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- PDB-6vso: DengueV-2 Capsid Structure -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6vso
TitleDengueV-2 Capsid Structure
ComponentsCapsid premembrane protein
KeywordsVIRAL PROTEIN / Capsid / Inhibitor
Function / homology
Function and homology information


flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / host cell mitochondrion / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / viral capsid / double-stranded RNA binding / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport ...flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / host cell mitochondrion / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / viral capsid / double-stranded RNA binding / nucleoside-triphosphate phosphatase / channel activity / monoatomic ion transmembrane transport / clathrin-dependent endocytosis of virus by host cell / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / methyltransferase cap1 activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / protein dimerization activity / host cell perinuclear region of cytoplasm / symbiont-mediated suppression of host innate immune response / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / symbiont-mediated activation of host autophagy / RNA-directed RNA polymerase / serine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell nucleus / virion membrane / structural molecule activity / ATP hydrolysis activity / proteolysis / extracellular region / ATP binding / metal ion binding / membrane
Similarity search - Function
Arc Repressor Mutant, subunit A - #930 / Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus / : / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus non-structural protein NS4B ...Arc Repressor Mutant, subunit A - #930 / Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus / : / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus non-structural protein NS4B / Flavivirus non-structural protein NS4A / Flavivirus NS2B domain profile. / mRNA cap 0 and cap 1 methyltransferase (EC 2.1.1.56 and EC 2.1.1.57) domain profile. / Flavivirus non-structural protein NS2A / Flavivirus non-structural protein NS2A / Flavivirus NS3, petidase S7 / Peptidase S7, Flavivirus NS3 serine protease / Flavivirus NS3 protease (NS3pro) domain profile. / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / RNA-directed RNA polymerase, flavivirus / Flavivirus RNA-directed RNA polymerase, fingers and palm domains / Flavivirus capsid protein C / Flavivirus capsid protein C / Flavivirus non-structural Protein NS1 / Flavivirus non-structural protein NS1 / Envelope glycoprotein M, flavivirus / Envelope glycoprotein M superfamily, flavivirus / Flavivirus envelope glycoprotein M / Flavivirus polyprotein propeptide / Flavivirus polyprotein propeptide superfamily / Flavivirus polyprotein propeptide / Flavivirus envelope glycoprotein E, stem/anchor domain / : / Flavivirus NS3 helicase, C-terminal helical domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain superfamily / Flavivirus glycoprotein E, immunoglobulin-like domain / Flavivirus glycoprotein, immunoglobulin-like domain / Flavivirus glycoprotein central and dimerisation domain / Flavivirus glycoprotein, central and dimerisation domains / Flaviviral glycoprotein E, central domain, subdomain 1 / Flaviviral glycoprotein E, central domain, subdomain 2 / Ribosomal RNA methyltransferase, FtsJ domain / FtsJ-like methyltransferase / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Flaviviral glycoprotein E, dimerisation domain / DEAD box, Flavivirus / Flavivirus DEAD domain / helicase superfamily c-terminal domain / Immunoglobulin E-set / Arc Repressor Mutant, subunit A / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal / Helicase superfamily 1/2, ATP-binding domain / RNA-directed RNA polymerase, catalytic domain / RdRp of positive ssRNA viruses catalytic domain profile. / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
NITRATE ION / Genome polyprotein / Genome polyprotein
Similarity search - Component
Biological speciesDengue virus 2
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.001 Å
AuthorsWhite, M. / Xia, H. / Shi, P.
Funding support United States, 4items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI142759 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI127744 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI136126 United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI145617 United States
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2020
Title: A cocrystal structure of dengue capsid protein in complex of inhibitor.
Authors: Xia, H. / Xie, X. / Zou, J. / Noble, C.G. / Russell, W.K. / Holthauzen, L.M.F. / Choi, K.H. / White, M.A. / Shi, P.Y.
History
DepositionFeb 11, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 15, 2020Provider: repository / Type: Initial release
