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- PDB-3hs0: Cobra Venom Factor (CVF) in complex with human factor B -

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Basic information

Entry
Database: PDB / ID: 3hs0
TitleCobra Venom Factor (CVF) in complex with human factor B
Components
  • (Cobra venom factor) x 3
  • Complement factor B
KeywordsIMMUNE SYSTEM / serine protease / glycosilated / multi-domain / complement system / convertase / Complement alternate pathway / Complement pathway / Disulfide bond / Glycoprotein / Immune response / Inflammatory response / Innate immunity / Secreted / Thioester bond / Cleavage on pair of basic residues / Glycation / Hydrolase / Protease / Sushi / Zymogen
Function / homology
Function and homology information


alternative-complement-pathway C3/C5 convertase / classical-complement-pathway C3/C5 convertase complex / complement binding / Alternative complement activation / Activation of C3 and C5 / complement activation, alternative pathway / complement activation / endopeptidase inhibitor activity / Regulation of Complement cascade / response to bacterium ...alternative-complement-pathway C3/C5 convertase / classical-complement-pathway C3/C5 convertase complex / complement binding / Alternative complement activation / Activation of C3 and C5 / complement activation, alternative pathway / complement activation / endopeptidase inhibitor activity / Regulation of Complement cascade / response to bacterium / toxin activity / blood microparticle / inflammatory response / serine-type endopeptidase activity / proteolysis / extracellular space / extracellular exosome / extracellular region / metal ion binding / plasma membrane
Similarity search - Function
ubp-family deubiquitinating enzyme fold - #20 / N-terminal domain of TfIIb - #160 / Complement factor B / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / Complement B/C2 / S-adenosyl-L-methionine-dependent methyltransferases / ubp-family deubiquitinating enzyme fold ...ubp-family deubiquitinating enzyme fold - #20 / N-terminal domain of TfIIb - #160 / Complement factor B / S-adenosyl-L-methionine-dependent methyltransferases - #20 / Immunoglobulin-like - #1940 / Alpha-macroglobulin, receptor-binding domain / Macroglobulin (MG2) domain / Complement B/C2 / S-adenosyl-L-methionine-dependent methyltransferases / ubp-family deubiquitinating enzyme fold / OB fold (Dihydrolipoamide Acetyltransferase, E2P) - #120 / N-terminal domain of TfIIb / : / : / Complement component 3, CUB domain 2 / Complement component 3, CUB domain 1 / Complement C3-like, NTR domain / 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/fibulin / Anaphylatoxin, complement system / Anaphylotoxin-like domain / Anaphylatoxin domain profile. / Anaphylatoxin homologous domain / Netrin C-terminal Domain / Netrin module, non-TIMP type / UNC-6/NTR/C345C module / Netrin domain / NTR domain profile. / 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 / 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 / Other non-globular / Sushi repeat (SCR repeat) / Domain abundant in complement control proteins; SUSHI repeat; short complement-like repeat (SCR) / Sushi/SCR/CCP domain / Sushi/SCR/CCP superfamily / Sushi/CCP/SCR domain profile. / 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 / Single Sheet / von Willebrand factor A-like domain superfamily / Special / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / 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 domain profile. / Serine proteases, trypsin family, serine active site. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Immunoglobulins / Peptidase S1, PA clan / Immunoglobulin-like fold / Immunoglobulin-like / Beta Barrel / Sandwich / Mainly Beta
Similarity search - Domain/homology
Complement factor B / Cobra venom factor
Similarity search - Component
Biological speciesHomo sapiens (human)
Naja kaouthia (monocled cobra)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3 Å
AuthorsJanssen, B.J.C. / Gomes, L. / Koning, R.I. / Svergun, D.I. / Koster, A.J. / Fritzinger, D.C. / Vogel, C.-W. / Gros, P.
CitationJournal: Embo J. / Year: 2009
Title: Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex
Authors: Janssen, B.J. / Gomes, L. / Koning, R.I. / Svergun, D.I. / Koster, A.J. / Fritzinger, D.C. / Vogel, C.W. / Gros, P.
History
DepositionJun 10, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 7, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Non-polymer description / Version format compliance
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / 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 / struct_asym / struct_conn / struct_ref_seq_dif / 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.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 / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _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_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Mar 31, 2021Group: Source and taxonomy / Structure summary / Category: chem_comp / entity_src_gen
Item: _chem_comp.pdbx_synonyms / _entity_src_gen.pdbx_host_org_cell_line / _entity_src_gen.pdbx_host_org_strain
Revision 2.2Oct 13, 2021Group: Database references / Category: database_2 / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 2.3Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cobra venom factor
B: Cobra venom factor
C: Cobra venom factor
D: Complement factor B
F: Cobra venom factor
G: Cobra venom factor
H: Cobra venom factor
I: Complement factor B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)452,13821
Polymers449,6448
Non-polymers2,49413
Water1448
1
F: Cobra venom factor
G: Cobra venom factor
H: Cobra venom factor
I: Complement factor B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)225,95910
Polymers224,8224
Non-polymers1,1376
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21900 Å2
ΔGint-98 kcal/mol
Surface area84870 Å2
MethodPISA
2
A: Cobra venom factor
B: Cobra venom factor
C: Cobra venom factor
D: Complement factor B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)226,18011
Polymers224,8224
Non-polymers1,3587
Water543
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area21840 Å2
ΔGint-97 kcal/mol
Surface area84730 Å2
MethodPISA
3
A: Cobra venom factor
B: Cobra venom factor
C: Cobra venom factor
D: Complement factor B
hetero molecules

