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- PDB-5hyn: Structure of Human Polycomb Repressive Complex 2 (PRC2) with onco... -

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Basic information

Entry
Database: PDB / ID: 5hyn
TitleStructure of Human Polycomb Repressive Complex 2 (PRC2) with oncogenic histone H3K27M peptide
Components
  • (Polycomb protein ...) x 2
  • H3K27M
  • Histone-lysine N-methyltransferase EZH2
  • JARID2 K116me3
KeywordsTRANSFERASE / chromatin modification complex
Function / homology
Function and homology information


protein localization to pericentric heterochromatin / hepatocyte homeostasis / cellular response to trichostatin A / regulation of gliogenesis / negative regulation of striated muscle cell differentiation / regulation of kidney development / [histone H3]-lysine27 N-trimethyltransferase / response to tetrachloromethane / negative regulation of keratinocyte differentiation / histone H3K27 trimethyltransferase activity ...protein localization to pericentric heterochromatin / hepatocyte homeostasis / cellular response to trichostatin A / regulation of gliogenesis / negative regulation of striated muscle cell differentiation / regulation of kidney development / [histone H3]-lysine27 N-trimethyltransferase / response to tetrachloromethane / negative regulation of keratinocyte differentiation / histone H3K27 trimethyltransferase activity / negative regulation of retinoic acid receptor signaling pathway / cerebellar cortex development / primary miRNA binding / random inactivation of X chromosome / regulation of adaxial/abaxial pattern formation / skeletal muscle satellite cell maintenance involved in skeletal muscle regeneration / regulatory ncRNA-mediated heterochromatin formation / negative regulation of cardiac muscle cell proliferation / histone H3K27 methyltransferase activity / sex chromatin / ubiquitin-modified histone reader activity / positive regulation of cell cycle G1/S phase transition / facultative heterochromatin formation / genomic imprinting / ESC/E(Z) complex / negative regulation of stem cell differentiation / RSC-type complex / protein-lysine N-methyltransferase activity / cardiac muscle hypertrophy in response to stress / chromatin silencing complex / histone H3K9me2/3 reader activity / pronucleus / positive regulation of dendrite development / G1 to G0 transition / histone H3 methyltransferase activity / histone methyltransferase activity / DNA methylation-dependent constitutive heterochromatin formation / negative regulation of G1/S transition of mitotic cell cycle / spinal cord development / lncRNA binding / negative regulation of gene expression, epigenetic / synaptic transmission, GABAergic / Transcriptional Regulation by E2F6 / : / positive regulation of MAP kinase activity / histone methyltransferase complex / oligodendrocyte differentiation / negative regulation of transcription elongation by RNA polymerase II / positive regulation of GTPase activity / positive regulation of protein serine/threonine kinase activity / negative regulation of cell differentiation / cardiac muscle cell proliferation / positive regulation of epithelial to mesenchymal transition / ribonucleoprotein complex binding / subtelomeric heterochromatin formation / pericentric heterochromatin / RNA polymerase II core promoter sequence-specific DNA binding / nucleosome binding / keratinocyte differentiation / Chromatin modifying enzymes / spleen development / protein localization to chromatin / liver regeneration / negative regulation of cytokine production involved in inflammatory response / telomere organization / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / thymus development / cellular response to leukemia inhibitory factor / central nervous system development / DNA methylation / B cell differentiation / epigenetic regulation of gene expression / Condensation of Prophase Chromosomes / ubiquitin binding / Chromatin modifications during the maternal to zygotic transition (MZT) / SIRT1 negatively regulates rRNA expression / Regulation of PTEN gene transcription / HCMV Late Events / transcription corepressor binding / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / hippocampus development / stem cell differentiation / HDACs deacetylate histones / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / promoter-specific chromatin binding / RNA Polymerase I Promoter Escape / enzyme activator activity / liver development / Transcriptional regulation by small RNAs / G1/S transition of mitotic cell cycle / Formation of the beta-catenin:TCF transactivating complex / protein-DNA complex / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3
Similarity search - Function
