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- PDB-7ciz: Crystal structure of DNAJC9 HBD helix2 in complex with H3.3-H4 di... -

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Basic information

Entry
Database: PDB / ID: 7ciz
TitleCrystal structure of DNAJC9 HBD helix2 in complex with H3.3-H4 dimer and MCM2 HBD
Components
  • DNA replication licensing factor MCM2
  • DnaJ homolog subfamily C member 9
  • Histone H3.3H3F3A
  • Histone H4
KeywordsCHAPERONE / Histone chaperone
Function / homology
Function and homology information


Switching of origins to a post-replicative state / Unwinding of DNA / nuclear origin of replication recognition complex / CMG complex / MCM complex / double-strand break repair via break-induced replication / mitotic DNA replication initiation / positive regulation of ATP-dependent activity / protein folding chaperone complex / nucleosomal DNA binding ...Switching of origins to a post-replicative state / Unwinding of DNA / nuclear origin of replication recognition complex / CMG complex / MCM complex / double-strand break repair via break-induced replication / mitotic DNA replication initiation / positive regulation of ATP-dependent activity / protein folding chaperone complex / nucleosomal DNA binding / regulation of DNA-templated DNA replication initiation / DNA unwinding involved in DNA replication / cochlea development / DNA replication origin binding / DNA replication initiation / Activation of the pre-replicative complex / RNA polymerase II core promoter sequence-specific DNA binding / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Replacement of protamines by nucleosomes in the male pronucleus / Activation of ATR in response to replication stress / CENP-A containing nucleosome / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / heat shock protein binding / Meiotic synapsis / telomere organization / cellular response to interleukin-4 / RNA Polymerase I Promoter Opening / SUMOylation of chromatin organization proteins / Assembly of the ORC complex at the origin of replication / DNA methylation / Condensation of Prophase Chromosomes / HCMV Late Events / Chromatin modifications during the maternal to zygotic transition (MZT) / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / SIRT1 negatively regulates rRNA expression / PRC2 methylates histones and DNA / helicase activity / Defective pyroptosis / Assembly of the pre-replicative complex / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Nonhomologous End-Joining (NHEJ) / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / G2/M DNA damage checkpoint / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / HDMs demethylate histones / DNA Damage/Telomere Stress Induced Senescence / PKMTs methylate histone lysines / RMTs methylate histone arginines / Meiotic recombination / Pre-NOTCH Transcription and Translation / nucleosome assembly / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Orc1 removal from chromatin / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / nucleosome / single-stranded DNA binding / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / RUNX1 regulates transcription of genes involved in differentiation of HSCs / chromatin organization / Factors involved in megakaryocyte development and platelet production / Processing of DNA double-strand break ends / HATs acetylate histones / histone binding / protein-folding chaperone binding / Senescence-Associated Secretory Phenotype (SASP) / positive regulation of cell growth / Oxidative Stress Induced Senescence / DNA helicase / Estrogen-dependent gene expression / DNA replication / chromosome, telomeric region / RNA polymerase II cis-regulatory region sequence-specific DNA binding / Amyloid fiber formation / protein heterodimerization activity / apoptotic process / chromatin / enzyme binding / ATP hydrolysis activity / protein-containing complex / DNA binding / extracellular space / RNA binding / extracellular exosome / extracellular region / nucleoplasm / ATP binding
Similarity search - Function
Nt-dnaJ domain signature. / DnaJ domain, conserved site / DNA replication licensing factor Mcm2 / Mini-chromosome maintenance protein 2 / Mini-chromosome maintenance, conserved site / MCM family signature. / DnaJ domain / MCM N-terminal domain / MCM N-terminal domain / MCM OB domain ...Nt-dnaJ domain signature. / DnaJ domain, conserved site / DNA replication licensing factor Mcm2 / Mini-chromosome maintenance protein 2 / Mini-chromosome maintenance, conserved site / MCM family signature. / DnaJ domain / MCM N-terminal domain / MCM N-terminal domain / MCM OB domain / MCM OB domain / Mini-chromosome maintenance protein / MCM, AAA-lid domain / MCM P-loop domain / MCM AAA-lid domain / MCM family domain profile. / minichromosome maintenance proteins / MCM domain / DnaJ molecular chaperone homology domain / dnaJ domain profile. / Chaperone J-domain superfamily / DnaJ domain / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Nucleic acid-binding, OB-fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
DNA replication licensing factor MCM2 / Histone H4 / Histone H3.3 / DnaJ homolog subfamily C member 9
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsBao, H. / Huang, H.
Funding support China, 3items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2018YFC1004500 China
National Natural Science Foundation of China (NSFC)the Thousand Young Talents Program China
National Natural Science Foundation of China (NSFC)31800619 China
CitationJournal: Mol.Cell / Year: 2021
Title: DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network.
Authors: Hammond, C.M. / Bao, H. / Hendriks, I.A. / Carraro, M. / Garcia-Nieto, A. / Liu, Y. / Reveron-Gomez, N. / Spanos, C. / Chen, L. / Rappsilber, J. / Nielsen, M.L. / Patel, D.J. / Huang, H. / Groth, A.
History
DepositionJul 8, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 14, 2021Provider: repository / Type: Initial release
Revision 1.1Apr 28, 2021Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Jun 30, 2021Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Nov 29, 2023Group: 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: Histone H3.3
B: Histone H4
C: DNA replication licensing factor MCM2
E: Histone H3.3
F: Histone H4
G: DNA replication licensing factor MCM2
I: Histone H3.3
J: Histone H4
K: DNA replication licensing factor MCM2
D: DnaJ homolog subfamily C member 9
H: DnaJ homolog subfamily C member 9
L: DnaJ homolog subfamily C member 9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)109,98814
Polymers109,79612
Non-polymers1922
Water13,349741
1
A: Histone H3.3
B: Histone H4
C: DNA replication licensing factor MCM2
H: DnaJ homolog subfamily C member 9
hetero molecules


