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- PDB-5esv: Crystal Structure of Broadly Neutralizing Antibody CH03, Isolated... -

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Basic information

Entry
Database: PDB / ID: 5esv
TitleCrystal Structure of Broadly Neutralizing Antibody CH03, Isolated from Donor CH0219, in Complex with Scaffolded Trimeric HIV-1 Env V1V2 Domain from the Clade C Superinfecting Strain of Donor CAP256.
Components
  • 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase,Envelope glycoprotein gp160
  • CH03 Heavy Chain
  • CH03 Light Chain
KeywordsIMMUNE SYSTEM / HIV-1 / Env / V1V2 / CH0219 / CHAVI / scaffold / CAP256
Function / homology
Function and homology information


2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase / 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity / virus-mediated perturbation of host defense response => GO:0019049 / : / IgD immunoglobulin complex / IgM immunoglobulin complex / IgA immunoglobulin complex / IgE immunoglobulin complex / isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway / CD22 mediated BCR regulation ...2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase / 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity / virus-mediated perturbation of host defense response => GO:0019049 / : / IgD immunoglobulin complex / IgM immunoglobulin complex / IgA immunoglobulin complex / IgE immunoglobulin complex / isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway / CD22 mediated BCR regulation / terpenoid biosynthetic process / IgG immunoglobulin complex / Fc epsilon receptor (FCERI) signaling / Classical antibody-mediated complement activation / Initial triggering of complement / FCGR activation / immunoglobulin mediated immune response / Role of phospholipids in phagocytosis / Role of LAT2/NTAL/LAB on calcium mobilization / Scavenging of heme from plasma / positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / FCERI mediated Ca+2 mobilization / FCGR3A-mediated IL10 synthesis / host cell endosome membrane / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / Regulation of Complement cascade / Cell surface interactions at the vascular wall / FCERI mediated MAPK activation / FCGR3A-mediated phagocytosis / antigen binding / B cell receptor signaling pathway / Regulation of actin dynamics for phagocytic cup formation / FCERI mediated NF-kB activation / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / clathrin-dependent endocytosis of virus by host cell / adaptive immune response / Potential therapeutics for SARS / membrane => GO:0016020 / viral protein processing / blood microparticle / immune response / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / structural molecule activity / virion membrane / extracellular space / extracellular exosome / extracellular region / membrane / metal ion binding / plasma membrane
Similarity search - Function
2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase / 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, conserved site / 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase superfamily / YgbB family / 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature. / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 ...2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase / 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase, conserved site / 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase superfamily / YgbB family / 2C-methyl-D-erythritol 2,4-cyclodiphosphate synthase signature. / Envelope glycoprotein Gp160 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Gp120 core superfamily / Envelope glycoprotein GP120 / Human immunodeficiency virus 1, envelope glycoprotein Gp120 / Immunoglobulin V-Type / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Immunoglobulin kappa constant / 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase / IgG H chain / Envelope glycoprotein gp160
Similarity search - Component
Biological speciesHomo sapiens (human)
Haemophilus influenzae (bacteria)
Human immunodeficiency virus 1
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.105 Å
AuthorsGorman, J. / Yang, M. / Kwong, P.D.
CitationJournal: Nat.Struct.Mol.Biol. / Year: 2016
Title: Structures of HIV-1 Env V1V2 with broadly neutralizing antibodies reveal commonalities that enable vaccine design.
Authors: Gorman, J. / Soto, C. / Yang, M.M. / Davenport, T.M. / Guttman, M. / Bailer, R.T. / Chambers, M. / Chuang, G.Y. / DeKosky, B.J. / Doria-Rose, N.A. / Druz, A. / Ernandes, M.J. / Georgiev, I.S. ...Authors: Gorman, J. / Soto, C. / Yang, M.M. / Davenport, T.M. / Guttman, M. / Bailer, R.T. / Chambers, M. / Chuang, G.Y. / DeKosky, B.J. / Doria-Rose, N.A. / Druz, A. / Ernandes, M.J. / Georgiev, I.S. / Jarosinski, M.C. / Joyce, M.G. / Lemmin, T.M. / Leung, S. / Louder, M.K. / McDaniel, J.R. / Narpala, S. / Pancera, M. / Stuckey, J. / Wu, X. / Yang, Y. / Zhang, B. / Zhou, T. / Program, N.C. / Mullikin, J.C. / Baxa, U. / Georgiou, G. / McDermott, A.B. / Bonsignori, M. / Haynes, B.F. / Moore, P.L. / Morris, L. / Lee, K.K. / Shapiro, L. / Mascola, J.R. / Kwong, P.D.
History
DepositionNov 17, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 16, 2015Provider: repository / Type: Initial release
Revision 1.1Jan 6, 2016Group: Database references
Revision 1.2Jan 13, 2016Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / database_PDB_caveat / 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_conn_angle / pdbx_struct_oper_list / pdbx_validate_chiral / pdbx_validate_close_contact / struct_asym / struct_conn / struct_conn_type / 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.pdbx_formal_charge / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _database_PDB_caveat.text / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_oper_list.symmetry_operation / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_id / _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.conn_type_id / _struct_conn.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.ptnr1_label_seq_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 / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 27, 2023Group: Data collection / Database references ...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 / 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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: CH03 Heavy Chain
B: CH03 Light Chain
C: CH03 Heavy Chain
D: CH03 Light Chain
E: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase,Envelope glycoprotein gp160
F: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase,Envelope glycoprotein gp160
G: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase,Envelope glycoprotein gp160
H: CH03 Heavy Chain
L: CH03 Light Chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)230,23624
Polymers218,9889
Non-polymers11,24715
Water724
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area43310 Å2
ΔGint70 kcal/mol
Surface area82670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)162.693, 98.211, 170.629
Angle α, β, γ (deg.)90.00, 112.82, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 1 types, 3 molecules EFG

