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- PDB-6p95: Structure of Lassa virus glycoprotein in complex with Fab 25.6A -

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Basic information

Entry
Database: PDB / ID: 6p95
TitleStructure of Lassa virus glycoprotein in complex with Fab 25.6A
Components
  • (FAB Antibody ...) x 2
  • (Pre-glycoprotein polyprotein GP ...) x 2
Keywordsviral protein/immune system / Lassa virus / glycoprotein / antibody / VIRAL PROTEIN / viral protein-immune system complex
Function / homology
Function and homology information


host cell Golgi membrane / receptor-mediated endocytosis of virus by host cell / host cell endoplasmic reticulum membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / metal ion binding / membrane
Similarity search - Function
Arenavirus glycoprotein, zinc binding domain / Arenavirus glycoprotein / Arenavirus glycoprotein / Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Pre-glycoprotein polyprotein GP complex
Similarity search - Component
Biological speciesLassa virus
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å
AuthorsSaphire, E.O. / Hastie, K.M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)U19AI109762-05 United States
CitationJournal: Cell / Year: 2019
Title: Convergent Structures Illuminate Features for Germline Antibody Binding and Pan-Lassa Virus Neutralization.
Authors: Hastie, K.M. / Cross, R.W. / Harkins, S.S. / Zandonatti, M.A. / Koval, A.P. / Heinrich, M.L. / Rowland, M.M. / Robinson, J.E. / Geisbert, T.W. / Garry, R.F. / Branco, L.M. / Saphire, E.O.
History
DepositionJun 9, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 11, 2019Provider: repository / Type: Initial release
Revision 1.1Dec 18, 2019Group: Author supporting evidence / Data collection / Category: chem_comp / pdbx_audit_support
Item: _chem_comp.type / _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_validate_close_contact / struct_asym / struct_conn / 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_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _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 / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 11, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Oct 30, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Pre-glycoprotein polyprotein GP complex
B: Pre-glycoprotein polyprotein GP complex
C: Pre-glycoprotein polyprotein GP complex
D: FAB Antibody heavy chain
E: FAB Antibody light chain
F: FAB Antibody heavy chain
G: FAB Antibody light chain
H: FAB Antibody heavy chain
L: FAB Antibody light chain
a: Pre-glycoprotein polyprotein GP complex
b: Pre-glycoprotein polyprotein GP complex
c: Pre-glycoprotein polyprotein GP complex
hetero molecules


Theoretical massNumber of molelcules
Total (without water)305,48240
Polymers292,39512
Non-polymers13,08728
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: light scattering, gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area44490 Å2
ΔGint-226 kcal/mol
Surface area92160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)152.242, 152.242, 453.889
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number178
Space group name H-MP6122
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 59 through 148 or resid 152...
21(chain B and (resid 59 through 253 or resid 1089...
31(chain C and (resid 59 through 148 or resid 152...
12chain D
22chain F
32(chain H and (resid 1 through 148 or resid 150 through 230))
13(chain E and resid 2 through 213)
23(chain G and resid 2 through 213)
33(chain L and resid 2 through 213)
14(chain a and (resid 262 through 266 or resid 275...
24(chain b and (resid 262 through 416 or resid 1374))
34(chain c and (resid 262 through 266 or resid 275 through 416 or resid 1366))

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 59 through 148 or resid 152...A59 - 148
121(chain A and (resid 59 through 148 or resid 152...A152 - 168
131(chain A and (resid 59 through 148 or resid 152...A180 - 253
141(chain A and (resid 59 through 148 or resid 152...A1080
151(chain A and (resid 59 through 148 or resid 152...A1089 - 1099
161(chain A and (resid 59 through 148 or resid 152...A1167 - 1224
211(chain B and (resid 59 through 253 or resid 1089...B59 - 253
221(chain B and (resid 59 through 253 or resid 1089...B1089
231(chain B and (resid 59 through 253 or resid 1089...B1099 - 1110
241(chain B and (resid 59 through 253 or resid 1089...B1167 - 1224
311(chain C and (resid 59 through 148 or resid 152...C59 - 148
321(chain C and (resid 59 through 148 or resid 152...C152 - 168
331(chain C and (resid 59 through 148 or resid 152...C180 - 253
341(chain C and (resid 59 through 148 or resid 152...C1089
351(chain C and (resid 59 through 148 or resid 152...C1099 - 1110
361(chain C and (resid 59 through 148 or resid 152...C1224 - 1225
112chain DD1 - 230
212chain FF1 - 230
312(chain H and (resid 1 through 148 or resid 150 through 230))H1 - 148
322(chain H and (resid 1 through 148 or resid 150 through 230))H150 - 230
113(chain E and resid 2 through 213)E2 - 213
213(chain G and resid 2 through 213)G2 - 213
313(chain L and resid 2 through 213)L2 - 213
114(chain a and (resid 262 through 266 or resid 275...a262 - 266
124(chain a and (resid 262 through 266 or resid 275...a275 - 329
134(chain a and (resid 262 through 266 or resid 275...a333 - 416
144(chain a and (resid 262 through 266 or resid 275...a1373
214(chain b and (resid 262 through 416 or resid 1374))b262 - 416
224(chain b and (resid 262 through 416 or resid 1374))b1374
314(chain c and (resid 262 through 266 or resid 275 through 416 or resid 1366))c262 - 266
324(chain c and (resid 262 through 266 or resid 275 through 416 or resid 1366))c275 - 416
334(chain c and (resid 262 through 266 or resid 275 through 416 or resid 1366))c1366

