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- PDB-7noz: Structure of the nanobody stablized properdin bound alternative p... -

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Basic information

Entry
Database: PDB / ID: 7noz
TitleStructure of the nanobody stablized properdin bound alternative pathway proconvertase C3b:FB:FP
Components
  • (Complement C3 ...) x 2
  • (Properdin) x 2
  • Complement factor B
  • hFPNb1 nanobody
KeywordsIMMUNE SYSTEM / protease / complement / cascade / proconvertase
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 / Activation of C3 and C5 / positive regulation of phagocytosis, engulfment / positive regulation of lipid storage / positive regulation of G protein-coupled receptor signaling pathway / complement receptor mediated signaling pathway / positive regulation of type IIa hypersensitivity / complement-dependent cytotoxicity / positive regulation of D-glucose transmembrane transport / complement activation / complement activation, alternative pathway / endopeptidase inhibitor activity / neuron remodeling / amyloid-beta clearance / B cell activation / positive regulation of vascular endothelial growth factor production / complement activation, classical pathway / Purinergic signaling in leishmaniasis infection / Peptide ligand-binding receptors / Regulation of Complement cascade / fatty acid metabolic process / Post-translational protein phosphorylation / response to bacterium / positive regulation of immune response / positive regulation of receptor-mediated endocytosis / specific granule lumen / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of angiogenesis / Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell / azurophil granule lumen / tertiary granule lumen / positive regulation of protein phosphorylation / G alpha (i) signalling events / secretory granule lumen / blood microparticle / defense response to bacterium / immune response / G protein-coupled receptor signaling pathway / inflammatory response / receptor ligand activity / endoplasmic reticulum lumen / signaling receptor binding / serine-type endopeptidase activity / Neutrophil degranulation / cell surface / signal transduction / protein-containing complex / proteolysis / extracellular space / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
TSP-1 type 1 repeat / Thrombospondin type-1 (TSP1) repeat / : / : / Thrombospondin type 1 repeat / CFP-like, C-terminal thrombospondin type 1 domain / : / Complement factor B / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Complement B/C2 ...TSP-1 type 1 repeat / Thrombospondin type-1 (TSP1) repeat / : / : / Thrombospondin type 1 repeat / CFP-like, C-terminal thrombospondin type 1 domain / : / Complement factor B / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Complement B/C2 / S-adenosyl-L-methionine-dependent methyltransferases / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / 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 / Anaphylatoxin, complement system domain / : / Anaphylatoxin domain signature. / Alpha-macro-globulin thiol-ester bond-forming region / 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 / Macroglobulin domain MG4 / Macroglobulin domain MG4 / Glycosyltransferase - #20 / Netrin domain / NTR domain profile. / Alpha-macroglobulin, receptor-binding / Alpha-macroglobulin, receptor-binding domain superfamily / Macroglobulin domain MG3 / : / A-macroglobulin receptor binding domain / Macroglobulin domain MG3 / A-macroglobulin receptor / Tissue inhibitor of metalloproteinases-like, OB-fold / 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 / 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 / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / von Willebrand factor type A domain / Sushi/SCR/CCP domain / Sushi/CCP/SCR domain profile. / Sushi/SCR/CCP superfamily / Terpenoid cyclases/protein prenyltransferase alpha-alpha toroid / Glycosyltransferase / Alpha/alpha barrel / von Willebrand factor (vWF) type A domain / VWFA domain profile. / von Willebrand factor, type A / Single Sheet / von Willebrand factor A-like domain superfamily / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin family, serine active site. / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Immunoglobulin-like fold / Peptidase S1, PA clan / Immunoglobulins / Beta Barrel / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
alpha-D-mannopyranose / Complement factor B / Complement C3 / Properdin
Similarity search - Component
Biological speciesHomo sapiens (human)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.9 Å
AuthorsLorenzen, J. / Pedersen, D.V. / Andersen, G.R.
Funding support Denmark, 1items
OrganizationGrant numberCountry
LundbeckfondenR155-2015-2666 Denmark
CitationJournal: Protein Sci. / Year: 2022
Title: Structure determination of an unstable macromolecular complex enabled by nanobody-peptide bridging.
Authors: Lorentzen, J. / Pedersen, D.V. / Gadeberg, T.A.F. / Andersen, G.R.
History
DepositionFeb 26, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 27, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 26, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 1.3Nov 20, 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: Complement C3 beta chain
B: Complement C3 alpha chain
C: Properdin
D: Properdin
F: Complement factor B
R: hFPNb1 nanobody
hetero molecules