F: Cobra venom factor
G: Cobra venom factor
H: Cobra venom factor
I: Complement factor B
hetero molecules


Theoretical massNumber of molelcules
Total (without water)452,13821
Polymers449,6448
Non-polymers2,49413
Water1086
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_544-x,y-1/2,-z-1/21
Buried area45130 Å2
ΔGint-193 kcal/mol
Surface area168220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)134.026, 136.975, 283.740
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

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Components

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Protein , 4 types, 8 molecules AFBGCHDI

#1: Protein Cobra venom factor / CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / ...CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / Cobra venom factor beta chain


Mass: 69581.984 Da / Num. of mol.: 2 / Fragment: residues 23-649 / Source method: isolated from a natural source / Details: Cobra venom / Source: (natural) Naja kaouthia (monocled cobra) / References: UniProt: Q91132
#2: Protein Cobra venom factor / CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / ...CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / Cobra venom factor beta chain


Mass: 28418.568 Da / Num. of mol.: 2 / Fragment: residues 733-984 / Source method: isolated from a natural source / Details: Cobra venom / Source: (natural) Naja kaouthia (monocled cobra) / References: UniProt: Q91132
#3: Protein Cobra venom factor / CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / ...CVF / Complement C3 homolog / Cobra venom factor alpha chain / Cobra venom factor gamma chain / Cobra venom factor beta chain


Mass: 43626.547 Da / Num. of mol.: 2 / Fragment: residues 1264-1642 / Source method: isolated from a natural source / Details: Cobra venom / Source: (natural) Naja kaouthia (monocled cobra) / References: UniProt: Q91132
#4: Protein Complement factor B / / C3/C5 convertase / Properdin factor B / Glycine-rich beta glycoprotein / GBG / PBF2 / Complement ...C3/C5 convertase / Properdin factor B / Glycine-rich beta glycoprotein / GBG / PBF2 / Complement factor B Ba fragment / Complement factor B Bb fragment


Mass: 83194.859 Da / Num. of mol.: 2 / Fragment: residues 26-764 / Mutation: D279G,N285D
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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Sugars , 2 types, 9 molecules

#5: 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.: 2
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
#6: 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 / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 7
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, 12 molecules

#7: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#8: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 2.9 Å3/Da / Density % sol: 57.53 %
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 9
Details: PEG 1500, 2,3 butanediol, malic acid 2-(N-morpholino)ethanesulfonic acid tris (hydroxymethyl)aminomethane buffer (MMT), pH 9.0, VAPOR DIFFUSION, SITTING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9834 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 15, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9834 Å / Relative weight: 1
ReflectionResolution: 3→35 Å / Num. all: 105184 / Num. obs: 104868 / % possible obs: 99.7 % / Observed criterion σ(F): -3 / Observed criterion σ(I): -3 / Redundancy: 3.8 % / Biso Wilson estimate: 80.9 Å2 / Rmerge(I) obs: 0.091 / Rsym value: 0.091 / Net I/σ(I): 12.6
Reflection shellResolution: 3→3.16 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.555 / Mean I/σ(I) obs: 2.8 / Num. measured all: 58990 / Num. unique all: 15157 / Rsym value: 0.555 / % possible all: 99.9

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
MOSFLMdata reduction
SCALA3.2.25data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACT3.005data extraction
DNAdata collection
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3HRZ

