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- PDB-6txj: Crystal structure of thermotoga maritima A42V E65D Ferritin -

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Basic information

Entry
Database: PDB / ID: 6txj
TitleCrystal structure of thermotoga maritima A42V E65D Ferritin
ComponentsFerritin
KeywordsMETAL BINDING PROTEIN / Metal binding / engineered protein
Function / homology
Function and homology information


bacterial non-heme ferritin / intracellular sequestering of iron ion / ferroxidase activity / ferric iron binding / ferrous iron binding / iron ion transport / cytosol / cytoplasm
Similarity search - Function
Ferritin, prokaryotic-type / Ferritin / Ferritin-like diiron domain / Ferritin-like diiron domain profile. / Ferritin/DPS protein domain / Ferritin-like domain / Ferritin-like / Ferritin-like superfamily
Similarity search - Domain/homology
: / EICOSANE / Ferritin
Similarity search - Component
Biological speciesThermotoga maritima (bacteria)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.17 Å
AuthorsWilk, P. / Grudnik, P. / Kumar, M. / Heddle, J. / Chakraborti, S. / Biela, A.P.
Funding support Poland, 1items
OrganizationGrant numberCountry
Foundation for Polish ScienceHoming/2017-3/22 Poland
CitationJournal: Nanoscale / Year: 2021
Title: A single residue can modulate nanocage assembly in salt dependent ferritin.
Authors: Kumar, M. / Markiewicz-Mizera, J. / Janna Olmos, J.D. / Wilk, P. / Grudnik, P. / Biela, A.P. / Jemiola-Rzeminska, M. / Gorecki, A. / Chakraborti, S. / Heddle, J.G.
History
DepositionJan 14, 2020Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 28, 2021Provider: repository / Type: Initial release
Revision 1.1Feb 9, 2022Group: Database references / Category: citation / citation_author / database_2
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._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 / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 1.2Jan 24, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / citation / pdbx_initial_refinement_model
Item: _citation.country

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Ferritin
B: Ferritin
C: Ferritin
D: Ferritin
E: Ferritin
F: Ferritin
G: Ferritin
H: Ferritin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)160,91162
Polymers155,3278
Non-polymers5,58454
Water2,630146
1
A: Ferritin
B: Ferritin
C: Ferritin
D: Ferritin
E: Ferritin
F: Ferritin
G: Ferritin
H: Ferritin
hetero molecules

A: Ferritin
B: Ferritin
C: Ferritin
D: Ferritin
E: Ferritin
F: Ferritin
G: Ferritin
H: Ferritin
hetero molecules

A: Ferritin
B: Ferritin
C: Ferritin
D: Ferritin
E: Ferritin
F: Ferritin
G: Ferritin
H: Ferritin
hetero molecules


