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- PDB-5t5m: TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE FROM METHANO... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 5t5m
TitleTUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE FROM METHANOTHERMOBACTER WOLFEII, TRIGONAL FORM AT 2.5 A.
Components
  • (Tungsten formylmethanofuran dehydrogenase subunit ...) x 5
  • Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C
KeywordsOXIDOREDUCTASE / CO2 fixation / metallohydrolase / formate dehydrogenase / tungstopterin / methanogenesis / green house gas / methanothermobacter wolfeii / iron sulfur cluster / ferredoxin / beta helicoidal / channel / formate / CO2 / methanofuran / formylmethanofuran / nanomachine / binuclear center / tungsten / gate / coupling / enzyme / anaerobic / carboxylysine
Function / homology
Function and homology information


formylmethanofuran dehydrogenase / formylmethanofuran dehydrogenase activity / methanogenesis, from carbon dioxide / methanogenesis / hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / molybdopterin cofactor binding / transition metal ion binding / 4 iron, 4 sulfur cluster binding / oxidoreductase activity / metal ion binding
Similarity search - Function
FwdD/FmdC, molybdopterin dinucleotide-binding domain / : / : / : / : / Formylmethanofuran dehydrogenase, subunit D / Polyferredoxin MvhB-like / : / Formylmethanofuran dehydrogenase, subunit B / Formylmethanofuran dehydrogenase, subunit A ...FwdD/FmdC, molybdopterin dinucleotide-binding domain / : / : / : / : / Formylmethanofuran dehydrogenase, subunit D / Polyferredoxin MvhB-like / : / Formylmethanofuran dehydrogenase, subunit B / Formylmethanofuran dehydrogenase, subunit A / Formylmethanofuran dehydrogenase subunit C / Glutamate synthase, alpha subunit, C-terminal domain superfamily / Amidohydrolase 3 / Amidohydrolase family / : / 4Fe-4S binding domain / Molybdopterin dinucleotide-binding domain / Molydopterin dinucleotide binding domain / : / Barwin-like endoglucanases - #20 / Barwin-like endoglucanases / Metal-dependent hydrolase, composite domain superfamily / : / Aspartate decarboxylase-like domain superfamily / Molybdopterin oxidoreductase / Molybdopterin oxidoreductase / Metal-dependent hydrolase / 4Fe-4S dicluster 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 / Beta Barrel / Mainly Beta
Similarity search - Domain/homology
HYDROSULFURIC ACID / : / Chem-MGD / IRON/SULFUR CLUSTER / : / 4Fe-4S binding protein / Protein fwdD / Tungsten formylmethanofuran dehydrogenase subunit fwdA / Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C / Tungsten formylmethanofuran dehydrogenase subunit fwdB / 4Fe-4S binding protein
Similarity search - Component
Biological speciesMethanothermobacter wolfeii (archaea)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.5 Å
AuthorsWagner, T. / Ermler, U. / Shima, S.
Funding support Germany, Japan, 2items
OrganizationGrant numberCountry
Max Planck Society Germany
PRESTO Japan
CitationJournal: Science / Year: 2016
Title: The methanogenic CO2 reducing-and-fixing enzyme is bifunctional and contains 46 [4Fe-4S] clusters.
Authors: Wagner, T. / Ermler, U. / Shima, S.
History
DepositionAug 31, 2016Deposition site: RCSB / Processing site: PDBE
Revision 1.0Oct 19, 2016Provider: repository / Type: Initial release
Revision 1.1Dec 21, 2016Group: Database references
Revision 1.2Jan 17, 2024Group: 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_conn_type
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.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.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_ptnr1_label_alt_id / _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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Tungsten formylmethanofuran dehydrogenase subunit fwdA
B: Tungsten formylmethanofuran dehydrogenase subunit fwdB
C: Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C
D: Tungsten formylmethanofuran dehydrogenase subunit fwdD
F: Tungsten formylmethanofuran dehydrogenase subunit fwdF
G: Tungsten formylmethanofuran dehydrogenase subunit fwdG
hetero molecules


