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- PDB-7ot4: Crystal structure of MsrA variant C198C206 from Escherichia coli,... -

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Basic information

Entry
Database: PDB / ID: 7ot4
TitleCrystal structure of MsrA variant C198C206 from Escherichia coli, oxidized
ComponentsPeptide methionine sulfoxide reductase MsrA
KeywordsOXIDOREDUCTASE / S-Methionine sulfoxide reductase / Oxidative stress / Redox chemistry / Disulfide exchange
Function / homology: / peptide-methionine (S)-S-oxide reductase / peptide-methionine (S)-S-oxide reductase activity / Peptide methionine sulphoxide reductase MsrA domain / Peptide methionine sulphoxide reductase MsrA superfamily / Peptide methionine sulfoxide reductase / protein modification process / : / Peptide methionine sulfoxide reductase MsrA
Function and homology information
Biological speciesEscherichia coli (E. coli)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.19 Å
AuthorsNapolitano, S. / Glockshuber, R.
CitationJournal: To Be Published
Title: Exploring the unique mechanism of methionine sulphoxide reduction by Escherichia coli
Authors: Napolitano, S. / Glockshuber, R.
History
DepositionJun 9, 2021Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jun 22, 2022Provider: repository / Type: Initial release
Revision 1.1Jan 31, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id
Revision 1.2Oct 16, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Peptide methionine sulfoxide reductase MsrA
B: Peptide methionine sulfoxide reductase MsrA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)46,6153
Polymers46,5762
Non-polymers391
Water19811
1
A: Peptide methionine sulfoxide reductase MsrA


Theoretical massNumber of molelcules
Total (without water)23,2881
Polymers23,2881
Non-polymers00
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Peptide methionine sulfoxide reductase MsrA
hetero molecules


Theoretical massNumber of molelcules
Total (without water)23,3272
Polymers23,2881
Non-polymers391
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)128.210, 128.210, 118.340
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number178
Space group name H-MP6122
Components on special symmetry positions
IDModelComponents
11A-304-

HOH

Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 8 through 124 or resid 126...
21(chain B and (resid 8 through 124 or resid 126...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11LEULEUMETMET(chain A and (resid 8 through 124 or resid 126...AA8 - 1249 - 125
12GLNGLNGLYGLY(chain A and (resid 8 through 124 or resid 126...AA126 - 127127 - 128
13ASPASPLYSLYS(chain A and (resid 8 through 124 or resid 126...AA129 - 192130 - 193
14PROPROPROPRO(chain A and (resid 8 through 124 or resid 126...AA194 - 209195 - 210
21LEULEUMETMET(chain B and (resid 8 through 124 or resid 126...BB8 - 1249 - 125
22GLNGLNGLYGLY(chain B and (resid 8 through 124 or resid 126...BB126 - 127127 - 128
23ASPASPLYSLYS(chain B and (resid 8 through 124 or resid 126...BB129 - 192130 - 193
24PROPROPROPRO(chain B and (resid 8 through 124 or resid 126...BB194 - 209195 - 210

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Components

#1: Protein Peptide methionine sulfoxide reductase MsrA / Protein-methionine-S-oxide reductase / Peptide-methionine (S)-S-oxide reductase / Peptide Met(O) reductase


