating enzyme E2-34 kDa
  • Ubiquitin
KeywordsLIGASE/TRANSFERASE / CONFORMATIONAL CHANGE / THIOESTER / ADENYLATION / THIOESTER TRANSFER / TRANSTHIOESTERIFICATION / ATP-BINDING / UBIQUITIN E2-BINDING / UBIQUITINATION / LIGASE / LIGASE-TRANSFERASE complex
Function / homology
Function and homology information


regulation of transcription by galactose / regulation of sulfur amino acid metabolic process / cellular response to methylmercury / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / Antigen processing: Ubiquitination & Proteasome degradation / regulation of metabolic process / positive regulation of glucose transmembrane transport / mitotic intra-S DNA damage checkpoint signaling ...regulation of transcription by galactose / regulation of sulfur amino acid metabolic process / cellular response to methylmercury / Synthesis of active ubiquitin: roles of E1 and E2 enzymes / E1 ubiquitin-activating enzyme / ubiquitin activating enzyme activity / Antigen processing: Ubiquitination & Proteasome degradation / regulation of metabolic process / positive regulation of glucose transmembrane transport / mitotic intra-S DNA damage checkpoint signaling / mitochondrial fusion / silent mating-type cassette heterochromatin formation / SCF ubiquitin ligase complex / E2 ubiquitin-conjugating enzyme / SCF-dependent proteasomal ubiquitin-dependent protein catabolic process / ubiquitin conjugating enzyme activity / subtelomeric heterochromatin formation / protein autoubiquitination / regulation of mitotic cell cycle / G1/S transition of mitotic cell cycle / modification-dependent protein catabolic process / protein polyubiquitination / protein tag activity / ubiquitin-protein transferase activity / G2/M transition of mitotic cell cycle / ubiquitin-dependent protein catabolic process / proteasome-mediated ubiquitin-dependent protein catabolic process / DNA replication / chromosome, telomeric region / protein ubiquitination / cell division / mRNA binding / DNA damage response / ubiquitin protein ligase binding / ATP binding / nucleus / 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, 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 / Structural Genomics Hypothetical 15.5 Kd Protein In mrcA-pckA Intergenic Region; Chain A / Ubiquitin-activating enzyme / THIF-type NAD/FAD binding fold / ThiF family / Ubiquitin Conjugating Enzyme / Ubiquitin Conjugating Enzyme / 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 / 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
ADENOSINE-5'-TRIPHOSPHATE / Uncharacterized protein / Ubiquitin-conjugating enzyme E2-34 kDa / Ubiquitin-activating enzyme E1 1 / Ubiquitin
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Triticum aestivum (bread wheat)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.065 Å
AuthorsOlsen, S.K. / Williams, K.M. / Atkison, J.H.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM115568 United States
CitationJournal: Nat Commun / Year: 2019
Title: Structural insights into E1 recognition and the ubiquitin-conjugating activity of the E2 enzyme Cdc34.
Authors: Williams, K.M. / Qie, S. / Atkison, J.H. / Salazar-Arango, S. / Alan Diehl, J. / Olsen, S.K.
History
DepositionFeb 11, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 7, 2019Provider: repository / Type: Initial release
Revision 1.1Jan 1, 2020Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Oct 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 / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.value / _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-activating enzyme E1 1
B: Ubiquitin
C: Ubiquitin-conjugating enzyme E2-34 kDa
D: Ubiquitin-activating enzyme E1 1
E: Ubiquitin
F: Ubiquitin-conjugating enzyme E2-34 kDa
hetero molecules


Theoretical massNumber of molelcules
Total (without water)295,71246
Polymers291,9056
Non-polymers3,80740
Water16,376909
1
A: Ubiquitin-activating enzyme E1 1
B: Ubiquitin
C: Ubiquitin-conjugating enzyme E2-34 kDa
hetero molecules


Theoretical massNumber of molelcules
Total (without water)147,99725
Polymers145,9523
Non-polymers2,04522
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11510 Å2
ΔGint-94 kcal/mol
Surface area52090 Å2
MethodPISA
2
D: Ubiquitin-activating enzyme E1 1
E: Ubiquitin
F: Ubiquitin-conjugating enzyme E2-34 kDa
hetero molecules


Theoretical massNumber of molelcules
Total (without water)147,71521
Polymers145,9523
Non-polymers1,76318
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11160 Å2
ΔGint-90 kcal/mol
Surface area52250 Å2
MethodPISA
Unit cell
Length a, b, c (Å)126.445, 68.544, 171.721
Angle α, β, γ (deg.)90.00, 110.72, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Protein , 3 types, 6 molecules ADBECF

