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Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp
Authors
Jeong, K., Kim, Y.
Assembly
cold shock protein, TaCsp
Entity
1. cold shock protein, TaCsp (polymer, Thiol state: not present), 68 monomers, 7679.549 Da Detail

MKKGTVKWFN AEKGYGFIQQ EEGPDVFVHF TAIEADGFRT LNEGEHVEFE VEPGRGGKGP QAKKVRRI


Formula weight
7679.549 Da
Source organism
Thermus aquaticus
Exptl. method
solution NMR
Refine. method
distance geometry
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 95.6 %, Completeness: 69.7 %, Completeness (bb): 78.4 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All69.7 % (566 of 812)79.9 % (342 of 428)50.5 % (158 of 313)93.0 % (66 of 71)
Backbone78.4 % (315 of 402)95.8 % (137 of 143)60.8 % (118 of 194)92.3 % (60 of 65)
Sidechain64.7 % (303 of 468)71.9 % (205 of 285)52.0 % (92 of 177)100.0 % (6 of 6)
Aromatic25.0 % (22 of 88)47.7 % (21 of 44) 0.0 % (0 of 43)100.0 % (1 of 1)
Methyl72.2 % (39 of 54)70.4 % (19 of 27)74.1 % (20 of 27)

1. entity

MKKGTVKWFN AEKGYGFIQQ EEGPDVFVHF TAIEADGFRT LNEGEHVEFE VEPGRGGKGP QAKKVRRI

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 6


#NameIsotope labelingTypeConcentration
1potassium phosphatenatural abundance50 mM
2KClnatural abundance100 mM
3EDTAnatural abundance0.1 mM
4Thermus aquaticus cold shock protein[U-99% 13C; U-99% 15N]0.8 mM
5H2Onatural abundance90 %
6D2Onatural abundance10 %

LACS Plot; CA
Referencing offset: -1.34 ppm, Outliers: 2 Detail
LACS Plot; CB
Referencing offset: -1.34 ppm, Outliers: 2 Detail
LACS Plot; HA
Referencing offset: -0.06 ppm, Outliers: 2 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2MO0, Strand ID: A Detail


Release date
2014-08-24
Citation
Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus
Jin, B., Jeong, K.W., Kim, Y.
Biochem. Biophys. Res. Commun. (2014), 451, 402-407, PubMed 25101648 , DOI 10.1016/j.bbrc.2014.07.127 ,
Related entities 1. cold shock protein, TaCsp, : 1 : 1 : 164 entities Detail
Experiments performed 10 experiments Detail
nullKeywords cold shock protein, nuclear magnetic resonance, protein binding, protien stability, thermus aquaticus