Theoretical massNumber of molelcules
Total (without water)207,51030
Polymers201,4246
Non-polymers6,08624
Water4,684260
1
A: Tungsten formylmethanofuran dehydrogenase subunit fwdA
B: Tungsten formylmethanofuran dehydrogenase subunit fwdB
C: Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C
D: Tungsten formylmethanofuran dehydrogenase subunit fwdD
F: Tungsten formylmethanofuran dehydrogenase subunit fwdF
G: Tungsten formylmethanofuran dehydrogenase subunit fwdG
hetero molecules

A: Tungsten formylmethanofuran dehydrogenase subunit fwdA
B: Tungsten formylmethanofuran dehydrogenase subunit fwdB
C: Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C
D: Tungsten formylmethanofuran dehydrogenase subunit fwdD
F: Tungsten formylmethanofuran dehydrogenase subunit fwdF
G: Tungsten formylmethanofuran dehydrogenase subunit fwdG
hetero molecules


Theoretical massNumber of molelcules
Total (without water)415,02060
Polymers402,84712
Non-polymers12,17248
Water21612
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_465y-1,x+1,-z1
Buried area60380 Å2
ΔGint-963 kcal/mol
Surface area115110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)105.543, 105.543, 340.549
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

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Components

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Tungsten formylmethanofuran dehydrogenase subunit ... , 5 types, 5 molecules ABDFG

#1: Protein Tungsten formylmethanofuran dehydrogenase subunit fwdA


Mass: 62806.594 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: FwdA contains a carboxylysine at the position 178 / Source: (natural) Methanothermobacter wolfeii (archaea)
References: UniProt: O74030*PLUS, formylmethanofuran dehydrogenase
#2: Protein Tungsten formylmethanofuran dehydrogenase subunit fwdB


Mass: 48411.355 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanothermobacter wolfeii (archaea)
References: UniProt: O74032*PLUS, formylmethanofuran dehydrogenase
#4: Protein Tungsten formylmethanofuran dehydrogenase subunit fwdD


Mass: 14408.779 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanothermobacter wolfeii (archaea)
References: UniProt: O74029*PLUS, formylmethanofuran dehydrogenase
#5: Protein Tungsten formylmethanofuran dehydrogenase subunit fwdF


Mass: 38618.570 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanothermobacter wolfeii (archaea) / References: UniProt: O74028*PLUS
#6: Protein Tungsten formylmethanofuran dehydrogenase subunit fwdG


Mass: 8564.948 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanothermobacter wolfeii (archaea) / References: UniProt: Q1MVD4*PLUS

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Protein , 1 types, 1 molecules C

#3: Protein Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C / Tungsten-containing formylmethanofuran dehydrogenase II subunit C


Mass: 28613.471 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Methanothermobacter wolfeii (archaea)
References: UniProt: O74031*PLUS, formylmethanofuran dehydrogenase

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Non-polymers , 9 types, 284 molecules

#7: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#8: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn
#9: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#10: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#11: Chemical
ChemComp-SF4 / IRON/SULFUR CLUSTER


Mass: 351.640 Da / Num. of mol.: 11 / Source method: obtained synthetically / Formula: Fe4S4
#12: Chemical ChemComp-W / TUNGSTEN ION


Mass: 183.840 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: W
#13: Chemical ChemComp-MGD / 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE / MOLYBDOPTERIN GUANOSINE DINUCLEOTIDE


Mass: 740.557 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Formula: C20H26N10O13P2S2
#14: Chemical ChemComp-H2S / HYDROSULFURIC ACID / HYDROGEN SULFIDE


Mass: 34.081 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: H2S
#15: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 260 / Source method: isolated from a natural source / Formula: H2O

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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: 2.72 Å3/Da / Density % sol: 54.84 % / Description: Large brown hexagons of 500 - 800 um cube
Crystal growTemperature: 291 K / Method: vapor diffusion, sitting drop / pH: 8
Details: 100 mM Tricine/NaOH, pH 8.0, 30% (v/v) pentaerythritol propoxylate 426 (5/4 PO/OH), and 400 mM KCl. The crystallized sample has to be perfectly anoxic and extremely fresh (crystallization ...Details: 100 mM Tricine/NaOH, pH 8.0, 30% (v/v) pentaerythritol propoxylate 426 (5/4 PO/OH), and 400 mM KCl. The crystallized sample has to be perfectly anoxic and extremely fresh (crystallization after 3 days of purification) without any freezing step. The optimal protein concentration is 30 mg/ml. Drops are made by mixing 1 ul of protein and 1 ul of precipitant. Crystals appeared usually after 7-10 days anoxically.
PH range: 7.5-8.5 / Temp details: Only one temperature has been tested

