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1H, 13C, and 15N Chemical Shift Assignments for E. coli Cold-shock Protein A (CspA)
Authors
Feng, W., Tejero, R., Zimmerman, D.E., Inouye, M., Montelione, G.T.
Assembly
Major cold shock protein from E. coli
Entity
1. Major cold shock protein from E. coli (polymer), 70 monomers, 7403.187 Da Detail

MSGKMTGIVK WFNADKGFGF ITPDDGSKDV FVHFSAIQND GYKSLDEGQK VSFTIESGAK GPAAGNVTSL


Formula weight
7403.187 Da
Source organism
Escherichia coli
Exptl. method
NMR
Refine. method
CONSTRAINT-VIOLATION MINIMIZATION IN DIHEDRAL ANGLE SPACE
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 98.6 %, Completeness: 90.0 %, Completeness (bb): 97.1 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All90.0 % (704 of 782)96.3 % (387 of 402)80.1 % (245 of 306)97.3 % (72 of 74)
Backbone97.1 % (404 of 416)98.0 % (145 of 148)96.5 % (193 of 200)97.1 % (66 of 68)
Sidechain84.0 % (358 of 426)95.3 % (242 of 254)66.3 % (110 of 166)100.0 % (6 of 6)
Aromatic51.2 % (43 of 84)100.0 % (42 of 42) 0.0 % (0 of 41)100.0 % (1 of 1)
Methyl90.3 % (56 of 62)100.0 % (31 of 31)80.6 % (25 of 31)

1. Cold shock protein A

MSGKMTGIVK WFNADKGFGF ITPDDGSKDV FVHFSAIQND GYKSLDEGQK VSFTIESGAK GPAAGNVTSL

Sample

Temperature 303 (±0.5) K, Details Samples were prepared in H2O containing 5% deuterium oxide for locking purposes. Solutions were buffered at pH* 6.0 +/- 0.1.


#NameIsotope labelingTypeConcentration
1Cold shock protein A[U-98% 13C; U-90% 15N]1.0 ~ 3.0 mM
2KH2PO450 mM
3NaEDTA0.1 mM
4NaN31 mM

LACS Plot; CA
Referencing offset: 0.04 ppm, Outliers: 2 Detail
LACS Plot; CB
Referencing offset: 0.04 ppm, Outliers: 2 Detail
LACS Plot; HA
Referencing offset: 0.03 ppm, Outliers: 4 Detail
LACS Plot; CO
Referencing offset: 0.66 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 16 models in PDB: 3MEF, Strand ID: A Detail


Release date
1999-02-09
Citation 1
Solution NMR structure and backbone dynamics of the major cold-shock protein (CspA) from Escherichia coli: evidence for conformational dynamics in the single-stranded RNA-binding site
Feng, W., Tejero, R., Zimmerman, D.E., Inouye, M., Montelione, G.T.
Biochemistry (1998), 37, 10881-10896, PubMed 9692981 , DOI 10.1021/bi980269j ,
Citation 2
Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA
Newkirk, K., Feng, W., Jiang, W., Tejero, R., Emerson, S.D., Inouye, M., Montelione, G.T.
Proc. Natl. Acad. Sci. U. S. A. (1994), 91, 5114-5118, PubMed 7515185 , DOI: ,
Citation 3
Automated analysis of protein NMR assignments using methods from artificial intelligence
Zimmerman, D.E., Kulikowski, C.A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C., Powers, R., Montelione, G.T.
J. Mol. Biol. (1997), 269, 592-610, PubMed 9217263 , DOI 10.1006/jmbi.1997.1052 ,
Related entities 1. Major cold shock protein from E. coli, : 1 : 2 : 3 : 203 entities Detail
Interaction partners 1. Major cold shock protein from E. coli, : 11 interactors Detail
Experiments performed 18 experiments Detail
Chemical shift validation 3 contents Detail
Keywords RNA-binding protein, DNA-binding protein, 15N relaxation, OB fold, transcriptional regulation