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- PDB-3l70: Cytochrome BC1 complex from chicken with trifloxystrobin bound -

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Entry
Database: PDB / ID: 3l70
TitleCytochrome BC1 complex from chicken with trifloxystrobin bound
Components
  • (Cytochrome b-c1 complex subunit Rieske, ...) x 2
  • (Mitochondrial ubiquinol-cytochrome c reductase ...) x 4
  • (Mitochondrial ubiquinol-cytochrome-c reductase complex core protein ...) x 2
  • Cytochrome b
  • Mitochondrial cytochrome c1, heme protein
KeywordsOXIDOREDUCTASE / CYTOCHROME BC1 / MEMBRANE PROTEIN / HEME PROTEIN / RIESKE IRON SULFUR PROTEIN / CYTOCHROME B / CYTOCHROME C1 / COMPLEX III / MITOCHONDRIAL PROCESSING PROTEIN / UBIQUINONE / TRIFLOXYSTROBIN OXIDOREDUCTASE / REDOX ENZYME RESPIRATORY CHAIN / ELECTRON TRANSPORT / HEME / INNER MEMBRANE / MEMBRANE / STROBILURINS BINDING / MITOCHONDRION / TRANSMEMBRANE / STIGMATELLIN / IRON / MITOCHONDRIAL INNER MEMBRANE / RESPIRATORY CHAIN / IRON-SULFUR / TRANSIT PEPTIDE / Metal-binding / Mitochondrion inner membrane / Transport / Disulfide bond
Function / homology
Function and homology information


Respiratory electron transport / Complex III assembly / quinol-cytochrome-c reductase / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / response to oxidative stress ...Respiratory electron transport / Complex III assembly / quinol-cytochrome-c reductase / respiratory chain complex III / quinol-cytochrome-c reductase / quinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / response to oxidative stress / electron transfer activity / mitochondrial inner membrane / oxidoreductase activity / heme binding / mitochondrion / metal ion binding / membrane / cytoplasm
Similarity search - Function
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 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 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 / Cytochrome b-c1 complex subunit 8 / UcrQ family / Cytochrome bc1 complex subunit Rieske, transmembrane domain superfamily / 3-layer Sandwich / 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 / Ubiquinol-cytochrome C reductase hinge domain / Ubiquinol-cytochrome C reductase hinge domain superfamily / Ubiquinol-cytochrome C reductase hinge protein / Cytochrome b-c1 complex subunit 9 / Cytochrome b-c1 complex subunit 9 superfamily / Ubiquinol-cytochrome C reductase, UQCRX/QCR9 like / 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 / 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
CARDIOLIPIN / FE2/S2 (INORGANIC) CLUSTER / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-JZV / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer / Cytochrome c / Complex III subunit 9 / Cytochrome b-c1 complex subunit 6 ...CARDIOLIPIN / FE2/S2 (INORGANIC) CLUSTER / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-JZV / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer / Cytochrome c / Complex III subunit 9 / Cytochrome b-c1 complex subunit 6 / Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2 / Cytochrome b-c1 complex subunit 7 / Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i / Cytochrome b-c1 complex subunit 8 / Cytochrome b / Cytochrome b-c1 complex subunit Rieske, mitochondrial
Similarity search - Component
Biological speciesGallus gallus (chicken)
MethodX-RAY DIFFRACTION / SYNCHROTRON / RIGID BODY REFINEMENT / Resolution: 2.75 Å
AuthorsHuang, L. / Berry, E.A.
CitationJournal: To be Published
Title: Famoxadone and related inhibitors bind like methoxy acrylate inhibitors in the Qo site of the BC1 compl and fix the rieske iron-sulfur protein in a positio close to but distinct from that seen ...Title: Famoxadone and related inhibitors bind like methoxy acrylate inhibitors in the Qo site of the BC1 compl and fix the rieske iron-sulfur protein in a positio close to but distinct from that seen with stigmatellin and other "distal" Qo inhibitors.
Authors: Huang, L. / Berry, E.A.
History
DepositionDec 27, 2009Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 2, 2010Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Oct 29, 2014Group: Non-polymer description
Revision 1.3Nov 1, 2017Group: Refinement description / Category: software / Item: _software.name
Revision 1.4Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_site / struct_site_gen
Item: _chem_comp.mon_nstd_flag / _chem_comp.name ..._chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.0Sep 6, 2023Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Non-polymer description / Refinement description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / chem_comp_atom / chem_comp_bond / database_2 / entity / pdbx_entity_nonpoly / pdbx_initial_refinement_model / pdbx_unobs_or_zero_occ_atoms
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_atom_id / _atom_site.label_atom_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _entity.formula_weight / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _pdbx_unobs_or_zero_occ_atoms.auth_atom_id / _pdbx_unobs_or_zero_occ_atoms.label_atom_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i
B: Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2
C: Cytochrome b
D: Mitochondrial cytochrome c1, heme protein
E: Cytochrome b-c1 complex subunit Rieske, mitochondrial
F: Mitochondrial ubiquinol-cytochrome c reductase 14 kda protein
G: Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c
H: Mitochondrial ubiquinol-cytochrome c reductase 11 kda protein, complex iii subunit viii
I: Cytochrome b-c1 complex subunit Rieske, mitochondrial
J: Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein
N: Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i
O: Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2
P: Cytochrome b
Q: Mitochondrial cytochrome c1, heme protein
R: Cytochrome b-c1 complex subunit Rieske, mitochondrial
S: Mitochondrial ubiquinol-cytochrome c reductase 14 kda protein
T: Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c
U: Mitochondrial ubiquinol-cytochrome c reductase 11 kda protein, complex iii subunit viii
V: Cytochrome b-c1 complex subunit Rieske, mitochondrial
W: Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)480,62949
Polymers462,06520
Non-polymers18,56429
Water34219
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area102060 Å2
ΔGint-695 kcal/mol
Surface area154440 Å2
MethodPISA
Unit cell
Length a, b, c (Å)169.614, 181.993, 240.540
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
DetailsThe deposited coordinates (20 chains plus hetero groups) make up the asymmetric unit which is the biological assembly. One other subunit of the biological assembly (Subunit 11) is lost during purification or crystallization and is not present in the deposited structure.