Theoretical massNumber of molelcules
Total (without water)36,7916
Polymers36,5994
Non-polymers1922
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10140 Å2
ΔGint-63 kcal/mol
Surface area12540 Å2
MethodPISA
2
E: Histone H3.3
F: Histone H4
G: DNA replication licensing factor MCM2
D: DnaJ homolog subfamily C member 9


Theoretical massNumber of molelcules
Total (without water)36,5994
Polymers36,5994
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10600 Å2
ΔGint-64 kcal/mol
Surface area13160 Å2
MethodPISA
3
I: Histone H3.3
J: Histone H4
K: DNA replication licensing factor MCM2
L: DnaJ homolog subfamily C member 9


Theoretical massNumber of molelcules
Total (without water)36,5994
Polymers36,5994
Non-polymers00
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10540 Å2
ΔGint-62 kcal/mol
Surface area13120 Å2
MethodPISA
Unit cell
Length a, b, c (Å)47.638, 176.816, 202.925
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11E-229-

HOH

21F-201-

HOH

31G-238-

HOH

41J-267-

HOH

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Components

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Protein , 4 types, 12 molecules AEIBFJCGKDHL

#1: Protein Histone H3.3 / H3F3A


Mass: 9026.496 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: H3-3A, H3.3A, H3F3, H3F3A, PP781, H3-3B, H3.3B, H3F3B
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P84243
#2: Protein Histone H4 /


Mass: 11263.231 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, ...Gene: HIST1H4A, H4/A, H4FA, HIST1H4B, H4/I, H4FI, HIST1H4C, H4/G, H4FG, HIST1H4D, H4/B, H4FB, HIST1H4E, H4/J, H4FJ, HIST1H4F, H4/C, H4FC, HIST1H4H, H4/H, H4FH, HIST1H4I, H4/M, H4FM, HIST1H4J, H4/E, H4FE, HIST1H4K, H4/D, H4FD, HIST1H4L, H4/K, H4FK, HIST2H4A, H4/N, H4F2, H4FN, HIST2H4, HIST2H4B, H4/O, H4FO, HIST4H4
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P62805
#3: Protein DNA replication licensing factor MCM2 / Minichromosome maintenance protein 2 homolog / Nuclear protein BM28


