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- PDB-6ruv: Structure of the SCIN stabilized C3bBb convertase bound to Proper... -

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Basic information

Entry
Database: PDB / ID: 6ruv
TitleStructure of the SCIN stabilized C3bBb convertase bound to Properdin and a the non-inhibitory nanobody hFPNb1
Components
  • (Complement C3) x 2
  • (Properdin) x 2
  • Complement factor B
  • Inhibitor
  • Nanobody hFPNb1
KeywordsIMMUNE SYSTEM / innate immunity / complement / proteolytic enzyme / regulator / nanobody
Function / homology
Function and homology information


cytoplasmic side of Golgi membrane / alternative-complement-pathway C3/C5 convertase / positive regulation of opsonization / Defective B3GALTL causes PpS / O-glycosylation of TSR domain-containing proteins / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / complement binding ...cytoplasmic side of Golgi membrane / alternative-complement-pathway C3/C5 convertase / positive regulation of opsonization / Defective B3GALTL causes PpS / O-glycosylation of TSR domain-containing proteins / C5L2 anaphylatoxin chemotactic receptor binding / oviduct epithelium development / regulation of triglyceride biosynthetic process / positive regulation of activation of membrane attack complex / complement binding / vertebrate eye-specific patterning / positive regulation of apoptotic cell clearance / complement-mediated synapse pruning / Alternative complement activation / positive regulation of lipid storage / positive regulation of phagocytosis, engulfment / positive regulation of G protein-coupled receptor signaling pathway / Activation of C3 and C5 / complement receptor mediated signaling pathway / positive regulation of type IIa hypersensitivity / positive regulation of D-glucose transmembrane transport / complement-dependent cytotoxicity / complement activation / complement activation, alternative pathway / endopeptidase inhibitor activity / neuron remodeling / B cell activation / amyloid-beta clearance / positive regulation of vascular endothelial growth factor production / Purinergic signaling in leishmaniasis infection / complement activation, classical pathway / Peptide ligand-binding receptors / Regulation of Complement cascade / fatty acid metabolic process / Post-translational protein phosphorylation / response to bacterium / positive regulation of receptor-mediated endocytosis / specific granule lumen / positive regulation of angiogenesis / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / positive regulation of immune response / azurophil granule lumen / tertiary granule lumen / G alpha (i) signalling events / secretory granule lumen / blood microparticle / receptor ligand activity / defense response to bacterium / inflammatory response / immune response / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / endoplasmic reticulum lumen / serine-type endopeptidase activity / signaling receptor binding / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Staphylococcal complement inhibitor SCIN / Staphylococcal complement inhibitor SCIN / : / : / Thrombospondin type 1 repeat / CFP-like, C-terminal thrombospondin type 1 domain / : / Complement factor B / Complement B/C2 / Complement C3-like, NTR domain ...Staphylococcal complement inhibitor SCIN / Staphylococcal complement inhibitor SCIN / : / : / Thrombospondin type 1 repeat / CFP-like, C-terminal thrombospondin type 1 domain / : / Complement factor B / Complement B/C2 / Complement C3-like, NTR domain / : / : / Complement component 3, CUB domain, second segment / Complement component 3, CUB domain, first segment / Alpha-2-macroglobulin, conserved site / Alpha-2-macroglobulin family thiolester region signature. / Complement C3/4/5, macroglobulin domain MG1 / Macroglobulin domain MG1 / : / Alpha-macro-globulin thiol-ester bond-forming region / Anaphylatoxin, complement system domain / Anaphylatoxin domain signature. / Anaphylatoxin, complement system / Anaphylatoxin/fibulin / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG4 / Macroglobulin domain MG3 / : / A-macroglobulin receptor binding domain / Macroglobulin domain MG4 / Macroglobulin domain MG3 / A-macroglobulin receptor / Netrin domain / NTR domain profile. / Alpha-2-macroglobulin / Macroglobulin domain / Alpha-2-macroglobulin, bait region domain / Alpha-macroglobulin-like, TED domain / Alpha-2-macroglobulin family / MG2 domain / A-macroglobulin TED domain / Alpha-2-macroglobulin bait region domain / Alpha-2-Macroglobulin / Alpha-2-macroglobulin family / Tissue inhibitor of metalloproteinases-like, OB-fold / Thrombospondin type 1 domain / Thrombospondin type-1 (TSP1) repeat superfamily / Thrombospondin type-1 (TSP1) repeat profile. / Thrombospondin type 1 repeats / Thrombospondin type-1 (TSP1) repeat / Heat shock protein 70kD, C-terminal domain superfamily / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / von Willebrand factor type A domain / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan / Immunoglobulin-like fold
Similarity search - Domain/homology
alpha-D-mannopyranose / Staphylococcal complement inhibitor / Complement factor B / Complement C3 / Properdin / Staphylococcal complement inhibitor
Similarity search - Component
Biological speciesLama glama (llama)
Homo sapiens (human)
Staphylococcus aureus (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 6.15 Å
AuthorsPedersen, D.V. / Andersen, G.R.
Funding support Denmark, 1items
OrganizationGrant numberCountry
LundbeckfondenR155-2015-2666 Denmark
Citation
Journal: Front Immunol / Year: 2019
Title: Structural Basis for Properdin Oligomerization and Convertase Stimulation in the Human Complement System.
Authors: Pedersen, D.V. / Gadeberg, T.A.F. / Thomas, C. / Wang, Y. / Joram, N. / Jensen, R.K. / Mazarakis, S.M.M. / Revel, M. / El Sissy, C. / Petersen, S.V. / Lindorff-Larsen, K. / Thiel, S. / ...Authors: Pedersen, D.V. / Gadeberg, T.A.F. / Thomas, C. / Wang, Y. / Joram, N. / Jensen, R.K. / Mazarakis, S.M.M. / Revel, M. / El Sissy, C. / Petersen, S.V. / Lindorff-Larsen, K. / Thiel, S. / Laursen, N.S. / Fremeaux-Bacchi, V. / Andersen, G.R.
#1: Journal: Febs Lett. / Year: 2019
Title: Crystal structure of peptide-bound neprilysin reveals key binding interactions.
Authors: Moss, S. / Subramanian, V. / Acharya, K.R.
History
DepositionMay 29, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 21, 2019Provider: repository / Type: Initial release
Revision 1.1Sep 25, 2019Group: Data collection / Database references / Category: chem_comp / citation / citation_author / Item: _chem_comp.type
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_validate_chiral / 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 / _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.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.type / _database_PDB_caveat.text / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_comp_id / _pdbx_validate_chiral.auth_seq_id / _pdbx_validate_close_contact.auth_asym_id_2 / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 24, 2024Group: 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
Revision 2.2Nov 20, 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
R: Nanobody hFPNb1
S: Nanobody hFPNb1
U: Properdin
V: Properdin
X: Properdin
Y: Properdin
A: Complement C3
B: Complement C3
G: Complement C3
H: Complement C3
J: Complement factor B
L: Complement factor B
N: Inhibitor
Q: Inhibitor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)610,52652
Polymers600,52614
Non-polymers10,00038
Water00
1


