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- PDB-6l50: Crystal structure of Zika NS2B-NS3 protease with compound 16 -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6l50
TitleCrystal structure of Zika NS2B-NS3 protease with compound 16
Components
  • NS3 protease
  • Serine protease subunit NS2B
KeywordsVIRAL PROTEIN / Viral protease / Protease inhibitor complex
Function / homology
Function and homology information


flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / ribonucleoside triphosphate phosphatase activity / viral capsid / double-stranded RNA binding / nucleoside-triphosphate phosphatase / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / symbiont-mediated suppression of host toll-like receptor signaling pathway ...flavivirin / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity / ribonucleoside triphosphate phosphatase activity / viral capsid / double-stranded RNA binding / nucleoside-triphosphate phosphatase / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity / symbiont-mediated suppression of host toll-like receptor signaling pathway / mRNA (guanine-N7)-methyltransferase / methyltransferase cap1 / clathrin-dependent endocytosis of virus by host cell / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / host cell perinuclear region of cytoplasm / protein dimerization activity / host cell endoplasmic reticulum membrane / RNA helicase / symbiont-mediated suppression of host innate immune response / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / induction by virus of host autophagy / symbiont entry into host cell / RNA-directed RNA polymerase / viral RNA genome replication / serine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / lipid binding / viral envelope / host cell nucleus / virion attachment to host cell / GTP binding / structural molecule activity / virion membrane / ATP hydrolysis activity / proteolysis / extracellular region / ATP binding / membrane / metal ion binding
Similarity search - Function
Thrombin, subunit H - #120 / Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus / : / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase ...Thrombin, subunit H - #120 / Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus / : / Flavivirus non-structural protein NS4A / Flavivirus non-structural protein NS2B / Flavivirus capsid protein C / Flavivirus non-structural protein NS4B / mRNA cap 0/1 methyltransferase / Flavivirus capsid protein C / 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 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 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 / : / Flavivirus NS3 helicase, C-terminal helical domain / 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 / Trypsin-like serine proteases / Immunoglobulin E-set / 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 / Thrombin, subunit H / 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 / DNA/RNA polymerase superfamily / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
2-sulfanylidene-1,3-thiazolidin-4-one / Genome polyprotein / Genome polyprotein
Similarity search - Component
Biological speciesZika virus
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.95 Å
AuthorsQuek, J.P.
Funding support Singapore, 3items
OrganizationGrant numberCountry
Other governmentStart up grant Singapore
Other governmentCBRG15May045 Singapore
Other governmentNRF2016NRF-CRP001-063 Singapore
CitationJournal: Antiviral Res. / Year: 2020
Title: Identification and structural characterization of small molecule fragments targeting Zika virus NS2B-NS3 protease.
Authors: Quek, J.P. / Liu, S. / Zhang, Z. / Li, Y. / Ng, E.Y. / Loh, Y.R. / Hung, A.W. / Luo, D. / Kang, C.
History
DepositionOct 21, 2019Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jul 15, 2020Provider: repository / Type: Initial release
Revision 1.1Nov 22, 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: Serine protease subunit NS2B
B: NS3 protease
C: Serine protease subunit NS2B
D: NS3 protease
E: Serine protease subunit NS2B
F: NS3 protease
G: Serine protease subunit NS2B
H: NS3 protease
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,7459
Polymers99,6128
Non-polymers1331
Water1,27971
1
A: Serine protease subunit NS2B
B: NS3 protease


Theoretical massNumber of molelcules
Total (without water)24,9032
Polymers24,9032
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3850 Å2
ΔGint-28 kcal/mol
Surface area9120 Å2
MethodPISA
2
C: Serine protease subunit NS2B
D: NS3 protease


Theoretical massNumber of molelcules
Total (without water)24,9032
Polymers24,9032
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3720 Å2
ΔGint-28 kcal/mol
Surface area8650 Å2
MethodPISA
3
E: Serine protease subunit NS2B
F: NS3 protease


Theoretical massNumber of molelcules
Total (without water)24,9032
Polymers24,9032
Non-polymers00
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3560 Å2
ΔGint-26 kcal/mol
Surface area9080 Å2
MethodPISA
4
G: Serine protease subunit NS2B
H: NS3 protease
hetero molecules


