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- PDB-7a3p: Crystal structure of dengue 3 virus envelope glycoprotein in comp... -

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Basic information

Entry
Database: PDB / ID: 7a3p
TitleCrystal structure of dengue 3 virus envelope glycoprotein in complex with the scFv fragment of the broadly neutralizing human antibody EDE1 C10
Components
  • (Single Chain Variable FragmentSingle-chain variable fragment) x 2
  • Envelope protein E
KeywordsVIRAL PROTEIN / FLAVIVIRUS / CLASS 2 FUSION PROTEIN / DENGUE / Antibody
Function / homology
Function and homology information


clathrin-dependent endocytosis of virus by host cell / host cell endoplasmic reticulum membrane / protein dimerization activity / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / virion membrane / extracellular region / membrane
Similarity search - Function
Flavivirus envelope glycoprotein E, stem/anchor domain / Envelope glycoprotein M, flavivirus / Flavivirus envelope glycoprotein M / 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 envelope glycoprotein E, stem/anchor domain / Envelope glycoprotein M, flavivirus / Flavivirus envelope glycoprotein M / 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 / Flavivirus/Alphavirus glycoprotein, immunoglobulin-like domain superfamily / Flavivirus glycoprotein, central and dimerisation domain superfamily / Flaviviral glycoprotein E, dimerisation domain / Immunoglobulin E-set
Similarity search - Domain/homology
Biological speciesDengue virus 3
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.19 Å
AuthorsSharma, A. / Vaney, M.C. / Guardado-Calvo, P. / Duquerroy, S. / Rouvinski, A. / 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Envelope protein E
B: Envelope protein E
H: Single Chain Variable Fragment
L: Single Chain Variable Fragment
I: Single Chain Variable Fragment
M: Single Chain Variable Fragment
hetero molecules


Theoretical massNumber of molelcules
Total (without water)156,4867
Polymers156,2646
Non-polymers2211
Water30617
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, envelope protein (Chain A and chain B) are present as dimers on virion surface and form a dimers in the asymmetric unit. Chain H (antibody heavy chain fragment) forms a ...Evidence: gel filtration, envelope protein (Chain A and chain B) are present as dimers on virion surface and form a dimers in the asymmetric unit. Chain H (antibody heavy chain fragment) forms a heterodimer with chain L (antibody light chain fragment) .
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11690 Å2
ΔGint-19 kcal/mol
Surface area53710 Å2
MethodPISA
Unit cell
Length a, b, c (Å)53.744, 101.412, 249.236
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 1 through 16 or resid 19...
21(chain B and (resid 1 through 221 or resid 224...
12chain H
22(chain I and resid 2 through 111)
13chain L
23(chain M and resid 2 through 106A)

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 1 through 16 or resid 19...A1 - 16
121(chain A and (resid 1 through 16 or resid 19...A19 - 145
131(chain A and (resid 1 through 16 or resid 19...A158 - 85
141(chain A and (resid 1 through 16 or resid 19...A1 - 390
151(chain A and (resid 1 through 16 or resid 19...A273 - 324
161(chain A and (resid 1 through 16 or resid 19...A328 - 389
211(chain B and (resid 1 through 221 or resid 224...B1 - 221
221(chain B and (resid 1 through 221 or resid 224...B224 - 238
231(chain B and (resid 1 through 221 or resid 224...B247 - 276
241(chain B and (resid 1 through 221 or resid 224...B279 - 337
251(chain B and (resid 1 through 221 or resid 224...B348 - 389
112chain HH2 - 111
212(chain I and resid 2 through 111)I2 - 111
113chain LL2 - 106
213(chain M and resid 2 through 106A)M2 - 106

NCS ensembles :
ID
1
2
3

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Components

#1: Protein Envelope protein E / / Matrix protein / Peptide pr / Protein prM / Small envelope protein M


Mass: 46820.219 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: DENGUE VIRUS SEROTYPE 3 ENVELOPE PROTEIN ECTODOMAIN
Source: (gene. exp.) Dengue virus 3 / Cell line (production host): SCHNEIDER 2 / Production host: Drosophila melanogaster (fruit fly) / References: UniProt: Q07019
#2: Antibody Single Chain Variable Fragment / Single-chain variable fragment