Revision 1.1Jul 29, 2020Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2Aug 12, 2020Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Oct 11, 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 / 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: Capsid premembrane protein
B: Capsid premembrane protein
C: Capsid premembrane protein
D: Capsid premembrane protein
E: Capsid premembrane protein
F: Capsid premembrane protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)57,91929
Polymers56,4036
Non-polymers1,51623
Water19811
1
A: Capsid premembrane protein
B: Capsid premembrane protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,2359
Polymers18,8012
Non-polymers4347
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5390 Å2
ΔGint-36 kcal/mol
Surface area8560 Å2
MethodPISA
2
C: Capsid premembrane protein
D: Capsid premembrane protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,1117
Polymers18,8012
Non-polymers3105
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5260 Å2
ΔGint-44 kcal/mol
Surface area8370 Å2
MethodPISA
3
E: Capsid premembrane protein
F: Capsid premembrane protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)19,57313
Polymers18,8012
Non-polymers77211
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5940 Å2
ΔGint-37 kcal/mol
Surface area8480 Å2
MethodPISA
Unit cell
Length a, b, c (Å)142.000, 142.000, 67.000
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number152
Space group name H-MP3121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 24 through 27 or (resid 28...
21(chain C and (resid 24 through 40 or (resid 41...
31(chain E and (resid 24 through 27 or (resid 28...
12(chain C and (resid 23 through 26 or (resid 27...
22(chain D and (resid 23 through 27 or (resid 28...
32(chain F and (resid 23 through 26 or (resid 27...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111SERSERGLNGLN(chain A and (resid 24 through 27 or (resid 28...AA24 - 275 - 8
121GLNGLNGLNGLN(chain A and (resid 24 through 27 or (resid 28...AA289
131VALVALARGARG(chain A and (resid 24 through 27 or (resid 28...AA23 - 994 - 80
141VALVALARGARG(chain A and (resid 24 through 27 or (resid 28...AA23 - 994 - 80
151VALVALARGARG(chain A and (resid 24 through 27 or (resid 28...AA23 - 994 - 80
161VALVALARGARG(chain A and (resid 24 through 27 or (resid 28...AA23 - 994 - 80
211SERSERGLYGLY(chain C and (resid 24 through 40 or (resid 41...CC24 - 405 - 21
221ARGARGARGARG(chain C and (resid 24 through 40 or (resid 41...CC4122
231VALVALARGARG(chain C and (resid 24 through 40 or (resid 41...CC23 - 984 - 79
241VALVALARGARG(chain C and (resid 24 through 40 or (resid 41...CC23 - 984 - 79
251VALVALARGARG(chain C and (resid 24 through 40 or (resid 41...CC23 - 984 - 79
261VALVALARGARG(chain C and (resid 24 through 40 or (resid 41...CC23 - 984 - 79
271VALVALARGARG(chain C and (resid 24 through 40 or (resid 41...CC23 - 984 - 79
311SERSERGLNGLN(chain E and (resid 24 through 27 or (resid 28...EE24 - 275 - 8
321GLNGLNGLNGLN(chain E and (resid 24 through 27 or (resid 28...EE289
331VALVALARGARG(chain E and (resid 24 through 27 or (resid 28...EE23 - 984 - 79
341VALVALARGARG(chain E and (resid 24 through 27 or (resid 28...EE23 - 984 - 79
351VALVALARGARG(chain E and (resid 24 through 27 or (resid 28...EE23 - 984 - 79
361VALVALARGARG(chain E and (resid 24 through 27 or (resid 28...EE23 - 984 - 79
112VALVALVALVAL(chain C and (resid 23 through 26 or (resid 27...CC23 - 264 - 7
122GLNGLNGLNGLN(chain C and (resid 23 through 26 or (resid 27...CC27 - 288 - 9
132VALVALARGARG(chain C and (resid 23 through 26 or (resid 27...CC23 - 984 - 79
142VALVALARGARG(chain C and (resid 23 through 26 or (resid 27...CC23 - 984 - 79
152VALVALARGARG(chain C and (resid 23 through 26 or (resid 27...CC23 - 984 - 79
162VALVALARGARG(chain C and (resid 23 through 26 or (resid 27...CC23 - 984 - 79
212VALVALGLNGLN(chain D and (resid 23 through 27 or (resid 28...DD23 - 274 - 8
222GLNGLNGLNGLN(chain D and (resid 23 through 27 or (resid 28...DD289
232ARGARGARGARG(chain D and (resid 23 through 27 or (resid 28...DD22 - 993 - 80
242ARGARGARGARG(chain D and (resid 23 through 27 or (resid 28...DD22 - 993 - 80
252ARGARGARGARG(chain D and (resid 23 through 27 or (resid 28...DD22 - 993 - 80
262ARGARGARGARG(chain D and (resid 23 through 27 or (resid 28...DD22 - 993 - 80
312VALVALVALVAL(chain F and (resid 23 through 26 or (resid 27...FF23 - 264 - 7
322GLNGLNGLNGLN(chain F and (resid 23 through 26 or (resid 27...FF27 - 288 - 9
332ASNASNARGARG(chain F and (resid 23 through 26 or (resid 27...FF21 - 992 - 80
342ASNASNARGARG(chain F and (resid 23 through 26 or (resid 27...FF21 - 992 - 80
352ASNASNARGARG(chain F and (resid 23 through 26 or (resid 27...FF21 - 992 - 80
362ASNASNARGARG(chain F and (resid 23 through 26 or (resid 27...FF21 - 992 - 80