Mass: 23287.852 Da / Num. of mol.: 2 / Mutation: C51S, C86A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli)
Gene: msrA, A6592_17460, A6V01_22160, A9819_24155, A9R57_13955, A9X72_22535, ACN68_19045, ACN81_01285, ACU57_15535, ACU90_02300, AM464_14885, AM465_01705, AMK83_03835, AML35_13410, APT94_15450, AUQ13_ ...Gene: msrA, A6592_17460, A6V01_22160, A9819_24155, A9R57_13955, A9X72_22535, ACN68_19045, ACN81_01285, ACU57_15535, ACU90_02300, AM464_14885, AM465_01705, AMK83_03835, AML35_13410, APT94_15450, AUQ13_10725, AUS26_22290, AW059_07990, AWB10_23285, AWP75_26990, B9N33_15470, BANRA_00188, BANRA_00230, BANRA_02702, BANRA_02915, BB545_15285, BFD68_08870, BHF03_14550, BHS87_23645, BIZ41_03105, BJJ90_23040, BK375_06465, BK383_13340, BMA87_05905, BMT91_05895, BN17_42051, BOH76_10610, BON63_02590, BON65_11980, BON75_01645, BON76_03840, BON83_23625, BON95_15255, BON98_15750, BTQ06_19075, BUE81_20720, BvCms12BK_04699, BvCms2454_04304, BvCms28BK_05285, BvCmsC61A_01635, BvCmsHHP001_04534, BvCmsHHP019_05480, BvCmsKKP061_03410, BvCmsKSNP073_00278, BvCmsKSNP081_02732, BvCmsKSNP120_00804, BvCmsKSP011_04615, BvCmsKSP024_01206, BvCmsKSP026_01492, BvCmsKSP045_02422, BvCmsKSP067_03789, BvCmsKSP076_04442, BvCmsNSP006_00888, BvCmsNSP047_01965, BvCmsNSP072_05264, BvCmsOUP014_01667, BvCmsSINP011_01393, BvCmsSINP022_01072, BvCmsSIP019_03154, BvCmsSIP044_02391, BW690_00830, BZL31_09640, C5F72_23370, C5P44_17370, C6669_06275, C7B02_22170, C7B06_04165, C7B07_05980, C9114_01095, C9160_23855, C9201_22630, C9306_17800, C9342_05495, C9E25_07850, C9Z03_24630, C9Z28_09220, C9Z70_20765, CCZ14_17380, CCZ17_16730, CDC27_22925, CG692_00495, CI693_13070, CI694_17565, CO706_21060, COD30_25450, CR538_22825, CR539_03060, CRD98_03870, CRM83_17080, CRT43_25425, CV83915_01803, CWS33_03825, D2184_07435, D2185_08065, D3821_06790, D3O91_01830, D3Y67_00980, D4011_01915, D4023_15585, D4M76_01215, D5H35_21445, D6004_20735, D6T60_20150, D6X63_00220, D7Z75_16660, D8Y65_09230, D9610_20340, D9C99_08370, D9D20_08010, D9D31_16930, D9D43_13455, D9D44_05500, D9E34_13765, D9E35_09520, D9E73_04160, D9F87_11530, D9G42_19950, D9G48_01620, D9G69_19855, D9G95_08975, D9H68_13095, D9H70_18045, D9H94_06035, D9I18_04110, D9I87_13570, D9I88_14655, D9J11_13215, D9J52_05515, D9K54_24800, D9Z28_11705, DAH30_08995, DAH34_12995, DB359_11580, DD762_15940, DEN89_12175, DEO04_15285, DEO20_14040, DIV22_06565, DJ503_08915, DL530_20830, DL545_22295, DL705_07780, DL800_29420, DLU82_15475, DLX40_05910, DM102_02755, DM155_20895, DMZ30_13865, DMZ50_17110, DN627_16845, DN660_13710, DNC98_05295, DND79_18280, DNI21_17925, DNQ45_11385, DOT59_23360, DOY22_05015, DOY61_24010, DOY67_21605, DP258_05820, DQF57_15420, DQO13_17920, DQP61_08220, DRW19_17935, DS143_21960, DS732_02935, DT034_15090, DTL43_02630, DTL90_15510, DXT69_10870, DXT71_04540, DXT73_19330, E0L04_15460, E2112_15545, E2119_06205, E2127_06610, E2128_01660, E2129_03740, E2134_14275, E2135_08520, E2855_05322, E2863_05108, E4K60_13295, E4K61_05415, E5P24_09045, E5P28_02650, E5S38_18510, E5S42_20885, E5S56_12105, EA167_13440, EA184_17925, EA191_15445, EA203_13320, EA214_16225, EA433_20540, EA435_16790, EA834_13075, EAI42_24725, EAI46_19520, EAI52_08400, EAM59_16090, EAX79_02640, EB525_RS06735, EBM08_19230, EBP16_19605, EC1094V2_4030, EC3234A_79c00360, EC382_06000, EC95NR1_04019, ECONIH1_25080, ECTO124_04467, ECTO6_04257, ED600_07980, EEP23_05875, EG599_21735, EG808_09990, EGT48_18060, EH412_13705, EHD79_06020, EHJ36_13695, EI032_03170, EI041_05275, EIA08_16840, EIA21_17575, EIZ93_19780, EJC75_20885, EKI52_12405, EL75_3920, EL79_4069, EL80_4014, ELT31_18190, ELU82_08075, ELU96_21205, ELV00_12325, ELV13_11150, ELV15_14980, ELV22_08835, ELV28_19765, ELX56_16620, ELX61_05255, ELX68_09325, ELX70_18095, ELX79_11575, ELX83_06775, ELX96_12310, ELY05_00265, ELY23_03385, ELY24_