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- PDB-8riu: Crystal structure of the F420-reducing carbon monoxide dehydrogen... -

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Basic information

Entry
Database: PDB / ID: 8riu
TitleCrystal structure of the F420-reducing carbon monoxide dehydrogenase component from the ethanotroph Candidatus Ethanoperedens thermophilum
Components
  • (Acetyl-CoA decarbonylase/synthase complex subunit ...) x 2
  • Coenzyme F420 hydrogenase/dehydrogenase, beta subunit C terminus
KeywordsOXIDOREDUCTASE / Carbon monoxide dehydrogenase / F420-reductase / acetyl-coenzyme A synthase-decarbonylase complex / anaerobic oxidoreductase / CO2-releasing enzyme / C-cluster / CO / CO2 / gas channelling.
Function / homology
Function and homology information


: / methanogenesis, from acetate / oxidoreductase activity, acting on CH or CH2 groups, with an iron-sulfur protein as acceptor / anaerobic carbon monoxide dehydrogenase / methanogenesis / anaerobic carbon-monoxide dehydrogenase activity / acetyl-CoA metabolic process / iron-sulfur cluster binding / nickel cation binding / 4 iron, 4 sulfur cluster binding / iron ion binding
Similarity search - Function
Acetyl-CoA decarbonylase/synthase complex subunit alpha / CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit / CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit / Coenzyme F420 hydrogenase/dehydrogenase beta subunit, N-terminal / Coenzyme F420 hydrogenase/dehydrogenase beta subunit, C-terminal / Oxidoreductase FRHB/FDHB/HCAR-like / Coenzyme F420 hydrogenase/dehydrogenase, beta subunit N-term / Coenzyme F420 hydrogenase/dehydrogenase, beta subunit C terminus / CO dehydrogenase, alpha-bundle / Hydroxylamine reductase/Ni-containing CO dehydrogenase ...Acetyl-CoA decarbonylase/synthase complex subunit alpha / CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit / CO dehydrogenase beta subunit/acetyl-CoA synthase epsilon subunit / Coenzyme F420 hydrogenase/dehydrogenase beta subunit, N-terminal / Coenzyme F420 hydrogenase/dehydrogenase beta subunit, C-terminal / Oxidoreductase FRHB/FDHB/HCAR-like / Coenzyme F420 hydrogenase/dehydrogenase, beta subunit N-term / Coenzyme F420 hydrogenase/dehydrogenase, beta subunit C terminus / CO dehydrogenase, alpha-bundle / Hydroxylamine reductase/Ni-containing CO dehydrogenase / Prismane/CO dehydrogenase family / Prismane-like, alpha/beta-sandwich / Prismane-like superfamily / DHS-like NAD/FAD-binding domain superfamily / 4Fe-4S ferredoxin-type iron-sulfur binding domain profile. / 4Fe-4S ferredoxin-type, iron-sulphur binding domain
Similarity search - Domain/homology
FLAVIN-ADENINE DINUCLEOTIDE / : / IRON/SULFUR CLUSTER / FE(4)-NI(1)-S(4) CLUSTER / Acetyl-CoA decarbonylase/synthase complex subunit alpha / Acetyl-CoA decarbonylase/synthase complex subunit epsilon / Coenzyme F420 hydrogenase/dehydrogenase, beta subunit C terminus
Similarity search - Component
Biological speciesCandidatus Methanoperedenaceae archaeon GB50 (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.89 Å
AuthorsLemaire, O.N. / Wagner, T.
Funding support Germany, 2items
OrganizationGrant numberCountry
Max Planck Society Germany
German Research Foundation (DFG)WA 4053/2-1 Germany
CitationJournal: Nat Commun / Year: 2024
Title: Ethane-oxidising archaea couple CO 2 generation to F 420 reduction.
Authors: Lemaire, O.N. / Wegener, G. / Wagner, T.
History
DepositionDec 19, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 2, 2024Provider: repository / Type: Initial release
Revision 1.1Apr 16, 2025Group: Database references / Structure summary / Category: citation / citation_author / pdbx_entry_details
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _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: Acetyl-CoA decarbonylase/synthase complex subunit alpha
B: Coenzyme F420 hydrogenase/dehydrogenase, beta subunit C terminus
C: Acetyl-CoA decarbonylase/synthase complex subunit epsilon
D: Acetyl-CoA decarbonylase/synthase complex subunit alpha
E: Coenzyme F420 hydrogenase/dehydrogenase, beta subunit C terminus
F: Acetyl-CoA decarbonylase/synthase complex subunit epsilon
hetero molecules


