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- PDB-7a3s: Crystal structure of dengue 3 virus envelope glycoprotein -

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Basic information

Entry
Database: PDB / ID: 7a3s
TitleCrystal structure of dengue 3 virus envelope glycoprotein
ComponentsGenome polyprotein
KeywordsVIRAL PROTEIN / FLAVIVIRUS / CLASS 2 FUSION PROTEIN
Function / homology
Function and homology information


symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / flavivirin / 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 / : / nucleoside-triphosphate phosphatase / double-stranded RNA binding / protein complex oligomerization ...symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / flavivirin / 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 / : / nucleoside-triphosphate phosphatase / double-stranded RNA binding / protein complex oligomerization / monoatomic ion channel activity / 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 endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / protein dimerization activity / RNA helicase / induction by virus of host autophagy / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / serine-type endopeptidase activity / fusion of virus membrane with host endosome membrane / viral envelope / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / structural molecule activity / virion attachment to host cell / virion membrane / ATP hydrolysis activity / proteolysis / extracellular region / ATP binding / membrane / metal ion binding
Similarity search - Function
: / : / Flavivirus envelope glycoprotein E, stem/anchor domain / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Flavivirus NS3 helicase, C-terminal helical domain / Genome polyprotein, Flavivirus / Flavivirus non-structural protein NS4A ...: / : / Flavivirus envelope glycoprotein E, stem/anchor domain / RNA-directed RNA polymerase, thumb domain, Flavivirus / Flavivirus RNA-directed RNA polymerase, thumb domain / Flavivirus capsid protein C superfamily / Flavivirus non-structural protein NS2B / Flavivirus NS3 helicase, C-terminal helical domain / 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. / Envelope glycoprotein M, flavivirus / Flavivirus envelope glycoprotein M / 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 superfamily, flavivirus / Flavivirus polyprotein propeptide / Flavivirus polyprotein propeptide superfamily / Flavivirus polyprotein propeptide / Flaviviral glycoprotein E, central domain, subdomain 1 / Flaviviral glycoprotein E, central domain, subdomain 2 / Flavivirus envelope glycoprotein E, Stem/Anchor domain / Flavivirus glycoprotein E, immunoglobulin-like domain / Flavivirus envelope glycoprotein E, Stem/Anchor domain superfamily / Flavivirus glycoprotein, immunoglobulin-like domain / Flavivirus glycoprotein central and dimerisation domain / Flavivirus glycoprotein, central and dimerisation domains / 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 / 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
Similarity search - Domain/homology
Biological speciesDengue virus 3 Philippines/H87/1956
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsSharma, A. / Vaney, M.C. / Guardado-Calvo, P. / Duquerroy, S. / Rouvinski, A. / Navarro-Sanchez, E. / Rey, F.A.
Funding support France, 1items
OrganizationGrant numberCountry
Wellcome Trust France
Citation
Journal: Cell / Year: 2021
Title: The epitope arrangement on flavivirus particles contributes to Mab C10's extraordinary neutralization breadth across Zika and dengue viruses.
Authors: Arvind Sharma / Xiaokang Zhang / Wanwisa Dejnirattisai / Xinghong Dai / Danyang Gong / Wiyada Wongwiwat / Stéphane Duquerroy / Alexander Rouvinski / Marie-Christine Vaney / Pablo Guardado- ...Authors: Arvind Sharma / Xiaokang Zhang / Wanwisa Dejnirattisai / Xinghong Dai / Danyang Gong / Wiyada Wongwiwat / Stéphane Duquerroy / Alexander Rouvinski / Marie-Christine Vaney / Pablo Guardado-Calvo / Ahmed Haouz / Patrick England / Ren Sun / Z Hong Zhou / Juthathip Mongkolsapaya / Gavin R Screaton / Felix A Rey /
Abstract: The human monoclonal antibody C10 exhibits extraordinary cross-reactivity, potently neutralizing Zika virus (ZIKV) and the four serotypes of dengue virus (DENV1-DENV4). Here we describe a comparative ...The human monoclonal antibody C10 exhibits extraordinary cross-reactivity, potently neutralizing Zika virus (ZIKV) and the four serotypes of dengue virus (DENV1-DENV4). Here we describe a comparative structure-function analysis of C10 bound to the envelope (E) protein dimers of the five viruses it neutralizes. We demonstrate that the C10 Fab has high affinity for ZIKV and DENV1 but not for DENV2, DENV3, and DENV4. We further show that the C10 interaction with the latter viruses requires an E protein conformational landscape that limits binding to only one of the three independent epitopes per virion. This limited affinity is nevertheless counterbalanced by the particle's icosahedral organization, which allows two different dimers to be reached by both Fab arms of a C10 immunoglobulin. The epitopes' geometric distribution thus confers C10 its exceptional neutralization breadth. Our results highlight the importance not only of paratope/epitope complementarity but also the topological distribution for epitope-focused vaccine design.
#1: Journal: Nature / Year: 2016
Title: Structural basis of potent Zika-dengue virus antibody cross-neutralization.
Authors: Barba-Spaeth, G. / Dejnirattisai, W. / Rouvinski, A. / Vaney, M.C. / Medits, I. / Sharma, A. / Simon-Loriere, E. / Sakuntabhai, A. / Cao-Lormeau, V.M. / Haouz, A. / England, P. / Stiasny, K. ...Authors: Barba-Spaeth, G. / Dejnirattisai, W. / Rouvinski, A. / Vaney, M.C. / Medits, I. / Sharma, A. / Simon-Loriere, E. / Sakuntabhai, A. / Cao-Lormeau, V.M. / Haouz, A. / England, P. / Stiasny, K. / Mongkolsapaya, J. / Heinz, F.X. / Screaton, G.R. / Rey, F.A.
#2: Journal: Nature / Year: 2015
Title: Recognition determinants of broadly neutralizing human antibodies against dengue viruses.
Authors: Rouvinski, A. / Guardado-Calvo, P. / Barba-Spaeth, G. / Duquerroy, S. / Vaney, M.C. / Kikuti, C.M. / Navarro Sanchez, M.E. / Dejnirattisai, W. / Wongwiwat, W. / Haouz, A. / Girard-Blanc, C. ...Authors: Rouvinski, A. / Guardado-Calvo, P. / Barba-Spaeth, G. / Duquerroy, S. / Vaney, M.C. / Kikuti, C.M. / Navarro Sanchez, M.E. / Dejnirattisai, W. / Wongwiwat, W. / Haouz, A. / Girard-Blanc, C. / Petres, S. / Shepard, W.E. / Despres, P. / Arenzana-Seisdedos, F. / Dussart, P. / Mongkolsapaya, J. / Screaton, G.R. / Rey, F.A.
History
DepositionAug 18, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 8, 2021Provider: repository / Type: Initial release
Revision 1.1Dec 15, 2021Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Dec 22, 2021Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Genome polyprotein
B: Genome polyprotein
C: Genome polyprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)131,69412
Polymers130,0793
Non-polymers1,6159
Water2,036113
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A: Genome polyprotein
hetero molecules

