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- PDB-6gfy: pVHL:EloB:EloC in complex with modified VH032 containing (3R,4S)-... -

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Basic information

Entry
Database: PDB / ID: 6gfy
TitlepVHL:EloB:EloC in complex with modified VH032 containing (3R,4S)-3-fluoro-4-hydroxyproline (ligand 14a)
Components
  • Elongin-B
  • Elongin-C
  • von Hippel-Lindau disease tumor suppressor
KeywordsLIGASE / protein complex / ubiquitin ligase / hypoxia inducible factor / fluorinated hydroxyproline
Function / homology
Function and homology information


regulation of cellular response to hypoxia / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / transcription elongation factor activity / target-directed miRNA degradation / elongin complex / VCB complex / Replication of the SARS-CoV-1 genome / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex ...regulation of cellular response to hypoxia / RHOBTB3 ATPase cycle / negative regulation of receptor signaling pathway via JAK-STAT / transcription elongation factor activity / target-directed miRNA degradation / elongin complex / VCB complex / Replication of the SARS-CoV-1 genome / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / intracellular non-membrane-bounded organelle / SUMOylation of ubiquitinylation proteins / negative regulation of transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / ubiquitin-like ligase-substrate adaptor activity / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / negative regulation of signal transduction / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / negative regulation of TORC1 signaling / RNA Polymerase II Pre-transcription Events / negative regulation of autophagy / transcription corepressor binding / Evasion by RSV of host interferon responses / transcription elongation by RNA polymerase II / transcription initiation at RNA polymerase II promoter / positive regulation of cell differentiation / TP53 Regulates Transcription of DNA Repair Genes / Vif-mediated degradation of APOBEC3G / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / cell morphogenesis / Inactivation of CSF3 (G-CSF) signaling / Regulation of expression of SLITs and ROBOs / ubiquitin-protein transferase activity / transcription corepressor activity / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / protein-macromolecule adaptor activity / Neddylation / Replication of the SARS-CoV-2 genome / cellular response to hypoxia / ubiquitin-dependent protein catabolic process / regulation of gene expression / proteasome-mediated ubiquitin-dependent protein catabolic process / protein-containing complex assembly / DNA-binding transcription factor binding / amyloid fibril formation / molecular adaptor activity / protein stabilization / protein ubiquitination / negative regulation of cell population proliferation / negative regulation of gene expression / ubiquitin protein ligase binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / enzyme binding / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / mitochondrion / proteolysis / nucleoplasm / nucleus / plasma membrane / cytosol
Similarity search - Function
von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / Elongin C; Chain C, domain 1 / von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain ...von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / Elongin C; Chain C, domain 1 / von Hippel-Lindau disease tumour suppressor, beta/alpha domain / von Hippel-Lindau disease tumour suppressor, alpha domain / von Hippel-Lindau disease tumour suppressor, beta domain / VHL superfamily / von Hippel-Lindau disease tumour suppressor, alpha domain superfamily / von Hippel-Lindau disease tumour suppressor, beta domain superfamily / VHL beta domain / VHL box domain / Elongin B / Elongin-C / Potassium Channel Kv1.1; Chain A / Potassium Channel Kv1.1; Chain A / S-phase kinase-associated protein 1-like / SKP1 component, POZ domain / Skp1 family, tetramerisation domain / Found in Skp1 protein family / SKP1/BTB/POZ domain superfamily / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / Ubiquitin-like (UB roll) / Ubiquitin family / Ubiquitin homologues / Ubiquitin domain profile. / Ubiquitin-like domain / Ubiquitin-like domain superfamily / Roll / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-EXH / von Hippel-Lindau disease tumor suppressor / Elongin-C / Elongin-B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
Model detailspVHL:EloB:EloC in complex with ........ (ligand 14a)
AuthorsGadd, M.S. / Testa, A. / Ciulli, A.
Funding support1items
OrganizationGrant numberCountry
European Research CouncilERC-2012-StG-311460 DrugE3CRLs
CitationJournal: J. Am. Chem. Soc. / Year: 2018
Title: 3-Fluoro-4-hydroxyprolines: Synthesis, Conformational Analysis, and Stereoselective Recognition by the VHL E3 Ubiquitin Ligase for Targeted Protein Degradation.
Authors: Testa, A. / Lucas, X. / Castro, G.V. / Chan, K.H. / Wright, J.E. / Runcie, A.C. / Gadd, M.S. / Harrison, W.T.A. / Ko, E.J. / Fletcher, D. / Ciulli, A.
History
DepositionMay 2, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 11, 2018Provider: repository / Type: Initial release
Revision 1.1Aug 1, 2018Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Jan 17, 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: Elongin-B
B: Elongin-C
C: von Hippel-Lindau disease tumor suppressor
D: Elongin-B
E: Elongin-C
F: von Hippel-Lindau disease tumor suppressor
G: Elongin-B
H: Elongin-C
I: von Hippel-Lindau disease tumor suppressor
J: Elongin-B
K: Elongin-C
L: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)168,91116
Polymers166,94912
Non-polymers1,9624
Water4,360242
1
A: Elongin-B
B: Elongin-C
C: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2284
Polymers41,7373
Non-polymers4911
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
D: Elongin-B
E: Elongin-C
F: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2284
Polymers41,7373
Non-polymers4911
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
G: Elongin-B
H: Elongin-C
I: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2284
Polymers41,7373
Non-polymers4911
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
J: Elongin-B
K: Elongin-C
L: von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2284
Polymers41,7373
Non-polymers4911
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)94.115, 94.115, 367.972
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number91
Space group name H-MP4122
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21D
31G
41J
12B
22E
32H
42K
13C
23F
33I
43L
14C
24F
34I
15C
25F
35I
45L