Theoretical massNumber of molelcules
Total (without water)304,17153
Polymers294,6766
Non-polymers9,49547
Water25,5451418
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: native gel electrophoresis, gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area43020 Å2
ΔGint-468 kcal/mol
Surface area76710 Å2
MethodPISA
Unit cell
Length a, b, c (Å)97.070, 159.213, 191.444
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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Acetyl-CoA decarbonylase/synthase complex subunit ... , 2 types, 4 molecules ADCF

#1: Protein Acetyl-CoA decarbonylase/synthase complex subunit alpha / ACDS complex subunit alpha / ACDS complex carbon monoxide dehydrogenase subunit alpha / ACDS CODH ...ACDS complex subunit alpha / ACDS complex carbon monoxide dehydrogenase subunit alpha / ACDS CODH subunit alpha


Mass: 87549.070 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: Ligands SF4, XCC and GOL are not part of the protein sequence
Source: (natural) Candidatus Methanoperedenaceae archaeon GB50 (archaea)
References: UniProt: A0A7R9N4A5, anaerobic carbon monoxide dehydrogenase
#3: Protein Acetyl-CoA decarbonylase/synthase complex subunit epsilon / ACDS complex subunit epsilon / ACDS complex carbon monoxide dehydrogenase subunit epsilon / ACDS ...ACDS complex subunit epsilon / ACDS complex carbon monoxide dehydrogenase subunit epsilon / ACDS CODH subunit epsilon


Mass: 19057.965 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Details: Ligand GOL is not part of the protein sequence
Source: (natural) Candidatus Methanoperedenaceae archaeon GB50 (archaea)
References: UniProt: A0A7R9N5A2

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Protein , 1 types, 2 molecules BE

#2: Protein Coenzyme F420 hydrogenase/dehydrogenase, beta subunit C terminus


Mass: 40730.809 Da / Num. of mol.: 2 / Source method: isolated from a natural source
Details: Ligands SF4, FAD and GOL are not part of the protein sequence
Source: (natural) Candidatus Methanoperedenaceae archaeon GB50 (archaea)
References: UniProt: A0A7R9R773

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Non-polymers , 9 types, 1465 molecules

#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 15 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: C2H6O2
#6: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 13 / Source method: obtained synthetically / Formula: Fe4S4 / Feature type: SUBJECT OF INVESTIGATION
#7: Chemical ChemComp-XCC / FE(4)-NI(1)-S(4) CLUSTER / C CLUSTER


Mass: 410.333 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Fe4NiS4 / Feature type: SUBJECT OF INVESTIGATION
#8: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: K
#9: Chemical ChemComp-FAD / FLAVIN-ADENINE DINUCLEOTIDE


Mass: 785.550 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H33N9O15P2 / Feature type: SUBJECT OF INVESTIGATION / Comment: FAD*YM
#10: Chemical ChemComp-PE4 / 2-{2-[2-(2-{2-[2-(2-ETHOXY-ETHOXY)-ETHOXY]-ETHOXY}-ETHOXY)-ETHOXY]-ETHOXY}-ETHANOL / POLYETHYLENE GLYCOL PEG4000


Mass: 354.436 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H34O8 / Comment: precipitant*YM
#11: Chemical ChemComp-CL / CHLORIDE ION


Mass: 35.453 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Cl
#12: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1418 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestY
Has protein modificationN