Mass: 7860.354 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: MCM2, BM28, CCNL1, CDCL1, KIAA0030
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P49736, DNA helicase
#4: Protein DnaJ homolog subfamily C member 9 / HDJC9 / DnaJ protein SB73


Mass: 8448.566 Da / Num. of mol.: 3 / Mutation: C243S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: DNAJC9
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: Q8WXX5

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Non-polymers , 2 types, 743 molecules

#5: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: SO4
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 741 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 1.95 Å3/Da / Density % sol: 36.79 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 0.05 M Lithium sulfate, 0.05 M Sodium sulfate; 0.05 M Tris, pH 8.5, 30% (v/v) PEG400.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.97736 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Jun 23, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97736 Å / Relative weight: 1
ReflectionResolution: 1.8→40 Å / Num. obs: 78310 / % possible obs: 97.7 % / Redundancy: 10 % / Rmerge(I) obs: 0.073 / Rpim(I) all: 0.024 / Net I/σ(I): 31.3
Reflection shellResolution: 1.8→1.83 Å / Mean I/σ(I) obs: 2.2 / Num. unique obs: 3667 / CC1/2: 0.793

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Processing

Software
NameVersionClassification
PHENIX(1.11.1_2575: ???)refinement
HKL-3000data reduction
HKL-3000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5BNV