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1.00005 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jun 11, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.00005 Å / Relative weight: 1
ReflectionResolution: 2.5→48.65 Å / Num. obs: 77304 / % possible obs: 100 % / Redundancy: 7.5 % / CC1/2: 0.998 / Rmerge(I) obs: 0.09 / Rsym value: 0.035 / Net I/σ(I): 13.6
Reflection shellResolution: 2.5→2.64 Å / Redundancy: 7.8 % / Rmerge(I) obs: 0.94 / Mean I/σ(I) obs: 2.2 / CC1/2: 0.799 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(1.10.1_2155: ???)refinement
XDSdata reduction
SCALA3.3.22data scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB : 5T5I

5t5i


Resolution: 2.5→48.218 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 19.77
Details: After molecular replacement by MOLREP the model was first refined by rigid body using REFMAC, then using the restrained refinement of REFMAC. The last refinement cycles were done by PHENIX.
RfactorNum. reflection% reflectionSelection details
Rfree0.1817 3638 4.71 %Random selection
Rwork0.1576 ---
obs0.1587 77174 99.91 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.5→48.218 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms13936 0 208 260 14404
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01114482
X-RAY DIFFRACTIONf_angle_d1.67119741
X-RAY DIFFRACTIONf_dihedral_angle_d16.5988738
X-RAY DIFFRACTIONf_chiral_restr0.1352210
X-RAY DIFFRACTIONf_plane_restr0.0052538
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.5-2.53290.27761290.25252764X-RAY DIFFRACTION100
2.5329-2.56760.26321470.24752803X-RAY DIFFRACTION100
2.5676-2.60430.27511300.24092775X-RAY DIFFRACTION100
2.6043-2.64320.28531490.23372823X-RAY DIFFRACTION100
2.6432-2.68450.27991280.2322784X-RAY DIFFRACTION100
2.6845-2.72850.271330.23232753X-RAY DIFFRACTION100
2.7285-2.77550.25441380.22682851X-RAY DIFFRACTION100
2.7755-2.8260.27611430.24152748X-RAY DIFFRACTION100
2.826-2.88030.29071380.2352813X-RAY DIFFRACTION100
2.8803-2.93910.26311520.21082787X-RAY DIFFRACTION100
2.9391-3.0030.21551090.20632840X-RAY DIFFRACTION100
3.003-3.07290.2081350.19892770X-RAY DIFFRACTION100
3.0729-3.14970.261480.19092811X-RAY DIFFRACTION100
3.1497-3.23490.23251420.19952784X-RAY DIFFRACTION100
3.2349-3.330.2061350.18572840X-RAY DIFFRACTION100
3.33-3.43750.21291210.1862831X-RAY DIFFRACTION100
3.4375-3.56030.17391170.16732830X-RAY DIFFRACTION100
3.5603-3.70280.17741320.15842830X-RAY DIFFRACTION100
3.7028-3.87120.18661640.14972833X-RAY DIFFRACTION100
3.8712-4.07520.16471320.13392839X-RAY DIFFRACTION100
4.0752-4.33040.13461370.11822836X-RAY DIFFRACTION100
4.3304-4.66450.13721540.10872836X-RAY DIFFRACTION100
4.6645-5.13350.14941420.11122864X-RAY DIFFRACTION100
5.1335-5.87520.14711680.12362900X-RAY DIFFRACTION100
5.8752-7.39780.15151690.142890X-RAY DIFFRACTION100
7.3978-48.2270.15781460.14813101X-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)
10.9116-0.3534-0.38591.19960.21840.8044-0.02330.1769-0.2416-0.12740.0067-0.38290.09040.5380.01690.5220.01120.16140.9539-0.13460.8096-11.186822.8642-35.2627
21.0317-0.0840.53370.991-0.05191.29350.06360.4481-0.0659-0.32570.0189-0.2056-0.0150.409-0.08710.5632-0.02450.14510.65-0.0990.5158-34.298930.4093-39.6463
31.1213-0.31480.45221.3045-0.57111.13790.09780.4195-0.2496-0.43960.037-0.03850.13030.3282-0.08450.62480.00180.06450.6616-0.17150.5788-40.271917.538-43.9892
41.1467-0.2443-0.06461.2172-0.09630.89210.07310.1533-0.3374-0.16010.0486-0.16220.22180.3113-0.12950.45890.05590.02460.5111-0.11620.5782-32.130413.5794-27.0248
51.12890.3311-0.70061.2415-0.33421.34620.04070.2315-0.1073-0.1526-0.0041-0.5818-0.10090.6005-0.09490.56390.02390.1530.9268-0.20810.7676-12.516820.7904-36.8084
61.7668-0.5619-0.15581.51450.54450.7426-0.02990.77720.2033-0.58260.1313-0.2277-0.2970.3689-0.0610.8015-0.09750.18670.89050.02870.5014-36.519240.2061-51.9056
71.464-0.25970.27612.72740.18780.196-0.34630.92880.3696-0.62580.0598-0.3705-0.31320.24690.17671.0318-0.20.1410.8110.23610.733-37.516362.9584-43.711
81.6031-0.8360.52951.6133-0.14640.7776-0.20030.40410.6171-0.05920.1655-0.3896-0.65140.59660.17940.9209-0.35090.14760.92870.16721.1281-14.521970.1547-29.3441
91.537-0.27240.38362.02880.28051.8025-0.04790.24880.1738-0.35090.0606-0.6869-0.04450.2422-0.03610.6168-0.23040.1730.7643-0.01120.778-18.866852.3029-25.2792
102.24230.29310.41061.36090.17340.8616-0.09380.13320.4129-0.22940.05190.0427-0.30620.14920.04950.5238-0.04140.04650.35060.0030.4392-48.99751.1051-26.4058
114.17730.05050.66685.01083.26435.94860.0921-0.42740.05720.2483-0.29570.40210.3796-0.4680.08730.5034-0.03730.06830.4791-0.05750.5142-57.121744.3825-7.8604
121.74690.69491.59473.22211.89174.25-0.10270.010.2536-0.0472-0.04830.4563-0.1042-0.240.10490.4484-0.00460.08770.3966-0.00760.5528-54.77646.5018-18.3093
132.54810.14610.39090.38980.06521.16120.04020.00030.0661-0.00130.0345-0.1056-0.14860.3091-0.06310.5174-0.0890.07720.5275-0.05120.5571-34.819744.1147-20.3277
143.21830.14170.2951.1021-0.50853.0262-0.34960.150.7311-0.04530.0203-0.3575-0.16490.3730.05410.7037-0.19690.01320.7165-0.02490.7693-21.785759.0557-14.8846
153.0436-0.3245-0.02741.11450.02710.0069-0.08310.12770.8703-0.06030.17060.1034-0.38060.14240.08930.7474-0.29880.02230.644-0.00790.9093-23.69866.9448-18.5373
160.5618-0.69410.4790.9256-0.20160.4742-0.2010.81960.5205-0.53630.1164-0.4626-0.11830.45010.01010.8324-0.32820.24010.8870.04940.805-20.761256.8074-35.475
172.38-0.31960.431.4729-0.24871.4155-0.0194-0.26410.06560.04970.0597-0.4588-0.17490.5629-0.0170.4256-0.0819-0.00790.7866-0.14660.6893-12.905342.35624.2693
181.25150.3652-0.22241.32230.00471.27940.0196-0.21010.0340.12190.0521-0.2573-0.17140.2386-0.0210.4497-0.080.01660.5992-0.02850.5734-32.003240.42051.6053
192.7709-0.31680.69890.75740.32432.55750.1585-0.3404-0.00660.1682-0.0067-0.0732-0.1820.1379-0.12140.5631-0.09620.05520.5831-0.05560.5468-43.490242.8764.194
201.14630.8517-0.4842.58281.74573.0250.1937-0.6270.05830.8737-0.2924-0.27131.2083-0.2610.02270.7752-0.1297-0.00390.99050.07080.6413-49.348134.966414.9159
212.60440.0295-0.6114.12662.14096.18110.1391-0.5826-0.03030.2805-0.1680.74580.0244-0.35630.0930.4002-0.11370.06630.5982-0.00310.5307-52.608439.37595.3763
