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- PDB-2wdv: E. coli succinate:quinone oxidoreductase (SQR) with an empty quin... -

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Basic information

Entry
Database: PDB / ID: 2wdv
TitleE. coli succinate:quinone oxidoreductase (SQR) with an empty quinone- binding pocket
Components(SUCCINATE DEHYDROGENASE ...) x 4
KeywordsOXIDOREDUCTASE / SUCCINATE DEHYDROGENASE ACTIVITY / CELL INNER MEMBRANE / TRICARBOXYLIC ACID CYCLE / METAL-BINDING / TRANSMEMBRANE / FLAVOPROTEIN / ELECTRON TRANSPORT
Function / homology
Function and homology information


plasma membrane succinate dehydrogenase complex / succinate dehydrogenase complex / succinate dehydrogenase activity / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / cytochrome complex assembly / aerobic electron transport chain / oxidoreductase activity, acting on the CH-CH group of donors / anaerobic respiration / 3 iron, 4 sulfur cluster binding ...plasma membrane succinate dehydrogenase complex / succinate dehydrogenase complex / succinate dehydrogenase activity / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / cytochrome complex assembly / aerobic electron transport chain / oxidoreductase activity, acting on the CH-CH group of donors / anaerobic respiration / 3 iron, 4 sulfur cluster binding / iron-sulfur cluster binding / ubiquinone binding / aerobic respiration / tricarboxylic acid cycle / respiratory electron transport chain / 2 iron, 2 sulfur cluster binding / flavin adenine dinucleotide binding / 4 iron, 4 sulfur cluster binding / electron transfer activity / heme binding / membrane / metal ion binding / plasma membrane
Similarity search - Function
Succinate dehydrogenase, hydrophobic membrane anchor / succinate dehydrogenase protein domain / Succinate dehydrogenase, cytochrome b556 subunit / Succinate dehydrogenase, cytochrome b subunit, conserved site / Succinate dehydrogenase cytochrome b subunit signature 1. / Succinate dehydrogenase cytochrome b subunit signature 2. / Succinate dehydrogenase, flavoprotein subunit / Fumarate reductase/succinate dehydrogenase, transmembrane subunit / Succinate dehydrogenase/fumarate reductase type B, transmembrane subunit / Succinate dehydrogenase/Fumarate reductase transmembrane subunit ...Succinate dehydrogenase, hydrophobic membrane anchor / succinate dehydrogenase protein domain / Succinate dehydrogenase, cytochrome b556 subunit / Succinate dehydrogenase, cytochrome b subunit, conserved site / Succinate dehydrogenase cytochrome b subunit signature 1. / Succinate dehydrogenase cytochrome b subunit signature 2. / 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 / FAD-dependent oxidoreductase SdhA/FrdA/AprA / Fumarate reductase / succinate dehydrogenase FAD-binding site. / 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 / 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 / 4Fe-4S ferredoxin, iron-sulphur binding, conserved site / 4Fe-4S ferredoxin-type iron-sulfur binding region signature. / FAD/NAD(P)-binding domain / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / FAD/NAD(P)-binding domain / 4Fe-4S ferredoxin-type, iron-sulphur binding domain / Methane Monooxygenase Hydroxylase; Chain G, domain 1 / 3-Layer(bba) Sandwich / FAD/NAD(P)-binding domain superfamily / Ubiquitin-like (UB roll) / Few Secondary Structures / Irregular / Roll / Alpha-Beta Complex / Up-down Bundle / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
FE3-S4 CLUSTER / FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / PROTOPORPHYRIN IX CONTAINING FE / IRON/SULFUR CLUSTER / MALATE LIKE INTERMEDIATE / Succinate dehydrogenase iron-sulfur subunit / Succinate dehydrogenase flavoprotein subunit / Succinate dehydrogenase hydrophobic membrane anchor subunit / Succinate dehydrogenase cytochrome b556 subunit
Similarity search - Component
Biological speciesESCHERICHIA COLI (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / OTHER / Resolution: 3.2 Å
AuthorsRuprecht, J. / Yankovskaya, V. / Maklashina, E. / Iwata, S. / Cecchini, G.
CitationJournal: J.Biol.Chem. / Year: 2009
Title: Structure of Escherichia Coli Succinate:Quinone Oxidoreductase with an Occupied and Empty Quinone- Binding Site.
Authors: Ruprecht, J. / Yankovskaya, V. / Maklashina, E. / Iwata, S. / Cecchini, G.
History
DepositionMar 26, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 25, 2009Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Advisory / Version format compliance
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
B: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
C: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
D: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN
E: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
F: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
G: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
H: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN
I: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
J: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
K: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
L: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)362,61533
Polymers355,47412
Non-polymers7,14121
Water0
1
A: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
B: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
C: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
D: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,87211
Polymers118,4914
Non-polymers2,3807
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14800 Å2
ΔGint-153.8 kcal/mol
Surface area38290 Å2
MethodPISA
2
E: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
F: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
G: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
H: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,87211
Polymers118,4914
Non-polymers2,3807
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14780 Å2
ΔGint-156.31 kcal/mol
Surface area38350 Å2
MethodPISA
3
I: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
J: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
K: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
L: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN
hetero molecules


