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- PDB-4uw1: X-ray crystal structure of human TNKS in complex with a small mol... -

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Basic information

Entry
Database: PDB / ID: 4uw1
TitleX-ray crystal structure of human TNKS in complex with a small molecule inhibitor
ComponentsTANKYRASE-1
KeywordsTRANSFERASE / TNKS / INHIBITOR / WNT SIGNALLING
Function / homology
Function and homology information


: / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / positive regulation of telomere maintenance via telomere lengthening / regulation of telomere maintenance via telomerase / XAV939 stabilizes AXIN / positive regulation of telomere capping / NAD+ ADP-ribosyltransferase / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / protein localization to chromosome, telomeric region ...: / negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric / positive regulation of telomere maintenance via telomere lengthening / regulation of telomere maintenance via telomerase / XAV939 stabilizes AXIN / positive regulation of telomere capping / NAD+ ADP-ribosyltransferase / negative regulation of telomere maintenance via telomere lengthening / protein auto-ADP-ribosylation / protein localization to chromosome, telomeric region / NAD+-protein-aspartate ADP-ribosyltransferase activity / protein poly-ADP-ribosylation / NAD+-protein-glutamate ADP-ribosyltransferase activity / mitotic spindle pole / NAD+-protein mono-ADP-ribosyltransferase activity / pericentriolar material / Transferases; Glycosyltransferases; Pentosyltransferases / NAD+ poly-ADP-ribosyltransferase activity / peptidyl-threonine phosphorylation / mRNA transport / nuclear pore / spindle assembly / positive regulation of telomere maintenance via telomerase / nucleotidyltransferase activity / mitotic spindle organization / TCF dependent signaling in response to WNT / Degradation of AXIN / peptidyl-serine phosphorylation / Wnt signaling pathway / Regulation of PTEN stability and activity / protein polyubiquitination / positive regulation of canonical Wnt signaling pathway / protein transport / nuclear membrane / histone binding / chromosome, telomeric region / Ub-specific processing proteases / nuclear body / Golgi membrane / cell division / Golgi apparatus / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / cytoplasm / cytosol
Similarity search - Function
Phosphoenolpyruvate Carboxykinase; domain 3 - #10 / Phosphoenolpyruvate Carboxykinase; domain 3 / Poly(ADP-ribose) polymerase catalytic domain / Poly(ADP-ribose) polymerase, catalytic domain / PARP catalytic domain profile. / SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily ...Phosphoenolpyruvate Carboxykinase; domain 3 - #10 / Phosphoenolpyruvate Carboxykinase; domain 3 / Poly(ADP-ribose) polymerase catalytic domain / Poly(ADP-ribose) polymerase, catalytic domain / PARP catalytic domain profile. / SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Ankyrin repeat / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Alpha-Beta Complex / Alpha Beta
Similarity search - Domain/homology
Chem-92R / Poly [ADP-ribose] polymerase tankyrase-1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.37 Å
AuthorsOliver, A.W. / Rajasekaran, M.B. / Pearl, L.H.
CitationJournal: Medchemcommm / Year: 2015
Title: Design and Discovery of 3-Aryl-5-Substituted-Isoquinolin-1-Ones as Potent and Selective Tankyrase Inhibitors
Authors: Elliot, R.J. / Jarvis, A. / Rajasekaran, M.B. / Menon, M. / Bowers, L. / Boffey, R. / Bayford, M. / Firth-Clark, S. / Beevers, R. / Aquil, R. / Kirton, S.B. / Niculescu-Duvaz, D. / Fish, L. ...Authors: Elliot, R.J. / Jarvis, A. / Rajasekaran, M.B. / Menon, M. / Bowers, L. / Boffey, R. / Bayford, M. / Firth-Clark, S. / Beevers, R. / Aquil, R. / Kirton, S.B. / Niculescu-Duvaz, D. / Fish, L. / Lopes, F. / Mcleary, R. / Trindade, I. / Vendrell, E. / Munkonge, F. / Porter, R. / Perrior, T. / Springer, C. / Oliver, A.W. / Pearl, L.H. / Ashworth, A. / Lord, C.J.
History
DepositionAug 8, 2014Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 8, 2015Provider: repository / Type: Initial release
Revision 1.1Jan 13, 2016Group: Database references
Revision 1.2Jan 10, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_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_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_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.pdbx_dist_value / _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_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_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: TANKYRASE-1
B: TANKYRASE-1
C: TANKYRASE-1
D: TANKYRASE-1
E: TANKYRASE-1
F: TANKYRASE-1
G: TANKYRASE-1
H: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)238,78930
Polymers235,3378
Non-polymers3,45322
Water00
1
A: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,9455
Polymers29,4171
Non-polymers5284
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
2
B: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,7913
Polymers29,4171
Non-polymers3742
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
3
C: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,9455
Polymers29,4171
Non-polymers5284
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
4
D: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,8834
Polymers29,4171
Non-polymers4663
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
5
E: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,7913
Polymers29,4171
Non-polymers3742
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
6
F: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,7913
Polymers29,4171
Non-polymers3742
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
7
G: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,8534
Polymers29,4171
Non-polymers4363
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
8
H: TANKYRASE-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,7913
Polymers29,4171
Non-polymers3742
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)80.589, 82.312, 86.727
Angle α, β, γ (deg.)71.38, 67.31, 89.51
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
TANKYRASE-1 / TANK1 / ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 5 / ARTD 5 / POLY ADP-RIBOSE POLYMERASE 5A / ...TANK1 / ADP-RIBOSYLTRANSFERASE DIPHTHERIA TOXIN-LIKE 5 / ARTD 5 / POLY ADP-RIBOSE POLYMERASE 5A / TNKS-1 / TRF1-INTERACTING ANKYRIN -RELATED ADP-RIBOSE POLYMERASE / TANKYRASE I / TANK1 / ADP-RIBOSYLTRA NSFERASE DIPHTHERIA TOXIN-LIKE 5 / ARTD 5 / POLY ADP-RIBOSE POLYMERA SE 5A / TNKS-1 / TRF1-INTERACTING ANKYRIN -RELATED ADP-RIBOSE POLYME RASE / TANKYRASE I


