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- PDB-5nvw: pVHL:EloB:EloC in complex with (2S,4R)-1-((S)-2-(cyclopropanecarb... -

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Basic information

Entry
Database: PDB / ID: 5nvw
TitlepVHL:EloB:EloC in complex with (2S,4R)-1-((S)-2-(cyclopropanecarboxamido)-3,3-dimethylbutanoyl)-4-hydroxy-N-(4-(4-methylthiazol-5-yl)benzyl)pyrrolidine-2-carboxamide (ligand 6)
Components
  • Elongin-B
  • Elongin-C
  • Von Hippel-Lindau disease tumor suppressor
KeywordsLIGASE / protein complex / ubiquitin ligase / hypoxia inducible factor
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 / Replication of the SARS-CoV-1 genome / VCB complex / 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 / Replication of the SARS-CoV-1 genome / VCB complex / Cul5-RING ubiquitin ligase complex / Cul2-RING ubiquitin ligase complex / intracellular membraneless organelle / SUMOylation of ubiquitinylation proteins / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / negative regulation of transcription elongation by RNA polymerase II / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / negative regulation of signal transduction / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / ubiquitin-like ligase-substrate adaptor activity / Formation of HIV elongation complex in the absence of HIV Tat / 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 / protein serine/threonine kinase binding / transcription corepressor binding / positive regulation of cell differentiation / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / Inactivation of CSF3 (G-CSF) signaling / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Evasion by RSV of host interferon responses / Regulation of expression of SLITs and ROBOs / cell morphogenesis / ubiquitin-protein transferase activity / transcription corepressor activity / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Neddylation / microtubule cytoskeleton / regulation of gene expression / protein-containing complex assembly / Replication of the SARS-CoV-2 genome / ubiquitin-dependent protein catabolic process / protein-macromolecule adaptor activity / cellular response to hypoxia / molecular adaptor activity / DNA-binding transcription factor binding / amyloid fibril formation / proteasome-mediated ubiquitin-dependent protein catabolic process / protein stabilization / protein ubiquitination / cilium / 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 / endoplasmic reticulum / negative regulation of transcription by RNA polymerase II / 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-C / Elongin B / 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 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / SKP1/BTB/POZ domain superfamily / 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-9BW / von Hippel-Lindau disease tumor suppressor / Elongin-C / Elongin-B
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
Model detailspVHL:EloB:EloC in complex with (2S,4R)-1-((S)-2-(cyclopropanecarboxamido)-3,3-dimethylbutanoyl)-4- ...pVHL:EloB:EloC in complex with (2S,4R)-1-((S)-2-(cyclopropanecarboxamido)-3,3-dimethylbutanoyl)-4-hydroxy-N-(4-(4-methylthiazol-5-yl)benzyl)pyrrolidine-2-carboxamide (ligand 6)
AuthorsGadd, M.S. / Soares, P. / Galdeano, C. / Ciulli, A.
Funding support1items
OrganizationGrant numberCountry
European Research CouncilERC-2012-StG-311460 DrugE3CRLs
CitationJournal: J. Med. Chem. / Year: 2018
Title: Group-Based Optimization of Potent and Cell-Active Inhibitors of the von Hippel-Lindau (VHL) E3 Ubiquitin Ligase: Structure-Activity Relationships Leading to the Chemical Probe (2S,4R)-1-((S)- ...Title: Group-Based Optimization of Potent and Cell-Active Inhibitors of the von Hippel-Lindau (VHL) E3 Ubiquitin Ligase: Structure-Activity Relationships Leading to the Chemical Probe (2S,4R)-1-((S)-2-(1-Cyanocyclopropanecarboxamido)-3,3-dimethylbutanoyl)-4-hydroxy-N-(4-(4-methylthiazol-5-yl)benzyl)pyrrolidine-2-carboxamide (VH298).
Authors: Soares, P. / Gadd, M.S. / Frost, J. / Galdeano, C. / Ellis, L. / Epemolu, O. / Rocha, S. / Read, K.D. / Ciulli, A.
History
DepositionMay 4, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 20, 2017Provider: repository / Type: Initial release
Revision 1.1Feb 7, 2018Group: 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.year / _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
Revision 1.3Nov 13, 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: 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)168,94416
Polymers166,94912
Non-polymers1,9954
Water16,556919
1
A: Elongin-B
B: Elongin-C
C: Von Hippel-Lindau disease tumor suppressor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,2364
Polymers41,7373
Non-polymers4991
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)42,2364
Polymers41,7373
Non-polymers4991
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)42,2364
Polymers41,7373
Non-polymers4991
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)42,2364
Polymers41,7373
Non-polymers4991
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)93.226, 93.226, 365.081
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(0.999643, 0.025787, -0.006987), (-0.025741, 0.999646, 0.006676), (0.007157, -0.006494, 0.999953)-3.89889, 47.965351, -0.18349
3given(0.998222, -0.059181, 0.007124), (0.059553, 0.995304, -0.076307), (-0.002575, 0.076595, 0.997059)41.994961, 55.266579, -0.663
4given(0.999055, -0.037232, 0.022428), (0.038617, 0.997145, -0.064881), (-0.019948, 0.065686, 0.997641)46.753151, 7.36128, -4.04788
5given(1), (1), (1)
6given(0.999792, 0.018885, -0.007765), (-0.018875, 0.999821, 0.001401), (0.00779, -0.001254, 0.999969)-3.92746, 47.925949, -0.30972
7given(0.99873, -0.045115, 0.022407), (0.047199, 0.993523, -0.10337), (-0.017599, 0.104296, 0.994391)40.968929, 56.681412, -0.66723
8given(0.999186, -0.02114, 0.034344), (0.024316, 0.995191, -0.094885), (-0.032173, 0.095643, 0.994896)45.255489, 9.06385, -5.53743
9given(1), (1), (1)
10given(0.999855, -0.016904, 0.001888), (0.016941, 0.999622, -0.021675), (-0.001521, 0.021704, 0.999763)-4.45758, 48.09798, 0.01741
11given(0.997222, -0.06681, 0.032946), (0.068355, 0.996494, -0.048249), (-0.029607, 0.050367, 0.998292)39.96595, 52.433029, -0.81878
12given(0.997896, -0.05139, 0.03953), (0.052684, 0.998085, -0.032412), (-0.037788, 0.034427, 0.998693)46.17284, 4.28303, -2.8315
13given(1), (1), (1)
14given(0.999967, 0.008063, 0.001098), (-0.008035, 0.999686, -0.023753), (-0.001289, 0.023743, 0.999717)-4.50098, 49.2425, 0.16391
15given(0.995503, -0.088182, -0.034602), (0.085499, 0.993691, -0.072582), (0.040784, 0.069297, 0.996762)45.198009, 54.97332, -0.4925
16given(1), (1), (1)
17given(0.999966, -0.005321, 0.006286), (0.005415, 0.999874, -0.014952), (-0.006205, 0.014986, 0.999868)-4.93854, 47.802559, 0.21615
18given(0.995847, -0.082102, 0.039345), (0.084535, 0.994314, -0.064759), (-0.033805, 0.067816, 0.997125)39.376308, 53.749729, -0.66612
19given(0.998974, -0.005894, 0.044901), (0.007739, 0.999128, -0.041024), (-0.04462, 0.041329, 0.998149)43.244862, 4.12761, -3.18303