Theoretical massNumber of molelcules
Total (without water)482,732186
Polymers465,98124
Non-polymers16,751162
Water43224
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_665-y+1,x-y+1,z1
crystal symmetry operation3_565-x+y,-x+1,z1
Buried area90210 Å2
ΔGint-602 kcal/mol
Surface area144640 Å2
MethodPISA
Unit cell
Length a, b, c (Å)176.203, 176.203, 352.794
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number155
Space group name H-MH32
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 2 through 38 or resid 40...
21(chain B and (resid 2 through 38 or resid 40...
31(chain C and (resid 2 through 38 or resid 40...
41(chain D and (resid 2 through 38 or resid 40...
51(chain E and (resid 2 through 38 or resid 40...
61(chain F and (resid 2 through 38 or resid 40...
71(chain G and (resid 2 through 38 or resid 40...
81(chain H and (resid 2 through 38 or resid 40...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 2 through 38 or resid 40...A2 - 38
121(chain A and (resid 2 through 38 or resid 40...A40 - 49
131(chain A and (resid 2 through 38 or resid 40...A51 - 57
141(chain A and (resid 2 through 38 or resid 40...A59 - 68
151(chain A and (resid 2 through 38 or resid 40...A86 - 111
161(chain A and (resid 2 through 38 or resid 40...A2 - 164
171(chain A and (resid 2 through 38 or resid 40...A132 - 134
181(chain A and (resid 2 through 38 or resid 40...A136 - 137
191(chain A and (resid 2 through 38 or resid 40...A139 - 1403
1101(chain A and (resid 2 through 38 or resid 40...A145 - 13
1111(chain A and (resid 2 through 38 or resid 40...A145 - 148
1121(chain A and (resid 2 through 38 or resid 40...A150 - 154
1131(chain A and (resid 2 through 38 or resid 40...A156 - 157
1141(chain A and (resid 2 through 38 or resid 40...A159 - 164
211(chain B and (resid 2 through 38 or resid 40...B2 - 38
221(chain B and (resid 2 through 38 or resid 40...B40 - 49
231(chain B and (resid 2 through 38 or resid 40...B51 - 57
241(chain B and (resid 2 through 38 or resid 40...B59 - 68
251(chain B and (resid 2 through 38 or resid 40...B86 - 111
261(chain B and (resid 2 through 38 or resid 40...B1 - 164
271(chain B and (resid 2 through 38 or resid 40...B132 - 134
281(chain B and (resid 2 through 38 or resid 40...B136 - 137
291(chain B and (resid 2 through 38 or resid 40...B139 - 1403
2101(chain B and (resid 2 through 38 or resid 40...B145 - 13
2111(chain B and (resid 2 through 38 or resid 40...B145 - 148
2121(chain B and (resid 2 through 38 or resid 40...B150 - 154
2131(chain B and (resid 2 through 38 or resid 40...B156 - 157
2141(chain B and (resid 2 through 38 or resid 40...B159 - 164
311(chain C and (resid 2 through 38 or resid 40...C2 - 38
321(chain C and (resid 2 through 38 or resid 40...C40 - 49
331(chain C and (resid 2 through 38 or resid 40...C1 - 164
341(chain C and (resid 2 through 38 or resid 40...C0
351(chain C and (resid 2 through 38 or resid 40...C86 - 3
361(chain C and (resid 2 through 38 or resid 40...C113 - 122
371(chain C and (resid 2 through 38 or resid 40...C12422
381(chain C and (resid 2 through 38 or resid 40...C124 - 130
391(chain C and (resid 2 through 38 or resid 40...C132 - 134
3101(chain C and (resid 2 through 38 or resid 40...C139 - 1403
3111(chain C and (resid 2 through 38 or resid 40...C145 - 1
3121(chain C and (resid 2 through 38 or resid 40...C145 - 13
3131(chain C and (resid 2 through 38 or resid 40...C145 - 148
3141(chain C and (resid 2 through 38 or resid 40...C150 - 154
3151(chain C and (resid 2 through 38 or resid 40...C156 - 157
3161(chain C and (resid 2 through 38 or resid 40...C159 - 164
411(chain D and (resid 2 through 38 or resid 40...D2 - 38
421(chain D and (resid 2 through 38 or resid 40...D40 - 49
431(chain D and (resid 2 through 38 or resid 40...D51 - 57
441(chain D and (resid 2 through 38 or resid 40...D86 - 111
451(chain D and (resid 2 through 38 or resid 40...D113 - 122
461(chain D and (resid 2 through 38 or resid 40...D2 - 164
471(chain D and (resid 2 through 38 or resid 40...D124 - 130
