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- PDB-5d6y: Crystal structure of double tudor domain of human lysine demethyl... -

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Basic information

Entry
Database: PDB / ID: 5d6y
TitleCrystal structure of double tudor domain of human lysine demethylase KDM4A complexed with histone H3K23me3
Components
  • Lysine-specific demethylase 4A
  • peptide H3K23me3 (19-28)
KeywordsOXIDOREDUCTASE / double tudor domain / reader domain / Structural Genomics / PSI-2 / Protein Structure Initiative / Enzyme Discovery for Natural Product Biosynthesis / NatPro
Function / homology
Function and homology information


[histone H3]-trimethyl-L-lysine36 demethylase / histone H3K36me2/H3K36me3 demethylase activity / apoptotic chromosome condensation / histone H4K20me2 reader activity / histone H3K36 demethylase activity / cardiac muscle hypertrophy in response to stress / [histone H3]-trimethyl-L-lysine9 demethylase / histone H3K9me2/H3K9me3 demethylase activity / histone H3K9 demethylase activity / negative regulation of astrocyte differentiation ...[histone H3]-trimethyl-L-lysine36 demethylase / histone H3K36me2/H3K36me3 demethylase activity / apoptotic chromosome condensation / histone H4K20me2 reader activity / histone H3K36 demethylase activity / cardiac muscle hypertrophy in response to stress / [histone H3]-trimethyl-L-lysine9 demethylase / histone H3K9me2/H3K9me3 demethylase activity / histone H3K9 demethylase activity / negative regulation of astrocyte differentiation / histone demethylase activity / pericentric heterochromatin / Chromatin modifying enzymes / NR1H3 & NR1H2 regulate gene expression linked to cholesterol transport and efflux / telomere organization / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / positive regulation of neuron differentiation / negative regulation of autophagy / Assembly of the ORC complex at the origin of replication / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA methylation / Condensation of Prophase Chromosomes / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / SIRT1 negatively regulates rRNA expression / epigenetic regulation of gene expression / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / response to nutrient levels / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / HDMs demethylate histones / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / PKMTs methylate histone lysines / Meiotic recombination / Pre-NOTCH Transcription and Translation / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / fibrillar center / Transcriptional regulation of granulopoiesis / HCMV Early Events / structural constituent of chromatin / nucleosome / nucleosome assembly / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromatin organization / HATs acetylate histones / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / regulation of gene expression / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / gene expression / Estrogen-dependent gene expression / cadherin binding / chromatin remodeling / Amyloid fiber formation / protein heterodimerization activity / negative regulation of gene expression / negative regulation of DNA-templated transcription / ubiquitin protein ligase binding / positive regulation of gene expression / chromatin / protein-containing complex / DNA binding / extracellular exosome / extracellular region / zinc ion binding / nucleoplasm / nucleus / membrane / cytosol
Similarity search - Function
Vcp-like ATPase; Chain A, domain 2 - #70 / : / : / : / Vcp-like ATPase; Chain A, domain 2 / Lysine-specific demethylase 4, Tudor domain / Jumonji domain-containing protein 2A Tudor domain / Tudor domain / Tudor domain / SH3 type barrels. - #140 ...Vcp-like ATPase; Chain A, domain 2 - #70 / : / : / : / Vcp-like ATPase; Chain A, domain 2 / Lysine-specific demethylase 4, Tudor domain / Jumonji domain-containing protein 2A Tudor domain / Tudor domain / Tudor domain / SH3 type barrels. - #140 / PHD-finger / PHD-zinc-finger like domain / JmjN domain / jmjN domain / JmjN domain profile. / Small domain found in the jumonji family of transcription factors / Extended PHD (ePHD) domain / Extended PHD (ePHD) domain profile. / JmjC domain, hydroxylase / A domain family that is part of the cupin metalloenzyme superfamily. / JmjC domain / JmjC domain profile. / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Zinc finger, FYVE/PHD-type / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / SH3 type barrels. / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Zinc finger, RING/FYVE/PHD-type / Roll / Roll / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Lysine-specific demethylase 4A / Histone H3.1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.287 Å
AuthorsWang, F. / Su, Z. / Miller, M.D. / Denu, J.M. / Phillips Jr., G.N. / Enzyme Discovery for Natural Product Biosynthesis (NatPro)
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)U01GM098248 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)2R37GM059785-15/P250VA United States
CitationJournal: Nat Commun / Year: 2016
Title: Reader domain specificity and lysine demethylase-4 family function.
Authors: Su, Z. / Wang, F. / Lee, J.H. / Stephens, K.E. / Papazyan, R. / Voronina, E. / Krautkramer, K.A. / Raman, A. / Thorpe, J.J. / Boersma, M.D. / Kuznetsov, V.I. / Miller, M.D. / Taverna, S.D. / ...Authors: Su, Z. / Wang, F. / Lee, J.H. / Stephens, K.E. / Papazyan, R. / Voronina, E. / Krautkramer, K.A. / Raman, A. / Thorpe, J.J. / Boersma, M.D. / Kuznetsov, V.I. / Miller, M.D. / Taverna, S.D. / Phillips, G.N. / Denu, J.M.
History
DepositionAug 13, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 10, 2016Provider: repository / Type: Initial release
Revision 1.1Dec 7, 2016Group: 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 1.4Apr 2, 2025Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / struct_ncs_dom_lim
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Lysine-specific demethylase 4A
a: peptide H3K23me3 (19-28)
B: Lysine-specific demethylase 4A
b: peptide H3K23me3 (19-28)
C: Lysine-specific demethylase 4A
c: peptide H3K23me3 (19-28)
D: Lysine-specific demethylase 4A
d: peptide H3K23me3 (19-28)
E: Lysine-specific demethylase 4A
F: Lysine-specific demethylase 4A


