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- PDB-3abv: Crystal structure of porcine heart mitochondrial complex II bound... -

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Basic information

Entry
Database: PDB / ID: 3abv
TitleCrystal structure of porcine heart mitochondrial complex II bound with N-Biphenyl-3-yl-2-trifluoromethyl-benzamide
Components
  • (Succinate dehydrogenase [ubiquinone] ...) x 3
  • Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
KeywordsOXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / respiratory complex II / inhibitors / Electron transport / Iron-sulfur / Metal-binding / Mitochondrion / Mitochondrion inner membrane / Oxidoreductase / Transit peptide / Transport / Tricarboxylic acid cycle / Heme / Transmembrane / FAD-binding protein / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex
Function / homology
Function and homology information


Maturation of TCA enzymes and regulation of TCA cycle / Citric acid cycle (TCA cycle) / Oxidoreductases; Acting on the CH-OH group of donors; With a quinone or similar compound as acceptor / respiratory chain complex II (succinate dehydrogenase) / : / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase (quinone) activity / succinate dehydrogenase / 3 iron, 4 sulfur cluster binding / ubiquinone binding ...Maturation of TCA enzymes and regulation of TCA cycle / Citric acid cycle (TCA cycle) / Oxidoreductases; Acting on the CH-OH group of donors; With a quinone or similar compound as acceptor / respiratory chain complex II (succinate dehydrogenase) / : / mitochondrial electron transport, succinate to ubiquinone / succinate dehydrogenase (quinone) activity / succinate dehydrogenase / 3 iron, 4 sulfur cluster binding / ubiquinone binding / tricarboxylic acid cycle / aerobic respiration / respiratory electron transport chain / mitochondrial membrane / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / mitochondrial inner membrane / electron transfer activity / heme binding / metal ion binding
Similarity search - Function
Single helix bin / Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, CybS / CybS, succinate dehydrogenase cytochrome B small subunit / succinate dehydrogenase protein domain / Succinate dehydrogenase, cytochrome b subunit, conserved site / Succinate dehydrogenase cytochrome b subunit signature 1. / Succinate dehydrogenase cytochrome b subunit signature 2. / Succinate dehydrogenase, cytochrome b556 subunit / Succinate dehydrogenase, flavoprotein subunit / Fumarate reductase/succinate dehydrogenase, transmembrane subunit ...Single helix bin / Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, CybS / CybS, succinate dehydrogenase cytochrome B small subunit / succinate dehydrogenase protein domain / Succinate dehydrogenase, cytochrome b subunit, conserved site / Succinate dehydrogenase cytochrome b subunit signature 1. / Succinate dehydrogenase cytochrome b subunit signature 2. / Succinate dehydrogenase, cytochrome b556 subunit / Succinate dehydrogenase, flavoprotein subunit / Fumarate reductase/succinate dehydrogenase, transmembrane subunit / Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit / Succinate dehydrogenase/Fumarate reductase transmembrane subunit / Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain / Alpha-helical ferredoxin / Fumarate Reductase Iron-sulfur Protein; Chain B, domain 2 / Fumarate reductase/succinate dehydrogenase, transmembrane subunit / : / Succinate dehydrogenase/fumarate reductase, flavoprotein subunit / Fumarate reductase/succinate dehydrogenase, FAD-binding site / Fumarate reductase / succinate dehydrogenase FAD-binding site. / FAD-dependent oxidoreductase SdhA/FrdA/AprA / 3 helical TM bundles of succinate and fumarate reductases / 4Fe-4S dicluster domain / Flavocytochrome C3; Chain A, domain 1 / Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain / Succinate dehydrogenase/fumarate reductase iron-sulphur protein / Succinate dehydogenase/fumarate reductase N-terminal / 2Fe-2S iron-sulfur cluster binding domain / Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal / Fumarate reductase flavoprotein C-term / Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain superfamily / Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain superfamily / FAD-dependent oxidoreductase 2, FAD binding domain / Alpha-helical ferredoxin / FAD binding domain / Rhinovirus 14, subunit 4 / 2Fe-2S ferredoxin, iron-sulphur binding site / 2Fe-2S ferredoxin-type iron-sulfur binding region signature. / Beta-grasp domain / Beta-grasp domain superfamily / 2Fe-2S ferredoxin-type iron-sulfur binding domain profile. / 2Fe-2S ferredoxin-type iron-sulfur binding domain / 2Fe-2S ferredoxin-like superfamily / FAD/NAD(P)-binding domain / FAD/NAD(P)-binding domain / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / Single alpha-helices involved in coiled-coils or other helix-helix interfaces / 3-Layer(bba) Sandwich / Ubiquitin-like (UB roll) / FAD/NAD(P)-binding domain superfamily / Few Secondary Structures / Irregular / Roll / Alpha-Beta Complex / Up-down Bundle / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-EPH / FE3-S4 CLUSTER / N-biphenyl-3-yl-2-(trifluoromethyl)benzamide / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / MALONATE ION / IRON/SULFUR CLUSTER / Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial / Succinate dehydrogenase cytochrome b560 subunit, mitochondrial ...Chem-EPH / FE3-S4 CLUSTER / N-biphenyl-3-yl-2-(trifluoromethyl)benzamide / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / MALONATE ION / IRON/SULFUR CLUSTER / Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial / Succinate dehydrogenase cytochrome b560 subunit, mitochondrial / Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial / Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
Similarity search - Component
Biological speciesSus scrofa (pig)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.24 Å
AuthorsHarada, S. / Sasaki, T. / Shindo, M. / Kido, Y. / Inaoka, D.K. / Omori, J. / Osanai, A. / Sakamoto, K. / Mao, J. / Matsuoka, S. ...Harada, S. / Sasaki, T. / Shindo, M. / Kido, Y. / Inaoka, D.K. / Omori, J. / Osanai, A. / Sakamoto, K. / Mao, J. / Matsuoka, S. / Inoue, M. / Honma, T. / Tanaka, A. / Kita, K.
CitationJournal: Int J Mol Sci / Year: 2015
Title: Structural Insights into the Molecular Design of Flutolanil Derivatives Targeted for Fumarate Respiration of Parasite Mitochondria
Authors: Inaoka, D.K. / Shiba, T. / Sato, D. / Balogun, E.O. / Sasaki, T. / Nagahama, M. / Oda, M. / Matsuoka, S. / Ohmori, J. / Honma, T. / Inoue, M. / Kita, K. / Harada, S.
History
DepositionDec 22, 2009Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 9, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Aug 5, 2015Group: Database references
Revision 1.3Oct 11, 2017Group: Refinement description / Category: software
Revision 1.4Nov 1, 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_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.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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id
Revision 1.5Oct 23, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial
B: Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
C: Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
D: Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
hetero molecules