481(chain D and (resid 2 through 38 or resid 40...D132 - 134
491(chain D and (resid 2 through 38 or resid 40...D139 - 1403
4101(chain D and (resid 2 through 38 or resid 40...D145 - 1
4111(chain D and (resid 2 through 38 or resid 40...D145 - 13
4121(chain D and (resid 2 through 38 or resid 40...D145 - 148
4131(chain D and (resid 2 through 38 or resid 40...D150 - 154
4141(chain D and (resid 2 through 38 or resid 40...D156 - 157
4151(chain D and (resid 2 through 38 or resid 40...D159 - 164
511(chain E and (resid 2 through 38 or resid 40...E2 - 38
521(chain E and (resid 2 through 38 or resid 40...E40 - 49
531(chain E and (resid 2 through 38 or resid 40...E51 - 57
541(chain E and (resid 2 through 38 or resid 40...E86 - 111
551(chain E and (resid 2 through 38 or resid 40...E113 - 122
561(chain E and (resid 2 through 38 or resid 40...E1 - 164
571(chain E and (resid 2 through 38 or resid 40...E124 - 130
581(chain E and (resid 2 through 38 or resid 40...E132 - 134
591(chain E and (resid 2 through 38 or resid 40...E139 - 1403
5101(chain E and (resid 2 through 38 or resid 40...E145 - 1
5111(chain E and (resid 2 through 38 or resid 40...E145 - 13
5121(chain E and (resid 2 through 38 or resid 40...E145 - 148
5131(chain E and (resid 2 through 38 or resid 40...E150 - 154
5141(chain E and (resid 2 through 38 or resid 40...E156 - 157
5151(chain E and (resid 2 through 38 or resid 40...E159 - 164
611(chain F and (resid 2 through 38 or resid 40...F2 - 38
621(chain F and (resid 2 through 38 or resid 40...F40 - 49
631(chain F and (resid 2 through 38 or resid 40...F51 - 57
641(chain F and (resid 2 through 38 or resid 40...F86 - 111
651(chain F and (resid 2 through 38 or resid 40...F113 - 122
661(chain F and (resid 2 through 38 or resid 40...F1 - 164
671(chain F and (resid 2 through 38 or resid 40...F124 - 130
681(chain F and (resid 2 through 38 or resid 40...F132 - 134
691(chain F and (resid 2 through 38 or resid 40...F139 - 1403
6101(chain F and (resid 2 through 38 or resid 40...F145 - 1
6111(chain F and (resid 2 through 38 or resid 40...F145 - 13
6121(chain F and (resid 2 through 38 or resid 40...F145 - 148
6131(chain F and (resid 2 through 38 or resid 40...F150 - 154
6141(chain F and (resid 2 through 38 or resid 40...F156 - 157
6151(chain F and (resid 2 through 38 or resid 40...F159 - 164
711(chain G and (resid 2 through 38 or resid 40...G2 - 38
721(chain G and (resid 2 through 38 or resid 40...G40 - 49
731(chain G and (resid 2 through 38 or resid 40...G51 - 57
741(chain G and (resid 2 through 38 or resid 40...G59 - 68
751(chain G and (resid 2 through 38 or resid 40...G86 - 111
761(chain G and (resid 2 through 38 or resid 40...G2 - 164
771(chain G and (resid 2 through 38 or resid 40...G132 - 134
781(chain G and (resid 2 through 38 or resid 40...G136 - 137
791(chain G and (resid 2 through 38 or resid 40...G139 - 1403
7101(chain G and (resid 2 through 38 or resid 40...G145 - 13
7111(chain G and (resid 2 through 38 or resid 40...G145 - 148
7121(chain G and (resid 2 through 38 or resid 40...G150 - 154
7131(chain G and (resid 2 through 38 or resid 40...G156 - 157
7141(chain G and (resid 2 through 38 or resid 40...G159 - 164
811(chain H and (resid 2 through 38 or resid 40...H2 - 38
821(chain H and (resid 2 through 38 or resid 40...H40 - 49
831(chain H and (resid 2 through 38 or resid 40...H51 - 57
841(chain H and (resid 2 through 38 or resid 40...H59 - 68
851(chain H and (resid 2 through 38 or resid 40...H86 - 111
861(chain H and (resid 2 through 38 or resid 40...H1 - 164
871(chain H and (resid 2 through 38 or resid 40...H132 - 134
881(chain H and (resid 2 through 38 or resid 40...H136 - 137
891(chain H and (resid 2 through 38 or resid 40...H139 - 1403
8101(chain H and (resid 2 through 38 or resid 40...H145 - 13
8111(chain H and (resid 2 through 38 or resid 40...H145 - 148
8121(chain H and (resid 2 through 38 or resid 40...H150 - 154
8131(chain H and (resid 2 through 38 or resid 40...H156 - 157
8141(chain H and (resid 2 through 38 or resid 40...H159 - 164

