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- PDB-5kkz: Rhodobacter sphaeroides bc1 with famoxadone -

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Basic information

Entry
Database: PDB / ID: 5kkz
TitleRhodobacter sphaeroides bc1 with famoxadone
Components
  • Cytochrome b
  • Cytochrome c1
  • Ubiquinol-cytochrome c reductase iron-sulfur subunit
KeywordsOXIDOREDUCTASE / Mitochondrial respiratory chain complex / cytochrome bc1 / inhibitors / electron transfer
Function / homology
Function and homology information


respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / respirasome / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / intracellular membrane-bounded organelle / heme binding / metal ion binding ...respiratory chain complex III / quinol-cytochrome-c reductase / ubiquinol-cytochrome-c reductase activity / respirasome / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / electron transfer activity / intracellular membrane-bounded organelle / heme binding / metal ion binding / plasma membrane / cytoplasm
Similarity search - Function
Ubiquitinol-cytochrome C reductase, Fe-S subunit, TAT signal / Ubiquitinol-cytochrome C reductase Fe-S subunit TAT signal / Single helix bin / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / Rieske Iron-sulfur Protein / Rieske [2Fe-2S] iron-sulphur domain / 3-layer Sandwich / Cytochrome b ...Ubiquitinol-cytochrome C reductase, Fe-S subunit, TAT signal / Ubiquitinol-cytochrome C reductase Fe-S subunit TAT signal / Single helix bin / Cytochrome Bc1 Complex; Chain C / Cytochrome Bc1 Complex; Chain C / Cytochrome c1, transmembrane anchor, C-terminal / Rieske Iron-sulfur Protein / Rieske [2Fe-2S] iron-sulphur domain / 3-layer Sandwich / 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 / Twin-arginine translocation pathway, signal sequence, bacterial/archaeal / 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 / Rieske [2Fe-2S] iron-sulphur domain / Rieske [2Fe-2S] domain / Rieske [2Fe-2S] iron-sulfur domain profile. / Rieske [2Fe-2S] iron-sulphur domain superfamily / Cytochrome c-like domain / Cytochrome Bc1 Complex; Chain D, domain 2 / Cytochrome c family profile. / Cytochrome c-like domain / Cytochrome c-like domain superfamily / Twin arginine translocation (Tat) signal profile. / Twin-arginine translocation pathway, signal sequence / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / Up-down Bundle / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
ASCORBIC ACID / FE2/S2 (INORGANIC) CLUSTER / FAMOXADONE / HEME C / PROTOPORPHYRIN IX CONTAINING FE / Chem-LOP / STRONTIUM ION / Cytochrome c1 / Cytochrome b / Ubiquinol-cytochrome c reductase iron-sulfur subunit
Similarity search - Component
Biological speciesRhodobacter sphaeroides (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.97 Å
AuthorsXia, D. / Esser, L. / Zhou, F. / Tang, W.K. / Yu, C.A.
CitationJournal: J.Biol.Chem. / Year: 2016
Title: Hydrogen Bonding to the Substrate Is Not Required for Rieske Iron-Sulfur Protein Docking to the Quinol Oxidation Site of Complex III.
Authors: Esser, L. / Zhou, F. / Zhou, Y. / Xiao, Y. / Tang, W.K. / Yu, C.A. / Qin, Z. / Xia, D.
History
DepositionJun 23, 2016Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 12, 2016Provider: repository / Type: Initial release
Revision 1.1Oct 19, 2016Group: Derived calculations
Revision 1.2Nov 2, 2016Group: Database references
Revision 1.3Dec 7, 2016Group: Database references
Revision 1.4Jul 29, 2020Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Structure summary
Category: chem_comp / citation ...chem_comp / citation / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_conn_type / 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 / _citation.journal_id_CSD / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _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_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.5Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Cytochrome b
B: Cytochrome c1
C: Ubiquinol-cytochrome c reductase iron-sulfur subunit
E: Cytochrome b
F: Cytochrome c1
G: Ubiquinol-cytochrome c reductase iron-sulfur subunit
K: Cytochrome b
L: Cytochrome c1
M: Ubiquinol-cytochrome c reductase iron-sulfur subunit
O: Cytochrome b
P: Cytochrome c1
Q: Ubiquinol-cytochrome c reductase iron-sulfur subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)413,07450
Polymers398,42012
Non-polymers14,65438
Water724
1
A: Cytochrome b
B: Cytochrome c1
C: Ubiquinol-cytochrome c reductase iron-sulfur subunit
E: Cytochrome b
F: Cytochrome c1
G: Ubiquinol-cytochrome c reductase iron-sulfur subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,53725
Polymers199,2106
Non-polymers7,32719
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area33960 Å2
ΔGint-384 kcal/mol
Surface area70960 Å2
MethodPISA
2
K: Cytochrome b
L: Cytochrome c1
M: Ubiquinol-cytochrome c reductase iron-sulfur subunit
O: Cytochrome b
P: Cytochrome c1
Q: Ubiquinol-cytochrome c reductase iron-sulfur subunit
hetero molecules


