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- PDB-8acw: X-ray structure of Na+-NQR from Vibrio cholerae at 3.4 A resolution -

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Basic information

Entry
Database: PDB / ID: 8acw
TitleX-ray structure of Na+-NQR from Vibrio cholerae at 3.4 A resolution
Components(Na(+)-translocating NADH-quinone reductase subunit ...) x 6
KeywordsMEMBRANE PROTEIN / respiratory complex / NADH ubiquinone oxido reducatase / Na+ pump
Function / homology
Function and homology information


NADH:ubiquinone reductase (Na+-transporting) / Gram-negative-bacterium-type cell wall / oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor / sodium ion transport / respiratory electron transport chain / transmembrane transport / 2 iron, 2 sulfur cluster binding / FMN binding / electron transfer activity / metal ion binding / plasma membrane
Similarity search - Function
Na(+)-translocating NADH-quinone reductase subunit B / Na(+)-translocating NADH-quinone reductase subunit E / Na(+)-translocating NADH-quinone reductase subunit D / NqrDE/RnfAE / Ion-translocating oxidoreductase NqrB/RnfD / Na(+)-translocating NADH-quinone reductase subunit A / Na(+)-translocating NADH-quinone reductase subunit A, C-terminal domain / Rnf-Nqr subunit, membrane protein / NQR2, RnfD, RnfE family / Na(+)-translocating NADH-quinone reductase subunit A (NQRA) ...Na(+)-translocating NADH-quinone reductase subunit B / Na(+)-translocating NADH-quinone reductase subunit E / Na(+)-translocating NADH-quinone reductase subunit D / NqrDE/RnfAE / Ion-translocating oxidoreductase NqrB/RnfD / Na(+)-translocating NADH-quinone reductase subunit A / Na(+)-translocating NADH-quinone reductase subunit A, C-terminal domain / Rnf-Nqr subunit, membrane protein / NQR2, RnfD, RnfE family / Na(+)-translocating NADH-quinone reductase subunit A (NQRA) / NQRA C-terminal domain / Na(+)-translocating NADH-quinone reductase subunit C / Na(+)-translocating NADH-quinone reductase subunit F / FMN-binding / FMN-binding domain / FMN_bind / Flavoprotein pyridine nucleotide cytochrome reductase-like, FAD-binding domain / Oxidoreductase FAD-binding domain / 2Fe-2S iron-sulfur cluster binding 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 / Oxidoreductase FAD/NAD(P)-binding / Oxidoreductase NAD-binding domain / FAD-binding domain, ferredoxin reductase-type / Ferredoxin-NADP reductase (FNR), nucleotide-binding domain / Ferredoxin reductase-type FAD binding domain profile. / Riboflavin synthase-like beta-barrel
Similarity search - Domain/homology
FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / : / LYSINE / RIBOFLAVIN / Na(+)-translocating NADH-quinone reductase subunit E / Na(+)-translocating NADH-quinone reductase subunit C / Na(+)-translocating NADH-quinone reductase subunit D / Na(+)-translocating NADH-quinone reductase subunit B ...FLAVIN-ADENINE DINUCLEOTIDE / FE2/S2 (INORGANIC) CLUSTER / FLAVIN MONONUCLEOTIDE / : / LYSINE / RIBOFLAVIN / Na(+)-translocating NADH-quinone reductase subunit E / Na(+)-translocating NADH-quinone reductase subunit C / Na(+)-translocating NADH-quinone reductase subunit D / Na(+)-translocating NADH-quinone reductase subunit B / Na(+)-translocating NADH-quinone reductase subunit F / Na(+)-translocating NADH-quinone reductase subunit A
Similarity search - Component
Biological speciesVibrio cholerae (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.4 Å
AuthorsFritz, G.
Funding support Germany, 1items
OrganizationGrant numberCountry
German Research Foundation (DFG)311211092 Germany
CitationJournal: Nat Struct Mol Biol / Year: 2023
Title: Conformational coupling of redox-driven Na-translocation in Vibrio cholerae NADH:quinone oxidoreductase.
Authors: Jann-Louis Hau / Susann Kaltwasser / Valentin Muras / Marco S Casutt / Georg Vohl / Björn Claußen / Wojtek Steffen / Alexander Leitner / Eckhard Bill / George E Cutsail / Serena DeBeer / ...Authors: Jann-Louis Hau / Susann Kaltwasser / Valentin Muras / Marco S Casutt / Georg Vohl / Björn Claußen / Wojtek Steffen / Alexander Leitner / Eckhard Bill / George E Cutsail / Serena DeBeer / Janet Vonck / Julia Steuber / Günter Fritz /
Abstract: In the respiratory chain, NADH oxidation is coupled to ion translocation across the membrane to build up an electrochemical gradient. In the human pathogen Vibrio cholerae, the sodium-pumping NADH: ...In the respiratory chain, NADH oxidation is coupled to ion translocation across the membrane to build up an electrochemical gradient. In the human pathogen Vibrio cholerae, the sodium-pumping NADH:quinone oxidoreductase (Na-NQR) generates a sodium gradient by a so far unknown mechanism. Here we show that ion pumping in Na-NQR is driven by large conformational changes coupling electron transfer to ion translocation. We have determined a series of cryo-EM and X-ray structures of the Na-NQR that represent snapshots of the catalytic cycle. The six subunits NqrA, B, C, D, E, and F of Na-NQR harbor a unique set of cofactors that shuttle the electrons from NADH twice across the membrane to quinone. The redox state of a unique intramembranous [2Fe-2S] cluster orchestrates the movements of subunit NqrC, which acts as an electron transfer switch. We propose that this switching movement controls the release of Na from a binding site localized in subunit NqrB.
History
DepositionJul 7, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 12, 2023Provider: repository / Type: Initial release
Revision 1.1Sep 20, 2023Group: Data collection / Database references
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / citation_author
Item: _citation.pdbx_database_id_DOI / _citation.title
Revision 1.2Sep 27, 2023Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3Nov 22, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 1.4Feb 7, 2024Group: Refinement description / Category: pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Na(+)-translocating NADH-quinone reductase subunit A
B: Na(+)-translocating NADH-quinone reductase subunit B
C: Na(+)-translocating NADH-quinone reductase subunit C
D: Na(+)-translocating NADH-quinone reductase subunit D
E: Na(+)-translocating NADH-quinone reductase subunit E
F: Na(+)-translocating NADH-quinone reductase subunit F
hetero molecules