Theoretical massNumber of molelcules
Total (without water)86,83610
Polymers86,83610
Non-polymers00
Water3,891216
1
A: Lysine-specific demethylase 4A
a: peptide H3K23me3 (19-28)


Theoretical massNumber of molelcules
Total (without water)14,8452
Polymers14,8452
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Lysine-specific demethylase 4A
b: peptide H3K23me3 (19-28)


Theoretical massNumber of molelcules
Total (without water)14,8452
Polymers14,8452
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Lysine-specific demethylase 4A
c: peptide H3K23me3 (19-28)


Theoretical massNumber of molelcules
Total (without water)14,8452
Polymers14,8452
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Lysine-specific demethylase 4A
d: peptide H3K23me3 (19-28)


Theoretical massNumber of molelcules
Total (without water)14,8452
Polymers14,8452
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
E: Lysine-specific demethylase 4A


Theoretical massNumber of molelcules
Total (without water)13,7271
Polymers13,7271
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
F: Lysine-specific demethylase 4A


Theoretical massNumber of molelcules
Total (without water)13,7271
Polymers13,7271
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)106.159, 106.159, 79.206
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number145
Space group name H-MP32
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11chain A
21chain B
31chain C
41chain D
51chain E
61chain F
12chain a
22chain b
13chain c
23chain d

NCS domain segments:

Component-ID: 1

Dom-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11SERSERTHRTHRchain AAA898 - 10058 - 115
21SERSERTHRTHRchain BBC898 - 10058 - 115
31SERSERVALVALchain CCE898 - 10038 - 113
41SERSERVALVALchain DDG898 - 10038 - 113
51SERSERTHRTHRchain EEI898 - 10058 - 115
61SERSERTHRTHRchain FFJ898 - 10058 - 115
12GLNGLNLYSLYSchain aaB19 - 271 - 9
22GLNGLNLYSLYSchain bbD19 - 271 - 9
13LEULEUARGARGchain ccF20 - 262 - 8
23LEULEUARGARGchain ddH20 - 262 - 8