3hrz


Resolution: 3→34.883 Å / Occupancy max: 1 / Occupancy min: 1 / FOM work R set: 0.83 / SU ML: 0.32 / Isotropic thermal model: isotropic / σ(F): 1.35 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.243 2093 2 %random
Rwork0.189 ---
all0.19 105184 --
obs0.19 104789 99.76 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 24.409 Å2 / ksol: 0.255 e/Å3
Displacement parametersBiso max: 305.5 Å2 / Biso mean: 89.093 Å2 / Biso min: 23.87 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2--0 Å20 Å2
3---0 Å2
Refinement stepCycle: LAST / Resolution: 3→34.883 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms30269 0 158 8 30435
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00431140
X-RAY DIFFRACTIONf_angle_d0.88842196
X-RAY DIFFRACTIONf_chiral_restr0.074754
X-RAY DIFFRACTIONf_plane_restr0.0045405
X-RAY DIFFRACTIONf_dihedral_angle_d16.65711431
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 15

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3-3.070.3561420.29467336875100
3.07-3.1470.3391350.27968086943100
3.147-3.2310.3551550.26367766931100
3.231-3.3260.3321340.25467696903100
3.326-3.4340.281250.23268476972100
3.434-3.5560.2691420.21167666908100
3.556-3.6990.2261420.268306972100
3.699-3.8670.2771420.1868016943100
3.867-4.070.2331520.17968336985100
4.07-4.3250.2031580.15768036961100
4.325-4.6580.21210.13868676988100
4.658-5.1260.1891260.13369097035100
5.126-5.8640.1861410.14569137054100
5.864-7.3770.2321470.17269687115100
7.377-34.8850.1941310.1657073720498
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)
12.16561.60410.94751.55060.12783.52750.6427-0.0814-0.3022-0.029-0.0424-0.4097-0.00381.367-0.53440.37880.0118-0.11110.8786-0.02250.5625-7.4915-13.04729.2871
22.35-0.32830.80373.7422-0.0575.1266-0.105-0.3721-0.09680.08540.2392-0.17690.07090.2881-0.10880.2607-0.00470.01640.30370.01060.2033-16.7841-2.3782-25.3737
31.12541.7281-1.63264.3888-2.74453.479-0.0710.03380.16220.0023-0.03010.12760.1316-0.46330.09770.2194-0.10190.04990.4074-0.01460.2937-49.921-1.0714-30.6163
44.8952-0.16533.15152.6124-0.82761.3450.2651-0.8819-0.3880.3301-0.14050.1303-0.3141-0.1493-0.11260.3463-0.13110.03640.86520.06490.3137-47.9714-10.20652.6795
54.275-0.65382.57512.5133-3.30553.53230.4215-1.6005-0.14770.43670.11530.078-0.619-0.8614-0.42340.4336-0.2101-0.03441.01540.06270.2121-28.8385-6.282316.0272
63.0241-0.2176-0.59792.1929-0.77662.10410.013-0.45540.29010.32090.13820.0384-0.21770.151-0.09240.3854-0.05230.0590.3172-0.12930.2869-23.067918.9522-19.1359
70.51210.75250.40040.3132-0.54791.89950.449-0.0615-0.3538-0.02280.12610.0585-0.13910.0263-0.25910.24180.0196-0.07360.4349-0.07910.3193-25.8648-10.6181-3.445
85.7517-4.73424.23675.4532-3.21627.7966-0.629-0.01661.22130.141-0.4512-1.2076-0.63780.40871.00930.2608-0.0741-0.00680.29640.13380.3553-27.362331.5436-48.1448
92.2932-1.04110.98642.63281.15692.282-0.01530.47760.16220.0443-0.02790.11830.06870.19050.01610.2281-0.02740.02240.50070.14420.2353-32.715820.8405-52.0844
104.2719-1.76550.21672.21470.20171.1611-0.18310.4328-0.308-0.3009-0.19740.18610.21010.30590.19750.5218-0.00090.02430.5155-0.13250.4391-6.5506-15.7873-45.6367
110.5920.1393-0.96444.337-1.74813.18490.13360.40540.2059-0.1575-0.02440.17770.2403-0.552-0.05630.22760.0012-0.05670.6260.00540.3328-50.67428.7562-57.3868
121.5338-1.37680.631.91270.3411.10370.81540.6073-0.0873-1.0685-0.347-0.0298-0.52590.4117-0.38680.52280.02660.0551.130.13690.22-29.474311.1832-70.3734