Theoretical massNumber of molelcules
Total (without water)206,53725
Polymers199,2106
Non-polymers7,32719
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area33920 Å2
ΔGint-383 kcal/mol
Surface area71150 Å2
MethodPISA
Unit cell
Length a, b, c (Å)120.773, 128.277, 128.283
Angle α, β, γ (deg.)63.92, 88.63, 63.38
Int Tables number1
Space group name H-MP1

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Components

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Protein , 3 types, 12 molecules AEKOBFLPCGMQ

#1: Protein
Cytochrome b /


Mass: 50087.422 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter sphaeroides (bacteria) / Gene: petB, fbcB / Production host: Rhodobacter sp. (bacteria) / References: UniProt: Q02761
#2: Protein
Cytochrome c1 /


Mass: 29589.158 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter sphaeroides (bacteria) / Gene: petC, fbcC / Production host: Rhodobacter sp. (bacteria) / References: UniProt: Q02760
#3: Protein
Ubiquinol-cytochrome c reductase iron-sulfur subunit / Rieske iron-sulfur protein / RISP


Mass: 19928.375 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rhodobacter sphaeroides (bacteria) / Gene: petA, fbcF / Production host: Rhodobacter sp. (bacteria) / References: UniProt: Q02762, quinol-cytochrome-c reductase

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Sugars , 2 types, 8 molecules

#6: Sugar
ChemComp-ASC / ASCORBIC ACID / Vitamin C / Vitamin C


Type: L-saccharide / Mass: 176.124 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C6H8O6 / Comment: medication*YM
#10: Sugar
ChemComp-BOG / octyl beta-D-glucopyranoside / Beta-Octylglucoside / octyl beta-D-glucoside / octyl D-glucoside / octyl glucoside / Octyl glucoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 4
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 , 7 types, 34 molecules

#4: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#5: Chemical
ChemComp-FMX / FAMOXADONE / 5-METHYL-5-(4-PHENOXYPHENYL)-3-(PHENYLAMINO)-2,4-OXAZOLIDINEDIONE / Famoxadone


Mass: 374.389 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C22H18N2O4
#7: Chemical
ChemComp-SR / STRONTIUM ION / Strontium


Mass: 87.620 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: Sr
#8: Chemical
ChemComp-LOP / (1R)-2-{[(R)-(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(DODECANOYLOXY)METHYL]ETHYL (9Z)-OCTADEC-9-ENOATE / LAURYL OLEYL PHOSPHATIDYL ETHANOLAMINE


Mass: 661.890 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C35H68NO8P / Comment: phospholipid*YM
#9: Chemical
ChemComp-HEC / HEME C / Heme C


Mass: 618.503 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H34FeN4O4
#11: Chemical
ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Fe2S2
#12: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: H2O

