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- PDB-1l0l: structure of bovine mitochondrial cytochrome bc1 complex with a b... -

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Basic information

Entry
Database: PDB / ID: 1l0l
Titlestructure of bovine mitochondrial cytochrome bc1 complex with a bound fungicide famoxadone
Components
  • (UBIQUINOL-CYTOCHROME C REDUCTASE ...) x 9
  • Cytochrome B
  • Cytochrome c1, heme protein
KeywordsOXIDOREDUCTASE / cytochrome bc1 / membrane protein / heme protein / iron sulfur protein / cytochrome b / cytochrome c1 / mitochondrial processing protease / mpp
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 / FAMOXADONE / 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 ...FE2/S2 (INORGANIC) CLUSTER / FAMOXADONE / 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 (cattle)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.35 Å
AuthorsGao, X. / Wen, X. / Yu, C.A. / Esser, L. / Tsao, S. / Quinn, B. / Zhang, L. / Yu, L. / Xia, D.
CitationJournal: Biochemistry / Year: 2003
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.A. / Esser, L. / Tsao, S. / Quinn, B. / Zhang, L. / Yu, L. / Xia, D.
History
DepositionFeb 11, 2002Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 8, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 28, 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_conn_type / struct_ref_seq_dif / 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.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.ptnr2_label_seq_id / _struct_conn_type.id / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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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
B: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2
C: Cytochrome B
D: Cytochrome c1, heme protein
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 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)243,73416
Polymers241,33411
Non-polymers2,4005
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I
B: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2
C: Cytochrome B
D: Cytochrome c1, heme protein
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 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
B: UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN 2
C: Cytochrome B
D: Cytochrome c1, heme protein
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 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)487,46832
Polymers482,66922
Non-polymers4,79910
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_665-x+1,-y+1,z1
Buried area98540 Å2
ΔGint-647 kcal/mol
Surface area168590 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)154.094, 154.094, 591.839
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 ... , 9 types, 9 molecules ABEFGHIJK

#1: Protein UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I


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 / 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
#5: Protein UBIQUINOL-CYTOCHROME C REDUCTASE IRON-SULFUR SUBUNIT / 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
#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
#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
#9: Protein UBIQUINOL-CYTOCHROME C REDUCTASE 8 KDA PROTEIN


Mass: 7964.259 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P13272, 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 , 2 types, 2 molecules CD

#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, heme protein


Mass: 27323.277 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (cattle) / References: UniProt: P00125

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Non-polymers , 3 types, 5 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-FMX / FAMOXADONE / 5-METHYL-5-(4-PHENOXYPHENYL)-3-(PHENYLAMINO)-2,4-OXAZOLIDINEDIONE


Mass: 374.389 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C22H18N2O4
#14: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe2S2

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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: 3.64 Å3/Da / Density % sol: 66.19 %
Crystal grow
*PLUS
pH: 7.2 / Method: vapor diffusion, sitting 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-mrthylglucamide1reservoir

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 5ID-B / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 4 / Detector: CCD
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.4→40 Å / Num. obs: 123427
Reflection
*PLUS
Lowest resolution: 80 Å / % possible obs: 95.2 % / Rmerge(I) obs: 0.057
Reflection shell
*PLUS
% possible obs: 96.7 % / Rmerge(I) obs: 0.339