Mass: 15679.234 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: variable domain from the heavy chain of antibody EDE1 C10
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): SCHNEIDER 2 / Production host: Drosophila melanogaster (fruit fly)
#3: Antibody Single Chain Variable Fragment / Single-chain variable fragment


Mass: 15632.767 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: variable domain from the light chain of antibody EDE1 C10
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): SCHNEIDER 2 / Production host: Drosophila melanogaster (fruit fly)
#4: 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.: 1 / Source method: obtained synthetically / 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
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 17 / 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: 2.17 Å3/Da / Density % sol: 43.36 %
Crystal growTemperature: 291 K / Method: vapor diffusion / pH: 7.5 / Details: 100 mM HEPES pH 7.5, 15% PEG 8,000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 3, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.19→49.59 Å / Num. obs: 23920 / % possible obs: 87.3 % / Redundancy: 5.4 % / Rmerge(I) obs: 0.171 / Net I/σ(I): 6.3
Reflection shellResolution: 3.19→3.37 Å / Rmerge(I) obs: 0.476 / Num. unique obs: 2139 / % possible all: 56.9

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Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
PDB_EXTRACT3.25data extraction
Aimlessdata scaling
PHENIXphasing
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: DENV1 sE from related PDB

Resolution: 3.19→19.95 Å / SU ML: 0.4 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 31.72 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2839 1220 5.35 %
Rwork0.2405 21602 -
obs0.243 22822 97.39 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 141.35 Å2 / Biso mean: 67.1441 Å2 / Biso min: 28.25 Å2
Refinement stepCycle: final / Resolution: 3.19→19.95 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9142 0 14 17 9173
Biso mean--96.39 46.48 -
Num. residues----1183
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1998X-RAY DIFFRACTION5.796TORSIONAL
12B1998X-RAY DIFFRACTION5.796TORSIONAL
21H756X-RAY DIFFRACTION5.796TORSIONAL
22I756X-RAY DIFFRACTION5.796TORSIONAL
31L648X-RAY DIFFRACTION5.796TORSIONAL
32M648X-RAY DIFFRACTION5.796TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 9