NCS ensembles :
ID
1
2
3

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Components

#1: Protein
Lysine-specific demethylase 4A / JmjC domain-containing histone demethylation protein 3A / Jumonji domain-containing protein 2A


Mass: 13727.131 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KDM4A, JHDM3A, JMJD2, JMJD2A, KIAA0677 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)
References: UniProt: O75164, Oxidoreductases; Acting on paired donors, with incorporation or reduction of molecular oxygen; With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
#2: Protein/peptide
peptide H3K23me3 (19-28)


Mass: 1118.350 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P68431*PLUS
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 216 / 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: 2.97 Å3/Da / Density % sol: 58.55 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: Protein-peptide Solution (30mg/ml KDM4A DTD and 3.5mg/ml peptide in 20mM HEPES pH 7.5, 150mM NaCl and 0.5mM TCEP) mixed in a 1:1 ratio with the well solution (1.2M sodium phosphate ...Details: Protein-peptide Solution (30mg/ml KDM4A DTD and 3.5mg/ml peptide in 20mM HEPES pH 7.5, 150mM NaCl and 0.5mM TCEP) mixed in a 1:1 ratio with the well solution (1.2M sodium phosphate monobasic, 0.8M potassium phosphate dibasic, 0.1M CAPS/sodium hydroxide pH10.5, 0.2M lithium sulfate) Cryoprotected with additional 20% glycerol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-F / Wavelength: 0.979 Å
DetectorType: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Oct 23, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.979 Å / Relative weight: 1
ReflectionResolution: 2.287→50 Å / Num. obs: 82623 / % possible obs: 91.5 % / Observed criterion σ(I): -3 / Redundancy: 5.68 % / Biso Wilson estimate: 35.63 Å2 / Rmerge F obs: 0.993 / Rmerge(I) obs: 0.217 / Rrim(I) all: 0.239 / Χ2: 0.959 / Net I/σ(I): 9.15 / Num. measured all: 466605
Reflection shell

Diffraction-ID: 1 / Rejects: _

Resolution (Å)Highest resolution (Å)Rmerge F obsRmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsRrim(I) all% possible all
2.29-2.420.3351.7521.127002914476144231.9799.6
2.42-2.590.5921.3621.828056113754137531.496100
2.59-2.80.8160.7913.12493581270086990.87168.5
2.8-3.060.9220.4925.136890911720117190.54100
3.06-3.420.980.2589.155967510574102320.28396.8
3.42-3.940.9910.13415.2534507935661380.14765.6
3.94-4.80.9970.06924.246435788678850.076100
4.8-6.690.9970.0723.4236634622862280.077100
6.690.9990.04429.1520497359035460.04998.8

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHENIXrefinement
PDB_EXTRACT3.15data extraction
XDSdata reduction
PHENIXphasing
RefinementResolution: 2.287→28.581 Å / SU ML: 0.33 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 30.44 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2947 3668 4.45 %
Rwork0.2636 78808 -
obs0.265 82476 91.4 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 177.26 Å2 / Biso mean: 59.3756 Å2 / Biso min: 20.83 Å2
Refinement stepCycle: final / Resolution: 2.287→28.581 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5317 0 0 216 5533
Biso mean---48.3 -
Num. residues----671
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0115428
X-RAY DIFFRACTIONf_angle_d1.3917357
X-RAY DIFFRACTIONf_chiral_restr0.066796
X-RAY DIFFRACTIONf_plane_restr0.008964
X-RAY DIFFRACTIONf_dihedral_angle_d14.8911937
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3037X-RAY DIFFRACTION12.379TORSIONAL
12B3037X-RAY DIFFRACTION12.379TORSIONAL
13C3037X-RAY DIFFRACTION12.379TORSIONAL
14D3037X-RAY DIFFRACTION12.379TORSIONAL
15E3037X-RAY DIFFRACTION12.379TORSIONAL
16F3037X-RAY DIFFRACTION12.379TORSIONAL
21a64X-RAY DIFFRACTION12.379TORSIONAL
22b64X-RAY DIFFRACTION12.379TORSIONAL
31c38X-RAY DIFFRACTION12.379TORSIONAL
32d38X-RAY DIFFRACTION12.379TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 26