02925, ELY32_08785, ELY41_11275, ELY48_12825, ELY50_08105, EO241_14620, EPT01_05865, EQ820_18660, EQ823_02285, EQ825_20995, ERS085366_02549, ERS085379_03314, ERS150873_03427, EST51_22625, ETECE1373_04211, ETECE1441_04282, ETECE1649_04094, ETECE36_05128, ETECE925_04220, ExPECSC065_03274, EXX13_21670, EXX23_18580, EXX24_18255, EXX53_16845, EXX71_14425, EXX87_19450, EYY34_12615, EYY78_02130, F1E19_03805, F6T45_09250, F6V70_02160, F7F23_22960, F7F26_24290, F7F56_08770, F9B07_18980, FAF34_006545, FNJ67_23665, FORC82_4265, FQ915_10240, FRV13_14375, FV293_01115, FV438_02020, FVA71_23160, FWK02_01540, G3565_21525, G5632_10450, G5668_21440, G5670_14635, G5680_22415, G5688_19665, G9448_11945, G9P49_19800, GE087_07420, GE400_14405, GHD50_06085, GIJ01_09270, GKF39_06735, GKF74_12125, GKF86_05755, GKF89_03710, GNZ05_12355, GP650_20315, GP662_17285, GP666_16615, GP698_01995, GP720_11320, GP935_18440, GP945_15925, GP946_15985, GP979_15915, GQE22_07830, GQE33_09510, GQE34_01440, GQE36_11865, GQE42_11730, GQE64_08850, GQM04_20020, GQM09_09185, GQM17_02345, GQN24_16985, GRC73_06690, GRW02_11095, GRW05_26995, GRW80_01610, GRW81_08665, GUB85_11035, GUB91_13005, GUB95_12125, GUC01_09315, GUC12_13155, GUI33_11120, GXC14_19820, H4P50_22505, H4P51_22355, HCR07_14670, HF523_08910, HFD31_004234, HFD39_002834, HFD59_004153, HFD69_004401, HFU80_002607, HGR36_13395, HGR87_08455, HGR88_04040, HGS82_06160, HGS97_09555, HGT58_01755, HH117_13715, HH707_003742, HH814_001391, HH830_000850, HHA77_003089, HHH24_003061, HHJ41_04860, HI083_002578, HIB31_000956, HIQ74_002789, HIQ82_003749, HIZ62_001860, HJO53_002365, HJQ03_001278, HJR60_001736, HJR92_003107, HJT66_003563, HJV81_002303, HKA45_001551, HKA57_002237, HKC58_000390, HL152_03135, HL186_17480, HL563_16800, HLI97_003230, HLQ75_20685, HLQ92_21545, HmCmsJML074_00463, HmCmsJML079_00342, HMG20_11140, HMG24_21700, HMG27_20805, HMG35_20970, HMT01_21425, HMT08_18515, HMW26_07810, HNC40_00945, HNC59_12305, HNC80_10860, HNC94_15570, HNC99_15735, HNN86_00180, HNO03_11350, HNV44_15800, HNX16_17490, HR075_15705, HS093_11360, HV005_18995, HV021_19940, HV022_21055, HV068_21310, HV109_21215, HV152_20700, HV156_10990, HV159_13150, HV188_02390, HV226_02385, HV244_19735, HV303_17205, HVV38_13050, HVV53_19330, HVV70_01715, HVV73_20800, HVV78_02090, HVW09_01805, HVW11_07660, HVW37_21770, HVW43_13740, HVW59_11650, HVW60_20400, HVW76_19850, HVW90_11360, HVW98_01840, HVX22_20520, HVX24_19855, HVX51_21410, HVX60_12690, HVX69_21685, HVY77_22850, HVY79_02025, HVY93_21140, HVZ20_02425, HVZ24_20100, HVZ53_21695, HVZ62_11985, HVZ71_22295, HX136_22430, HZT35_14855, NCTC10090_02527, NCTC10963_04521, NCTC11022_04563, NCTC11341_03130, NCTC13216_02361, NCTC7922_05378, NCTC7927_04920, NCTC8009_07871, NCTC8179_00863, NCTC8500_04992, NCTC8621_04456, NCTC8959_04230, NCTC8960_01968, NCTC8985_03657, NCTC9001_04918, NCTC9036_04349, NCTC9044_02719, NCTC9045_05157, NCTC9055_01336, NCTC9058_02464, NCTC9062_03772, NCTC9073_03861, NCTC9111_04633, NCTC9119_04655, NCTC9702_05217, NCTC9706_01736, NCTC9777_00817, PGD_03408, PU06_09400, RG28_05635, RK56_012680, RX35_04489, SAMEA3472043_02207, SAMEA3472044_01471, SAMEA3472047_03207, SAMEA3472055_03047, SAMEA3472056_04781, SAMEA3472070_02714, SAMEA3472080_00044, SAMEA3472114_01822, SAMEA3484427_02138, SAMEA3484429_03178, SAMEA3484434_02297, SAMEA3485101_00769, SAMEA3752553_03605, SAMEA3752557_01725, SAMEA3752559_00096, SAMEA3753064_01666, SAMEA3753097_01293, SAMEA3753290_02155, SAMEA3753300_00596, SK85_04588, SY51_24315, TUM18780_39120, U14A_04626, UN86_21090, WP2S18E08_42160, WP4S17E03_41820, WP4S17E08_40640, WP4S18E08_40750, WP7S17E04_39140, WQ89_17475, WR15_06740
Production host: Escherichia coli BL21(DE3) (bacteria)
References: UniProt: J7RCD1, peptide-methionine (S)-S-oxide reductase
#2: Chemical ChemComp-K / POTASSIUM ION