5bnv


Resolution: 1.8→36.884 Å / SU ML: 0.18 / Cross valid method: FREE R-VALUE / Phase error: 20.79 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2138 3911 5.04 %
Rwork0.1706 --
obs0.1727 77571 96.84 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.8→36.884 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5956 0 10 741 6707
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0066013
X-RAY DIFFRACTIONf_angle_d0.7928055
X-RAY DIFFRACTIONf_dihedral_angle_d7.043762
X-RAY DIFFRACTIONf_chiral_restr0.05906
X-RAY DIFFRACTIONf_plane_restr0.0051059
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.8-1.8210.30461160.23472149X-RAY DIFFRACTION80
1.821-1.8440.26581180.23112372X-RAY DIFFRACTION88
1.844-1.86830.2931270.22292440X-RAY DIFFRACTION91
1.8683-1.89390.25691300.23032467X-RAY DIFFRACTION92
1.8939-1.92090.26691280.22382522X-RAY DIFFRACTION94
1.9209-1.94960.25931260.20262553X-RAY DIFFRACTION95
1.9496-1.98010.23731530.19332517X-RAY DIFFRACTION94
1.9801-2.01250.20271330.17782570X-RAY DIFFRACTION97
2.0125-2.04720.21691490.17532578X-RAY DIFFRACTION96
2.0472-2.08440.22831240.16662652X-RAY DIFFRACTION97
2.0844-2.12450.21711570.1622600X-RAY DIFFRACTION98
2.1245-2.16790.21461470.1622654X-RAY DIFFRACTION97
2.1679-2.2150.19071380.1632615X-RAY DIFFRACTION98
2.215-2.26650.22481380.15752673X-RAY DIFFRACTION98
2.2665-2.32320.20661490.16032651X-RAY DIFFRACTION99
2.3232-2.3860.20451330.15952709X-RAY DIFFRACTION99
2.386-2.45620.19041680.16052630X-RAY DIFFRACTION99
2.4562-2.53550.21281530.1572705X-RAY DIFFRACTION100
2.5355-2.62610.21611390.16042706X-RAY DIFFRACTION100
2.6261-2.73120.17991550.16492680X-RAY DIFFRACTION100
2.7312-2.85540.19371440.16672742X-RAY DIFFRACTION100
2.8554-3.00590.24881400.16962719X-RAY DIFFRACTION100
3.0059-3.19410.23391290.17772752X-RAY DIFFRACTION100
3.1941-3.44060.20871410.15762755X-RAY DIFFRACTION100
3.4406-3.78650.16731470.15232736X-RAY DIFFRACTION100
3.7865-4.33370.19411480.15322798X-RAY DIFFRACTION100
4.3337-5.45720.2141510.16522781X-RAY DIFFRACTION100
5.4572-36.8840.24821300.20342934X-RAY DIFFRACTION99
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)
15.95321.51.16965.89151.33774.4334-0.07710.59520.0401-0.8845-0.0198-0.3271-0.2807-0.07130.23120.2465-0.01180.01460.23670.01320.2655.821732.8229-13.0939
23.89841.02390.28835.8704-2.523.06780.0194-0.59330.40110.5525-0.2229-0.2479-0.37820.44240.23530.181-0.0327-0.04470.2737-0.03670.236110.652427.36252.8409
30.71420.0605-1.42152.7830.52853.0383-0.0534-0.99640.23050.59870.0637-0.84010.24050.90090.0220.26140.1031-0.08760.54790.07580.231615.103418.70656.7333
47.797-1.88651.26492.6905-1.00762.00340.06010.07580.0203-0.0823-0.01130.3284-0.0367-0.2310.0060.13920.00560.0220.18120.01770.1645-4.491425.4325-7.8559
51.4435-1.35410.0792.21760.67690.65180.1652-0.43050.54510.62610.11610.8215-0.3404-0.5901-0.00490.15610.05720.10020.37070.02270.4296-16.217229.1421-3.3163
64.7282-0.76120.3863.0450.75073.85460.0274-0.00190.50240.0438-0.07530.167-0.4613-0.11330.00210.1960.04470.06630.14480.01090.244-3.754836.4-9.134
72.0144-1.58920.49154.1598-1.07840.9902-0.0894-0.49110.05180.5790.0590.0893-0.2789-0.00630.04120.2046-0.00730.02740.2624-0.00460.09763.6621.06374.1407
86.0104-0.3591-1.3251.94420.24891.1046-0.0078-0.1553-0.24040.0697-0.09360.35420.2756-0.26220.02290.1978-0.01270.01440.30790.05710.1440.874711.8011-1.1112
91.8617-0.42190.78781.4414-0.57112.60340.0519-0.11170.450.1579-0.2695-0.519-1.02380.3610.02850.1676-0.0530.00010.18620.02250.3526.037938.2444-10.0012