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.2867-2.31680.32561520.33713183333596
2.3168-2.34850.33961430.3253237338099
2.3485-2.38210.37121600.337233613521100
2.3821-2.41760.36971440.34233143458100
2.4176-2.45540.34691620.328933343496100
2.4554-2.49560.31051520.333532943446100
2.4956-2.53860.36351560.320633453501100
2.5386-2.58470.34261560.313932943450100
2.5847-2.63440.3631560.31813277343398
2.6344-2.68820.277820.2661192113
2.6882-2.74660.42391390.31592821296098
2.7466-2.81040.35231400.301533163456100
2.8104-2.88060.28941560.293833503506100
2.8806-2.95840.3121520.28433413493100
2.9584-3.04540.29231640.276832663430100
3.0454-3.14360.29231600.278332883448100
3.1436-3.25580.2871600.246532863446100
3.2558-3.38590.26111480.245133693517100
3.3859-3.53980.2661880.24041915200358
3.5398-3.7260.2996920.23822199229167
3.726-3.95890.31461120.24052425253773
3.9589-4.26360.2631600.217133703530100
4.2636-4.6910.22521480.216132793427100
4.691-5.36590.28631600.219132903450100
5.3659-6.74580.34841400.266533283468100
6.7458-28.5830.22261660.26433073473100
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)
13.29360.91632.28260.49710.18382.52171.1332-0.4754-0.6245-0.05950.34821.26210.6675-1.34260.05310.43-0.2854-0.13871.20310.15540.411134.1245-40.21869.5639
23.98360.90432.71344.44840.12772.51130.34790.2563-0.10310.3746-0.7389-0.42340.48020.0983-0.10140.5554-0.0216-0.1020.26970.11140.283745.0675-39.77027.5191
31.82831.71911.01164.8143-1.05083.244-0.3123-0.30421.02530.27990.03530.3175-0.3922-0.05380.07260.40790.01450.08470.52970.28580.650353.6832-35.82192.5093
42.01041.44322.52511.30650.01852.4584-0.0668-0.233-0.127-0.00290.072-0.1671-0.3266-0.36420.03340.18430.028-0.0050.37770.03970.280337.551-38.9596-3.8973
51.44771.01470.66732.3251.00110.8486-0.26090.426-0.3965-0.41270.2836-0.3017-0.12360.1371-0.0280.364-0.07180.10370.3101-0.03950.427235.27-40.6092-20.824
62.94641.13471.43452.86180.51832.74590.0895-0.0399-0.0942-0.6503-0.4728-0.31450.1316-0.86890.06390.3146-0.06730.16870.1590.00620.322724.4461-39.9983-20.7876
70.5310.26111.2541.93350.12452.0176-0.50910.18730.078-1.12180.4119-0.1239-0.48770.56180.06250.4997-0.19550.13780.4512-0.10910.354938.7244-37.8885-25.7889
82.69781.1931.39840.86030.06032.43760.12350.59350.1527-0.70940.75721.079-0.33130.3973-0.16940.4304-0.14330.19180.3386-0.07540.287634.8174-44.3839-25.3345
91.97921.90281.36370.88140.02482.50870.2819-0.7183-0.4819-0.0464-0.1064-0.23980.2492-0.63440.06850.15370.0021-0.03820.36530.05320.328835.9427-38.6504-1.9319
103.16380.35651.30252.3043-0.59753.22130.0106-0.1026-0.23280.20780.1286-0.09720.2665-0.52230.00690.3416-0.0292-0.05210.45150.08790.335743.0978-38.28613.097
114.8032-1.47260.07894.5854-0.11075.2705-0.20990.2611-0.44360.70670.0373-0.08760.69330.22290.18090.4071-0.00360.08470.3761-0.05490.605643.3555-45.8439-17.4646