#3: Protein 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase,Envelope glycoprotein gp160 / MECPS / Endogenous retrovirus group K member 113 Env polyprotein / Endogenous retrovirus group K ...MECPS / Endogenous retrovirus group K member 113 Env polyprotein / Endogenous retrovirus group K member 13-1 Env polyprotein / Endogenous retrovirus group K member 18 Env polyprotein / Endogenous retrovirus group K member 19 Env polyprotein / Endogenous retrovirus group K member 21 Env polyprotein / Endogenous retrovirus group K member 24 Env polyprotein / Endogenous retrovirus group K member 25 Env polyprotein / Endogenous retrovirus group K member 6 Env polyprotein / Endogenous retrovirus group K member 7 Env polyprotein / Endogenous retrovirus group K member 8 Env polyprotein / Endogenous retrovirus group K member 9 Env polyprotein / Envelope glycoprotein gp160 / MECPS


Mass: 23142.422 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Haemophilus influenzae (bacteria), (gene. exp.) Human immunodeficiency virus 1, (gene. exp.) Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) (bacteria)
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd / Gene: ispF, HI_0671, env / Cell line (production host): Expi293 / Production host: Homo sapiens (human)
References: UniProt: P44815, UniProt: W6ICC0, 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase

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Antibody , 2 types, 6 molecules ACHBDL

#1: Antibody CH03 Heavy Chain


Mass: 26301.475 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): Expi293 / Production host: Homo sapiens (human) / References: UniProt: S6BGE0
#2: Antibody CH03 Light Chain


Mass: 23552.207 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IGKC / Cell line (production host): Expi293 / Production host: Homo sapiens (human) / References: UniProt: P01834

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Sugars , 6 types, 12 molecules

#4: 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.: 1
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
#5: 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
#6: Polysaccharide
alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[alpha-D- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[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: 1235.105 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1_e6-g1WURCSPDB2Glycan 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]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#7: 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.: 2
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
#8: Polysaccharide alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D- ...alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[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: 1072.964 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpa1-6[DManpa1-3]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3/a4-b1_b4-c1_c3-d1_c6-e1_e3-f1WURCSPDB2Glycan 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]{[(3+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#10: 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 , 2 types, 7 molecules