NCS ensembles :
ID
1
2

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Components

#1: Protein
Capsid premembrane protein


Mass: 9400.506 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Dengue virus 2 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: A0A2D2BF61, UniProt: P07564*PLUS
#2: Chemical
ChemComp-NO3 / NITRATE ION


Mass: 62.005 Da / Num. of mol.: 20 / Source method: obtained synthetically / Formula: NO3
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Formula: H2O
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: 3.49 Å3/Da / Density % sol: 64.8 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.2 / Details: 3.0 M NaNO3, 100 mM HEPES pH 7.2, 5% glycerol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 21-ID-G / Wavelength: 0.97857 Å
DetectorType: RAYONIX MX300-HS / Detector: CCD / Date: Jun 13, 2018 / Details: Be lenses
RadiationMonochromator: C(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97857 Å / Relative weight: 1
ReflectionResolution: 3→50 Å / Num. obs: 15870 / % possible obs: 100 % / Redundancy: 11.1 % / Rmerge(I) obs: 0.132 / Rpim(I) all: 0.042 / Rrim(I) all: 0.139 / Χ2: 0.937 / Net I/av σ(I): 19.722 / Net I/σ(I): 5 / Num. measured all: 176644
Reflection shell

Diffraction-ID: 1 / % possible all: 100

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2CC starRpim(I) allRrim(I) allΧ2
3-3.0511.10.9262.837850.9390.9840.290.970.871
3.05-3.1111.20.8672.957830.9290.9810.270.9080.838
3.11-3.1711.20.8483.147750.9130.9770.2650.8890.888
3.17-3.2311.30.7143.797770.9470.9860.2220.7480.881
3.23-3.311.20.5065.367920.9680.9920.1580.530.942
3.3-3.3811.20.4575.917860.9750.9940.1420.4790.962
3.38-3.4611.30.3777.067760.9780.9940.1170.3950.923
3.46-3.5611.30.3527.97940.9870.9940.1090.3690.956
3.56-3.6611.30.2859.917830.9820.9960.0880.2981.003
3.66-3.7811.20.23112.17810.9880.9970.0720.2421.009
3.78-3.9111.30.20313.168040.9920.9980.0630.2130.959
3.91-4.0711.30.15716.987800.9940.9990.0490.1650.975
4.07-4.2611.20.13419.347990.9960.9990.0420.1410.985
4.26-4.4811.20.12621.737910.9950.9990.0390.1321.042
4.48-4.7611.20.12423.447990.9950.9990.0390.131.172
4.76-5.1311.10.10825.417960.9950.9990.0340.1141.136
5.13-5.6411.10.10124.687860.9960.9990.0320.1060.952
5.64-6.46110.09125.888090.9970.9990.0290.0960.877
6.46-8.1310.90.04840.378170.99810.0150.0510.734
8.13-50100.03347.658570.9970.9990.0110.0350.61