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Components

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Mitochondrial ubiquinol-cytochrome-c reductase complex core protein ... , 2 types, 4 molecules ANBO

#1: Protein Mitochondrial ubiquinol-cytochrome-c reductase complex core protein i


Mass: 49503.840 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: D0VX31, quinol-cytochrome-c reductase
#2: Protein Mitochondrial ubiquinol-cytochrome-c reductase complex core protein 2


Mass: 46683.809 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: D0VX29, quinol-cytochrome-c reductase

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Protein , 2 types, 4 molecules CPDQ

#3: Protein Cytochrome b / Ubiquinol-cytochrome-c reductase complex cytochrome b subunit / Cytochrome b-c1 complex subunit 3 / ...Ubiquinol-cytochrome-c reductase complex cytochrome b subunit / Cytochrome b-c1 complex subunit 3 / Complex III subunit 3 / Complex III subunit III


Mass: 42622.977 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: P18946, quinol-cytochrome-c reductase
#4: Protein Mitochondrial cytochrome c1, heme protein


Mass: 26973.744 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: D0VX26, quinol-cytochrome-c reductase

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Cytochrome b-c1 complex subunit Rieske, ... , 2 types, 4 molecules ERIV

#5: Protein Cytochrome b-c1 complex subunit Rieske, mitochondrial / Ubiquinol-cytochrome c reductase iron-sulfur subunit / Rieske iron-sulfur protein / RISP / Complex ...Ubiquinol-cytochrome c reductase iron-sulfur subunit / Rieske iron-sulfur protein / RISP / Complex III subunit 5


Mass: 21506.188 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 77-272 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: Q5ZLR5, quinol-cytochrome-c reductase
#9: Protein/peptide Cytochrome b-c1 complex subunit Rieske, mitochondrial / Ubiquinol-cytochrome c reductase iron-sulfur subunit / Rieske iron-sulfur protein / RISP / Complex ...Ubiquinol-cytochrome c reductase iron-sulfur subunit / Rieske iron-sulfur protein / RISP / Complex III subunit 5


Mass: 4785.649 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 45-76 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: Q5ZLR5, quinol-cytochrome-c reductase

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Mitochondrial ubiquinol-cytochrome c reductase ... , 4 types, 8 molecules FSGTHUJW

#6: Protein Mitochondrial ubiquinol-cytochrome c reductase 14 kda protein


Mass: 13394.397 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: D0VX30, quinol-cytochrome-c reductase
#7: Protein Mitochondrial ubiquinol-cytochrome c reductase ubiquinone-binding protein qp-c


Mass: 9498.735 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: D0VX32, quinol-cytochrome-c reductase
#8: Protein Mitochondrial ubiquinol-cytochrome c reductase 11 kda protein, complex iii subunit viii


Mass: 9057.119 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: D0VX28, quinol-cytochrome-c reductase
#10: Protein Mitochondrial ubiquinol-cytochrome c reductase 7.2 kda protein


Mass: 7005.963 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Gallus gallus (chicken) / References: UniProt: D0VX27, quinol-cytochrome-c reductase

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Sugars , 1 types, 5 molecules

#18: Sugar
ChemComp-BOG / octyl beta-D-glucopyranoside / Beta-Octylglucoside / octyl beta-D-glucoside / octyl D-glucoside / octyl glucoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 5
Source method: isolated from a genetically manipulated source
Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 9 types, 43 molecules

#11: Chemical
ChemComp-PEE / 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine / DOPE


Mass: 744.034 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C41H78NO8P / Comment: DOPE, phospholipid*YM
#12: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#13: Chemical ChemComp-JZV / methyl (2E)-(methoxyimino)(2-{[({(1Z)-1-[3-(trifluoromethyl)phenyl]ethylidene}amino)oxy]methyl}phenyl)ethanoate