Mass: 29417.082 Da / Num. of mol.: 8 / Fragment: CATALYTIC DOMAIN, RESIDUES 1091-1325
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC-BSA4-TNKS1 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / Variant (production host): ROSETTA / References: UniProt: O95271, NAD+ ADP-ribosyltransferase
#2: Chemical
ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: Zn
#3: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#4: Chemical ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C2H6O2
#5: Chemical
ChemComp-92R / 3-{4-[(dimethylamino)methyl]phenyl}-5-methoxyisoquinolin-1(2H)-one


Mass: 308.374 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C19H20N2O2

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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: 2.12 Å3/Da / Density % sol: 53.7 % / Description: NONE
Crystal growpH: 6
Details: 0.1M MES PH 6.0, 0.1M AMMONIUM TATRATE, 12-16% PEG 3350

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795
DetectorType: DECTRIS PILATUS / Detector: PIXEL
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9795 Å / Relative weight: 1
ReflectionResolution: 3.37→46.92 Å / Num. obs: 27052 / % possible obs: 99.1 % / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 37.27 Å2 / Rmerge(I) obs: 0.09 / Net I/σ(I): 3.5
Reflection shellResolution: 3.37→3.57 Å / Redundancy: 3.2 % / Rmerge(I) obs: 1.12 / Mean I/σ(I) obs: 1.3 / % possible all: 98.6

