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- PDB-6txk: Crystal structure of thermotoga maritima E65K Ferritin -

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Basic information

Entry
Database: PDB / ID: 6txk
TitleCrystal structure of thermotoga maritima E65K Ferritin
ComponentsFerritin
KeywordsMETAL BINDING PROTEIN / Metal binding / engineered protein
Function / homology
Function and homology information


bacterial non-heme ferritin / ferroxidase activity / intracellular sequestering of iron ion / 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: 2.359 Å
AuthorsWilk, P. / Grudnik, P. / Kumar, M. / Heddle, J. / Chakraborti, S.
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 1.1Aug 10, 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)160,97164
Polymers155,2158
Non-polymers5,75656
Water7,963442
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)482,914192
Polymers465,64624
Non-polymers17,268168
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 area93910 Å2
ΔGint-597 kcal/mol
Surface area147320 Å2
MethodPISA
Unit cell
Length a, b, c (Å)175.811, 175.811, 354.136
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 6 or resid 8...
21(chain B and (resid 2 through 6 or resid 8...
31(chain C and (resid 2 through 6 or resid 8...
41(chain D and (resid 2 through 6 or resid 8...
51(chain E and (resid 2 through 6 or resid 8...
61(chain F and (resid 2 through 6 or resid 8...
71(chain G and (resid 2 through 6 or resid 8...
81(chain H and (resid 2 through 6 or resid 8...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 2 through 6 or resid 8...A2 - 6
121(chain A and (resid 2 through 6 or resid 8...A8 - 9
131(chain A and (resid 2 through 6 or resid 8...A11 - 17
141(chain A and (resid 2 through 6 or resid 8...A19 - 49
151(chain A and (resid 2 through 6 or resid 8...A0
161(chain A and (resid 2 through 6 or resid 8...A59 - 60
171(chain A and (resid 2 through 6 or resid 8...A1 - 203
181(chain A and (resid 2 through 6 or resid 8...A70 - 75
191(chain A and (resid 2 through 6 or resid 8...A77 - 80
1101(chain A and (resid 2 through 6 or resid 8...A1 - 203
1111(chain A and (resid 2 through 6 or resid 8...A81 - 111
1121(chain A and (resid 2 through 6 or resid 8...A0
1131(chain A and (resid 2 through 6 or resid 8...A1 - 203
1141(chain A and (resid 2 through 6 or resid 8...A1 - 203
1151(chain A and (resid 2 through 6 or resid 8...A156 - 157
1161(chain A and (resid 2 through 6 or resid 8...A159 - 164
211(chain B and (resid 2 through 6 or resid 8...B2 - 6
221(chain B and (resid 2 through 6 or resid 8...B8 - 9
231(chain B and (resid 2 through 6 or resid 8...B11 - 17
241(chain B and (resid 2 through 6 or resid 8...B19 - 49
251(chain B and (resid 2 through 6 or resid 8...B59 - 60
261(chain B and (resid 2 through 6 or resid 8...B2 - 68
271(chain B and (resid 2 through 6 or resid 8...B70 - 75
281(chain B and (resid 2 through 6 or resid 8...B77 - 80
291(chain B and (resid 2 through 6 or resid 8...B82
2101(chain B and (resid 2 through 6 or resid 8...B1 - 205
2111(chain B and (resid 2 through 6 or resid 8...B1 - 205
2121(chain B and (resid 2 through 6 or resid 8...B1 - 205
2131(chain B and (resid 2 through 6 or resid 8...B1 - 205
2141(chain B and (resid 2 through 6 or resid 8...B136 - 154
2151(chain B and (resid 2 through 6 or resid 8...B156 - 157
2161(chain B and (resid 2 through 6 or resid 8...B159 - 164
311(chain C and (resid 2 through 6 or resid 8...C2 - 6
321(chain C and (resid 2 through 6 or resid 8...C8 - 9
331(chain C and (resid 2 through 6 or resid 8...C11 - 17
341(chain C and (resid 2 through 6 or resid 8...C19 - 49
351(chain C and (resid 2 through 6 or resid 8...C59 - 60
361(chain C and (resid 2 through 6 or resid 8...C2 - 68
371(chain C and (resid 2 through 6 or resid 8...C70 - 75
381(chain C and (resid 2 through 6 or resid 8...C77 - 80
391(chain C and (resid 2 through 6 or resid 8...C82
3101(chain C and (resid 2 through 6 or resid 8...C1 - 200
3111(chain C and (resid 2 through 6 or resid 8...C1 - 200
3121(chain C and (resid 2 through 6 or resid 8...C1 - 200
3131(chain C and (resid 2 through 6 or resid 8...C1 - 200
3141(chain C and (resid 2 through 6 or resid 8...C136 - 154
3151(chain C and (resid 2 through 6 or resid 8...C156 - 157
3161(chain C and (resid 2 through 6 or resid 8...C159 - 164
