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- PDB-1nu1: Crystal Structure of Mitochondrial Cytochrome bc1 Complexed with ... -

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Basic information

Entry
Database: PDB / ID: 1nu1
TitleCrystal Structure of Mitochondrial Cytochrome bc1 Complexed with 2-nonyl-4-hydroxyquinoline N-oxide (NQNO)
Components
  • (Ubiquinol-cytochrome C reductase complex ...) x 7
  • Cytochrome b
  • UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial
  • Ubiquinol-cytochrome C reductase 8 kDa protein
  • cytochrome c1
KeywordsOXIDOREDUCTASE / BC1 / QCR / MEMBRANE PROTEIN / PROTON TRANSLOCATION / ELECTRON TRANSFER / PROTEASE / MPP / MITOCHONDRIAL PROCESSING PEPTIDASE / CYTOCHROME C1 / CYTOCHROME B / RIESKE / IRON SULFUR PROTEIN / 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE (NQNO)
Function / homology
Function and homology information


Complex III assembly / respiratory chain complex III / Respiratory electron transport / : / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / ubiquinone binding / Mitochondrial protein degradation / : ...Complex III assembly / respiratory chain complex III / Respiratory electron transport / : / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / ubiquinone binding / Mitochondrial protein degradation / : / respiratory electron transport chain / mitochondrial membrane / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / mitochondrial inner membrane / oxidoreductase activity / heme binding / mitochondrion / proteolysis / membrane / metal ion binding
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 / Ubiquinol cytochrome reductase, transmembrane domain / Cytochrome Bc1 Complex; Chain F / Cytochrome b-c1 complex subunit 7 / Ubiquinol-cytochrome C reductase hinge domain / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit 9 / Cytochrome Bc1 Complex; Chain C ...Single alpha-helices involved in coiled-coils or other helix-helix interfaces - #220 / Cytochrome Bc1 Complex; Chain I / Cytochrome Bc1 Complex; Chain I / Ubiquinol cytochrome reductase, transmembrane domain / Cytochrome Bc1 Complex; Chain F / Cytochrome b-c1 complex subunit 7 / Ubiquinol-cytochrome C reductase hinge domain / Cytochrome b-c1 complex subunit 8 / Cytochrome b-c1 complex subunit 9 / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / 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 / Cytochrome b-c1 complex, subunit 6 / Globular protein, non-globular alpha/beta subunit / 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 9 / Cytochrome b-c1 complex subunit 8 superfamily / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / Cytochrome b-c1 complex subunit Rieske, transmembrane domain / Ubiquinol cytochrome reductase transmembrane region / 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. / Cytochrome b/b6, C-terminal domain superfamily / Cytochrome b/b6/petB / Peptidase M16, zinc-binding site / Insulinase family, zinc-binding region signature. / 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 / PROTOPORPHYRIN IX CONTAINING FE / 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE / 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 ...FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE / 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 (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / FOURIER SYNTHESIS / Resolution: 3.2 Å
AuthorsGao, X. / Wen, X. / Esser, L. / Quinn, B. / Yu, L. / Yu, C.-A. / Xia, D.
CitationJournal: Biochemistry / Year: 2003
Title: Structural basis for the quinone reduction in the bc(1) complex: a comparative analysis of crystal structures of mitochondrial cytochrome bc(1) with bound substrate and inhibitors at the Q(i) site
Authors: Gao, X. / Wen, X. / Esser, L. / Quinn, B. / Yu, L. / Yu, C.-A. / Xia, D.
History
DepositionJan 30, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 7, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Nov 20, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_entry_details / pdbx_modification_feature / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _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_auth_asym_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_atom_id / _pdbx_struct_conn_angle.ptnr2_label_comp_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.pdbx_dist_value / _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.ptnr2_label_seq_id / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Remark 999Authors informed that for residue 22 of chain K, a GLN fits better in the density map than a SER. ...Authors informed that for residue 22 of chain K, a GLN fits better in the density map than a SER. They do not know if this represents a natural mutation or variant.