#9: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Zn
#11: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.74 Å3/Da / Density % sol: 55.1 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5
Details: 10% PEG8000, .1M CaCl, 20% MPD, .1M Na Acetate pH 5.5, frozen in 15% sucrose as cryoprotectant

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å
DetectorType: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 6, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.1→50 Å / Num. obs: 44647 / % possible obs: 99.7 % / Redundancy: 3.4 % / Net I/σ(I): 7.3

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Processing

Software
NameVersionClassification
PHENIX(dev_2247: ???)refinement
HKL-2000data reduction
HKL-2000data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3TCL, 4TVP and 1VH8

3tcl

4tvp

1vh8


Resolution: 3.105→41.987 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 28.29 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2591 2004 4.49 %
Rwork0.2085 --
obs0.2109 44635 99.15 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.105→41.987 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14297 0 743 4 15044
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00515394
X-RAY DIFFRACTIONf_angle_d0.86920973
X-RAY DIFFRACTIONf_dihedral_angle_d12.7069204
X-RAY DIFFRACTIONf_chiral_restr0.0732525
X-RAY DIFFRACTIONf_plane_restr0.0032586
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.1046-3.18220.35351250.30312796X-RAY DIFFRACTION91
3.1822-3.26830.30081470.27523030X-RAY DIFFRACTION99
3.2683-3.36440.30621300.25063032X-RAY DIFFRACTION100
3.3644-3.47290.30571510.243013X-RAY DIFFRACTION100
3.4729-3.5970.2851360.23643055X-RAY DIFFRACTION100
3.597-3.74090.30191470.22823064X-RAY DIFFRACTION100
3.7409-3.91110.26641400.21283054X-RAY DIFFRACTION100
3.9111-4.11710.27071520.20333056X-RAY DIFFRACTION100
4.1171-4.37480.26991470.18083043X-RAY DIFFRACTION100
4.3748-4.71220.2011460.16713075X-RAY DIFFRACTION100
4.7122-5.18560.18531420.16533083X-RAY DIFFRACTION100
5.1856-5.93410.25521420.19533093X-RAY DIFFRACTION100
5.9341-7.46950.25621490.233084X-RAY DIFFRACTION100
7.4695-41.99130.25551500.20253153X-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)
12.05640.51250.35421.0509-0.09720.89980.01730.0647-0.242-0.01790.0578-0.09120.11290.103200.2050.01830.01560.187-0.04960.2875-33.469940.699261.8186
20.81980.32220.34220.0181-0.86530.99830.08390.2028-0.0742-0.0879-0.0984-0.02270.0893-0.0382-00.41160.0699-0.01870.4772-0.03050.4501-65.107837.922943.8477
30.83740.0430.58211.5561-0.30770.4058-0.04590.03270.1601-0.07650.025-0.0638-0.22070.11500.3883-0.01340.05590.29650.01050.3581-39.384660.706355.4823
40.59530.19760.53171.6093-0.68180.3657-0.104-0.1682-0.3045-0.0621-0.02580.0745-0.3002-0.33630.00010.35340.11660.02250.5963-0.00940.4767-72.961650.028651.4231
51.588-1.19140.08581.10740.49120.4587-0.2736-0.22680.36160.1362-0.064-0.1504-0.32240.0238-00.9663-0.1051-0.17310.62280.05790.6282-16.350560.940830.361
