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- PDB-6fol: Domain II of the human copper chaperone in complex with human Cu,... -

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Basic information

Entry
Database: PDB / ID: 6fol
TitleDomain II of the human copper chaperone in complex with human Cu,Zn superoxide dismutase
Components
  • Copper chaperone for superoxide dismutase
  • Superoxide dismutase [Cu-Zn]
KeywordsMETAL BINDING PROTEIN / heterodimer / copper-chaperone / hSOD1 / protein maturation
Function / homology
Function and homology information


superoxide dismutase copper chaperone activity / action potential initiation / neurofilament cytoskeleton organization / protein phosphatase 2B binding / regulation of organ growth / relaxation of vascular associated smooth muscle / anterograde axonal transport / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / response to superoxide / regulation of T cell differentiation in thymus ...superoxide dismutase copper chaperone activity / action potential initiation / neurofilament cytoskeleton organization / protein phosphatase 2B binding / regulation of organ growth / relaxation of vascular associated smooth muscle / anterograde axonal transport / positive regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / response to superoxide / regulation of T cell differentiation in thymus / peripheral nervous system myelin maintenance / retina homeostasis / auditory receptor cell stereocilium organization / hydrogen peroxide biosynthetic process / retrograde axonal transport / superoxide anion generation / regulation of GTPase activity / myeloid cell homeostasis / muscle cell cellular homeostasis / superoxide metabolic process / heart contraction / superoxide dismutase / Detoxification of Reactive Oxygen Species / transmission of nerve impulse / negative regulation of reproductive process / negative regulation of developmental process / superoxide dismutase activity / protein-disulfide reductase activity / regulation of multicellular organism growth / response to axon injury / ectopic germ cell programmed cell death / neuronal action potential / positive regulation of phagocytosis / ovarian follicle development / axon cytoplasm / dendrite cytoplasm / embryo implantation / glutathione metabolic process / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / removal of superoxide radicals / reactive oxygen species metabolic process / protein maturation / regulation of mitochondrial membrane potential / thymus development / positive regulation of superoxide anion generation / positive regulation of cytokine production / determination of adult lifespan / locomotory behavior / placenta development / sensory perception of sound / response to hydrogen peroxide / small GTPase binding / mitochondrial intermembrane space / regulation of blood pressure / negative regulation of inflammatory response / peroxisome / Platelet degranulation / protein-folding chaperone binding / response to heat / cellular response to oxidative stress / cytoplasmic vesicle / gene expression / spermatogenesis / negative regulation of neuron apoptotic process / response to ethanol / intracellular iron ion homeostasis / positive regulation of MAPK cascade / mitochondrial matrix / cadherin binding / positive regulation of apoptotic process / copper ion binding / response to xenobiotic stimulus / neuronal cell body / apoptotic process / protein homodimerization activity / protein-containing complex / mitochondrion / extracellular space / extracellular exosome / extracellular region / zinc ion binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Heavy-metal-associated domain / Heavy metal-associated domain superfamily / Heavy-metal-associated domain profile. / Heavy metal-associated domain, HMA / Copper/Zinc superoxide dismutase signature 1. / Superoxide dismutase (Cu/Zn) / superoxide dismutase copper chaperone / Superoxide dismutase, copper/zinc, binding site / Copper/Zinc superoxide dismutase signature 2. / Superoxide dismutase, copper/zinc binding domain / Copper/zinc superoxide dismutase (SODC) / Superoxide dismutase-like, copper/zinc binding domain superfamily
Similarity search - Domain/homology
3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL / Copper chaperone for superoxide dismutase / Superoxide dismutase [Cu-Zn]
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsSala, F.A. / Wright, G.S.A. / Antonyuk, S.V. / Garratt, R.C. / Hasnain, S.S.
Funding support United Kingdom, Brazil, 5items
OrganizationGrant numberCountry
Motor Neurone Disease AssociationHasnain/Apr15/833-791 United Kingdom
Medical Research Council (United Kingdom)MRF-060-0002-RG-HASNA United Kingdom
Sao Paulo Research Fundation2015/00062-1 Brazil
Sao Paulo Research Fundation2016/24686-7 Brazil
National Council for Scientific and Technological Development407438/2013-0 Brazil
CitationJournal: Plos Biol. / Year: 2019
Title: Molecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS.
Authors: Sala, F.A. / Wright, G.S.A. / Antonyuk, S.V. / Garratt, R.C. / Hasnain, S.S.
History
DepositionFeb 7, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 30, 2019Provider: repository / Type: Initial release
Revision 1.1Jun 19, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID
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 1.3Oct 23, 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: Copper chaperone for superoxide dismutase
B: Superoxide dismutase [Cu-Zn]
C: Superoxide dismutase [Cu-Zn]
D: Copper chaperone for superoxide dismutase
E: Copper chaperone for superoxide dismutase
F: Superoxide dismutase [Cu-Zn]
G: Superoxide dismutase [Cu-Zn]
H: Copper chaperone for superoxide dismutase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)127,67619
Polymers126,3208
Non-polymers1,35611
Water4,864270
1
A: Copper chaperone for superoxide dismutase
B: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,7114
Polymers31,5802
Non-polymers1312
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1640 Å2
ΔGint-8 kcal/mol
Surface area14080 Å2
MethodPISA
2
C: Superoxide dismutase [Cu-Zn]
D: Copper chaperone for superoxide dismutase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)32,4526
Polymers31,5802
Non-polymers8724
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1830 Å2
ΔGint-11 kcal/mol
Surface area13970 Å2
MethodPISA
3
E: Copper chaperone for superoxide dismutase
F: Superoxide dismutase [Cu-Zn]
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,8035
Polymers31,5802
Non-polymers2233
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1620 Å2
ΔGint-10 kcal/mol
Surface area13910 Å2
MethodPISA
4
G: Superoxide dismutase [Cu-Zn]
H: Copper chaperone for superoxide dismutase
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,7114
Polymers31,5802
Non-polymers1312
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1330 Å2
ΔGint-9 kcal/mol
Surface area13930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)244.689, 244.689, 182.332
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number155
Space group name H-MH32