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1114A1 - 999
2114D1 - 999
3114G1 - 999
4114J1 - 999
1124B1 - 999
2124E1 - 999
3124H1 - 999
4124K1 - 999
1134C1 - 169
2134F1 - 169
3134I1 - 169
4134L1 - 169
1144C170 - 186
2144F170 - 186
3144I170 - 186
1154C186 - 999
2154F186 - 999
3154I186 - 999
4154L186 - 999

NCS ensembles :
ID
1
2
3
4
5

NCS oper:
IDCodeMatrixVector
1given(1), (1), (1)
2given(0.999802, 0.018972, -0.006076), (-0.018956, 0.999817, 0.002615), (0.006124, -0.002499, 0.999978)-3.90169, 48.347172, -0.24389
3given(0.998603, -0.052277, 0.007747), (0.052713, 0.995759, -0.075404), (-0.003773, 0.075707, 0.997123)42.541069, 55.40733, -0.67847
4given(0.999122, -0.034562, 0.023683), (0.036017, 0.997296, -0.064052), (-0.021405, 0.064849, 0.997666)47.15929, 7.33448, -4.05129
5given(1), (1), (1)
6given(0.999873, 0.015713, -0.002601), (-0.015722, 0.99987, -0.003485), (0.002546, 0.003525, 0.999991)-4.27047, 48.550579, -0.17384
7given(0.999073, -0.038002, 0.020222), (0.039832, 0.994244, -0.099459), (-0.016326, 0.100173, 0.994836)41.599579, 56.62093, -0.7333
8given(0.999297, -0.018962, 0.032337), (0.021916, 0.995372, -0.093568), (-0.030413, 0.094211, 0.995088)45.81052, 8.97837, -5.53233
9given(1), (1), (1)
10given(0.999884, -0.015058, 0.002234), (0.01511, 0.999552, -0.025839), (-0.001844, 0.02587, 0.999664)-4.48626, 48.931641, 0.01741
11given(0.998546, -0.050434, 0.019021), (0.05138, 0.997267, -0.053095), (-0.016291, 0.053995, 0.998408)41.34626, 52.971581, -0.61888
12given(0.998659, -0.042758, 0.029183), (0.043818, 0.998365, -0.036711), (-0.027565, 0.037941, 0.9989)47.02293, 4.48019, -2.80375
13given(1), (1), (1)
14given(0.999884, 0.012185, 0.009161), (-0.011863, 0.999337, -0.034427), (-0.009574, 0.034314, 0.999365)-5.12823, 50.706661, 0.52175
15given(0.997787, -0.056503, -0.035059), (0.05402, 0.996214, -0.068113), (0.038775, 0.066069, 0.997061)45.73436, 54.76759, -0.55586
16given(1), (1), (1)
17given(0.999913, -0.003978, 0.012589), (0.004204, 0.99983, -0.017975), (-0.012516, 0.018026, 0.999759)-5.45085, 48.636719, 0.46928
18given(0.997414, -0.067366, 0.025029), (0.068991, 0.995085, -0.071037), (-0.02012, 0.07258, 0.99716)40.93124, 54.642189, -0.48828
19given(0.998925, -0.010097, 0.045241), (0.012033, 0.999014, -0.042723), (-0.044765, 0.043222, 0.998062)43.8792, 4.40396, -3.14375