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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
E: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial
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 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)241,50816
Polymers239,19511
Non-polymers2,3135
Water362
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
E: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial
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 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
E: UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial
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 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)483,01532
Polymers478,39022
Non-polymers4,62510
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_665-x+1,-y+1,z1
Buried area97780 Å2
ΔGint-653 kcal/mol
Surface area165400 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)153.842, 153.842, 590.374
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number98
Space group name H-MI4122
DetailsThe biological assembly is a dimer generated from the monomer in the asymmetric unit by the two-fold axis: -x+1, -y+1, z.

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Components

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Ubiquinol-cytochrome C reductase complex ... , 7 types, 7 molecules ABFGHJK

#1: Protein Ubiquinol-cytochrome C reductase complex core protein I, mitochondrial


Mass: 49266.254 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (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 (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 (cattle) / References: UniProt: P00129, quinol-cytochrome-c reductase
#7: Protein Ubiquinol-cytochrome C reductase complex ubiquinone-binding protein QP-C / Ubiquinol-cytochrome C reductase complex 9.5 kDa protein / Complex III subunit VII


Mass: 9606.027 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P13271, quinol-cytochrome-c reductase
#8: Protein Ubiquinol-cytochrome C reductase complex 11 kDa protein / Mitochondrial hinge protein / Cytochrome C1 / nonheme 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 (cattle) / References: UniProt: P00126, quinol-cytochrome-c reductase
#10: Protein Ubiquinol-cytochrome C reductase complex 7.2 kDa protein / Cytochrome C1 / nonheme 7 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 (cattle) / References: UniProt: P00130, quinol-cytochrome-c reductase
#11: Protein Ubiquinol-cytochrome C reductase complex 6.4 kDa protein / Complex III subunit XI


Mass: 6568.655 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P07552, quinol-cytochrome-c reductase

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Protein , 4 types, 4 molecules CDEI

#3: Protein Cytochrome b


Mass: 42620.340 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00157
#4: Protein cytochrome c1


Mass: 27323.277 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00125
#5: Protein UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT, mitochondrial / Rieske iron-sulfur protein / RISP


Mass: 21640.580 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P13272, quinol-cytochrome-c reductase
#9: Protein Ubiquinol-cytochrome C reductase 8 kDa protein / Complex III subunit IX


Mass: 5824.802 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P13272, quinol-cytochrome-c reductase

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Non-polymers , 4 types, 7 molecules

#12: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#13: Chemical ChemComp-QNO / 2-NONYL-4-HYDROXYQUINOLINE N-OXIDE


Mass: 287.397 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C18H25NO2
#14: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe2S2
#15: 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 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: 3.65 Å3/Da / Density % sol: 66.29 %
Crystal growTemperature: 277 K / Method: vapor diffusion / pH: 7.2
Details: PEG 4000, ammonium acetate, potassium chloride, glycerol, DMG/SPC, MOPS, pH 7.2, VAPOR DIFFUSION, temperature 277K
Crystal grow
*PLUS
Method: vapor diffusion, hanging drop
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDDetails
120 mg/mlprotein1drop
250 mMMOPS1reservoirpH7.2
320 mMammonium acetate1reservoir
420 %(w/v)glycerol1reservoir
50.1 %decanoyl-N-methylglucamide1reservoir

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 17-ID / Wavelength: 1.2 Å
DetectorType: MARRESEARCH / Detector: CCD
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.2 Å / Relative weight: 1
ReflectionResolution: 3.2→50 Å / Num. all: 59010 / Num. obs: 58833 / % possible obs: 99.7 % / Observed criterion σ(I): -1
Reflection shellResolution: 3.201→3.275 Å / % possible all: 98.3
Reflection
*PLUS
Lowest resolution: 50 Å / Rmerge(I) obs: 0.085
Reflection shell
*PLUS
% possible obs: 98.3 % / Rmerge(I) obs: 0.679 / Mean I/σ(I) obs: 1.8