Theoretical massNumber of molelcules
Total (without water)120,87211
Polymers118,4914
Non-polymers2,3807
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14830 Å2
ΔGint-158.79 kcal/mol
Surface area38330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)120.340, 184.847, 204.720
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11A
21E
31I
12B
22F
32J
13C
23G
33K
14D
24H
34L

NCS domain segments:
Dom-IDComponent-IDEns-IDRefine codeAuth asym-IDAuth seq-ID
1111A1 - 588
2111E1 - 588
3111I1 - 588
1121B1 - 238
2121F1 - 238
3121J1 - 238
1131C8 - 128
2131G8 - 128
3131K8 - 128
1141D11 - 115
2141H11 - 115
3141L11 - 115

NCS ensembles :
ID
1
2
3
4

NCS oper:
IDCodeMatrixVector
1given(0.947, 0.28, 0.158), (0.275, -0.453, -0.848), (-0.166, 0.847, -0.506)18.60481, -98.21925, -30.48576
2given(0.947, 0.283, -0.154), (0.275, -0.46, 0.844), (0.168, -0.842, -0.513)4.62437, -24.23799, -102.70898
3given(0.949, 0.277, 0.151), (0.268, -0.455, -0.849), (-0.166, 0.847, -0.506)18.35585, -98.17055, -30.53743
4given(0.945, 0.28, -0.167), (0.285, -0.461, 0.84), (0.158, -0.842, -0.516)4.30147, -24.56494, -102.51515
5given(0.948, 0.282, 0.151), (0.268, -0.446, -0.854), (-0.173, 0.849, -0.499)18.53692, -98.29104, -29.98937
6given(0.943, 0.282, -0.18), (0.296, -0.455, 0.84), (0.155, -0.845, -0.512)4.08289, -24.80969, -102.36908
7given(0.947, 0.285, 0.15), (0.269, -0.447, -0.853), (-0.176, 0.848, -0.5)18.58489, -98.35662, -29.94057
8given(0.945, 0.277, -0.176), (0.289, -0.449, 0.846), (0.155, -0.85, -0.504)4.00906, -24.09944, -102.11641

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Components

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SUCCINATE DEHYDROGENASE ... , 4 types, 12 molecules AEIBFJCGKDHL

#1: Protein SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT


Mass: 64502.766 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: FAD ATOM C8M IS COVALENTLY LINKED TO NE2 OF SDHA HIS45
Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PFAS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): DW35
References: UniProt: P0AC41, succinate dehydrogenase, succinate dehydrogenase
#2: Protein SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT


Mass: 26800.912 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PFAS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): DW35
References: UniProt: P07014, succinate dehydrogenase, succinate dehydrogenase
#3: Protein SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT


Mass: 14313.100 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: RESIDUES 8-128 MODELLED / Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PFAS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): DW35 / References: UniProt: P69054, succinate dehydrogenase
#4: Protein SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN


Mass: 12874.438 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: RESIDUES 11-115 MODELLED / Source: (gene. exp.) ESCHERICHIA COLI (E. coli) / Plasmid: PFAS / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): DW35 / References: UniProt: P0AC44, succinate dehydrogenase

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Non-polymers , 7 types, 21 molecules

#5: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE / Flavin adenine dinucleotide