100.2747-0.58440.11753.0460.12522.92720.0257-0.1609-0.12220.2008-0.0815-0.19870.07790.01140.03540.2450.0021-0.02610.34260.11890.18327.50996.9256.249
112.41780.40520.7324.27582.27042.8939-0.06240.05680.2012-0.2602-0.09640.2687-0.1549-0.17750.06450.0940.0209-0.01030.09390.04350.1387-9.455730.56333.0877
122.55520.93-1.82244.337-0.34711.57950.08560.52860.1282-0.5945-0.01030.7152-0.1375-0.7515-0.06410.1982-0.0105-0.05880.24480.01450.1582-15.324520.152525.9959
132.53840.29270.56542.46670.23451.4154-0.04410.06360.34640.1104-0.0262-0.3818-0.07680.3007-0.06970.0943-0.0104-0.02010.0990.02590.16517.399130.120140.2645
143.53660.03410.66852.6928-1.37512.53730.26590.40710.234-0.7619-0.3387-0.51550.06320.014-0.11850.12850.04780.06120.28520.03310.262915.587629.265833.321
151.9531-0.84751.2725.4782-1.90721.19010.31871.3938-0.0241-1.2448-0.6805-0.81010.26620.445-0.32350.25980.11610.05080.363-0.02540.225512.452821.899932.0322
169.19154.39516.88093.36763.90225.4443-0.01380.09680.4584-0.8537-0.1190.749-0.443-0.47380.14370.3981-0.0294-0.07840.27650.08050.3487-7.480536.425827.6944
172.84950.5444-0.79653.556-0.04511.6823-0.02240.21840.23620.08060.0278-0.1026-0.35970.3678-0.14930.1299-0.0577-0.0140.05750.06570.14274.735138.889842.027
181.42111.61060.21183.29430.53010.7442-0.15850.22870.0824-0.47680.07160.0182-0.11430.06390.06180.13440.0019-0.00390.13640.03240.0757-3.882422.694428.5571
198.21021.4935-0.41272.7202-0.22642.02260.0110.1527-0.1812-0.0066-0.0279-0.36720.09520.27080.0390.17760.0267-0.00410.135-0.00750.126-1.235713.799434.4546
203.11280.0852-3.06370.4231-0.3343.0477-0.109-0.06230.30540.09590.0174-0.18580.04780.2373-0.02240.2786-0.0716-0.01140.19990.05880.275412.995847.423540.6946
211.27530.1760.720.5764-0.40351.026-0.0876-0.20270.46650.0639-0.24310.5674-0.283-0.28120.25610.1540.0563-0.01060.1713-0.03160.2972-12.200937.53740.6541
224.3456-3.9525-0.20144.93850.17172.4695-0.0781-0.18750.03630.39270.08331.0503-0.0603-0.7091-0.0750.21410.02960.00440.2774-0.01890.3727-19.671510.933633.2167
230.355-0.66570.91565.3102-0.48412.90190.06880.4154-0.205-0.2491-0.1375-0.73170.06350.88860.01820.23690.00150.02240.3383-0.0280.1425-0.80877.260524.0931
245.14894.0078-1.17654.3305-1.57333.5036-0.23920.79690.2174-0.66280.11620.3490.307-0.30160.16820.16060.0018-0.01660.15970.0420.185417.7656.557824.9814
254.01210.918-0.23714.50681.26523.69750.1073-0.3082-0.27770.5811-0.19410.43250.2487-0.4421-0.05430.1251-0.00020.04320.11980.05340.180812.899963.183639.3464
263.5483-0.48330.36092.7218-1.32956.2169-0.1609-0.6524-0.03520.64630.06750.5796-0.3208-0.62180.09630.22930.0360.08630.2087-0.01350.23178.478372.342242.2641
272.5004-0.4987-0.49962.59970.19081.3326-0.0556-0.0721-0.2992-0.0644-0.044-0.24820.07380.2568-0.06450.07970.00890.00640.10640.03660.132231.202261.573928.4076
283.9399-0.9203-0.22746.30150.29031.05920.1701-0.83980.00511.2414-0.2831-0.72280.09680.26730.0790.2038-0.0692-0.05410.30290.03640.230338.486464.514935.4548
293.4595-2.42940.39045.86993.41673.44950.1002-0.137-0.67071.1767-0.32970.4523-0.2793-0.73710.12940.49010.05510.09020.38110.0990.401916.019856.488342.0246
304.1206-0.36340.6933.1667-0.09791.96050.0302-0.0608-0.0887-0.1304-0.0564-0.10060.38920.222-0.06760.1450.044-0.00420.11110.02120.167128.564152.73927.2735
311.7419-3.07-0.23555.44350.68570.2998-0.2778-0.2519-0.19130.61690.1910.1630.13930.08240.04230.1840.0089-0.01180.14280.03590.137622.962967.419439.8998