Theoretical massNumber of molelcules
Total (without water)217,76117
Polymers213,6176
Non-polymers4,14411
Water0
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: electron microscopy
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)93.720, 142.940, 103.390
Angle α, β, γ (deg.)90.000, 109.930, 90.000
Int Tables number4
Space group name H-MP1211

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Components

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Na(+)-translocating NADH-quinone reductase subunit ... , 6 types, 6 molecules ABCDEF

#1: Protein Na(+)-translocating NADH-quinone reductase subunit A / Na(+)-NQR subunit A / Na(+)-translocating NQR subunit A / NQR complex subunit A / NQR-1 subunit A


Mass: 51125.391 Da / Num. of mol.: 1 / Mutation: N-terminal His tag
Source method: isolated from a genetically manipulated source
Details: N-terminal His tag: MGSSHHHHHHSSGLEVLFQGP / Source: (gene. exp.) Vibrio cholerae (bacteria)
Gene: nqrA, ERS013165_00619, ERS013186_02081, ERS013199_02394, ERS013202_01882, ERS013206_02986, ERS013207_01957
Production host: Vibrio cholerae (bacteria)
References: UniProt: A0A655PZA5, NADH:ubiquinone reductase (Na+-transporting)
#2: Protein Na(+)-translocating NADH-quinone reductase subunit B / Na(+)-NQR subunit B / Na(+)-translocating NQR subunit B / NQR complex subunit B / NQR-1 subunit B


Mass: 45390.883 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae (bacteria)
Gene: nqrB, D6U24_04465, ERS013186_02082, ERS013198_02508, ERS013199_02395, ERS013200_04117, ERS013202_01883, ERS013206_02987, ERS013207_01958, EYB64_17950, F0H40_10090, FLM02_04820, FLM12_12920, FXE67_12105, HPY07_02915
Production host: Vibrio cholerae (bacteria)
References: UniProt: A0A085SSI3, NADH:ubiquinone reductase (Na+-transporting)
#3: Protein Na(+)-translocating NADH-quinone reductase subunit C / Na(+)-NQR subunit C / Na(+)-translocating NQR subunit C / NQR complex subunit C / NQR-1 subunit C