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.19-3.320.34341460.307823652511100
3.32-3.470.37411510.27823882539100
3.47-3.650.27651310.2752409254099
3.65-3.880.34491060.25472446255299
3.88-4.170.33071010.24592432253398
4.17-4.590.2171970.20612436253398
4.59-5.240.24221500.20642396254697
5.24-6.560.28451860.24082350253696
6.56-19.950.25241520.22982380253291
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)
11.59690.25370.85753.87540.14753.83790.0752-0.0098-0.20840.77620.22430.1208-0.8789-0.7408-0.22170.61110.05560.09290.48980.05180.4464-77.4038122.440476.1144
21.1637-0.1588-1.61720.31370.11213.2658-0.00020.40770.1011-0.0294-0.05720.0008-0.0218-0.6585-0.02640.37450.02820.00130.49070.04940.4952-70.756111.679538.6144
33.25481.6858-4.08130.2211-1.39876.0087-0.04380.06110.4071-0.0340.68120.5434-0.306-0.5276-0.61830.49930.065-0.03630.7812-0.04470.6702-78.7377119.224953.8806
43.30230.308-1.20973.26720.52715.11170.22640.70.36420.1585-0.0130.0498-0.0565-0.5013-0.33010.26650.02250.02330.49360.05860.5074-64.9865115.851334.6627
50.8199-0.58691.23730.6922-0.53631.6134-0.0379-0.54280.10760.35340.38770.1327-0.1785-0.4471-0.07940.58870.11670.04210.95650.03460.6261-80.2284113.651881.2825
64.1270.0125-1.10790.8793-0.70454.8609-0.0363-1.1184-0.2240.8314-0.1499-0.0665-0.43570.07040.20280.55790.1167-0.05140.92510.01980.5147-70.1564113.897993.175
70.9549-0.2467-0.9493-0.0296-0.13354.11190.0645-0.01870.1022-0.0841-0.2729-0.0971-0.56191.0170.20840.4877-0.11230.01820.49150.06050.5101-37.978113.563732.0767
80.9825-1.5681-0.83541.02540.52093.83060.11140.7370.3554-0.05140.021-0.5850.07830.6163-0.14870.5551-0.06330.0421.3829-0.00580.8119-26.4706116.059314.1812
95.78160.1157-0.47082.3726-1.00976.9321-0.0111-0.02580.6879-0.11430.21830.11430.4254-0.3784-0.15510.33960.0190.00820.40380.05290.3333-44.9709114.822945.6846
100.9962-0.3675-0.072-0.39860.25830.4692-0.01940.9123-0.1535-0.4799-0.1498-0.00040.0924-0.3709-0.00030.8138-0.00390.1310.7184-0.01420.6077-32.4446117.303711.9697
113.2266-0.51-0.70361.17550.03973.6773-0.7087-0.0171-0.20680.0550.08730.01240.79750.81220.65140.6546-0.0330.11670.85240.06110.7277-34.8427109.9978-20.1283
122.21980.5440.2380.81451.05283.5737-0.33390.013-0.1207-0.17050.2347-0.02820.5007-0.75820.0920.8556-0.04590.18530.99350.22520.5053-37.3683109.6788-20.455
131.40930.13892.02615.74191.10392.8771-0.11970.0942-0.58690.6721-0.0085-0.8880.3116-0.0017-0.01950.62850.0449-0.07370.8326-0.0280.5221-41.542881.461614.384
141.45530.61431.23155.10311.65694.42580.2607-0.609-0.06170.5265-0.52490.4107-0.2045-0.70220.36570.5374-0.0409-0.00020.86480.12790.3988-49.692290.708510.6934
155.14062.0293-0.52914.27561.79522.314-0.5807-1.30220.62290.1816-0.37610.21480.0959-0.18681.06360.7725-0.0836-0.20810.7990.12880.5048-47.564785.574517.9147
161.99080.98680.0011.90480.07181.0219-0.0156-0.2223-0.11840.01340.1147-0.3056-0.0307-0.2075-0.11310.46230.0810.00130.75970.04590.3624-43.356592.2865.7794
173.45590.31410.97594.34721.70880.9076-0.47710.1305-0.8240.7942-0.00030.87770.9817-0.96770.07691.2144-0.5262-0.16841.54590.06080.4441-59.527586.6515-6.7886
180.7768-0.1508-0.62580.02680.12120.51-0.44250.6538-0.8889-1.17140.9046-0.3496-0.13650.4696-0.10681.12270.0232-0.05341.1831-0.95091.1176-50.589577.6914-21.0425
195.1881-0.19030.63361.3953-0.61043.6318-0.3432-0.40280.826-0.67620.26230.16490.9476-0.75170.2350.5229-0.0959-0.11990.78330.01910.3962-53.258592.985-7.7544