NCS ensembles :
ID
1
2
3
4

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Components

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Pre-glycoprotein polyprotein GP ... , 2 types, 6 molecules ABCabc

#1: Protein Pre-glycoprotein polyprotein GP complex


Mass: 29098.430 Da / Num. of mol.: 3 / Mutation: R207C, L258R, L259RG
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lassa virus / Strain: Mouse/Sierra Leone/Josiah/1976 / Gene: GPC, GP-C / Production host: Drosophila melanogaster (fruit fly) / References: UniProt: P08669
#4: Protein Pre-glycoprotein polyprotein GP complex / Pre-GP-C


Mass: 20800.529 Da / Num. of mol.: 3 / Mutation: G360P, M332T, E329C
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lassa virus (strain Mouse/Sierra Leone/Josiah/1976)
Strain: Mouse/Sierra Leone/Josiah/1976 / Gene: GPC, GP-C / Production host: Drosophila melanogaster (fruit fly) / References: UniProt: P08669

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Antibody , 2 types, 6 molecules DFHEGL

#2: Antibody FAB Antibody heavy chain


Mass: 24513.430 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Cricetulus griseus (Chinese hamster)
#3: Antibody FAB Antibody light chain


Mass: 23052.520 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Production host: Cricetulus griseus (Chinese hamster)

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Sugars , 7 types, 28 molecules

#5: Polysaccharide
beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#6: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 7
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#7: Polysaccharide alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 748.682 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3/a4-b1_b4-c1_c3-d1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#8: Polysaccharide alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_d2-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#9: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 910.823 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#10: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#11: 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


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 9
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6 / Feature type: SUBJECT OF INVESTIGATION
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

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Details

Has ligand of interestY
Has protein modificationY

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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: 2.6 Å3/Da / Density % sol: 52.63 % / Description: Hexagonal rods
Crystal growTemperature: 295 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 0.1 M Tris pH 8, 15-18% PEG 3350 and 0.1 M-0.3 M magnesium acetate

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Data collection

DiffractionMean temperature: 80 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-B / Wavelength: 1.033188 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 17, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033188 Å / Relative weight: 1
ReflectionResolution: 3.5→29.982 Å / Num. obs: 40281 / % possible obs: 99.8 % / Redundancy: 13.3 % / CC1/2: 0.999 / Rmerge(I) obs: 0.148 / Rpim(I) all: 0.041 / Rrim(I) all: 0.153 / Net I/σ(I): 17.4
Reflection shell

Diffraction-ID: 1 / Resolution: 3.5→3.64 Å

Redundancy (%)Rmerge(I) obsNum. unique obsCC1/2Rpim(I) allRrim(I) all% possible all
13.31.42944480.6830.4041.486100
11.70.02894210.0080.02992.5

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Processing

Software
NameVersionClassification
PHENIX1.15.2_3472refinement
Aimless0.5.27data scaling
PDB_EXTRACT3.25data extraction
XDSdata reduction
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5VK2

