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- PDB-2fyu: Crystal structure of bovine heart mitochondrial bc1 with jg144 in... -

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Basic information

Entry
Database: PDB / ID: 2fyu
TitleCrystal structure of bovine heart mitochondrial bc1 with jg144 inhibitor
Components
  • (Ubiquinol-cytochrome c reductase complex ...) x 4
  • (Ubiquinol-cytochrome c reductase iron-sulfur subunit, ...) x 2
  • (Ubiquinol-cytochrome-c reductase complex core protein ...) x 2
  • Cytochrome b
  • Cytochrome c1, heme protein, mitochondrial
  • Hypothetical protein LOC616871
KeywordsOXIDOREDUCTASE / Transmembrane helices / 11 protein complex
Function / homology
Function and homology information


Complex III assembly / Respiratory electron transport / respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / Mitochondrial protein degradation / ubiquinone binding / respiratory electron transport chain / mitochondrial membrane ...Complex III assembly / Respiratory electron transport / respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / mitochondrial electron transport, ubiquinol to cytochrome c / Mitochondrial protein degradation / ubiquinone binding / respiratory electron transport chain / mitochondrial membrane / metalloendopeptidase activity / 2 iron, 2 sulfur cluster binding / oxidoreductase activity / mitochondrial inner membrane / 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 / 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 / Ubiquinol-cytochrome c reductase 8kDa, N-terminal / Ubiquinol-cytochrome c reductase 8 kDa, N-terminal / Cytochrome Bc1 Complex; Chain A, domain 1 / Metalloenzyme, LuxS/M16 peptidase-like / 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 / Cytochrome b-c1 complex subunit 7 / Cytochrome b-c1 complex subunit 7 superfamily / Ubiquinol-cytochrome C reductase complex 14kD subunit / 3-layer Sandwich / 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. / 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
Chem-FDN / 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 ...Chem-FDN / 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 / MOLECULAR REPLACEMENT / Resolution: 2.26 Å
AuthorsXia, D. / Esser, L.
CitationJournal: Proc.Natl.Acad.Sci.Usa / Year: 2006
Title: Surface-modulated motion switch: Capture and release of iron-sulfur protein in the cytochrome bc1 complex.
Authors: Esser, L. / Gong, X. / Yang, S. / Yu, L. / Yu, C.A. / Xia, D.
History
DepositionFeb 8, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Aug 29, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Derived calculations / Version format compliance
Revision 1.3Aug 30, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_conn_type / 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_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_label_atom_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.4Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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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, heme protein, mitochondrial
E: Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial
F: Hypothetical protein LOC616871
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 iron-sulfur subunit, mitochondrial
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)243,63716
Polymers241,29311
Non-polymers2,3445
Water4,810267
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, heme protein, mitochondrial
E: Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial
F: Hypothetical protein LOC616871
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 iron-sulfur subunit, mitochondrial
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, heme protein, mitochondrial
E: Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial
F: Hypothetical protein LOC616871
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 iron-sulfur subunit, mitochondrial
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)487,27432
Polymers482,58722
Non-polymers4,68710
Water36020
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation10_665-x+1,-y+1,z1
Buried area101970 Å2
ΔGint-676 kcal/mol
Surface area163640 Å2
MethodPISA, PQS
Unit cell
Length a, b, c (Å)154.263, 154.263, 590.191
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number98
Space group name H-MI4122
DetailsThe second part of the biological assembly (dimer) is generated by the two fold rotation axis: 1-x,1-y, z.

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Components

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Ubiquinol-cytochrome-c reductase complex core protein ... , 2 types, 2 molecules AB

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


Mass: 49266.254 Da / Num. of mol.: 1 / Fragment: Core1 / 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 / Fragment: Core2 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P23004, quinol-cytochrome-c reductase

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Protein , 3 types, 3 molecules CDF

#3: Protein Cytochrome b


Mass: 42620.340 Da / Num. of mol.: 1 / Fragment: cytochrome b / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00157
#4: Protein Cytochrome c1, heme protein, mitochondrial / Cytochrome c-1


Mass: 27323.277 Da / Num. of mol.: 1 / Fragment: cytochrome c1 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00125
#6: Protein Hypothetical protein LOC616871


Mass: 13371.190 Da / Num. of mol.: 1 / Fragment: subunit 6 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P00129

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Ubiquinol-cytochrome c reductase iron-sulfur subunit, ... , 2 types, 2 molecules EI

#5: Protein Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial / RISP


Mass: 21640.580 Da / Num. of mol.: 1 / Fragment: Iron-sulfur protein / 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 iron-sulfur subunit, mitochondrial


Mass: 7964.259 Da / Num. of mol.: 1 / Fragment: Iron-sulfur protein signal sequence / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P13272

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Ubiquinol-cytochrome c reductase complex ... , 4 types, 4 molecules GHJK