Theoretical massNumber of molelcules
Total (without water)25,0363
Polymers24,9032
Non-polymers1331
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3900 Å2
ΔGint-24 kcal/mol
Surface area9730 Å2
MethodPISA
Unit cell
Length a, b, c (Å)59.744, 59.909, 214.833
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and resid 51 through 87)
21chain C
31chain E
41(chain G and resid 51 through 87)
12(chain B and (resid 19 through 29 or resid 32 through 169))
22(chain D and (resid 19 through 29 or resid 32 through 169))
32(chain F and resid 19 through 169)
42(chain H and resid 19 through 169)

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
111METMETVALVAL(chain A and resid 51 through 87)AA51 - 878 - 44
211METMETVALVALchain CCC51 - 878 - 44
311METMETVALVALchain EEE51 - 878 - 44
411METMETVALVAL(chain G and resid 51 through 87)GG51 - 878 - 44
112THRTHRARGARG(chain B and (resid 19 through 29 or resid 32 through 169))BB19 - 2920 - 30
122GLYGLYLYSLYS(chain B and (resid 19 through 29 or resid 32 through 169))BB32 - 16933 - 170
212THRTHRARGARG(chain D and (resid 19 through 29 or resid 32 through 169))DD19 - 2920 - 30
222GLYGLYLYSLYS(chain D and (resid 19 through 29 or resid 32 through 169))DD32 - 16933 - 170
312THRTHRLYSLYS(chain F and resid 19 through 169)FF19 - 16920 - 170
412THRTHRLYSLYS(chain H and resid 19 through 169)HH19 - 16920 - 170

NCS ensembles :
ID
1
2

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Components

#1: Protein
Serine protease subunit NS2B / NS2B cofactor


Mass: 5865.384 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Zika virus / Production host: Escherichia coli (E. coli)
References: UniProt: Q32ZE1, flavivirin, nucleoside-triphosphate phosphatase, RNA helicase, mRNA (guanine-N7)-methyltransferase, methyltransferase cap1, RNA-directed RNA polymerase
#2: Protein
NS3 protease


Mass: 19037.592 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Zika virus (strain Mr 766) / Strain: Mr 766 / Gene: GP1, A2G93_63394gpGP1 / Production host: Escherichia coli (E. coli) / References: UniProt: A0A142IX72, UniProt: Q32ZE1*PLUS
#3: Chemical ChemComp-E60 / 2-sulfanylidene-1,3-thiazolidin-4-one


Mass: 133.192 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H3NOS2 / Feature type: SUBJECT OF INVESTIGATION
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 71 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

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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: 1.93 Å3/Da / Density % sol: 36.26 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop
Details: 0.2 M Ammonium sulfate, 0.1 M Sodium acetate trihydrate pH 4.6, 30% PEG2000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX1 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 210r / Detector: CCD / Date: Feb 28, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
Reflection twinOperator: k,h,-l / Fraction: 0.43
ReflectionResolution: 1.95→42.304 Å / Num. obs: 56428 / % possible obs: 98.46 % / Redundancy: 7.4 % / CC1/2: 0.977 / Rpim(I) all: 0.09903 / Rrim(I) all: 0.2698 / Net I/σ(I): 27.73
Reflection shellResolution: 1.95→2.02 Å / Mean I/σ(I) obs: 3.2 / Num. unique obs: 5506 / CC1/2: 0.586 / Rpim(I) all: 0.2515 / Rrim(I) all: 0.6946

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Processing

Software
NameVersionClassification
PHENIX1.16_3549refinement
Aimlessdata scaling
PDB_EXTRACT3.25data extraction
iMOSFLMdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5gpi