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Components

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Protein , 1 types, 8 molecules ABCDEFGH

#1: Protein
Ferritin /


Mass: 19415.867 Da / Num. of mol.: 8 / Mutation: A42V, E65D
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) (bacteria)
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099 / Gene: TM_1128 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9X0L2, bacterial non-heme ferritin

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Non-polymers , 5 types, 200 molecules

#2: Chemical...
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 35 / Source method: obtained synthetically / Formula: SO4
#3: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 7 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical
ChemComp-FE / FE (III) ION / Iron


Mass: 55.845 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Fe
#5: Chemical
ChemComp-LFA / EICOSANE / LIPID FRAGMENT / Icosane


Mass: 282.547 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C20H42
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 146 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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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: 3.39 Å3/Da / Density % sol: 63.76 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / Details: 2.4 M (NH4)2 SO4, 0.1M MES. pH 6.0 / PH range: 6

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.2 / Wavelength: 0.9184 Å
DetectorType: DECTRIS PILATUS3 S 2M / Detector: PIXEL / Date: Apr 13, 2019
RadiationMonochromator: DCM Si111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9184 Å / Relative weight: 1
ReflectionResolution: 2.167→24.863 Å / Num. obs: 111200 / % possible obs: 99.7 % / Redundancy: 10.147 % / Biso Wilson estimate: 63.455 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.129 / Rrim(I) all: 0.136 / Χ2: 1.298 / Net I/σ(I): 12.99
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
2.17-2.310.3064.0470.5318174117855176340.3244.25898.8
2.3-2.4610.0532.5040.8616891416812168020.5392.63999.9
2.46-2.6510.061.4351.5415755415681156610.7121.51299.9
2.65-2.910.7560.7363.2715542614480144500.9150.77399.8
2.9-3.2510.510.3157.7313730613097130640.9790.33199.7
3.25-3.749.3470.12818.6210813111591115680.9950.13599.8
3.74-4.5810.3770.06138.03102517988798790.9990.06599.9
4.58-6.459.7810.04747.8475183769276870.9990.0599.9
6.45-24.8639.340.02864.94416084478445510.02999.5

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation7.59 Å48.27 Å
Translation7.59 Å48.27 Å

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Processing

Software
NameVersionClassification
PHENIX1.15.1-3469refinement
XSCALEdata scaling
PHASER2.8.2phasing
PDB_EXTRACT3.25data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1vlg