Mass: 27652.270 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae (bacteria)
Gene: nqrC, BC353_01370, D6U24_04470, ERS013165_00616, ERS013186_02083, ERS013198_02507, ERS013199_02396, ERS013200_04118, ERS013201_01110, ERS013202_01884, ERS013206_02988, ERS013207_01959, F0H40_ ...Gene: nqrC, BC353_01370, D6U24_04470, ERS013165_00616, ERS013186_02083, ERS013198_02507, ERS013199_02396, ERS013200_04118, ERS013201_01110, ERS013202_01884, ERS013206_02988, ERS013207_01959, F0H40_10095, FLM02_04815, FLM12_12915
Production host: Vibrio cholerae (bacteria)
References: UniProt: A0A085R7S2, NADH:ubiquinone reductase (Na+-transporting)
#4: Protein Na(+)-translocating NADH-quinone reductase subunit D / Na(+)-NQR subunit D / Na(+)-translocating NQR subunit D / NQR complex subunit D / NQR-1 subunit D


Mass: 22853.217 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae (bacteria)
Gene: nqrD, BC353_01365, D6U24_04475, ERS013165_00615, ERS013186_02084, ERS013198_02506, ERS013199_02397, ERS013200_04119, ERS013201_01111, ERS013202_01885, ERS013206_02989, ERS013207_01960, EYB64_ ...Gene: nqrD, BC353_01365, D6U24_04475, ERS013165_00615, ERS013186_02084, ERS013198_02506, ERS013199_02397, ERS013200_04119, ERS013201_01111, ERS013202_01885, ERS013206_02989, ERS013207_01960, EYB64_17940, F0315_08345, F0H40_10100, F0M16_14020, FLM02_04810, FLM12_12910, HPY07_02925
Production host: Vibrio cholerae (bacteria)
References: UniProt: A0A085RHY8, NADH:ubiquinone reductase (Na+-transporting)
#5: Protein Na(+)-translocating NADH-quinone reductase subunit E / Na(+)-NQR subunit E / Na(+)-translocating NQR subunit E / NQR complex subunit E / NQR-1 subunit E


Mass: 21481.678 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae (bacteria)
Gene: nqrE, BC353_01360, D6U24_04480, ERS013165_00614, ERS013186_02085, ERS013198_02505, ERS013199_02398, ERS013200_04120, ERS013201_01112, ERS013202_01886, ERS013206_02990, ERS013207_01961, EYB64_ ...Gene: nqrE, BC353_01360, D6U24_04480, ERS013165_00614, ERS013186_02085, ERS013198_02505, ERS013199_02398, ERS013200_04120, ERS013201_01112, ERS013202_01886, ERS013206_02990, ERS013207_01961, EYB64_17935, F0315_08350, F0H40_10105, F0M16_14025, FLM02_04805, FLM12_12905, HPY07_02930
Production host: Vibrio cholerae (bacteria)
References: UniProt: A0A085QWM0, NADH:ubiquinone reductase (Na+-transporting)
#6: Protein Na(+)-translocating NADH-quinone reductase subunit F / Na(+)-NQR subunit F / Na(+)-translocating NQR subunit F / NQR complex subunit F / NQR-1 subunit F


Mass: 45113.492 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Vibrio cholerae (bacteria)
Gene: nqrF, D6U24_04485, ERS013198_02504, ERS013199_02399, ERS013201_01113, ERS013202_01887, ERS013206_02991, EYB64_17930, FLM12_12900
Production host: Vibrio cholerae (bacteria)
References: UniProt: A0A085ST13, NADH:ubiquinone reductase (Na+-transporting)

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Sugars , 1 types, 3 molecules

#9: Sugar ChemComp-LMT / DODECYL-BETA-D-MALTOSIDE


Type: D-saccharide / Mass: 510.615 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C24H46O11 / Comment: detergent*YM

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Non-polymers , 6 types, 8 molecules

#7: Chemical ChemComp-FMN / FLAVIN MONONUCLEOTIDE / RIBOFLAVIN MONOPHOSPHATE / Flavin mononucleotide


Mass: 456.344 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H21N4O9P
#8: Chemical ChemComp-RBF / RIBOFLAVIN / RIBOFLAVINE / VITAMIN B2 / Riboflavin