5gpi


Resolution: 1.95→42.304 Å / Cross valid method: NONE / σ(F): 10.5 / Phase error: 42.89
RfactorNum. reflection% reflection
Rfree0.2348 2006 3.56 %
Rwork0.2149 --
obs0.2229 56423 98.48 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 79.1 Å2 / Biso mean: 31.6319 Å2 / Biso min: 10.51 Å2
Refinement stepCycle: final / Resolution: 1.95→42.304 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5629 0 7 71 5707
Biso mean--35.19 26.25 -
Num. residues----759
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A440X-RAY DIFFRACTION2.818TORSIONAL
12C440X-RAY DIFFRACTION2.818TORSIONAL
13E440X-RAY DIFFRACTION2.818TORSIONAL
14G440X-RAY DIFFRACTION2.818TORSIONAL
21B1788X-RAY DIFFRACTION2.818TORSIONAL
22D1788X-RAY DIFFRACTION2.818TORSIONAL
23F1788X-RAY DIFFRACTION2.818TORSIONAL
24H1788X-RAY DIFFRACTION2.818TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
1.95-1.99880.27061420.2904384194
1.9988-2.05280.24831370.2917375694
2.0528-2.11320.32281380.3164379494
2.1132-2.18140.28461380.2736382295
2.1814-2.25940.28161410.2774381594
2.2594-2.34990.26271410.2614384995
2.3499-2.45680.2831450.2614384095
2.4568-2.58630.30451450.264385595
2.5863-2.74830.23891400.2515389595
2.7483-2.96050.25641420.2304388295
2.9605-3.25830.25061430.216392795
3.2583-3.72950.25191440.2123395996
3.7295-4.69780.20821420.1822399396
4.6978-42.30.20141610.17419396
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)
12.62190.1461.8151.8648-0.85774.83380.2662-0.0056-0.1072-0.3429-0.2480.0848-0.741-0.4842-0.0110.49570.0738-0.06290.2921-0.09250.1957-3.6964-1.637844.3379
21.4761-1.30851.74985.3243-2.46249.1734-0.0701-0.50360.04750.4704-0.11820.25210.1043-0.23080.09310.5137-0.080.10580.5782-0.01610.295.1629-13.810559.0721
31.0422-0.2299-0.93571.7390.22952.6818-0.01090.070.1247-0.38990.18160.0236-0.0853-0.1016-0.04680.77940.06820.28840.7190.1350.345-3.6968-20.26260.0743
40.82651.64910.0883.29330.09061.37910.0138-0.0429-0.0796-0.0495-0.13790.14440.09770.09890.01370.3397-0.00060.05530.23540.16680.66-5.018-32.366449.3999
50.4340.13410.44480.64140.02880.7962-0.16240.1057-0.0242-0.0091-0.01680.0181-0.1719-0.0491-0.07530.1488-0.1527-0.10060.5163-0.20890.1533-8.7023-28.493734.4648
63.5177-0.26180.43791.61040.46822.1125-0.19650.01920.39610.05420.3128-0.3461-0.19310.2436-0.08380.4456-0.10550.06260.3353-0.16310.2357-2.0529-2.3744.0316
71.16960.4912-1.06980.9714-0.07562.01010.02330.60260.1973-0.14870.00410.1714-0.1682-0.1341-0.13840.3722-0.03820.0790.2689-0.03660.2134-9.8421-4.106141.6854
81.23340.4067-0.45861.849-0.89410.97910.11010.09270.06310.3771-0.0190.3725-0.29370.3853-0.00170.33350.00130.01320.2711-0.03120.1180.8621-11.032136.4375
90.5278-0.14570.10281.78640.94461.9043-0.01460.0953-0.00110.2368-0.0718-0.03-0.0068-0.08730.12620.31490.05960.05280.31560.04170.1421-3.0849-20.049446.8907
100.9038-0.3640.2671.0272-1.53223.87570.06570.08750.0965-0.06320.13420.0479-0.33920.0755-0.06290.4391-0.00310.07710.2411-0.01360.0522-27.1157-3.538160.855
111.8961-0.61590.10732.64890.17381.3301-0.19410.39740.145-0.38470.2676-0.5041-0.1797-0.41870.1070.4506-0.14240.01380.3691-0.18680.1914-28.4049-24.887451.9374
122.0537-0.5477-0.7450.9948-1.13532.5874-0.1034-0.3449-0.35910.72960.0912-0.4895-0.17240.14930.13450.2719-0.0397-0.0750.27830.04920.3018-19.9132-28.908472.761