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation4.11 Å48.73 Å
Translation4.11 Å48.73 Å

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Processing

Software
NameVersionClassification
PHENIX1.16_3549refinement
HKL-20002.3.12data scaling
PHASER2.8.1phasing
PDB_EXTRACT3.22data extraction
HKL-20002.3.12data reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6VG5

6vg5


Resolution: 3.001→45.302 Å / SU ML: 0.35 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 21.37 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2246 1442 10.05 %Random
Rwork0.1858 12906 --
obs0.1896 14348 90.78 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 121.83 Å2 / Biso mean: 55.3994 Å2 / Biso min: 18.42 Å2
Refinement stepCycle: final / Resolution: 3.001→45.302 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3592 0 98 11 3701
Biso mean--73.67 37.27 -
Num. residues----464
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A903X-RAY DIFFRACTION7.633TORSIONAL
12C903X-RAY DIFFRACTION7.633TORSIONAL
13E903X-RAY DIFFRACTION7.633TORSIONAL
21C891X-RAY DIFFRACTION7.633TORSIONAL
22D891X-RAY DIFFRACTION7.633TORSIONAL
23F891X-RAY DIFFRACTION7.633TORSIONAL
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.0012-3.10840.2744740.2324656X-RAY DIFFRACTION47
3.1084-3.23290.32941000.2362895X-RAY DIFFRACTION64
3.2329-3.37990.26041520.21991352X-RAY DIFFRACTION95
3.3799-3.55810.28741570.22511400X-RAY DIFFRACTION100
3.5581-3.78090.22171600.18451407X-RAY DIFFRACTION100
3.7809-4.07260.20871590.17911415X-RAY DIFFRACTION100
4.0726-4.48220.20311620.15951434X-RAY DIFFRACTION100
4.4822-5.130.18411560.15831414X-RAY DIFFRACTION100
5.13-6.46020.22841620.20151441X-RAY DIFFRACTION100
6.4602-45.3020.211600.17461492X-RAY DIFFRACTION100
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)
10.14430.24430.04450.42860.08740.0246-0.00350.00620.00480.0048-0.0109-0.0129-0.02550.0006-0.00060.76260.0934-0.12910.8634-0.00510.940620.31275.5662.732
20.00010.0002-0.00040.0035-0.00090.0006-0.00740.01120.0136-0.0111-0.00950.0189-0.00560.0055-0.00010.4390.1603-0.0560.65150.03260.506517.90980.8631.763
30.0002-0.00190.00370.0106-0.01190.01420.0150.04310.010.0027-0.005-0.0011-0.0254-0.00320.00880.42790.3196-0.20260.3211-0.08090.545813.28589.384.311
40.023-0.0211-0.01170.02780.01230.02570.0287-0.0157-0.0207-0.0286-0.01130.00880.02330.0101-0.01340.41970.48990.06210.13330.14330.190715.8690.95713.339
50.01030.0079-0.0130.0279-0.02030.02040.00630.01310.0134-0.0148-0.0104-0.0613-0.04860.0301-0.01840.45820.25790.00720.0751-0.05770.233920.79299.15511.987
60.00590.00860.00910.0175-0.00940.0243-0.0185-0.1055-0.06570.0019-0.0423-0.0034-0.0030.05960.00040.45670.27530.05360.44060.10790.348316.02290.1822.26