Mass: 785.550 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM
#6: Chemical ChemComp-TEO / MALATE LIKE INTERMEDIATE


Mass: 132.072 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C4H4O5
#7: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Na
#8: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Fe2S2
#9: Chemical ChemComp-SF4 / IRON/SULFUR CLUSTER / Iron–sulfur cluster


Mass: 351.640 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Fe4S4
#10: Chemical ChemComp-F3S / FE3-S4 CLUSTER / Iron–sulfur cluster


Mass: 295.795 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Fe3S4
#11: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C34H32FeN4O4

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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: 3.16 Å3/Da / Density % sol: 61.1 % / Description: NONE
Crystal growpH: 8.5 / Details: 0.1M TRIS PH 8.5, 0.1M MGSO4, 10% PEG4000

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.9762
DetectorType: ADSC CCD / Detector: CCD / Date: Feb 17, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9762 Å / Relative weight: 1
ReflectionResolution: 3.2→52.85 Å / Num. obs: 76081 / % possible obs: 99.8 % / Observed criterion σ(I): 6 / Redundancy: 3.6 % / Rmerge(I) obs: 0.15 / Net I/σ(I): 8.7
Reflection shellResolution: 3.2→3.37 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.7 / Mean I/σ(I) obs: 2.2 / % possible all: 100

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Processing

Software
NameVersionClassification
REFMAC5.4.0067refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: OTHER / Resolution: 3.2→51.85 Å / Cor.coef. Fo:Fc: 0.912 / Cor.coef. Fo:Fc free: 0.884 / SU B: 40.751 / SU ML: 0.334 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.447 / Stereochemistry target values: MAXIMUM LIKELIHOOD
Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DENSITY FOR THE N-TERMINUS OF SDH C (RESIDUES 1-7 OF CHAINS C, G, K) AND THE N-TERMINUS OF SDHD (RESIDUES 1-10 OF CHAINS D, H AND L) WAS ...Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. DENSITY FOR THE N-TERMINUS OF SDH C (RESIDUES 1-7 OF CHAINS C, G, K) AND THE N-TERMINUS OF SDHD (RESIDUES 1-10 OF CHAINS D, H AND L) WAS WEAK AND THESE REGIONS ARE NOT INCLUDED IN THE MODEL. THE SIDE CHAIN OF SDHD TRP113 IS TRUNCATED AT THE CBETA ATOM SINCE DENSITY FOR THE SIDE CHAIN WAS POOR.
RfactorNum. reflection% reflectionSelection details
Rfree0.233 3844 5.1 %SELECTED TO BE IDENTICAL TO 2WDQ
Rwork0.205 ---
obs0.206 71862 99.7 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK
Displacement parametersBiso mean: 54.96 Å2
Baniso -1Baniso -2Baniso -3
1--4.71 Å20 Å20 Å2
2--1.74 Å20 Å2
3---2.97 Å2
Refinement stepCycle: LAST / Resolution: 3.2→51.85 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24480 0 375 0 24855
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.02225458
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2641.98734521
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.28153144
X-RAY DIFFRACTIONr_dihedral_angle_2_deg35.59723.3881107
X-RAY DIFFRACTIONr_dihedral_angle_3_deg16.194154200
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.78915192
X-RAY DIFFRACTIONr_chiral_restr0.0860.23831
X-RAY DIFFRACTIONr_gen_planes_refined0.0040.02119194
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.1491.515636
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.284225125
X-RAY DIFFRACTIONr_mcangle_other
X-RAY DIFFRACTIONr_scbond_it1.06739822
X-RAY DIFFRACTIONr_scbond_other
X-RAY DIFFRACTIONr_scangle_it0.9694.59345
X-RAY DIFFRACTIONr_scangle_other
X-RAY DIFFRACTIONr_long_range_B_refined
X-RAY DIFFRACTIONr_long_range_B_other
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
Refine LS restraints NCS

