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- PDB-4ut9: Crystal structure of dengue 2 virus envelope glycoprotein dimer i... -

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Basic information

Entry
Database: PDB / ID: 4ut9
TitleCrystal structure of dengue 2 virus envelope glycoprotein dimer in complex with the ScFv fragment of the broadly neutralizing human antibody EDE1 C10
Components
  • (BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10) x 2
  • ENVELOPE GLYCOPROTEIN E
KeywordsVIRAL PROTEIN / IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX / MEMBRANE FUSION / CLASS 2 FUSION PROTEIN / DENGUE VIRUS / BROADLY NEUTRALIZING ANTIBODY / IMMUNE SYSTEM / SCFV FRAGMENT
Function / homology
Function and homology information


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 / ribonucleoside triphosphate phosphatase activity / viral capsid / : / double-stranded RNA binding / protein complex oligomerization / monoatomic ion channel activity ...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 / ribonucleoside triphosphate phosphatase activity / viral capsid / : / double-stranded RNA binding / protein complex oligomerization / monoatomic ion channel activity / 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 / protein dimerization activity / induction by virus of host autophagy / 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 / virion attachment to host cell / virion membrane / structural molecule activity / proteolysis / extracellular region / ATP binding / membrane / metal ion binding
Similarity search - Function
Viral Envelope Glycoprotein; domain 3 / Viral Envelope Glycoprotein, domain 3 / Viral Envelope Glycoprotein, domain 2 / Tick-borne Encephalitis virus Glycoprotein, domain 1 / Viral Envelope Glycoprotein; domain 2 / Tick-borne Encephalitis virus Glycoprotein; domain 1 / Immunoglobulin-like - #350 / : / Flavivirus envelope glycoprotein E, stem/anchor domain / RNA-directed RNA polymerase, thumb domain, Flavivirus ...Viral Envelope Glycoprotein; domain 3 / Viral Envelope Glycoprotein, domain 3 / Viral Envelope Glycoprotein, domain 2 / Tick-borne Encephalitis virus Glycoprotein, domain 1 / Viral Envelope Glycoprotein; domain 2 / Tick-borne Encephalitis virus Glycoprotein; domain 1 / Immunoglobulin-like - #350 / : / 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 / Immunoglobulins / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan / DNA/RNA polymerase superfamily / Immunoglobulin-like / Sandwich / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Biological speciesDENGUE VIRUS 2
HOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å
AuthorsRouvinski, A. / Guardado-Calvo, P. / Barba-Spaeth, G. / Duquerroy, S. / Vaney, M.C. / Rey, F.A.
Citation
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. / Kikuti, C.M. / Sanchez, M.E.N. / Dejnirattisai, W. / Wongwiwat, W. / Haouz, A. / Girard-Blanc, C. / ...Authors: Rouvinski, A. / Guardado-Calvo, P. / Barba-Spaeth, G. / Duquerroy, S. / Vaney, M. / Kikuti, C.M. / Sanchez, M.E.N. / 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.
#1: Journal: Nat Immunol / Year: 2015
Title: A new class of highly potent, broadly neutralizing antibodies isolated from viremic patients infected with dengue virus.
Authors: Wanwisa Dejnirattisai / Wiyada Wongwiwat / Sunpetchuda Supasa / Xiaokang Zhang / Xinghong Dai / Alexander Rouvinski / Amonrat Jumnainsong / Carolyn Edwards / Nguyen Than Ha Quyen / Thaneeya ...Authors: Wanwisa Dejnirattisai / Wiyada Wongwiwat / Sunpetchuda Supasa / Xiaokang Zhang / Xinghong Dai / Alexander Rouvinski / Amonrat Jumnainsong / Carolyn Edwards / Nguyen Than Ha Quyen / Thaneeya Duangchinda / Jonathan M Grimes / Wen-Yang Tsai / Chih-Yun Lai / Wei-Kung Wang / Prida Malasit / Jeremy Farrar / Cameron P Simmons / Z Hong Zhou / Felix A Rey / Juthathip Mongkolsapaya / Gavin R Screaton /
Abstract: Dengue is a rapidly emerging, mosquito-borne viral infection, with an estimated 400 million infections occurring annually. To gain insight into dengue immunity, we characterized 145 human monoclonal ...Dengue is a rapidly emerging, mosquito-borne viral infection, with an estimated 400 million infections occurring annually. To gain insight into dengue immunity, we characterized 145 human monoclonal antibodies (mAbs) and identified a previously unknown epitope, the envelope dimer epitope (EDE), that bridges two envelope protein subunits that make up the 90 repeating dimers on the mature virion. The mAbs to EDE were broadly reactive across the dengue serocomplex and fully neutralized virus produced in either insect cells or primary human cells, with 50% neutralization in the low picomolar range. Our results provide a path to a subunit vaccine against dengue virus and have implications for the design and monitoring of future vaccine trials in which the induction of antibody to the EDE should be prioritized.
History
DepositionJul 18, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 28, 2015Provider: repository / Type: Initial release
Revision 1.1Apr 8, 2015Group: Database references
Revision 1.2Dec 6, 2017Group: Refinement description / Category: pdbx_refine_tls_group / Item: _pdbx_refine_tls_group.selection_details
Revision 1.3Jul 29, 2020Group: Data collection / Derived calculations ...Data collection / Derived calculations / Other / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_database_status / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_database_status.status_code_sf / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: ENVELOPE GLYCOPROTEIN E
B: ENVELOPE GLYCOPROTEIN E
C: ENVELOPE GLYCOPROTEIN E
D: ENVELOPE GLYCOPROTEIN E
H: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
I: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
J: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
K: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
L: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
M: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
N: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
O: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)315,05716
Polymers314,17212
Non-polymers8854
Water0
1
A: ENVELOPE GLYCOPROTEIN E
H: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
L: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,7644
Polymers78,5433
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4210 Å2
ΔGint-27 kcal/mol
Surface area35070 Å2
MethodPQS
2
B: ENVELOPE GLYCOPROTEIN E
I: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
M: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,7644
Polymers78,5433
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4210 Å2
ΔGint-25.9 kcal/mol
Surface area35510 Å2
MethodPQS
3
C: ENVELOPE GLYCOPROTEIN E
K: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
O: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,7644
Polymers78,5433
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3820 Å2
ΔGint-23.9 kcal/mol
Surface area35030 Å2
MethodPQS
4
D: ENVELOPE GLYCOPROTEIN E
J: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
N: BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,7644
Polymers78,5433
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area4100 Å2
ΔGint-24.1 kcal/mol
Surface area35090 Å2
MethodPQS
Unit cell
Length a, b, c (Å)57.522, 102.235, 131.092
Angle α, β, γ (deg.)88.52, 85.69, 83.90
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
ENVELOPE GLYCOPROTEIN E


Mass: 47230.980 Da / Num. of mol.: 4 / Fragment: SOLUBLE ECTODOMAIN, RESIDUES 281-671
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) DENGUE VIRUS 2 / Strain: FGA-02 / Plasmid: PMT/BIP/V5-HIS / Cell line (production host): SCHNEIDER 2 / Production host: DROSOPHILA MELANOGASTER (fruit fly) / References: UniProt: Q68Y26
#2: Antibody
BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10


Mass: 15679.234 Da / Num. of mol.: 4 / Fragment: SCFV, HEAVY CHAIN DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Description: SEE SECONDARY REFERENCE / Cell: B-LYMPHOCYTE / Plasmid: PMT-SCFV-STREP / Cell line (production host): SCHNEIDER 2 / Production host: DROSOPHILA MELANOGASTER (fruit fly)
#3: Antibody
BROADLY NEUTRALIZING HUMAN ANTIBODY EDE1 C10


Mass: 15632.767 Da / Num. of mol.: 4 / Fragment: SCFV, LIGHT CHAIN DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Description: SEE SECONDARY REFERENCE / Cell: B-LYMPHOCYTE / Plasmid: PMT-SCFV-STREP / Cell line (production host): SCHNEIDER 2 / Production host: DROSOPHILA MELANOGASTER (fruit fly)
#4: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 4
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
Sequence detailsTHE RESIDUES AFTER W391 DERIVE FROM THE VECTOR. THE RESIDUES ARE NUMBERED FROM 1392. RESIDUES 1392 ...THE RESIDUES AFTER W391 DERIVE FROM THE VECTOR. THE RESIDUES ARE NUMBERED FROM 1392. RESIDUES 1392 TO 1394 COMPLETE THE G STRAND OF ENVELOPE GLYCOPROTEIN DOMAIN III SEE SECONDARY REFERENCE. THE SEQUENCE FOR CHAINS A,B,C,D MATCHES UNRELEASED GENBANK GB KM087965

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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: 2.83 Å3/Da / Density % sol: 56.6 % / Description: NONE
Crystal growDetails: 20% (W/V) PEG 8000, 100MM HEPES PH7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 2 / Wavelength: 0.9801
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 3, 2013 / Details: KIRKPATRICK-BAEZ PAIR OF BI-MORPH MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9801 Å / Relative weight: 1
ReflectionResolution: 3.2→30 Å / Num. obs: 46477 / % possible obs: 95.2 % / Observed criterion σ(I): 0 / Redundancy: 1.9 % / Biso Wilson estimate: 82.9 Å2 / Rmerge(I) obs: 0.19 / Net I/σ(I): 5
Reflection shellResolution: 3.2→3.3 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.56 / Mean I/σ(I) obs: 1.2 / % possible all: 96.7

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Processing

Software
NameVersionClassification
BUSTER2.11.4refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 10AN

10an


Resolution: 3.2→20 Å / Cor.coef. Fo:Fc: 0.9108 / Cor.coef. Fo:Fc free: 0.8685 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.492
RfactorNum. reflection% reflectionSelection details
Rfree0.2487 2343 5.06 %RANDOM
Rwork0.1975 ---
obs0.2001 46344 95.32 %-
Displacement parametersBiso mean: 96.93 Å2
Baniso -1Baniso -2Baniso -3
1-4.4588 Å20.8862 Å29.8113 Å2
2---4.7577 Å2-6.1824 Å2
3---0.2989 Å2
Refine analyzeLuzzati coordinate error obs: 0.637 Å
Refinement stepCycle: LAST / Resolution: 3.2→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms19085 0 56 0 19141
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.00819593HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.126554HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d6745SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes448HARMONIC2
X-RAY DIFFRACTIONt_gen_planes2812HARMONIC5
X-RAY DIFFRACTIONt_it19593HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion2.3
X-RAY DIFFRACTIONt_other_torsion21.66
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion2594SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact20801SEMIHARMONIC4
LS refinement shellResolution: 3.2→3.28 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.289 168 4.85 %
Rwork0.2369 3299 -
all0.2394 3467 -
obs--95.32 %
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)
13.78631.03433.327-0.17091.43756.88180.2572-0.21590.54960.2113-0.28290.11470.0145-0.52990.0257-0.3025-0.07660.19260.33150.06940.0834-53.5772-16.005177.9236
23.4462-0.21891.2256-0.0899-1.91118.23050.2226-0.5928-0.2523-0.2652-0.1162-0.23430.02020.0471-0.1064-0.3358-0.119-0.0033-0.09780.1642-0.1221-56.7775-18.295113.0642
33.29650.34553.26160.1369-0.24017.8626-0.0760.2620.0997-0.17310.11420.0581-0.12-0.5581-0.0381-0.3126-0.06480.08980.32820.0561-0.3195-60.52086.716692.5666
42.82260.3923.0518-0.08920.24877.87930.1159-0.0649-0.05620.0854-0.13370.04520.32570.52150.0178-0.3085-0.03250.08160.32550.1373-0.2605-10.57864.9851136.4966
53.25341.19313.3039-0.02570.21647.83780.0455-0.51830.01550.20890.26790.0380.3454-0.5599-0.3134-0.3227-0.0730.05130.33440.1475-0.1057-74.3939-26.932935.2027
62.80631.05461.2054-0.258-0.1318.16970.01990.1564-0.2997-0.02710.4010.01090.28880.426-0.4209-0.3307-0.0741-0.00350.33430.1448-0.1518-34.081-20.720157.08
71.03290.75022.3674-0.05941.93965.8224-0.008-0.5819-0.03020.2135-0.02640.0242-0.4207-0.35550.0344-0.2776-0.08230.04030.33290.0904-0.1498-39.650611.1663138.326
82.63490.77072.57950.3-1.69468.0204-0.22410.37230.2336-0.0009-0.0946-0.0297-0.46580.37640.3188-0.3047-0.06070.07040.32780.0718-0.1813-31.938213.371891.9742
98.95541.24512.0571.02250.86277.96960.2044-0.5645-0.08770.5099-0.35350.14530.58870.53740.14920.10740.05990.1145-0.1718-0.0669-0.3214-23.8233-15.257397.661
102.5419-0.3764-0.1066.9128-2.95023.54660.00930.5580.2052-0.43890.48710.53840.458-0.6594-0.49640.0893-0.1541-0.15190.03290.1757-0.1527-86.8336-23.4836-4.716
118.86412.18112.50962.7857-3.27658.0478-0.12830.56420.3527-0.5719-0.2201-0.29040.14470.24890.3484-0.0329-0.11310.00670.33360.0343-0.3077-57.134913.568757.5761
123.60461.63743.28884.88620.27927.833-0.072-0.5251-0.17070.5427-0.0564-0.09610.15130.10410.1284-0.2255-0.08330.0480.33530.1424-0.3168-11.726910.6182171.7251
130.0365-0.08510.0050.3369-0.22070.1804-0.00960.01570.0052-0.0250.01670.0328-0.01940.0192-0.00710.1239-0.09260.17850.17370.14510.2731-69.5937-42.242339.0096
140.17490.27780.3345-0.0736-0.28920.2929-0.0021-0.00070.0067-0.01430.0023-0.034-0.0522-0.0186-0.00030.1028-0.1404-0.10120.20550.11250.2063-33.015-35.627452.5974
15-0.2344-0.4944-1.52850.0843-0.26260.24250.0028-0.09130.01760.12860.00870.01610.0487-0.0493-0.01160.33160.10640.0029-0.11360.01690.3026-43.765124.9399134.3221
160.21890.4098-0.10790.1971-1.17880.546-0.0106-0.0336-0.0583-0.05860.0588-0.08980.0017-0.0003-0.04830.34710.15020.07540.18990.1119-0.0158-28.895727.994997.1072
174.12671.3263-1.58066.4504-2.17844.19510.0514-0.4952-0.5527-0.55410.3077-0.4630.4616-0.5757-0.3590.0472-0.1804-0.1328-0.26120.18670.0511-74.8352-48.99216.2438
183.33690.42430.79898.2405-0.93773.07890.02530.598-0.63170.03710.4442-0.35950.53130.1514-0.4694-0.04860.0158-0.08680.2868-0.125-0.2881-28.8624-41.870775.5766
192.5997-0.62692.58717.10110.38853.197-0.1801-0.06070.641-0.0431-0.17530.498-0.50250.03880.3554-0.1934-0.1461-0.1244-0.18110.1805-0.0708-44.599936.472480.6857
202.5195-0.21191.19724.0465-0.9623.6316-0.1413-0.05730.53890.4971-0.2273-0.4731-0.5436-0.21860.3686-0.1859-0.0282-0.13370.26530.1259-0.1048-25.022332.9758148.4807
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{A|1:61 123:216 256:296}
2X-RAY DIFFRACTION2{B|1:61 123:216 256:296}
3X-RAY DIFFRACTION3{C|1:61 123:216 256:296}
4X-RAY DIFFRACTION4{D|1:61 123:216 256:296}
5X-RAY DIFFRACTION5{A|62:122 217:255}
6X-RAY DIFFRACTION6{B|62:122 217:255}
7X-RAY DIFFRACTION7{C|62:122 217:255}
8X-RAY DIFFRACTION8{D|62:122 217:255}
9X-RAY DIFFRACTION9{A|297:394}
10X-RAY DIFFRACTION10{B|297:394}
11X-RAY DIFFRACTION11{C|297:394}
12X-RAY DIFFRACTION12{D|297:394}
13X-RAY DIFFRACTION13{A|567:567}
14X-RAY DIFFRACTION14{B|567:567}
15X-RAY DIFFRACTION15{C|567:567}
16X-RAY DIFFRACTION16{D|567:567}
17X-RAY DIFFRACTION17{H|1:112 L|1:106A}
18X-RAY DIFFRACTION18{I|1:112 M|1:106A}
19X-RAY DIFFRACTION19{J|1:112 N|2:106A}
20X-RAY DIFFRACTION20{K|1:112 O|3:106A}

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