A: Genome polyprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,7968
Polymers86,7192
Non-polymers1,0776
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation5_435x-y-1,-y-2,-z+2/31
Buried area4100 Å2
ΔGint-26 kcal/mol
Surface area37890 Å2
MethodPISA
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B: Genome polyprotein
C: Genome polyprotein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)87,7968
Polymers86,7192
Non-polymers1,0776
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4250 Å2
ΔGint-22 kcal/mol
Surface area37900 Å2
MethodPISA
Unit cell
Length a, b, c (Å)142.030, 142.030, 159.588
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 (resseq 1:26 or resseq 28:51 or resseq...
21(chain B and (resseq 1:26 or resseq 28:51 or resseq...
31(chain C and (resseq 1:26 or resseq 28:51 or resseq...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 26
121(chain A and (resseq 1:26 or resseq 28:51 or resseq...A28 - 51
131(chain A and (resseq 1:26 or resseq 28:51 or resseq...A53 - 85
141(chain A and (resseq 1:26 or resseq 28:51 or resseq...A87 - 95
151(chain A and (resseq 1:26 or resseq 28:51 or resseq...A96
161(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
171(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
181(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
191(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
1101(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
1111(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
1121(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
1131(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
1141(chain A and (resseq 1:26 or resseq 28:51 or resseq...A1 - 610
211(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 26
221(chain B and (resseq 1:26 or resseq 28:51 or resseq...B28 - 51
231(chain B and (resseq 1:26 or resseq 28:51 or resseq...B53 - 85
241(chain B and (resseq 1:26 or resseq 28:51 or resseq...B87 - 95
251(chain B and (resseq 1:26 or resseq 28:51 or resseq...B96
261(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
271(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
281(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
291(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
2101(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
2111(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
2121(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
2131(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
2141(chain B and (resseq 1:26 or resseq 28:51 or resseq...B1 - 610
311(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 26
321(chain C and (resseq 1:26 or resseq 28:51 or resseq...C28 - 51
331(chain C and (resseq 1:26 or resseq 28:51 or resseq...C53 - 85
341(chain C and (resseq 1:26 or resseq 28:51 or resseq...C87 - 95
351(chain C and (resseq 1:26 or resseq 28:51 or resseq...C96
361(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610
371(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610
381(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610
391(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610
3101(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610
3111(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610
3121(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610
3131(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610
3141(chain C and (resseq 1:26 or resseq 28:51 or resseq...C1 - 610