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Components

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Protein , 2 types, 8 molecules ADEHBCFG

#1: Protein
Copper chaperone for superoxide dismutase / Superoxide dismutase copper chaperone


Mass: 15816.517 Da / Num. of mol.: 4 / Mutation: Truncation of Domains: I and III
Source method: isolated from a genetically manipulated source
Details: hCCS Domain II with additional residues (GA) from HISTAG
Source: (gene. exp.) Homo sapiens (human) / Gene: CCS / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: O14618
#2: Protein
Superoxide dismutase [Cu-Zn] / Superoxide dismutase 1 / hSod1


Mass: 15763.432 Da / Num. of mol.: 4 / Mutation: C57A; C146A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SOD1 / Production host: Escherichia coli BL21 (bacteria) / References: UniProt: P00441, superoxide dismutase

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Non-polymers , 4 types, 281 molecules

#3: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#4: Chemical ChemComp-PE8 / 3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL


Mass: 370.436 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C16H34O9
#5: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 270 / Source method: isolated from a natural source / Formula: H2O

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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: 4.15 Å3/Da / Density % sol: 70.38 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop
Details: 25% (w/v) PEG 1500 and 0.1 M PCTP buffer pH 7.0 (sodium propionate, sodium cacodylate, and BIS-TRIS propane in the molar ratios 2:1:2, respectively)

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.97857 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Sep 26, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 2.55→49.4 Å / Num. obs: 64704 / % possible obs: 95.7 % / Redundancy: 6.8 % / Biso Wilson estimate: 39.2 Å2 / CC1/2: 0.995 / Rmerge(I) obs: 0.13 / Rpim(I) all: 0.053 / Rrim(I) all: 0.14 / Net I/σ(I): 9.5
Reflection shellResolution: 2.55→2.69 Å / Redundancy: 6.7 % / Rmerge(I) obs: 0.806 / Mean I/σ(I) obs: 2 / Num. unique obs: 9558 / CC1/2: 0.409 / Rpim(I) all: 0.335 / Rrim(I) all: 0.877 / % possible all: 97.2