203.87291.16710.51781.40250.71131.50760.760.3218-1.1137-0.7526-0.1019-0.60490.0892-0.048-0.38720.6002-0.08440.1030.5579-0.01430.4916-43.066182.1807-4.7294
216.5214-2.1084-2.27935.16254.18334.32350.86410.63090.4377-1.271-0.4603-0.95191.4143-0.0818-0.48550.90820.00270.04920.63830.06650.4872-40.505292.4957-12.3809
225.89452.0138-3.32572.515-0.96843.7177-0.45290.015-0.4102-0.0467-0.27610.0625-0.1483-0.68230.68460.48650.0054-0.06630.8035-0.03480.399-51.689692.5867-15.008
230.55660.8477-0.01461.1047-0.43282.4066-0.10190.2683-0.1081-0.51290.4875-0.76190.47080.2419-0.40050.8309-0.01770.0970.63150.04470.4844-47.393682.712-10.5895
241.8960.37730.68525.98441.11342.7778-0.12250.23340.27230.31060.62990.50940.573-0.3772-0.26410.56960.0179-0.01280.40150.18240.4579-55.332294.29361.8303
252.59961.1863-0.22621.3924-1.33731.8181-0.01160.345-0.7273-0.2310.2176-0.4710.9061-0.2186-0.3040.729-0.23870.10890.7998-0.23520.6939-51.424875.3825-14.3813
264.6892.7262.20866.8283-1.93873.03110.0237-0.7134-0.27241.2518-0.7883-0.07770.1204-0.57910.26760.7125-0.016-0.00651.1838-0.18160.1493-73.599684.134370.2581
27-0.01020.14190.03030.07380.0274-0.0026-0.54530.7927-0.4163-0.00720.04930.44270.11360.20580.06180.56530.1459-0.22980.2215-0.2360.6333-57.582374.715956.7246
283.3746-3.7073-2.37334.08862.61882.0382-0.4376-0.5418-0.31040.52930.38540.78451.5092-1.01340.37950.4643-0.053-0.06170.3317-0.10550.5706-70.62886.403863.0055
293.4019-2.67621.20114.2171-1.00592.01220.2472-0.887-0.14270.06450.25580.25770.1608-0.8769-0.06530.63270.0422-0.0088-1.0678-0.02420.4878-64.190590.167966.5744
300.2984-0.1093-0.44764.9355-1.01092.56240.59840.01320.2287-0.4441-0.6496-0.3590.38121.0009-0.01670.5166-0.14740.04590.584-0.13840.3885-55.884988.741968.2622
310.3333-0.6389-0.31212.83630.05081.35640.50120.36630.7278-0.08990.0606-0.56-1.42970.5035-0.18960.77030.29530.07090.14270.17250.5976-57.427595.609360.5898
322.7547-2.46960.43653.4302-0.98785.3191-0.60170.08250.6036-0.3665-0.4784-0.3349-0.25131.06650.8610.7569-0.0381-0.05950.51380.10730.5101-58.983790.386656.4088
333.1362-0.24451.28310.9883-0.1261.2905-0.53510.01560.5645-1.0062-0.8117-0.4836-0.5820.59590.18090.8295-0.3382-0.2557-1.4235-0.46950.5301-67.355987.308757.5658
340.03930.10680.85392.40070.48071.72470.04530.15510.0406-0.79240.2953-0.28290.16830.2257-0.23970.4468-0.15250.07090.46690.02840.37-57.350583.788565.0996
353.09031.18690.77221.8568-0.47846.2990.67330.58870.0951-0.27140.45550.3695-1.1181-0.8559-1.11540.56650.0641-0.06710.56990.05460.5401-66.2233105.489166.8348
360.3115-0.2455-0.62812.58981.07290.53030.64490.43460.72110.0984-0.8033-0.420.2775-0.7673-0.11570.3806-0.1039-0.01790.32750.02370.4662-63.81987.265971.6711
372.3333-0.75121.24440.8984-0.13230.75240.58680.9275-0.4611-1.9010.0239-1.88920.4280.609-0.2251.07770.1758-0.19110.3258-0.13170.5979-46.804588.031679.8419
381.3262-0.2783-0.12934.973-2.19674.8832-0.4714-0.1674-0.03220.2475-0.1523-0.97590.094-0.32130.61630.30930.0149-0.02360.436-0.04470.4958-52.787292.797287.5452
390.9344-0.66480.40041.2509-0.08142.0988-0.05780.35880.51071.5748-0.65380.70080.48070.470.48460.6051-0.0077-0.00590.0644-0.07460.429-61.93585.773681.4672
401.34950.9836-1.18762.8741-3.26494.54460.20760.09230.2072-0.17080.06060.31640.04770.1421-0.30270.30020.0619-0.05040.65460.01250.5244-66.514394.392788.0187