131.2871-0.0236-0.78080.38890.04721.92530.3239-0.10970.390.1192-0.1180.0482-0.25640.2405-0.18760.36-0.05960.05620.214-0.02370.1708-25.1724-7.097269.85
140.5137-0.17110.40921.69210.19140.71530.07530.1308-0.0878-0.2768-0.01670.01070.0340.0756-0.02720.4428-0.02050.0010.2133-0.00420.101-28.0271-20.708460.8335
152.07020.3066-0.50153.84482.032.4420.1292-0.08990.3468-0.0470.06290.1983-0.2365-0.5648-0.4860.24510.14110.11280.38090.15740.1652-10.4468-8.21949.3809
163.07251.12-0.28351.2611-0.68880.4306-0.05870.6668-0.4186-0.95370.08710.32440.3593-0.1319-0.2070.50650.0362-0.25470.2302-0.03230.31031.6875-18.9356-2.8229
170.64070.44520.12050.6471-0.37162.4154-0.16050.16560.0858-0.320.2280.0558-0.0642-0.3887-0.0490.5990.08530.07520.46080.16070.129813.8793-10.0532-4.1779
180.0357-0.0853-0.23240.91110.27131.87470.1765-0.1460.18260.1917-0.1353-0.251-0.34110.23480.04370.2348-0.13550.03730.4488-0.03450.144618.9441-6.21216.3872
190.55640.1590.423.20590.50592.1266-0.0204-0.12030.0750.2867-0.02910.14550.0359-0.4333-0.05140.02990.0788-0.08790.41490.10220.1129-7.8285-11.84278.1822
202.88151.243-1.30231.4769-0.91182.7691-0.0315-0.00320.49810.10630.20550.4538-0.053-0.2136-0.14730.0756-0.07920.03430.26690.12950.2352-6.5433-6.259410.0892
210.9719-0.1666-0.78572.58040.31191.73410.16220.0226-0.10220.1258-0.14940.0985-0.2497-0.38820.10350.24960.01570.03690.1946-0.00890.1151-5.3193-11.394718.5511
220.58750.0811-0.13570.35020.17590.14710.1623-0.0767-0.05680.0050.0044-0.0053-0.11550.03260.2680.2841-0.0419-0.05210.2410.08980.0593.2225-11.307120.6431
231.51110.4463-0.35480.75440.30250.3556-0.21390.53740.0850.22440.1717-0.0880.2457-0.09590.06280.27870.00950.03790.28610.08160.19025.4618-15.78294.8767
241.62120.6323-0.90531.79220.31890.90420.0659-0.0191-0.0463-0.0047-0.1584-0.07390.18610.38060.10960.16550.04230.03270.24570.07160.123214.5422-9.90899.5387
251.3957-0.7546-0.52863.35781.40031.97220.08230.1824-0.41590.03590.04110.08260.56340.21380.20690.21730.0565-0.03620.19430.04170.38936.1242-20.66324.5592
262.197-0.23280.62440.5381-0.81592.0078-0.1468-0.04440.30080.1254-0.1314-0.1363-0.27290.3069-0.13750.1952-0.0417-0.0690.21150.0438-0.11049.4399-9.640910.3131
273.8272-0.77891.742.00250.66063.1274-0.05830.30440.3223-0.3121-0.2895-0.35150.02720.24910.33250.23180.0595-0.05630.26050.07120.188213.6756-7.29389.5852
288.64230.84-0.32715.6738-0.10220.54290.3145-0.28060.70170.40630.20050.6101-0.3648-0.4156-0.26010.20880.04220.17670.67380.0960.4063-45.5616-36.652113.9428
290.0093-0.0678-0.05022.00550.30410.2565-0.0539-0.30210.0323-0.07180.17230.03820.00160.13910.02760.0813-0.03670.07280.33630.07460.3956-41.0688-47.2333.5939
305.8642-2.7326-2.33182.27772.38812.63190.0138-0.17310.1393-0.7564-0.18980.13120.05260.450.03020.50640.06360.02830.38490.08020.2246-31.2169-50.3021-5.3881
312.07342.9634-1.1425.1486-0.62522.2698-0.13270.38070.2474-0.4970.06610.13690.006-0.10350.07930.35010.07480.05190.61150.17280.3638-24.839-41.855-7.6132
320.047-0.1224-0.17811.30930.79381.8345-0.01330.1064-0.01270.3016-0.00290.03050.20640.18620.19060.3194-0.17510.05590.4445-0.00310.0679-13.1012-39.11032.7315
330.24510.2245-0.09290.2114-0.10370.0702-0-0.02920.22250.12930.1133-0.067-0.11730.0398-0.05770.299-0.0078-0.00430.28110.04580.1732-16.5384-34.367917.7713