Theoretical massNumber of molelcules
Total (without water)317,06022
Polymers311,4986
Non-polymers5,56216
Water362
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)148.690, 179.460, 192.600
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Space group name HallP22ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x+1/2,y+1/2,-z
#4: -x,-y,z

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Components

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Complement C3 ... , 2 types, 2 molecules AB

#1: Protein Complement C3 beta chain


Mass: 71393.320 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P01024
#2: Protein Complement C3 alpha chain


Mass: 103759.797 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Homo sapiens (human) / References: UniProt: P01024

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Protein , 3 types, 3 molecules CDF

#3: Protein Properdin / Complement factor P


Mass: 17744.971 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CFP, PFC / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P27918
#4: Protein Properdin / Complement factor P


Mass: 22958.279 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CFP, PFC / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P27918
#5: Protein Complement factor B / C3/C5 convertase / Glycine-rich beta glycoprotein / GBG / PBF2 / Properdin factor B


Mass: 82084.609 Da / Num. of mol.: 1 / Mutation: D279G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: CFB, BF, BFD / Cell line (production host): HEK293 / Production host: Homo sapiens (human)
References: UniProt: P00751, alternative-complement-pathway C3/C5 convertase

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Antibody , 1 types, 1 molecules R

#6: Antibody hFPNb1 nanobody


Mass: 13557.077 Da / Num. of mol.: 1
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 , 5 types, 15 molecules

#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.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam 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
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}LINUCSPDB-CARE
#8: Polysaccharide beta-D-glucopyranose-(1-3)-alpha-L-fucopyranose


Type: oligosaccharide / Mass: 326.297 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpb1-3LFucpa1-ROHGlycam 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
[][L-1-deoxy-Fucp]{[(3+1)][b-D-Glcp]{}}LINUCSPDB-CARE
#9: 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.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam 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
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#10: Sugar
ChemComp-MAN / alpha-D-mannopyranose / alpha-D-mannose / D-mannose / mannose


Type: D-saccharide, alpha linking / Mass: 180.156 Da / Num. of mol.: 6
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
#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.: 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, 3 molecules

#12: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#13: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN
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: 4.16 Å3/Da / Density % sol: 70.47 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 0.05 M Na-acetate pH 5.3, 0.1 M Mg-formate,7% PEG5000 MME

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: MAX IV / Beamline: BioMAX / Wavelength: 1.033 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: May 23, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.033 Å / Relative weight: 1
ReflectionResolution: 3.9→48.59 Å / Num. obs: 47647 / % possible obs: 99.8 % / Redundancy: 39.7 % / Biso Wilson estimate: 196.03 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.1949 / Net I/σ(I): 10.84
Reflection shellResolution: 3.9→4.039 Å / Redundancy: 43.8 % / Mean I/σ(I) obs: 0.84 / Num. unique obs: 4688 / CC1/2: 0.392 / % possible all: 99.91

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Processing

Software
NameVersionClassification
PHENIX1.19.2_4158refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2XWB