411(chain D and (resid 2 through 6 or resid 8...D2 - 6
421(chain D and (resid 2 through 6 or resid 8...D8 - 9
431(chain D and (resid 2 through 6 or resid 8...D0
441(chain D and (resid 2 through 6 or resid 8...D52
451(chain D and (resid 2 through 6 or resid 8...D52 - 68
461(chain D and (resid 2 through 6 or resid 8...D70 - 75
471(chain D and (resid 2 through 6 or resid 8...D70 - 75
481(chain D and (resid 2 through 6 or resid 8...D77 - 80
491(chain D and (resid 2 through 6 or resid 8...D1 - 201
4101(chain D and (resid 2 through 6 or resid 8...D1 - 201
4111(chain D and (resid 2 through 6 or resid 8...D1 - 201
4121(chain D and (resid 2 through 6 or resid 8...D1 - 201
4131(chain D and (resid 2 through 6 or resid 8...D136 - 154
4141(chain D and (resid 2 through 6 or resid 8...D156 - 157
4151(chain D and (resid 2 through 6 or resid 8...D159 - 164
511(chain E and (resid 2 through 6 or resid 8...E2 - 6
521(chain E and (resid 2 through 6 or resid 8...E8 - 9
531(chain E and (resid 2 through 6 or resid 8...E0
541(chain E and (resid 2 through 6 or resid 8...E52
551(chain E and (resid 2 through 6 or resid 8...E59 - 6068
561(chain E and (resid 2 through 6 or resid 8...E84
571(chain E and (resid 2 through 6 or resid 8...E82
581(chain E and (resid 2 through 6 or resid 8...E0
591(chain E and (resid 2 through 6 or resid 8...E113 - 122
5101(chain E and (resid 2 through 6 or resid 8...E1 - 202
5111(chain E and (resid 2 through 6 or resid 8...E132 - 134
5121(chain E and (resid 2 through 6 or resid 8...E156 - 157
5131(chain E and (resid 2 through 6 or resid 8...E159 - 164
611(chain F and (resid 2 through 6 or resid 8...F2 - 6
621(chain F and (resid 2 through 6 or resid 8...F8 - 9
631(chain F and (resid 2 through 6 or resid 8...F0
641(chain F and (resid 2 through 6 or resid 8...F52
651(chain F and (resid 2 through 6 or resid 8...F52 - 68
661(chain F and (resid 2 through 6 or resid 8...F70 - 75
671(chain F and (resid 2 through 6 or resid 8...F70 - 75
681(chain F and (resid 2 through 6 or resid 8...F77 - 80
691(chain F and (resid 2 through 6 or resid 8...F1 - 201
6101(chain F and (resid 2 through 6 or resid 8...F1 - 201
6111(chain F and (resid 2 through 6 or resid 8...F1 - 201
6121(chain F and (resid 2 through 6 or resid 8...F1 - 201
6131(chain F and (resid 2 through 6 or resid 8...F136 - 154
6141(chain F and (resid 2 through 6 or resid 8...F156 - 157
6151(chain F and (resid 2 through 6 or resid 8...F159 - 164
711(chain G and (resid 2 through 6 or resid 8...G2 - 6
721(chain G and (resid 2 through 6 or resid 8...G8 - 9
731(chain G and (resid 2 through 6 or resid 8...G11 - 17
741(chain G and (resid 2 through 6 or resid 8...G19 - 49
751(chain G and (resid 2 through 6 or resid 8...G0
761(chain G and (resid 2 through 6 or resid 8...G59 - 60
771(chain G and (resid 2 through 6 or resid 8...G1 - 200
781(chain G and (resid 2 through 6 or resid 8...G70 - 75
791(chain G and (resid 2 through 6 or resid 8...G77 - 80
7101(chain G and (resid 2 through 6 or resid 8...G1 - 200
7111(chain G and (resid 2 through 6 or resid 8...G81 - 111
7121(chain G and (resid 2 through 6 or resid 8...G0
7131(chain G and (resid 2 through 6 or resid 8...G1 - 200
7141(chain G and (resid 2 through 6 or resid 8...G1 - 200
7151(chain G and (resid 2 through 6 or resid 8...G156 - 157
7161(chain G and (resid 2 through 6 or resid 8...G159 - 164
811(chain H and (resid 2 through 6 or resid 8...H2 - 6
821(chain H and (resid 2 through 6 or resid 8...H8 - 9
831(chain H and (resid 2 through 6 or resid 8...H11 - 17
841(chain H and (resid 2 through 6 or resid 8...H19 - 49
851(chain H and (resid 2 through 6 or resid 8...H0
861(chain H and (resid 2 through 6 or resid 8...H59 - 60
871(chain H and (resid 2 through 6 or resid 8...H1 - 201
881(chain H and (resid 2 through 6 or resid 8...H70 - 75
891(chain H and (resid 2 through 6 or resid 8...H77 - 80
8101(chain H and (resid 2 through 6 or resid 8...H1 - 201
8111(chain H and (resid 2 through 6 or resid 8...H81 - 111
8121(chain H and (resid 2 through 6 or resid 8...H0
8131(chain H and (resid 2 through 6 or resid 8...H1 - 201
8141(chain H and (resid 2 through 6 or resid 8...H1 - 201
8151(chain H and (resid 2 through 6 or resid 8...H156 - 157
8161(chain H and (resid 2 through 6 or resid 8...H159 - 164