#1: Protein Ubiquitin-activating enzyme E1 1


Mass: 113704.211 Da / Num. of mol.: 2 / Fragment: residues 11-1024
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: UBA1, YKL210W / Plasmid: pET29NTEV / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) codon plus / References: UniProt: P22515, E1 ubiquitin-activating enzyme
#2: Protein Ubiquitin /


Mass: 9821.071 Da / Num. of mol.: 2 / Fragment: residues 77-152 / Mutation: K6R, K11R, K27R, K29R, K33R, K48R, K63R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Triticum aestivum (bread wheat) / Plasmid: pET28b / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) codon plus / References: UniProt: A0A1D6RLC6, UniProt: P69326*PLUS
#3: Protein Ubiquitin-conjugating enzyme E2-34 kDa / Cell division control protein 34 / E2 ubiquitin-conjugating enzyme 3 / E3 ubiquitin ligase complex ...Cell division control protein 34 / E2 ubiquitin-conjugating enzyme 3 / E3 ubiquitin ligase complex SCF subunit CDC34 / Ubiquitin carrier protein / Ubiquitin-protein ligase


Mass: 22427.152 Da / Num. of mol.: 2 / Fragment: residues 3-195
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: CDC34, DNA6, UBC3, YDR054C, D4211, YD9609.08C / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) codon plus
References: UniProt: P14682, E2 ubiquitin-conjugating enzyme

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Non-polymers , 5 types, 949 molecules

#4: Chemical ChemComp-ATP / ADENOSINE-5'-TRIPHOSPHATE / Adenosine triphosphate


Mass: 507.181 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O13P3 / Comment: ATP, energy-carrying molecule*YM
#5: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#6: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: SO4
#7: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 21 / Source method: isolated from a natural source / Formula: C2H6O2
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 909 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.48 Å3/Da / Density % sol: 50.38 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 0.2 M ammonium sulfate, 25% PEG 3,350, 0.1 M Bis-Tris pH 6.5

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Data collection

DiffractionMean temperature: 108 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.979 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Aug 13, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.07→160.6 Å / Num. obs: 167880 / % possible obs: 99.2 % / Redundancy: 4.5 % / Rmerge(I) obs: 0.135 / Rpim(I) all: 0.072 / Net I/σ(I): 10.6
Reflection shellResolution: 2.07→2.1 Å / Rmerge(I) obs: 0.142 / Num. unique obs: 29564 / CC1/2: 0.347 / Rpim(I) all: 0.781