223.6037-0.1867-0.55884.09950.85915.6428-0.4896-0.4810.60130.1150.18360.159-0.62330.48930.15780.688-0.0755-0.00580.4041-0.05880.8017-45.670867.2172-11.7497
232.36671.39160.46751.3296-0.81292.4247-0.43390.38750.4093-0.00920.0262-0.2086-1.272-0.36960.10921.0727-0.27910.06050.59620.08810.9201-39.732169.7354-29.8765
244.77171.3193-2.90542.1365-0.12794.31290.1641-0.03270.5314-0.3925-0.2585-0.3022-0.11760.0564-0.08650.924-0.2704-0.12790.50320.16480.9342-35.913776.138-26.2039
255.1227-1.1181-0.90452.48610.44133.6822-0.0368-0.1632-0.106-0.07640.01580.1559-0.5941-0.02180.010.86570.0678-0.05510.4511-0.04810.9761-52.528476.1148-12.4543
262.8006-2.4510.70244.9594-1.86031.0823-0.3577-0.36250.4022-0.05220.1064-0.1052-0.4833-0.2450.09190.8048-0.0510.01680.5728-0.16110.8869-42.921877.0027-9.0117
274.58341.85940.7414.5451-0.7070.5439-0.2133-0.20250.89020.28550.00290.1593-0.52810.00380.38020.8708-0.04150.00760.3887-0.04690.7966-48.946573.0571-15.1966
281.5945-0.4138-0.2042.0687-0.74060.79060.0066-0.29720.4994-0.0031-0.02470.1474-0.45260.1880.0930.7542-0.09350.02730.5358-0.10690.7453-38.866265.2522-10.5289
291.648-2.5458-2.17353.92183.34192.87590.3254-0.2630.2341-0.407-0.49280.4653-0.70980.26150.3420.9896-0.163-0.06710.54010.05870.9881-36.970284.1158-13.3572
300.68220.6626-1.33074.248-1.28472.62320.0230.03230.4119-0.28520.2-0.4347-0.14730.2945-0.08111.0457-0.2937-0.01920.5292-0.05311.1178-25.608675.6677-15.4768
316.3423-3.23510.35584.7765-0.2153.0193-0.272-0.64681.1128-0.11940.0751-0.4027-0.6241-0.3580.11391.21460.186-0.16720.6327-0.12860.8336-89.814778.0335-42.4272
323.2345-1.69310.46091.2301-0.66791.2809-0.0810.09330.5304-0.0165-0.0286-0.1401-0.3541-0.04130.15741.08250.1034-0.12570.62790.01330.7419-82.956671.1871-46.6531
330.3741-0.01390.25110.3930.16910.5541-0.1145-0.49010.13110.3450.28140.378-0.4849-0.45960.00190.84190.25250.0030.95650.06650.7682-99.463260.3841-38.0397
340.437-0.58120.1771-0.03950.34844.57690.1376-0.1105-0.0361-0.11170.04650.0453-0.242-0.2269-0.22180.49130.043-0.07210.69040.01010.4856-87.150740.56616.4931
350.33890.49750.38490.34640.46310.70750.224-0.08960.08470.0508-0.04720.0364-0.391-0.7023-0.27110.76180.26650.04580.87770.12540.6127-97.256744.3612-15.2987
361.8922-0.46160.18271.0879-0.87221.3193-0.04240.17920.3616-0.19020.0127-0.024-0.2031-0.18290.06780.75030.0891-0.02230.53270.02390.5116-81.517349.2401-41.7509
375.8756-1.28821.31970.6914-0.93711.30150.28750.1372-0.5592-0.3316-0.19550.3312-0.23520.2419-0.01070.73030.0499-0.00440.5405-00.5919-71.687741.7912-39.9573
382.0327-0.7241.18890.4995-1.03832.0116-0.18170.2380.22830.07170.08460.0215-0.1785-0.11780.04470.81360.0956-0.05020.59230.03850.5313-87.328858.503-53.5339
392.3409-0.86530.62871.9279-0.87690.956-0.08210.47310.80250.1589-0.1966-0.2574-0.28330.11770.47550.8891-0.1067-0.02650.62360.18810.6875-56.764465.2282-42.3353
408.1809-1.8185-1.69942.1272.813.76480.33140.8730.7255-0.720.06810.00970.1387-0.2913-0.57731.0234-0.07360.0430.75990.15090.6407-50.648556.467-50.1693