70.00440.00880.00970.0320.03360.03940.034-0.0149-0.0642-0.0030.0118-0.0555-0.0325-0.0360.01320.22910.16250.01860.45090.12750.470135.21278.9421.125
80.0015-0.0004-0.00560.0020.00630.0224-0.0262-0.00520.0428-0.0002-0.0109-0.03260.0008-0.0027-0.00470.37870.16810.13950.3580.00910.460919.238104.3565.817
90.020.00540.01880.00430.01270.0294-0.03430.01190.02730.0151-0.00520.0151-0.05150.03840.00340.41930.22920.00960.15360.23460.380424.4595.2750.082
100.0301-0.0003-0.00760.00090.00010.0024-0.0182-0.03310.02390.0159-0.0032-0.0109-0.01460.04330.00460.43210.33780.05120.60530.21710.451233.07988.0763.974
110.0294-0.01420.01020.0185-0.00160.00540.01730.0146-0.0312-0.0572-0.0307-0.04730.01780.04120.01570.37390.37580.09860.01290.16090.161726.28182.97610.471
120.02510.02270.02710.0210.02270.02560.01850.0058-0.01410.01120.0192-0.0619-0.02530.0398-0.01430.36860.42760.03280.4815-0.12110.34437.98282.18310.574
13-0.00010.001400.00570.0030.0019-0.0111-0.02360.05890.0413-0.01330.0054-0.06430.030800.48440.165-0.03250.60220.04280.456731.75291.10621.745
140.00210.0018-0.00160.00460.00150.00290.0226-0.03190.02090.02480.0154-0.0511-0.0346-0.0112-00.53790.26880.00050.487-0.05430.262817.98597.72326.719
150.00460.00260.00160.0022-0.00080.0021-0.01690.0054-0.00740.00530.01640.00110.0064-0.00590.00010.87140.0466-0.0250.53870.08760.496619.579.341-6.834
160.0049-0.01230.00010.0351-0.01010.0051-0.0394-0.0099-0.03660.0113-0.0527-0.03390.00160.0176-0.06420.4810.39930.05530.3056-0.04970.40231.45781.109-9.845
170.00320.00220.00070.00110.00230.00280.08220.0024-0.00190.06410.0017-0.0463-0.04670.01670.00010.4530.1635-0.03660.5005-0.0830.277832.65583.558-18.703
180.00080.0018-0.00020.0025-0.00060.00380.05480.0038-0.0030.02480.0562-0.025-0.04270.045200.52140.02510.01510.56690.04680.522335.51192.654-18.215
190.00320.002-00.00170.00110.00090.02770.0136-0.01670.0203-0.036-0.0029-0.01970.0017-00.77060.09830.01621.0745-0.17190.924841.24682.975-23.399
200.00150.0025-0.00360.0068-0.00690.0014-0.01670.07510.0163-0.02230.01820.08430.00590.0366-0.00170.60530.2461-0.09150.5958-0.07590.311626.89282.955-30.148
210.0009-0.0001-0.00010.0003-0.00010.00220.0306-0.0307-0.00550.0182-0.0186-0.0112-0.01260.022100.48970.3037-0.00780.7874-0.02360.385510.85590.072-27.847
22-0.00020.00280.0005-0.0010.00130.0008-0.0076-0.00090.00780.03610.00330.0296-0.04960.0775-00.40870.07250.03480.3239-0.11470.454432.89892.725-8.154
230.0017-0.0025-0.0030.00180.0030.0033-0.0185-0.00760.0156-0.0142-0.0225-0.0292-0.01530.01400.7820.144-0.05690.75650.11110.419219.04395.535-10.552