Mass: 39.098 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: K
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 11 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestN
Has protein modificationY

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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: 2.94 Å3/Da / Density % sol: 58.2 %
Crystal growTemperature: 277.15 K / Method: vapor diffusion, sitting drop / pH: 6.5
Details: 0.1 M BIS-TRIS propane pH 6.5, 0.15 M KSCN, 20% PEG 3350

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Data collection

DiffractionMean temperature: 90 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1.283 Å
DetectorType: DECTRIS PILATUS 2M-F / Detector: PIXEL / Date: Nov 5, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.283 Å / Relative weight: 1
ReflectionResolution: 2.19→43.48 Å / Num. obs: 30052 / % possible obs: 99.9 % / Redundancy: 36.505 % / Biso Wilson estimate: 56.16 Å2 / CC1/2: 1 / Rmerge(I) obs: 0.124 / Rpim(I) all: 0.021 / Rrim(I) all: 0.126 / Χ2: 0.757 / Net I/σ(I): 24.84
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
2.19-2.2524.8315.6820.7221760.5335.79499.6
2.25-2.3129.544.5171.121020.7244.59699.8
2.31-2.3733.5973.7611.4320760.8133.81899.9
2.37-2.4538.2963.3381.7820040.8473.382100
2.45-2.5338.6422.3082.619590.9532.33999.9
2.53-2.6238.9711.5183.9218960.951.538100
2.62-2.7237.9961.0885.2618180.9751.102100
2.72-2.8339.020.7777.3217800.9910.78799.9
2.83-2.9539.3620.53110.3716910.9930.53899.9
2.95-3.138.7760.38113.7416150.9960.38699.9
3.1-3.2640.8250.24420.9415540.9980.24799.9
3.26-3.4640.0270.17627.2514840.9990.178100
3.46-3.738.6570.09941.27138810.1100
3.7-437.0390.07649.6129610.077100
4-4.3837.7580.05566120810.055100
4.38-4.938.4510.04678.94109410.047100
4.9-5.6538.6510.04187.9699110.041100
5.65-6.9235.7440.03791.2884010.038100
6.92-9.7934.6070.028122.7767910.029100
9.79-43.4832.7520.027131.1540810.02798.3

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHENIX1.19rc5_4047refinement
PDB_EXTRACT3.27data extraction
XDSdata reduction
BALBESphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1FF3

