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Solution structure of the peptidyl prolyl cis-trans isomerase domain of human Pin1 with sulfate ion
Authors
Xu, N., Tamari, Y., Tochio, N., Tate, S.
Assembly
wild type hPin1 PPIase domain
Entity
1. wild type hPin1 PPIase domain (polymer, Thiol state: all free), 117 monomers, 13100.56 Da Detail

GSHMEPARVR CSHLLVKHSQ SRRPSSWRQE KITRTKEEAL ELINGYIQKI KSGEEDFESL ASQFSDCSSA KARGDLGAFS RGQMQKPFED ASFALRTGEM SGPVFTDSGI HIILRTE


Formula weight
13100.56 Da
Source organism
Homo sapiens
Exptl. method
solution NMR
Refine. method
distance geometry
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.3 %, Completeness: 98.4 %, Completeness (bb): 97.1 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All98.4 % (1324 of 1346)98.9 % (700 of 708)98.3 % (508 of 517)95.9 % (116 of 121)
Backbone97.1 % (674 of 694)97.5 % (233 of 239)97.4 % (333 of 342)95.6 % (108 of 113)
Sidechain99.5 % (756 of 760)99.6 % (467 of 469)99.3 % (281 of 283)100.0 % (8 of 8)
Aromatic100.0 % (96 of 96)100.0 % (48 of 48)100.0 % (47 of 47)100.0 % (1 of 1)
Methyl100.0 % (98 of 98)100.0 % (49 of 49)100.0 % (49 of 49)

1. wild type hPin1 PPIase domain

GSHMEPARVR CSHLLVKHSQ SRRPSSWRQE KITRTKEEAL ELINGYIQKI KSGEEDFESL ASQFSDCSSA KARGDLGAFS RGQMQKPFED ASFALRTGEM SGPVFTDSGI HIILRTE

Sample

Solvent system 94.12% H2O/5.88% D2O, Pressure 1 atm, Temperature 299 K, pH 6.6


#NameIsotope labelingTypeConcentration
1wild type hPin1 PPIase domain[U-13C; U-15N]protein0.8 mM
2sodium sulfatenatural abundancesalt100 mM
3sodium phosphatenatural abundancebuffer50 mM
4EDTAnatural abundance5 mM
5DTTnatural abundance1 mM
6sodium azidenatural abundance0.03 %
7H2Onatural abundancesolvent94.12 %
8D2Onatural abundancesolvent5.88 %

LACS Plot; CA
Referencing offset: -0.53 ppm, Outliers: 1 Detail
LACS Plot; CB
Referencing offset: -0.53 ppm, Outliers: 1 Detail
LACS Plot; HA
Referencing offset: 0.0 ppm, Outliers: 3 Detail
LACS Plot; CO
Referencing offset: -0.31 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 10 models in PDB: 2RUC, Strand ID: A Detail


Release date
2014-12-14
Citation
The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif
Xu, N., Tochio, N., Wang, J., Tamari, Y., Uewaki, J., Utsunomiya-Tate, N., Igarashi, K., Shiraki, T., Kobayashi, N., Tate, S.
Biochemistry (2014), 53, 5568-5578, PubMed 25100325 , DOI 10.1021/bi5007817 ,
Related entities 1. wild type hPin1 PPIase domain, : 1 : 1 : 58 : 116 entities Detail
Interaction partners 1. wild type hPin1 PPIase domain, : 141 interactors Detail
Experiments performed 14 experiments Detail
nullKeywords PPIase, protein/cis-trans-isomerase