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3CMM

3cmm


Resolution: 2.065→117.035 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 23.39 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2168 2005 1.2 %
Rwork0.1872 --
obs0.1875 167601 99.03 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.065→117.035 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19573 0 223 909 20705
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00320170
X-RAY DIFFRACTIONf_angle_d0.5927274
X-RAY DIFFRACTIONf_dihedral_angle_d12.07312165
X-RAY DIFFRACTIONf_chiral_restr0.0423017
X-RAY DIFFRACTIONf_plane_restr0.0033546
LS refinement shellResolution: 2.07→2.12 Å
RfactorNum. reflection% reflection
Rfree0.337 --
Rwork0.311 --
obs-10692 89 %
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)
11.19350.41230.23810.5655-0.07130.972-0.0325-0.16910.20560.02910.01460.1207-0.0755-0.22880.00260.1710.02530.01160.2433-0.02190.1906-48.126410.8536-16.522
21.18770.06960.35030.8754-0.09971.3030.01350.0069-0.1801-0.22330.0049-0.09360.24090.19260.00670.29380.02150.02550.1804-0.02920.2025-27.6371-8.2285-46.0616
31.20420.20010.09030.7405-0.10670.85330.0153-0.29730.00860.1003-0.02730.00210.0476-0.0573-0.00530.23040.01090.01350.28680.00060.1714-33.92735.9885-5.221
40.4156-0.0626-0.03780.3515-0.29130.92-0.047-0.06690.1346-0.0305-0.0863-0.1628-0.01250.2669-0.02770.1816-0.0280.00560.23440.00690.2708-9.063520.2441-34.2326
50.71840.4230.22420.5883-0.35550.8127-0.04870.32960.1841-0.3235-0.096-0.13040.0279-0.0353-0.19040.2642-0.01920.05640.20250.00650.2032-16.919721.4156-56.0398
60.5982-0.0223-0.04160.5883-0.39350.946-0.00160.05790.1469-0.0616-0.017-0.1026-0.13180.1269-0.00320.2401-0.0380.02680.1838-0.00280.2491-17.026622.2513-38.7949
71.18660.2252-0.14770.9257-0.03560.77770.0749-0.3383-0.1319-0.0186-0.07-0.3756-0.03650.2183-0.00210.16330.01660.01270.2565-0.0040.26044.70368.6069-8.1481
80.01850.0186-0.00660.0388-0.03140.0135-0.17210.4014-0.66810.1908-0.17270.08970.2407-0.1288-0.00010.7012-0.0263-0.07960.2996-0.10220.6146-22.7321-18.5137-24.6532
90.12020.0433-0.04670.03520.01330.0705-0.12120.6505-0.4208-0.3665-0.0144-0.41330.5354-0.23990.00020.6360.0325-0.00670.5198-0.08550.6267-19.2881-16.8981-25.9515
100.7840.11880.06690.7874-0.98061.2887-0.13940.4288-0.5745-0.53220.5132-0.41130.38450.10970.25990.46740.03530.09530.5015-0.19480.5157-12.011-13.9357-27.468
110.06350.02360.06980.0327-0.02150.1534-0.290.4263-0.0549-0.16770.1139-0.5185-0.21010.4913-0.00890.35650.0290.05660.5041-0.0660.498-13.0148-5.9327-23.8055
120.02660.03690.00220.04630.01240.0593-0.0067-0.4293-0.60950.23390.1306-0.43520.62990.47280.00140.4230.1526-0.05310.4276-0.00990.5807-14.7301-13.6501-13.9898
130.0298-0.0293-0.05750.04510.04130.0706-0.1078-0.0525-0.92340.0775-0.0547-0.12250.65840.0691-0.00010.60150.0698-0.03240.35120.01410.6693-21.3308-17.5426-18.0202
140.0432-0.0377-0.01280.03590.01050.0206-0.10650.15240.0923-0.26750.0070.2210.137-0.32410.00050.22990.0512-0.00940.25850.00230.1911-19.42926.7808-21.6689
150.3202-0.0730.33680.0128-0.10990.4660.1836-0.0739-0.04890.436-0.03340.00270.39940.4974-00.53450.04850.06320.58770.07490.53813.18597.7184-26.0829
160.6780.25440.6130.27330.01210.66320.2470.2654-0.1262-0.2249-0.14390.01570.34360.31170.00140.45590.09060.10190.66080.12930.47285.99447.9133-39.4413
171.35550.46490.38731.8147-0.01040.18430.0920.98950.0327-0.72850.0899-0.24050.06710.9728-0.15240.49210.22770.13441.02330.11640.622913.35288.5621-49.4193
181.6620.4152-0.12050.8913-0.16891.11420.1152-0.08330.41910.033-0.04920.1367-0.19540.09060.13280.2885-0.04060.02410.1179-0.00430.2664-51.513620.8755-56.746
191.22110.33070.0641.0124-0.3690.9564-0.0503-0.0252-0.3101-0.21510.01760.00750.3517-0.002500.3173-0.0073-0.00270.15410.00820.2536-44.3048-17.2787-43.4536
201.32390.674-0.52760.9953-0.40141.0531-0.05430.37880.14-0.2230.1480.15150.0273-0.16450.49370.2551-0.0184-0.03930.22270.03210.1795-62.1317.8519-68.4184
210.15520.1164-0.06270.3703-0.1720.0925-0.01-0.1328-0.41590.159-0.17960.58150.2819-0.6856-0.78610.1867-0.13060.01380.7546-0.0980.5717-89.9335-12.577-30.0031