Theoretical massNumber of molelcules
Total (without water)126,69712
Polymers123,3184
Non-polymers3,3798
Water00
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area12710 Å2
ΔGint-52 kcal/mol
Surface area42210 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.702, 84.170, 294.432
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Succinate dehydrogenase [ubiquinone] ... , 3 types, 3 molecules ABD

#1: Protein Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial / Flavoprotein subunit of complex II / Fp


Mass: 68313.172 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: heart / Tissue: muscle / References: UniProt: Q0QF01, succinate dehydrogenase
#2: Protein Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial / Iron-sulfur subunit of complex II / Ip


Mass: 28764.217 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: heart / Tissue: muscle / References: UniProt: Q007T0, succinate dehydrogenase
#4: Protein Succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial / Succinate-ubiquinone oxidoreductase cytochrome b small subunit / CybS / Succinate-ubiquinone ...Succinate-ubiquinone oxidoreductase cytochrome b small subunit / CybS / Succinate-ubiquinone reductase membrane anchor subunit / QPs3 / CII-4 / Succinate dehydrogenase complex subunit D


Mass: 10936.758 Da / Num. of mol.: 1 / Fragment: residues 57-159 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: heart / Tissue: muscle / References: UniProt: A5GZW8

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Protein , 1 types, 1 molecules C

#3: Protein Succinate dehydrogenase cytochrome b560 subunit, mitochondrial / Succinate-ubiquinone oxidoreductase cytochrome B large subunit / CYBL


Mass: 15304.081 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Sus scrofa (pig) / Organ: heart / Tissue: muscle / References: UniProt: D0VWV4

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Non-polymers , 8 types, 8 molecules

#5: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#6: Chemical ChemComp-MLI / MALONATE ION


Mass: 102.046 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H2O4
#7: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER


Mass: 175.820 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe2S2
#8: Chemical ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe4S4
#9: Chemical ChemComp-F6A / N-biphenyl-3-yl-2-(trifluoromethyl)benzamide


Mass: 341.326 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C20H14F3NO
#10: Chemical ChemComp-F3S / FE3-S4 CLUSTER


Mass: 295.795 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Fe3S4
#11: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#12: Chemical ChemComp-EPH / L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE


Mass: 709.933 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C39H68NO8P / Comment: phospholipid*YM

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Details

Compound detailsTHESE COMPLEX FORMS MITOCHONDRIAL RESPIRATORY COMPLEX II.
Has protein modificationY
Sequence detailsTHE SEQUENCE OF CHAIN D IS REFERRED IN REF 2 IN A5GZW8, UNIPROT.