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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 (E. coli) / Strain (production host): BL21(DE3) / 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 (E. coli) / Strain (production host): BL21(DE3) / 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 (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P40337
#4: Chemical
ChemComp-9BW / (2~{S},4~{R})-1-[(2~{S})-2-(cyclopropylcarbonylamino)-3,3-dimethyl-butanoyl]-~{N}-[[4-(4-methyl-1,3-thiazol-5-yl)phenyl]methyl]-4-oxidanyl-pyrrolidine-2-carboxamide


Mass: 498.638 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C26H34N4O4S
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 919 / 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: 2.44 Å3/Da / Density % sol: 49.55 % / Mosaicity: 0.04 °
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: 0.9174 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Nov 24, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9174 Å / Relative weight: 1
ReflectionResolution: 2.2→48.93 Å / Num. obs: 82957 / % possible obs: 99.8 % / Redundancy: 6.7 % / CC1/2: 0.997 / Rmerge(I) obs: 0.141 / Rpim(I) all: 0.058 / Rrim(I) all: 0.153 / Net I/σ(I): 8.6
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Rpim(I) allRrim(I) all% possible all
2.2-2.247.10.8570.8370.3420.924100
11.43-48.935.70.0540.9980.0250.0698.9

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Processing

Software
NameVersionClassification
Aimless0.3.11data scaling
REFMAC5.8.0073refinement
PDB_EXTRACT3.22data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1VCB

