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- PDB-2wu5: Crystal structure of the E. coli succinate:quinone oxidoreductase... -

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Basic information

Entry
Database: PDB / ID: 2wu5
TitleCrystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhD His71Met mutant
Components(SUCCINATE DEHYDROGENASE ...) x 4
KeywordsOXIDOREDUCTASE / CELL INNER MEMBRANE / TRICARBOXYLIC ACID CYCLE / METAL-BINDING / TRANSMEMBRANE / TRANSPORT / FLAVOPROTEIN / ELECTRON TRANSPORT
Function / homology
Function and homology information


: / : / succinate dehydrogenase activity / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / cytochrome complex assembly / oxidoreductase activity, acting on the CH-CH group of donors / aerobic electron transport chain / anaerobic respiration / 3 iron, 4 sulfur cluster binding ...: / : / succinate dehydrogenase activity / succinate dehydrogenase / succinate dehydrogenase (quinone) activity / cytochrome complex assembly / oxidoreductase activity, acting on the CH-CH group of donors / aerobic electron transport chain / anaerobic respiration / 3 iron, 4 sulfur cluster binding / iron-sulfur cluster binding / ubiquinone binding / tricarboxylic acid cycle / aerobic respiration / 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 / FAD/NAD(P)-binding domain / 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. / 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
Chem-CBE / 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 / MOLECULAR REPLACEMENT / Resolution: 2.803 Å
AuthorsRuprecht, J. / Yankovskaya, V. / Maklashina, E. / Iwata, S. / Cecchini, G.
CitationJournal: To be Published
Title: Crystal Structure of the E. Coli Succinate:Quinone Oxidoreductase (Sqr) Sdhd His71met Mutant
Authors: Ruprecht, J. / Yankovskaya, V. / Maklashina, E. / Iwata, S. / Cecchini, G.
History
DepositionSep 29, 2009Deposition site: PDBE / Processing site: PDBE
Revision 1.0Aug 25, 2010Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Nov 20, 2019Group: Advisory / Derived calculations / Other
Category: pdbx_database_status / pdbx_struct_conn_angle ...pdbx_database_status / pdbx_struct_conn_angle / pdbx_validate_close_contact / struct_conn / struct_conn_type
Item: _pdbx_database_status.status_code_sf / _struct_conn_type.id
Revision 1.4Dec 20, 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 / 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 / _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
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 SUBUNIT
E: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
F: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
G: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
H: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN SUBUNIT
I: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
J: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
K: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
L: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)363,30036
Polymers355,45312
Non-polymers7,84724
Water3,999222
1
E: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
F: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
G: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
H: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,10012
Polymers118,4844
Non-polymers2,6168
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15570 Å2
ΔGint-158.6 kcal/mol
Surface area38130 Å2
MethodPISA
2
A: SUCCINATE DEHYDROGENASE FLAVOPROTEIN SUBUNIT
B: SUCCINATE DEHYDROGENASE IRON-SULFUR SUBUNIT
C: SUCCINATE DEHYDROGENASE CYTOCHROME B556 SUBUNIT
D: SUCCINATE DEHYDROGENASE HYDROPHOBIC MEMBRANE ANCHOR PROTEIN SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,10012
Polymers118,4844
Non-polymers2,6168
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15630 Å2
ΔGint-158.1 kcal/mol
Surface area38020 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 SUBUNIT
hetero molecules


Theoretical massNumber of molelcules
Total (without water)121,10012
Polymers118,4844
Non-polymers2,6168
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area15500 Å2
ΔGint-158.4 kcal/mol
Surface area38160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)120.060, 183.820, 203.420
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-ID
11
21
31
12
22
32
13
23
33
14
24
34

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 1:588 )
211CHAIN E AND (RESSEQ 1:588 )
311CHAIN I AND (RESSEQ 1:588 )
112CHAIN B AND (RESSEQ 1:238 )
212CHAIN F AND (RESSEQ 1:238 )
312CHAIN J AND (RESSEQ 1:238 )
113CHAIN C AND (RESSEQ 8:129 )
213CHAIN G AND (RESSEQ 8:129 )
313CHAIN K AND (RESSEQ 8:129 )
114CHAIN D AND (RESSEQ 11:115 )
214CHAIN H AND (RESSEQ 11:115 )
314CHAIN L AND (RESSEQ 11:115 )

NCS ensembles :
ID
1
2
3
4

NCS oper:
IDCodeMatrixVector
1given(0.948352, 0.261599, -0.179427), (0.28616, -0.461406, 0.839772), (0.136895, -0.847744, -0.512435)3.59932, -25.5496, -101.224
2given(0.949003, 0.27519, 0.153833), (0.270737, -0.461337, -0.844908), (-0.161541, 0.843468, -0.512315)19.2963, -99.1376, -30.5321
3given(0.950821, 0.253151, -0.178478), (0.281291, -0.464491, 0.839716), (0.129673, -0.848624, -0.512857)2.96397, -25.5265, -101.121
4given(0.948528, 0.284187, 0.139759), (0.263207, -0.462001, -0.846922), (-0.176116, 0.840115, -0.51302)18.5433, -99.0898, -30.3104
5given(0.949935, 0.251144, -0.185877), (0.285784, -0.457918, 0.841807), (0.126299, -0.852782, -0.506765)2.568, -25.2997, -100.961
6given(0.945986, 0.296256, 0.13169), (0.262476, -0.461407, -0.847473), (-0.190306, 0.836263, -0.514245)18.3815, -98.9944, -29.9682
7given(0.950258, 0.249125, -0.186939), (0.285201, -0.454751, 0.843719), (0.125181, -0.855066, -0.503182)2.4106, -25.0807, -100.946
8given(0.947171, 0.292875, 0.130732), (0.257585, -0.451779, -0.854135), (-0.191093, 0.842686, -0.503352)18.1219, -98.7966, -29.0938