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Components

#1: Protein
Elongin-B / EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / ...EloB / Elongin 18 kDa subunit / RNA polymerase II transcription factor SIII subunit B / SIII p18 / Transcription elongation factor B polypeptide 2


Mass: 11956.372 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Plasmid: pCDFDuet-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15370
#2: Protein
Elongin-C / EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / ...EloC / Elongin 15 kDa subunit / RNA polymerase II transcription factor SIII subunit C / SIII p15 / Transcription elongation factor B polypeptide 1


Mass: 10974.616 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Plasmid: pCDFDuet-1 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: Q15369
#3: Protein
von Hippel-Lindau disease tumor suppressor / Protein G7 / pVHL


Mass: 18806.273 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: VHL / Plasmid: pHAT4 / Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: P40337
#4: Chemical
ChemComp-EXH / (2~{R},3~{R},4~{S})-1-[(2~{S})-2-acetamido-3,3-dimethyl-butanoyl]-3-fluoranyl-~{N}-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide


Mass: 490.591 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C24H31FN4O4S / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 242 / 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: 2.44 Å3/Da / Density % sol: 49.6 % / Mosaicity: 0.13 °
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 6.4 / Details: PEG 3350, MgOAc, Sodium cacodylate, DTT

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.9282 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Aug 2, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9282 Å / Relative weight: 1
ReflectionResolution: 2.7→49.36 Å / Num. obs: 46704 / % possible obs: 99.9 % / Redundancy: 8.7 % / CC1/2: 0.997 / Rmerge(I) obs: 0.149 / Rpim(I) all: 0.054 / Rrim(I) all: 0.159 / Net I/σ(I): 8.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
2.7-2.7980.7644400.8150.2850.81399.8
10.46-49.367.10.0539690.9980.0210.05799.2

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Processing

Software
NameVersionClassification
XDSdata reduction
Aimless0.3.11data scaling
REFMACrefinement
PDB_EXTRACT3.24data extraction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5NVV