133.5441.3261-0.23763.5106-0.7720.2217-0.86423.17860.3937-0.9190.95090.11430.3337-0.2682-0.04270.5782-0.5713-0.01983.01990.39330.353-15.942520.8309-86.1337
144.5560.8286-0.35882.95721.50982.22250.90371.05350.136-0.34560.5827-0.3586-1.25410.059-0.83841.05960.26790.07970.85710.38210.7489-10.495348.3233-60.5832
153.0074-0.9191-1.87421.24010.42693.46780.25930.28470.40420.04420.0392-0.0545-0.1354-0.117-0.28580.2957-0.06110.10030.39270.07680.3756-7.69721.2323-41.717
163.0887-0.834-0.96653.6296-0.01872.9634-0.13120.41830.37630.00420.3739-0.19610.2628-0.2289-0.2010.2271-0.01690.06730.51290.05940.253412.828924.271-63.8519
173.14-3.40480.72324.27840.45131.9756-0.4329-0.83880.55690.25880.5649-0.94710.1021-0.0012-0.1220.30.2035-0.13980.7092-0.25530.763713.869156.2223-35.1839
183.16660.15790.74552.01520.57731.5886-0.0583-0.5976-0.30520.0335-0.06330.257-0.373-0.5959-0.04030.41580.1990.16161.61190.06150.38-51.958683.386826.2551
193.1206-1.40431.50623.549-2.04314.3250.0232-0.7285-0.00660.05740.2350.3024-0.0202-0.2918-0.25980.2831-0.1050.03760.5423-0.06790.3099-45.438883.1531-9.6138
203.94342.08381.95952.99171.9843.87860.1708-0.2992-0.19460.16720.0583-0.1981-0.00960.1763-0.23530.2861-0.0798-0.05240.38590.00170.2777-12.704984.0651-17.4219
213.79140.3668-1.26482.33010.47853.06260.0199-0.5705-0.08020.22820.1335-0.09160.0439-0.5404-0.12220.31060.0451-0.11090.8091-0.04370.3786-11.995982.703217.096
221.91630.21440.31081.78910.43582.6284-0.119-1.2281-0.15610.41520.21620.0253-0.03490.0324-0.11610.43990.0253-0.03111.47460.15120.3443-30.017474.496729.8949
231.96670.1771-0.01871.3631-0.26321.55340.0914-0.4965-0.36930.04680.0415-0.01150.1738-0.0212-0.12920.3863-0.188-0.14020.5190.19980.4276-38.978660.9809-10.6927
24-0.0057-0.6473-0.36740.20260.16742.44820.0052-0.3910.03690.04250.138-0.1326-0.1818-0.6586-0.25210.19690.0721-0.01970.7871-0.01120.2566-34.648584.471312.798
254.01990.940.18240.8759-2.75653.59390.28240.0011-1.1526-0.1849-0.2606-0.12530.5394-0.7897-0.09470.4239-0.0168-0.20620.252-0.01850.3598-37.018158.1476-42.4644
261.126-0.2523-0.51693.045-0.93511.53820.1850.4306-0.29590.0451-0.1785-0.10720.0464-0.10710.05740.17910.0241-0.03590.3998-0.10130.3574-31.893969.5633-43.1069
273.319-2.38480.6842.86020.5817-0.34910.1777-0.1130.1547-0.2407-0.10460.06580.0085-0.4127-0.06630.53310.01790.27160.5059-0.05770.6403-57.5664101.5086-23.7278
282.49320.01141.85914.13812.06234.00290.07940.75410.0952-0.18160.0957-0.242-0.24680.624-0.16980.2133-0.03370.12680.4811-0.02890.2534-14.315982.8923-46.1399
291.9053-0.63960.95882.3129-0.10370.74890.42320.37450.0491-0.69910.39060.1581-0.14140.126-0.68060.4428-0.0133-0.0550.8036-0.00210.2751-36.308484.3975-57.3108
304.99512.14480.61242.91630.35032.4197-0.03531.12890.218-0.54360.10150.1250.1513-0.3266-0.03120.55040.0162-0.11981.01950.22060.3982-50.591879.5807-74.4825
312.0389-0.2722-0.78852.5478-0.8691-0.32410.2241.9265-0.1683-0.6835-0.39340.13170.2687-0.73580.27750.97220.21990.11431.8202-0.25240.9061-53.746746.4098-58.0495
321.74440.4176-0.26741.94720.35131.12940.35960.0121-0.3743-0.0411-0.17230.10980.03720.0563-0.14270.2272-0.0326-0.1260.4370.00780.4964-56.090165.5813-31.8027
332.3386-0.1224-1.09693.3199-1.14392.5831-0.30030.6994-0.1374-0.00530.48070.6699-0.1034-0.8413-0.20060.23060.0282-0.15180.74420.09670.5114-77.758768.7485-52.5888