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Processing

Software
NameVersionClassification
DENZOdata reduction
SCALEPACKdata scaling
CCP4model building
REFMAC5refinement
CCP4phasing
RefinementResolution: 2.35→40 Å / Cor.coef. Fo:Fc: 0.925 / Cor.coef. Fo:Fc free: 0.893 / SU B: 11.764 / SU ML: 0.263 / Cross valid method: THROUGHOUT / ESU R: 0.311 / ESU R Free: 0.26
RfactorNum. reflection% reflectionSelection details
Rfree0.30596 2842 2 %RANDOM
Rwork0.2588 ---
obs0.25975 138934 96 %-
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: 27.285 Å2
Baniso -1Baniso -2Baniso -3
1-1.99 Å20 Å20 Å2
2--1.99 Å20 Å2
3----3.99 Å2
Refinement stepCycle: LAST / Resolution: 2.35→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16634 0 161 0 16795
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.020.02117595
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.9541.98523854
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg3.98132108
X-RAY DIFFRACTIONr_dihedral_angle_3_deg21.5152986
X-RAY DIFFRACTIONr_chiral_restr0.2960.22605
X-RAY DIFFRACTIONr_gen_planes_refined0.0070.0213127
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.2730.39333
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.2130.51104
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.2220.3103
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.2130.514
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_mcbond_it1.2111.510559
X-RAY DIFFRACTIONr_mcangle_it2.088216982
X-RAY DIFFRACTIONr_scbond_it3.64937036
X-RAY DIFFRACTIONr_scangle_it5.3914.56870
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.35→2.411 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.373 216
Rwork0.377 10241
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)
10.5795-0.16290.35310.9183-0.35041.56820.0938-0.04240.06050.0087-0.02790.3595-0.0281-0.5386-0.06580.3904-0.13180.09260.3309-0.00430.502840.017690.3293103.7205
20.5808-0.04840.32110.83180.14121.50270.06610.0290.0678-0.0859-0.05650.1869-0.0621-0.1405-0.00960.3845-0.06870.00130.01320.01820.352763.363296.067783.4244
30.72160.17110.17690.57250.26171.1730.0898-0.2882-0.07310.2903-0.0652-0.0489-0.0049-0.0365-0.02470.6399-0.35240.03740.36850.05880.38766.452760.3967155.9532
40000000000000000.5101000.510100.5101000
50000000000000000.5101000.510100.5101000
60000000000000000.5101000.510100.5101000
70000000000000000.5101000.510100.5101000
80000000000000000.5101000.510100.5101000
90000000000000000.5101000.510100.5101000
100000000000000000.5101000.510100.5101000
110000000000000000.5101000.510100.5101000
120.7272-0.287-0.62070.39120.9084.86860.1386-0.22640.06470.299-0.19230.23710.1019-0.58770.05370.6666-0.37440.17360.45010.01330.45245.448972.994145.9721
131.58830.4170.43753.02540.51430.83340.017-0.4916-0.13980.64710.01590.06210.1334-0.2043-0.03291.228-0.3630.24591.09020.06720.473353.419467.8326192.8092
145.83313.51113.810417.040316.56661.3232-1.22060.9674-0.76290.98890.33460.0165-0.391-0.10980.8860.5757-0.090.11170.53160.11640.453853.042881.3228160.5833
151.690.32731.37310.66230.78834.49650.1193-0.4767-0.02230.1984-0.11490.1771-0.1157-0.9641-0.00440.5702-0.22320.1980.43260.0030.516943.324782.3367142.1197
164.3692-3.53761.94434.7077-2.920911.8915-0.6521-1.98350.25031.74610.84880.0498-1.2252-1.5255-0.19671.8791-0.17440.10861.4811-0.31740.778273.2488112.9638189.4209
174.2757-0.6915-1.86790.87810.17191.9067-0.0443-0.0431-0.51280.1173-0.06620.22070.464-0.20710.11050.5888-0.30590.03120.18960.01340.411558.907246.2807122.1502
180.38610.0028-0.23662.1887-1.45252.01240.0718-0.4009-0.15720.54180.02470.2361-0.0451-0.2828-0.09660.6461-0.37540.09550.52950.06440.491848.117954.3349145.8547
194.5831-1.7761-1.98763.06470.91458.4450.1235-0.27350.4613-0.006-0.00490.29410.0495-1.0195-0.11871.0466-0.47880.17221.2180.20761.108535.059847.4602198.2426
205.23-11.65290.312126.5-6.25815.1154-0.3225-0.77040.56680.29380.0438-0.43130.8664-0.38780.27870.9919-0.66690.26991.06460.21620.770341.803347.4154189.4506
213.10840.0065-0.82257.93750.0799-4.4721-0.24110.09660.2565-0.5827-0.65640.30840.7472-1.34290.89750.7602-0.11980.09060.4209-0.03640.680760.707595.006689.1193
2210.94173.474715.600311.6391-6.265531.11740.705-0.63270.36560.1401-0.60541.14511.7115-0.89-0.09950.79480.01210.0430.9565-0.13290.917754.548480.714794.2375
23266.9657-0.401-82.30053.631150.084380.80780.68934.19560.749-1.6811-0.7404-0.1420.6327-1.89680.05110.7905-0.07320.01410.72570.12450.759947.066498.9166104.6526
240.8988-0.2348-0.70973.663-1.86745.2466-0.0235-0.38530.0090.78930.10140.4352-0.8165-0.9821-0.07780.8571-0.17250.37640.8437-0.14360.612438.760589.4518160.1477
251.98852.0439-4.07274.9823-6.993316.27330.2549-0.33870.1840.58350.01030.2561-1.1105-0.4745-0.26520.8014-0.140.08980.5291-0.21610.577652.5647104.7473147.8209
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
1X-RAY DIFFRACTION1AA1 - 2281 - 228
2X-RAY DIFFRACTION1AA229 - 446229 - 446
3X-RAY DIFFRACTION2BB17 - 23517 - 235
4X-RAY DIFFRACTION2BB236 - 439236 - 439
5X-RAY DIFFRACTION3CC3 - 3793 - 379
6X-RAY DIFFRACTION3CL - N609 - 611
15X-RAY DIFFRACTION12DD197 - 240197 - 240
16X-RAY DIFFRACTION13DD1 - 1961 - 196
17X-RAY DIFFRACTION13DO242
19X-RAY DIFFRACTION15EE1 - 711 - 71
20X-RAY DIFFRACTION16EE72 - 19672 - 196
21X-RAY DIFFRACTION17FF2 - 1102 - 110
22X-RAY DIFFRACTION18GG1 - 771 - 77
23X-RAY DIFFRACTION19HH1 - 481 - 48
24X-RAY DIFFRACTION20HH49 - 7849 - 78
25X-RAY DIFFRACTION21II2 - 262 - 26
26X-RAY DIFFRACTION22II27 - 5127 - 51
27X-RAY DIFFRACTION23II52 - 5752 - 57
28X-RAY DIFFRACTION24JJ2 - 612 - 61
29X-RAY DIFFRACTION25KK1 - 531 - 53
Refinement
*PLUS
Highest resolution: 2.4 Å / Lowest resolution: 80 Å / Num. reflection obs: 123427 / Num. reflection Rfree: 2461 / Rfactor Rfree: 0.306 / Rfactor Rwork: 0.259
Solvent computation
*PLUS
Displacement parameters
*PLUS
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONr_bond_d0.03
X-RAY DIFFRACTIONr_angle_d
X-RAY DIFFRACTIONr_angle_deg2.1

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