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Phosphorylation of Cytoplasmic Tail of Tissue Factor and its Role in Modulating Structure and Binding Affinity.
Authors
Sen, M., Agrawal, S., Craft, J., Ruf, W., Legge, G.B.
Assembly
TFSP253
Entity
1. TFSP253 (polymer, Thiol state: all free), 19 monomers, 2140.272 × 2 Da Detail

CRKAGVGQXW KENSPLNVS


Total weight
4280.544 Da
Max. entity weight
2140.272 Da
Source organism
Homo sapiens
Exptl. method
NMR
Refine. method
SIMULATED ANNEALING
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 89.5 %, Completeness: 72.9 %, Completeness (bb): 77.4 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All72.9 % (151 of 207)78.2 % (86 of 110)59.2 % (45 of 76)95.2 % (20 of 21)
Backbone77.4 % (82 of 106)91.9 % (34 of 37)61.5 % (32 of 52)94.1 % (16 of 17)
Sidechain70.9 % (83 of 117)71.2 % (52 of 73)67.5 % (27 of 40)100.0 % (4 of 4)
Aromatic58.3 % (7 of 12)100.0 % (6 of 6) 0.0 % (0 of 5)100.0 % (1 of 1)
Methyl57.1 % (8 of 14)57.1 % (4 of 7)57.1 % (4 of 7)

1. TFSP253

CRKAGVGQXW KENSPLNVS

Sample

Pressure 1 (±0) atm, Temperature 285 (±0.3) K, pH 6.0 (±0.05), Details 6mM TFSP253 in 10% D2O pH 6.0


#NameIsotope labelingTypeConcentration
1TFSP253protein6 (±0.05) mM
2D2Osolvent10 %

Protein Blocks Logo
Calculated from 10 models in PDB: 2CEZ, Strand ID: A Detail


Release date
2006-02-19
Citation
Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region
Sen, M., Herzik, M., Craft, J.W., Creath, A.L., Agrawal, S., Ruf, W., Legge, G.B.
Open Spectrosc. J. (2009), 3, 58-64, PubMed 20076769 , DOI 10.2174/1874383800903010058 ,
Related entities 1. TFSP253, : 1 : 5 : 2 entities Detail
Interaction partners 1. TFSP253, : 3 interactors Detail
Experiments performed 6 experiments Detail
nullKeywords NMR, Phosphorylation, Homonuclear NMR, Tissue Factor, phosphorylation