BMRB Entry 11037

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR11037

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Title:
1H, 13C, and 15N chemical shift assignments for Thermus thermophilus HB8 TTHA1718 protein in living E. coli cells
Deposition date:
2008-03-20
Original release date:
2009-02-27
Authors:
Sakakibara, Daisuke; Sasaki, Atsuko; Ikeya, Teppei; Hamatsu, Junpei; Koyama, Hiroko; Mishima, Masaki; Mikawa, Tsutomu; Waelchli, Markus; Smith, Brian; Shirakawa, Masahiro; Guentert, Peter; Ito, Yutaka
Citation:

Citation: Sakakibara, Daisuke; Sasaki, Atsuko; Ikeya, Teppei; Hamatsu, Junpei; Hanashima, Tomomi; Mishima, Masaki; Yoshimasu, Masatoshi; Hayashi, Nobuhiro; Mikawa, Tsutomu; Waelchli, Markus; Smith, Brian; Shirakawa, Masahiro; Guentert, Peter; Ito, Yutaka. "Protein structure determination in living cells by in-cell NMR spectroscopy"  Nature 458, 102-105 (2009).
PubMed: 19262674

Assembly members:

Assembly members:
TTHA1718 heavy metal binding protein, polymer, 66 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Thermus thermophilus   Taxonomy ID: 300852   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
TTHA1718 heavy metal binding protein: MLKLKVEGMTCNHCVMAVTK ALKKVPGVEKVEVSLEKGEA LVEGTADPKALVQAVEEEGY KAEVLA

Data sets:
Data typeCount
13C chemical shifts207
15N chemical shifts62
1H chemical shifts356

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TTHA1718 heavy metal binding protein1

Entities:

Entity 1, TTHA1718 heavy metal binding protein 66 residues - Formula weight is not available

1   METLEULYSLEULYSVALGLUGLYMETTHR
2   CYSASNHISCYSVALMETALAVALTHRLYS
3   ALALEULYSLYSVALPROGLYVALGLULYS
4   VALGLUVALSERLEUGLULYSGLYGLUALA
5   LEUVALGLUGLYTHRALAASPPROLYSALA
6   LEUVALGLNALAVALGLUGLUGLUGLYTYR
7   LYSALAGLUVALLEUALA

Samples:

sample_1: TTHA1718 heavy metal binding protein, [U-13C; U-15N], 3 – 4 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.5; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D H(CCCO)NHsample_1isotropicsample_conditions_1
3D CC(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
4D HCC(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin - collection

AZARA v2.7, Boucher - peak picking, processing

ANSIG, Kraulis - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE 600 MHz

Related Database Links:

BMRB 11035
PDB
DBJ BAD71541
GB AAS81698 AEG34130 AFH38237
REF WP_011173740 WP_011228864 WP_014629043 YP_144984

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