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
iMOSFLMdata reduction
SCALAdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1DO5, 2C9V

1do5

2c9v


Resolution: 2.55→46.974 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 27.37 / Details: TLS and NCS were used
RfactorNum. reflection% reflection
Rfree0.2482 3136 4.85 %
Rwork0.208 --
obs0.2099 64691 95.26 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.55→46.974 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8841 0 64 270 9175
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0039136
X-RAY DIFFRACTIONf_angle_d0.47412338
X-RAY DIFFRACTIONf_dihedral_angle_d7.9585380
X-RAY DIFFRACTIONf_chiral_restr0.0481327
X-RAY DIFFRACTIONf_plane_restr0.0031699
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5501-2.58990.39451520.34622826X-RAY DIFFRACTION97
2.5899-2.63240.38291570.34572819X-RAY DIFFRACTION97
2.6324-2.67780.37771400.32812820X-RAY DIFFRACTION97
2.6778-2.72640.33131300.32162829X-RAY DIFFRACTION97
2.7264-2.77890.36931560.3112816X-RAY DIFFRACTION97
2.7789-2.83560.27031510.30012815X-RAY DIFFRACTION97
2.8356-2.89720.31971510.30132815X-RAY DIFFRACTION96
2.8972-2.96460.28981440.28762830X-RAY DIFFRACTION97
2.9646-3.03880.32771410.28172763X-RAY DIFFRACTION95
3.0388-3.12090.29871320.26232798X-RAY DIFFRACTION95
3.1209-3.21270.29511500.24072825X-RAY DIFFRACTION96
3.2127-3.31640.27291310.23152797X-RAY DIFFRACTION96
3.3164-3.43490.26291250.22232806X-RAY DIFFRACTION96
3.4349-3.57240.25791290.21622824X-RAY DIFFRACTION96
3.5724-3.73490.22041680.19922763X-RAY DIFFRACTION95
3.7349-3.93170.22551360.18272772X-RAY DIFFRACTION94
3.9317-4.17790.20461450.16032769X-RAY DIFFRACTION94
4.1779-4.50020.22241180.14362800X-RAY DIFFRACTION94
4.5002-4.95270.19851450.14152787X-RAY DIFFRACTION94
4.9527-5.66830.18981560.15922743X-RAY DIFFRACTION93
5.6683-7.13740.20531530.17292748X-RAY DIFFRACTION93
7.1374-46.98170.18341260.1492790X-RAY DIFFRACTION91
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)
11.33331.58950.2535.5799-4.78037.6508-0.2703-0.0474-0.26050.2999-0.3581-0.3105-0.0945-0.44880.60140.5162-0.0811-0.2210.38120.0680.6362-61.659216.0268-43.6382
22.4805-0.3119-1.39783.9461.08238.56030.1650.20640.2886-0.20940.12140.5094-0.3054-0.2277-0.3190.4367-0.0605-0.13280.37270.01030.6092-63.849910.3657-45.3397
31.0782-0.10920.57334.9005-0.09391.4996-0.04560.13010.1569-0.1204-0.0427-0.3035-0.09950.00480.0820.4013-0.0918-0.0690.37440.08230.539-55.4632.9619-46.0998
41.66580.4193-1.99053.2237-3.63596.78840.00450.4828-0.0918-0.6818-0.254-0.18250.75680.46590.17430.4979-0.0987-0.11660.37390.10390.7613-44.773423.6306-49.1794
51.3949-0.1121-0.46692.8251-0.16193.80740.1163-0.00910.0747-0.1611-0.03010.4273-0.376-0.1039-0.09910.5439-0.1502-0.070.39310.08210.7404-50.022832.2172-44.7356
67.12141.3562-6.12598.7592-1.24235.58240.1162-0.64251.11710.46870.25111.1602-0.6911.001-0.20740.5509-0.0618-0.12640.52430.01150.8653-50.237939.4462-38.448