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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: 2.51 Å3/Da / Density % sol: 51.1 % / Description: Brown thick square plate
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 6
Details: Crystallisation was performed anaerobically at 20 degree Celsius using the sitting drop method on 96-Well MRC 2-Drop polystyrene Crystallisation Plates (SWISSCI) in a Coy tent containing a ...Details: Crystallisation was performed anaerobically at 20 degree Celsius using the sitting drop method on 96-Well MRC 2-Drop polystyrene Crystallisation Plates (SWISSCI) in a Coy tent containing a N2/H2 (97:3%) atmosphere. The reservoir chamber was filled with 90 ul of crystallisation condition and the drop was formed by spotting 0.6 ul protein with 0.6 ul of 20% (w/v) PEG 6,000; 100 mM MES pH6 and 200 mM Ammonium chloride. The protein was crystallized at 13.0 mg/ml in 25 mM Tris/HCl pH 7.6, 2 mM dithiothreitol, 1 mM flavin adenine dinucleotide and 1 mM Flavin mononuleotide and 10% (v/v) glycerol. Crystals were cryo-protected by soaking in 20% (w/v) PEG 6,000; 100 mM MES pH6 and 200 mM Ammonium chloride supplemented with 30% v/v glycerol for a few seconds.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SOLEIL / Beamline: PROXIMA 1 / Wavelength: 0.97856 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 22, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97856 Å / Relative weight: 1
ReflectionResolution: 1.89→122.41 Å / Num. obs: 164775 / % possible obs: 95.9 % / Redundancy: 13.6 % / CC1/2: 0.999 / Rmerge(I) obs: 0.149 / Rpim(I) all: 0.042 / Rrim(I) all: 0.155 / Net I/σ(I): 10.8
Reflection shellResolution: 1.89→2.1 Å / Redundancy: 12.2 % / Rmerge(I) obs: 1.583 / Mean I/σ(I) obs: 1.7 / Num. unique obs: 8240 / CC1/2: 0.639 / Rpim(I) all: 0.46 / Rrim(I) all: 1.65 / % possible all: 73.6

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Processing

Software
NameVersionClassification
PHENIX(1.20.1_4487: ???)refinement
autoPROCdata reduction
autoPROCdata scaling
PHENIXphasing
RefinementMethod to determine structure: SAD / Resolution: 1.89→39.8 Å / SU ML: 0.16 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 22.39 / Stereochemistry target values: ML
Details: The last refinement steps were performed by refining with a translation libration screw (TLS) and with modelled hydrogens in the riding position. Hydrogens were omitted in the final deposited models.
RfactorNum. reflection% reflection
Rfree0.1873 8278 5.03 %
Rwork0.1651 --
obs0.1662 164728 69.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 44.12 Å2
Refinement stepCycle: LAST / Resolution: 1.89→39.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20332 0 128 1418 21878
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.009
X-RAY DIFFRACTIONf_angle_d1.233
X-RAY DIFFRACTIONf_dihedral_angle_d14.3147894
X-RAY DIFFRACTIONf_chiral_restr0.2613215
X-RAY DIFFRACTIONf_plane_restr0.0093606
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.89-1.910.401230.2302121X-RAY DIFFRACTION2
1.91-1.940.2429150.2836320X-RAY DIFFRACTION4
1.94-1.960.2889300.2755575X-RAY DIFFRACTION8
1.96-1.990.2871380.2686858X-RAY DIFFRACTION12
1.99-2.010.2861550.26011068X-RAY DIFFRACTION14
2.01-2.040.2278720.24921237X-RAY DIFFRACTION17
2.04-2.070.2739860.24531493X-RAY DIFFRACTION20
2.07-2.10.2865850.24281830X-RAY DIFFRACTION25
2.1-2.130.26611260.23292248X-RAY DIFFRACTION31
2.13-2.170.25411750.22983076X-RAY DIFFRACTION42
2.17-2.20.242190.22574118X-RAY DIFFRACTION56
2.2-2.240.24962590.21645270X-RAY DIFFRACTION71
2.24-2.290.25044020.22216819X-RAY DIFFRACTION93
2.29-2.330.2593850.21347387X-RAY DIFFRACTION100
2.33-2.380.26763650.20247438X-RAY DIFFRACTION100
2.38-2.440.24154090.19547390X-RAY DIFFRACTION100
2.44-2.50.22834340.19177383X-RAY DIFFRACTION100
2.5-2.570.1914260.18727400X-RAY DIFFRACTION100
2.57-2.640.19563760.187439X-RAY DIFFRACTION100
2.64-2.730.19533990.18177423X-RAY DIFFRACTION100
2.73-2.830.20894120.17987438X-RAY DIFFRACTION100
2.83-2.940.19893910.17067468X-RAY DIFFRACTION100
2.94-3.070.19244060.16967442X-RAY DIFFRACTION100
3.07-3.240.20433810.16697491X-RAY DIFFRACTION100
3.24-3.440.17853960.16147486X-RAY DIFFRACTION100
3.44-3.70.17373820.14677546X-RAY DIFFRACTION100
3.7-4.080.16113800.13657545X-RAY DIFFRACTION100
4.08-4.670.12874190.12087559X-RAY DIFFRACTION100
4.67-5.880.15613280.14147685X-RAY DIFFRACTION100
5.88-39.80.19354240.17877897X-RAY DIFFRACTION100
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)
11.33720.4545-1.27610.9466-0.55751.8141-0.1157-0.1279-0.12410.15320.0205-0.12840.0950.10150.11380.28840.0479-0.03570.3079-0.00120.2855-0.421666.289853.1205
20.651-0.3862-0.19121.45590.20350.5927-0.0369-0.25350.0420.49130.0682-0.0618-0.0351-0.0212-0.03210.40510.0256-0.03750.3544-0.00840.2195-6.419483.423468.088
32.36480.56380.22891.6075-0.50350.53910.035-0.15280.23840.34440.00120.1035-0.2244-0.0226-0.03390.40880.05740.00980.2785-0.05060.2238-11.8062100.820559.845
41.50170.73131.51821.63581.57193.7777-0.1248-0.03290.27250.13560.01070.0534-0.4634-0.00270.11760.34210.0470.04160.2598-0.00830.259-10.3145107.731552.1919
50.70380.3624-0.44871.5424-0.95841.6179-0.0162-0.07020.01370.28120.0230.1254-0.1402-0.2264-0.02080.31080.06280.04420.3849-0.02360.2436-25.513987.96753.1551
60.96310.093-0.07781.17710.16980.5072-0.0192-0.2108-0.06620.3033-0.01650.06310.0284-0.08840.03570.34850.01490.02230.36030.00970.2141-17.086771.795662.3815
70.3439-0.19680.50571.2748-0.55151.34130.02090.0495-0.14140.19730.0060.2250.0916-0.1593-0.03460.34250.0170.08260.41060.01270.3417-27.338460.331754.7847
88.36180.21743.11021.2075-0.2372.60750.0868-0.1056-0.61270.16870.08340.28090.1511-0.1773-0.16450.33440.03570.13340.33790.01460.393-33.747150.410956.8253
92.1301-0.90452.29624.78230.0532.9876-0.12160.15160.0525-0.34090.04-0.4169-0.0312-0.09510.10250.2676-0.02380.11030.3783-0.07650.2464-2.05664.039213.2085
101.628-0.2461-0.41581.23050.67462.71990.03820.4791-0.073-0.3685-0.0306-0.14470.1396-0.0411-0.06490.3094-0.00480.09250.4233-0.04880.27881.441660.8802-0.7852
111.7516-1.6315-0.95531.74560.75044.21840.00060.6333-0.4131-0.2821-0.0182-0.42730.50880.43650.03230.52670.13050.13650.6109-0.24860.52899.956446.1612-6.1129
124.98050.51592.1261.1593-0.85572.33010.2126-0.1153-0.5485-0.06460.0390.12290.46480.0463-0.23620.5780.00270.05460.4084-0.11270.4952-1.659942.83410.0908
131.59450.410.88333.53721.16943.6130.1069-0.033-0.1366-0.02050.001-0.02770.243-0.0495-0.08510.34590.0310.11410.3917-0.06520.28761.341154.6642.1421
146.1369-1.60372.2348.5335-2.97888.41140.40181.0036-0.7671-1.29170.01660.58241.143-0.3346-0.36460.7391-0.0965-0.0180.823-0.20950.5142-15.775541.0463-9.2855
150.86270.0723-0.16342.0606-0.13672.84090.23550.6981-0.4658-0.5398-0.2168-0.12540.2334-0.1198-0.00010.54140.0790.08230.6884-0.18670.3769-1.98855.5033-12.764
162.6324-3.1369-3.62295.92395.45157.5460.13371.0608-0.0316-0.6455-0.58330.0122-0.3991-0.96760.46530.4790.0586-0.01580.6759-0.03120.2797-10.506966.4595-12.6881
170.61030.4897-0.11485.1341-1.18421.04330.00210.1161-0.2401-0.5408-0.17390.47310.38380.06670.19530.4760.05250.01340.4626-0.08120.4085-12.35583.74640.9561
180.7484-0.20660.02771.63450.8610.4911-0.00040.0724-0.07120.0448-0.0273-0.18560.1082-0.05230.0560.28970.02650.02060.3607-0.01310.2657-7.634579.585727.2366
193.0877-0.1377-1.14234.4809-2.90712.583-0.08660.8188-0.262-0.71250.08770.12030.478-0.24280.04410.3508-0.02990.0210.5396-0.1030.2817-18.504665.662216.9383
201.70511.50990.79471.87420.11411.01910.12670.22380.1627-0.0961-0.0879-0.2330.0227-0.0862-0.01680.2926-0.0110.05670.41260.00430.2331-25.090169.738829.8381
211.72540.96531.89482.11150.35742.5249-0.01770.2149-0.02520.0869-0.07670.26010.1238-0.48350.11080.2671-0.00620.04010.4677-0.03750.3558-31.374268.047330.7659
228.052-0.05815.79972.47810.20256.12670.0413-0.6177-0.3830.0666-0.05470.40190.1857-0.66830.04560.24140.00580.03220.3336-0.00890.3124-24.725163.195737.3879
239.75273.6301-2.39836.0324-4.63263.5967-0.11130.1495-0.2659-0.32090.20990.09510.3805-0.2948-0.0990.2890.02560.0550.2699-0.07780.2494-17.886854.87135.3919
241.3309-0.3015-0.35771.7531-0.28811.1218-0.0120.2183-0.0782-0.0327-0.06180.0498-0.0858-0.03960.07830.23330.00120.00110.3509-0.02470.2416-13.658972.019229.9237
253.52372.91660.38998.59661.48980.2655-0.12920.31410.3031-0.6021-0.01610.3417-0.1445-0.08610.14510.3070.007-0.040.4469-0.01120.2514-25.259977.973419.1021
260.7137-0.21410.09831.1038-0.10820.496-0.0613-0.1779-0.10380.30050.053-0.36130.01920.08620.00160.29010.0229-0.10140.31240.00390.353818.646374.857.1086
270.5210.0544-0.03741.4284-1.2222.4915-0.0613-0.0406-0.21220.04360.0583-0.26440.29370.0140.02140.26520.0409-0.03630.3208-0.00780.474617.175552.460144.2536
280.54590.21390.06560.88010.1020.4047-0.0237-0.01990.02910.14090.0255-0.4583-0.0410.1881-0.0170.23180.0082-0.07810.3507-0.01550.517631.472584.83345.2976
294.03171.1332-3.8292.0181-1.0736.9010.2059-0.12220.2976-0.00050.0914-0.4739-0.30960.5274-0.32690.3198-0.0319-0.06470.3558-0.04910.671641.2468109.59943.2151
300.9842-1.4331-0.96955.07541.17465.0239-0.0799-0.05330.0001-0.0562-0.06540.20010.0873-0.07450.15220.2515-0.0230.00320.31870.03390.2456-5.644698.678915.378
311.073-0.52390.82521.541-0.61332.2549-0.0420.12770.1078-0.2163-0.02830.056-0.1212-0.07670.07370.29190.01470.00860.35760.01690.2214-17.0287106.19524.6274
327.0003-2.5852-4.24351.9272-0.09376.48630.0496-0.4290.6476-0.2457-0.0099-0.3154-0.79580.5157-0.00850.5694-0.0789-0.06690.3007-0.05040.3384-11.119120.96275.7699
333.61630.91650.05672.6439-1.06762.3015-0.12270.43920.253-0.22150.0283-0.1856-0.32960.22870.07670.4278-0.0012-0.03740.3662-0.00680.2013-8.6826113.33391.3838
