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- PDB-1sqv: Crystal Structure Analysis of Bovine Bc1 with UHDBT -

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Basic information

Entry
Database: PDB / ID: 1sqv
TitleCrystal Structure Analysis of Bovine Bc1 with UHDBT
Components
  • (Ubiquinol-cytochrome C reductase complex ...) x 8
  • Cytochrome b
  • Cytochrome c1, heme protein, mitochondrial
  • Ubiquinol-cytochrome c reductase iron-sulfur subunit
KeywordsOXIDOREDUCTASE / cytochrome bc1 / Qo inhibitor / membrane protein / electron transport
Function / homology
Function and homology information


Complex III assembly / subthalamus development / pons development / cerebellar Purkinje cell layer development / pyramidal neuron development / Respiratory electron transport / thalamus development / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity ...Complex III assembly / subthalamus development / pons development / cerebellar Purkinje cell layer development / pyramidal neuron development / Respiratory electron transport / thalamus development / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / Mitochondrial protein degradation / hypothalamus development / midbrain development / ubiquinone binding / hippocampus development / respiratory electron transport chain / mitochondrial membrane / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / oxidoreductase activity / mitochondrial inner membrane / heme binding / mitochondrion / proteolysis / metal ion binding / membrane
Similarity search - Function
Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #220 / Cytochrome Bc1 Complex; Chain I / Cytochrome Bc1 Complex; Chain I / Cytochrome Bc1 Complex; Chain F / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit 9 / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol cytochrome reductase, transmembrane domain / Cytochrome c1, transmembrane anchor, C-terminal ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #220 / Cytochrome Bc1 Complex; Chain I / Cytochrome Bc1 Complex; Chain I / Cytochrome Bc1 Complex; Chain F / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit 9 / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol cytochrome reductase, transmembrane domain / Cytochrome c1, transmembrane anchor, C-terminal / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome b-c1 complex subunit 10 / Single alpha-helix domain superfamily / Ubiquinol-cytochrome C reductase complex, 6.4kD protein / Cytochrome Bc1 Complex; Chain A, domain 1 / Metalloenzyme, LuxS/M16 peptidase-like / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Globular protein, non-globular alpha/beta subunit / Cytochrome b-c1 complex, subunit 6 / Rieske Iron-sulfur Protein / Rieske [2Fe-2S] iron-sulphur domain / 3-layer Sandwich / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome c1, transmembrane anchor, C-terminal / : / Cytochrome b / Ubiquinol-cytochrome c reductase, iron-sulphur subunit / : / Cytochrome c1 / Cytochrome C1 family / : / Cytochrome b/b6, C-terminal / Cytochrome b(C-terminal)/b6/petD / Cytochrome b/b6 C-terminal region profile. / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Rieske iron-sulphur protein, C-terminal / Cytochrome b/b6, N-terminal / Cytochrome b/b6-like domain superfamily / Cytochrome b/b6 N-terminal region profile. / Di-haem cytochrome, transmembrane / Rieske iron-sulphur protein / Peptidase M16, C-terminal / Peptidase M16 inactive domain / Peptidase M16, N-terminal / Insulinase (Peptidase family M16) / Metalloenzyme, LuxS/M16 peptidase-like / Cytochrome c-like domain / Cytochrome Bc1 Complex; Chain D, domain 2 / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Ribbon / Helix Hairpins / Up-down Bundle / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