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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 / CYTOCHROME B-556


Mass: 14313.100 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: RESIDUES 8-129 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 SUBUNIT


Mass: 12867.486 Da / Num. of mol.: 3 / Mutation: YES
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 , 9 types, 246 molecules

#5: Chemical ChemComp-FAD / 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


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


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


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


Mass: 616.487 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#12: Chemical ChemComp-CBE / 2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE / 5,6-DIHYDRO-2-METHYL-1,4-OXATHIIN-3-CARBOXANILID / CARBOXIN / CBX


Mass: 235.302 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C12H13NO2S
#13: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 222 / Source method: isolated from a natural source / Formula: H2O

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Details

Compound detailsENGINEERED RESIDUE IN CHAIN D, HIS 71 TO MET ENGINEERED RESIDUE IN CHAIN H, HIS 71 TO MET ...ENGINEERED RESIDUE IN CHAIN D, HIS 71 TO MET ENGINEERED RESIDUE IN CHAIN H, HIS 71 TO MET ENGINEERED RESIDUE IN CHAIN L, HIS 71 TO MET

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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: 3.12 Å3/Da / Density % sol: 60.57 % / Description: NONE
Crystal growpH: 8.5
Details: 0.1M TRIS PH 8.5, 0.1M MGSO4, 11.5% PEG4000, 1MM CARBOXIN

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID23-1 / Wavelength: 0.97625
DetectorType: ADSC CCD / Detector: CCD / Date: Jul 24, 2008
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 2.8→48.97 Å / Num. obs: 110749 / % possible obs: 99.9 % / Observed criterion σ(I): 6 / Redundancy: 3.7 % / Biso Wilson estimate: 51.32 Å2 / Rmerge(I) obs: 0.1 / Net I/σ(I): 12.2
Reflection shellResolution: 2.8→2.95 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.57 / Mean I/σ(I) obs: 2.9 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
SCALAdata scaling
REFMACphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2WDQ