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Components

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Protein , 1 types, 8 molecules ABCDEFGH

#1: Protein
Ferritin


Mass: 19401.906 Da / Num. of mol.: 8 / Mutation: E65K
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) (bacteria)
Gene: TM_1128 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9X0L2, bacterial non-heme ferritin

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Non-polymers , 5 types, 498 molecules

#2: Chemical
ChemComp-FE / FE (III) ION


Mass: 55.845 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Fe
#3: Chemical...
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 32 / Source method: obtained synthetically / Formula: SO4
#4: Chemical
ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 12 / Source method: obtained synthetically / Formula: C3H8O3
#5: Chemical
ChemComp-LFA / EICOSANE / LIPID FRAGMENT


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


Mass: 18.015 Da / Num. of mol.: 442 / 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: 63.75 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6 / Details: 2.4 M (NH4)2 SO4, 0.1M MES. pH 6.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: BESSY / Beamline: 14.3 / Wavelength: 0.895 Å
DetectorType: RAYONIX MX-225 / Detector: CCD / Date: May 18, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.895 Å / Relative weight: 1
ReflectionResolution: 2.359→20.44 Å / Num. obs: 86438 / % possible obs: 99.8 % / Redundancy: 7.516 % / Biso Wilson estimate: 40.582 Å2 / CC1/2: 0.992 / Rmerge(I) obs: 0.23 / Rrim(I) all: 0.248 / Χ2: 1.049 / Net I/σ(I): 8.72
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
2.36-2.57.6481.5311.3310561413863138090.4641.64599.6
2.5-2.677.6831.061.9510013913034130330.6651.138100
2.67-2.897.6670.6753.159321912160121590.8290.725100
2.89-3.167.6360.4075.258552711202112000.9330.438100
3.16-3.537.5150.2069.787644710176101730.9810.222100
3.53-4.087.4930.12415.3567501901290090.9920.133100
4.08-4.987.4090.0822.256686765376510.9960.086100
4.98-7.017.2730.09618.343568599559900.9950.10499.9
7.01-20.446.1450.0528.0420980350234140.9980.05597.5