FE2/S2 (INORGANIC) CLUSTER / HEME C / 6-HYDROXY-5-UNDECYL-1,3-BENZOTHIAZOLE-4,7-DIONE / UBIQUINONE-2 / Cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 9 / Cytochrome b / Cytochrome b-c1 complex subunit 10 ...FE2/S2 (INORGANIC) CLUSTER / HEME C / 6-HYDROXY-5-UNDECYL-1,3-BENZOTHIAZOLE-4,7-DIONE / UBIQUINONE-2 / Cytochrome c1, heme protein, mitochondrial / Cytochrome b-c1 complex subunit 6, mitochondrial / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 9 / Cytochrome b / Cytochrome b-c1 complex subunit 10 / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit Rieske, mitochondrial / Cytochrome b-c1 complex subunit 2, mitochondrial / Cytochrome b-c1 complex subunit 1, mitochondrial
Similarity search - Component
Biological speciesBos taurus (domestic cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 2.85 Å
AuthorsEsser, L. / Quinn, B. / Li, Y.F. / Zhang, M. / Elberry, M. / Yu, L. / Yu, C.A. / Xia, D.
Citation
Journal: J.Mol.Biol. / Year: 2004
Title: Crystallographic studies of quinol oxidation site inhibitors: a modified classification of inhibitors for the cytochrome bc(1) complex.
Authors: Esser, L. / Quinn, B. / Li, Y.F. / Zhang, M. / Elberry, M. / Yu, L. / Yu, C.A. / Xia, D.
#1: Journal: Science / Year: 1997
Title: Crystal structure of the cytochrome bc1 complex from bovine heart mitochondria
Authors: Xia, D. / Yu, C.A. / Kim, H. / Xia, J.Z. / Kachurin, A.M. / Zhang, L. / Yu, L. / Deisenhofer, J.
#2: Journal: Biochemistry / Year: 2002
Title: The crystal structure of mitochondrial cytochrome bc1 in complex with famoxadone: the role of aromatic-aromatic interaction in inhibition
Authors: Gao, X. / Wen, X. / Yu, C. / Esser, L. / Tsao, S. / Quinn, B. / Zhang, L. / Yu, L. / Xia, D.
History
DepositionMar 19, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 6, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 2.0Mar 3, 2021Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_conn_angle / 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_atom_id / _atom_site.auth_comp_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.name / _chem_comp.pdbx_synonyms / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.comp_id / _pdbx_entity_nonpoly.name / _pdbx_nonpoly_scheme.mon_id / _pdbx_nonpoly_scheme.pdb_mon_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_auth_comp_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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.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 / _struct_site.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id / _struct_site_gen.auth_comp_id / _struct_site_gen.label_comp_id
Revision 2.1Oct 30, 2024Group: Data collection / Database references / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ubiquinol-cytochrome c reductase complex core protein I, mitochondrial
B: Ubiquinol-cytochrome c reductase complex core protein 2, mitochondrial
C: Cytochrome b
D: Cytochrome c1, heme protein, mitochondrial
E: Ubiquinol-cytochrome c reductase iron-sulfur subunit
F: Ubiquinol-cytochrome C reductase complex 14 kDa protein
G: Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein QP-C
H: Ubiquinol-cytochrome C reductase complex 11 kDa protein
I: Ubiquinol-cytochrome C reductase complex 8 kDa protein
J: Ubiquinol-cytochrome C reductase complex 7.2 kDa protein
K: Ubiquinol-cytochrome C reductase complex 6.4 kDa protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)243,97917
Polymers241,29311
Non-polymers2,6856
Water5,242291
1
A: Ubiquinol-cytochrome c reductase complex core protein I, mitochondrial
B: Ubiquinol-cytochrome c reductase complex core protein 2, mitochondrial
C: Cytochrome b
D: Cytochrome c1, heme protein, mitochondrial
E: Ubiquinol-cytochrome c reductase iron-sulfur subunit
F: Ubiquinol-cytochrome C reductase complex 14 kDa protein
G: Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein QP-C
H: Ubiquinol-cytochrome C reductase complex 11 kDa protein
I: Ubiquinol-cytochrome C reductase complex 8 kDa protein
J: Ubiquinol-cytochrome C reductase complex 7.2 kDa protein
K: Ubiquinol-cytochrome C reductase complex 6.4 kDa protein
hetero molecules