5vk2


Resolution: 3.5→29.66 Å / SU ML: 0.49 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 24.66
RfactorNum. reflection% reflection
Rfree0.2472 2001 4.98 %
Rwork0.205 --
obs0.2072 40161 99.93 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 296.64 Å2 / Biso mean: 123.5259 Å2 / Biso min: 55.16 Å2
Refinement stepCycle: final / Resolution: 3.5→29.66 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17729 0 864 0 18593
Biso mean--168.83 --
Num. residues----2299
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1722X-RAY DIFFRACTION2.873TORSIONAL
12B1722X-RAY DIFFRACTION2.873TORSIONAL
13C1722X-RAY DIFFRACTION2.873TORSIONAL
21D1971X-RAY DIFFRACTION2.873TORSIONAL
22F1971X-RAY DIFFRACTION2.873TORSIONAL
23H1971X-RAY DIFFRACTION2.873TORSIONAL
31E1902X-RAY DIFFRACTION2.873TORSIONAL
32G1902X-RAY DIFFRACTION2.873TORSIONAL
33L1902X-RAY DIFFRACTION2.873TORSIONAL
41a1302X-RAY DIFFRACTION2.873TORSIONAL
42b1302X-RAY DIFFRACTION2.873TORSIONAL
43c1302X-RAY DIFFRACTION2.873TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
3.5001-3.58740.41091360.3577264999
3.5874-3.68430.34661350.29092669100
3.6843-3.79250.27831360.25942680100
3.7925-3.91460.29011380.24022677100
3.9146-4.05420.27191440.22852657100
4.0542-4.21610.26871230.21742713100
4.2161-4.40750.20841330.18192686100
4.4075-4.6390.23491410.16862710100
4.639-4.92850.23231420.17522716100
4.9285-5.30710.22931540.17532709100
5.3071-5.83760.2621490.19632747100
5.8376-6.67420.23991450.21072758100
6.6742-8.37830.24221560.20542810100
8.37-29.660.22141690.19292979100
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.00310.3259-0.0712.0493-0.175.6999-0.08830.78170.1745-0.47220.2623-0.1364-0.2033-0.1596-0.08820.93880.0890.20051.20090.26450.9596-54.210860.3509-10.8053
20.7166-0.03340.80113.61952.58344.10490.0740.1426-0.1040.521-0.0808-0.02240.2673-0.1338-0.13410.64850.12930.01710.99150.18330.8712-55.047752.24712.7265
33.47130.5058-0.42141.4645-0.03475.3868-0.00571.04930.5953-0.420.0350.34690.2021-0.1385-0.0720.77040.0911-0.22561.39090.26731.0097-89.26759.3401-11.5071
44.03852.11110.86132.5298-0.12514.23710.3874-0.48290.34750.3888-0.2641-0.1601-0.0047-0.3103-0.05510.75480.0806-0.03731.0560.01041.0149-85.165258.21812.0664
53.6649-0.4001-1.1842.2628-1.83055.35770.09870.8128-0.3552-0.4356-0.16440.1190.13880.52120.06971.11950.2077-0.05931.4291-0.24561.1022-69.990429.2726-14.1659
64.3012-1.7201-0.14712.3775-0.28884.0717-0.1464-0.9575-0.12650.42230.230.76350.0787-0.1187-0.00190.63350.08850.08331.1536-0.02371.2112-75.85530.37519.9755
71.6371-1.42850.48595.6102-0.68764.4719-0.1849-0.0070.03410.4589-0.1039-0.01190.0203-0.12250.27030.68370.0375-0.01960.68680.12680.708-63.034685.674623.2832
83.32741.9188-1.38882.50020.26663.16950.1625-0.1602-0.28090.2536-0.0275-0.1020.3638-0.2997-0.1050.6713-0.0846-0.14661.18620.16030.8003-110.925534.680716.0893
95.4816-1.7531-0.1662.555-1.38324.5976-0.3403-0.1985-0.15540.37680.24310.176-0.2167-0.52720.08590.61180.16020.01250.7196-0.00730.7139-43.452519.402518.8566
102.70330.2970.52275.91961.90135.48770.40190.00250.09590.0569-0.1985-0.4691-0.28-0.025-0.21480.6069-0.0148-0.18540.82810.0560.8355-56.8692117.219427.6541
112.77460.2412-1.03282.47310.94885.85770.01260.00860.227-0.14720.04140.3707-0.1346-0.3374-0.11240.678-0.06250.05221.17250.21320.9821-142.147426.23314.9085
123.3339-0.3899-0.3385.8995-1.73646.1233-0.11540.1169-0.3069-0.03520.049-0.32490.39650.01390.05260.65840.0928-0.11930.67170.11460.728-20.0796-2.916820.6141
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and ((resseq 59:255))A59 - 255
2X-RAY DIFFRACTION2chain 'a' and ((resseq 262:416))a262 - 416
3X-RAY DIFFRACTION3chain 'B' and ((resseq 59:253))B59 - 253
4X-RAY DIFFRACTION4chain 'b' and ((resseq 261:416))b261 - 416
5X-RAY DIFFRACTION5chain 'C' and ((resseq 59:256))C59 - 256
6X-RAY DIFFRACTION6chain 'c' and ((resseq 262:416))c262 - 416
7X-RAY DIFFRACTION7(chain 'D' and ((resseq 2:123))) or (chain 'E' and ((resseq 2:111)))D0
8X-RAY DIFFRACTION8(chain 'F' and ((resseq 2:123))) or (chain 'G' and ((resseq 3:111)))F0
9X-RAY DIFFRACTION9(chain 'H' and ((resseq 2:123))) or (chain 'L' and ((resseq 3:111)))H0
10X-RAY DIFFRACTION10(chain 'D' and ((resseq 124:226))) or (chain 'E' and ((resseq 112:214)))D0
11X-RAY DIFFRACTION11(chain 'F' and ((resseq 124:226))) or (chain 'G' and ((resseq 112:214)))F0
12X-RAY DIFFRACTION12(chain 'H' and ((resseq 124:226))) or (chain 'L' and ((resseq 112:214)))H0

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