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Processing

Software
NameVersionClassification
REFMAC5refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 3.2→10 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.87 / SU B: 24.233 / SU ML: 0.424 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.538 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.29554 1742 3.1 %RANDOM
Rwork0.21478 ---
all0.2172 58833 --
obs0.21728 54977 99.89 %-
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: 30.899 Å2
Baniso -1Baniso -2Baniso -3
1-1.62 Å20 Å20 Å2
2--1.62 Å20 Å2
3----3.24 Å2
Refinement stepCycle: LAST / Resolution: 3.2→10 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16510 0 154 2 16666
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0190.02117536
X-RAY DIFFRACTIONr_angle_refined_deg2.0561.98423769
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.58532094
X-RAY DIFFRACTIONr_dihedral_angle_2_deg22.569152958
X-RAY DIFFRACTIONr_chiral_restr0.3560.22596
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0213067
X-RAY DIFFRACTIONr_nbd_refined0.260.310173
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2230.51330
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2310.3124
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.3210.513
X-RAY DIFFRACTIONr_mcbond_it0.7650.410490
X-RAY DIFFRACTIONr_mcangle_it3.313.80116876
X-RAY DIFFRACTIONr_scbond_it6.94137046
X-RAY DIFFRACTIONr_scangle_it9.8514.56891
LS refinement shellResolution: 3.201→3.275 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.384 115
Rwork0.286 3698
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)
10.78540.05370.35671.3924-0.75191.77410.0709-0.0110.0479-0.09460.06750.77260.0283-0.7706-0.13840.5368-0.09190.06020.6652-0.03160.723731.746787.164892.8797
20.1446-0.46070.09511.37990.00320.72670.0162-0.12660.10330.2943-0.01310.326-0.1177-0.3844-0.00310.5999-0.13490.1810.3798-0.01690.396348.615793.2251114.495
31.3657-0.44920.01992.18730.37552.21610.05280.02470.23970.0239-0.00910.089-0.2569-0.1401-0.04370.3968-0.14170.02280.0506-0.00760.165668.6858104.329291.9242
40.6373-0.31030.24042.53390.31031.93640.07260.1192-0.1108-0.1751-0.04930.54360.0686-0.2732-0.02320.3513-0.0758-0.04830.2106-0.00370.284257.634387.031474.016
50.934-0.09520.01030.16870.54391.04590.0511-0.38580.01550.33090.0844-0.0286-0.133-0.0568-0.13550.9712-0.24630.10630.49240.02960.392164.679768.4485153.8186
65.5106-1.9406-0.49993.56924.06461.0449-0.1102-0.2011-0.10530.62210.141-0.12290.03410.1801-0.03081.3112-0.2213-0.08420.83160.21590.581481.269156.8742171.9593
71.3512-0.17970.94930.52550.08853.28090.034-0.4427-0.17030.38880.0113-0.08650.07840.0464-0.04530.9365-0.29220.110.47290.11720.492564.800844.8534152.9646
8-1.9483-1.07920.1351-0.47441.08450.443-0.1665-0.3153-0.00610.7694-0.0374-0.0438-0.1048-0.26850.20391.13-0.20630.16250.96180.02670.799751.854273.313146.5301
90.8348-0.3421-1.2783-0.1904-0.54616.23480.0322-0.3595-0.01670.33230.0480.0017-0.0276-0.9017-0.08021.0067-0.29390.22820.59750.02980.526245.177471.2471159.0156
100.489-0.1040.6620.36840.06871.2512-0.1003-0.4805-0.10230.52010.2221-0.0440.0333-0.0734-0.12181.4005-0.13970.20831.26440.07630.772454.265667.2921191.9024