72.57190.7872-1.01542.6319-1.57453.8087-0.02980.22640.2153-0.21850.08280.365-0.4504-0.0992-0.04530.5688-0.1137-0.12990.39560.06020.6605-48.572333.9962-46.9561
83.2964-1.0836-1.64731.0781-0.18245.1954-0.2856-0.1850.0790.00450.2966-0.01291.03840.6533-0.11190.576-0.1267-0.10770.36320.07990.5078-57.4786-6.7812-12.7544
92.0696-0.63560.81230.3585-0.72613.39480.1871-0.2773-0.3645-0.1030.17-0.08871.0795-0.8798-0.39630.6614-0.2677-0.17010.43040.09280.7233-64.3078-11.5382-16.0588
101.9443-0.778-2.86295.69391.19624.61780.2432-0.4137-0.63950.17090.09460.15140.0726-0.6968-0.33880.4899-0.1374-0.07070.67840.19390.7107-72.38132.0849-14.4477
115.5374-0.5135-6.34492.6592-0.0287.41890.688-0.31830.26590.0667-0.47722.11090.8736-1.2178-0.23810.6082-0.2702-0.15670.7150.07050.7399-76.755-6.3149-19.0401
124.0822.025-0.88272.4168-1.7434.19020.1814-0.286-0.20040.09010.22170.23150.5935-1.1229-0.38610.5641-0.2212-0.18310.6440.12080.6685-69.1519-8.8278-13.6405
132.7758-0.93453.24982.2046-1.4073.55490.0149-0.8476-0.28620.26250.18680.07060.0492-1.4754-0.19650.5296-0.1904-0.09830.71560.06490.4744-68.0633-2.9611-10.2829
143.70114.11360.99417.65812.89783.58130.8499-0.3129-0.2090.2215-0.0394-0.38830.74330.6005-1.03760.5331-0.1473-0.00620.5386-0.01750.4706-54.318410.2525-11.1258
152.17540.4701-0.06523.6979-1.21813.59070.0298-0.06040.26640.5426-0.00130.0983-0.52120.42480.0590.5417-0.1403-0.09230.4666-0.02390.591-50.294416.3095-13.6896
166.86590.6061-5.08257.1243-1.81194.127-0.3757-0.25470.3629-0.31380.4732-0.23610.80060.5525-0.21040.6489-0.1375-0.05510.40550.01320.7347-47.34-1.5284-15.6166
174.76452.0524-1.56757.2824-2.9537.8082-0.1005-0.41190.4155-0.1846-0.00990.1017-0.03410.54530.1720.4314-0.0605-0.08810.4660.03530.6482-41.826911.4217-25.2624
183.46910.8613-0.35632.774-0.51044.5169-0.0507-0.19890.08880.2767-0.0284-0.2377-0.23650.55130.06970.4985-0.1329-0.13140.4380.02140.6248-44.129113.282-16.7452
194.24091.68042.50592.4758-2.44148.1086-0.136-0.85130.42070.0546-0.06160.8274-0.6955-1.23250.030.33310.0074-0.05280.43680.11350.9091-18.133164.6181-42.8079
205.312-0.1762-1.87812.48251.1442.67980.0047-0.06610.7723-0.32040.10.333-0.13140.4546-0.12080.4132-0.0818-0.04350.38610.18550.7142-22.738561.1815-47.3538
219.8190.19794.99940.9179-0.71893.62240.20171.4323-0.3731-0.43860.34340.7071.03820.5781-0.28450.5679-0.2235-0.19280.44750.15180.5052-27.797152.0627-53.9623
223.38411.8507-0.53213.3773.75377.7303-0.73220.8549-1.3269-0.51110.94970.90071.6345-0.2675-0.0960.6563-0.1184-0.02780.57940.00760.9018-13.365945.3605-49.2978
234.60151.04590.64720.66540.23921.6916-0.0774-0.14750.0259-0.11370.05470.20320.3082-0.21050.02490.4502-0.0832-0.04060.37060.14080.6578-28.78848.8348-41.4695
243.62131.57770.25791.7462-0.23681.6508-0.2030.02350.5253-0.21530.08550.4092-0.0665-0.09930.11680.4346-0.0588-0.06250.37370.12090.6311-27.711352.8794-46.0926