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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: 3.6 Å3/Da / Density % sol: 65.86 % / Mosaicity: 0.62 °
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.4
Details: 25mM HEPES-NAOH, 7% PEG 4000, 200mM Sucrose, 100mM NaCl, 10mM CaCl2, 0.5mM EDTA, 3% 1,6-haxanediol, 0.5% n-decyl-beta-D-maltoside, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: AR-NW12A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Dec 8, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.2→50 Å / Num. obs: 29008 / % possible obs: 99.8 % / Redundancy: 4.8 % / Rmerge(I) obs: 0.076 / Χ2: 1.04 / Net I/σ(I): 19.333
Reflection shellResolution: 3.2→3.31 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.277 / Mean I/σ(I) obs: 5.22 / Num. unique all: 2822 / Χ2: 0.965 / % possible all: 100

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation3.46 Å37.63 Å
Translation3.46 Å37.63 Å

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Processing

Software
NameVersionClassificationNB
DENZOdata reduction
SCALEPACKdata scaling
MOLREPphasing
REFMACrefinement
PDB_EXTRACT3.005data extraction
HKL-2000data collection
HKL-2000data reduction
HKL-2000data scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1ZOY

1zoy


Resolution: 3.24→37.63 Å / Cor.coef. Fo:Fc: 0.921 / Cor.coef. Fo:Fc free: 0.882 / WRfactor Rfree: 0.243 / WRfactor Rwork: 0.194 / Occupancy max: 1 / Occupancy min: 0.5 / FOM work R set: 0.815 / SU B: 45.584 / SU ML: 0.377 / SU R Cruickshank DPI: 0.38 / SU Rfree: 0.47 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.47 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : RESIDUAL ONLY
RfactorNum. reflection% reflectionSelection details
Rfree0.253 1474 5.1 %RANDOM
Rwork0.203 ---
obs0.206 28950 98.71 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso max: 102.27 Å2 / Biso mean: 70.868 Å2 / Biso min: 2 Å2
Baniso -1Baniso -2Baniso -3
1-0.33 Å20 Å20 Å2
2--0.27 Å20 Å2
3----0.59 Å2
Refinement stepCycle: LAST / Resolution: 3.24→37.63 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8480 0 191 0 8671
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0070.0228876
X-RAY DIFFRACTIONr_angle_refined_deg1.0751.99312035
X-RAY DIFFRACTIONr_dihedral_angle_1_deg4.96151088
X-RAY DIFFRACTIONr_dihedral_angle_2_deg33.86223.413375
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.073151469
X-RAY DIFFRACTIONr_dihedral_angle_4_deg15.2681559
X-RAY DIFFRACTIONr_chiral_restr0.0750.21305
X-RAY DIFFRACTIONr_gen_planes_refined0.0030.0216667
X-RAY DIFFRACTIONr_mcbond_it0.171.55412
X-RAY DIFFRACTIONr_mcangle_it0.32328677
X-RAY DIFFRACTIONr_scbond_it0.42933464
X-RAY DIFFRACTIONr_scangle_it0.7644.53341
LS refinement shellResolution: 3.236→3.319 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.37 86 -
Rwork0.281 1659 -
all-1745 -
obs-1745 83.97 %
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)
12.0704-0.416-0.51.5091-0.10073.63780.0286-0.154-0.0243-0.088-0.042-0.03920.0253-0.00190.01330.019-0.05230.02670.17020.04580.4976-17.544-21.22818.164
21.4238-0.4831-0.07281.119-0.46083.23750.0153-0.05580.0622-0.0065-0.03630.013-0.34170.1180.0210.0743-0.09530.03290.16440.01460.5106-15.69-16.07418.049
34.09020.6824-1.25744.2308-1.08344.10370.4766-0.14080.74760.4196-0.11450.0462-1.41250.2632-0.3620.5563-0.11410.10990.0204-0.04110.6471-19.3659.08223.542