220.9614-0.06130.00520.81690.5421.47370.0525-0.1978-0.1510.0973-0.10230.07140.0731-0.3142-0.05420.2262-0.07150.03280.3550.07630.246-76.019-11.5253-25.9911
231.7916-0.3746-0.89941.6314-0.08750.3692-0.12860.842-0.5877-0.572-0.01450.70550.121-0.4308-0.59290.2914-0.2082-0.23090.4308-0.21750.5382-80.282-12.2939-71.6727
241.8366-0.36250.09190.25890.28690.52880.1821-0.0538-0.46050.2041-0.2302-0.67390.46380.2737-0.21080.52610.1510.01310.26520.03820.546-46.0355-15.7185-63.3449
250.101-0.0125-0.00850.0023-0.00230.00720.027-0.08180.024-0.09410.02940.02880.084-0.1156-0.00051.63580.1819-0.1120.6499-0.32061.076-47.4711-25.3826-74.7979
260.01630.05030.07080.19050.27920.4146-0.2142-0.2467-0.4398-0.2687-0.0064-0.29240.26650.2313-0.16840.79110.11310.0410.29160.21091.0044-54.0684-22.8554-64.1578
271.14660.38660.31840.1836-0.04120.930.09680.3795-0.5377-0.51090.0150.120.34320.04250.3860.5376-0.0075-0.00280.2274-0.10990.2914-55.0226-13.6974-69.9746
280.27220.2154-0.20860.185-0.20660.266-0.11670.24490.43780.04570.08670.37180.1395-0.2473-0.05250.399-0.2557-0.12190.32970.1341.2516-86.3915-31.6112-64.4884
290.01210.002-0.0265-0.0001-0.00890.06770.1620.00460.6019-0.0249-0.17250.3871-0.0761-0.1867-0.12450.4556-0.1779-0.09380.29130.13731.3401-88.1522-26.8233-57.5784
300.21030.1758-0.18340.1346-0.18680.2435-0.2166-0.01090.89310.1644-0.04080.5225-0.1272-0.0187-0.63840.4717-0.27230.1540.1424-0.14911.4032-83.7507-32.1975-50.147
310.20560.220.2110.38030.0960.33340.2868-0.16140.20750.2808-0.07550.0646-0.08780.0290.50280.4785-0.27620.25370.2853-0.32161.1959-77.8206-28.3604-43.0973
320.0322-0.0063-0.0120.0336-0.01320.0098-0.0773-0.6393-0.33540.24680.32050.27230.06670.397-0.00050.5367-0.1070.03670.5821-0.04281.0131-68.5243-25.9724-55.572
331.4797-0.6918-0.43211.01090.09443.0507-0.1441-0.76080.67860.6957-0.4395-0.06260.00140.2671-0.37050.5551-0.28380.07940.4526-0.18331.0342-75.3911-36.4189-41.786
340.9044-0.4377-0.74890.25730.22411.0726-0.0666-0.4690.38710.6336-0.35670.5196-0.14350.2188-0.09180.778-0.30590.22140.6146-0.17631.1484-91.1152-40.9808-41.3392
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 11 through 166 )
2X-RAY DIFFRACTION2chain 'A' and (resid 167 through 264 )
3X-RAY DIFFRACTION3chain 'A' and (resid 265 through 545 )
4X-RAY DIFFRACTION4chain 'A' and (resid 546 through 684 )
5X-RAY DIFFRACTION5chain 'A' and (resid 685 through 763 )
6X-RAY DIFFRACTION6chain 'A' and (resid 764 through 885 )
7X-RAY DIFFRACTION7chain 'A' and (resid 886 through 1024 )
8X-RAY DIFFRACTION8chain 'B' and (resid -1 through 7 )
9X-RAY DIFFRACTION9chain 'B' and (resid 8 through 22 )
10X-RAY DIFFRACTION10chain 'B' and (resid 23 through 34 )
11X-RAY DIFFRACTION11chain 'B' and (resid 35 through 44 )
12X-RAY DIFFRACTION12chain 'B' and (resid 45 through 56 )
13X-RAY DIFFRACTION13chain 'B' and (resid 57 through 70 )
14X-RAY DIFFRACTION14chain 'B' and (resid 71 through 76 )
15X-RAY DIFFRACTION15chain 'C' and (resid 3 through 47 )
16X-RAY DIFFRACTION16chain 'C' and (resid 48 through 120 )
17X-RAY DIFFRACTION17chain 'C' and (resid 121 through 181 )
18X-RAY DIFFRACTION18chain 'D' and (resid 11 through 166 )
19X-RAY DIFFRACTION19chain 'D' and (resid 167 through 264 )
20X-RAY DIFFRACTION20chain 'D' and (resid 265 through 624 )
21X-RAY DIFFRACTION21chain 'D' and (resid 625 through 684 )
22X-RAY DIFFRACTION22chain 'D' and (resid 685 through 844 )
23X-RAY DIFFRACTION23chain 'D' and (resid 845 through 1024 )
24X-RAY DIFFRACTION24chain 'E' and (resid 0 through 17 )
25X-RAY DIFFRACTION25chain 'E' and (resid 18 through 22 )
26X-RAY DIFFRACTION26chain 'E' and (resid 23 through 34 )
27X-RAY DIFFRACTION27chain 'E' and (resid 35 through 76 )
28X-RAY DIFFRACTION28chain 'F' and (resid 5 through 37 )
29X-RAY DIFFRACTION29chain 'F' and (resid 38 through 46 )
30X-RAY DIFFRACTION30chain 'F' and (resid 47 through 84 )
31X-RAY DIFFRACTION31chain 'F' and (resid 85 through 99 )
32X-RAY DIFFRACTION32chain 'F' and (resid 100 through 120 )
33X-RAY DIFFRACTION33chain 'F' and (resid 121 through 152 )
34X-RAY DIFFRACTION34chain 'F' and (resid 153 through 178 )

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