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- PDB-1ntz: Crystal Structure of Mitochondrial Cytochrome bc1 Complex Bound w... -

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Basic information

Entry
Database: PDB / ID: 1ntz
TitleCrystal Structure of Mitochondrial Cytochrome bc1 Complex Bound with Ubiquinone
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 / UBIQUINONE
Function / homology
Function and homology information


Complex III assembly / subthalamus development / pons development / cerebellar Purkinje cell layer development / Respiratory electron transport / pyramidal neuron development / 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 / Respiratory electron transport / pyramidal neuron development / 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 / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / mitochondrial membrane / 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 / 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 ...FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / 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: 2.6 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 6, 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_seq_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_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)241,85717
Polymers239,19511
Non-polymers2,6626
Water3,729207
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)483,71434
Polymers478,39022
Non-polymers5,32412
Water39622
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_665-x+1,-y+1,z1
Buried area101140 Å2
ΔGint-680 kcal/mol
Surface area164220 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)153.828, 153.828, 596.671
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 , 4 types, 213 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-UQ2 / UBIQUINONE-2


Mass: 318.407 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H26O4
#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.: 207 / 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: 66.64 %
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: 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: 2.6→40 Å / Num. all: 109744 / Num. obs: 104476 / % possible obs: 95.2 % / Observed criterion σ(I): -1
Reflection shellResolution: 2.602→2.669 Å / % possible all: 96.7
Reflection
*PLUS
Highest resolution: 2.6 Å / Lowest resolution: 40 Å / Rmerge(I) obs: 0.061
Reflection shell
*PLUS
% possible obs: 96.7 % / Rmerge(I) obs: 0.52 / Mean I/σ(I) obs: 1.7