40.87510.1136-0.071.23280.03541.56230.13460.17960.1321-0.1396-0.17260.0982-0.4727-0.04570.0380.2416-0.04730.0530.27320.06250.5779-13.821-12.31614.228
52.8705-0.0939-0.66932.9555-0.64432.30350.0188-0.32450.0826-0.1877-0.1449-0.492-0.23851.15110.12620.0639-0.18110.06220.6720.09040.50166.52-15.15520.668
62.2208-0.61310.01471.1837-0.58393.98930.11050.16240.4792-0.2946-0.2162-0.3076-0.8190.6640.10570.3383-0.1660.07050.23450.0640.5165-4.537-6.4185.039
72.5240.0933-0.4932-3.61653.19733.9907-0.3715-0.7381-0.1936-0.00880.5177-0.3307-0.56961.7306-0.14620.3799-0.3032-0.1031.3080.12550.82063.443-13.34648.948
86.472-1.4058-2.60284.9471.28640.17980.0924-0.17350.4572-0.38510.0816-0.2862-0.15860.3556-0.17390.2705-0.2817-0.02970.77590.08360.5803-4.233-11.32640.407
91.312-1.2812-0.45572.6573-0.64862.68660.1894-0.73430.49820.171-0.23720.0898-0.49570.77590.04790.3853-0.30980.01280.7656-0.15440.6957-7.842-12.73749.511
103.8294-1.03920.57340.8379-0.84254.93040.24060.1012-0.1073-0.015-0.12020.15760.2899-0.138-0.12050.1282-0.04150.05730.0806-0.01810.5454-27.018-23.41736.135
110.66360.3978-2.01120.317-0.97967.6114-0.25080.13980.09530.159-0.05810.35110.9015-0.80.30890.4354-0.1110.17070.2981-0.08740.7435-32.589-27.35942.359
121.2667-2.5738-1.55913.5618-1.96586.87040.17730.14440.2083-0.0684-0.0280.0927-0.229-0.79-0.14930.2458-0.01820.10850.1814-0.11860.6539-33.491-21.07546.464
134.55383.27253.735711.02936.28567.11490.29960.13660.11731.1356-0.6052-0.03571.73290.92770.30560.5870.18460.12450.52340.1820.7621-11.737-31.04247.18
141.92151.18921.05212.82781.50810.379-0.0246-0.2590.10130.4628-0.04320.21520.0590.07730.06780.5312-0.03080.23750.11360.01950.6094-30.082-29.73174.21
151.52374.9128-4.22389.02241.151715.65530.2298-0.863-0.12330.443-0.6565-0.0394-0.63440.67990.42670.89380.0397-0.07580.71930.07780.8394-33.962-27.195.039
160.73151.4759-4.31763.7389-3.451511.97150.3558-0.18950.07040.4229-0.3132-0.1555-1.22090.8565-0.04270.48870.00630.10910.1459-0.01220.6718-34.651-17.67567.32
173.8105-1.76343.197.91684.070.3666-0.03620.0583-0.05110.04310.0970.1801-0.30130.014-0.06080.7496-0.11710.24780.0907-0.06350.5257-34.436-11.10471.936
180.99312.14722.10993.7563-1.47487.7486-0.42510.0671-0.2024-0.04930.19080.037-0.1577-0.6470.23430.6199-0.04080.34430.4155-0.0340.9675-45.48-29.68766.869
198.42842.1526-2.68540.5457-2.693510.6262-0.239-0.3749-0.7702-0.1668-0.2356-0.15060.66430.99910.47460.4626-0.04950.13530.16740.00390.7244-30.936-36.01863.741
202.1829-2.8345-3.5329.55042.04036.92230.0254-0.2503-0.0849-0.3846-0.1257-0.29560.4792-0.12490.10030.5117-0.05530.06850.29550.07060.738-37.106-42.22274.937
210.3316-6.9381-2.7026-9.41436.0939-2.39870.3578-0.9051-0.12220.2862-0.76871.0342-1.704-0.47770.41091.98190.02130.16341.1743-0.20061.0453-42.532-26.43288.334
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A10 - 85
2X-RAY DIFFRACTION2A86 - 260
3X-RAY DIFFRACTION3A261 - 344
4X-RAY DIFFRACTION4A345 - 430
5X-RAY DIFFRACTION5A431 - 511
6X-RAY DIFFRACTION6A512 - 622
7X-RAY DIFFRACTION7B9 - 40
8X-RAY DIFFRACTION8B41 - 79
9X-RAY DIFFRACTION9B80 - 109
10X-RAY DIFFRACTION10B110 - 177
11X-RAY DIFFRACTION11B178 - 219
12X-RAY DIFFRACTION12B220 - 247
13X-RAY DIFFRACTION13C6 - 35
14X-RAY DIFFRACTION14C36 - 68
15X-RAY DIFFRACTION15C69 - 88
16X-RAY DIFFRACTION16C89 - 120
17X-RAY DIFFRACTION17C121 - 143
18X-RAY DIFFRACTION18D35 - 72
19X-RAY DIFFRACTION19D73 - 96
20X-RAY DIFFRACTION20D97 - 124
21X-RAY DIFFRACTION21D125 - 136

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