Polycomb protein SUZ12-like, Zn domain / EZH2, SET domain / Polycomb protein, VEFS-Box / VEFS-Box of polycomb protein / Histone-lysine N-methyltransferase EZH1/EZH2 / Polycomb repressive complex 2 subunit EZH1/EZH2, tri-helical domain / Pre-SET CXC domain / : / WD repeat binding protein EZH2 / Polycomb repressive complex 2 tri-helical domain ...Polycomb protein SUZ12-like, Zn domain / EZH2, SET domain / Polycomb protein, VEFS-Box / VEFS-Box of polycomb protein / Histone-lysine N-methyltransferase EZH1/EZH2 / Polycomb repressive complex 2 subunit EZH1/EZH2, tri-helical domain / Pre-SET CXC domain / : / WD repeat binding protein EZH2 / Polycomb repressive complex 2 tri-helical domain / CXC domain / Ezh2, MCSS domain / Tesmin/TSO1-like CXC domain / Tesmin/TSO1-like CXC domain / CXC domain / Histone-lysine N-methyltransferase EZH1/2-like / CXC domain profile. / : / Zinc finger, C5HC2-type / C5HC2 zinc finger / ARID DNA-binding domain / ARID DNA-binding domain superfamily / ARID/BRIGHT DNA binding domain / ARID domain profile. / BRIGHT, ARID (A/T-rich interaction domain) domain / ARID/BRIGHT DNA binding domain / JmjN domain / jmjN domain / JmjN domain profile. / Small domain found in the jumonji family of transcription factors / SET (Su(var)3-9, Enhancer-of-zeste, Trithorax) domain / JmjC domain, hydroxylase / SET domain / SET domain superfamily / SET domain profile. / SET domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / A domain family that is part of the cupin metalloenzyme superfamily. / JmjC domain / JmjC domain profile. / SANT/Myb domain / Zinc finger C2H2 type domain signature. / YVTN repeat-like/Quinoprotein amine dehydrogenase / 7 Propeller / Methylamine Dehydrogenase; Chain H / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 domain / Histone-fold / WD domain, G-beta repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40 repeats / WD40 repeat / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily / Mainly Beta
Similarity search - Domain/homology
S-ADENOSYL-L-HOMOCYSTEINE / Polycomb protein EED / Histone H3.1 / Polycomb protein SUZ12 / Histone-lysine N-methyltransferase EZH2 / Protein Jumonji
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.95 Å
AuthorsZhang, Y. / Justin, N. / Wilson, J.R. / Gamblin, S.J.
Funding support United Kingdom, 1items
OrganizationGrant numberCountry
Francis Crick Institute10078 United Kingdom
CitationJournal: Nat Commun / Year: 2016
Title: Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2.
Authors: Justin, N. / Zhang, Y. / Tarricone, C. / Martin, S.R. / Chen, S. / Underwood, E. / De Marco, V. / Haire, L.F. / Walker, P.A. / Reinberg, D. / Wilson, J.R. / Gamblin, S.J.
History
DepositionFeb 1, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0May 11, 2016Provider: repository / Type: Initial release
Revision 1.1Apr 9, 2025Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / struct_conn_type
Item: _chem_comp.mon_nstd_flag / _chem_comp.type ..._chem_comp.mon_nstd_flag / _chem_comp.type / _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_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _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 / _struct_conn.ptnr2_label_seq_id / _struct_conn_type.id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Histone-lysine N-methyltransferase EZH2
B: Polycomb protein EED
C: Polycomb protein SUZ12
D: H3K27M
E: JARID2 K116me3
F: Histone-lysine N-methyltransferase EZH2
G: Polycomb protein EED
H: Polycomb protein SUZ12
I: H3K27M
J: JARID2 K116me3
K: Histone-lysine N-methyltransferase EZH2
L: Polycomb protein EED
M: Polycomb protein SUZ12
O: H3K27M
P: JARID2 K116me3
Q: Histone-lysine N-methyltransferase EZH2
R: Polycomb protein EED
S: Polycomb protein SUZ12
T: H3K27M
U: JARID2 K116me3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)586,81556
Polymers583,18420
Non-polymers3,63136
Water00
1
A: Histone-lysine N-methyltransferase EZH2
B: Polycomb protein EED
C: Polycomb protein SUZ12
D: H3K27M
E: JARID2 K116me3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,70414
Polymers145,7965
Non-polymers9089
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
F: Histone-lysine N-methyltransferase EZH2
G: Polycomb protein EED
H: Polycomb protein SUZ12
I: H3K27M
J: JARID2 K116me3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,70414
Polymers145,7965
Non-polymers9089
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
K: Histone-lysine N-methyltransferase EZH2
L: Polycomb protein EED
M: Polycomb protein SUZ12
O: H3K27M
P: JARID2 K116me3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,70414
Polymers145,7965
Non-polymers9089
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
Q: Histone-lysine N-methyltransferase EZH2
R: Polycomb protein EED
S: Polycomb protein SUZ12
T: H3K27M
U: JARID2 K116me3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,70414
Polymers145,7965
Non-polymers9089
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
A: Histone-lysine N-methyltransferase EZH2
B: Polycomb protein EED
C: Polycomb protein SUZ12
D: H3K27M
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,19813
Polymers144,2904
Non-polymers9089
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16660 Å2
ΔGint-106 kcal/mol
Surface area50120 Å2
MethodPISA
6
F: Histone-lysine N-methyltransferase EZH2
G: Polycomb protein EED
H: Polycomb protein SUZ12
I: H3K27M
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,19813
Polymers144,2904
Non-polymers9089
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16980 Å2
ΔGint-107 kcal/mol
Surface area48710 Å2
MethodPISA
7
K: Histone-lysine N-methyltransferase EZH2
L: Polycomb protein EED
M: Polycomb protein SUZ12
O: H3K27M
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,19813
Polymers144,2904
Non-polymers9089
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16530 Å2
ΔGint-74 kcal/mol
Surface area48620 Å2
MethodPISA
8
Q: Histone-lysine N-methyltransferase EZH2
R: Polycomb protein EED
S: Polycomb protein SUZ12
T: H3K27M
hetero molecules