61.6426-0.70340.34570.9075-0.51780.1848-0.154-0.4748-0.04090.5580.35710.251-0.3263-0.49340.00040.78070.07840.06560.85150.18610.386-50.121856.520221.2067
71.1457-0.3011.41962.10941.21341.49230.1830.374-0.15310.1906-0.04280.0095-0.06350.000200.6642-0.10230.03370.65790.12480.5244-17.00545.086515.2355
81.21920.07470.24411.1890.03931.0783-0.0012-0.1749-0.2192-0.03180.19520.1746-0.0518-0.239-00.6858-0.0140.04190.84250.1830.5148-49.784356.12765.0062
91.3854-0.95460.09561.0701-0.67460.4178-0.1947-0.04260.11980.080.10660.31290.22230.042100.31110.06260.05650.511-0.09020.4673-1.440536.374569.4529
100.84140.31790.09831.13290.75940.91280.1057-0.47590.12280.0329-0.2361-0.0994-0.0522-0.2099-00.42020.02170.05540.5101-0.01430.427621.151443.620978.9345
11-0.4678-0.00460.4371-0.02540.09620.1164-0.1039-0.0433-0.3743-0.18060.16520.0493-0.40220.296500.5324-0.0575-0.02040.47140.04160.46968.926658.423351.0843
12-0.64940.0885-0.15390.4794-0.18160.0332-0.09070.05790.1686-0.0775-0.0003-0.15950.0681-0.0459-00.3761-0.01680.01220.3077-0.02390.373420.414154.837557.1162
130.55211.40020.18280.30730.65760.5783-0.3198-0.09280.0492-0.06590.1477-0.2532-0.2898-0.2904-0.00010.41210.0431-0.05590.45360.03940.632212.240229.999343.4689
140.7597-0.46320.27011.5857-0.60851.3901-0.0083-0.0053-0.1790.1709-0.0191-0.12250.2585-0.019400.2833-0.03270.0040.28680.00890.456527.878129.769762.7622
151.84240.23320.04430.4854-0.49271.8039-0.1240.17050.1116-0.11190.0698-0.07130.09120.319100.33860.02630.0120.3413-0.03730.335-17.77120.932631.9545
160.6771-0.7339-0.1652-0.30650.30030.97420.13590.46390.3038-0.13780.0044-0.1342-0.0262-0.360500.4955-0.0611-0.00180.65730.05970.4713-51.772225.515619.199
171.76860.1954-0.43670.5381-0.44711.6254-0.0101-0.183-0.04530.0480.04670.00920.1356-0.029800.36130.0307-0.03650.1952-0.05160.3406-31.828615.327547.7743
181.5765-0.3337-0.85620.17680.08922.06230.0330.2062-0.12890.04750.0251-0.12940.5463-0.665300.4321-0.2339-0.04590.54430.00080.3367-58.065311.132224.0111
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 110 )
2X-RAY DIFFRACTION2chain 'A' and (resid 111 through 213 )
3X-RAY DIFFRACTION3chain 'B' and (resid 1 through 110 )
4X-RAY DIFFRACTION4chain 'B' and (resid 111 through 212 )
5X-RAY DIFFRACTION5chain 'C' and (resid 1 through 110 )
6X-RAY DIFFRACTION6chain 'C' and (resid 111 through 213 )
7X-RAY DIFFRACTION7chain 'D' and (resid 1 through 110 )
8X-RAY DIFFRACTION8chain 'D' and (resid 111 through 213 )
9X-RAY DIFFRACTION9chain 'E' and (resid 111 through 202 )
10X-RAY DIFFRACTION10chain 'E' and (resid 203 through 326 )
11X-RAY DIFFRACTION11chain 'F' and (resid 112 through 202 )
12X-RAY DIFFRACTION12chain 'F' and (resid 203 through 326 )
13X-RAY DIFFRACTION13chain 'G' and (resid 111 through 200 )
14X-RAY DIFFRACTION14chain 'G' and (resid 201 through 326 )
15X-RAY DIFFRACTION15chain 'H' and (resid 1 through 110 )
16X-RAY DIFFRACTION16chain 'H' and (resid 111 through 213 )
17X-RAY DIFFRACTION17chain 'L' and (resid 1 through 110 )
18X-RAY DIFFRACTION18chain 'L' and (resid 111 through 213 )

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