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- PDB-5jlv: Receptor binding domain of Botulinum neurotoxin A in complex with... -

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Basic information

Entry
Database: PDB / ID: 5jlv
TitleReceptor binding domain of Botulinum neurotoxin A in complex with human glycosylated SV2C
Components
  • Botulinum neurotoxin type A
  • Synaptic vesicle glycoprotein 2C
KeywordsHYDROLASE / glycosylation / botulinum neurotoxin / receptor binding domain
Function / homology
Function and homology information


Toxicity of botulinum toxin type F (botF) / host cell junction / Toxicity of botulinum toxin type D (botD) / Toxicity of botulinum toxin type A (botA) / negative regulation of neurotransmitter secretion / bontoxilysin / dopaminergic synapse / host cell presynaptic membrane / host cell cytoplasmic vesicle / host cell cytosol ...Toxicity of botulinum toxin type F (botF) / host cell junction / Toxicity of botulinum toxin type D (botD) / Toxicity of botulinum toxin type A (botA) / negative regulation of neurotransmitter secretion / bontoxilysin / dopaminergic synapse / host cell presynaptic membrane / host cell cytoplasmic vesicle / host cell cytosol / neurotransmitter transport / regulation of synaptic vesicle exocytosis / protein transmembrane transporter activity / transmembrane transporter activity / membrane => GO:0016020 / metalloendopeptidase activity / synaptic vesicle / synaptic vesicle membrane / toxin activity / chemical synaptic transmission / host cell plasma membrane / proteolysis / extracellular region / zinc ion binding / membrane / plasma membrane
Similarity search - Function
E3 ubiquitin-protein ligase SopA / : / SV2A/B/C luminal domain / Synaptic vesicle protein SV2 / Sugar transporter, conserved site / Major facilitator, sugar transporter-like / Sugar (and other) transporter / Clostridium neurotoxin, translocation / Clostridium neurotoxin, Translocation domain / Clostridium neurotoxin, translocation domain ...E3 ubiquitin-protein ligase SopA / : / SV2A/B/C luminal domain / Synaptic vesicle protein SV2 / Sugar transporter, conserved site / Major facilitator, sugar transporter-like / Sugar (and other) transporter / Clostridium neurotoxin, translocation / Clostridium neurotoxin, Translocation domain / Clostridium neurotoxin, translocation domain / Clostridial neurotoxin zinc protease / Botulinum/Tetanus toxin, catalytic chain / Clostridium neurotoxin, receptor-binding C-terminal / Clostridium neurotoxin, receptor binding N-terminal / Clostridium neurotoxin, C-terminal receptor binding / Clostridium neurotoxin, N-terminal receptor binding / Pectate Lyase C-like / Kunitz inhibitor STI-like superfamily / Major facilitator superfamily / Major Facilitator Superfamily / 3 Solenoid / Major facilitator superfamily domain / Major facilitator superfamily (MFS) profile. / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / MFS transporter superfamily / Jelly Rolls - #200 / Neutral zinc metallopeptidases, zinc-binding region signature. / Concanavalin A-like lectin/glucanase domain superfamily / Jelly Rolls / Sandwich / Mainly Beta
Similarity search - Domain/homology
ACETATE ION / PHOSPHATE ION / Botulinum neurotoxin type A / Botulinum neurotoxin type A / Synaptic vesicle glycoprotein 2C
Similarity search - Component
Biological speciesClostridium botulinum (bacteria)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsYao, G. / Zhang, S. / Mahrhold, S. / Lam, K. / Stern, D. / Bagramyan, K. / Perry, K. / Kalkum, M. / Rummel, A. / Dong, M. / Jin, R.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI123920 United States
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2016
Title: N-linked glycosylation of SV2 is required for binding and uptake of botulinum neurotoxin A.
Authors: Yao, G. / Zhang, S. / Mahrhold, S. / Lam, K.H. / Stern, D. / Bagramyan, K. / Perry, K. / Kalkum, M. / Rummel, A. / Dong, M. / Jin, R.
History
DepositionApr 27, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 15, 2016Provider: repository / Type: Initial release
Revision 1.1Aug 3, 2016Group: Database references
Revision 1.2Sep 27, 2017Group: Advisory / Author supporting evidence / Derived calculations
Category: pdbx_audit_support / pdbx_struct_oper_list / pdbx_unobs_or_zero_occ_atoms
Item: _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Dec 11, 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: Atomic model / Data collection ...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_struct_special_symmetry / 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.occupancy / _atom_site.type_symbol / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_special_symmetry.label_asym_id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 27, 2023Group: Advisory / Data collection ...Advisory / Data collection / Database references / Derived calculations / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_unobs_or_zero_occ_atoms / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag
Revision 2.2Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Botulinum neurotoxin type A
B: Botulinum neurotoxin type A
C: Synaptic vesicle glycoprotein 2C
D: Synaptic vesicle glycoprotein 2C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)128,92313
Polymers126,9374
Non-polymers1,9869
Water11,872659
1
A: Botulinum neurotoxin type A
C: Synaptic vesicle glycoprotein 2C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,6717
Polymers63,4682
Non-polymers1,2035
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Botulinum neurotoxin type A
D: Synaptic vesicle glycoprotein 2C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,2526
Polymers63,4682
Non-polymers7844
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)109.002, 111.853, 126.253
Angle α, β, γ (deg.)90.00, 101.29, 90.00
Int Tables number5
Space group name H-MC121
Components on special symmetry positions
IDModelComponents
11B-1619-

