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- PDB-1ntm: Crystal Structure of Mitochondrial Cytochrome bc1 Complex at 2.4 ... -

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Basic information

Entry
Database: PDB / ID: 1ntm
TitleCrystal Structure of Mitochondrial Cytochrome bc1 Complex at 2.4 Angstrom
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
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 / respiratory electron transport chain / hippocampus development / 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 / Cytochrome b-c1 complex subunit 9 / 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 / PROTOPORPHYRIN IX CONTAINING FE / 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 ...FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / 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: 2.4 Å
AuthorsGao, X. / Wen, X. / Esser, L. / Quinn, B. / Yu, L. / Yu, C. / 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 1.3Oct 30, 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_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)241,22015
Polymers239,19511
Non-polymers2,0254
Water8,179454
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)482,44130
Polymers478,39022
Non-polymers4,0518
Water39622
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_665-x+1,-y+1,z1
Buried area95850 Å2
ΔGint-669 kcal/mol
Surface area164320 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)154.325, 154.325, 593.161
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 (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 / 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 (domestic 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 (domestic 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 (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: 6568.655 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 , 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 (domestic 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 (domestic 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 (domestic 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 (domestic cattle) / References: UniProt: P13272, quinol-cytochrome-c reductase

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Non-polymers , 3 types, 458 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-FES / FE2/S2 (INORGANIC) CLUSTER


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


Mass: 18.015 Da / Num. of mol.: 454 / 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: 3.69 Å3/Da / Density % sol: 66.66 %
Crystal growTemperature: 277 K / Method: vapor diffusion / pH: 7.2
Details: PEG 4000, ammonium acetate, potassium chloride, glyerol, 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: NSLS / Beamline: X9B / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Details: Si(111)
RadiationMonochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→50 Å / Num. all: 139726 / Num. obs: 119745 / % possible obs: 85.7 % / Observed criterion σ(I): -1
Reflection shellResolution: 2.4→2.461 Å / % possible all: 77.8
Reflection
*PLUS
Lowest resolution: 50 Å / Rmerge(I) obs: 0.058
Reflection shell
*PLUS
% possible obs: 77.8 % / Rmerge(I) obs: 0.392 / Mean I/σ(I) obs: 1.1