341.0505-1.4796-0.61675.46630.32181.6097-0.2698-0.54780.02210.45090.41680.21090.028-0.1537-0.15290.45220.11090.01950.8090.04090.4461-77.219929.9165-35.8985
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain A and resseq 1:101A1 - 101
2X-RAY DIFFRACTION2chain A and (resseq 102:199 or resseq 187:187)A102 - 199
3X-RAY DIFFRACTION2chain A and (resseq 102:199 or resseq 187:187)A187
4X-RAY DIFFRACTION3chain A and resseq 200:318A200 - 318
5X-RAY DIFFRACTION4chain A and resseq 319:412A319 - 412
6X-RAY DIFFRACTION5chain A and resseq 413:520A413 - 520
7X-RAY DIFFRACTION6(chain A or chain B) and (resseq 521:559 or resseq 729:789)A0
8X-RAY DIFFRACTION7chain A and resseq 560:627A560 - 627
9X-RAY DIFFRACTION8chain B and resseq 711:728B711 - 728
10X-RAY DIFFRACTION9chain B and resseq 790:896B790 - 896
11X-RAY DIFFRACTION10(chain B or chain C) and (resseq 897:946 or resseq 1251:1313)B0
12X-RAY DIFFRACTION11chain C and (resseq 1314:1452 or resseq 1324:1324)C1314 - 1452
13X-RAY DIFFRACTION11chain C and (resseq 1314:1452 or resseq 1324:1324)C1324
14X-RAY DIFFRACTION12chain C and resseq 1453:1475C1453 - 1475
15X-RAY DIFFRACTION13chain C and resseq 1476:1620C1476 - 1620
16X-RAY DIFFRACTION14chain D and resseq 1:75D1 - 75
17X-RAY DIFFRACTION15chain D and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)D76 - 199
18X-RAY DIFFRACTION15chain D and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)D9097 - 9099
19X-RAY DIFFRACTION15chain D and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)D9117 - 9118
20X-RAY DIFFRACTION16chain D and (resseq 200:449 or resseq 9353:9353)D200 - 449
21X-RAY DIFFRACTION16chain D and (resseq 200:449 or resseq 9353:9353)D9353
22X-RAY DIFFRACTION17chain D and resseq 450:742D450 - 742
23X-RAY DIFFRACTION18chain F and resseq 1:101F1 - 101
24X-RAY DIFFRACTION19chain F and (resseq 102:199 or resseq 187:187)F102 - 199
25X-RAY DIFFRACTION19chain F and (resseq 102:199 or resseq 187:187)F187
26X-RAY DIFFRACTION20chain F and resseq 200:318F200 - 318
27X-RAY DIFFRACTION21chain F and resseq 319:412F319 - 412
28X-RAY DIFFRACTION22chain F and resseq 413:520F413 - 520
29X-RAY DIFFRACTION23(chain F or chain G) and (resseq 521:559 or resseq 729:789)F0
30X-RAY DIFFRACTION24chain F and resseq 560:627F560 - 627
31X-RAY DIFFRACTION25chain G and resseq 711:728G711 - 728
32X-RAY DIFFRACTION26chain G and resseq 790:896G790 - 896
33X-RAY DIFFRACTION27(chain G or chain H) and (resseq 897:946 or resseq 1251:1313)G0
34X-RAY DIFFRACTION28chain H and (resseq 1314:1452 or resseq 1324:1324)H1314 - 1452
35X-RAY DIFFRACTION28chain H and (resseq 1314:1452 or resseq 1324:1324)H1324
36X-RAY DIFFRACTION29chain H and resseq 1453:1475H1453 - 1475
37X-RAY DIFFRACTION30chain H and resseq 1476:1620H1476 - 1620
38X-RAY DIFFRACTION31chain I and resseq 1:75I1 - 75
39X-RAY DIFFRACTION32chain I and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)I76 - 199
40X-RAY DIFFRACTION32chain I and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)I9097 - 9099
41X-RAY DIFFRACTION32chain I and (resseq 76:199 or resseq 9097:9099 or resseq 9117:9118)I9117 - 9118
42X-RAY DIFFRACTION33chain I and (resseq 200:449 or resseq 9353:9353)I200 - 449
43X-RAY DIFFRACTION33chain I and (resseq 200:449 or resseq 9353:9353)I9353
44X-RAY DIFFRACTION34chain I and resseq 450:742I450 - 742

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