HOH

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein Botulinum neurotoxin type A / BoNT/A / Bontoxilysin-A / BOTOX


Mass: 49877.488 Da / Num. of mol.: 2 / Fragment: UNP residues 872-1296 / Mutation: T1158A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Clostridium botulinum (bacteria) / Gene: botA, atx, bna / Production host: Escherichia coli (E. coli)
References: UniProt: P10845, UniProt: P0DPI1*PLUS, bontoxilysin
#2: Protein Synaptic vesicle glycoprotein 2C


Mass: 13590.926 Da / Num. of mol.: 2 / Fragment: UNP residues 473-567
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SV2C, KIAA1054 / Production host: Mammalian expression vector pCBio (others) / References: UniProt: Q496J9

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Sugars , 3 types, 3 molecules

#3: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 732.682 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,4,3/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1221m-1a_1-5]/1-1-2-3/a4-b1_a6-d1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#4: 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.: 1
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
#7: 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.: 1
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

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Non-polymers , 3 types, 665 molecules

#5: Chemical ChemComp-ACT / ACETATE ION


Mass: 59.044 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H3O2
#6: Chemical ChemComp-PO4 / PHOSPHATE ION


Mass: 94.971 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: PO4
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 659 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 3.06 Å3/Da / Density % sol: 59.83 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop
Details: 0.1 M sodium acetate pH 4.6, 20% PEG 3350, 0.2 M ammonium phosphate monobasic, 4% polypropylene glycol P 400

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 2, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2→123.809 Å / Num. obs: 99668 / % possible obs: 99.6 % / Redundancy: 2.9 % / Net I/σ(I): 6.7