2xwb


Resolution: 3.9→48.59 Å / SU ML: 0.6713 / Cross valid method: FREE R-VALUE / σ(F): 1.45 / Phase error: 34.0027
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2654 1849 3.88 %
Rwork0.2488 45746 -
obs0.2494 47595 99.88 %
Solvent computationShrinkage radii: 0.8 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 288.94 Å2
Refinement stepCycle: LAST / Resolution: 3.9→48.59 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21631 0 361 2 21994
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.003722465
X-RAY DIFFRACTIONf_angle_d0.712530457
X-RAY DIFFRACTIONf_chiral_restr0.07643426
X-RAY DIFFRACTIONf_plane_restr0.00783913
X-RAY DIFFRACTIONf_dihedral_angle_d14.11483204
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.9-4.010.44651360.47033489X-RAY DIFFRACTION99.89
4.01-4.120.44681460.42893457X-RAY DIFFRACTION100
4.12-4.260.36311400.38063471X-RAY DIFFRACTION100
4.26-4.410.35711450.33843464X-RAY DIFFRACTION99.97
4.41-4.580.30421390.28833506X-RAY DIFFRACTION99.89
4.58-4.790.27691370.25623493X-RAY DIFFRACTION99.94
4.79-5.050.24171460.25163483X-RAY DIFFRACTION100
5.05-5.360.28711380.24653503X-RAY DIFFRACTION99.95
5.36-5.770.23841400.25163511X-RAY DIFFRACTION99.92
5.77-6.350.28171440.27553517X-RAY DIFFRACTION99.95
6.35-7.270.29381460.27933544X-RAY DIFFRACTION99.95
7.27-9.150.28491410.25543599X-RAY DIFFRACTION99.95
9.15-48.590.21381510.1873709X-RAY DIFFRACTION99.05
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)
10.200173168266-0.3412312444940.0636149201724-0.239576599669-0.7742768685152.24706788613-0.215074778143-0.0517508454411-0.1200700117390.2052699384260.0745067258043-0.07151518302010.1104328814650.1912782845791.85901439428E-51.95013083267-0.169553884584-0.03373216070991.73740652405-0.1451086441182.1569022848867.882315969733.6401225071-9.07888849736
20.523772863544-0.7208468161780.243356656810.9791381740950.4051851471350.513353764491-0.06954339247140.2298601110270.1467147422550.5413809428130.418583853774-0.606962840663-0.1808318325620.616391174487-4.75647730098E-51.984233783550.1490009996180.09483085798042.101757237760.06414115419261.9463052217445.60005031152.8896864301310.15419473
30.5431956798070.757013800507-0.05583196692051.21810986904-0.4504947532230.309268333298-0.44250051045-0.263371904151-0.3818701588260.4868628657970.495883375024-0.5802072744460.152016688743-0.823255238604-2.7242408991E-53.09779679830.8891699522170.2359492288763.14553524558-0.1053447368681.9102273243148.412324657917.155332459761.1282099272
42.85191118328-0.553369881947-0.1132016945881.349598475690.853090325923.14633973301-1.12649227983-0.343128115549-0.603425728836-0.5890715727020.6040499630540.7203052598292.078374902310.506039952939-0.8997260503922.2586943632-1.35880698938-0.548166955514-0.210703234164-0.07180087927721.9373103281636.1965451824-3.57749863175-43.0257810814
51.085605571471.00061464907-0.4111827680560.946914854856-0.07957329875611.37529355993-0.122870229847-0.6704012432380.07919397874070.228525142448-0.323117711362-0.3924513567280.674657378050.506125429329.46598821311E-52.452173460640.549391582589-0.02127954884932.5994138650.08277337740991.8822369338284.183181808721.660311242436.7617764804
61.42264502313-2.79026325866-1.026894495985.356689754441.880567593480.652888856851-2.487738837483.95880262857-0.9105323151782.96082996271-0.381743536962.12858777787-0.7884423835992.30735077089-1.739538965266.66843234202-0.130216121927-0.7986450529696.5322376811.102863833193.601018162011.3861154808513.267545245157.631538568
70.5843353637360.2096430779710.006922787283170.08186428573720.00983182198231-0.0002327766064220.708982116596-1.27474266805-1.442828002310.6249416213210.7245180364750.02029298348771.10715867738-0.1882173019230.01733703885046.024092369413.12629392124-0.02827441379747.691409628290.4494747224613.3139412314672.6592513309-14.217348316126.681169765