  • Idetical with deposited unit
  • defined by software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area58820 Å2
ΔGint-109 kcal/mol
Surface area249760 Å2
MethodPISA
Unit cell
Length a, b, c (Å)123.990, 354.030, 367.840
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 6 types, 12 molecules UXVYAGBHJLNQ

#2: Protein Properdin / Complement factor P


Mass: 18636.939 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: TSR2 is not modelled and therefore missing residues
Source: (gene. exp.) Homo sapiens (human) / Gene: CFP, PFC / Production host: Homo sapiens (human) / Variant (production host): HEK293F / References: UniProt: P27918
#3: Protein Properdin / Complement factor P


Mass: 24724.129 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Properdin TSR4-TSR5-TSR6 and a few additional residues from vector
Source: (gene. exp.) Homo sapiens (human) / Gene: CFP, PFC / Production host: Homo sapiens (human) / References: UniProt: P27918
#4: Protein Complement C3 / C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1


Mass: 71393.320 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: beta-chain / Source: (natural) Homo sapiens (human) / References: UniProt: P01024
#5: Protein Complement C3 / C3 and PZP-like alpha-2-macroglobulin domain-containing protein 1


Mass: 104073.164 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: alpha-prime chain / Source: (natural) Homo sapiens (human) / References: UniProt: P01024
#6: Protein Complement factor B / C3/C5 convertase / Glycine-rich beta glycoprotein / GBG / PBF2 / Properdin factor B