1vlg


Resolution: 2.17→24.863 Å / SU ML: 0.48 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 36.32 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2462 2097 1.89 %
Rwork0.2098 108863 -
obs0.2105 110960 99.54 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 171.16 Å2 / Biso mean: 85.1996 Å2 / Biso min: 45.38 Å2
Refinement stepCycle: final / Resolution: 2.17→24.863 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10920 0 305 146 11371
Biso mean--106.55 76.64 -
Num. residues----1309
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3216X-RAY DIFFRACTION5.487TORSIONAL
12B3216X-RAY DIFFRACTION5.487TORSIONAL
13C3216X-RAY DIFFRACTION5.487TORSIONAL
14D3216X-RAY DIFFRACTION5.487TORSIONAL
15E3216X-RAY DIFFRACTION5.487TORSIONAL
16F3216X-RAY DIFFRACTION5.487TORSIONAL
17G3216X-RAY DIFFRACTION5.487TORSIONAL
18H3216X-RAY DIFFRACTION5.487TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.17-2.21690.40391350.3989700597
2.2169-2.27230.40221380.37737183100
2.2723-2.33370.37391400.36147253100
2.3337-2.40230.36041390.34457216100
2.4023-2.47980.33191400.3419722399
2.4798-2.56830.39391390.34327189100
2.5683-2.6710.3781400.32757283100
2.671-2.79240.35351390.31317215100
2.7924-2.93940.31191400.28927281100
2.9394-3.12330.33511390.27917244100
3.1233-3.36390.27471400.24677268100
3.3639-3.70140.24461410.2127295100
3.7014-4.23480.21661400.17877314100
4.2348-5.32670.18371420.15257383100
5.3267-24.8630.20121450.1571751199
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)
10.2814-0.66210.18081.0914-0.00790.52270.04010.10250.06230.0319-0.04780.05490.32930.17020.00030.67370.0750.01860.57990.04980.690827.735976.3867108.0766
20.46821.10260.76510.68250.0811-0.08190.1459-0.1738-0.25570.2145-0.0658-0.08650.26040.08880.00010.73640.0590.01130.69360.00760.738125.170780.3718112.3557
31.21560.09930.43060.3067-0.09640.20.0474-0.1335-0.09930.1524-0.0510.03060.43110.07280.00010.83990.0546-0.00440.58760.06350.684720.891267.5144115.634
40.1168-0.27660.22410.2363-0.64370.98540.14490.02550.06140.0873-0.0934-0.03050.23760.1326-0.00070.59590.0414-0.00610.58660.02030.736919.573987.932798.5071
50.09050.3723-0.13990.8989-0.3608-0.2049-0.0592-0.0535-0.01020.0370.04660.1240.04660.051-0.00050.6030.00270.03450.5698-0.01420.675816.774388.6655104.514
60.01560.0014-0.07790.1003-0.00230.2409-0.2341-0.5390.4581-0.61570.2017-0.06950.83070.8069-0.00060.60460.00430.03240.78620.00510.739134.980691.988199.2388
70.89960.23450.63640.05640.03461.1533-0.1153-0.1457-0.0795-0.2454-0.0051-0.0929-0.10140.0851-00.4514-0.008-0.01680.52440.01870.638616.6908100.469296.9796
80.3894-0.29660.39610.4458-0.05210.6920.0609-0.04730.05870.372-0.05170.2863-0.07920.06460.00350.6134-0.0531-0.04480.79310.0030.855231.6136107.6272114.2206
90.42380.0690.06780.15650.25390.2914-0.1429-0.276-0.2510.1990.084-0.59570.03310.5023-0.00020.71310.0306-0.10261.14540.03770.807353.362799.3613152.9995
10-0.41350.25090.0970.35790.28640.97970.0998-0.08930.07480.0146-0.08350.3646-0.10.32650.00070.61450.0239-0.10541.08390.030.859147.265699.5108151.4032