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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: 3.91 Å3/Da / Density % sol: 68.55 %
Crystal growTemperature: 289 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 7% PEG400, 200 mM histidine, 150 mM NaCl, 10 mM sodium ascorbate, famoxadone, b-OG, sucrose mono caparate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å
DetectorType: MAR CCD 165 mm / Detector: CCD / Date: Apr 4, 2009
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.97→50 Å / Num. obs: 122242 / % possible obs: 96.3 % / Redundancy: 2 % / Biso Wilson estimate: 59.32 Å2 / Rmerge(I) obs: 0.102 / Net I/σ(I): 6.2
Reflection shellResolution: 2.97→3.03 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.558 / % possible all: 82.5

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
PHENIX(1.11rc1_2513: ???)refinement
SCALEPACKdata scaling
MOLREPphasing
PDB_EXTRACT3.2data extraction
HKL-2000data reduction
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 2QJY chains A, B and C only

2qjy


Resolution: 2.97→29.981 Å / SU ML: 0.44 / Cross valid method: FREE R-VALUE / σ(F): 1.16 / Phase error: 29.48 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2583 1990 1.65 %
Rwork0.2154 --
obs0.2161 120381 96.72 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.97→29.981 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms26956 0 958 4 27918
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01428948
X-RAY DIFFRACTIONf_angle_d1.33939664
X-RAY DIFFRACTIONf_dihedral_angle_d12.36216288
X-RAY DIFFRACTIONf_chiral_restr0.0714176
X-RAY DIFFRACTIONf_plane_restr0.0114980
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.97-3.04420.3621480.33798109X-RAY DIFFRACTION93
3.0442-3.12640.34441330.31318366X-RAY DIFFRACTION95
3.1264-3.21830.35391400.29868332X-RAY DIFFRACTION95
3.2183-3.32210.33191530.28778363X-RAY DIFFRACTION96
3.3221-3.44070.29061370.26288491X-RAY DIFFRACTION97
3.4407-3.57820.28251310.24228502X-RAY DIFFRACTION97
3.5782-3.74080.2731500.22548517X-RAY DIFFRACTION97
3.7408-3.93760.2551330.2028441X-RAY DIFFRACTION97
3.9376-4.18370.21791430.19488558X-RAY DIFFRACTION98
4.1837-4.50570.22441420.18568547X-RAY DIFFRACTION98
4.5057-4.95730.22031470.17138609X-RAY DIFFRACTION98
4.9573-5.67040.23031490.18448576X-RAY DIFFRACTION98
5.6704-7.12830.24591450.19968680X-RAY DIFFRACTION99
7.1283-29.98260.22281390.17828300X-RAY DIFFRACTION95
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)
10.2160.6964-1.22.214-3.84146.6396-0.00580.75620.3007-0.69950.61760.64690.1859-1.4068-0.62331.0701-0.1542-0.22881.10390.31520.8736-32.003-46.796110.0805
20.3074-0.14670.07540.2313-0.26940.29210.0036-0.13530.0684-0.08260.04640.06930.2031-0.16360.01780.7229-0.2148-0.36940.5840.11930.7131-9.4471-53.588634.6335