410.2235-0.5625-0.26321.4660.61010.2661-0.243-1.04790.07260.81490.54280.9012-0.14350.25380.06270.5627-0.1884-0.04890.2825-0.2180.2828-55.322695.351989.727
420.6504-0.7423-0.00080.6091.25833.4126-0.4242-0.3456-0.3838-0.00850.3773-0.24760.918-0.88210.51190.5457-0.10760.10030.3726-0.06920.5391-59.231884.965487.0327
431.3885-0.7531-0.26012.489-1.4081.8598-0.2836-0.60820.2108-0.6726-0.7005-1.5202-0.03940.55050.36870.5111-0.1711-0.11350.2044-0.03470.5824-53.270889.322679.768
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 26 )A1 - 26
2X-RAY DIFFRACTION2chain 'A' and (resid 27 through 176 )A27 - 176
3X-RAY DIFFRACTION3chain 'A' and (resid 177 through 201 )A177 - 201
4X-RAY DIFFRACTION4chain 'A' and (resid 202 through 269 )A202 - 269
5X-RAY DIFFRACTION5chain 'A' and (resid 270 through 308 )A270 - 308
6X-RAY DIFFRACTION6chain 'A' and (resid 309 through 390 )A309 - 390
7X-RAY DIFFRACTION7chain 'B' and (resid 1 through 167 )B1 - 167
8X-RAY DIFFRACTION8chain 'B' and (resid 168 through 201 )B168 - 201
9X-RAY DIFFRACTION9chain 'B' and (resid 202 through 254 )B202 - 254
10X-RAY DIFFRACTION10chain 'B' and (resid 255 through 296 )B255 - 296
11X-RAY DIFFRACTION11chain 'B' and (resid 297 through 355 )B297 - 355
12X-RAY DIFFRACTION12chain 'B' and (resid 356 through 388 )B356 - 388
13X-RAY DIFFRACTION13chain 'H' and (resid 2 through 28 )H2 - 28
14X-RAY DIFFRACTION14chain 'H' and (resid 29 through 66 )H29 - 66
15X-RAY DIFFRACTION15chain 'H' and (resid 67 through 87 )H67 - 87
16X-RAY DIFFRACTION16chain 'H' and (resid 88 through 111 )H88 - 111
17X-RAY DIFFRACTION17chain 'L' and (resid 2 through 8 )L2 - 8
18X-RAY DIFFRACTION18chain 'L' and (resid 9 through 18 )L9 - 18
19X-RAY DIFFRACTION19chain 'L' and (resid 19 through 38 )L19 - 38
20X-RAY DIFFRACTION20chain 'L' and (resid 39 through 48 )L39 - 48
21X-RAY DIFFRACTION21chain 'L' and (resid 49 through 61 )L49 - 61
22X-RAY DIFFRACTION22chain 'L' and (resid 62 through 75 )L62 - 75
23X-RAY DIFFRACTION23chain 'L' and (resid 76 through 91 )L76 - 91
24X-RAY DIFFRACTION24chain 'L' and (resid 92 through 101 )L92 - 101
25X-RAY DIFFRACTION25chain 'L' and (resid 102 through 106A)L102 - 106
26X-RAY DIFFRACTION26chain 'I' and (resid 1 through 6 )I1 - 6
27X-RAY DIFFRACTION27chain 'I' and (resid 7 through 17 )I7 - 17
28X-RAY DIFFRACTION28chain 'I' and (resid 18 through 28 )I18 - 28
29X-RAY DIFFRACTION29chain 'I' and (resid 29 through 40 )I29 - 40
30X-RAY DIFFRACTION30chain 'I' and (resid 41 through 52 )I41 - 52
31X-RAY DIFFRACTION31chain 'I' and (resid 52A through 63 )I52
32X-RAY DIFFRACTION32chain 'I' and (resid 64 through 72 )I64 - 72
33X-RAY DIFFRACTION33chain 'I' and (resid 73 through 82 )I73 - 82
34X-RAY DIFFRACTION34chain 'I' and (resid 82A through 96 )I82
35X-RAY DIFFRACTION35chain 'I' and (resid 97 through 100F)I97 - 100
36X-RAY DIFFRACTION36chain 'I' and (resid 100G through 111 )I100
37X-RAY DIFFRACTION37chain 'M' and (resid 0 through 8 )M0 - 8
38X-RAY DIFFRACTION38chain 'M' and (resid 9 through 32 )M9 - 32
39X-RAY DIFFRACTION39chain 'M' and (resid 33 through 48 )M33 - 48
40X-RAY DIFFRACTION40chain 'M' and (resid 49 through 61 )M49 - 61
41X-RAY DIFFRACTION41chain 'M' and (resid 62 through 75 )M62 - 75
42X-RAY DIFFRACTION42chain 'M' and (resid 76 through 91 )M76 - 91
43X-RAY DIFFRACTION43chain 'M' and (resid 92 through 106A)M92 - 106

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