122.27032.03771.11532.42032.17812.97930.23810.7370.2591-0.17211.2196-0.8181-0.99221.23960.10770.9748-0.7101-0.19120.7318-0.9019-1.639117.7424-49.6644-34.244
135.33950.71921.18543.32462.6122.0985-0.26140.4713-0.14460.65690.09550.1306-0.08130.0189-0.05770.34530.08530.01610.401-0.14330.318211.8997-58.9316-32.1602
144.5631-0.4296-0.16342.34771.52692.94170.03340.59191.1011-0.5533-0.32380.19110.0124-0.03360.08990.525-0.02330.16710.4363-0.13650.53834.1665-64.3966-27.1806
152.16521.54591.10911.18181.71452.0577-0.1090.0244-0.2851-0.18740.16260.0746-0.38370.19540.0650.3096-0.07160.02130.2551-00.300814.945-52.0041-20.7456
163.31240.18341.11011.37150.48870.93940.4383-0.5246-0.6563-0.1229-0.4138-0.4820.39080.1923-0.09530.2294-0.0595-0.00780.340.13280.476619.1235-56.237-5.1868
171.69170.60871.38970.78051.04492.50030.1192-0.5543-0.14190.495-0.12320.35980.07640.02370.17650.26170.0040.04470.3780.07820.322115.5458-44.0065-2.0809
183.5090.89091.07612.09391.04032.8666-0.230.1363-0.1450.1244-0.0458-0.1369-0.17240.09940.10720.2295-0.02980.0350.35210.13080.261322.4111-41.1682-3.8334
191.4012-0.38670.60420.47780.79011.5439-0.5157-1.1534-0.4377-0.05780.1986-0.02590.5128-0.38290.09740.2787-0.0516-0.01890.68360.16370.42113.4385-52.49551.1426
203.09041.65471.12980.77611.26011.8498-0.1369-0.1783-0.3554-0.16610.092-0.1179-0.20350.23530.04030.2713-0.04880.04790.2339-0.00520.29617.4142-51.1195-14.6162
212.66561.1416-0.01512.6391.62413.2389-0.19640.3836-0.4302-0.18010.2134-0.1894-0.43770.56550.03290.3896-0.05050.06150.3741-0.12760.301811.5587-56.4349-27.7217
224.0391-1.15191.24885.7931-0.20886.32560.17980.4196-0.29030.3007-0.6032-0.13160.50240.28160.37720.3494-0.016-0.04190.30490.06150.678318.0334-60.4604-7.1831
233.2910.8656-1.20824.0476-0.91724.5560.573-0.27060.21460.611-0.26930.1887-0.9270.62170.23320.6777-0.22980.15440.48790.00670.28671.9668-47.585912.7971
240.4343-0.186-2.03522.1986-2.29322.86170.0971-0.32090.04870.1679-0.37220.012-0.21720.4720.19550.29-0.0695-0.01350.27940.00570.33141.9671-44.8893-2.3007
252.26210.7747-0.46522.1202-0.67751.8459-0.0563-0.03250.1342-0.1982-0.1338-0.0075-0.22860.10280.1720.2564-0.0317-0.02230.16520.020.30894.4031-42.0918-13.0162
261.64412.5288-2.04614.0793-1.29675.39790.7646-0.46310.00780.044-0.49380.4754-0.22960.24910.27450.382-0.0570.07270.44670.00830.27343.5397-47.55518.6072
274.53360.6024-3.34175.46622.30836.5295-0.5381-0.69980.5929-0.32920.66860.3712-0.48250.1388-0.44050.3124-0.0294-0.07610.1740.07820.3499-4.3239-49.5621-9.7409
284.4390.037-1.66612.6378-1.17824.60030.13760.90570.58280.30720.2553-0.02840.0625-1.19780.26440.2668-0.06730.13130.89080.21570.293640.2353-25.5075-37.4452
291.8052-1.8704-3.11470.435-0.09882.9061-0.25590.6618-0.0225-0.102-0.06560.00920.4851-0.63420.25540.2821-0.12170.01110.4265-0.00460.374836.1667-25.657-26.9605