1ff3


Resolution: 2.19→43.48 Å / SU ML: 0.49 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 43.79 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3076 2800 5.03 %
Rwork0.286 52917 -
obs0.2871 29958 99.43 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 192.6 Å2 / Biso mean: 96.4038 Å2 / Biso min: 46.42 Å2
Refinement stepCycle: final / Resolution: 2.19→43.48 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3123 0 1 11 3135
Biso mean--167.76 76.34 -
Num. residues----405
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A1818X-RAY DIFFRACTION8.302TORSIONAL
12B1818X-RAY DIFFRACTION8.302TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.19-2.230.50271260.49242492261894
2.23-2.270.5051410.46122637277899
2.27-2.310.43261380.448826442782100
2.31-2.360.42981410.45472657279899
2.36-2.410.49951400.435426462786100
2.41-2.470.37441410.416726662807100
2.47-2.530.41631420.381626452787100
2.53-2.60.40641400.360226522792100
2.6-2.670.40671410.36326632804100
2.67-2.760.36161400.371926332773100
2.76-2.860.31231430.348626782821100
2.86-2.970.35871440.360726412785100
2.97-3.110.38851420.386126502792100
3.11-3.270.34321340.323626662800100
3.27-3.480.32441420.307826402782100
3.48-3.740.32871430.287626452788100
3.74-4.120.2931400.266826582798100
4.12-4.720.23721420.228626832825100
4.72-5.940.2711400.217526442784100
5.94-43.480.23461400.212426772817100
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)
10.86040.1734-0.21031.2633-0.63161.7595-0.2120.0991-0.1475-0.17090.07720.08460.9174-0.14520.1022.0677-0.17940.14150.4143-0.06090.639555.8225-11.8885-17.8962
21.24840.2996-0.28721.6847-1.03641.4115-0.4337-0.0902-0.17180.1310.24420.21750.5537-0.15460.00872.2744-0.23360.13850.52670.02160.574151.6539-11.5258-11.0023
30.63020.2965-0.39370.139-0.18810.2526-0.0301-0.3599-0.20580.2333-0.11570.14530.1839-0.0184-0.01172.4711-0.41010.1180.66630.08830.645448.9016-15.6084-5.9729
40.4573-0.1463-0.49120.17920.69732.7302-0.2812-0.54460.0279-0.05940.16960.0357-0.1403-0.38640.13541.8920.0631-0.01010.6664-0.05620.758356.18466.6581-10.7096
50.0180.043-0.09422.5107-0.880.64160.2-0.33540.35620.1392-0.09630.54941.1093-0.8969-0.09431.483-0.5424-0.00160.71810.00560.756845.6866-4.4833-35.8855
61.61860.4133-0.69730.7726-0.55443.4004-0.15810.3216-0.008-0.60660.3629-0.10270.578-0.7028-0.14460.9859-0.164-0.14680.29320.14850.69150.966613.9739-38.1584
71.27441.0551-0.39451.1771-1.08913.5851-0.47720.6844-0.2187-0.82370.33190.14810.8396-0.93930.17591.6086-0.7096-0.20940.95390.04120.773240.4794-3.3041-38.5649
82.54260.00380.14612.1735-0.30365.1027-0.02320.13860.1977-0.24220.2451-0.01790.2317-1.1711-0.35480.9361-0.051-0.09070.46710.20260.604445.014719.6379-33.491
94.3439-0.1109-0.08220.8917-0.95321.13280.19670.9362-0.8393-0.43050.27040.65710.8815-2.0036-0.43951.1809-0.464-0.35171.94780.39011.263930.597711.1032-43.0559
103.7368-0.47341.15781.15070.16993.4850.00050.1915-0.1737-0.18290.48340.46230.3061-1.823-0.44240.9265-0.3027-0.11611.2550.35170.704334.895616.7021-29.9174
110.6542-0.86930.7871.7294-1.45983.4791-0.51440.0638-0.28440.29520.56270.62540.2038-1.1029-0.09571.2756-0.522-0.0990.95910.19260.863136.009710.3598-33.6274
123.69151.0696-0.68321.7358-0.06443.47320.21650.77970.4803-0.89550.02650.34280.0849-0.4958-0.19381.4595-0.2481-0.24620.79680.1380.646550.05519.7289-51.2067
131.0026-0.0612-1.32234.67392.22952.76740.2044-0.308-0.13810.44250.1727-0.21290.6557-0.0393-0.33521.3595-0.0404-0.34291.18320.27621.166440.94216.7025-61.5072
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 8 through 61 )A8 - 61
2X-RAY DIFFRACTION2chain 'A' and (resid 62 through 131 )A62 - 131
3X-RAY DIFFRACTION3chain 'A' and (resid 132 through 188 )A132 - 188
4X-RAY DIFFRACTION4chain 'A' and (resid 189 through 209 )A189 - 209
5X-RAY DIFFRACTION5chain 'B' and (resid 8 through 27 )B8 - 27
6X-RAY DIFFRACTION6chain 'B' and (resid 28 through 73 )B28 - 73
7X-RAY DIFFRACTION7chain 'B' and (resid 74 through 92 )B74 - 92
8X-RAY DIFFRACTION8chain 'B' and (resid 93 through 117 )B93 - 117
9X-RAY DIFFRACTION9chain 'B' and (resid 118 through 131 )B118 - 131
10X-RAY DIFFRACTION10chain 'B' and (resid 132 through 163 )B132 - 163
11X-RAY DIFFRACTION11chain 'B' and (resid 164 through 183 )B164 - 183
12X-RAY DIFFRACTION12chain 'B' and (resid 184 through 197 )B184 - 197
13X-RAY DIFFRACTION13chain 'B' and (resid 198 through 210 )B198 - 210

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