Theoretical massNumber of molelcules
Total (without water)145,19813
Polymers144,2904
Non-polymers9089
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16660 Å2
ΔGint-107 kcal/mol
Surface area48680 Å2
MethodPISA
Unit cell
Length a, b, c (Å)131.640, 171.510, 274.550
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 1 types, 4 molecules AFKQ

#1: Protein
Histone-lysine N-methyltransferase EZH2 / ENX-1 / Enhancer of zeste homolog 2 / Lysine N-methyltransferase 6


Mass: 85492.297 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EZH2, KMT6 / Production host: Escherichia coli (E. coli)
References: UniProt: Q15910, histone-lysine N-methyltransferase

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Polycomb protein ... , 2 types, 8 molecules BGLRCHMS

#2: Protein
Polycomb protein EED / hEED / WD protein associating with integrin cytoplasmic tails 1 / WAIT-1


Mass: 42314.145 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EED / Production host: Escherichia coli (E. coli) / References: UniProt: O75530
#3: Protein
Polycomb protein SUZ12 / Chromatin precipitated E2F target 9 protein / ChET 9 protein / Joined to JAZF1 protein / Suppressor ...Chromatin precipitated E2F target 9 protein / ChET 9 protein / Joined to JAZF1 protein / Suppressor of zeste 12 protein homolog


Mass: 15249.510 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SUZ12, CHET9, JJAZ1, KIAA0160 / Production host: Escherichia coli (E. coli) / References: UniProt: Q15022

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Protein/peptide , 2 types, 8 molecules DIOTEJPU

#4: Protein/peptide
H3K27M


Mass: 1234.426 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P68431*PLUS
#5: Protein/peptide
JARID2 K116me3


Mass: 1505.743 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: Q92833*PLUS

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Non-polymers , 2 types, 36 molecules

#6: Chemical...
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 32 / Source method: obtained synthetically / Formula: Zn
#7: Chemical
ChemComp-SAH / S-ADENOSYL-L-HOMOCYSTEINE


Mass: 384.411 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C14H20N6O5S

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Details

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: 2.82 Å3/Da / Density % sol: 56.33 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 6.5 / Details: 25% PEG3350, 400mM Ammonian Citrate pH6.5 / PH range: 6.5-6.8