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Processing

Software
NameVersionClassification
REFMAC5refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: FOURIER SYNTHESIS / Resolution: 2.6→28.99 Å / Cor.coef. Fo:Fc: 0.922 / Cor.coef. Fo:Fc free: 0.903 / SU B: 14.031 / SU ML: 0.288 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.466 / ESU R Free: 0.305 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.28316 2075 2 %RANDOM
Rwork0.24655 ---
all0.2473 104476 --
obs0.2473 102423 100 %-
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: 39.826 Å2
Baniso -1Baniso -2Baniso -3
1-1.11 Å20 Å20 Å2
2--1.11 Å20 Å2
3----2.23 Å2
Refinement stepCycle: LAST / Resolution: 2.6→28.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16510 0 179 207 16896
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.02117515
X-RAY DIFFRACTIONr_angle_refined_deg1.8591.98323744
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.06632094
X-RAY DIFFRACTIONr_dihedral_angle_2_deg19.589152982
X-RAY DIFFRACTIONr_chiral_restr0.3210.22596
X-RAY DIFFRACTIONr_gen_planes_refined0.0090.0213063
X-RAY DIFFRACTIONr_nbd_refined0.2120.38654
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1890.51052
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.180.392
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2460.59
X-RAY DIFFRACTIONr_mcbond_it0.6670.410490
X-RAY DIFFRACTIONr_mcangle_it2.8683.80116876
X-RAY DIFFRACTIONr_scbond_it6.24937025
X-RAY DIFFRACTIONr_scangle_it8.4354.56866
LS refinement shellResolution: 2.602→2.669 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.35 148
Rwork0.326 7491
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)
10.93280.04270.27271.4216-0.60341.63660.11810.00270.0392-0.1603-0.01910.58920.0433-0.6322-0.0990.4126-0.13220.02570.48780.00760.647331.720887.280693.8114
20.1577-0.18370.09071.4441-0.11570.76640.0755-0.11120.15690.2046-0.06370.2478-0.1328-0.3095-0.01180.4247-0.16930.14630.2614-0.01270.399348.711193.3342115.5964
30.8556-0.5008-0.10292.11690.1781.78290.1410.03790.1846-0.1302-0.07010.0275-0.2831-0.1521-0.07090.3628-0.13420.00670.05050.01260.268268.8125104.347192.8
40.8021-0.2540.23521.89760.11851.50470.0540.076-0.0504-0.1822-0.05170.39720.0925-0.2008-0.00230.3954-0.099-0.06510.1350.01120.356257.277186.675674.5739
50.6635-0.16740.18540.19550.431.31310.0153-0.28380.03790.25440.03190.0006-0.1437-0.0419-0.04720.6956-0.34520.07540.38850.03480.35864.723468.345154.9219
62.3374-3.44230.6762.28070.7355-1.50870.2526-0.0496-0.52610.3696-0.32690.01140.29870.13380.07430.9981-0.2416-0.110.76410.14090.492981.026656.703173.2053
71.2585-0.33790.35820.97220.43592.39550.0707-0.3652-0.21860.32410.0863-0.10590.2310.0872-0.1570.6924-0.36520.03340.36950.16890.47664.706645.0116153.9036
8-1.5176-1.2891-0.5634-1.15271.119-0.35220.0089-0.28520.08250.9238-0.0990.0328-0.15060.00520.09020.9692-0.24990.05550.79770.00580.713851.907173.4801147.484
90.9194-0.5384-1.0393-0.1736-0.55211.9880.0604-0.33720.02190.26310.08260.11-0.0665-0.9411-0.1430.9147-0.40990.21480.52330.04110.497445.16371.5523159.835
100.61710.00880.74180.40230.34661.4828-0.0725-0.55-0.02020.47930.2103-0.1904-0.0102-0.1359-0.13781.1525-0.2020.16781.10440.05010.763354.273367.6113192.8381
111.222-0.08871.1050.7890.8733.88330.0197-0.386-0.10310.20950.01260.1856-0.172-0.6906-0.03230.5745-0.27410.24190.50730.04110.514443.201482.2098142.5747
12-1.6081-0.62260.6314-1.47921.14880.7858-0.165-0.22870.06030.27230.0748-0.2652-0.3953-0.31240.09021.9893-0.07390.08461.84-0.08161.658573.6708112.99189.4269
133.0901-0.8633-1.14381.12840.0951.31720.0811-0.2133-0.36610.1127-0.06230.22360.4087-0.1414-0.01880.561-0.34020.01620.23770.02120.348558.728446.9933123.1553
140.0785-0.1461-0.35221.7209-1.91742.6486-0.0087-0.3178-0.14540.46720.06570.104-0.1917-0.3071-0.0570.663-0.40610.09780.52680.0650.540747.858754.8318145.4734
152.6924-2.2467-1.73713.26362.58642.6996-0.2079-0.498-0.27380.50020.21470.0661-0.01910.0561-0.00691.2062-0.28630.16981.24750.20040.927339.138142.0437196.1252
1610.3522-7.4427-1.200514.47642.44111.3856-0.214-0.5853-0.29560.41720.38790.5357-0.0491-0.3085-0.17390.9901-0.31550.24531.11040.22290.665839.550249.8045188.2326
170000000000000000.5583000.558300.5583000
182.98542.67885.66340.7288-0.3478-4.8180.05940.31510.2390.0181-0.65370.30150.4382-1.61850.59430.8248-0.06760.1010.5401-0.13110.723260.372295.240888.8431
19-6.0354-0.58453.6026-11.1854-5.4883-4.05130.3294-0.54290.3852-0.2073-0.43740.65270.2416-0.76460.1081.4093-0.0445-0.11981.33-0.19941.409354.505780.667394.4769
2036.525-28.9367-34.080925.856125.07285.55870.4542.24310.5742-0.00830.280.3363-0.0314-1.6448-0.7341.1479-0.1405-0.0581.15590.0280.847247.06398.9584104.8445
210.9590.27510.27312.1495-1.04024.9268-0.0843-0.3170.00710.44710.17520.1383-0.418-1.2075-0.09090.8025-0.08870.33990.8083-0.13230.710238.869589.3774160.6415
220.18850.777-2.02393.8268-4.276911.64120.2109-0.48970.25290.4249-0.05210.1686-0.5719-0.1617-0.15880.749-0.14940.06410.603-0.23670.67952.5392104.723148.0208
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 DIFFRACTION10DP242
18X-RAY DIFFRACTION11EE1 - 711 - 71
20X-RAY DIFFRACTION12EE72 - 19672 - 196
21X-RAY DIFFRACTION12EQ2001
22X-RAY DIFFRACTION13FF6 - 1106 - 110
24X-RAY DIFFRACTION14GG1 - 751 - 75
26X-RAY DIFFRACTION15HH9 - 529 - 52
27X-RAY DIFFRACTION16HH53 - 7853 - 78
28X-RAY DIFFRACTION17HH49 - 7849 - 78
29X-RAY DIFFRACTION18II1 - 261 - 26
31X-RAY DIFFRACTION19II27 - 5127 - 51
32X-RAY DIFFRACTION20II52 - 5752 - 57
33X-RAY DIFFRACTION21JJ2 - 612 - 61
35X-RAY DIFFRACTION22KK1 - 531 - 53
Software
*PLUS
Version: 5 / Classification: refinement
Refinement
*PLUS
Lowest resolution: 40 Å / Num. reflection Rfree: 2122 / Rfactor Rfree: 0.285 / Rfactor Rwork: 0.243
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONr_bond_d0.021
X-RAY DIFFRACTIONr_angle_d
X-RAY DIFFRACTIONr_angle_deg1.732
LS refinement shell
*PLUS
Rfactor Rwork: 0.31

+
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