Refine-ID: X-RAY DIFFRACTION

Ens-IDDom-IDAuth asym-IDNumberTypeRms dev position (Å)Weight position
11A4522tight positional0.050.05
12E4522tight positional0.040.05
13I4522tight positional0.040.05
21B1869tight positional0.050.05
22F1869tight positional0.040.05
23J1869tight positional0.050.05
31C933tight positional0.030.05
32G933tight positional0.030.05
33K933tight positional0.030.05
41D836tight positional0.030.05
42H836tight positional0.030.05
43L836tight positional0.030.05
11A4522tight thermal0.070.5
12E4522tight thermal0.050.5
13I4522tight thermal0.060.5
21B1869tight thermal0.080.5
22F1869tight thermal0.060.5
23J1869tight thermal0.080.5
31C933tight thermal0.050.5
32G933tight thermal0.040.5
33K933tight thermal0.040.5
41D836tight thermal0.040.5
42H836tight thermal0.040.5
43L836tight thermal0.040.5
LS refinement shellResolution: 3.2→3.28 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.326 302 -
Rwork0.32 5146 -
obs--99.02 %
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)
11.6518-0.06420.21551.8317-0.24811.7933-0.009-0.00720.17080.2507-0.02320.3548-0.0659-0.20920.0322-0.36430.01940.0704-0.46760.0225-0.31441.1817-11.1648-24.1821
22.574-0.22570.14472.9805-0.86861.765-0.02720.23240.35380.1835-0.0513-0.3341-0.09630.22420.0785-0.4505-0.0093-0.0559-0.38740.0545-0.44528.6109-8.285-30.4189
35.5934-0.87921.09591.847-0.01220.9684-0.13210.10580.76920.15740.0182-0.73520.00280.18980.1139-0.1857-0.0231-0.061-0.1330.03950.227260.6526-4.6393-31.233
43.1971-0.8135-0.49372.2423-1.56843.0802-0.11050.56110.2281-0.147-0.1091-0.8024-0.01020.60090.2196-0.30360.01570.0151-0.09530.07230.23567.0129-17.0052-37.6872
51.83140.28090.45551.82220.45211.85950.21460.0094-0.39460.4491-0.06770.18150.3681-0.0729-0.1469-0.0502-0.0339-0.1092-0.384-0.0874-0.194512.7809-72.3481-27.918
62.3080.3840.0312.16230.18892.1910.09920.1006-0.18670.3819-0.0048-0.45730.30270.3108-0.0944-0.17280.0766-0.2356-0.3892-0.1789-0.205838.609-60.9153-26.9317
75.52251.6564-2.1182.1459-0.43661.9480.1096-0.1072-0.77930.0661-0.1973-0.96790.25250.45130.0877-0.06020.2344-0.3356-0.0436-0.08530.511770.0012-53.2979-28.8563
81.8090.6264-0.13722.26810.56393.94550.15090.5080.002-0.11830.0603-1.0483-0.04330.7103-0.2111-0.25770.1149-0.10970.0458-0.05470.440871.5438-40.5794-37.3377
92.0132-0.0080.10972.11970.32081.32250.02161.12290.058-0.75710.12010.4649-0.0168-0.3565-0.14170.3070.1558-0.25111.19150.07740.02956.3377-39.2263-80.7045
102.81940.65290.09262.461-0.08772.04590.00631.1639-0.1288-0.73660.1668-0.1736-0.00810.0475-0.17320.12740.16070.01420.80590.0033-0.24534.1106-38.1841-75.306
114.86841.88230.74542.633-0.03251.5682-0.18751.48280.0323-0.59730.3723-0.4737-0.15890.4707-0.18480.28680.06890.3071.1613-0.07170.014865.5097-30.9972-73.0719
121.95610.02250.89614.14680.39351.7033-0.17850.7128-0.2114-0.2420.2082-1.016-0.12320.5688-0.0297-0.080.05570.19530.6749-0.09020.144769.2446-29.0338-58.2938
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A1 - 588
2X-RAY DIFFRACTION2B1 - 238
3X-RAY DIFFRACTION3C8 - 128
4X-RAY DIFFRACTION4D11 - 115
5X-RAY DIFFRACTION5E1 - 588
6X-RAY DIFFRACTION6F1 - 238
7X-RAY DIFFRACTION7G8 - 128
8X-RAY DIFFRACTION8H11 - 115
9X-RAY DIFFRACTION9I1 - 588
10X-RAY DIFFRACTION10J1 - 238
11X-RAY DIFFRACTION11K8 - 128
12X-RAY DIFFRACTION12L11 - 115

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