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- PDB-5kve: Zika specific antibody, ZV-48, bound to ZIKA envelope DIII -

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Basic information

Entry
Database: PDB / ID: 5kve
TitleZika specific antibody, ZV-48, bound to ZIKA envelope DIII
Components
  • Genome polyprotein
  • ZV-48 Antibody scFv
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Zika virus / envelope protein / viral protein / single-chain variable fragment / structural genomics / Center for Structural Genomics of Infectious Diseases / CSGID / VIRAL PROTEIN-IMMUNE SYSTEM complex
Function / homology
Function and homology information


symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / flavivirin / 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 / negative regulation of innate immune response / ribonucleoside triphosphate phosphatase activity / viral capsid / nucleoside-triphosphate phosphatase / double-stranded RNA binding / 4 iron, 4 sulfur cluster binding ...symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / flavivirin / 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 / negative regulation of innate immune response / ribonucleoside triphosphate phosphatase activity / viral capsid / nucleoside-triphosphate phosphatase / double-stranded RNA binding / 4 iron, 4 sulfur cluster binding / 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 / molecular adaptor activity / host cell endoplasmic reticulum membrane / host cell perinuclear region of cytoplasm / protein dimerization activity / RNA helicase / induction by virus of host autophagy / symbiont entry into host cell / RNA-directed RNA polymerase / viral RNA genome replication / RNA-dependent RNA polymerase activity / serine-type endopeptidase activity / centrosome / fusion of virus membrane with host endosome membrane / viral envelope / lipid binding / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / host cell nucleus / virion attachment to host cell / GTP binding / virion membrane / structural molecule activity / ATP hydrolysis activity / proteolysis / extracellular region / ATP binding / membrane / metal ion binding
Similarity search - Function
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 NS3 helicase, C-terminal helical domain / Flavivirus non-structural protein NS2B / Genome polyprotein, Flavivirus ...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 NS3 helicase, C-terminal helical domain / 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 / Envelope glycoprotein M, flavivirus / Flavivirus envelope glycoprotein M / Flavivirus NS3, petidase S7 / Peptidase S7, Flavivirus NS3 serine protease / Flavivirus NS3 protease (NS3pro) domain profile. / 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 / DNA/RNA polymerase superfamily / Immunoglobulin-like / Sandwich / P-loop containing nucleoside triphosphate hydrolase / Mainly Beta
Similarity search - Domain/homology
ACETATE ION / Genome polyprotein / Genome polyprotein
Similarity search - Component
Biological speciesZika virus
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.7 Å
AuthorsZhao, H. / Nelson, C.A. / Fremont, D.H. / Center for Structural Genomics of Infectious Diseases (CSGID)
CitationJournal: Cell / Year: 2016
Title: Structural Basis of Zika Virus-Specific Antibody Protection.
Authors: Zhao, H. / Fernandez, E. / Dowd, K.A. / Speer, S.D. / Platt, D.J. / Gorman, M.J. / Govero, J. / Nelson, C.A. / Pierson, T.C. / Diamond, M.S. / Fremont, D.H.
History
DepositionJul 14, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 10, 2016Provider: repository / Type: Initial release
Revision 1.1Aug 24, 2016Group: Database references
Revision 2.0Dec 25, 2019Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Polymer sequence / Refinement description / Source and taxonomy / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / entity / entity_poly / entity_poly_seq / entity_src_gen / entity_src_nat / pdbx_distant_solvent_atoms / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_poly_seq_scheme / pdbx_refine_tls_group / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_oper_list / pdbx_struct_sheet_hbond / pdbx_struct_special_symmetry / pdbx_unobs_or_zero_occ_residues / pdbx_validate_close_contact / pdbx_validate_symm_contact / pdbx_validate_torsion / struct_asym / struct_conf / struct_conn / struct_mon_prot_cis / struct_ref / struct_ref_seq / struct_sheet_range / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _atom_site.label_seq_id / _atom_site.pdbx_PDB_ins_code / _atom_site_anisotrop.pdbx_PDB_ins_code / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_seq_id / _entity_poly_seq.entity_id / _entity_poly_seq.num / _pdbx_distant_solvent_atoms.auth_asym_id / _pdbx_distant_solvent_atoms.auth_seq_id / _pdbx_distant_solvent_atoms.neighbor_ligand_distance / _pdbx_distant_solvent_atoms.neighbor_macromolecule_distance / _pdbx_entity_nonpoly.entity_id / _pdbx_nonpoly_scheme.asym_id / _pdbx_nonpoly_scheme.auth_seq_num / _pdbx_nonpoly_scheme.entity_id / _pdbx_nonpoly_scheme.ndb_seq_num / _pdbx_nonpoly_scheme.pdb_seq_num / _pdbx_nonpoly_scheme.pdb_strand_id / _pdbx_poly_seq_scheme.asym_id / _pdbx_poly_seq_scheme.entity_id / _pdbx_poly_seq_scheme.ndb_seq_num / _pdbx_poly_seq_scheme.pdb_ins_code / _pdbx_poly_seq_scheme.pdb_seq_num / _pdbx_poly_seq_scheme.pdb_strand_id / _pdbx_poly_seq_scheme.seq_id / _pdbx_refine_tls_group.beg_auth_asym_id / _pdbx_refine_tls_group.beg_auth_seq_id / _pdbx_refine_tls_group.end_auth_asym_id / _pdbx_refine_tls_group.end_auth_seq_id / _pdbx_refine_tls_group.selection_details / _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_assembly.oligomeric_count / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_PDB_ins_code / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_PDB_ins_code / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_oper_list.symmetry_operation / _pdbx_struct_sheet_hbond.range_1_PDB_ins_code / _pdbx_struct_sheet_hbond.range_1_auth_asym_id / _pdbx_struct_sheet_hbond.range_1_auth_seq_id / _pdbx_struct_sheet_hbond.range_1_label_asym_id / _pdbx_struct_sheet_hbond.range_1_label_seq_id / _pdbx_struct_sheet_hbond.range_2_PDB_ins_code / _pdbx_struct_sheet_hbond.range_2_auth_asym_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_asym_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _pdbx_struct_special_symmetry.label_asym_id / _pdbx_unobs_or_zero_occ_residues.auth_asym_id / _pdbx_unobs_or_zero_occ_residues.auth_seq_id / _pdbx_unobs_or_zero_occ_residues.label_asym_id / _pdbx_unobs_or_zero_occ_residues.label_seq_id / _pdbx_validate_close_contact.PDB_ins_code_1 / _pdbx_validate_close_contact.auth_asym_id_1 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_1 / _pdbx_validate_close_contact.auth_seq_id_2 / _pdbx_validate_symm_contact.auth_seq_id_2 / _pdbx_validate_torsion.auth_asym_id / _pdbx_validate_torsion.auth_seq_id / _struct_conf.beg_auth_asym_id / _struct_conf.beg_auth_seq_id / _struct_conf.beg_label_asym_id / _struct_conf.beg_label_seq_id / _struct_conf.end_auth_asym_id / _struct_conf.end_auth_seq_id / _struct_conf.end_label_asym_id / _struct_conf.end_label_seq_id / _struct_conn.pdbx_ptnr1_PDB_ins_code / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_seq_id / _struct_mon_prot_cis.auth_seq_id / _struct_mon_prot_cis.pdbx_auth_seq_id_2 / _struct_sheet_range.beg_auth_asym_id / _struct_sheet_range.beg_auth_seq_id / _struct_sheet_range.beg_label_asym_id / _struct_sheet_range.beg_label_seq_id / _struct_sheet_range.end_auth_asym_id / _struct_sheet_range.end_auth_seq_id / _struct_sheet_range.end_label_asym_id / _struct_sheet_range.end_label_seq_id / _struct_sheet_range.pdbx_beg_PDB_ins_code / _struct_sheet_range.pdbx_end_PDB_ins_code / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_seq_id / _struct_site_gen.auth_asym_id / _struct_site_gen.auth_seq_id / _struct_site_gen.label_asym_id / _struct_site_gen.label_seq_id / _struct_site_gen.pdbx_auth_ins_code

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
E: Genome polyprotein
L: ZV-48 Antibody scFv
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,07212
Polymers38,3622
Non-polymers70910
Water11,115617
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3150 Å2
ΔGint-64 kcal/mol
Surface area15220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)63.240, 87.980, 147.520
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
Components on special symmetry positions
IDModelComponents
11E-642-

HOH

21E-728-

HOH

31E-778-

HOH

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Components

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Protein / Antibody , 2 types, 2 molecules EL

#1: Protein Genome polyprotein


Mass: 11935.734 Da / Num. of mol.: 1 / Fragment: UNP residues 589-697
Source method: isolated from a genetically manipulated source
Details: refolded / Source: (gene. exp.) Zika virus / Strain: Mr 766 / Plasmid: pET21a(+) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)RIL / References: UniProt: A0A142DS37, UniProt: A0A024B7W1*PLUS
#2: Antibody ZV-48 Antibody scFv


Mass: 26426.490 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Strain: C57BL/6, Irf3 knockout / Description: HYBRIDOMA MONOCLONAL ANTIBODY / Production host: Escherichia coli BL21(DE3) (bacteria)

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Non-polymers , 5 types, 627 molecules

#3: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Na
#4: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: SO4
#5: Chemical ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: C2H6O2
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 617 / Source method: isolated from a natural source / Formula: H2O

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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: 2.47 Å3/Da / Density % sol: 50.23 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: 0.2 M Ammonium sulfate,15 %(w/v) PEG 4000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 4.2.2 / Wavelength: 1.00004 Å
DetectorType: RDI CMOS_8M / Detector: CMOS / Date: May 28, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00004 Å / Relative weight: 1
ReflectionResolution: 1.65→37.441 Å / Num. obs: 44574 / % possible obs: 98.9 % / Observed criterion σ(I): -3 / Redundancy: 14.5 % / Biso Wilson estimate: 20.95 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.059 / Net I/σ(I): 18.76
Reflection shell
Resolution (Å)Highest resolution (Å)Rmerge(I) obsMean I/σ(I) obsCC1/2Diffraction-ID% possible all
1.65-1.690.9892.040.711100
1.69-1.740.8012.590.767199.9
1.74-1.790.593.440.8541100
1.79-1.840.4574.180.9051100
1.84-1.910.4754.080.925194.4
1.91-1.970.2716.570.971194.2
1.97-2.050.2018.980.979199.9
2.05-2.130.1611.950.985199.8
2.13-2.220.12814.280.992199.2
2.22-2.330.10816.470.992197
2.33-2.460.08220.770.9961100
2.46-2.610.06526.390.9971100
2.61-2.790.05330.850.9981100
2.79-3.010.04137.510.9991100
3.01-3.30.03344.210.9991100
3.3-3.690.03245.840.999199.9
3.69-4.260.03148.130.999199.7
4.26-5.220.02460.690.999199.9
5.22-7.380.02261.190.9991100
7.380.02161.040.999194.6

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Processing

Software
NameVersionClassification
PHENIX1.10_2155refinement
XSCALEdata scaling
PDB_EXTRACT3.2data extraction
XDSdata reduction
PHASERphasing
RefinementResolution: 1.7→48.497 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.87 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2127 2078 5.15 %
Rwork0.1868 --
obs0.1881 44558 97.66 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.7→48.497 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2554 0 39 617 3210
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0032648
X-RAY DIFFRACTIONf_angle_d0.6673591
X-RAY DIFFRACTIONf_dihedral_angle_d11.7391563
X-RAY DIFFRACTIONf_chiral_restr0.046390
X-RAY DIFFRACTIONf_plane_restr0.004449
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.7-1.7370.32191460.30992547X-RAY DIFFRACTION96
1.737-1.77740.33841430.30012555X-RAY DIFFRACTION96
1.7774-1.82180.29991460.282585X-RAY DIFFRACTION97
1.8218-1.87110.25261260.25442620X-RAY DIFFRACTION97
1.8711-1.92610.25041540.25132581X-RAY DIFFRACTION97
1.9261-1.98830.23421410.22072579X-RAY DIFFRACTION97
1.9883-2.05940.23861390.19952598X-RAY DIFFRACTION98
2.0594-2.14180.23431370.19642630X-RAY DIFFRACTION98
2.1418-2.23930.23871260.19262640X-RAY DIFFRACTION98
2.2393-2.35740.21921540.19572644X-RAY DIFFRACTION98
2.3574-2.50510.22831470.18992641X-RAY DIFFRACTION98
2.5051-2.69850.19711360.18042687X-RAY DIFFRACTION98
2.6985-2.970.21751360.17822683X-RAY DIFFRACTION99
2.97-3.39970.20871470.16192707X-RAY DIFFRACTION99
3.3997-4.28280.18781610.1462713X-RAY DIFFRACTION99
4.2828-48.51620.15781560.16452853X-RAY DIFFRACTION99
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)
14.5584-0.00051.60462.6381-1.33567.1618-0.1741-0.24430.13480.08440.07150.0744-0.65380.32940.10.206-0.060.0050.2152-0.03080.149743.31315.8589165.1202
21.315-0.00050.87472.4058-0.35.85550.00690.2847-0.0803-0.18680.1217-0.2561-0.17940.5077-0.13010.1662-0.04420.03180.21050.02540.200941.988512.4882149.5055
36.37540.43632.67261.0238-0.48462.4069-0.1772-0.15930.19580.07440.0432-0.0349-0.35310.13130.12320.1763-0.02870.01960.17660.01680.100936.175414.5613162.8277
42.0225-2.2185-4.32993.73362.78853.7942-0.4866-0.3705-0.36810.41110.323-0.09560.49720.41260.12820.19710.0253-0.01560.2330.03430.191234.39955.2907158.6356
55.75894.24052.46138.04793.06576.0003-0.20090.31350.0626-0.19410.1514-0.3707-0.3910.98070.03430.1725-0.03870.02460.33750.03240.232448.055514.8436159.5551
62.0415-0.16375.15932.1907-0.27639.4955-0.0930.1037-0.2849-0.50820.16770.1751-0.0201-0.02120.03880.1196-0.01690.02140.13310.00930.207130.239.4413152.0991
72.00780.67220.21232.0046-1.14152.0082-0.0219-1.1331.23030.35760.01171.1422-1.0417-0.22920.03050.34280.02850.01140.314-0.08620.43733.507521.6842164.0568
86.66910.68112.28915.65692.12399.8548-0.09070.51540.0573-0.3802-0.05350.25710.0653-0.42520.09240.2179-0.0522-0.0010.14860.06870.147731.360312.5351148.4889
94.07871.3664-3.04822.88711.1699.6928-0.3768-0.1152-0.45540.143-0.011-0.03870.91580.30770.36210.2650.02760.05240.17980.05060.267919.0254-3.5579171.5716
100.7389-0.5339-1.08632.85342.04762.2658-0.354-0.4326-0.2080.42690.18340.31530.7180.13530.14720.3076-0.01150.06630.47030.10320.226110.22575.388190.968
118.8827-5.0619-8.9889.87289.89522.0077-0.0809-0.63480.0456-0.03510.2032-0.18220.57280.4468-0.08620.23190.050.03030.28270.06450.172218.94391.8257182.2884
125.74781.1178-1.30081.7333-2.17344.8892-0.1092-0.1908-0.1962-0.1277-0.1251-0.13450.17930.61140.21270.13310.03090.01310.20060.0450.121630.73525.2439169.1561
138.69580.1115-1.48370.7585-0.79612.1407-0.0478-0.11560.21030.00170.03180.18140.089-0.49280.0270.1650.00290.02210.3363-0.01210.132711.2411.5044175.4161
