BMRB Entry 19916

Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp with dT7
Deposition date:
2014-04-17
Original release date:
2014-08-25
Authors:
Jin, Bonghwan; Jeong, Ki-woong; Kim, Yangmee
Citation:

Citation: Jin, Bonghwan; Jeong, Ki-Woong; Kim, Yangmee. "Structure and flexibility of the thermophilic cold-shock protein of Thermus aquaticus."  Biochem. Biophys. Res. Commun. 451, 402-407 (2014).
PubMed: 25101648

Assembly members:

Assembly members:
entity, polymer, 68 residues, 7692.736 Da.
6,7-dimethoxy-3,4-dihydroisoquinoline-2(1H)-sulfonamide, non-polymer, 272.321 Da.

Natural source:

Natural source:   Common Name: thermophilic bacteria   Taxonomy ID: 271   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus aquaticus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-11a

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts380
13C chemical shifts155
15N chemical shifts66

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1
2entity_DT72

Entities:

Entity 1, entity 68 residues - 7692.736 Da.

1   METLYSLYSGLYTHRVALLYSTRPPHEASN
2   ALAGLULYSGLYTYRGLYPHEILEGLNGLN
3   GLUGLUGLYPROASPVALPHEVALHISPHE
4   THRALAILEGLUALAASPGLYPHEARGTHR
5   LEUASNGLUGLYGLUHISVALGLUPHEGLU
6   VALGLUPROGLYARGGLYGLYLYSGLYPRO
7   GLNALALYSLYSVALARGARGILE

Entity 2, entity_DT7 - C11 H16 N2 O4 S - 272.321 Da.

1   DT7

Samples:

tacspcom: potassium phosphate 50 mM; KCl 100 mM; EDTA 0.1 mM; thermus aquaticus cold shock protein, [U-99% 13C; U-99% 15N], 0.8 mM; heptathymidine 0.8 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOtacspcomisotropicsample_conditions_1
3D HN(CA)COtacspcomisotropicsample_conditions_1
3D CBCA(CO)NHtacspcomisotropicsample_conditions_1
3D HN(CO)CAtacspcomisotropicsample_conditions_1
3D HBHA(CO)NHtacspcomisotropicsample_conditions_1
3D HNHAtacspcomisotropicsample_conditions_1
3D HCCH-TOCSYtacspcomisotropicsample_conditions_1
3D 1H-15N NOESYtacspcomisotropicsample_conditions_1
3D 1H-13C NOESYtacspcomisotropicsample_conditions_1
2D 1H-15N HSQCtacspcomisotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 19915
PDB
GB ALJ89896 EED09135 KOX89549
REF WP_003049060 WP_018110812 WP_022797725 WP_053768577

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