254.5205-0.42560.9055-0.0276-0.87837.4432-0.28880.4938-0.1182-0.8170.3766-0.24910.44570.1726-0.10550.3503-0.0375-0.05640.30690.13680.6377-21.151148.883-49.5817
266.52075.2926-5.33138.501-5.90395.39-0.36410.29160.0856-0.41060.32010.0930.5518-0.67750.1430.451-0.01660.01150.3283-0.07690.5445-2.700450.4135-49.7585
275.4390.9479-4.96513.5741-2.46667.3895-0.1563-0.5442-0.59350.07490.064-0.17291.25860.61860.0920.38050.064-0.05710.34140.05110.65622.397547.3834-39.7589
289.27191.0159-3.49065.0618-1.19662.3267-0.43440.3628-0.4028-0.2859-0.0014-0.77470.18010.39120.50190.3378-0.00370.02050.3411-0.02930.38537.639457.417-52.6584
294.62510.61831.60552.2895-1.83462.3176-0.14640.26580.8981-0.7270.42561.1756-0.4134-1.3399-0.35240.5096-0.0402-0.11610.55120.11240.7479-5.065766.2136-46.1673
309.7169-4.1932-2.04912.8046-0.0886.2191-0.1619-1.28-0.38060.6247-0.1268-0.8539-0.24840.62090.19880.2747-0.01220.05480.5121-0.01680.34498.391565.2908-36.7542
314.36350.7848-1.44672.93020.40973.4658-0.0348-0.1156-0.0095-0.03490.0532-0.09670.21170.2732-0.02640.34260.0234-0.03810.32460.00360.42156.673557.8067-44.2614
329.51170.40880.89133.8273-0.32576.2112-0.01160.22580.653-0.1917-0.05640.7053-0.7073-0.3675-0.17010.3904-0.0620.04210.36150.05220.43949.235470.3032-48.2133
334.62942.7936-1.51443.3521-1.46065.22870.07340.05860.3097-0.58020.03080.6910.70620.0209-0.22850.3726-0.0069-0.06320.37030.02850.5156-5.352153.6882-48.0417
344.7720.3952-3.12674.9972-3.40553.8168-0.0504-0.7746-0.54660.647-0.28190.1525-0.0885-0.56430.20380.5978-0.18680.04960.82980.06050.591-37.195749.9854-14.2007
353.51510.418-3.92353.4173-3.81988.44690.0653-0.14360.00750.24310.08160.77890.1935-0.9536-0.30550.4686-0.2280.05730.8080.03480.8273-42.483851.2087-23.182
368.9321-2.34340.11023.74770.76365.1285-0.86050.8757-1.09990.3160.56320.2165-0.4183-0.46870.24230.689-0.0160.1570.6453-0.01520.6559-38.418560.2597-9.5354
373.89390.84161.93277.85984.48928.79280.06470.09130.61380.0004-0.1304-0.0094-0.753-0.17410.00880.6082-0.05070.09730.6277-0.01690.8549-38.341468.6482-18.081
387.41852.40621.30847.61152.47564.5482-0.0871-0.7051.1331-0.2047-0.7419-0.0846-0.3404-1.15460.75750.5758-0.05020.08820.7545-0.02130.7933-44.090767.3803-21.3929
392.8251-2.4468-2.80692.07821.42248.02770.0548-0.0193-0.2710.40350.15750.4979-0.075-0.5543-0.22890.5064-0.13290.1230.7935-0.00390.8872-42.803657.6634-15.6561
402.6235-4.1625-0.13157.1328-1.28854.161-0.287-0.80120.91320.86090.4709-0.4357-1.4061-0.6622-0.32181.02230.06880.27050.8380.01140.8072-45.261672.8149-10.3605
411.9975-4.4425-1.99379.96676.20088.811-0.5069-0.03430.01520.72930.62850.89320.530.4887-0.00310.6073-0.1650.10870.7180.0280.5736-33.53152.6461-14.0522
429.1003-7.00095.56998.9028-4.92693.4560.2936-0.3651-0.72330.20670.51540.6192-0.04690.2083-0.77610.5657-0.14210.00430.9048-0.06850.6035-20.063153.884-11.3897