240.0005-0.0004-0.00070.0021-0.00220.0047-0.0178-0.0387-0.0441-0.02-0.04780.0183-0.04390.0407-00.56070.28510.03370.58170.01550.459620.24289.766-17.264
250.00560.00220.00130.0034-0.00260.0048-0.0019-0.041-0.01620.0168-0.00510.0171-0.0253-0.0353-00.4784-0.10140.11680.6354-0.07850.48417.72483.63-14.702
260.00610.0059-0.0060.0082-0.00550.0276-0.0508-0.01810.0099-0.0024-0.01640.0458-0.00070.0058-0.00080.88060.3575-0.01670.67260.05470.617710.85995.932-17.721
270.0016-0.00060.0009-0.0005-0.00030.0058-0.0120.03860.02120.05170.0247-0.0256-0.0380.0105-00.54240.17-0.01330.4391-0.05070.365422.18395.699-27.967
280.004-0.00030.0025-0.0002-0.00050.0034-0.02920.0188-0.0001-0.0146-0.0233-0.01580.0098-0.0068-00.68580.23970.07770.8145-0.09110.452436.47388.865-33.05
290.03510.0303-0.05070.0262-0.04370.07450.0352-0.0190.0001-0.01510.04970.0064-0.0127-0.02920.0210.26920.24620.12540.55060.1530.455143.54962.2766.127
300.00190.00190.00030.00690.00160.0001-0.01790.0120.0142-0.0133-0.0173-0.01270.0021-0.0005-0.0150.23390.13860.17570.45440.00410.583846.42555.2627.8
310.02360.0220.00820.02870.00770.00080.0056-0.0098-0.01160.0490.05920.0311-0.01810.06650.06790.10940.4374-0.08660.2059-0.160.219243.16655.96416.205
32-0.0009-0.0113-0.00270.0243-0.00550.00190.0256-0.00270.00110.02370.0432-0.06650.11320.05610.03640.2350.427-0.04850.233-0.15860.380641.36448.73817.219
330.01160.0009-0.0160.00140.00080.0285-0.0058-0.05120.0313-0.0225-0.0740.1034-0.07390.0399-0.0430.15630.2428-0.00730.2736-0.02070.237140.09760.17927.469
340.0557-0.0322-0.03070.02840.01230.02010.02740.00080.0416-0.0255-0.011-0.0489-0.0229-0.02770.00080.36280.33640.11580.2362-0.02010.237924.73369.70324.459
350.00480.0007-0.00190.0054-0.00280.0017-0.0029-0.02560.0074-0.0235-0.0137-0.00080-0.0043-0.00790.38410.27250.0080.15360.0760.47539.24143.7648.312
360.0134-0.00740.00830.015-0.00250.0077-0.0043-0.0168-0.0398-0.0119-0.01040.01610.0168-0.04690.00530.16510.1435-0.00670.49560.02160.576134.10553.4673.337
370.00540.0051-0.00240.0215-0.00150.0099-0.0275-0.0118-0.0352-0.0164-0.03060.0572-0.0006-0.0015-0.02360.37960.35690.0070.4615-0.18130.154826.00360.9146.943
380.0109-0.0157-0.01660.02060.0210.02890.05340.027-0.00780.009-0.0506-0.0028-0.02750.02250.01270.36330.2797-0.05790.35750.07280.40432.94465.14913.381
390.00390.00110.00130.00180.00030.0002-0.0208-0.002-0.0019-0.0273-0.03130.0759-0.0245-0.0521-0.02590.19560.30410.04570.40620.05820.313420.5866.50714.061
400.02920.0181-0.01210.0114-0.01090.0108-0.0459-0.0343-0.0211-0.032-0.12390.0388-0.0901-0.078-0.0370.21380.16090.06160.26170.07090.211527.05357.18224.791
410.00880.005-0.00580.0067-0.0020.01490.0003-0.0087-0.0290.0163-0.0254-0.01430.03590.0179-0.00260.28730.34220.00110.29590.03230.401140.50348.88630.16