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Phasing

PhasingMethod: molecular replacement
Phasing MR
Highest resolutionLowest resolution
Rotation7.82 Å48.25 Å
Translation7.82 Å48.25 Å

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHASER2.8.3phasing
PHENIX1.15.1_3469refinement
PDB_EXTRACT3.25data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1vlg

1vlg


Resolution: 2.359→20.44 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 25.61
RfactorNum. reflection% reflection
Rfree0.2365 2092 2.43 %
Rwork0.2011 --
obs0.2019 86126 99.65 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 144.23 Å2 / Biso mean: 51.2991 Å2 / Biso min: 28.16 Å2
Refinement stepCycle: final / Resolution: 2.359→20.44 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10936 0 320 442 11698
Biso mean--75.88 54.02 -
Num. residues----1312
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A3088X-RAY DIFFRACTION4.943TORSIONAL
12B3088X-RAY DIFFRACTION4.943TORSIONAL
13C3088X-RAY DIFFRACTION4.943TORSIONAL
14D3088X-RAY DIFFRACTION4.943TORSIONAL
15E3088X-RAY DIFFRACTION4.943TORSIONAL
16F3088X-RAY DIFFRACTION4.943TORSIONAL
17G3088X-RAY DIFFRACTION4.943TORSIONAL
18H3088X-RAY DIFFRACTION4.943TORSIONAL
LS refinement shell