5nvv


Resolution: 2.7→49.36 Å / Cor.coef. Fo:Fc: 0.954 / Cor.coef. Fo:Fc free: 0.931 / SU B: 27.884 / SU ML: 0.284 / SU R Cruickshank DPI: 3.7381 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 3.738 / ESU R Free: 0.354
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2584 2380 5.1 %RANDOM
Rwork0.1991 ---
obs0.2022 44252 99.76 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 135.45 Å2 / Biso mean: 51.899 Å2 / Biso min: 20.19 Å2
Baniso -1Baniso -2Baniso -3
1--0.32 Å2-0 Å20 Å2
2---0.32 Å20 Å2
3---0.63 Å2
Refinement stepCycle: final / Resolution: 2.7→49.36 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10626 0 136 242 11004
Biso mean--35.81 39.09 -
Num. residues----1338
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.01911008
X-RAY DIFFRACTIONr_bond_other_d0.0020.0210534
X-RAY DIFFRACTIONr_angle_refined_deg1.1762.00114971
X-RAY DIFFRACTIONr_angle_other_deg0.7563.00424215
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.79351322
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.36523.292486
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.566151813
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.5071590
X-RAY DIFFRACTIONr_chiral_restr0.0620.21709
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02112173
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022449
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1584MEDIUM POSITIONAL0.290.5
12D1584MEDIUM POSITIONAL0.260.5
13G1584MEDIUM POSITIONAL0.30.5
14J1584MEDIUM POSITIONAL0.330.5
11A1584MEDIUM THERMAL4.162
12D1584MEDIUM THERMAL3.792
13G1584MEDIUM THERMAL4.122
14J1584MEDIUM THERMAL4.482
21B1358MEDIUM POSITIONAL0.310.5
22E1358MEDIUM POSITIONAL0.330.5
23H1358MEDIUM POSITIONAL0.370.5
24K1358MEDIUM POSITIONAL0.350.5
21B1358MEDIUM THERMAL6.472
22E1358MEDIUM THERMAL4.822
23H1358MEDIUM THERMAL6.682
24K1358MEDIUM THERMAL4.672
31C1690MEDIUM POSITIONAL0.340.5
32F1690MEDIUM POSITIONAL0.380.5
33I1690MEDIUM POSITIONAL0.370.5
34L1690MEDIUM POSITIONAL0.370.5
31C1690MEDIUM THERMAL3.392
32F1690MEDIUM THERMAL3.232
33I1690MEDIUM THERMAL3.862
34L1690MEDIUM THERMAL3.362
41C252MEDIUM POSITIONAL0.310.5
42F252MEDIUM POSITIONAL0.320.5
43I252MEDIUM POSITIONAL0.570.5
41C252MEDIUM THERMAL5.262
42F252MEDIUM THERMAL2.812
43I252MEDIUM THERMAL5.82
51C244MEDIUM POSITIONAL0.40.5
52F244MEDIUM POSITIONAL0.470.5
53I244MEDIUM POSITIONAL0.410.5
54L244MEDIUM POSITIONAL0.440.5
51C244MEDIUM THERMAL5.662
52F244MEDIUM THERMAL6.422
53I244MEDIUM THERMAL6.742
54L244MEDIUM THERMAL5.122
LS refinement shellResolution: 2.7→2.77 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.364 166 -
Rwork0.297 3207 -
all-3373 -
obs--99.35 %
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)
12.1977-1.2920.97583.7236-1.54293.87530.05710.3533-0.0149-0.5506-0.1734-0.13910.0360.24570.11620.1412-0.01480.03270.19440.01290.014744.71464.80647.6
25.97010.7774-0.41911.7143-1.05513.2302-0.0415-0.0840.0411-0.03750.003-0.2506-0.0352-0.08040.03850.05810.02250.00290.21390.0060.046948.32561.13165.186
35.2351-1.0984-2.38021.85891.01132.1349-0.11090.0386-0.1050.1061-0.0088-0.10030.08920.05580.11980.1056-0.066-0.01530.21110.05880.037527.31654.33182.344
43.2118-0.63721.96451.9123-1.43065.3597-0.03260.7720.1818-0.39430.00240.0656-0.61911.16370.03010.344-0.1853-0.00140.58820.00030.040848.2718.07447.317
56.10151.15341.42090.7919-0.70383.8132-0.07910.7381-0.0160.0950.1215-0.0878-0.09050.5489-0.04240.1653-0.05970.01750.4528-0.04450.04652.814.08865.121
65.6409-1.1221-1.26062.16450.86152.1377-0.1186-0.0165-0.21070.10690.0304-0.09130.0144-0.05630.08820.0961-0.0714-0.01790.15470.02290.026231.7917.7582.037
73.8291-0.83960.21141.4413-1.09133.97430.16820.26090.3025-0.3622-0.15430.0151-0.19420.2481-0.01380.2581-0.05930.01990.36560.01960.04453.13412.98347.459
85.37551.3282-0.53421.69-1.51442.5394-0.1011-0.59990.21030.0557-0.0054-0.0194-0.1790.4190.10650.1749-0.03830.00040.6251-0.04880.02186.76910.83565.243
93.3157-0.9904-1.79721.3050.3854.6542-0.1244-0.2992-0.05710.00830.0040.03580.08710.6970.12040.0324-0.05270.00390.30650.00680.0049-14.4736.78982.326
103.0629-1.2256-0.13832.6359-0.70143.29670.07960.2346-0.0051-0.3257-0.17610.1265-0.00120.20260.09650.1687-0.0313-0.01360.19630.0150.0157-0.88760.62347.726
114.0746-0.1114-0.38051.2892-1.18722.6878-0.0284-0.2699-0.0952-0.021-0.12430.0399-0.10710.33520.15270.0672-0.0173-0.00820.3360.03510.02532.12658.50665.494
123.7924-0.5387-2.13981.50720.5413.9358-0.2702-0.2367-0.06980.00570.02880.0340.10710.32470.24140.0414-0.0315-0.00640.19160.04750.0214-19.06653.9682.603
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 104
2X-RAY DIFFRACTION2B16 - 112
3X-RAY DIFFRACTION3C62 - 202
4X-RAY DIFFRACTION4D1 - 103
5X-RAY DIFFRACTION5E16 - 112
6X-RAY DIFFRACTION6F62 - 204
7X-RAY DIFFRACTION7G1 - 103
8X-RAY DIFFRACTION8H16 - 112
9X-RAY DIFFRACTION9I62 - 204
10X-RAY DIFFRACTION10J1 - 103
11X-RAY DIFFRACTION11K16 - 112
12X-RAY DIFFRACTION12L62 - 204

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