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 2R5F

2r5f


Resolution: 3.37→46.923 Å / SU ML: 0.52 / σ(F): 0.02 / Phase error: 35.2 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3218 2714 5 %
Rwork0.266 --
obs0.2688 27052 98.94 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.37→46.923 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12693 0 216 0 12909
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00213304
X-RAY DIFFRACTIONf_angle_d0.47418024
X-RAY DIFFRACTIONf_dihedral_angle_d10.6654745
X-RAY DIFFRACTIONf_chiral_restr0.0211835
X-RAY DIFFRACTIONf_plane_restr0.0022563
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.3697-3.4310.39021120.36732719X-RAY DIFFRACTION98
3.431-3.49690.41831460.33392726X-RAY DIFFRACTION98
3.4969-3.56830.33741180.33762681X-RAY DIFFRACTION98
3.5683-3.64580.38221220.31722702X-RAY DIFFRACTION99
3.6458-3.73060.36021660.31432682X-RAY DIFFRACTION99
3.7306-3.82390.37951500.30732701X-RAY DIFFRACTION99
3.8239-3.92720.37151280.29742678X-RAY DIFFRACTION99
3.9272-4.04270.2951460.26962695X-RAY DIFFRACTION99
4.0427-4.17310.33791540.25652696X-RAY DIFFRACTION99
4.1731-4.32220.34331320.25172700X-RAY DIFFRACTION99
4.3222-4.49510.26351300.23212740X-RAY DIFFRACTION99
4.4951-4.69950.33141180.22692714X-RAY DIFFRACTION99
4.6995-4.9470.24041280.21582726X-RAY DIFFRACTION99
4.947-5.25660.28411380.23262706X-RAY DIFFRACTION99
5.2566-5.66180.32211640.24512694X-RAY DIFFRACTION100
5.6618-6.23040.31861700.26732726X-RAY DIFFRACTION100
6.2304-7.12930.33771560.2552656X-RAY DIFFRACTION99
7.1293-8.97180.26411700.21632713X-RAY DIFFRACTION100
8.9718-46.92730.27391660.21192650X-RAY DIFFRACTION98
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)
10.4088-0.26260.72080.8152-0.26231.3116-0.0147-0.15750.00450.31090.05390.0964-0.0335-0.37370.14920.2504-0.151-0.0130.15060.10050.060215.2554-26.1164-12.1655
20.48020.08110.37550.3525-0.31220.7119-0.0284-0.35370.11770.24840.0744-0.0569-0.2707-0.38520.66530.3706-0.03650.15130.3445-0.13540.296913.809-11.0252-11.5773
31.2906-1.07630.52061.0292-0.52550.30290.0970.49310.03160.1903-0.1516-0.15660.2250.2383-0.21380.4407-0.0619-0.04680.36730.00210.076922.9484-21.9027-20.7839
40.60680.4054-0.43610.43420.09711.2072-0.13690.0628-0.21060.0235-0.04140.10470.1396-0.12650.06840.54590.0464-0.26440.1752-0.09720.480712.5645-3.8255-22.2875
50.0493-0.04840.07410.22480.16470.44890.12790.15950.1108-0.0173-0.06790.0179-0.0936-0.27230.43280.25630.00570.24960.31920.07340.248914.4764-18.0145-19.7661
61.2216-0.1374-0.12261.0581-0.3110.1996-0.2201-0.1269-0.4580.05320.14230.14920.3028-0.3109-1.29150.4499-0.10870.11130.35090.18040.250353.04819.455-2.4089
70.3782-0.1859-0.68530.1110.32581.582-0.2230.193-0.2230.0095-0.0523-0.01550.3001-0.2503-0.58570.249-0.0921-0.08460.1660.13240.464953.766216.4981-13.807
81.03160.57220.26110.52230.05480.83270.10060.0710.03780.1157-0.069-0.2463-0.0111-0.0019-0.01130.1812-0.04230.03990.17610.05460.340959.62719.0719-18.2092
91.859-0.4392-1.21451.4181-0.25681.02250.1890.68070.0624-0.5459-0.09680.46070.0337-0.4322-0.38120.19970.0451-0.12150.28030.07030.351452.804230.5949-25.4849
100.5450.08490.06360.7947-0.38920.39360.0217-0.0211-0.1036-0.11960.10540.08260.1325-0.05680.17570.0755-0.0552-0.04060.2513-0.06930.162956.606912.5259-13.6683
111.3510.8081-1.72070.5604-0.89542.47020.23320.2780.30260.20720.02770.2929-0.6925-0.31610.34770.31850.1399-0.03710.27090.03780.1545.077427.786816.2213