Mass: 57042.082 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Details: Bb fragment / Source: (gene. exp.) Homo sapiens (human) / Gene: CFB, BF, BFD / Production host: Homo sapiens (human) / Variant (production host): HEK293F
References: UniProt: P00751, alternative-complement-pathway C3/C5 convertase
#7: Protein Inhibitor / Involved in expression of fibrinogen binding protein / phage associated / Staphylococcal complement inhibitor


Mass: 9876.188 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Staphylococcus aureus (bacteria)
Gene: scn_3, scn, scn_2, scn_4, BN1321_320035, CV021_13080, D1G05_09530, D1G09_13565, D1G21_11725, EP54_10460, EQ90_13920, ERS072840_02186, NCTC10654_02112, NCTC10702_03129, NCTC13196_02025, ...Gene: scn_3, scn, scn_2, scn_4, BN1321_320035, CV021_13080, D1G05_09530, D1G09_13565, D1G21_11725, EP54_10460, EQ90_13920, ERS072840_02186, NCTC10654_02112, NCTC10702_03129, NCTC13196_02025, NCTC13196_03045, NCTC6133_02657, NCTC7878_02651
Production host: Escherichia coli (E. coli) / References: UniProt: A0A0H2DUF0, UniProt: Q931M7*PLUS

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Antibody / Non-polymers , 2 types, 4 molecules RS

#12: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg
#1: Antibody Nanobody hFPNb1


Mass: 14517.155 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli)

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Sugars , 4 types, 36 molecules

#8: Polysaccharide
beta-D-glucopyranose-(1-3)-alpha-L-fucopyranose


Type: oligosaccharide / Mass: 326.297 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpb1-3LFucpa1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a1221m-1a_1-5][a2122h-1b_1-5]/1-2/a3-b1WURCSPDB2Glycan 1.1.0
[]{[(3+1)][a-L-Fucp]{[(3+1)][b-D-Glcp]{}}}LINUCSPDB-CARE
#9: 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.: 2
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)][b-L-Fucp]{}}}LINUCSPDB-CARE
#10: 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.: 8
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
#11: Sugar...
ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 21
Source method: isolated from a genetically manipulated source
Formula: C6H12O6
IdentifierTypeProgram
DManpaCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
a-D-mannopyranoseCOMMON NAMEGMML 1.0
a-D-ManpIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
ManSNFG CARBOHYDRATE SYMBOLGMML 1.0

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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: 6.72 Å3/Da / Density % sol: 81.7 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 5.8
Details: 100 mM NaCl, 5 % (w/v) PEG4000, 10 mM MgCl2, 100 mM Sodium Cacodylate trihydrate pH 5.8.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P13 (MX1) / Wavelength: 0.97625 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 14, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 6.15→50 Å / Num. obs: 38393 / % possible obs: 99.6 % / Redundancy: 13 % / Net I/σ(I): 12.2
Reflection shellResolution: 6.15→6.31 Å / Num. unique obs: 2738

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Processing

Software
NameVersionClassification
PHENIX(1.14_3260: ???)refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2WIN