304.2434-0.0018-1.68411.5226-0.78234.5098-0.4919-0.48961.18840.2494-0.93720.45230.5224-0.55150.13610.27150.0892-0.01590.2439-0.0290.239941.4064-20.8965-12.7211
316.50790.1848-1.97131.993-2.69134.27210.2151-0.82080.09160.0566-0.1638-0.0824-0.10090.05630.31530.27170.02510.05970.3434-0.02250.292432.1256-28.189-6.7379
323.53350.9948-0.57471.08890.19462.4102-0.2128-0.08360.28450.31380.45580.47180.0416-0.00910.10530.23790.0733-0.00380.3254-0.09280.340830.491-23.2053-6.1178
332.36370.7882-1.63141.48650.34053.7914-0.2630.18150.0718-0.3263-0.0254-0.0301-0.0136-0.32920.21560.1687-0.01640.00950.2391-0.02330.267237.4011-24.8091-16.8195
345.2996-0.0537-2.32580.3042-0.97875.8214-0.02060.69360.2528-0.12670.01980.42650.0389-0.49230.3040.3733-0.03550.09190.39680.03760.287739.408-26.8366-33.2573
354.36240.68371.08580.94-1.8224.9770.4984-0.48050.6185-0.39280.05160.08190.2224-0.8757-0.36240.1104-0.01960.00080.3667-0.10970.425745.0578-21.0254-14.9349
363.8503-1.6325-2.29222.69463.02773.5469-0.41690.1069-1.15190.52180.1693-0.49932.75160.63610.16561.4650.1486-0.03751.2140.18350.868414.349-8.7734.9311
371.4019-0.838-2.00292.14823.1164.9914-0.4186-0.4908-0.45550.3492-0.34060.00340.87971.41670.33570.95190.16880.05260.94380.29770.734512.6058-7.902-6.4865
382.7225-1.3406-1.31732.25373.02554.38181.0412-0.54790.7612-0.53722.6412-3.278-0.15730.8324-0.04130.83081.2714-0.57350.39923.15-1.994718.6583-7.1141-23.1177
390.4403-0.3748-0.56680.2290.47430.93820.20830.1829-0.55510.74630.55920.80530.0933-0.88490.34920.99680.14920.17841.23840.16680.508314.4439-19.1564-26.6918
402.794-0.04-1.06341.35631.82794.4164-0.12330.31580.1039-0.11720.10420.31710.0484-0.62090.23230.83070.1665-0.08311.32630.2460.799816.8865-16.1987-27.6014
411.4952-0.6472-2.4321.71212.14283.2607-0.5285-0.2050.50080.67820.2092-0.35371.6860.61890.21771.07880.30660.02081.01550.12460.592414.5341-9.2316-7.6131
421.4425-0.07850.95193.482-3.22383.90540.10910.38940.2402-0.2902-0.4888-0.85560.39461.0601-0.00870.9706-0.03040.14811.3078-0.25460.9321-1.3259-11.988-27.4348
431.173-0.60661.51982.5504-3.13253.00870.43650.0947-1.211-0.3125-0.55930.19691.2576-0.62870.09691.31480.33870.36460.6425-0.24060.70760.2736-18.4525-11.8473
44-0.02960.02790.02760.05030.01610.03840.42330.76331.4072-0.1013-0.3652-0.3529-1.36790.37210.221.79660.06080.11780.84160.07491.03939.6082-22.14551.9125
451.5210.83350.67031.9707-1.69543.5820.3762-0.34290.7161.3605-0.2546-0.3063-0.8862-0.01950.13671.4062-0.27060.11010.9132-0.22151.13885.7678-23.042.5944
460.5082-0.20650.56091.9633-2.69592.4282-0.06170.0782-0.0875-0.7782-0.40670.32441.07490.6190.09541.27760.15610.16080.8971-0.06730.60860.6388-17.2662-16.3081
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 898 through 903 )A0
2X-RAY DIFFRACTION2chain 'A' and (resid 904 through 908 )A0