120.004-0.01160.01790.0365-0.05440.07920.06350.0054-0.07220.009-0.00740.05130.128-0.01270.07090.5506-0.1805-0.17590.4318-0.13520.377351.48284.35799.3377
130.18380.1876-0.16260.1897-0.16790.14470.15690.3649-0.2252-0.29510.14730.0240.8365-0.16450.04850.5237-0.0529-0.05910.34930.03450.474148.279812.421316.9447
140.86780.09170.02530.00880.01080.04740.1733-0.47150.1068-0.1902-0.07840.23590.07510.10050.01050.387-0.03750.00480.2886-0.04170.319647.570417.732426.8832
150.6670.05090.33571.757-0.50890.52720.1502-0.0955-0.29650.2567-0.00210.29610.0315-0.13260.27230.17-0.0308-0.05310.180.00750.22542.798113.870123.0977
160.99150.0702-0.02680.31040.56241.03140.38930.20350.077-0.38820.0831-0.1537-0.2499-0.14290.12030.31870.12010.02980.20970.01230.25195.855-25.954315.1274
172.382-0.22662.28680.2597-0.07922.2793-0.0523-0.5626-0.04410.2126-0.05320.44340.2059-0.510.04710.50330.06380.09680.2672-0.08750.37912.7358-34.224625.2659
180.3338-0.48380.01350.9269-0.1080.1594-0.1458-0.00560.13510.40890.0734-0.1754-0.2055-0.0063-0.10510.29460.13570.02380.28430.26560.34256.907-23.781328.4502
190.21930.01980.13470.0788-0.22080.79830.06240.10780.12720.11070.00280.007-0.3842-0.05820.08740.4156-0.00880.17760.3090.00320.14134.8539-28.676625.0541
200.79750.0766-0.06570.7808-0.20020.3241-0.04320.08050.32040.17950.10640.0657-0.27-0.17330.04730.2396-0.0272-0.07220.23140.10130.17672.1839-29.103822.2227
210.93640.4258-0.16640.2101-0.13870.31480.188-0.039-0.3481-0.2894-0.2877-0.28140.57780.38980.01620.64180.09910.07470.2886-0.0120.571760.0698-28.433321.4086
220.5385-0.25510.12740.22330.14790.46270.2561-0.18690.1112-0.2324-0.3328-0.0504-0.13410.0879-0.07590.3715-0.0790.09060.13440.0420.32156.1804-15.183719.3441
231.0376-0.073-0.11390.393-0.09240.51250.0472-0.16360.2270.03810.16750.0517-0.1039-0.19521.39780.05960.05770.07830.30440.03740.183656.458-18.302629.5789
240.92480.12670.00670.1897-0.30.51750.406-0.50060.19970.1397-0.177-0.0055-0.2517-0.30980.27560.4815-0.12150.01150.47920.01220.350452.5857-23.110828.3127
250.6736-0.1248-0.00871.08610.35780.12270.1314-0.13490.26280.4241-0.1055-0.24020.18760.0904-0.04020.2844-0.00330.10450.2127-0.05530.259158.6867-14.710226.6077
260.3418-0.238-0.17170.46490.27770.4256-0.1808-0.031-0.21080.09480.0421-0.07910.33390.207-0.04450.2730.10560.18160.17630.06540.132422.58089.08113.1039
270.83210.3302-0.35821.0443-0.43430.57570.0874-0.3001-0.0890.1831-0.07870.1664-0.06030.07360.00540.12890.13740.06940.3279-0.00730.141620.239519.612221.03
280.2375-0.01410.09590.56870.28310.28040.0588-0.0908-0.13720.16360.1964-0.24230.11070.06640.83110.04390.1711-0.04560.42780.0880.213513.561220.703427.2905
291.711-1.032-0.20651.91650.62060.214-0.2428-0.3019-0.32250.32450.18690.0480.14450.1180.0450.12240.09530.12670.23050.01630.294520.657326.414929.3801
300.21380.17960.09730.37470.1550.0690.09080.0167-0.0852-0.1508-0.0286-0.00470.0637-0.0337-0.01580.35390.1392-0.03770.22610.13130.161616.9437.599821.6076
310.3331-0.1561-0.31740.5683-0.30670.71720.0728-0.05110.22960.34520.1896-0.11660.1460.18780.35790.276-0.0415-0.12440.3026-0.060.282530.949226.0819-11.3869
321.8799-0.1974-0.42690.80430.06420.18430.3061-0.4319-0.14090.5523-0.05960.15840.09710.2790.21270.4091-0.0161-0.08070.2548-0.03380.281825.480513.3662-7.4675