Mass: 376.364 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C17H20N4O6 / Feature type: SUBJECT OF INVESTIGATION
#10: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#11: Chemical ChemComp-LYS / LYSINE / Lysine


Type: L-peptide linking / Mass: 147.195 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C6H15N2O2
#12: Chemical ChemComp-FES / FE2/S2 (INORGANIC) CLUSTER / Iron–sulfur cluster


Mass: 175.820 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe2S2
#13: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE / Flavin adenine dinucleotide


Mass: 785.550 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Comment: FAD*YM

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Details

Has ligand of interestY

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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: 3.05 Å3/Da / Density % sol: 59.64 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop / pH: 8.5
Details: 40 mM KSCN, 21.0% PEG 2000MME, 100 mM Tris-acetic acid, 8% 1-propanol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P14 (MX2) / Wavelength: 0.91 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 9, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.91 Å / Relative weight: 1
ReflectionResolution: 3.4→48.6 Å / Num. obs: 35115 / % possible obs: 99.3 % / Redundancy: 62.725 % / Biso Wilson estimate: 157.33 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.266 / Rrim(I) all: 0.269 / Χ2: 0.723 / Net I/σ(I): 13.61 / Num. measured all: 2202591 / Scaling rejects: 1302
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
3.4-3.663.3527.020.63348501555755010.3217.07599
3.6-3.863.2023.7521.54278153444144010.6353.78299.1
3.8-463.6242.1832.93226946358735670.8452.20199.4
4-562.4770.7768.6465625610568105040.9810.78299.4
5-663.6990.41815.46297603469646720.9940.42199.5
6-862.1930.1928.14231420374237210.9990.19299.4
8-1060.9710.08158.4809701335132810.08299.5
10-48.658.2280.05378.77827421453142110.05397.8

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Processing

Software
NameVersionClassification
XDSdata reduction
XSCALEdata scaling
PHENIX1.20.1-4487refinement
PDB_EXTRACT3.27data extraction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4P6V

4p6v
PDB Unreleased entry


Resolution: 3.4→48.6 Å / SU ML: 0.68 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 37.61 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3061 1788 5.09 %
Rwork0.2704 33308 -
obs0.2722 35096 99.4 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 601.93 Å2 / Biso mean: 217.1455 Å2 / Biso min: 74.44 Å2
Refinement stepCycle: final / Resolution: 3.4→48.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms14045 0 499 0 14544
Biso mean--209.57 --
Num. residues----1833
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 13