2win


Resolution: 6.15→49.819 Å / SU ML: 1.19 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 35.76
RfactorNum. reflection% reflection
Rfree0.2707 1990 5.19 %
Rwork0.2422 --
obs0.2437 38338 99.62 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 6.15→49.819 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms41278 0 638 0 41916
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00542911
X-RAY DIFFRACTIONf_angle_d0.95158292
X-RAY DIFFRACTIONf_dihedral_angle_d16.54826312
X-RAY DIFFRACTIONf_chiral_restr0.0576549
X-RAY DIFFRACTIONf_plane_restr0.0087437
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
6.1501-6.30360.46371480.43722485X-RAY DIFFRACTION98
6.3036-6.47370.42281330.41092581X-RAY DIFFRACTION100
6.4737-6.66380.40381410.39172551X-RAY DIFFRACTION100
6.6638-6.87840.39591490.3682561X-RAY DIFFRACTION100
6.8784-7.12350.3411300.34252553X-RAY DIFFRACTION100
7.1235-7.40790.34081430.31892595X-RAY DIFFRACTION100
7.4079-7.74380.3431420.30062598X-RAY DIFFRACTION100
7.7438-8.15040.29091400.27662571X-RAY DIFFRACTION100
8.1504-8.65860.30911400.24662587X-RAY DIFFRACTION100
8.6586-9.32310.22571450.22762603X-RAY DIFFRACTION100
9.3231-10.2540.22831430.20042628X-RAY DIFFRACTION100
10.254-11.72080.22581390.19082623X-RAY DIFFRACTION99
11.7208-14.70380.23191450.20342648X-RAY DIFFRACTION99
14.7038-49.82030.26961520.23252764X-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)
11.17671.16560.12983.43390.65350.673-0.2402-0.14780.17930.37080.3754-0.2265-0.37230.3528-0.08164.4023-0.0071-0.08934.3225-0.00384.2883-4.2255-49.69489.947
24.151-2.44090.60623.066-0.27610.885-0.04960.0076-0.1259-0.91690.3136-0.0243-0.1801-0.1289-0.18484.4482-0.29860.01244.3328-0.03943.9286-14.7996-53.0208-34.8429
36.6091.02360.96629.5688-2.52316.3367-1.087-2.18520.07333.36330.7585-0.9123-4.77561.44250.31684.63370.0554-0.49414.1732-0.17393.1272-9.0606-47.531148.9092
45.3996-2.171-0.36715.96220.87852.01580.74531.5867-0.4102-1.4692-0.7674-1.1403-1.4868-1.90550.15097.0602-0.45010.30795.24310.12054.6213-14.1921-46.5243-73.6161
57.00190.16241.76848.02334.17392.7509-0.0469-0.1885-0.98682.55150.2580.56090.1625-0.6092-0.13834.88140.77910.29615.17690.37845.00833.7483-99.568351.2353
63.7356-5.2342-4.82350.03650.23215.7570.55610.38330.569-1.78880.33160.0621-0.42671.1232-0.65195.5344-0.19830.58233.8992-0.17984.393314.5242-91.6122-78.5732
74.42642.40852.23185.44232.90223.2532-0.3488-0.62460.79030.27350.0950.7127-0.524-0.62820.35323.76330.67110.46224.4260.23794.2098-55.4654-26.237216.9681
82.4499-1.59230.44592.7145-1.23482.6509-0.15050.35630.2753-0.49640.0985-1.1081-0.910.72010.01124.7737-0.41020.55044.36110.36145.34772.57211.2725-39.9546
91.84571.74380.77815.93914.43597.94890.67550.57081.0167-3.53530.20560.5682-2.5584-1.2084-0.5264.6769-0.0326-0.40194.86810.94255.7012-10.3685-7.9041-18.3933
105.7116-3.88431.64335.9615-3.13368.2370.1546-2.87151.60162.66890.6769-4.4059-1.2647-0.5107-0.30094.65310.1071-0.35193.9391-0.63325.0484-40.3683-21.6399-4.6265
111.78180.2768-0.09491.4786-0.29451.1133-2.0234-0.9518-5.61861.49331.7469-1.67321.24761.82010.68857.96240.88570.73227.9576-1.90589.7127-47.995450.371562.7407
121.0197-0.2059-0.83850.4193-0.46991.2237-2.83352.4173-0.4527-0.94262.10983.23295.2114-4.99190.175911.68520.0478-4.23468.1976-2.0315.4115-70.033844.764453.6126
130.79180.1654-0.5597-0.1970.36610.40390.89840.58190.73390.39180.87142.40531.6315-1.0255-0.89027.89321.3479-0.58488.3206-4.654312.058-33.035652.76181.265
145.7062-1.3391-2.70783.18551.36475.6284-3.41232.31731.08450.82154.03922.4469-2.58031.9026-1.66015.1691-0.22060.06795.06730.08826.3907-54.758520.356539.1745