11-0.18860.21990.05361.9476-0.25020.6296-0.0084-0.19560.10460.17950.04760.1650.00250.38690.00030.70170.0376-0.10741.1404-0.01120.764146.937297.123164.8128
12-0.29750.13950.32460.26330.1383-0.0932-0.0732-0.21790.1301-0.27740.05540.24920.13780.5972-0.00020.67590.1905-0.04461.02840.09440.778751.860188.1011140.1623
13-0.34731.00930.17510.7248-0.40371.38720.1711-0.1889-0.005-0.096-0.16840.05760.29960.2489-0.0010.67290.1282-0.04380.91950.08750.87445.795689.1701142.0274
140.3240.0735-0.36670.0810.2366-0.06-0.0817-0.0276-0.169-0.17840.1843-0.34980.16170.4492-0.00030.73970.1062-0.08231.01610.07180.885452.654886.7476130.9278
150.716-0.7544-0.49860.67260.45790.24840.0263-0.07870.0463-0.18510.27640.68250.19820.14530.00010.66890.0648-0.11730.91670.03390.790742.931787.5074127.5691
160.2992-0.05250.17690.89540.71910.57710.04150.3197-0.11450.08480.43360.0512-0.1309-0.78220.00430.6891-0.0781-0.10530.88170.08170.855740.727108.1903125.2137
17-0.1648-0.26830.14850.2741-0.62360.4073-0.05980.07140.05320.1215-0.1143-0.0739-0.42140.512-0.00070.7934-0.2402-0.07370.9306-0.04610.778639.5328138.1895150.5221
18-0.66190.06070.2089-0.46480.07140.2751-0.01-0.00620.13290.08360.23140.00070.08980.1288-0.00180.8132-0.2278-0.09270.9209-0.00390.756333.6464131.6872148.4237
190.0821-0.1320.04990.0439-0.01550.07630.2947-0.6525-0.041-0.21320.6132-0.34111.30162.04010.00130.9343-0.3019-0.09661.1637-0.19780.894236.8734144.8628157.0997
200.7255-0.5941-0.2220.0684-0.06350.06180.0274-0.0860.2136-0.0839-0.0578-0.1439-0.07270.41020.00040.6991-0.2609-0.08120.9245-0.03780.745347.3137133.0066147.7868
210.55820.3340.42120.3309-0.15310.5752-0.0336-0.1045-0.0920.15-0.122-0.0997-0.1325-0.14-0.00530.7471-0.1813-0.08590.95820.02810.77143.7423123.3557147.6312
220.3872-0.28230.26380.4817-0.1210.2376-0.38810.9803-0.5734-0.0062-0.0328-0.27350.5678-0.9329-0.00010.7627-0.24580.00650.895-0.04660.716336.6649122.2847128.0097
230.0290.0612-0.030.67480.13560.06920.3540.3386-0.8046-0.23010.08071.1911-1.0863-0.0512-0.00071.0519-0.2381-0.23980.8098-0.06330.913827.3023148.1605120.9314
241.1162-0.42140.3313-0.3884-0.22920.3262-0.0388-0.00380.17290.1669-0.0147-0.1207-0.42290.26770.00010.9289-0.2559-0.0780.7172-0.1050.796124.2279148.2464145.2329
25-0.1917-0.40850.18210.2071-0.27650.2904-0.19960.10070.12520.08760.0381-0.02930.0776-0.3933-0.00020.9916-0.1066-0.06350.7953-0.08260.808512.0935149.3087146.2484
260.78530.33970.17540.4348-0.32850.8833-0.33710.0310.2320.3709-0.11220.9366-0.30420.0241-0.0661.21-0.0851-0.0131.0241-0.140.883412.1181141.8648165.5296
270.05220.1454-0.4820.5370.2830.14650.1378-0.1304-0.0109-0.1138-0.08140.1162-0.24020.34340.00030.9145-0.0969-0.12381.055-0.03230.654630.8534116.8686182.9235
28-0.20390.11890.34190.5814-1.04331.24280.1231-0.11690.08440.2438-0.1881-0.0579-0.20770.46-0.00010.8043-0.1114-0.16981.018-0.10840.673337.5339121.4796183.8671