A: Ubiquinol-cytochrome c reductase complex core protein I, mitochondrial
B: Ubiquinol-cytochrome c reductase complex core protein 2, mitochondrial
C: Cytochrome b
D: Cytochrome c1, heme protein, mitochondrial
E: Ubiquinol-cytochrome c reductase iron-sulfur subunit
F: Ubiquinol-cytochrome C reductase complex 14 kDa protein
G: Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein QP-C
H: Ubiquinol-cytochrome C reductase complex 11 kDa protein
I: Ubiquinol-cytochrome C reductase complex 8 kDa protein
J: Ubiquinol-cytochrome C reductase complex 7.2 kDa protein
K: Ubiquinol-cytochrome C reductase complex 6.4 kDa protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)487,95734
Polymers482,58722
Non-polymers5,37012
Water32418
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_665-x+1,-y+1,z1
Buried area101840 Å2
ΔGint-690 kcal/mol
Surface area162040 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)153.672, 153.672, 589.219
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number98
Space group name H-MI4122

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Components

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Ubiquinol-cytochrome C reductase complex ... , 8 types, 8 molecules ABFGHIJK

#1: Protein Ubiquinol-cytochrome c reductase complex core protein I, mitochondrial / Complex III subunit I


Mass: 49266.254 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P31800, quinol-cytochrome-c reductase
#2: Protein Ubiquinol-cytochrome c reductase complex core protein 2, mitochondrial / Complex III subunit II


Mass: 46575.469 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P23004, quinol-cytochrome-c reductase
#6: Protein Ubiquinol-cytochrome C reductase complex 14 kDa protein / Complex III subunit VI


Mass: 13371.190 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00129, quinol-cytochrome-c reductase
#7: Protein Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein QP-C / Complex III subunit VII


Mass: 9606.027 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P13271, quinol-cytochrome-c reductase
#8: Protein Ubiquinol-cytochrome C reductase complex 11 kDa protein / Complex III subunit VIII


Mass: 9189.116 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00126, quinol-cytochrome-c reductase
#9: Protein Ubiquinol-cytochrome C reductase complex 8 kDa protein / Complex III subunit IX


Mass: 7964.259 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P13272, quinol-cytochrome-c reductase
#10: Protein Ubiquinol-cytochrome C reductase complex 7.2 kDa protein / Complex III subunit X


Mass: 7209.311 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00130, quinol-cytochrome-c reductase
#11: Protein Ubiquinol-cytochrome C reductase complex 6.4 kDa protein / Complex III subunit XI


Mass: 6527.604 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P07552, quinol-cytochrome-c reductase

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Protein , 3 types, 3 molecules CDE

#3: Protein Cytochrome b


Mass: 42620.340 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00157, quinol-cytochrome-c reductase
#4: Protein Cytochrome c1, heme protein, mitochondrial / Cytochrome c-1


Mass: 27323.277 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00125, quinol-cytochrome-c reductase
#5: Protein Ubiquinol-cytochrome c reductase iron-sulfur subunit / Complex III subunit IX


Mass: 21640.580 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P13272, quinol-cytochrome-c reductase

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Non-polymers , 5 types, 297 molecules

#12: Chemical ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#13: Chemical ChemComp-UHD / 6-HYDROXY-5-UNDECYL-1,3-BENZOTHIAZOLE-4,7-DIONE / 3-UNDECYL-2-HYDROXYDIOXOBENZOTHIAZOL / UHDBT


Mass: 335.461 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H25NO3S
#14: Chemical ChemComp-UQ2 / UBIQUINONE-2