143.41330.6424-1.57572.1701-1.14464.53290.0298-0.34020.16360.26250.00060.1211-0.4419-0.062-0.00430.2071-0.00640.00640.2837-0.00730.15621.051915.0538179.4649
152.0411-7.9998-7.72252.04532.00292.023-0.6765-0.9573-0.41570.77720.32070.24040.94340.68770.33830.21980.02390.03250.4036-0.01470.246622.42394.6834181.4963
166.52883.26154.81145.47992.8097.0980.0346-0.09320.29030.0633-0.22020.0454-0.2575-0.31630.15090.18920.04440.0180.3795-0.01730.18078.903114.1825188.2427
171.2359-0.0388-0.17421.44770.6252.1149-0.1993-0.1813-0.22860.08610.0470.09270.32910.12920.12690.16250.01910.02280.16450.02040.153916.9464.0918169.907
184.0985-0.9766-2.34126.88053.62292.0064-0.7938-0.3703-0.55860.8268-0.32011.08220.9881-0.85191.1280.2564-0.02660.08280.59980.03160.29985.44695.344187.8546
196.46936.51450.29042.0695-0.72295.1790.1949-0.19031.32430.2323-0.55611.6439-0.3065-0.5540.40990.21330.08040.00820.2282-0.1060.533-0.134715.055161.4059
206.11533.32791.02537.69471.32283.27850.01070.05330.0391-0.1431-0.36910.0437-0.2035-0.24610.34250.14330.05-0.02580.1799-0.00740.13755.16113.8209155.4598
217.10060.3814-0.79366.0420.14364.56740.0373-0.6826-0.28250.3624-0.17830.54280.4888-0.4190.12420.162-0.03710.02670.2423-0.00910.14338.16325.3477164.4452
225.5537-1.97840.14733.51-1.9279.294-0.13460.37450.1162-0.2931-0.2326-0.2585-0.03270.38210.29810.11380.0064-0.01540.1426-0.01410.147814.63269.374154.62
237.99273.8586-0.09384.6687-0.50094.46350.22670.4893-0.5253-0.0254-0.2286-0.01660.40020.1102-0.02880.23550.02920.01220.1892-0.05720.189712.103-0.8935154.7122
241.7513-1.2880.05158.0682-2.77353.32020.11710.275-0.058-0.2694-0.17650.28410.0259-0.18750.05660.16560.0118-0.04130.1888-0.02460.16575.687812.3932150.8389
254.8920.40751.54431.40341.11574.7254-0.126-0.0451-0.2058-0.108-0.14760.12490.2745-0.08350.28380.14040.01250.03330.1157-0.00140.1216.43416.4614162.4275
262.13365.43134.06177.2053.19025.6248-0.1254-0.29280.07510.0671-0.16490.69880.1406-0.3350.33120.1326-0.01260.0640.2676-0.08660.2552.28119.7573164.6076
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN E AND RESID 303:311 )E303 - 311
2X-RAY DIFFRACTION2( CHAIN E AND RESID 312:329 )E312 - 329
3X-RAY DIFFRACTION3( CHAIN E AND RESID 330:348 )E330 - 348
4X-RAY DIFFRACTION4( CHAIN E AND RESID 349:358 )E349 - 358
5X-RAY DIFFRACTION5( CHAIN E AND RESID 359:375 )E359 - 375
6X-RAY DIFFRACTION6( CHAIN E AND RESID 376:386 )E376 - 386
7X-RAY DIFFRACTION7( CHAIN E AND RESID 387:392 )E387 - 392
8X-RAY DIFFRACTION8( CHAIN E AND RESID 393:400 )E393 - 400
9X-RAY DIFFRACTION9( CHAIN L AND RESID 0:7 )L0 - 7
10X-RAY DIFFRACTION10( CHAIN L AND RESID 8:18 )L8 - 18
11X-RAY DIFFRACTION11( CHAIN L AND RESID 19:25 )L19 - 25
12X-RAY DIFFRACTION12( CHAIN L AND RESID 26:38 )L26 - 38
13X-RAY DIFFRACTION13( CHAIN L AND RESID 39:54 )L39 - 54
14X-RAY DIFFRACTION14( CHAIN L AND RESID 55:73 )L55 - 73
15X-RAY DIFFRACTION15( CHAIN L AND RESID 74:81 )L74 - 81
16X-RAY DIFFRACTION16( CHAIN L AND RESID 82:89 )L82 - 89
17X-RAY DIFFRACTION17( CHAIN L AND RESID 90:107 )L90 - 107
18X-RAY DIFFRACTION18( CHAIN L AND RESID 108:114 )L108 - 114
19X-RAY DIFFRACTION19( CHAIN L AND RESID 129:140 )L129 - 140
20X-RAY DIFFRACTION20( CHAIN L AND RESID 141:160 )L141 - 160
21X-RAY DIFFRACTION21( CHAIN L AND RESID 161:173 )L161 - 173
22X-RAY DIFFRACTION22( CHAIN L AND RESID 174:185 )L174 - 185
23X-RAY DIFFRACTION23( CHAIN L AND RESID 186:195 )L186 - 195
24X-RAY DIFFRACTION24( CHAIN L AND RESID 196:214 )L196 - 214
25X-RAY DIFFRACTION25( CHAIN L AND RESID 215:231 )L215 - 231
26X-RAY DIFFRACTION26( CHAIN L AND RESID 232:243 )L232 - 243

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