30.33850.0005-0.15360.1419-0.11690.46310.1062-0.0839-0.0130.2243-0.1802-0.01210.2542-0.21-0.30860.8225-0.1962-0.42940.5970.12990.7438-14.0493-58.809140.504
41.0085-0.10080.62760.7731-0.65362.10880.0829-0.2425-0.2189-0.2195-0.11060.25190.2734-0.25970.04660.8192-0.2341-0.31590.57250.17630.6766-19.1311-72.992741.3289
54.81250.0770.38831.95790.50643.07370.2045-0.3690.19860.208-0.12290.3073-0.235-0.3917-0.02210.6772-0.1197-0.2910.66860.06230.6736-1.7063-31.931361.3457
65.0625-0.4206-0.63442.4646-0.25053.48690.05620.27080.2416-0.37550.0314-0.4707-0.23880.2539-0.16790.8578-0.1915-0.10250.66690.00410.849612.2393-19.212151.0555
71.40011.1685-0.75651.8180.28591.70140.2731-0.10260.1230.1203-0.07140.13910.0948-0.3804-0.04150.694-0.1987-0.30990.70270.09710.7158-0.7224-42.087859.1132
83.8489-0.69260.44437.45210.40732.85020.0977-0.4347-0.3430.9206-0.28160.43170.3920.36170.0910.8658-0.1535-0.31660.7330.16920.75438.8065-52.499374.5039
94.16161.43213.39931.99861.06822.8737-0.0634-0.34920.62550.2701-0.17170.1768-0.0759-0.33550.22510.5114-0.0392-0.04280.6848-0.03070.5415-14.8766-34.966155.577
106.0601-0.2071-7.33720.48810.18198.89260.1448-0.65470.61830.7345-0.1701-0.658-0.72250.6983-0.02051.99120.235-0.31311.6669-0.18791.8579-48.6504-33.944832.7628
117.40622.2569-0.67294.30270.67683.5435-0.65111.17480.88530.40110.24380.5509-0.5727-0.44090.34160.83440.0547-0.08740.7550.17590.8953-18.9985-29.856434.1445
123.4518-1.2454-0.53732.0145-3.04246.77970.4529-0.69250.5981-0.0715-0.12520.1297-0.84521.0406-0.2791.1132-0.3602-0.1560.84760.13461.299818.8049-6.776432.1288
132.0457-0.3638-0.58622.3991-0.23981.16740.08110.21710.8213-0.0096-0.4332-0.663-0.7830.4250.32131.2577-0.1239-0.24460.63630.11681.130311.3066-2.288524.6516
141.20062.5274-2.59046.9905-4.84725.7643-0.30160.3588-0.33-1.42620.1579-0.62911.1174-1.8033-0.03591.2366-0.1916-0.16640.93580.03640.8609-19.0905-65.79835.5973
150.30150.0539-0.15331.308-0.73380.55990.03720.26680.0222-0.33520.1702-0.07870.2778-0.10440.00410.671-0.1082-0.22490.56220.14120.6553-0.3244-38.041811.7324
160.7029-0.32190.3831.2562-0.29671.1177-0.06780.42530.2216-0.4080.0220.25280.0946-0.16260.10720.546-0.0681-0.08110.51860.12060.4191.1093-34.44293.5283
171.83680.2219-0.18361.5761-0.39570.4232-0.05710.7362-0.1815-0.68880.24230.48980.2034-0.2497-0.04130.70380.0049-0.12750.51690.43790.4313-6.7758-26.9616-6.9204
182.95150.4879-0.23591.68290.76545.345-0.08370.2008-0.1351-0.0404-0.0321-0.55580.09530.6260.06770.5160.0261-0.020.43580.08740.893734.4699-38.1816.5714
192.44441.6704-1.51525.20291.87649.5672-0.0041-0.4019-0.14660.8086-0.2138-0.85940.01140.82160.32880.5805-0.0472-0.23120.69070.16760.8934.5028-43.533337.4382
203.29540.714-0.10182.1754-0.16522.5044-0.00720.19480.3256-0.2008-0.2642-0.1861-0.03020.05710.36910.5247-0.0646-0.04540.52120.09990.67726.9971-31.326314.0425