111.9787-0.01331.93930.96640.70285.1392-0.114-0.53660.04520.2543-0.12980.2629-0.4381-0.94520.24380.7384-0.1990.30890.6134-0.0070.633843.184481.9703141.6186
121.4961-1.54410.3965-0.79141.50191.0921-0.2208-0.73690.21320.6040.10180.0148-0.1025-0.38130.1191.8923-0.19310.06461.4203-0.24691.112373.6771112.6351188.12
134.9014-1.093-1.81721.5746-0.19491.657-0.0379-0.1985-0.48090.2434-0.00680.3190.3755-0.15630.04470.7227-0.32360.05750.35120.00380.293658.846846.9935122.0467
140.3223-0.0846-0.01111.4817-1.92033.3274-0.0336-0.4147-0.17030.41880.21270.29640.0073-0.397-0.17910.8519-0.27480.18140.58720.05380.575947.973354.6777144.2233
154.0071-3.5059-2.67813.65913.32413.3063-0.0328-0.2717-0.25580.39130.08850.0846-0.3263-0.1762-0.05571.4206-0.28150.111.42740.29021.154539.375141.8221194.8585
166.5626-6.8466-0.743718.13123.121.7137-0.1245-0.58730.46310.26570.1132-0.3504-0.123-0.51210.01141.3351-0.26130.35891.38120.19690.859239.74749.6601187.2544
170000000000000000.6738000.673800.6738000
185.355-2.81535.24665.14763.0182-6.1309-0.11460.2130.42090.0553-0.71090.37881.0185-0.70510.82540.6264-0.23040.14780.54-0.0760.492160.334295.046388.3521
19-2.5099-0.1248-0.307-11.63070.9065-2.76020.2036-0.18580.1898-0.3517-0.19130.43620.3186-0.5856-0.01231.41180.0019-0.15551.1508-0.11231.110154.678380.516194.0082
2019.0527-3.0256-13.2119-14.04317.0696-10.942-1.00022.8157-0.0023-0.28960.36840.226-0.0446-1.50990.63181.6961-0.04970.16271.3090.01721.234146.901898.6152104.3662
211.24520.426-0.78382.0649-1.91266.145-0.1195-0.34840.01880.42660.1290.2215-0.5389-0.9825-0.00961.0538-0.03890.33490.9527-0.10280.758538.830388.9761159.9496
222.86421.3649-3.90564.1152-4.814314.55970.194-0.6768-0.07360.6389-0.050.2279-0.82860.1139-0.14390.8552-0.04440.0820.5615-0.24050.696452.388104.3825147.4375
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
4X-RAY DIFFRACTION3BB17 - 23517 - 235
5X-RAY DIFFRACTION4BB236 - 439236 - 439
7X-RAY DIFFRACTION5CC3 - 1333 - 133
8X-RAY DIFFRACTION5CC173 - 264173 - 264
9X-RAY DIFFRACTION5CL - M381 - 3821
12X-RAY DIFFRACTION6CC134 - 172134 - 172
13X-RAY DIFFRACTION7CC265 - 379265 - 379
14X-RAY DIFFRACTION9DD173 - 241173 - 241
15X-RAY DIFFRACTION10DD1 - 1721 - 172
16X-RAY DIFFRACTION10DN242
18X-RAY DIFFRACTION11EE1 - 711 - 71
20X-RAY DIFFRACTION12EE72 - 19672 - 196
21X-RAY DIFFRACTION12EO2001
22X-RAY DIFFRACTION13FF6 - 1106 - 110
24X-RAY DIFFRACTION14GG1 - 751 - 75
26X-RAY DIFFRACTION15HH9 - 529 - 52
28X-RAY DIFFRACTION16HH53 - 7853 - 78
29X-RAY DIFFRACTION17HH49 - 7849 - 78
30X-RAY DIFFRACTION18II1 - 261 - 26
32X-RAY DIFFRACTION19II27 - 5127 - 51
33X-RAY DIFFRACTION20II52 - 5752 - 57
34X-RAY DIFFRACTION21JJ2 - 612 - 61
36X-RAY DIFFRACTION22KK1 - 531 - 53
Software
*PLUS
Version: 5 / Classification: refinement
Refinement
*PLUS
Highest resolution: 3.2 Å / Lowest resolution: 50 Å / Rfactor Rfree: 0.296 / Rfactor Rwork: 0.215
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONr_bond_d0.019
X-RAY DIFFRACTIONr_angle_d
X-RAY DIFFRACTIONr_angle_deg2.056
LS refinement shell
*PLUS
Rfactor Rfree: 0.38 / Rfactor Rwork: 0.29

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