431.7753-1.4385-1.37492.6583-1.2767.00640.314-1.1406-0.13760.3349-0.036-0.0912-0.4260.6716-0.28150.5191-0.2462-0.05531.2423-0.03440.6201-12.631152.2787-13.2712
441.5324-0.8813-1.32641.65850.75713.56660.0327-0.9802-0.44970.3495-0.02980.06280.37330.26560.02980.6332-0.1652-0.08691.07170.20360.6589-14.603344.6073-17.7411
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 85 through 94 )
2X-RAY DIFFRACTION2chain 'A' and (resid 95 through 120 )
3X-RAY DIFFRACTION3chain 'A' and (resid 121 through 232 )
4X-RAY DIFFRACTION4chain 'B' and (resid 1 through 22 )
5X-RAY DIFFRACTION5chain 'B' and (resid 23 through 75 )
6X-RAY DIFFRACTION6chain 'B' and (resid 76 through 85 )
7X-RAY DIFFRACTION7chain 'B' and (resid 86 through 153 )
8X-RAY DIFFRACTION8chain 'C' and (resid 1 through 21 )
9X-RAY DIFFRACTION9chain 'C' and (resid 22 through 47 )
10X-RAY DIFFRACTION10chain 'C' and (resid 48 through 75 )
11X-RAY DIFFRACTION11chain 'C' and (resid 76 through 85 )
12X-RAY DIFFRACTION12chain 'C' and (resid 86 through 132 )
13X-RAY DIFFRACTION13chain 'C' and (resid 133 through 153 )
14X-RAY DIFFRACTION14chain 'D' and (resid 85 through 99 )
15X-RAY DIFFRACTION15chain 'D' and (resid 100 through 132 )
16X-RAY DIFFRACTION16chain 'D' and (resid 133 through 142 )
17X-RAY DIFFRACTION17chain 'D' and (resid 143 through 162 )
18X-RAY DIFFRACTION18chain 'D' and (resid 163 through 232 )
19X-RAY DIFFRACTION19chain 'E' and (resid 83 through 93 )
20X-RAY DIFFRACTION20chain 'E' and (resid 94 through 120 )
21X-RAY DIFFRACTION21chain 'E' and (resid 121 through 132 )
22X-RAY DIFFRACTION22chain 'E' and (resid 133 through 142 )
23X-RAY DIFFRACTION23chain 'E' and (resid 143 through 173 )
24X-RAY DIFFRACTION24chain 'E' and (resid 174 through 216 )
25X-RAY DIFFRACTION25chain 'E' and (resid 217 through 232 )
26X-RAY DIFFRACTION26chain 'F' and (resid 1 through 21 )
27X-RAY DIFFRACTION27chain 'F' and (resid 22 through 36 )
28X-RAY DIFFRACTION28chain 'F' and (resid 37 through 48 )
29X-RAY DIFFRACTION29chain 'F' and (resid 49 through 65 )
30X-RAY DIFFRACTION30chain 'F' and (resid 66 through 75 )
31X-RAY DIFFRACTION31chain 'F' and (resid 76 through 131 )
32X-RAY DIFFRACTION32chain 'F' and (resid 132 through 142 )
33X-RAY DIFFRACTION33chain 'F' and (resid 143 through 153 )
34X-RAY DIFFRACTION34chain 'G' and (resid 1 through 22 )
35X-RAY DIFFRACTION35chain 'G' and (resid 23 through 36 )
36X-RAY DIFFRACTION36chain 'G' and (resid 37 through 56 )
37X-RAY DIFFRACTION37chain 'G' and (resid 57 through 75 )
38X-RAY DIFFRACTION38chain 'G' and (resid 76 through 85 )
39X-RAY DIFFRACTION39chain 'G' and (resid 86 through 125 )
40X-RAY DIFFRACTION40chain 'G' and (resid 126 through 142 )
41X-RAY DIFFRACTION41chain 'G' and (resid 143 through 153 )
42X-RAY DIFFRACTION42chain 'H' and (resid 85 through 99 )
43X-RAY DIFFRACTION43chain 'H' and (resid 100 through 132 )
44X-RAY DIFFRACTION44chain 'H' and (resid 133 through 232 )

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