340.7655-0.1901-0.02191.7082-0.61210.9571-0.03990.20070.0414-0.45390.00030.08790.0183-0.06750.00740.50270.0219-0.03070.4149-0.03090.245-16.814105.115-7.4825
350.19570.6593-0.17662.8542-0.20320.6517-0.05610.34650.1564-0.6033-0.1679-0.5543-0.10340.00170.1890.55660.05970.08110.5130.04660.4582-2.655778.6814-1.6557
360.2294-0.60120.7491.6574-1.62842.7227-0.01660.0699-0.0140.0658-0.01220.0062-0.1965-0.03760.04660.27250.00330.0090.3172-0.01820.28785.008882.18924.5935
377.14422.27422.38928.48857.43368.6779-0.13170.79090.4784-1.01670.1857-0.1712-0.8244-0.2526-0.04120.340600.03660.39120.09270.315210.818497.036311.7698
381.4471.0247-0.3670.7218-0.38984.0426-0.02380.091-0.1898-0.18360.10020.03540.1240.0965-0.11730.2559-0.0506-0.01060.36830.0170.402522.206492.121220.5165
392.19021.31360.63732.14040.68893.1752-0.06820.4166-0.0087-0.4102-0.0086-0.4788-0.03840.64840.0310.3541-0.00450.12260.50780.04180.489925.701794.420612.9581
401.52810.02090.37851.12060.29452.17440.04890.17480.1595-0.265-0.0126-0.2969-0.23340.49270.04730.2788-0.04630.03250.37830.03270.434727.246395.997825.6078
411.38140.65550.59111.99910.55231.3075-0.06870.07910.0715-0.1395-0.0251-0.1286-0.0450.02810.09070.27490.00990.03590.35240.01340.341913.2293.574826.1477
422.73780.7552-0.49342.9453-2.14811.6694-0.240.2722-0.2512-0.79810.4602-0.31010.19670.005-0.19050.391-0.02020.10460.4319-0.0360.388417.305584.361910.3708
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 31 through 89 )
2X-RAY DIFFRACTION2chain 'A' and (resid 90 through 257 )
3X-RAY DIFFRACTION3chain 'A' and (resid 258 through 337 )
4X-RAY DIFFRACTION4chain 'A' and (resid 338 through 417 )
5X-RAY DIFFRACTION5chain 'A' and (resid 418 through 552 )
6X-RAY DIFFRACTION6chain 'A' and (resid 553 through 656 )
7X-RAY DIFFRACTION7chain 'A' and (resid 657 through 739 )
8X-RAY DIFFRACTION8chain 'A' and (resid 740 through 789 )
9X-RAY DIFFRACTION9chain 'B' and (resid 1 through 36 )
10X-RAY DIFFRACTION10chain 'B' and (resid 37 through 108 )
11X-RAY DIFFRACTION11chain 'B' and (resid 109 through 131 )
12X-RAY DIFFRACTION12chain 'B' and (resid 132 through 162 )
13X-RAY DIFFRACTION13chain 'B' and (resid 163 through 229 )
14X-RAY DIFFRACTION14chain 'B' and (resid 230 through 253 )
15X-RAY DIFFRACTION15chain 'B' and (resid 254 through 324 )
16X-RAY DIFFRACTION16chain 'B' and (resid 325 through 346 )
17X-RAY DIFFRACTION17chain 'B' and (resid 347 through 370 )
18X-RAY DIFFRACTION18chain 'C' and (resid 1 through 20 )
19X-RAY DIFFRACTION19chain 'C' and (resid 21 through 30 )
20X-RAY DIFFRACTION20chain 'C' and (resid 31 through 47 )
21X-RAY DIFFRACTION21chain 'C' and (resid 48 through 74 )
22X-RAY DIFFRACTION22chain 'C' and (resid 75 through 92 )
23X-RAY DIFFRACTION23chain 'C' and (resid 93 through 107 )
24X-RAY DIFFRACTION24chain 'C' and (resid 108 through 156 )
25X-RAY DIFFRACTION25chain 'C' and (resid 157 through 174 )
26X-RAY DIFFRACTION26chain 'D' and (resid 31 through 337 )
27X-RAY DIFFRACTION27chain 'D' and (resid 338 through 417 )
28X-RAY DIFFRACTION28chain 'D' and (resid 418 through 739 )
29X-RAY DIFFRACTION29chain 'D' and (resid 740 through 790 )
30X-RAY DIFFRACTION30chain 'E' and (resid 1 through 36 )
31X-RAY DIFFRACTION31chain 'E' and (resid 37 through 131 )
32X-RAY DIFFRACTION32chain 'E' and (resid 132 through 162 )
33X-RAY DIFFRACTION33chain 'E' and (resid 163 through 266 )
34X-RAY DIFFRACTION34chain 'E' and (resid 267 through 349 )
35X-RAY DIFFRACTION35chain 'E' and (resid 350 through 370 )
36X-RAY DIFFRACTION36chain 'F' and (resid 1 through 20 )
37X-RAY DIFFRACTION37chain 'F' and (resid 21 through 30 )
38X-RAY DIFFRACTION38chain 'F' and (resid 31 through 47 )
39X-RAY DIFFRACTION39chain 'F' and (resid 48 through 57 )
40X-RAY DIFFRACTION40chain 'F' and (resid 58 through 92 )
41X-RAY DIFFRACTION41chain 'F' and (resid 93 through 156 )
42X-RAY DIFFRACTION42chain 'F' and (resid 157 through 174 )

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