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Processing

Software
NameVersionClassification
REFMAC5refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.4→20 Å / Cor.coef. Fo:Fc: 0.935 / Cor.coef. Fo:Fc free: 0.901 / SU B: 14.347 / SU ML: 0.291 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.361 / ESU R Free: 0.279 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.285 3584 3 %RANDOM
Rwork0.23662 ---
all0.238 119745 --
obs0.23808 115874 85.82 %-
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: 25.561 Å2
Baniso -1Baniso -2Baniso -3
1-1.02 Å20 Å20 Å2
2--1.02 Å20 Å2
3----2.04 Å2
Refinement stepCycle: LAST / Resolution: 2.4→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16462 0 133 454 17049
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0150.02117006
X-RAY DIFFRACTIONr_angle_refined_deg1.8941.9823054
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.42632032
X-RAY DIFFRACTIONr_dihedral_angle_2_deg20.535152874
X-RAY DIFFRACTIONr_chiral_restr0.2810.22519
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0212679
X-RAY DIFFRACTIONr_nbd_refined0.2330.38811
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2080.51218
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2180.399
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.4540.512
X-RAY DIFFRACTIONr_mcbond_it0.6570.410175
X-RAY DIFFRACTIONr_mcangle_it2.6793.80116372
X-RAY DIFFRACTIONr_scbond_it6.24436831
X-RAY DIFFRACTIONr_scangle_it8.2954.56680
LS refinement shellResolution: 2.4→2.461 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.495 236
Rwork0.48 7646
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)
10.3754-0.03130.32941.0821-0.44391.83250.08770.03050.0975-0.24910.01360.49460.0804-0.6462-0.10130.4016-0.09740.01480.49950.01250.619332.75187.811694.0003
20.0898-0.0540.05711.2813-0.19620.71810.0614-0.11140.14020.1927-0.02740.2055-0.1323-0.3006-0.0340.3889-0.11860.1210.2446-0.01710.379349.09393.7868115.2713
30.9011-0.2325-0.21921.5930.37211.82460.08170.03860.1967-0.1255-0.0310.0571-0.2626-0.1426-0.05070.3255-0.08780.00790.02510.01730.272269.1512104.509292.1519
40.9948-0.73320.08662.9813-0.27091.39320.0510.0009-0.0728-0.21250.06610.40090.1252-0.2387-0.11710.3743-0.0739-0.04520.12430.01530.31457.294586.731273.7077
50.5888-0.0110.23090.46250.6452.20980.0358-0.25560.08750.3083-0.04490.0814-0.152-0.27570.0090.6331-0.28070.07210.40930.03160.379162.758269.6371153.0406
60000000000000000.4956000.495600.4956000
73.7389-2.5267-1.71722.19351.034-0.76460.0007-0.0698-0.50760.5904-0.13520.11060.49090.03620.13451.1095-0.2692-0.13140.75450.14630.482481.18857.0395172.6184
81.7726-0.06430.19320.9358-0.00492.69360.0902-0.4045-0.20690.3591-0.0054-0.12670.16940.2053-0.08480.6473-0.28110.02640.3380.13540.448964.785345.2419153.3504
90.5999-0.2443-0.41580.30620.05742.76740.0015-0.3277-0.03110.32540.02330.1035-0.0815-0.4363-0.02480.7315-0.29010.16980.54680.0350.46545.422571.7988159.4618
100.3942-0.14610.33820.61380.2581.516-0.0225-0.568-0.09680.69410.13620.01580.0823-0.0841-0.11371.2393-0.26590.19311.1570.08860.649154.433767.762192.2309
111.5149-0.06971.51740.60750.54094.3795-0.0821-0.35320.00370.2094-0.02930.1956-0.2863-0.69670.11140.5126-0.22390.21850.45290.04780.498243.453482.4828141.8554
120.4748-0.86661.835-2.18521.0642-0.434-0.2054-0.70370.26350.66820.0057-0.5014-0.7201-0.53230.19972.4871-0.20670.042.0781-0.20981.498674.0151113.1859188.7679
133.1642-1.044-1.48190.8190.34941.729-0.0476-0.17-0.3840.1281-0.010.1480.3528-0.21960.05760.5134-0.26510.00590.20630.03080.353258.988547.3452122.5092
140.23690.2688-0.65891.921-1.59772.2650.059-0.3421-0.14260.4794-0.09260.1399-0.1389-0.07280.03360.557-0.31540.05650.5020.05490.424648.111455.1769144.7309
154.9659-3.43-3.56714.59721.86053.8783-0.3482-0.4833-0.6131.07540.14650.5117-0.0556-0.17470.20171.3767-0.49080.15781.31110.27210.891239.551841.0413194.2377
1613.5717-11.87360.355616.04432.285-0.81090.0971-0.15520.00050.47320.12820.0334-0.0892-0.0817-0.22531.1538-0.30080.31451.26280.26030.740940.018649.9579187.7912
170000000000000000.4956000.495600.4956000
180000000000000000.4956000.495600.4956000
190000000000000000.4956000.495600.4956000
200000000000000000.4956000.495600.4956000
211.86170.0579-0.60863.7168-0.65124.5041-0.0099-0.44870.04930.79840.09460.5395-0.6477-1.2426-0.08470.7129-0.09260.28820.8386-0.07890.667438.643689.6712159.8124
222.28860.1296-3.75013.0775-3.781213.20250.2623-0.59940.1330.4357-0.00190.1849-0.66560.1431-0.26040.7391-0.13440.02510.483-0.19770.558253.2896105.0525146.862
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1 - 2311 - 231
3X-RAY DIFFRACTION2AA232 - 446232 - 446
4X-RAY DIFFRACTION3BB17 - 23517 - 235
6X-RAY DIFFRACTION4BB236 - 439236 - 439
7X-RAY DIFFRACTION5CC2 - 1332 - 133
8X-RAY DIFFRACTION5CC173 - 264173 - 264
9X-RAY DIFFRACTION5CL - M381 - 3821
13X-RAY DIFFRACTION7CC134 - 172134 - 172
14X-RAY DIFFRACTION8CC265 - 379265 - 379
15X-RAY DIFFRACTION9DD173 - 241173 - 241
16X-RAY DIFFRACTION10DD1 - 1721 - 172
17X-RAY DIFFRACTION10DN2421
19X-RAY DIFFRACTION11EE1 - 711 - 71
21X-RAY DIFFRACTION12EE - O72 - 19772 - 1
22X-RAY DIFFRACTION13FF6 - 1106 - 110
24X-RAY DIFFRACTION14GG1 - 751 - 75
26X-RAY DIFFRACTION15HH12 - 5212 - 52
27X-RAY DIFFRACTION16HH53 - 7853 - 78
29X-RAY DIFFRACTION17HH49 - 7849 - 78
30X-RAY DIFFRACTION18II2 - 262 - 26
31X-RAY DIFFRACTION19II27 - 5127 - 51
32X-RAY DIFFRACTION20II52 - 5752 - 57
33X-RAY DIFFRACTION21JJ1 - 601 - 60
35X-RAY DIFFRACTION22KK1 - 511 - 51
Software
*PLUS
Version: 5 / Classification: refinement
Refinement
*PLUS
Highest resolution: 2.4 Å / Lowest resolution: 50 Å / Rfactor Rfree: 0.282 / Rfactor Rwork: 0.232
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONr_bond_d0.015
X-RAY DIFFRACTIONr_angle_d
X-RAY DIFFRACTIONr_angle_deg1.929
LS refinement shell
*PLUS
Rfactor Rfree: 0.49

+
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