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.4-3.490.38051410.39252556269799
3.49-3.590.47561220.41612548267099
3.59-3.710.48351320.38192539267199
3.71-3.840.39381450.31382555270099
3.84-40.39351360.278925372673100
4-4.180.28491380.272558269699
4.18-4.40.31921290.26742564269399
4.4-4.670.25691770.22732521269899
4.67-5.030.30091250.23125742699100
5.03-5.540.32191290.24642582271199
5.54-6.340.33041550.273525512706100
6.34-7.980.28961350.289225862721100
7.98-48.60.27511240.25822637276199
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)
13.1179-0.7659-1.09133.06330.03360.4040.0294-0.59530.1458-0.2144-0.00930.1039-0.6892-0.3915-0.00061.62840.07580.29221.76870.33961.4997-35.7042-22.2129-26.3462
20.81831.1852-0.90641.7078-1.21090.95860.07480.0323-0.52141.90820.0924-1.0176-0.43310.0049-0.00021.9203-0.2103-0.27131.5080.18811.5521-38.082-29.2588-44.6068
32.8273-0.1560.63491.01090.38190.28260.285-1.0379-0.59440.0153-0.86290.47890.4525-0.3017-01.5141-0.2199-0.14261.38540.05271.4197-27.2606-31.6377-30.6833
41.418-0.77490.69141.0075-0.7650.55920.4086-0.1787-0.9312-1.1773-0.41460.3730.59030.4644-0.00052.2165-0.2302-0.26871.64370.20742.2718-18.9018-31.5316-24.6819
50.4012-0.4886-0.71370.41810.76781.0572-0.46890.3869-0.6459-0.56840.5507-0.1782-0.0179-1.1535-0.00091.51550.1593-0.05321.4880.12531.5384-39.93-30.0736-28.1256
60.2610.28740.07760.95610.05472.2146-0.61070.0271-0.04520.2723-0.4396-0.23260.27520.5055-0.32671.3669-0.2629-0.430.7103-0.03592.4909-42.692-16.4349-25.9082
70.6614-0.7172-0.23710.79960.63491.55640.3277-0.05030.7207-0.7547-0.1949-1.0412-0.3588-0.0241-0.00021.3577-0.28420.16321.24010.36752.577-22.6888-9.8376-20.5495
80.6985-0.13410.86821.0946-0.71161.4018-1.2354-0.06990.7084-0.30410.58981.4482-0.6589-1.21130.00051.6077-0.0131-0.20081.36090.0091.4833-20.2111-9.3265-29.9406
93.7615-1.33742.40611.7059-1.6952.1333-0.2075-0.40740.57130.9203-0.71640.2534-1.0950.0391-0.29081.3457-0.24930.48311.0530.17850.8224-20.949918.3131.2818
102.9116-0.97840.17270.49460.23320.6583-0.24080.4942-1.4375-0.3290.17351.40410.42090.2333-0.00241.1373-0.2061-0.33551.5601-0.0561.5689-17.806822.0437-8.9323
112.09071.20830.01941.96241.51222.95380.8307-0.5106-0.44030.4242-0.40610.0858-0.0049-0.79230.00250.8715-0.0966-0.02671.18210.16940.8236-3.1717.7181-3.3156
122.9103-0.3184-0.20120.2032-0.51391.7914-0.93410.39980.2517-0.1192-1.0669-0.39710.5630.3621-3.4686-0.91680.35980.63651.01890.64141.755233.792828.0197-36.0249
134.64231.9746-1.01642.6622-1.93591.3426-0.117-0.47861.4986-0.6906-1.07960.82860.75072.7375-0.38082.9945-0.53410.18741.7252-0.0751.021738.618734.2851-9.0533
141.379-1.2626-0.04081.27740.13510.01650.43930.9648-1.3317-0.61730.09320.84620.269-1.66560.11151.8631-0.66460.24871.87960.39971.303622.429833.6675-6.9368
150.0324-0.23710.03862.0192-0.08060.0904-0.59043.349-0.88660.79280.81680.56061.0881-0.51670.02922.0867-0.9798-0.0045.5337-0.52272.813133.941632.79583.2508
161.2340.914-0.25150.7813-0.43672.3346-0.95410.0054-0.0786-0.65740.0580.1507-0.72670.1793-0.26931.1849-0.56160.0991.22340.41080.947214.857825.3138-41.5943
170.17120.23460.18110.61680.30020.3037-0.2359-0.3360.2584-0.2181-0.0264-0.3632-0.58651.1459-2.22281.9645-1.25780.0032.46550.67070.073623.154932.146-30.7072
181.18270.6917-0.8462.28010.70341.4177-0.27390.45881.09020.9419-0.78670.3715-0.74790.1534-0.09021.0233-0.1742-0.13251.33010.05841.02432.784228.5957-31.6865
190.30170.5404-0.30733.6895-1.870.9529-10.3306-19.59060.31053.820617.74441.30751.6198-1.1155-6.77611.6182-0.43910.26084.5953-0.4811.7166-13.68358.4071-39.0092
203.1308-1.2653-1.60762.31751.36761.17080.66460.39380.9886-0.4547-0.66710.3647-0.785-0.34970.29750.7755-0.3542-0.03680.31230.02561.121212.73198.9458-21.1054