414.0391-0.60462.42520.098-0.37481.46380.01281.1351.575-0.3627-0.2283-0.4333-0.66210.898-0.16991.1231-0.1647-0.09490.61170.19940.8001-49.589367.8716-44.8783
421.00660.4579-0.78110.2983-0.22450.7686-0.42240.57940.6292-0.29380.02780.5475-0.50640.20530.28291.1614-0.0829-0.14460.63720.22820.7755-62.112565.1066-45.698
432.03441.02660.01680.86151.20115.67960.1094-0.16890.8236-0.3213-0.58040.2959-0.2099-0.14920.22690.937-0.0878-0.06170.52740.07770.8126-61.333971.4292-37.9058
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 87 )
2X-RAY DIFFRACTION2chain 'A' and (resid 88 through 200 )
3X-RAY DIFFRACTION3chain 'A' and (resid 201 through 275 )
4X-RAY DIFFRACTION4chain 'A' and (resid 276 through 449 )
5X-RAY DIFFRACTION5chain 'A' and (resid 450 through 525 )
6X-RAY DIFFRACTION6chain 'A' and (resid 526 through 569 )
7X-RAY DIFFRACTION7chain 'B' and (resid 1 through 42 )
8X-RAY DIFFRACTION8chain 'B' and (resid 43 through 80 )
9X-RAY DIFFRACTION9chain 'B' and (resid 81 through 107 )
10X-RAY DIFFRACTION10chain 'B' and (resid 108 through 205 )
11X-RAY DIFFRACTION11chain 'B' and (resid 206 through 231 )
12X-RAY DIFFRACTION12chain 'B' and (resid 232 through 261 )
13X-RAY DIFFRACTION13chain 'B' and (resid 262 through 325 )
14X-RAY DIFFRACTION14chain 'B' and (resid 326 through 344 )
15X-RAY DIFFRACTION15chain 'B' and (resid 345 through 375 )
16X-RAY DIFFRACTION16chain 'B' and (resid 376 through 429 )
17X-RAY DIFFRACTION17chain 'C' and (resid 2 through 124 )
18X-RAY DIFFRACTION18chain 'C' and (resid 125 through 169 )
19X-RAY DIFFRACTION19chain 'C' and (resid 170 through 222 )
20X-RAY DIFFRACTION20chain 'C' and (resid 223 through 240 )
21X-RAY DIFFRACTION21chain 'C' and (resid 241 through 270 )
22X-RAY DIFFRACTION22chain 'D' and (resid 1 through 10 )
23X-RAY DIFFRACTION23chain 'D' and (resid 11 through 19 )
24X-RAY DIFFRACTION24chain 'D' and (resid 20 through 30 )
25X-RAY DIFFRACTION25chain 'D' and (resid 31 through 43 )
26X-RAY DIFFRACTION26chain 'D' and (resid 44 through 58 )
27X-RAY DIFFRACTION27chain 'D' and (resid 59 through 74 )
28X-RAY DIFFRACTION28chain 'D' and (resid 75 through 109 )
29X-RAY DIFFRACTION29chain 'D' and (resid 110 through 116 )
30X-RAY DIFFRACTION30chain 'D' and (resid 117 through 126 )
31X-RAY DIFFRACTION31chain 'F' and (resid 2 through 35 )
32X-RAY DIFFRACTION32chain 'F' and (resid 36 through 85 )
33X-RAY DIFFRACTION33chain 'F' and (resid 86 through 119 )
34X-RAY DIFFRACTION34chain 'F' and (resid 120 through 208 )
35X-RAY DIFFRACTION35chain 'F' and (resid 209 through 243 )
36X-RAY DIFFRACTION36chain 'F' and (resid 244 through 285 )
37X-RAY DIFFRACTION37chain 'F' and (resid 286 through 307 )
38X-RAY DIFFRACTION38chain 'F' and (resid 308 through 349 )
39X-RAY DIFFRACTION39chain 'G' and (resid 2 through 28 )
40X-RAY DIFFRACTION40chain 'G' and (resid 29 through 45 )
41X-RAY DIFFRACTION41chain 'G' and (resid 46 through 55 )
42X-RAY DIFFRACTION42chain 'G' and (resid 56 through 70 )
43X-RAY DIFFRACTION43chain 'G' and (resid 71 through 81 )

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