BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 4296

Title: 1H, 13C, and 15N Chemical Shift Assignments for E. coli Cold-shock Protein A (CspA)

Authors: Feng, Wenqing; Tejero, Roberto; Zimmerman, Diane; Inouye, Masayori; Montelione, Gaetano

Citation: Feng, Wenqing; Tejero, Roberto; Zimmerman, Diane; Inouye, Masayori; Montelione, Gaetano. "Solution NMR Structure and Backbone Dynamics of the Major Cold-shock Protein (CspA) from Escherichia coli: Evidence for Conformational Dyanamics in the Single-stranded RNA-binding Site"  Biochemistry 37, 10881-10896 (1998).

Assembly members:
Cold shock protein A, polymer, 70 residues, 7400 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
Cold shock protein A: MSGKMTGIVKWFNADKGFGF ITPDDGSKDVFVHFSAIQND GYKSLDEGQKVSFTIESGAK GPAAGNVTSL

Data sets:
Data typeCount
1H chemical shifts449
13C chemical shifts244
15N chemical shifts72

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1CspA monomer1

Entities:

Entity 1, CspA monomer 70 residues - 7400 Da.

1   METSERGLYLYSMETTHRGLYILEVALLYS
2   TRPPHEASNALAASPLYSGLYPHEGLYPHE
3   ILETHRPROASPASPGLYSERLYSASPVAL
4   PHEVALHISPHESERALAILEGLNASNASP
5   GLYTYRLYSSERLEUASPGLUGLYGLNLYS
6   VALSERPHETHRILEGLUSERGLYALALYS
7   GLYPROALAALAGLYASNVALTHRSERLEU

Samples:

sample_1: Cold shock protein A, [U-98% 13C; U-90% 15N], 1.0 – 3.0 mM; KH2PO4 50 mM; NaEDTA 0.1 mM; NaN3 1 mM

Ex-cond_1: pH*: 6.0 na; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
Most of the triple resonance experiments were exectutedsample_1not availablenot available
with C-H or C-C phase labeling to aid assignmentssample_1not availablenot available
[Tashiro et al. J. Biomol. NMR (1995) 6: 211 - 216;sample_1not availablenot available
Feng et al., J. Biomol. NMR (1996) 8, 98 - 104; Rios et al.,sample_1not availablenot available
J. Biomol. NMR (1996) 8, 345 - 350].sample_1not availablenot available
HSQCsample_1not availablenot available
HNCOsample_1not availablenot available
HNCAsample_1not availablenot available
CANHsample_1not availablenot available
CA(CO)NHsample_1not availablenot available
HA(CA)NHsample_1not availablenot available
HA(CA)(CO)NHsample_1not availablenot available
CBCANHsample_1not availablenot available
CBCA(CO)NHsample_1not availablenot available
HCCNH-TOCSYsample_1not availablenot available
HCC(CO)NH-TOCSYsample_1not availablenot available
homonuclear 2D H-TOCSYsample_1not availablenot available
15N-edited 3D NOESY"sample_1not availablenot available

Software:

AutoAssign v1.0 - automated analysis of backbone N, C, H, and sidechain Cb resonance assignments

Varian_VNMR v5.3, Varian Associates - Data collection and processing of 3D Fourier transforms

NMRCompass, MSI - Automatic peak pick of frequency-domain 2D and 3D data sets.

NMR spectrometers:

  • Varian Unity 500 MHz

Related Database Links:

BMRB 4107 4108
PDB
DBJ BAB37864 BAE77739 BAG79354 BAH65698 BAI28199
EMBL CAD07979 CAP78016 CAQ33874 CAQ91030 CAR00519
GB AAA23617 AAB18533 AAB66357 AAB69447 AAC06036
PIR AG0981
REF NP_312468 NP_418012 NP_458276 NP_462550 NP_709333
SP P0A9X9 P0A9Y0 P0A9Y1 P0A9Y2 P0A9Y3