Mass: 318.407 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C19H26O4
#15: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe2S2
#16: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 291 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 3.6 Å3/Da / Density % sol: 65.87 %
Crystal growTemperature: 277 K / Method: vapor diffusion / pH: 7.2
Details: 20mM ammonium acetate, 20% glycerol, 12% PEG4000, 0.5M KCl, 0.1% diheptanoyl-phosphatidylcholine, pH 7.2, VAPOR DIFFUSION, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1.2 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Jan 8, 2002 / Details: mirrors
RadiationMonochromator: SAGITTALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.2 Å / Relative weight: 1
ReflectionResolution: 2.85→50 Å / Num. all: 70581 / Num. obs: 68441 / Observed criterion σ(F): 0 / Observed criterion σ(I): -0.5

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
HKL-2000data reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.85→40 Å / Cor.coef. Fo:Fc: 0.918 / Cor.coef. Fo:Fc free: 0.873 / SU B: 20.576 / SU ML: 0.377 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.435 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.28495 2124 3 %RANDOM
Rwork0.21698 ---
all0.2191 68441 --
obs0.2191 68441 85.46 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 34.742 Å2
Baniso -1Baniso -2Baniso -3
1-2.22 Å20 Å20 Å2
2--2.22 Å20 Å2
3----4.43 Å2
Refinement stepCycle: LAST / Resolution: 2.85→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16483 0 179 291 16953
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.02117473
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.871.98523681
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg12.404102089
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.1910.22579
X-RAY DIFFRACTIONr_gen_planes_refined0.020.0213018
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1850.28913
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1440.2752
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined0.0110.21
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.1630.2106
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.170.223
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_mcbond_it0.5120.410466
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.4473.80116841
X-RAY DIFFRACTIONr_scbond_it5.1237004
X-RAY DIFFRACTIONr_scangle_it7.5454.56832
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.851→2.924 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.412 30
Rwork0.345 973
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)
10.96170.10330.53631.3571-0.85392.02470.0645-0.02730.0618-0.10480.06390.7553-0.0019-0.7274-0.12840.4384-0.06820.03080.57350.00160.726731.652387.014692.6812
20.0979-0.3140.13051.5950.12590.905-0.0338-0.09790.11530.24480.0010.2777-0.1174-0.38090.03280.431-0.10760.12970.2894-0.00090.44448.619293.1821114.6354
31.0945-0.3345-0.01471.88430.25342.31340.05190.0460.2165-0.0379-0.00530.1481-0.3489-0.1268-0.04650.2729-0.09340.01510.03640.01080.254268.6117104.210991.762
41.1329-0.75670.04243.1785-0.08881.60660.01580.0169-0.1175-0.18480.03940.43530.0693-0.2717-0.05520.2716-0.0875-0.0520.1559-0.00960.310156.913486.221873.1542
51.0942-0.02010.29320.33330.64380.810.0379-0.32080.03020.3628-0.0129-0.0193-0.0025-0.0591-0.0250.8294-0.25490.07290.41250.040.433564.631368.4054153.7852