212.73032.105-0.53951.98860.75963.92670.00380.42451.4593-0.2225-0.4101-0.265-1.50270.44330.17971.0822-0.13410.19040.59990.2131.232634.3203-12.171311.3562
222.8441.83821.25682.13161.00142.19440.36660.3185-0.38150.227-0.1573-0.43410.4486-0.0158-0.07540.53770.00960.05290.49450.03210.630826.7232-45.70766.7993
231.15310.87-1.40390.7195-1.18642.36470.12120.14860.63490.055-0.0657-0.0243-0.734-0.0454-0.06051.594-0.0226-0.70821.5450.49962.41935.2737-74.8146-11.6501
242.4714-1.0273-0.12922.90131.33036.51840.54980.4342-0.6888-0.0238-0.3275-0.45251.1294-0.6782-0.2440.9003-0.0844-0.18480.62260.02150.818111.6369-60.715113.918
251.9077-0.1347-0.13334.0208-0.12712.4048-0.096-0.7458-0.3370.6084-0.0789-0.56220.19660.66120.22630.66520.0626-0.21650.9260.20160.739726.8286-57.382855.1844
261.62710.1505-0.23220.44280.28091.227-0.1087-0.6593-0.10380.5033-0.0329-0.47160.49770.77360.08340.89420.0497-0.33940.93010.33110.99222.1304-67.858853.7314
271.7874-0.0947-1.49482.0102-3.46037.6652-0.41410.71720.4975-0.28670.41030.62140.4271-0.9471-0.06350.9191-0.2492-0.24390.86730.04470.7755-36.461535.0366-46.0425
281.73970.28390.74110.9333-0.17531.42120.3284-0.2132-0.5237-0.0227-0.0693-0.11550.6173-0.25050.28390.1761-0.04010.0470.2703-0.04210.1193-13.604430.1964-21.4671
291.6947-0.2110.51050.9487-0.13211.3017-0.0349-0.155-0.4047-0.1605-0.07810.08440.6625-0.125-1.0576-0.0795-0.2025-0.22640.1981-0.0479-0.0408-17.968225.0229-15.3603
300.7725-0.58340.95891.0414-0.15731.94780.499-0.3742-0.3564-0.329-0.18040.53720.667-0.6588-0.2990.4686-0.1125-0.10.32560.1180.2974-22.263710.5531-14.012
314.57890.75530.18092.6121-0.2362.36060.0464-0.11870.52790.2091-0.2884-0.2699-0.6936-0.02050.14590.4290.0782-0.11180.4347-0.03410.3268-6.891953.22014.2644
325.2299-0.0384-1.94931.8359-0.09455.54320.2235-0.00020.4827-0.2958-0.087-0.6593-0.7080.9018-0.08320.9073-0.1473-0.2780.55820.02380.85626.780165.9048-6.2675
331.7438-0.03961.43722.48760.05092.8542-0.0204-0.11030.3558-0.0705-0.12670.302-0.0098-0.16220.17610.3882-0.1062-0.03850.542-0.02020.2563-5.510743.00272.3954
345.4303-2.60450.56393.5007-0.12753.97150.0774-0.6607-1.1841.0274-0.1038-0.13060.71480.67-0.22320.84520.0348-0.23460.79010.20760.69784.038133.246617.8373
354.47091.2152.49511.92020.99122.5705-0.134-0.09730.5570.0449-0.19080.1105-0.1849-0.36510.34470.42520.0398-0.08580.5301-0.05160.4207-19.84949.3339-1.2695
361.15291.2538-1.50861.3874-1.66032.0039-0.1058-0.3278-0.4327-0.1548-0.0527-0.32620.01920.15010.0931.9462-0.1566-0.22111.29660.29542.1462-53.682248.3077-23.8222
377.31572.6755-1.35284.5861-1.32550.4411-0.0688-0.08460.56680.4432-0.11190.189-0.5453-0.5155-0.01450.50530.0619-0.06660.6484-0.10610.3519-24.31453.4992-22.736
381.2974-0.5244-1.04513.0136-1.0161.5818-0.2148-0.33050.5144-0.1855-0.0431-0.4907-0.67460.3253-0.02910.9041-0.2697-0.27630.62040.08941.110112.140978.5828-25.995