325.1538-0.1445-0.45113.31330.11142.6086-0.0635-0.0796-0.06340.17370.0299-0.119-0.04160.18540.02590.1713-0.0057-0.01630.1078-0.01020.11918.232678.583635.476
330.9793-0.04460.14181.36540.16640.530.0063-0.0281-0.39960.0048-0.06520.29140.2344-0.05520.02770.203-0.01040.00850.12190.0350.236722.594748.684127.8985
341.61251.9963-0.06922.57550.21971.6392-0.19120.203-0.0138-0.38940.24411.2038-0.4474-0.378-0.0750.088-0.00910.00270.2324-0.03390.53334.033577.51935.1856
353.3262-0.84322.82952.1231-1.70295.9394-0.12480.06060.16460.3259-0.0347-0.4264-0.26260.69540.13890.264-0.0185-0.0290.2006-0.02040.171523.390185.292743.7169
367.44793.18980.02621.91990.31321.0665-0.0540.055-0.18260.0521-0.0098-0.15870.27250.18130.040.23260.018-0.02140.21770.05080.15384.836216.877744.1246
372.5238-1.7197-0.78382.6122-0.84712.0918-0.06090.06760.0327-0.09120.01940.21410.2875-0.17880.05660.2683-0.0143-0.00780.2972-0.01010.1844-5.712914.8745-11.1541
386.1215-2.679-0.2542.41980.83861.3706-0.1606-0.13410.2788-0.05880.017-0.1357-0.33780.10590.08610.2679-0.0277-0.01140.25690.06410.172428.365674.987924.1232
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 57 through 63 )
2X-RAY DIFFRACTION2chain 'A' and (resid 64 through 77 )
3X-RAY DIFFRACTION3chain 'A' and (resid 78 through 85 )
4X-RAY DIFFRACTION4chain 'A' and (resid 86 through 113 )
5X-RAY DIFFRACTION5chain 'A' and (resid 114 through 134 )
6X-RAY DIFFRACTION6chain 'B' and (resid 28 through 47 )
7X-RAY DIFFRACTION7chain 'B' and (resid 48 through 82 )
8X-RAY DIFFRACTION8chain 'B' and (resid 83 through 98 )
9X-RAY DIFFRACTION9chain 'C' and (resid 68 through 95 )
10X-RAY DIFFRACTION10chain 'C' and (resid 96 through 125 )
11X-RAY DIFFRACTION11chain 'E' and (resid 59 through 77 )
12X-RAY DIFFRACTION12chain 'E' and (resid 78 through 85 )
13X-RAY DIFFRACTION13chain 'E' and (resid 86 through 120 )
14X-RAY DIFFRACTION14chain 'E' and (resid 121 through 130 )
15X-RAY DIFFRACTION15chain 'E' and (resid 131 through 135 )
16X-RAY DIFFRACTION16chain 'F' and (resid 22 through 30 )
17X-RAY DIFFRACTION17chain 'F' and (resid 31 through 47 )
18X-RAY DIFFRACTION18chain 'F' and (resid 48 through 82 )
19X-RAY DIFFRACTION19chain 'F' and (resid 83 through 98 )
20X-RAY DIFFRACTION20chain 'G' and (resid 62 through 76 )
21X-RAY DIFFRACTION21chain 'G' and (resid 77 through 96 )
22X-RAY DIFFRACTION22chain 'G' and (resid 97 through 106 )
23X-RAY DIFFRACTION23chain 'G' and (resid 107 through 125 )
24X-RAY DIFFRACTION24chain 'I' and (resid 58 through 63 )
25X-RAY DIFFRACTION25chain 'I' and (resid 64 through 77 )
26X-RAY DIFFRACTION26chain 'I' and (resid 78 through 85 )
27X-RAY DIFFRACTION27chain 'I' and (resid 86 through 120 )
28X-RAY DIFFRACTION28chain 'I' and (resid 121 through 135 )
29X-RAY DIFFRACTION29chain 'J' and (resid 21 through 30 )
30X-RAY DIFFRACTION30chain 'J' and (resid 31 through 47 )
31X-RAY DIFFRACTION31chain 'J' and (resid 48 through 75 )
32X-RAY DIFFRACTION32chain 'J' and (resid 76 through 98 )
33X-RAY DIFFRACTION33chain 'K' and (resid 63 through 92 )
34X-RAY DIFFRACTION34chain 'K' and (resid 93 through 106 )
35X-RAY DIFFRACTION35chain 'K' and (resid 107 through 125 )
36X-RAY DIFFRACTION36chain 'D' and (resid 212 through 245 )
37X-RAY DIFFRACTION37chain 'H' and (resid 212 through 243 )
38X-RAY DIFFRACTION38chain 'L' and (resid 212 through 245 )

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