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3FUO

3fuo


Resolution: 2→123.809 Å / SU ML: 0.21 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.54
RfactorNum. reflection% reflection
Rfree0.2158 4975 4.99 %
Rwork0.1755 --
obs0.1776 99659 99.53 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2→123.809 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8677 0 27 659 9363
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0098965
X-RAY DIFFRACTIONf_angle_d1.00312123
X-RAY DIFFRACTIONf_dihedral_angle_d13.7753336
X-RAY DIFFRACTIONf_chiral_restr0.0761306
X-RAY DIFFRACTIONf_plane_restr0.0051553
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2-2.02270.28481550.25373146X-RAY DIFFRACTION100
2.0227-2.04650.27211440.23853198X-RAY DIFFRACTION100
2.0465-2.07150.28831720.2373137X-RAY DIFFRACTION100
2.0715-2.09770.28921630.22633170X-RAY DIFFRACTION100
2.0977-2.12530.24561580.21753159X-RAY DIFFRACTION100
2.1253-2.15440.26481440.21813175X-RAY DIFFRACTION100
2.1544-2.18520.25481710.21923153X-RAY DIFFRACTION100
2.1852-2.21780.28191610.21343159X-RAY DIFFRACTION100
2.2178-2.25250.24171540.21313172X-RAY DIFFRACTION100
2.2525-2.28940.25771660.20763179X-RAY DIFFRACTION100
2.2894-2.32890.26251840.2143098X-RAY DIFFRACTION100
2.3289-2.37130.26211670.20673218X-RAY DIFFRACTION100
2.3713-2.41690.27191610.19473148X-RAY DIFFRACTION100
2.4169-2.46620.23791590.19643150X-RAY DIFFRACTION100
2.4662-2.51980.20411710.2013180X-RAY DIFFRACTION100
2.5198-2.57850.24931710.19553158X-RAY DIFFRACTION100
2.5785-2.64290.2771620.20593123X-RAY DIFFRACTION100
2.6429-2.71440.23471460.1953204X-RAY DIFFRACTION100
2.7144-2.79430.23971880.19393180X-RAY DIFFRACTION100
2.7943-2.88450.24091520.18393164X-RAY DIFFRACTION100
2.8845-2.98760.22981820.183146X-RAY DIFFRACTION100
2.9876-3.10720.20431710.16943164X-RAY DIFFRACTION100
3.1072-3.24860.20441690.17793155X-RAY DIFFRACTION100
3.2486-3.41990.21521830.17143151X-RAY DIFFRACTION100
3.4199-3.63420.20891680.15513165X-RAY DIFFRACTION100
3.6342-3.91480.18461820.15193159X-RAY DIFFRACTION100
3.9148-4.30880.16731900.13863151X-RAY DIFFRACTION100
4.3088-4.93230.15741630.12433162X-RAY DIFFRACTION99
4.9323-6.21420.19611710.15713167X-RAY DIFFRACTION99
6.2142-124.04640.22151470.18372993X-RAY DIFFRACTION91
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)
13.4285-0.1202-0.32981.64710.54753.93140.0119-0.57330.10460.15160.1341-0.0527-0.45730.79450.02160.2033-0.25110.00470.2571-0.00650.175816.350130.9918273.0494
20.7069-0.03860.16453.9996-0.73821.00410.09940.0278-0.1193-0.0643-0.148-0.03570.11640.00660.00250.2269-0.0985-0.00210.20830.03160.2777-3.33113.2344267.0681
33.88270.40680.53962.25930.20313.3313-0.0495-0.28570.537-0.0251-0.0680.6185-0.2858-0.5320.04860.3261-0.00860.00340.7752-0.03850.4874-67.279726.4668293.2051
42.8684-0.3144-0.2882.10270.4092.60450.1182-0.3732-1.01320.1319-0.20740.32270.5285-0.7220.01060.2625-0.2835-0.03780.39790.0820.4692-56.890412.0454289.4646
52.40010.7837-0.20942.25830.12941.3457-0.03740.09880.1114-0.2341-0.16930.4152-0.0425-0.538-0.07680.2255-0.0612-0.02970.3234-0.00440.2403-56.9125.0419282.7152
61.98580.5322-0.00262.5957-0.63211.32840.0755-0.0583-0.03570.0465-0.2058-0.4552-0.09620.22960.0540.2498-0.0872-0.01610.26890.03930.3052-30.968132.2325286.3211
72.76371.08130.20543.0458-0.38592.1101-0.2426-0.39070.64220.4778-0.0736-0.0812-0.3553-0.0043-0.02180.3354-0.097-0.01180.2271-0.04360.292-37.892945.9968289.5466
83.21150.765-0.50344.7726-0.69662.0153-0.00820.17290.8995-0.0276-0.0767-0.3928-0.34840.36480.08240.3811-0.13560.00240.31810.10650.4846-30.292850.6188279.9791
92.09350.399-0.01224.3976-1.27772.64760.00010.36280.3367-0.2864-0.0637-0.12860.09250.21350.03210.2767-0.07360.00260.25560.05750.2735-35.711242.184274.2108
102.1574-0.2478-0.37934.03-2.5273.94220.14510.14030.0231-0.1591-0.02490.08110.0445-0.0656-0.05940.1819-0.0755-0.01210.21230.01640.2351-37.716632.2011280.7836