391.4012-0.29790.10940.77980.80880.96990.16890.0110.87610.092-0.2252-0.3956-0.47510.3682-0.16341.2059-0.2562-0.29620.57520.12781.18334.289882.2433-33.6856
402.6864.0746-4.50268.3606-6.70037.5438-0.34160.1232-0.3659-0.92450.3943-0.03921.6558-1.2292-0.17361.1539-0.168-0.15170.82260.06070.7701-22.649316.5028-49.8175
411.33130.32281.04581.68810.1161.3993-0.50390.52270.384-0.60840.29670.4057-0.29240.1575-0.38240.3142-0.12080.00710.42510.06850.2709-5.193145.3939-44.8766
420.3696-0.1470.10541.0626-0.84540.7455-0.17560.45050.1796-0.1490.03790.03-0.01550.07970.10440.6976-0.1212-0.19990.62040.1290.7184-3.964148.7564-53.2
430.60660.50570.14831.7514-0.56831.148-0.11220.4168-0.0113-0.60260.18650.0681-0.01550.16460.02390.7479-0.1126-0.18940.60550.20880.5573-12.218355.3797-63.9667
442.06030.6970.7472.5461.19253.6656-0.12430.33990.1433-0.42130.0084-0.41020.220.87450.15170.4797-0.05560.05940.73610.14470.848429.645847.2246-40.1717
453.85880.7917-0.14233.2489-0.5064.84620.14130.0618-0.27210.4598-0.1526-0.3124-0.63250.50190.18910.61560.0352-0.14120.91640.13640.859929.979342.2361-19.2493
462.91520.45961.53023.8598-2.05886.0544-0.1910.6263-0.0742-0.7623-0.0983-0.28960.7370.44280.0850.4223-0.1138-0.03380.67430.14850.660421.867153.6362-42.9367
471.6162-0.80920.40936.6784-2.70444.1672-0.07640.06310.3538-0.32980.0547-0.301-0.68740.1950.05090.9229-0.1716-0.09130.89790.3621.267228.659273.2399-46.0264
481.8316-0.3490.72171.3546-0.31811.215-0.19240.61930.3236-0.16770.0053-0.29350.09490.55440.00480.4942-0.01080.190.66890.06290.460922.203338.9195-49.6785
492.86581.2724-4.06580.6485-1.99176.23060.1711-0.36840.09850.45060.0273-0.0871-0.25640.2118-0.09691.6598-0.2127-0.42621.54250.46661.89642.06318.0381-66.6537
502.78831.15821.88292.87191.57241.84350.28040.1121-0.2185-0.0184-0.3069-0.79360.4031-0.0677-0.36640.6390.08110.14950.6162-0.01420.62277.704723.4592-41.908
511.22640.3963-1.51854.0123-1.88522.96210.1899-0.7173-0.4890.16950.1146-0.24470.48330.8418-0.24690.96010.0192-0.36591.24440.21310.98422.805129.5342-0.8157
521.5543-0.3658-0.03820.78980.93111.2022-0.1029-0.6691-0.58540.5873-0.1309-0.27750.6280.74480.08460.88470.1-0.24041.05860.40041.097318.811118.7691-1.7815
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 3:36 )A3 - 36
2X-RAY DIFFRACTION2( CHAIN A AND ( RESID 37:227 OR RESID 1006:1006 OR RESID 1003:1003 OR RESID 1001:1002 ) )A37 - 227
3X-RAY DIFFRACTION2( CHAIN A AND ( RESID 37:227 OR RESID 1006:1006 OR RESID 1003:1003 OR RESID 1001:1002 ) )A1006
4X-RAY DIFFRACTION2( CHAIN A AND ( RESID 37:227 OR RESID 1006:1006 OR RESID 1003:1003 OR RESID 1001:1002 ) )A1003
5X-RAY DIFFRACTION2( CHAIN A AND ( RESID 37:227 OR RESID 1006:1006 OR RESID 1003:1003 OR RESID 1001:1002 ) )A1001 - 1002
6X-RAY DIFFRACTION3( CHAIN A AND RESID 228:326 )A228 - 326
7X-RAY DIFFRACTION4( CHAIN A AND ( RESID 327:431 OR RESID 1005:1005 ) )A327 - 431
8X-RAY DIFFRACTION4( CHAIN A AND ( RESID 327:431 OR RESID 1005:1005 ) )A1005
9X-RAY DIFFRACTION5( CHAIN B AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )B1 - 58
10X-RAY DIFFRACTION5( CHAIN B AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )B1002
11X-RAY DIFFRACTION5( CHAIN B AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )B1001
12X-RAY DIFFRACTION6( CHAIN B AND RESID 59:84 )B59 - 84
13X-RAY DIFFRACTION7( CHAIN B AND RESID 85:133 )B85 - 133
14X-RAY DIFFRACTION8( CHAIN B AND RESID 134:184 )B134 - 184
15X-RAY DIFFRACTION9( CHAIN B AND RESID 185:256 )B185 - 256
16X-RAY DIFFRACTION10( CHAIN C AND RESID 9:13 )C9 - 13
17X-RAY DIFFRACTION11( CHAIN C AND RESID 14:46 )C14 - 46
18X-RAY DIFFRACTION12( CHAIN C AND RESID 47:83 )C47 - 83
19X-RAY DIFFRACTION13( CHAIN C AND ( RESID 84:187 OR RESID 1001:1001 ) )C84 - 187
20X-RAY DIFFRACTION13( CHAIN C AND ( RESID 84:187 OR RESID 1001:1001 ) )C1001
21X-RAY DIFFRACTION14( CHAIN E AND RESID 3:36 )E3 - 36
22X-RAY DIFFRACTION15( CHAIN E AND ( RESID 37:227 OR RESID 1005:1005 OR RESID 1003:1003 OR RESID 1001:1002 ) )E37 - 227
23X-RAY DIFFRACTION15( CHAIN E AND ( RESID 37:227 OR RESID 1005:1005 OR RESID 1003:1003 OR RESID 1001:1002 ) )E1005
24X-RAY DIFFRACTION15( CHAIN E AND ( RESID 37:227 OR RESID 1005:1005 OR RESID 1003:1003 OR RESID 1001:1002 ) )E1003
25X-RAY DIFFRACTION15( CHAIN E AND ( RESID 37:227 OR RESID 1005:1005 OR RESID 1003:1003 OR RESID 1001:1002 ) )E1001 - 1002
26X-RAY DIFFRACTION16( CHAIN E AND RESID 228:326 )E228 - 326
27X-RAY DIFFRACTION17( CHAIN E AND RESID 327:431 )E327 - 431
28X-RAY DIFFRACTION18( CHAIN F AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )F1 - 58
29X-RAY DIFFRACTION18( CHAIN F AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )F1002
30X-RAY DIFFRACTION18( CHAIN F AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )F1001
31X-RAY DIFFRACTION19( CHAIN F AND RESID 59:84 )F59 - 84
32X-RAY DIFFRACTION20( CHAIN F AND RESID 85:133 )F85 - 133
33X-RAY DIFFRACTION21( CHAIN F AND RESID 134:184 )F134 - 184
34X-RAY DIFFRACTION22( CHAIN F AND RESID 185:256 )F185 - 256
35X-RAY DIFFRACTION23( CHAIN G AND RESID 9:13 )G9 - 13
36X-RAY DIFFRACTION24( CHAIN G AND RESID 14:46 )G14 - 46
37X-RAY DIFFRACTION25( CHAIN G AND RESID 47:83 )G47 - 83
38X-RAY DIFFRACTION26( CHAIN G AND ( RESID 84:187 OR RESID 1001:1001 ) )G84 - 187
39X-RAY DIFFRACTION26( CHAIN G AND ( RESID 84:187 OR RESID 1001:1001 ) )G1001
40X-RAY DIFFRACTION27( CHAIN K AND RESID 3:36 )K3 - 36
41X-RAY DIFFRACTION28( CHAIN K AND ( RESID 37:227 OR RESID 1006:1006 OR RESID 1003:1003 OR RESID 1001:1002 ) )K37 - 227
42X-RAY DIFFRACTION28( CHAIN K AND ( RESID 37:227 OR RESID 1006:1006 OR RESID 1003:1003 OR RESID 1001:1002 ) )K1006
43X-RAY DIFFRACTION28( CHAIN K AND ( RESID 37:227 OR RESID 1006:1006 OR RESID 1003:1003 OR RESID 1001:1002 ) )K1003