#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 / Fragment: subunit 7 / 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 / Fragment: subunit 8 / 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 / Fragment: subunit 10 / 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: 6527.604 Da / Num. of mol.: 1 / Fragment: subunit 11 / Source method: isolated from a natural source / Source: (natural) Bos taurus (domestic cattle) / References: UniProt: P07552, quinol-cytochrome-c reductase

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Non-polymers , 4 types, 272 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-FDN / (5S)-3-ANILINO-5-(2,4-DIFLUOROPHENYL)-5-METHYL-1,3-OXAZOLIDINE-2,4-DIONE / 5-(2,4-DIFLUORO-PHENYL)-5-METHYL-3-PHENYLAMINO-OXAZOLIDINE-2,4-DIONE


Mass: 318.275 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H12F2N2O3
#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.: 267 / 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: 3.64 Å3/Da / Density % sol: 66.17 %
Crystal growTemperature: 277.2 K / Method: vapor diffusion, sitting drop / pH: 7.2
Details: 50 mM MOPS 7.2pH, 20 mM Ammonium acetate, 20% glycerol.Incubation with 2-5 mol excess of JG144. Precipitant 12% PEG4000, 0.5 M KCl, 0.1% DHPC; Protein:PPT ratio 1:0.57, VAPOR DIFFUSION, ...Details: 50 mM MOPS 7.2pH, 20 mM Ammonium acetate, 20% glycerol.Incubation with 2-5 mol excess of JG144. Precipitant 12% PEG4000, 0.5 M KCl, 0.1% DHPC; Protein:PPT ratio 1:0.57, VAPOR DIFFUSION, SITTING DROP, temperature 277.2K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 1.009 Å
DetectorType: MARRESEARCH / Detector: AREA DETECTOR / Date: Jul 3, 2004
RadiationMonochromator: SAGITALLY FOCUSED Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.009 Å / Relative weight: 1
ReflectionResolution: 2.26→50 Å / Num. obs: 157290 / % possible obs: 86.1 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -0.3 / Redundancy: 4 % / Rsym value: 0.056 / Net I/σ(I): 17.2
Reflection shellResolution: 2.26→2.34 Å / Redundancy: 1.8 % / Rmerge(I) obs: 0.382 / Num. unique all: 13582 / % possible all: 42.4

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Processing

Software
NameVersionClassification
REFMAC5.1.24refinement
HKL-2000data reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1l0n