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Components

#1: Protein Genome polyprotein


Mass: 43359.609 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: FRAGMENT: SOLUBLE ECTODOMAIN / Source: (gene. exp.) Dengue virus 3 Philippines/H87/1956 / Cell line (production host): SCHNEIDER 2 / Production host: Drosophila melanogaster (fruit fly)
References: UniProt: P27915, flavivirin, nucleoside-triphosphate phosphatase, RNA helicase, mRNA (guanine-N7)-methyltransferase, methyltransferase cap1, RNA-directed RNA polymerase
#2: Chemical ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: SO4
#3: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 113 / 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: 3.64 Å3/Da / Density % sol: 66.25 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 7.5 / Details: 0.1 M HEPES (7.5), 1.5 M (NH4)2SO4, 280 mM NACL

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Aug 8, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.8→50.2 Å / Num. obs: 46309 / % possible obs: 100 % / Redundancy: 8.3 % / Biso Wilson estimate: 64.99 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.223 / Net I/σ(I): 9.2
Reflection shellResolution: 2.8→2.9 Å / Redundancy: 6.7 % / Rmerge(I) obs: 2.98 / Num. unique obs: 4527 / CC1/2: 0.303

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Processing

Software
NameVersionClassification
Aimlessdata scaling
PHENIX1.10.1_2155refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1UZG