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.9763 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Oct 8, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9763 Å / Relative weight: 1
ReflectionResolution: 2.94→104.43 Å / Num. obs: 132394 / % possible obs: 99.9 % / Redundancy: 5.6 % / CC1/2: 0.996 / Rmerge(I) obs: 0.165 / Net I/σ(I): 9.9
Reflection shellResolution: 2.94→3.02 Å / Redundancy: 5.6 % / Rmerge(I) obs: 1.607 / Mean I/σ(I) obs: 1.4 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
XDSdata reduction
xia2data scaling
PHASERphasing
RefinementMethod to determine structure: SAD / Resolution: 2.95→95.013 Å / SU ML: 0.5 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 32.32
RfactorNum. reflection% reflection
Rfree0.2733 6476 4.95 %
Rwork0.2191 --
obs0.2218 130834 99.75 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.95→95.013 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms34892 0 136 0 35028
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01335790
X-RAY DIFFRACTIONf_angle_d1.52348294
X-RAY DIFFRACTIONf_dihedral_angle_d15.89521664
X-RAY DIFFRACTIONf_chiral_restr0.0745135
X-RAY DIFFRACTIONf_plane_restr0.016253
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.95-2.98350.43252240.36714100X-RAY DIFFRACTION100
2.9835-3.01860.39362140.35514082X-RAY DIFFRACTION100
3.0186-3.05540.43562120.3314128X-RAY DIFFRACTION100
3.0554-3.09410.3912370.32474061X-RAY DIFFRACTION100
3.0941-3.13480.3922090.324119X-RAY DIFFRACTION100
3.1348-3.17780.38332180.29974087X-RAY DIFFRACTION100
3.1778-3.22320.36642170.30234091X-RAY DIFFRACTION100
3.2232-3.27130.38421930.34136X-RAY DIFFRACTION100
3.2713-3.32240.37632390.29544084X-RAY DIFFRACTION100
3.3224-3.37690.33932140.28144148X-RAY DIFFRACTION100
3.3769-3.43510.32142200.25784092X-RAY DIFFRACTION100
3.4351-3.49760.30191840.24934167X-RAY DIFFRACTION100
3.4976-3.56490.30992020.24444111X-RAY DIFFRACTION100
3.5649-3.63760.28262030.23174136X-RAY DIFFRACTION100
3.6376-3.71670.27652300.22374112X-RAY DIFFRACTION100
3.7167-3.80320.28781880.2174122X-RAY DIFFRACTION100
3.8032-3.89830.27372140.21364141X-RAY DIFFRACTION100
3.8983-4.00370.27282180.19894148X-RAY DIFFRACTION100
4.0037-4.12150.25542020.20364131X-RAY DIFFRACTION100
4.1215-4.25460.26262090.19084158X-RAY DIFFRACTION100
4.2546-4.40660.24122340.17894122X-RAY DIFFRACTION100
4.4066-4.5830.2282190.1734148X-RAY DIFFRACTION100
4.583-4.79160.23551970.16514171X-RAY DIFFRACTION100
4.7916-5.04420.21052360.16924142X-RAY DIFFRACTION100
5.0442-5.36020.2312180.184167X-RAY DIFFRACTION100
5.3602-5.77410.26592000.18984207X-RAY DIFFRACTION100
5.7741-6.3550.25142380.20214194X-RAY DIFFRACTION100
6.355-7.27430.2622070.21644240X-RAY DIFFRACTION100
7.2743-9.16370.22872250.19414258X-RAY DIFFRACTION100
9.1637-95.06250.22652550.21064355X-RAY DIFFRACTION98
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)
10.3331-0.25350.10070.30360.48740.33750.0387-0.2570.0947-0.1479-0.0095-0.01770.1086-0.1322-00.2763-0.03810.02610.47050.00310.427570.3478-71.216815.2517
20.0791-0.0265-0.03390.4132-0.23670.12930.01730.21660.0464-0.02910.00460.01460.09460.121300.38290.0151-0.00970.47820.04880.442344.08-70.474-34.0922
3-0.0684-0.0350.03780.19970.23120.472-0.01060.0585-0.02790.05840.0746-0.02510.05250.0429-00.3120.0204-0.00650.2972-0.00520.322373.596-96.7503-15.4972
40.3559-0.07330.4910.48410.1960.78210.0375-0.26480.11060.1199-0.10910.01990.1115-0.297200.4031-0.06250.00590.659-0.03110.380164.064-81.514426.277