1l0n


Resolution: 2.26→40 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.917 / SU B: 9.1 / SU ML: 0.212 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.253 / ESU R Free: 0.216 / Stereochemistry target values: MAXIMUM LIKELIHOOD
RfactorNum. reflection% reflectionSelection details
Rfree0.28328 3230 2 %RANDOM
Rwork0.24843 ---
all0.24916 157290 --
obs0.24916 157290 96.89 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 25.239 Å2
Baniso -1Baniso -2Baniso -3
1-2.36 Å20 Å20 Å2
2--2.36 Å20 Å2
3----4.71 Å2
Refinement stepCycle: LAST / Resolution: 2.26→40 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms16477 0 156 267 16900
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0210.02117444
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg2.0631.98323647
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg11.115102088
X-RAY DIFFRACTIONr_dihedral_angle_2_deg
X-RAY DIFFRACTIONr_dihedral_angle_3_deg
X-RAY DIFFRACTIONr_dihedral_angle_4_deg
X-RAY DIFFRACTIONr_chiral_restr0.20.22575
X-RAY DIFFRACTIONr_gen_planes_refined0.0260.0213008
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined0.1170.27426
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.0960.2621
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined0.0940.2193
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined0.0680.218
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.5920.410459
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it2.5143.80116826
X-RAY DIFFRACTIONr_scbond_it5.68636985
X-RAY DIFFRACTIONr_scangle_it7.3144.56819
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.26→2.319 Å / Total num. of bins used: 20 /
RfactorNum. reflection
Rfree0.31 200
Rwork0.316 10142
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)
10.6387-0.0310.38091.1171-0.9111.93340.10770.02880.0087-0.19850.0510.48240.0513-0.6601-0.15870.409-0.1203-0.02160.51920.00040.648431.848587.378192.8341
20.40190.04650.05191.2591-0.27081.21260.0627-0.10140.1320.0991-0.05440.1683-0.1467-0.3382-0.00830.3791-0.13150.07820.2501-0.0220.429948.955493.6085114.8425
30.7853-0.47420.04761.68350.22322.16170.08850.03660.1677-0.1045-0.06210.0211-0.257-0.1692-0.02640.3716-0.10620.01210.03050.00410.380468.9613104.585991.8809
40.9661-0.5856-0.00492.51750.01181.40070.03560.057-0.0577-0.18780.00940.32910.1252-0.1548-0.04490.4149-0.0943-0.07230.12530.00660.386557.164186.605373.2507
50.67740.15260.2280.36060.57391.06570.0555-0.23010.04180.1964-0.02140.0307-0.0985-0.0703-0.03410.5667-0.29450.04320.30590.02340.408364.906868.7511154.1684
61.8003-0.78590.00812.81950.55981.7729-0.03-0.1901-0.06520.35760.0574-0.25210.15070.2677-0.02740.7502-0.3258-0.07880.49330.10510.422481.270957.0226172.1093
71.21750.13270.40991.06840.26073.00460.1008-0.3079-0.18690.2534-0.0423-0.04360.41710.0118-0.05850.5908-0.30950.00580.27410.11520.505364.794544.9222152.9122
80000000000000000.52000.5200.52000
90.5907-0.1591-0.6957-0.1286-0.08287.78640.0257-0.2403-0.0080.2387-0.09270.15730.2128-0.60550.0670.6332-0.34220.14870.50520.03240.491345.351371.5948159.1567
101.84740.35720.29362.54280.17841.34420.0143-0.5153-0.13530.63180.00970.04380.0101-0.1603-0.0240.981-0.31050.16610.91810.08510.430654.585867.6302192.8498
111.23560.3402-1.15970.5191-0.38352.96050.0755-0.3259-0.0270.1692-0.087-0.17510.03460.65960.01160.4672-0.2006-0.16130.424-0.00440.5649110.936172.0527141.5949
124.8487-1.63980.43475.0189-0.22114.4109-0.3117-1.1715-0.12150.83050.5055-0.13550.35010.6179-0.19391.0334-0.0993-0.02050.9830.25110.575282.338742.078188.3545
133.0455-0.9906-1.26721.19160.00511.75740.0234-0.0737-0.29960.0907-0.06650.20120.4608-0.17690.04310.5112-0.30320.01370.19760.02240.424459.045347.1643122.0445
140.3252-0.0878-0.14471.42-1.5012.26130.0528-0.2983-0.07940.41690.05240.1455-0.0529-0.3633-0.10520.5626-0.34880.07540.44550.04280.497448.046154.8256144.5844
153.6388-5.8928-1.095116.0242-3.53815.61790.0331-0.2262-0.76020.0920.00510.88150.4103-0.134-0.03820.7231-0.24930.08860.72740.09040.857940.081539.2536193.3643
165.5433-7.7302-3.484124.966-5.16082.8251-0.27790.2280.40050.38620.0625-0.26680.2818-0.65140.21540.7106-0.26220.05170.73640.07520.610939.858350.2342187.5459
170000000000000000.52000.5200.52000
181.38661.99983.50310.26.6415.59020.13930.5135-0.1719-0.4218-0.41410.47980.4614-1.9490.27480.53-0.0241-0.00950.5219-0.08130.692660.473994.92288.45
1918.47134.40517.76658.8431-5.157926.5690.8166-0.06050.2125-0.1709-0.03520.02570.7781-0.1364-0.78140.52560.02380.06340.59620.01050.811854.526280.928293.656
2083.762715.513-6.435449.178312.994326.3317-1.06531.9731-1.5905-0.29761.06841.4086-0.4297-0.044-0.00310.5201-0.0004-0.00220.5206-0.00280.521147.063598.0961104.0711
211.13420.0579-0.07022.2396-2.2327.4889-0.0997-0.42640.03580.38490.06060.1708-0.5538-0.95830.03910.6615-0.11830.22570.7295-0.10570.605738.913789.4213161.1124
221.94551.2355-2.41853.9323-4.031810.70330.2282-0.46930.25150.39230.06920.1913-0.5432-0.3154-0.29730.6605-0.08640.04780.5104-0.16290.609952.5445104.6869147.9947
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
3X-RAY DIFFRACTION3BB17 - 23517 - 235
4X-RAY DIFFRACTION4BB236 - 439236 - 439
5X-RAY DIFFRACTION5CC3 - 1333 - 133
6X-RAY DIFFRACTION5CC173 - 264173 - 264
7X-RAY DIFFRACTION5CL381
8X-RAY DIFFRACTION6CC134 - 172134 - 172
9X-RAY DIFFRACTION7CC265 - 379265 - 379
10X-RAY DIFFRACTION8CM382
11X-RAY DIFFRACTION9DD173 - 241173 - 241
12X-RAY DIFFRACTION10DD1 - 1721 - 172
13X-RAY DIFFRACTION10DO242
14X-RAY DIFFRACTION11EE1 - 711 - 71
15X-RAY DIFFRACTION12EE72 - 19672 - 196
16X-RAY DIFFRACTION13FF6 - 1106 - 110
17X-RAY DIFFRACTION14GG1 - 751 - 75
18X-RAY DIFFRACTION15HH15 - 5215 - 52
19X-RAY DIFFRACTION16HH53 - 7853 - 78
20X-RAY DIFFRACTION17HH49 - 7849 - 78
21X-RAY DIFFRACTION18II2 - 262 - 26
22X-RAY DIFFRACTION19II27 - 5127 - 51
23X-RAY DIFFRACTION20II52 - 5752 - 57
24X-RAY DIFFRACTION21JJ2 - 612 - 61
25X-RAY DIFFRACTION22KK1 - 531 - 53

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