342.77010.04840.13590.0508-0.45864.3670.1482-0.14290.29190.11860.21160.9626-0.3771-0.4791-0.34420.1661-0.03240.07090.32580.05160.3459-41.5348-39.373710.2501
350.55390.4039-1.15480.8246-0.32862.80260.01050.2677-0.0830.2974-0.02710.1072-0.0846-0.5698-0.02360.27510.02140.02710.2334-0.00680.2103-36.8153-42.329619.9572
360.5826-1.0365-0.10152.7361-1.1842.1434-0.14850.15440.2409-0.1753-0.2589-0.68510.2388-0.0452-0.0520.2108-0.1102-0.04690.2137-0.02820.1973-30.0143-46.55676.2436
371.88980.28890.1461.9833-0.30981.2561-0.0517-0.0202-0.17050.10670.01070.0375-0.05590.09170.06250.1329-0.00270.01240.15340.04490.1469-23.4786-41.59677.0193
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 50 through 59 )A50 - 59
2X-RAY DIFFRACTION2chain 'A' and (resid 60 through 64 )A60 - 64
3X-RAY DIFFRACTION3chain 'A' and (resid 65 through 69 )A65 - 69
4X-RAY DIFFRACTION4chain 'A' and (resid 70 through 74 )A70 - 74
5X-RAY DIFFRACTION5chain 'A' and (resid 75 through 87 )A75 - 87
6X-RAY DIFFRACTION6chain 'B' and (resid 17 through 27 )B17 - 27
7X-RAY DIFFRACTION7chain 'B' and (resid 28 through 42 )B28 - 42
8X-RAY DIFFRACTION8chain 'B' and (resid 43 through 94 )B43 - 94
9X-RAY DIFFRACTION9chain 'B' and (resid 95 through 171 )B95 - 171
10X-RAY DIFFRACTION10chain 'C' and (resid 51 through 60 )C51 - 60
11X-RAY DIFFRACTION11chain 'C' and (resid 61 through 75 )C61 - 75
12X-RAY DIFFRACTION12chain 'C' and (resid 76 through 87 )C76 - 87
13X-RAY DIFFRACTION13chain 'D' and (resid 17 through 79 )D17 - 79
14X-RAY DIFFRACTION14chain 'D' and (resid 80 through 170 )D80 - 170
15X-RAY DIFFRACTION15chain 'E' and (resid 51 through 55 )E51 - 55
16X-RAY DIFFRACTION16chain 'E' and (resid 56 through 65 )E56 - 65
17X-RAY DIFFRACTION17chain 'E' and (resid 66 through 70 )E66 - 70
18X-RAY DIFFRACTION18chain 'E' and (resid 71 through 87 )E71 - 87
19X-RAY DIFFRACTION19chain 'F' and (resid 18 through 27 )F18 - 27
20X-RAY DIFFRACTION20chain 'F' and (resid 28 through 42 )F28 - 42
21X-RAY DIFFRACTION21chain 'F' and (resid 43 through 71 )F43 - 71
22X-RAY DIFFRACTION22chain 'F' and (resid 72 through 79 )F72 - 79
23X-RAY DIFFRACTION23chain 'F' and (resid 80 through 111 )F80 - 111
24X-RAY DIFFRACTION24chain 'F' and (resid 112 through 136 )F112 - 136
25X-RAY DIFFRACTION25chain 'F' and (resid 137 through 145 )F137 - 145
26X-RAY DIFFRACTION26chain 'F' and (resid 146 through 155 )F146 - 155
27X-RAY DIFFRACTION27chain 'F' and (resid 156 through 169 )F156 - 169
28X-RAY DIFFRACTION28chain 'G' and (resid 50 through 54 )G50 - 54
29X-RAY DIFFRACTION29chain 'G' and (resid 55 through 59 )G55 - 59
30X-RAY DIFFRACTION30chain 'G' and (resid 60 through 64 )G60 - 64
31X-RAY DIFFRACTION31chain 'G' and (resid 65 through 69 )G65 - 69
32X-RAY DIFFRACTION32chain 'G' and (resid 70 through 74 )G70 - 74
33X-RAY DIFFRACTION33chain 'G' and (resid 75 through 87 )G75 - 87
34X-RAY DIFFRACTION34chain 'H' and (resid 19 through 42 )H19 - 42
35X-RAY DIFFRACTION35chain 'H' and (resid 43 through 79 )H43 - 79
36X-RAY DIFFRACTION36chain 'H' and (resid 80 through 106 )H80 - 106
37X-RAY DIFFRACTION37chain 'H' and (resid 107 through 170 )H107 - 170

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