50.1143-0.16150.00460.2384-0.19050.0665-0.0085-0.2725-0.07980.05380.088-0.01050.0488-0.347-00.3294-0.01980.00590.51380.0390.389847.7266-82.1232-18.1243
60.6339-0.12010.39390.699-0.31190.4823-0.09720.27740.20250.2813-0.06060.06250.07050.1093-00.3041-0.0906-0.0320.63-0.04140.4264-6.3164-70.5034-24.8669
7-0.00290.1882-0.10530.14280.09990.2191-0.09610.0672-0.02130.04340.14320.021-0.14920.1356-00.3813-0.1155-0.04710.6566-0.08250.408319.3443-68.704525.0938
80.0003-0.2014-0.07270.63440.06260.53210.0155-0.0769-0.0363-0.064-0.0073-0.00360.03760.071200.2728-0.03020.02750.2692-0.0090.3087-7.9053-96.20465.7928
90.4932-0.28330.28240.554-0.20420.64730.02590.4820.08510.0266-0.1323-0.02040.05140.3985-00.2776-0.037-0.02160.75120.02040.36320.5978-79.0863-35.5123
100.12060.1009-0.06540.16360.21880.13890.00680.216-0.0116-0.108-0.01340.04680.02450.712300.3926-0.07070.01280.91480.0080.456316.8405-80.14528.9425
110.47590.32970.10490.60640.4801-0.0389-0.21590.0478-0.1239-0.125-0.0792-0.0144-0.04090.5922-00.3143-0.1485-0.05120.1126-0.03170.2699103.3211-56.3825-61.4357
120.02880.0587-0.1836-0.0014-0.01090.19950.17810.2507-0.0123-0.1263-0.1030.21650.0740.557700.7117-0.124-0.0340.53890.2160.643396.0527-32.316-111.5367
130.39070.6403-0.10520.34480.23410.63240.1123-0.02830.0935-0.0067-0.06780.01030.05260.020600.29750.0463-0.04850.2459-0.02440.327179.8932-67.1571-92.3491
140.57170.05240.54190.4818-0.17950.3581-0.0768-0.28410.0282-0.068-0.05460.0382-0.0860.1652-00.3617-0.0719-0.04130.2062-0.06510.397892.7342-53.0488-50.7854
150.0028-0.0371-0.07780.15710.07310.09490.15880.1754-0.0020.1583-0.1610.0255-0.14370.1283-00.5597-0.01730.02480.38860.04870.583486.1284-38.592-95.2085
160.50660.1596-0.01150.94570.04780.00670.01290.0680.02530.0030.01380.2409-0.1422-0.1488-00.309-0.01180.02490.30060.0510.283327.1678-28.5682-51.9793
17-0.0197-0.0440.0856-0.06650.03480.09370.60822.13332.2425-0.2974-0.3036-0.1678-0.0196-0.699700.7278-0.9657-0.7044-0.9873-1.9923-2.329234.8717-52.9628-101.5491
180.0360.127-0.43110.2755-0.43140.49960.08210.069-0.0104-0.02970.0166-0.0147-0.1315-0.121100.3221-0.0423-0.00770.36970.03980.309551.3675-17.8945-82.0975
190.4850.0071-0.15790.40380.25210.64530.0013-0.2316-0.0205-0.06190.0501-0.04880.0392-0.3057-00.3445-0.0496-0.00420.14980.01230.310636.8466-31.9049-41.3466
200.08730.06390.07480.08490.06570.0401-0.2085-0.22120.1449-0.0989-0.1476-0.08560.4307-0.2314-00.7563-0.3990.07460.1308-0.05920.484544.3777-46.8397-85.2903
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain A and resid 10:246)
2X-RAY DIFFRACTION2(chain A and resid 262:476)
3X-RAY DIFFRACTION3(chain A and resid 522:750)
4X-RAY DIFFRACTION4(chain B and resid 77:438)
5X-RAY DIFFRACTION5(chain C and resid 589:684)
6X-RAY DIFFRACTION6(chain F and resid 10:246)
7X-RAY DIFFRACTION7(chain F and resid 262:476)
8X-RAY DIFFRACTION8(chain F and resid 522:750)
9X-RAY DIFFRACTION9(chain G and resid 77:438)
10X-RAY DIFFRACTION10(chain H and resid 589:684)
11X-RAY DIFFRACTION11(chain K and resid 10:246)
12X-RAY DIFFRACTION12(chain K and resid 262:476)
13X-RAY DIFFRACTION13(chain K and resid 522:750)
14X-RAY DIFFRACTION14(chain L and resid 77:438)
15X-RAY DIFFRACTION15(chain M and resid 589:684)
16X-RAY DIFFRACTION16(chain Q and resid 10:246)
17X-RAY DIFFRACTION17(chain Q and resid 262:476)
18X-RAY DIFFRACTION18(chain Q and resid 522:750)
19X-RAY DIFFRACTION19(chain R and resid 77:438)
20X-RAY DIFFRACTION20(chain S and resid 589:684)

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