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

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.359-2.41370.33271360.2993549199
2.4137-2.4740.36681390.3045608100
2.474-2.54080.32191380.28795539100
2.5408-2.61540.35071390.2825580100
2.6154-2.69960.29621400.26755583100
2.6996-2.79590.31231390.26365604100
2.7959-2.90750.28531390.23735566100
2.9075-3.03940.24941390.22435601100
3.0394-3.19910.25251400.22695603100
3.1991-3.39870.23481390.20245601100
3.3987-3.65970.23541400.17815626100
3.6597-4.02550.2041400.17355635100
4.0255-4.60220.17091410.14735664100
4.6022-5.77650.20061420.17395691100
5.7765-20.440.21571410.1809564296
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)
19.0432-5.9397-1.3479.25375.27573.8169-0.2649-0.0920.4052-0.36740.5126-1.1553-0.72130.3247-0.2920.37720.0883-0.08570.58340.02230.6148.024784.6062115.9064
20.870.38010.67670.41130.12350.80840.0915-0.1208-0.02380.1166-0.08870.01980.0971-0.0442-0.01120.3890.01530.02430.3153-0.02490.406823.320472.7795113.5054
31.4385-0.81260.62070.6381-0.30011.2946-0.04170.04190.1445-0.033-0.0180.0189-0.00190.05780.05640.33340.00250.03370.2998-0.01540.413919.340191.0399.5859
45.84774.13692.41054.15812.24411.7535-0.0037-0.3201-0.13970.0582-0.0074-0.241-0.0227-0.04570.07420.35090.0347-0.03190.36080.03150.410616.2474103.1533101.5379
54.72623.4280.84314.9257-0.21881.70660.6867-1.10450.77150.9053-0.77640.0239-0.13-0.06480.030.5614-0.0272-0.12550.6325-0.19260.907331.774107.1224115.0263
64.1248-3.18994.01368.88610.37735.7763-0.13270.0891.2832-0.1018-0.4618-0.9125-0.20890.5090.55930.588-0.1824-0.05510.5478-0.09660.676856.4335120.4302146.2028
70.4631.1121-0.29765.2472-0.49950.36210.2331-0.283-0.2290.3322-0.2736-0.30810.01840.17980.01760.33070.0178-0.0950.48330.00770.402952.974896.621154.5535
80.14791.5416-0.84555.8813-2.35881.7172-0.0006-0.03850.196-0.16680.26650.7672-0.0076-0.134-0.30820.34010.0101-0.07420.47170.01730.45244.099497.9457153.6045
90.54360.2217-0.41522.40710.28231.07920.0509-0.1049-0.02490.3982-0.12940.03840.0925-0.05690.07670.3726-0.0195-0.08730.4824-0.01050.427247.814298.1193163.1133
102.0395-1.6673-2.15362.20931.82832.2928-0.67020.0115-0.5830.4279-0.5782-0.43150.5840.36731.21090.59960.1013-0.10760.52620.01610.793448.647366.9476148.3783
110.87481.2170.16344.20130.10121.14770.10360.0093-0.0878-0.2384-0.1669-0.3213-0.04740.276-0.06250.28930.0061-0.02380.4085-0.00380.351152.314490.6965140.0028
120.47630.6750.28645.3061-2.59581.7994-0.0175-0.07380.0376-0.24130.22310.28830.0924-0.1758-0.27140.34150.0125-0.01670.42440.01950.450443.902189.6331141.9233
130.68260.59490.04372.1490.29460.85650.0326-0.0204-0.0784-0.2511-0.0505-0.08890.02530.09890.04270.3322-0.0008-0.0110.3990.00650.44148.910787.3232131.2828
142.89340.07730.31964.6021-1.95465.5817-0.2590.32220.3644-0.80130.79561.3896-0.0802-0.9031-0.40020.6895-0.0784-0.240.43720.13690.708940.1922108.5137126.6756
153.09752.35931.80954.2071-2.07756.03240.5079-0.8150.17631.1490.16850.4769-0.144-0.4789-0.46440.6341-0.0997-0.04230.63080.03710.519438.7403138.4228173.4337
160.5239-0.32-0.12850.3362-0.33571.7775-0.02220.00160.06870.0187-0.0062-0.03080.208-0.03990.05280.3755-0.08670.00860.3675-0.00260.440340.0791131.6237146.7638
171.1012-0.18120.72960.4681-1.36484.92020.0073-0.02540.17990.20580.1588-0.06-0.4537-0.29940.01020.4047-0.0387-0.01160.3686-0.04420.511626.952148.1573143.6112
180.6745-0.0367-1.2074-0.0939-0.22736.9382-0.04050.03050.04810.0478-0.06070.02330.0583-0.62630.10050.3793-0.09010.0110.4344-0.06390.472521.9429140.7518146.667