62.10860.9977-1.42262.93332.03322.5608-0.1856-0.20690.23780.93060.3471-0.52920.15820.3169-0.16151.1787-0.2007-0.06510.69750.20570.527781.316856.8636171.5416
71.1947-0.05791.07751.1577-0.52224.10450.0506-0.3474-0.13250.4074-0.0621-0.07650.22150.22120.01150.8006-0.270.06350.39070.09790.514964.644844.7772152.7457
80000000000000000.5761000.576100.5761000
90.9065-0.066-1.3157-0.0133-0.54427.65730.0534-0.40070.05340.36960.0280.12970.3711-0.7086-0.08140.8842-0.24410.21940.5290.03490.542945.070570.957158.6773
101.29150.5460.63212.6321.00151.16860.0246-0.5346-0.16150.57160.1549-0.04040.0138-0.0212-0.17951.4741-0.22080.23721.25230.09880.690154.320666.9101192.0144
111.51740.39111.23431.10751.28343.87820.0919-0.4524-0.03890.3169-0.16230.1721-0.2116-0.82220.07040.6724-0.20140.25880.50990.04930.650743.020681.8827141.4039
124.0512-1.4241-1.46391.34870.3395.621-0.0233-1.16070.39830.78740.01750.0637-0.1579-0.36890.00591.6894-0.30440.08051.2326-0.34110.890473.6699112.4094187.7514
133.3611-1.3454-1.40211.7826-0.09911.7138-0.076-0.2382-0.45050.30120.02470.30420.4789-0.29120.05130.6363-0.27080.05970.28040.01170.368458.748746.8256121.9518
140.28310.1417-0.21381.351-1.77653.63250.0458-0.4582-0.11650.34190.01370.15860.2117-0.2779-0.05960.7554-0.26460.13970.55950.03440.557547.864654.3432144.2213
155.6836-3.5537-3.47517.47530.002512.40470.3136-0.1573-0.5178-0.8672-0.25290.14110.3954-0.3455-0.06070.9237-0.37050.03781.03660.13650.952439.344140.2349193.3021
1610.7765-15.2241-7.826335.68930.7146.81470.16640.4350.18380.1242-0.7638-0.26710.3498-0.68460.59740.9075-0.4030.00571.00890.02020.7639.660149.3723186.6306
170000000000000000.5761000.576100.5761000
180.8502-0.3863.818911.76422.4944-13.3594-0.13060.22190.1007-0.3404-0.46910.24380.7344-1.47150.59970.6077-0.10120.13890.5936-0.05730.634960.323394.540888.4712
199.29314.58715.720412.25074.879921.67110.5921-0.6230.05760.1378-0.13640.78210.7617-0.9942-0.45570.6455-0.03760.11010.7813-0.04330.809654.474680.601393.6741
20159.49740.9357-0.150258.645119.140159.007-0.77874.7042-0.4789-0.31421.1071-0.5736-0.809-1.2483-0.32840.577-0.00250.00020.579-0.00380.57946.860197.8409104.1184
211.47550.413-1.05842.79920.2740.7435-0.0644-0.3202-0.06770.65790.17520.3293-0.2612-1.2502-0.11080.9234-0.13170.28680.9938-0.08150.713438.415288.2708160.365
222.262.2148-4.4814.9854-5.916.3470.2224-0.38160.05370.52260.07790.1852-0.5953-0.3863-0.30030.821-0.0470.08050.5893-0.19890.696552.6112104.3757146.0771
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1 - 2311 - 231
2X-RAY DIFFRACTION2AA232 - 446232 - 446
3X-RAY DIFFRACTION3BB17 - 23517 - 235
4X-RAY DIFFRACTION4BB236 - 439236 - 439
5X-RAY DIFFRACTION5CC3 - 1333 - 133
6X-RAY DIFFRACTION5CC173 - 264173 - 264
7X-RAY DIFFRACTION5CL - M381 - 382
8X-RAY DIFFRACTION6CC134 - 172134 - 172
9X-RAY DIFFRACTION7CC265 - 379265 - 379
11X-RAY DIFFRACTION9DD173 - 241173 - 241
12X-RAY DIFFRACTION10DD1 - 1721 - 172
13X-RAY DIFFRACTION10DN242
14X-RAY DIFFRACTION11EE1 - 711 - 71
15X-RAY DIFFRACTION12EE - O72 - 19772
16X-RAY DIFFRACTION13FF6 - 1106 - 110
17X-RAY DIFFRACTION14GG1 - 751 - 75
18X-RAY DIFFRACTION15HH12 - 5212 - 52
19X-RAY DIFFRACTION16HH53 - 7853 - 78
20X-RAY DIFFRACTION17HH49 - 7849 - 78
21X-RAY DIFFRACTION18II2 - 262 - 26
22X-RAY DIFFRACTION19II27 - 5127 - 51
23X-RAY DIFFRACTION20II52 - 5752 - 57
24X-RAY DIFFRACTION21JJ2 - 612 - 61
25X-RAY DIFFRACTION22KK1 - 511 - 51

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