2wdq


Resolution: 2.803→46.827 Å / SU ML: 0.35 / σ(F): 0.01 / Phase error: 23.76 / Stereochemistry target values: ML
Details: 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. ...Details: 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% reflection
Rfree0.2515 5417 5.1 %
Rwork0.2134 --
obs0.2153 106952 96.49 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 39.97 Å2 / ksol: 0.327 e/Å3
Displacement parameters
Baniso -1Baniso -2Baniso -3
1--18.621 Å2-0 Å2-0 Å2
2---11.3313 Å2-0 Å2
3----3.4983 Å2
Refinement stepCycle: LAST / Resolution: 2.803→46.827 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms24519 0 423 222 25164
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00525555
X-RAY DIFFRACTIONf_angle_d0.56534647
X-RAY DIFFRACTIONf_dihedral_angle_d15.4759240
X-RAY DIFFRACTIONf_chiral_restr0.0393831
X-RAY DIFFRACTIONf_plane_restr0.0024437
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A4522X-RAY DIFFRACTIONPOSITIONAL
12E4522X-RAY DIFFRACTIONPOSITIONAL0.003
13I4522X-RAY DIFFRACTIONPOSITIONAL0.003
21B1869X-RAY DIFFRACTIONPOSITIONAL
22F1869X-RAY DIFFRACTIONPOSITIONAL0.003
23J1869X-RAY DIFFRACTIONPOSITIONAL0.003
31C948X-RAY DIFFRACTIONPOSITIONAL
32G948X-RAY DIFFRACTIONPOSITIONAL0.002
33K948X-RAY DIFFRACTIONPOSITIONAL0.002
41D834X-RAY DIFFRACTIONPOSITIONAL
42H834X-RAY DIFFRACTIONPOSITIONAL0.004
43L834X-RAY DIFFRACTIONPOSITIONAL0.034
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.803-2.83490.36381700.2883024X-RAY DIFFRACTION88
2.8349-2.86820.33331630.26443061X-RAY DIFFRACTION88
2.8682-2.90320.33381620.26363067X-RAY DIFFRACTION89
2.9032-2.93990.33771630.26053177X-RAY DIFFRACTION90
2.9399-2.97860.30581410.25683195X-RAY DIFFRACTION92
2.9786-3.01940.33371890.24993234X-RAY DIFFRACTION93
3.0194-3.06250.31891640.2463216X-RAY DIFFRACTION93
3.0625-3.10820.29161870.24863234X-RAY DIFFRACTION94
3.1082-3.15680.31361740.24783319X-RAY DIFFRACTION95
3.1568-3.20850.28851800.2283300X-RAY DIFFRACTION96
3.2085-3.26380.28871980.22833316X-RAY DIFFRACTION96
3.2638-3.32320.27351930.21793376X-RAY DIFFRACTION97
3.3232-3.38710.26661780.20783385X-RAY DIFFRACTION97
3.3871-3.45620.22421860.2063414X-RAY DIFFRACTION98
3.4562-3.53130.28331870.19983462X-RAY DIFFRACTION99
3.5313-3.61340.22921870.19683424X-RAY DIFFRACTION99
3.6134-3.70380.24041790.18963475X-RAY DIFFRACTION99
3.7038-3.80390.24751840.19293441X-RAY DIFFRACTION99
3.8039-3.91570.22641880.18733507X-RAY DIFFRACTION99
3.9157-4.04210.22392040.19613462X-RAY DIFFRACTION100
4.0421-4.18640.25241710.19733490X-RAY DIFFRACTION100
4.1864-4.3540.2422010.19873498X-RAY DIFFRACTION100
4.354-4.5520.20751800.18383515X-RAY DIFFRACTION100
4.552-4.79170.22961840.18393532X-RAY DIFFRACTION100
4.7917-5.09160.20681870.18643526X-RAY DIFFRACTION100
5.0916-5.48420.23461810.1923548X-RAY DIFFRACTION100
5.4842-6.0350.19781840.20283540X-RAY DIFFRACTION99
6.035-6.90590.23211930.21523551X-RAY DIFFRACTION99
6.9059-8.69160.19631890.19883593X-RAY DIFFRACTION99
8.6916-46.83380.25341700.23843653X-RAY DIFFRACTION96
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)
10.1172-0.02420.04460.66890.13930.31550.02420.1250.03040.1269-0.15430.29320.116-0.10920.04590.01460.02490.00690.02050.07550.04531.5439-11.3503-24.2218
20.5481-0.26820.40220.7038-0.2630.3871-0.05530.3210.20150.0568-0.0514-0.1511-0.00510.24830.1050.0796-0.0254-0.03860.19620.10920.153228.976-8.7535-30.3883
30.10070.03130.31280.8172-0.03760.9898-0.05660.40890.1958-0.0024-0.0473-0.4919-0.03990.31290.12350.1184-0.0624-0.08530.39660.19320.490860.9567-5.701-31.4346
40.0206-0.1061-0.13420.89060.34161.1799-0.09050.42380.0285-0.01960.1637-0.44620.05330.6077-0.05020.0419-0.01270.03050.61390.18870.44667.0466-17.7337-37.9493
50.46490.15570.21951.1080.41480.37210.1679-0.0432-0.44040.58670.04630.27240.103-0.0745-0.10830.2524-0.1222-0.2201-0.1844-0.3149-0.027512.6564-72.3672-27.1661
60.64060.32290.28530.52520.5110.58820.12230.2486-0.18030.20820.0397-0.26320.23030.1435-0.21830.23450.1115-0.21570.2003-0.12220.155238.6248-61.2289-26.8333
70.5037-0.54540.36480.8812-0.23650.35280.02550.27230.06440.0263-0.1275-0.38660.10210.18670.0693-0.09530.2404-0.25250.2238-0.06340.314669.847-53.6098-29.5882
80.3962-0.28440.38232.1750.20550.60980.07480.62140.2217-0.01320.0053-0.93850.11040.3482-0.0853-0.17840.1329-0.23110.39520.00190.354571.4022-41.1047-37.5828
90.80450.03510.12341.41980.08210.00670.1530.90540.2623-1.12990.1486-0.07270.02360.029-0.13420.45940.1837-0.32330.9347-0.0394-0.14525.9018-40.0618-80.1364
100.7781-0.12570.01051.3181-0.25280.04470.15420.7005-0.0982-0.8165-0.0421-0.05540.0651-0.0504-0.0830.41230.19360.07980.9986-0.0664-0.006733.6884-38.8354-75.0103
110.99180.3117-0.91340.2226-0.30120.8426-0.0066-0.0857-0.047-0.22020.0654-0.1643-0.06420.24-0.05810.5580.06460.27251.199-0.01010.556865.036-31.6568-72.7062
120.005-0.06930.01090.7591-0.2850.42720.0679-0.18820.0278-0.1678-0.3393-0.30870.0070.3460.22570.22290.18350.16821.10830.01990.355868.9129-29.756-58.3853
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A
2X-RAY DIFFRACTION2CHAIN B
3X-RAY DIFFRACTION3CHAIN C
4X-RAY DIFFRACTION4CHAIN D
5X-RAY DIFFRACTION5CHAIN E
6X-RAY DIFFRACTION6CHAIN F
7X-RAY DIFFRACTION7CHAIN G
8X-RAY DIFFRACTION8CHAIN H
9X-RAY DIFFRACTION9CHAIN I
10X-RAY DIFFRACTION10CHAIN J
11X-RAY DIFFRACTION11CHAIN K
12X-RAY DIFFRACTION12CHAIN L

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