3X-RAY DIFFRACTION3chain 'A' and (resid 909 through 913 )A0
4X-RAY DIFFRACTION4chain 'A' and (resid 914 through 932 )A0
5X-RAY DIFFRACTION5chain 'A' and (resid 933 through 950 )A0
6X-RAY DIFFRACTION6chain 'A' and (resid 951 through 961 )A0
7X-RAY DIFFRACTION7chain 'A' and (resid 962 through 971 )A0
8X-RAY DIFFRACTION8chain 'A' and (resid 972 through 978 )A0
9X-RAY DIFFRACTION9chain 'A' and (resid 979 through 990 )A0
10X-RAY DIFFRACTION10chain 'A' and (resid 991 through 1005 )A0
11X-RAY DIFFRACTION11chain 'a' and (resid 19 through 27 )a0
12X-RAY DIFFRACTION12chain 'B' and (resid 898 through 903 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 904 through 908 )B0
14X-RAY DIFFRACTION14chain 'B' and (resid 909 through 913 )B0
15X-RAY DIFFRACTION15chain 'B' and (resid 914 through 932 )B0
16X-RAY DIFFRACTION16chain 'B' and (resid 933 through 942 )B0
17X-RAY DIFFRACTION17chain 'B' and (resid 943 through 950 )B0
18X-RAY DIFFRACTION18chain 'B' and (resid 951 through 961 )B0
19X-RAY DIFFRACTION19chain 'B' and (resid 962 through 971 )B0
20X-RAY DIFFRACTION20chain 'B' and (resid 972 through 990 )B0
21X-RAY DIFFRACTION21chain 'B' and (resid 991 through 1005 )B0
22X-RAY DIFFRACTION22chain 'b' and (resid 19 through 27 )b0
23X-RAY DIFFRACTION23chain 'C' and (resid 898 through 913 )C0
24X-RAY DIFFRACTION24chain 'C' and (resid 914 through 942 )C0
25X-RAY DIFFRACTION25chain 'C' and (resid 943 through 989 )C0
26X-RAY DIFFRACTION26chain 'C' and (resid 990 through 1003 )C0
27X-RAY DIFFRACTION27chain 'c' and (resid 20 through 26 )c0
28X-RAY DIFFRACTION28chain 'D' and (resid 898 through 913 )D0
29X-RAY DIFFRACTION29chain 'D' and (resid 914 through 932 )D0
30X-RAY DIFFRACTION30chain 'D' and (resid 933 through 942 )D0
31X-RAY DIFFRACTION31chain 'D' and (resid 943 through 950 )D0
32X-RAY DIFFRACTION32chain 'D' and (resid 951 through 966 )D0
33X-RAY DIFFRACTION33chain 'D' and (resid 967 through 989 )D0
34X-RAY DIFFRACTION34chain 'D' and (resid 990 through 1003 )D0
35X-RAY DIFFRACTION35chain 'd' and (resid 20 through 26 )d0
36X-RAY DIFFRACTION36chain 'E' and (resid 898 through 908 )E0
37X-RAY DIFFRACTION37chain 'E' and (resid 909 through 932 )E0
38X-RAY DIFFRACTION38chain 'E' and (resid 933 through 942 )E0
39X-RAY DIFFRACTION39chain 'E' and (resid 943 through 950 )E0
40X-RAY DIFFRACTION40chain 'E' and (resid 951 through 972 )E0
41X-RAY DIFFRACTION41chain 'E' and (resid 973 through 1005 )E0
42X-RAY DIFFRACTION42chain 'F' and (resid 898 through 913 )F0
43X-RAY DIFFRACTION43chain 'F' and (resid 914 through 942 )F0
44X-RAY DIFFRACTION44chain 'F' and (resid 943 through 950 )F0
45X-RAY DIFFRACTION45chain 'F' and (resid 951 through 971 )F0
46X-RAY DIFFRACTION46chain 'F' and (resid 972 through 1005 )F0

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