190.6014-0.00850.30970.2039-0.40490.9716-0.0273-0.0770.17350.1130.0663-0.1263-0.1997-0.0584-0.05310.3982-0.0285-0.01830.3566-0.06740.49918.35151.3451145.0884
202.7137-1.6401-1.87963.72391.94115.3034-0.0957-0.41650.10820.8034-0.04640.26930.5735-0.81820.14410.5754-0.06990.04690.8299-0.03410.49412.3397141.3451166.3383
219.69453.71161.72712.83221.94942.1957-0.2799-0.2547-1.25090.03310.4261-0.56670.7914-0.0123-0.13330.52270.0156-0.01150.6710.06510.611150.6599103.6357178.1784
221.506-0.4142-1.20040.32640.13130.99810.0904-0.1510.12660.0976-0.055-0.1104-0.12710.1165-0.06840.4969-0.0345-0.08940.4847-0.06080.383932.9968119.5014183.9536
232.8319-0.6361-1.42040.93760.92931.40430.19080.23450.3172-0.1428-0.12030.0208-0.2788-0.2177-0.04020.59750.0026-0.03970.5250.01620.401725.4176128.5831175.3975
244.5009-1.46082.03853.3866-2.72552.672-0.3658-0.35420.62010.4718-0.17790.4609-0.9889-0.46950.40080.68170.0096-0.01550.8141-0.07050.63616.2651121.832203.2856
252.5169-0.6578-1.00321.33270.39290.6064-0.1794-0.0594-0.2370.1586-0.00450.06090.11070.01180.14380.4734-0.0287-0.04920.47750.01090.299122.109108.2706192.2588
262.4938-0.5344-0.91341.7694-0.00861.5577-0.1817-0.2708-0.31460.1417-0.1061-0.04550.26090.20590.20970.521-0.0072-0.05880.58320.0730.392821.792100.4354200.2586
272.4733-2.7424-1.56823.96251.72851.07940.19330.2693-0.3993-0.7025-0.32070.2627-0.0061-0.06420.09870.5391-0.0210.01590.55720.05030.406415.118995.2578193.6983
282.0614-0.5391-1.22435.20530.40214.5126-0.16310.1675-0.5276-0.6541-0.4049-0.27310.71390.18410.53620.9137-0.08930.15760.6497-0.09660.816428.661686.3929180.1239
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 1 through 5 )A1 - 5
2X-RAY DIFFRACTION2chain 'A' and (resid 6 through 164 )A6 - 164
3X-RAY DIFFRACTION3chain 'B' and (resid 1 through 115 )B1 - 115
4X-RAY DIFFRACTION4chain 'B' and (resid 116 through 146 )B116 - 146
5X-RAY DIFFRACTION5chain 'B' and (resid 147 through 164 )B147 - 164
6X-RAY DIFFRACTION6chain 'C' and (resid 1 through 5 )C1 - 5
7X-RAY DIFFRACTION7chain 'C' and (resid 6 through 36 )C6 - 36
8X-RAY DIFFRACTION8chain 'C' and (resid 37 through 65 )C37 - 65
9X-RAY DIFFRACTION9chain 'C' and (resid 66 through 164 )C66 - 164
10X-RAY DIFFRACTION10chain 'D' and (resid 1 through 5 )D1 - 5
11X-RAY DIFFRACTION11chain 'D' and (resid 6 through 36 )D6 - 36
12X-RAY DIFFRACTION12chain 'D' and (resid 37 through 70 )D37 - 70
13X-RAY DIFFRACTION13chain 'D' and (resid 71 through 146 )D71 - 146
14X-RAY DIFFRACTION14chain 'D' and (resid 147 through 164 )D147 - 164
15X-RAY DIFFRACTION15chain 'E' and (resid 1 through 5 )E1 - 5
16X-RAY DIFFRACTION16chain 'E' and (resid 6 through 164 )E6 - 164
17X-RAY DIFFRACTION17chain 'F' and (resid 1 through 36 )F1 - 36
18X-RAY DIFFRACTION18chain 'F' and (resid 37 through 65 )F37 - 65
19X-RAY DIFFRACTION19chain 'F' and (resid 66 through 146 )F66 - 146
20X-RAY DIFFRACTION20chain 'F' and (resid 147 through 164 )F147 - 164
21X-RAY DIFFRACTION21chain 'G' and (resid 1 through 5 )G1 - 5
22X-RAY DIFFRACTION22chain 'G' and (resid 6 through 115 )G6 - 115
23X-RAY DIFFRACTION23chain 'G' and (resid 116 through 164 )G116 - 164
24X-RAY DIFFRACTION24chain 'H' and (resid 1 through 5 )H1 - 5
25X-RAY DIFFRACTION25chain 'H' and (resid 6 through 75 )H6 - 75
26X-RAY DIFFRACTION26chain 'H' and (resid 76 through 115 )H76 - 115
27X-RAY DIFFRACTION27chain 'H' and (resid 116 through 146 )H116 - 146
28X-RAY DIFFRACTION28chain 'H' and (resid 147 through 164 )H147 - 164

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