BMRB Entry 19915

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19915
MolProbity Validation Chart

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for cold shock protein, TaCsp
Deposition date:
2014-04-17
Original release date:
2014-08-25
Authors:
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.

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: pET11-a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MKKGTVKWFNAEKGYGFIQQ EEGPDVFVHFTAIEADGFRT LNEGEHVEFEVEPGRGGKGP QAKKVRRI

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

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 68 residues - 7692.736 Da.

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

Samples:

sample_1: 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; H2O 90%; D2O 10%

Tacsp_free_condition1: pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_1isotropicTacsp_free_condition1
3D HN(CA)COsample_1isotropicTacsp_free_condition1
3D CBCA(CO)NHsample_1isotropicTacsp_free_condition1
3D HN(CO)CAsample_1isotropicTacsp_free_condition1
3D HBHA(CO)NHsample_1isotropicTacsp_free_condition1
3D HNHAsample_1isotropicTacsp_free_condition1
3D HCCH-TOCSYsample_1isotropicTacsp_free_condition1
3D 1H-15N NOESYsample_1isotropicTacsp_free_condition1
3D 1H-13C NOESYsample_1isotropicTacsp_free_condition1
2D 1H-15N HSQCsample_1isotropicTacsp_free_condition1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift calculation

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 500 MHz

Related Database Links:

BMRB 19916
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