210.80620.28440.34121.27790.08450.5885-0.1055-0.8823-0.16270.14570.7236-1.8569-0.12440.35220.25640.42440.71780.30351.27490.25221.750920.7884.6612-29.3156
224.08171.8850.8651.1850.60680.40510.28370.79921.65120.16491.2725-0.9917-0.58430.94430.12741.32920.72671.14822.08980.40423.309542.775316.9642-27.6228
230.71140.0611-0.55360.2466-0.7812.84010.36161.70770.024-0.43980.4122-0.09520.951-0.93150.17260.43770.49950.4851.5645-0.0580.901721.03117.2749-38.4092
242.50780.59590.83471.47521.55051.6582-1.46360.03921.99851.0013-0.2841-1.37180.10610.9241-1.05631.30860.54570.04430.48350.5721.932413.375811.4339-37.3179
250.0527-0.0045-0.17380.0192-0.02780.67460.70850.72171.13880.84890.8562-2.2442-0.099-0.42320.05140.95650.096-0.31561.34010.27842.585925.858313.8954-22.8628
260.1383-0.3754-0.57352.32021.91532.51320.26670.39760.03850.8885-0.14580.2182-1.2812-0.27520.14071.54860.28930.08351.82171.22772.71789.94964.6905-24.0738
270.68910.4161-0.12621.58092.4794.9149-1.2152.186-1.763-1.1-0.2851.5294-1.1087-0.0256-0.91171.0493-0.8038-0.30381.6578-0.4731.2649-12.666412.3813-31.0155
283.54040.0011-0.27420.3818-0.21610.174-0.17270.99120.1854-0.25130.11911.24940.0393-0.27520.23390.9268-0.31740.23510.2016-0.18911.30114.040914.5468-18.2922
291.39791.04091.14941.4043-0.54881.6473-0.224-0.5355-0.7516-0.76430.16820.56090.4701-0.96310.00041.47850.24680.16281.5090.09961.19199.9611-2.9043-54.0233
301.5106-0.06920.17130.1944-0.57944.55650.12160.4883-0.5343-0.66880.5098-0.2274-0.1557-2.60290.3581.61680.20570.0610.52680.04251.8009-24.76460.4091-73.8217
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 43 )A1 - 43
2X-RAY DIFFRACTION2chain 'A' and (resid 44 through 124 )A44 - 124
3X-RAY DIFFRACTION3chain 'A' and (resid 125 through 184 )A125 - 184
4X-RAY DIFFRACTION4chain 'A' and (resid 185 through 236 )A185 - 236
5X-RAY DIFFRACTION5chain 'A' and (resid 237 through 286 )A237 - 286
6X-RAY DIFFRACTION6chain 'A' and (resid 287 through 321 )A287 - 321
7X-RAY DIFFRACTION7chain 'A' and (resid 322 through 399 )A322 - 399
8X-RAY DIFFRACTION8chain 'A' and (resid 400 through 446 )A400 - 446
9X-RAY DIFFRACTION9chain 'B' and (resid 35 through 117 )B35 - 117
10X-RAY DIFFRACTION10chain 'B' and (resid 118 through 188 )B118 - 188
11X-RAY DIFFRACTION11chain 'B' and (resid 189 through 414 )B189 - 414
12X-RAY DIFFRACTION12chain 'C' and (resid 7 through 52 )C7 - 52
13X-RAY DIFFRACTION13chain 'C' and (resid 53 through 127 )C53 - 127
14X-RAY DIFFRACTION14chain 'C' and (resid 128 through 237 )C128 - 237
15X-RAY DIFFRACTION15chain 'C' and (resid 238 through 254 )C238 - 254
16X-RAY DIFFRACTION16chain 'D' and (resid 6 through 92 )D6 - 92
17X-RAY DIFFRACTION17chain 'D' and (resid 93 through 110 )D93 - 110
18X-RAY DIFFRACTION18chain 'D' and (resid 111 through 208 )D111 - 208
19X-RAY DIFFRACTION19chain 'D' and (resid 209 through 209 )D209
20X-RAY DIFFRACTION20chain 'E' and (resid 2 through 34 )E2 - 34
21X-RAY DIFFRACTION21chain 'E' and (resid 35 through 62 )E35 - 62
22X-RAY DIFFRACTION22chain 'E' and (resid 63 through 72 )E63 - 72
23X-RAY DIFFRACTION23chain 'E' and (resid 73 through 109 )E73 - 109
24X-RAY DIFFRACTION24chain 'E' and (resid 110 through 121 )E110 - 121
25X-RAY DIFFRACTION25chain 'E' and (resid 122 through 135 )E122 - 135
26X-RAY DIFFRACTION26chain 'E' and (resid 136 through 165 )E136 - 165
27X-RAY DIFFRACTION27chain 'E' and (resid 166 through 175 )E166 - 175
28X-RAY DIFFRACTION28chain 'E' and (resid 176 through 198 )E176 - 198
29X-RAY DIFFRACTION29chain 'F' and (resid 1 through 124 )F1 - 124
30X-RAY DIFFRACTION30chain 'F' and (resid 125 through 407 )F125 - 407

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