1uzg


Resolution: 2.8→19.925 Å / SU ML: 0.46 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 31.42 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2739 2526 5.49 %
Rwork0.2331 43514 -
obs0.2353 46040 99.79 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 226.07 Å2 / Biso mean: 82.8077 Å2 / Biso min: 30.88 Å2
Refinement stepCycle: final / Resolution: 2.8→19.925 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8871 0 99 113 9083
Biso mean--122.14 56.3 -
Num. residues----1149
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0049185
X-RAY DIFFRACTIONf_angle_d0.71612450
X-RAY DIFFRACTIONf_chiral_restr0.0481449
X-RAY DIFFRACTIONf_plane_restr0.0051566
X-RAY DIFFRACTIONf_dihedral_angle_d13.7445532
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5200X-RAY DIFFRACTION7.197TORSIONAL
12B5200X-RAY DIFFRACTION7.197TORSIONAL
13C5200X-RAY DIFFRACTION7.197TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.8001-2.85380.41951470.3816239399
2.8538-2.91190.39341410.35482368100
2.9119-2.9750.36731410.34732374100
2.975-3.0440.38531190.34282431100
3.044-3.11980.36641290.31782395100
3.1198-3.20390.29751450.28712373100
3.2039-3.29770.29771290.29392421100
3.2977-3.40370.32411460.27912387100
3.4037-3.52470.32341310.26852414100
3.5247-3.6650.27271290.24212422100
3.665-3.83060.30341490.2372396100
3.8306-4.0310.28061460.2242417100
4.031-4.28130.25221380.20822412100
4.2813-4.6080.21611470.17992416100
4.608-5.06480.22881530.18142429100
5.0648-5.7820.22991380.19372447100
5.782-7.22650.24341550.21782463100
7.2265-19.9250.2421430.1927255699
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)
1-0.2780.48610.16747.85492.51330.38650.0065-0.08820.068-0.1941-0.17570.13760.0029-0.06240.12770.840.0259-0.0590.3514-0.04990.7004-19.1507-114.5441.9464
24.05810.313-0.22634.64773.42688.69180.39570.4162-0.4807-0.485-0.46410.4240.5333-0.62290.13520.62380.0563-0.01560.2616-0.00170.5684-19.7922-80.510346.9909
33.1114-0.47460.02559.09460.9551.98590.3073-0.1681-0.0657-0.2548-0.4838-0.3960.3220.06330.27870.98880.0417-0.10110.33650.07220.5576-17.801-119.02242.7364
43.7259-1.1807-1.35965.04270.08534.3304-0.0064-0.32080.1370.70660.17040.0946-0.39680.065-0.21210.52970.0042-0.08010.26840.01010.4911-17.9698-68.154266.1607
50.4752-0.2643-0.21147.28490.970.6603-0.0322-0.00290.11190.60390.0630.875-0.1843-0.06770.03750.50860.05010.08680.3587-0.0340.5824-24.8839-138.87519.9652
65.09040.97791.48659.76153.95726.3204-0.1860.05670.3807-0.03880.09920.1788-0.6948-0.04830.18890.54010.01330.12870.33440.02150.4747-22.8733-167.11518.5646
73.72260.18170.36316.75150.26463.22390.0210.36410.25770.44280.15210.1173-0.428-0.10870.04760.53790.040.06580.31870.10490.3959-24.0186-128.40910.2338
82.36040.76180.60795.65051.46672.75180.04780.3336-0.1786-0.95740.47860.1167-0.1510.1754-0.45260.5055-0.0746-0.05790.5078-0.07760.5373-23.158-181.0769-12.6003
90.39780.53950.08518.17540.5380.0349-0.03260.02950.222-0.92510.14910.51240.0093-0.1101-0.050.7109-0.0328-0.15750.53190.11990.8421-24.9499-112.9263-9.8998
106.4354-0.8888-0.72762.67812.23597.5042-0.47680.11730.3786-0.08460.32750.73410.5278-0.11970.42710.58450.0524-0.06510.5440.12151.0096-22.103-86.1958-10.3315
112.96152.07-0.02985.63181.31883.81410.08170.20380.0139-0.5373-0.20560.40970.052-0.30620.09540.59680.0532-0.09020.45360.13060.5609-24.1676-124.0597-10.3946
121.3061-1.8935-0.80475.31761.34683.71440.1791-0.13670.4340.75910.230.4712-0.2392-0.2198-0.28210.64580.05280.15050.483-0.04181.3531-23.6464-71.413612.2694
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(chain A and resid 1:130)A1 - 130
2X-RAY DIFFRACTION2(chain A and resid 131:186)A131 - 186
3X-RAY DIFFRACTION3(chain A and resid 187:271)A187 - 271
4X-RAY DIFFRACTION4(chain A and resid 274:393)A274 - 393
5X-RAY DIFFRACTION5(chain B and resid 1:149)B1 - 149
6X-RAY DIFFRACTION6(chain B and resid 150:192)B150 - 192
7X-RAY DIFFRACTION7(chain B and resid 193:270)B193 - 270
8X-RAY DIFFRACTION8(chain B and resid 274:394)B274 - 394
9X-RAY DIFFRACTION9(chain C and resid 1:152)C1 - 152
10X-RAY DIFFRACTION10(chain C and resid 153:193)C153 - 193
11X-RAY DIFFRACTION11(chain C and resid 194:270)C194 - 270
12X-RAY DIFFRACTION12(chain C and resid 274:394)C274 - 394

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