119.9033-6.9528-3.88424.89482.61552.20910.4184-0.0271.125-0.26590.1997-0.4797-0.52290.0439-0.18030.5426-0.01640.11830.5974-0.00520.4545-30.477132.4965261.0649
123.9905-1.16610.28722.1431.86822.1350.2128-0.2327-0.29320.18250.02980.17360.0563-0.2731-0.1260.3926-0.0456-0.02991.1183-0.02530.6412-32.793124.5705247.0042
132.4899-1.99661.55564.8215-3.90683.157-0.0452-0.11770.00620.46660.04430.4386-0.2234-0.7379-0.12920.37480.10360.08980.51930.05060.4157-26.879434.2739254.9281
143.80460.05851.37752.0418-0.06366.49230.30320.1464-0.12030.1193-0.23190.3240.0582-0.8529-0.03580.1760.06760.0390.35940.0360.2485-22.73428.1146250.3829
154.4846-0.27581.08192.8896-1.95196.73850.20240.3989-0.256-0.069-0.1406-0.13170.3691-0.1388-0.10180.15270.03050.01590.25540.02720.2173-14.183624.6461250.4665
163.97270.46393.86721.48070.71143.81380.0915-0.4663-0.33470.28590.0943-0.08760.478-0.4272-0.33530.66420.0773-0.10621.3865-0.06360.759-21.32115.4558314.5266
173.04041.25883.32953.1994-0.86285.9587-0.26470.0630.173-0.0315-0.1768-0.7338-0.60131.00920.39940.4265-0.2007-0.16980.7380.00380.6884-8.774921.7242305.0175
182.459-1.77762.9372.279-0.65825.574-0.0645-0.133-0.2066-0.03530.0907-0.2596-0.32490.31910.02110.3345-0.088-0.12450.57190.03740.5455-13.116317.6379304.7303
192.6255-1.80913.17012.7911-1.05085.25950.18-1.0915-1.56590.17520.311-0.14860.6143-0.0471-0.40610.3085-0.0489-0.16010.52830.14260.6289-17.411811.577305.5523
202.3337-1.99481.64581.9887-0.23435.8369-0.16690.93680.7916-0.34610.0787-0.552-0.67111.04780.1630.4479-0.1999-0.11810.62880.08180.5163-14.436620.9226296.9538
212.1881-1.09232.96091.8203-0.69434.44280.5201-0.1153-1.6199-0.00880.4484-0.23620.85020.2381-0.42330.3702-0.0089-0.21170.43570.03060.8215-17.06579.5235300.4949
222.0119-0.84640.55471.5549-1.2048.6329-0.15930.10990.3892-0.02360.0837-0.1726-0.74010.17420.09090.4113-0.1047-0.03620.40150.08380.3646-22.548620.9755296.5437
236.91282.89030.03013.39184.11037.68740.2081.269-1.2063-0.24830.3928-0.50720.06750.4744-0.44710.5506-0.3054-0.09711.11140.09430.4884-14.273116.9292290.832
249.9274-6.55012.45764.4253-0.72528.34420.63560.288-0.8022-0.45140.1708-0.34631.18960.8229-0.82150.516-0.0202-0.21060.5369-0.18530.7454-17.30356.9629294.855
254.571-5.22412.32126.6951-0.49667.54560.1201-0.0422-0.5201-0.323-0.01110.08670.12140.2421-0.35450.3256-0.0278-0.07790.3780.06190.4132-25.133917.0822294.2507
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 870 through 1102 )
2X-RAY DIFFRACTION2chain 'A' and (resid 1103 through 1296 )
3X-RAY DIFFRACTION3chain 'B' and (resid 870 through 906 )
4X-RAY DIFFRACTION4chain 'B' and (resid 907 through 1065 )
5X-RAY DIFFRACTION5chain 'B' and (resid 1066 through 1102 )
6X-RAY DIFFRACTION6chain 'B' and (resid 1103 through 1164 )
7X-RAY DIFFRACTION7chain 'B' and (resid 1165 through 1194 )
8X-RAY DIFFRACTION8chain 'B' and (resid 1195 through 1225 )
9X-RAY DIFFRACTION9chain 'B' and (resid 1226 through 1268 )
10X-RAY DIFFRACTION10chain 'B' and (resid 1269 through 1296 )
11X-RAY DIFFRACTION11chain 'C' and (resid 470 through 483 )
12X-RAY DIFFRACTION12chain 'C' and (resid 484 through 489 )
13X-RAY DIFFRACTION13chain 'C' and (resid 490 through 499 )
14X-RAY DIFFRACTION14chain 'C' and (resid 500 through 538 )
15X-RAY DIFFRACTION15chain 'C' and (resid 539 through 566 )
16X-RAY DIFFRACTION16chain 'D' and (resid 474 through 479 )
17X-RAY DIFFRACTION17chain 'D' and (resid 480 through 489 )
18X-RAY DIFFRACTION18chain 'D' and (resid 490 through 509 )
19X-RAY DIFFRACTION19chain 'D' and (resid 510 through 518 )
20X-RAY DIFFRACTION20chain 'D' and (resid 519 through 528 )
21X-RAY DIFFRACTION21chain 'D' and (resid 529 through 538 )
22X-RAY DIFFRACTION22chain 'D' and (resid 539 through 543 )
23X-RAY DIFFRACTION23chain 'D' and (resid 544 through 548 )
24X-RAY DIFFRACTION24chain 'D' and (resid 549 through 555 )
25X-RAY DIFFRACTION25chain 'D' and (resid 556 through 564 )

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