330.3246-0.0310.42010.48290.41960.98430.13330.47630.1374-0.19480.3351-0.05760.11670.03040.58170.1925-0.0597-0.02680.27160.07820.405324.845119.9715-20.9447
340.10110.01630.08190.48060.95042.25280.01920.0157-0.0780.12030.2588-0.3082-0.1810.23290.57690.16080.0206-0.10470.17530.00490.374334.39565.2557-17.7556
350.5618-0.25190.07260.7695-0.33590.52470.03450.08240.1314-0.04340.0044-0.0507-0.0384-0.0140.6330.0740.0208-0.06370.03950.02870.181326.737326.8411-12.0723
360.75150.2335-0.84540.2571-0.58811.5240.05160.14880.16040.30040.02240.0546-0.42180.11040.5720.3639-0.19840.05090.2272-0.04850.129569.9271-17.2234-11.2642
370.4173-0.5260.12041.2577-0.32950.0828-0.1558-0.0382-0.08040.11960.18150.1983-0.1782-0.13680.18750.44660.09640.03020.22240.12450.072164.673-32.4413-6.404
380.56320.3973-0.18691.0241-0.46210.76680.06050.1755-0.01910.05950.19860.0337-0.29360.13870.38080.1772-0.0744-0.00830.25130.04280.10264.3965-25.9555-19.1693
390.1188-0.12390.15450.1299-0.16130.19880.05550.13160.0781-0.07540.1278-0.1327-0.04920.04841.43430.11550.06630.20760.24370.00260.111373.7674-39.1049-17.598
400.11010.1238-0.06080.2949-0.01790.16530.0149-0.0392-0.02720.0946-0.05920.06080.0584-0.049-0.32360.1901-0.16820.07970.2193-0.1120.088766.1929-15.7331-13.0436
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 1105:1164)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 1165:1192)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 1193:1252)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 1253:1276)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 1277:1313)
6X-RAY DIFFRACTION6(CHAIN B AND RESID 1105:1118)
7X-RAY DIFFRACTION7(CHAIN B AND RESID 1119:1171)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 1172:1259)
9X-RAY DIFFRACTION9(CHAIN B AND RESID 1260:1297)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 1298:1313)
11X-RAY DIFFRACTION11(CHAIN C AND RESID 1105:1154)
12X-RAY DIFFRACTION12(CHAIN C AND RESID 1155:1171)
13X-RAY DIFFRACTION13(CHAIN C AND RESID 1172:1195)
14X-RAY DIFFRACTION14(CHAIN C AND RESID 1196:1267)
15X-RAY DIFFRACTION15(CHAIN C AND RESID 1268:1314)
16X-RAY DIFFRACTION16(CHAIN D AND RESID 1105:1188)
17X-RAY DIFFRACTION17(CHAIN D AND RESID 1189:1210)
18X-RAY DIFFRACTION18(CHAIN D AND RESID 1211:1236)
19X-RAY DIFFRACTION19(CHAIN D AND RESID 1237:1273)
20X-RAY DIFFRACTION20(CHAIN D AND RESID 1274:1315)
21X-RAY DIFFRACTION21(CHAIN E AND RESID 1105:1139)
22X-RAY DIFFRACTION22(CHAIN E AND RESID 1140:1208)
23X-RAY DIFFRACTION23(CHAIN E AND RESID 1209:1224)
24X-RAY DIFFRACTION24(CHAIN E AND RESID 1225:1264)
25X-RAY DIFFRACTION25(CHAIN E AND RESID 1265:1314)
26X-RAY DIFFRACTION26(CHAIN F AND RESID 1105:1125)
27X-RAY DIFFRACTION27(CHAIN F AND RESID 1126:1187)
28X-RAY DIFFRACTION28(CHAIN F AND RESID 1188:1276)
29X-RAY DIFFRACTION29(CHAIN F AND RESID 1277:1301)
30X-RAY DIFFRACTION30(CHAIN F AND RESID 1302:1313)
31X-RAY DIFFRACTION31(CHAIN G AND RESID 1105:1141)
32X-RAY DIFFRACTION32(CHAIN G AND RESID 1142:1195)
33X-RAY DIFFRACTION33(CHAIN G AND RESID 1196:1252)
34X-RAY DIFFRACTION34(CHAIN G AND RESID 1253:1300)
35X-RAY DIFFRACTION35(CHAIN G AND RESID 1301:1313)
36X-RAY DIFFRACTION36(CHAIN H AND RESID 1105:1144)
37X-RAY DIFFRACTION37(CHAIN H AND RESID 1145:1192)
38X-RAY DIFFRACTION38(CHAIN H AND RESID 1193:1258)
39X-RAY DIFFRACTION39(CHAIN H AND RESID 1259:1301)
40X-RAY DIFFRACTION40(CHAIN H AND RESID 1302:1314)

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