Mass: 408.371 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C20H19F3N2O4
#14: Chemical ChemComp-UQ / Coenzyme Q10, (2Z,6E,10Z,14E,18E,22E,26Z)-isomer


Mass: 863.343 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C59H90O4
#15: Chemical
ChemComp-CDL / CARDIOLIPIN / DIPHOSPHATIDYL GLYCEROL / BIS-(1,2-DIACYL-SN-GLYCERO-3-PHOSPHO)-1',3'-SN-GLYCEROL


Mass: 1464.043 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C81H156O17P2 / Comment: phospholipid*YM
#16: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H8O3
#17: Chemical ChemComp-HEC / HEME C


Mass: 618.503 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#19: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe2S2
#20: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 19 / Source method: isolated from a natural source / Formula: H2O

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Details

Sequence detailsTHE COMPLETE SEQUENCE OF CHAIN I AND V IS ...THE COMPLETE SEQUENCE OF CHAIN I AND V IS MLSVAARSGPFAPYLSAAAHAVPGPLKALAPAALRAEKVVLDLKRPLLCRESMSGRSARRDLVAGISLNAPASVRY, UNP residues 1-76. THE N-TERMINUS IS DISORDERED.

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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: 4.02 Å3/Da / Density % sol: 69.38 %
Description: REMARK: THE DATA WAS COLLECTED IN TWO PASSES- HIGH RES PASS WAS INTEGRATED 60 TO 2.8 A, LOW RES 60 TO 3.26 A, AND BOTH PASSES WERE SCALED SIMULTANEOUSLY IN SCALEPACK. DISTANCE 400 MM FOR ...Description: REMARK: THE DATA WAS COLLECTED IN TWO PASSES- HIGH RES PASS WAS INTEGRATED 60 TO 2.8 A, LOW RES 60 TO 3.26 A, AND BOTH PASSES WERE SCALED SIMULTANEOUSLY IN SCALEPACK. DISTANCE 400 MM FOR HI RES, 700 MM FOR LOW RES PASS. RESOLUTION USED IN REFINEMENT WAS 25 TO 2.75 A.
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 6.77
Details: FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH ...Details: FINAL CONCENTRATIONS BEFORE DIFFUSION: 50 MM CACODYLATE, 9.4 MM TRISHCL, 10 MM MGCL2, 50 G/L GLYCEROL, 30 G/L PEG 3350DA, 0.23 MM EDTA, 0.47 G/L UNDECYL MALTOSIDE, 31 MM OCTYL GLUCOSIDE, PH 6.77, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 28, 2006
RadiationMonochromator: DOUBLE CRYSTAL SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
IDWavelength (Å)Relative weight
111
211
ReflectionResolution: 2.69→99 Å / Num. all: 206245 / Num. obs: 206245 / % possible obs: 99 % / Observed criterion σ(I): -3 / Redundancy: 8.1 % / Biso Wilson estimate: 70.9 Å2 / Rsym value: 0.114 / Net I/σ(I): 23.6
Reflection shellResolution: 2.69→2.74 Å / Redundancy: 6.3 % / Mean I/σ(I) obs: 1.136 / Num. unique all: 8284 / % possible all: 80.3

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Processing

Software
NameClassification
Blu-Icedata collection
CNSrefinement
DENZOdata reduction
SCALEPACKdata scaling
CNSphasing
RefinementMethod to determine structure: RIGID BODY REFINEMENT
Starting model: PDB ENTRY 3H1H

3h1h


Resolution: 2.75→24.99 Å / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.297 9570 -RANDOM
Rwork0.267 ---
all0.268 191247 --
obs0.268 191247 99.3 %-
Displacement parametersBiso mean: 68.8 Å2
Baniso -1Baniso -2Baniso -3
1-31.49 Å20 Å20 Å2
2---16.64 Å20 Å2
3----14.85 Å2
Refine analyze
FreeObs
Luzzati coordinate error0.55 Å0.47 Å
Luzzati d res low-5 Å
Luzzati sigma a0.68 Å0.63 Å
Refinement stepCycle: LAST / Resolution: 2.75→24.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms31794 0 840 19 32653
Refine LS restraints
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONc_bond_d0.008
X-RAY DIFFRACTIONc_angle_deg1.4
X-RAY DIFFRACTIONc_dihedral_angle_d21.3
X-RAY DIFFRACTIONc_improper_angle_d0.89
X-RAY DIFFRACTIONc_mcbond_it1.26
X-RAY DIFFRACTIONc_mcangle_it2.19
X-RAY DIFFRACTIONc_scbond_it1.79
X-RAY DIFFRACTIONc_scangle_it2.81
LS refinement shellResolution: 2.75→2.89 Å / Rfactor Rfree error: 0.012
RfactorNum. reflection% reflection
Rfree0.44 1350 -
Rwork0.408 --
obs-27083 99.4 %

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