420.01410.0095-0.00210.02730.01270.0107-0.01720.01530.0025-0.008-0.0321-0.0129-0.0075-0.0219-0.02230.41230.11590.25040.4910.00240.388340.69569.185.201
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 23:25 )A23 - 25
2X-RAY DIFFRACTION2( CHAIN A AND RESID 26:30 )A26 - 30
3X-RAY DIFFRACTION3( CHAIN A AND RESID 31:39 )A31 - 39
4X-RAY DIFFRACTION4( CHAIN A AND RESID 40:54 )A40 - 54
5X-RAY DIFFRACTION5( CHAIN A AND RESID 55:66 )A55 - 66
6X-RAY DIFFRACTION6( CHAIN A AND RESID 67:89 )A67 - 89
7X-RAY DIFFRACTION7( CHAIN A AND RESID 90:99 )A90 - 99
8X-RAY DIFFRACTION8( CHAIN B AND RESID 21:27 )B21 - 27
9X-RAY DIFFRACTION9( CHAIN B AND RESID 28:36 )B28 - 36
10X-RAY DIFFRACTION10( CHAIN B AND RESID 37:45 )B37 - 45
11X-RAY DIFFRACTION11( CHAIN B AND RESID 46:64 )B46 - 64
12X-RAY DIFFRACTION12( CHAIN B AND RESID 65:76 )B65 - 76
13X-RAY DIFFRACTION13( CHAIN B AND RESID 77:89 )B77 - 89
14X-RAY DIFFRACTION14( CHAIN B AND RESID 90:98 )B90 - 98
15X-RAY DIFFRACTION15( CHAIN C AND RESID 23:28 )C23 - 28
16X-RAY DIFFRACTION16( CHAIN C AND RESID 29:39 )C29 - 39
17X-RAY DIFFRACTION17( CHAIN C AND RESID 40:54 )C40 - 54
18X-RAY DIFFRACTION18( CHAIN C AND RESID 55:66 )C55 - 66
19X-RAY DIFFRACTION19( CHAIN C AND RESID 67:73 )C67 - 73
20X-RAY DIFFRACTION20( CHAIN C AND RESID 74:89 )C74 - 89
21X-RAY DIFFRACTION21( CHAIN C AND RESID 90:98 )C90 - 98
22X-RAY DIFFRACTION22( CHAIN D AND RESID 22:36 )D22 - 36
23X-RAY DIFFRACTION23( CHAIN D AND RESID 37:45 )D37 - 45
24X-RAY DIFFRACTION24( CHAIN D AND RESID 46:55 )D46 - 55
25X-RAY DIFFRACTION25( CHAIN D AND RESID 56:65 )D56 - 65
26X-RAY DIFFRACTION26( CHAIN D AND RESID 66:76 )D66 - 76
27X-RAY DIFFRACTION27( CHAIN D AND RESID 77:89 )D77 - 89
28X-RAY DIFFRACTION28( CHAIN D AND RESID 90:99 )D90 - 99
29X-RAY DIFFRACTION29( CHAIN E AND RESID 29:33 )E29 - 33
30X-RAY DIFFRACTION30( CHAIN E AND RESID 34:39 )E34 - 39
31X-RAY DIFFRACTION31( CHAIN E AND RESID 40:54 )E40 - 54
32X-RAY DIFFRACTION32( CHAIN E AND RESID 55:73 )E55 - 73
33X-RAY DIFFRACTION33( CHAIN E AND RESID 74:89 )E74 - 89
34X-RAY DIFFRACTION34( CHAIN E AND RESID 90:98 )E90 - 98
35X-RAY DIFFRACTION35( CHAIN F AND RESID 21:27 )F21 - 27
36X-RAY DIFFRACTION36( CHAIN F AND RESID 28:36 )F28 - 36
37X-RAY DIFFRACTION37( CHAIN F AND RESID 37:45 )F37 - 45
38X-RAY DIFFRACTION38( CHAIN F AND RESID 46:65 )F46 - 65
39X-RAY DIFFRACTION39( CHAIN F AND RESID 66:76 )F66 - 76
40X-RAY DIFFRACTION40( CHAIN F AND RESID 77:89 )F77 - 89
41X-RAY DIFFRACTION41( CHAIN F AND RESID 90:99 )F90 - 99
42X-RAY DIFFRACTION42( CHAIN E AND RESID 23:28 )E23 - 28

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