1vcb


Resolution: 2.2→48.93 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.925 / SU B: 11.968 / SU ML: 0.164 / SU R Cruickshank DPI: 0.2718 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.272 / ESU R Free: 0.215
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : WITH TLS ADDED
RfactorNum. reflection% reflectionSelection details
Rfree0.2489 4192 5.1 %RANDOM
Rwork0.2007 ---
obs0.2032 78650 99.74 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso max: 120.73 Å2 / Biso mean: 36.545 Å2 / Biso min: 12.74 Å2
Baniso -1Baniso -2Baniso -3
1--0.04 Å2-0 Å2-0 Å2
2---0.04 Å20 Å2
3---0.09 Å2
Refinement stepCycle: final / Resolution: 2.2→48.93 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10616 0 140 919 11675
Biso mean--24.57 36.72 -
Num. residues----1338
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.01911006
X-RAY DIFFRACTIONr_bond_other_d0.0010.0210530
X-RAY DIFFRACTIONr_angle_refined_deg1.2922.00114972
X-RAY DIFFRACTIONr_angle_other_deg0.7553.00424208
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.04651322
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.05223.32485
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.972151806
X-RAY DIFFRACTIONr_dihedral_angle_4_deg19.1211589
X-RAY DIFFRACTIONr_chiral_restr0.0680.21709
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.02112168
X-RAY DIFFRACTIONr_gen_planes_other0.0010.022445
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A1584MEDIUM POSITIONAL0.270.5
12D1584MEDIUM POSITIONAL0.220.5
13G1584MEDIUM POSITIONAL0.280.5
14J1584MEDIUM POSITIONAL0.330.5
11A1584MEDIUM THERMAL3.142
12D1584MEDIUM THERMAL3.992
13G1584MEDIUM THERMAL3.62
14J1584MEDIUM THERMAL4.452
21B1358MEDIUM POSITIONAL0.350.5
22E1358MEDIUM POSITIONAL0.390.5
23H1358MEDIUM POSITIONAL0.420.5
24K1358MEDIUM POSITIONAL0.410.5
21B1358MEDIUM THERMAL5.842
22E1358MEDIUM THERMAL4.022
23H1358MEDIUM THERMAL5.842
24K1358MEDIUM THERMAL5.062
31C1690MEDIUM POSITIONAL0.360.5
32F1690MEDIUM POSITIONAL0.40.5
33I1690MEDIUM POSITIONAL0.330.5
34L1690MEDIUM POSITIONAL0.430.5
31C1690MEDIUM THERMAL3.252
32F1690MEDIUM THERMAL3.142
33I1690MEDIUM THERMAL3.232
34L1690MEDIUM THERMAL3.582
41C238MEDIUM POSITIONAL0.30.5
42F238MEDIUM POSITIONAL0.250.5
43I238MEDIUM POSITIONAL0.50.5
41C238MEDIUM THERMAL5.142
42F238MEDIUM THERMAL1.992
43I238MEDIUM THERMAL4.752
51C228MEDIUM POSITIONAL0.450.5
52F228MEDIUM POSITIONAL0.410.5
53I228MEDIUM POSITIONAL0.520.5
54L228MEDIUM POSITIONAL0.560.5
51C228MEDIUM THERMAL5.212
52F228MEDIUM THERMAL6.092
53I228MEDIUM THERMAL7.032
54L228MEDIUM THERMAL5.112
LS refinement shellResolution: 2.2→2.257 Å / Rfactor Rfree error: 0 / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.308 307 -
Rwork0.249 5687 -
all-5994 -
obs--99.85 %
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)
11.6879-1.04260.99773.1674-1.70512.72590.02920.23540.0558-0.3706-0.2071-0.17190.09120.30560.17790.09930.03070.02590.12320.03010.016544.71464.80647.6
22.9647-0.27690.23661.4063-1.02452.5472-0.1174-0.1760.05630.0437-0.0108-0.1723-0.06650.01140.12820.03060.0320.00080.15240.02750.026848.32561.13165.186
34.2711-0.6902-1.92491.12740.5481.51170.0275-0.09050.03290.0986-0.0283-0.07010.04550.06750.00080.0653-0.05-0.02180.22560.07010.026127.31654.33182.344
42.5628-0.89872.65632.0273-1.21775.3685-0.11080.7980.1934-0.2138-0.0841-0.0034-0.50461.32140.19490.1684-0.1391-0.00450.49290.04830.025948.2718.07447.317
54.12820.29391.91260.2484-0.54123.757-0.13190.58030.01070.08430.0093-0.0417-0.19050.51230.12260.1058-0.03220.00650.3139-0.00760.026252.814.08865.121
64.6307-0.7257-1.11541.26680.5131.83830.0128-0.0606-0.04260.0910.025-0.1046-0.0155-0.0637-0.03780.0594-0.0179-0.00880.14660.03810.022331.7917.7582.037
73.3771-1.20230.58161.7464-0.85472.35780.01210.29350.2373-0.0777-0.05270.0422-0.18590.19790.04070.116-0.01390.0130.26290.05790.04173.13412.98347.459
85.24160.2058-0.05571.5811-0.66951.8542-0.1815-0.73290.24270.10950.04690.0124-0.20840.2640.13450.12520.0120.00590.4518-0.00250.0326.76910.83565.243
92.2437-0.4448-1.51431.157-0.00312.9272-0.0821-0.3370.02150.0146-0.07260.01710.02490.56690.15460.0497-0.0053-0.00690.37330.03330.0181-14.4736.78982.326
102.4215-0.7972-0.47152.3753-0.59492.24270.0420.1134-0.0348-0.1272-0.09320.0793-0.03570.1280.05130.1093-0.0168-0.00970.1220.01720.0075-0.88760.62347.726
112.1508-0.3807-0.07550.6597-0.66771.8138-0.0951-0.18430.0050.1063-0.013-0.0071-0.05940.23230.10810.0862-0.00370.00620.23230.04630.01512.12658.50665.494
122.7084-0.2303-1.44991.09240.01622.9689-0.0974-0.2930.0857-0.0196-0.00980.00590.03420.30540.10710.0385-0.0059-0.01760.21740.0550.0326-19.06653.9682.603
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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