81.365205799030.0423625228553-0.340239968402-0.02108572436550.1898758136210.370970551549-0.421543335372-0.5013864048420.149495820051-0.06813413403430.3524788904360.5930095739870.4628716284720.2313806466832.74035344496E-53.25734768460.7066608118730.3075813886743.61943638481-0.02293834503342.4313165100629.807254623727.413204523399.207569196
90.0428053296032-0.0933655678716-0.06298580858270.1613906303160.21832813330.2579900762530.919030214412-1.22548970534-1.53997947582-1.56423193108-1.16720605005-0.92494808135-0.323964511348-0.890564909064-5.36072807309E-53.873625064260.6297671758420.6252279494714.054122720010.2303833100633.2593533979660.3158030067.88450566042111.967998846
100.1323573622670.03087632628680.2017496221150.01138521472850.0681853685570.3525378267921.181623344960.351662967772-0.0554977257126-0.05260582235180.701503370101-0.2043938541770.04599556079841.269834248860.0013825996084.372041906660.368222242782-0.6639941303052.387166705860.00372443192193.1736843510341.770436011147.382986655953.2919523605
111.74726411308-0.490426067954-0.243035942510.5041856289290.4893929490970.764824623177-0.233704654617-0.08805810784030.0003075492844130.2138339705630.0948867526450.646315810297-0.290066522806-0.193232113187-3.70325532262E-52.636999078050.2325646030070.4251122208512.306174952390.05293571879063.2403177818341.176064167136.27056861922.7109739526
123.15836522893-0.02008956039980.2652966634511.92691738330.6355050916543.493285677-0.7217101022470.2123729143930.01069094544570.6729975169250.247192259906-0.00533577011821-0.0137467692058-0.542443876792-8.83976721228E-62.088337875620.5175660279660.3191381611952.370211507020.1694772499742.1441376107818.979604211826.305714842641.7535242517
131.21000188086-0.1254828915140.1213793938251.766987435290.5439756580872.30675255485-0.0106928721726-0.31783395881-0.0303447802713-0.2827066811010.01348904721530.3076996693110.1816023981220.115394871272-7.89963097753E-52.024131964050.174261710592-0.09902785325522.329577032740.1109829964213.0036357808816.153322344823.5964656047-0.169481132077
140.1262777486420.22957508724-0.02884833299590.2463940512740.0920322850930.107256119242-0.9226890227570.37203161716-0.9326750276560.730382249911.15802265426-0.348960954085-0.963460764561-2.199674967550.0003949419621393.840558233851.378856525170.5378451144286.102418698721.249468091514.6570392816753.95414183-18.5762314095105.830121108
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-IDEnd label seq-ID
11(chain A or (chain B and resid 751:932))A - BA - E23 - 9321 - 181
22(chain B and (resid 933:1356 or resid 1664:1666) and not (resid 989:1299))BE - H933 - 1666182
33(chain B and resid 1500:1663 )BE1500 - 1663743 - 906
44(chain B and resid 989:1299)BE989 - 1299238 - 548
55(chain B and resid 1357:1499)BE1357 - 1499606 - 742
66(chain C and (resid 134:190 or resid 1029:1031 or resid 1023:1024))CI - P134 - 1031107
77(chain D and (resid 255:264 or resid 281:301 or resid 1096:1097))DQ255 - 3011 - 47
88((chain D and not (resid 255:310 or resid 1036:1037 or resid 1096:1097)) or (chain C and not (resid 28:75 or resid 134:190 or resid 1029:1031 or resid 1023:1024)))C - KI - L76 - 110149
99((chain D and (resid 265:280 or resid 302:310 or resid 1036:1037)) or (chain C and resid 28:75))C - DI - S28 - 10371
1010(chain F and resid 35:101)FE35 - 1011 - 67
1111(chain F and (resid 102:224 or resid 767:768 or resid 1025:1026 or resid 1032:1034))F - ME - N102 - 103368
1212(chain F and (resid 225:248 or resid 260:476 or resid 1027:1030 )) or (chain E)FV - E1 - 476423
1313(chain F and resid 477:766)FE477 - 765424 - 712
1414(chain R)RF2 - 1251 - 124

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