44X-RAY DIFFRACTION28( CHAIN K AND ( RESID 37:227 OR RESID 1006:1006 OR RESID 1003:1003 OR RESID 1001:1002 ) )K1001 - 1002
45X-RAY DIFFRACTION29( CHAIN K AND RESID 228:326 )K228 - 326
46X-RAY DIFFRACTION30( CHAIN K AND ( RESID 327:431 OR RESID 1005:1005 ) )K327 - 431
47X-RAY DIFFRACTION30( CHAIN K AND ( RESID 327:431 OR RESID 1005:1005 ) )K1005
48X-RAY DIFFRACTION31( CHAIN L AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )L1 - 58
49X-RAY DIFFRACTION31( CHAIN L AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )L1002
50X-RAY DIFFRACTION31( CHAIN L AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )L1001
51X-RAY DIFFRACTION32( CHAIN L AND RESID 59:84 )L59 - 84
52X-RAY DIFFRACTION33( CHAIN L AND RESID 85:133 )L85 - 133
53X-RAY DIFFRACTION34( CHAIN L AND RESID 134:184 )L134 - 184
54X-RAY DIFFRACTION35( CHAIN L AND RESID 185:256 )L185 - 256
55X-RAY DIFFRACTION36( CHAIN M AND RESID 9:13 )M9 - 13
56X-RAY DIFFRACTION37( CHAIN M AND RESID 14:46 )M14 - 46
57X-RAY DIFFRACTION38( CHAIN M AND RESID 47:83 )M47 - 83
58X-RAY DIFFRACTION39( CHAIN M AND ( RESID 84:187 OR RESID 1001:1001 ) )M84 - 187
59X-RAY DIFFRACTION39( CHAIN M AND ( RESID 84:187 OR RESID 1001:1001 ) )M1001
60X-RAY DIFFRACTION40( CHAIN O AND RESID 3:36 )O3 - 36
61X-RAY DIFFRACTION41( CHAIN O AND ( RESID 37:227 OR RESID 1005:1005 OR RESID 1003:1003 OR RESID 1001:1002 ) )O37 - 227
62X-RAY DIFFRACTION41( CHAIN O AND ( RESID 37:227 OR RESID 1005:1005 OR RESID 1003:1003 OR RESID 1001:1002 ) )O1005
63X-RAY DIFFRACTION41( CHAIN O AND ( RESID 37:227 OR RESID 1005:1005 OR RESID 1003:1003 OR RESID 1001:1002 ) )O1003
64X-RAY DIFFRACTION41( CHAIN O AND ( RESID 37:227 OR RESID 1005:1005 OR RESID 1003:1003 OR RESID 1001:1002 ) )O1001 - 1002
65X-RAY DIFFRACTION42( CHAIN O AND RESID 228:326 )O228 - 326
66X-RAY DIFFRACTION43( CHAIN O AND RESID 327:431 )O327 - 431
67X-RAY DIFFRACTION44( CHAIN P AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )P1 - 58
68X-RAY DIFFRACTION44( CHAIN P AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )P1002
69X-RAY DIFFRACTION44( CHAIN P AND ( RESID 1:58 OR RESID 1002:1002 OR RESID 1001:1001 ) )P1001
70X-RAY DIFFRACTION45( CHAIN P AND RESID 59:84 )P59 - 84
71X-RAY DIFFRACTION46( CHAIN P AND RESID 85:133 )P85 - 133
72X-RAY DIFFRACTION47( CHAIN P AND RESID 134:184 )P134 - 184
73X-RAY DIFFRACTION48( CHAIN P AND RESID 185:256 )P185 - 256
74X-RAY DIFFRACTION49( CHAIN Q AND RESID 9:13 )Q9 - 13
75X-RAY DIFFRACTION50( CHAIN Q AND RESID 14:46 )Q14 - 46
76X-RAY DIFFRACTION51( CHAIN Q AND RESID 47:83 )Q47 - 83
77X-RAY DIFFRACTION52( CHAIN Q AND ( RESID 84:187 OR RESID 1001:1001 ) )Q84 - 187
78X-RAY DIFFRACTION52( CHAIN Q AND ( RESID 84:187 OR RESID 1001:1001 ) )Q1001

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