290.3404-0.1330.28510.18110.70.39960.2235-0.6537-0.0819-0.45570.14960.138-0.20960.52010.00330.9017-0.1263-0.02121.0568-0.04690.735932.624126.6177173.452
300.79920.1834-0.18990.2038-0.2080.19590.29250.15870.1436-0.6492-0.0655-0.6062-0.32690.19380.00610.9385-0.0283-0.06850.9102-0.06770.738913.4776133.1102177.5655
310.39150.582-0.30120.5302-0.39510.3999-0.0647-0.51090.06140.29410.1319-0.11230.16630.4166-0.00010.93580.0422-0.10381.0964-0.01520.594422.6977108.8113195.5355
320.20790.2305-0.32070.3812-0.42370.82530.2310.2815-0.3739-0.1942-0.4280.3301-0.1843-0.1661-0.00130.76810.0462-0.1010.934-0.05180.601120.4879105.5268187.0574
33-0.05370.19740.31210.9612-0.41740.6318-0.0803-0.2208-0.03960.1319-0.002-0.08560.07850.14340.00050.91960.0343-0.0751.00880.0250.668820.539997.8881193.7933
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 2 through 36 )A2 - 36
2X-RAY DIFFRACTION2chain 'A' and (resid 37 through 76 )A37 - 76
3X-RAY DIFFRACTION3chain 'A' and (resid 77 through 164 )A77 - 164
4X-RAY DIFFRACTION4chain 'B' and (resid 1 through 36 )B1 - 36
5X-RAY DIFFRACTION5chain 'B' and (resid 37 through 75 )B37 - 75
6X-RAY DIFFRACTION6chain 'B' and (resid 76 through 84 )B76 - 84
7X-RAY DIFFRACTION7chain 'B' and (resid 85 through 146 )B85 - 146
8X-RAY DIFFRACTION8chain 'B' and (resid 147 through 164 )B147 - 164
9X-RAY DIFFRACTION9chain 'C' and (resid 1 through 36 )C1 - 36
10X-RAY DIFFRACTION10chain 'C' and (resid 37 through 76 )C37 - 76
11X-RAY DIFFRACTION11chain 'C' and (resid 77 through 164 )C77 - 164
12X-RAY DIFFRACTION12chain 'D' and (resid 2 through 36 )D2 - 36
13X-RAY DIFFRACTION13chain 'D' and (resid 37 through 76 )D37 - 76
14X-RAY DIFFRACTION14chain 'D' and (resid 77 through 115 )D77 - 115
15X-RAY DIFFRACTION15chain 'D' and (resid 116 through 146 )D116 - 146
16X-RAY DIFFRACTION16chain 'D' and (resid 147 through 164 )D147 - 164
17X-RAY DIFFRACTION17chain 'E' and (resid 1 through 36 )E1 - 36
18X-RAY DIFFRACTION18chain 'E' and (resid 37 through 66 )E37 - 66
19X-RAY DIFFRACTION19chain 'E' and (resid 67 through 76 )E67 - 76
20X-RAY DIFFRACTION20chain 'E' and (resid 77 through 115 )E77 - 115
21X-RAY DIFFRACTION21chain 'E' and (resid 116 through 146 )E116 - 146
22X-RAY DIFFRACTION22chain 'E' and (resid 147 through 164 )E147 - 164
23X-RAY DIFFRACTION23chain 'F' and (resid 1 through 5 )F1 - 5
24X-RAY DIFFRACTION24chain 'F' and (resid 6 through 115 )F6 - 115
25X-RAY DIFFRACTION25chain 'F' and (resid 116 through 146 )F116 - 146
26X-RAY DIFFRACTION26chain 'F' and (resid 147 through 164 )F147 - 164
27X-RAY DIFFRACTION27chain 'G' and (resid 2 through 65 )G2 - 65
28X-RAY DIFFRACTION28chain 'G' and (resid 66 through 115 )G66 - 115
29X-RAY DIFFRACTION29chain 'G' and (resid 116 through 146 )G116 - 146
30X-RAY DIFFRACTION30chain 'G' and (resid 147 through 164 )G147 - 164
31X-RAY DIFFRACTION31chain 'H' and (resid 1 through 36 )H1 - 36
32X-RAY DIFFRACTION32chain 'H' and (resid 37 through 65 )H37 - 65
33X-RAY DIFFRACTION33chain 'H' and (resid 66 through 164 )H66 - 164

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