151.11211.55530.95361.4257-0.37421.2256-0.4754-0.26440.4858-1.6217-1.63583.37550.1299-1.05891.84726.23040.71580.17057.5584-1.21068.4644-76.666229.568140.1967
161.53160.7977-2.29990.4238-1.20373.4522-0.5775-1.348-0.4149-0.0797-0.31620.06360.8174-1.18060.73478.7019-2.5149-4.02897.1276-0.256511.8243-67.27912.511652.7457
171.1985-1.0321-0.8333.34020.6482.23150.4269-0.44341.526-5.00391.1541-2.1137-0.6249-3.058-0.53397.9199-0.12741.05625.992.00995.8652-60.868448.7983-81.4962
181.7645-1.0541.32614.20980.24271.23033.9069-2.95380.43821.165-4.14250.53760.84211.22581.19076.9827-1.42420.69746.52850.79754.4406-42.718261.8554-71.1013
196.2968-0.31380.25550.6453-0.51071.5573-1.69821.94011.01181.0248-2.1659-3.2952-4.84960.42162.2696.89670.15181.02824.79950.86595.895-23.3673105.933-92.1196
206.40294.6509-0.10189.94891.3122.47680.7744-0.5417-1.26450.0662-0.8361-1.132-4.08441.45650.84587.2690.09770.76364.40810.43025.749-73.221142.0993-99.539
216.0094-0.63253.95774.6455-0.63181.68552.7711-3.58081.930.3143-1.7330.00711.9798-2.5145-1.87354.2221-1.06620.10694.9450.21233.8094-33.389532.997-59.264
221.08421.567-1.46893.6127-1.70225.2552-1.02440.60321.1384-0.58421.40420.2704-3.26321.132-0.74126.9081-0.31270.51334.88180.17495.1315-26.892155.8095-57.9164
234.63636.3281.35168.60181.81746.2358-0.16161.14160.3683-0.4776-0.3240.3262-0.12850.91450.13374.9419-3.6003-0.89085.38-3.541710.3265-19.819839.4931-71.0767
245.620.5924-0.03633.70451.92560.5055-1.038-3.1017-0.37361.7030.4181.5491-2.7559-2.35120.05348.37990.80390.62698.42170.09156.8748-54.913932.675-107.6228
253.0399-0.45690.21020.6903-0.79070.2534-3.0039-1.99860.3386-3.06771.6047-0.2403-0.77620.51680.381610.80392.2605-2.268613.5674-6.846811.3842-37.109331.837887.7084
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1((chain A) or (chain B and resseq 729:910) or (chain B and resseq 1335:1479))
2X-RAY DIFFRACTION2((chain G) or (chain H and resseq 729:910) or (chain H and resseq 1335:1479))
3X-RAY DIFFRACTION3(chain B and resseq 911:966) or (chain B and resseq 1268:1334 ) or (chain B and resseq 2001:2003))
4X-RAY DIFFRACTION4(chain H and resseq 911:966) or (chain H and resseq 1268:1334 ) or (chain H and resseq 2001:2003))
5X-RAY DIFFRACTION5(chain B and resseq 967:1267)
6X-RAY DIFFRACTION6(chain H and resseq 967:1267)
7X-RAY DIFFRACTION7(chain B and resseq 1480:1641 ) or (chain L) )
8X-RAY DIFFRACTION8(chain H and resseq 1480:1641 ) or (chain J) )
9X-RAY DIFFRACTION9chain Q
10X-RAY DIFFRACTION10chain N
11X-RAY DIFFRACTION11chain U and resid 28:75
12X-RAY DIFFRACTION12chain U and ((resid 76:133) or (resid 1025) or (resid 1026) or (resid 1027:1028))
13X-RAY DIFFRACTION13chain V and ((resid 255:312) or (resid 1097) or (resid 1096) or (resid 1036:1037))
14X-RAY DIFFRACTION14chain V and ((resid 313:378) or (resid 1038) or (resid 1039) )
15X-RAY DIFFRACTION15chain V and ((resid 379:480) or (resid 1040) or (resid 1046) or (resid 1048))
16X-RAY DIFFRACTION16chain V and resid 1042:1044
17X-RAY DIFFRACTION17chain X and resid 28:75
18X-RAY DIFFRACTION18chain X and ((resid 76:133) or (resid 1025) or (resid 1026) or (resid 1027:1028))
19X-RAY DIFFRACTION19chain X and ((resid 134:191) or (resid 1029) or (resid 1030) or (resid 1031) or (resid 1023:1024))
20X-RAY DIFFRACTION20chain Y and ((resid 255:312) or (resid 1097) or (resid 1096) or (resid 1036:1037))
21X-RAY DIFFRACTION21chain Y and ((resid 313:378) or (resid 1038) or (resid 1039) )
22X-RAY DIFFRACTION22chain Y and ((resid 379:480) or (resid 1040) or (resid 1046) or (resid 1048))
23X-RAY DIFFRACTION23chain Y and resid 1042:1044
24X-RAY DIFFRACTION24chain R
25X-RAY DIFFRACTION25chain S

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