BMRB Entry 35048

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR35048
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
NMR Solution Structure of Cold Shock Protein CspA
Deposition date:
2026-04-28
Original release date:
2026-06-25
Authors:
Wanko, M.; Dambon, C.; Feller, G.; Volkov, O.
Citation:

Citation: Wanko Nembot, M.; Feller, G.; Volkov, A.; le Paige, U.; Bouvignies, G.; Damblon, C.. "Structural and functional insights into a mesophilic cold shock protein CspA with enhanced precision. "  J. Magn. Reson. 388, 108077-108077 (2026).
PubMed: 42102648

Assembly members:

Assembly members:
entity_1, polymer, 70 residues, 7411.253 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MSGKMTGIVKWFNADKGFGF ITPDDGSKDVFVHFSAIQND GYKSLDEGQKVSFTIESGAK GPAAGNVTSL

Data sets:
Data typeCount
13C chemical shifts253
15N chemical shifts70
1H chemical shifts411

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 70 residues - 7411.253 Da.

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

Samples:

sample_1: Mesophilic cold shock protein, [U-100% 13C; U-100% 15N], 500 uM; potassium phosphate 50 mM; KCl 100 mM; EDTA 0.1 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(COCA)CBsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TopSpin, Bruker Biospin - collection, processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

CcpNmr Analysis, CCPN - chemical shift assignment, data analysis, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMR spectrometers:

  • Bruker AVANCE III HD 700 MHz
  • Bruker AVANCE III 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks