BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 15787

Title: 1H and 15N chemical shift assignments for HINT1 protein   PubMed: 19636947

Deposition date: 2008-05-29 Original release date: 2009-01-28

Authors: Shapiro, Michael; Bai, Guoyun; Feng, Bo

Citation: Bai, Guoyun; Feng, Bo; Wang, Jia Bei; Varney, Kristen; Shapiro, Michael. "Backbone assignment of HINT1 protein, a mouse histidine triad nucleotide binding protein"  Biomol. NMR Assignments 3, 57-59 (2009).

Assembly members:
HINT1, polymer, 126 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
HINT1: MADEIAKAQVAQPGGDTIFG KIIRKEIPAKIIFEDDRCLA FHDISPQAPTHFLVIPKKHI SQISVADDDDESLLGHLMIV GKKCAADLGLKRGYRMVVNE GADGGQSVYHIHLHVLGGRQ MNWPPG

Data sets:
Data typeCount
13C chemical shifts347
15N chemical shifts116
1H chemical shifts116

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1HINT11

Entities:

Entity 1, HINT1 126 residues - Formula weight is not available

1   METALAASPGLUILEALALYSALAGLNVAL
2   ALAGLNPROGLYGLYASPTHRILEPHEGLY
3   LYSILEILEARGLYSGLUILEPROALALYS
4   ILEILEPHEGLUASPASPARGCYSLEUALA
5   PHEHISASPILESERPROGLNALAPROTHR
6   HISPHELEUVALILEPROLYSLYSHISILE
7   SERGLNILESERVALALAASPASPASPASP
8   GLUSERLEULEUGLYHISLEUMETILEVAL
9   GLYLYSLYSCYSALAALAASPLEUGLYLEU
10   LYSARGGLYTYRARGMETVALVALASNGLU
11   GLYALAASPGLYGLYGLNSERVALTYRHIS
12   ILEHISLEUHISVALLEUGLYGLYARGGLN
13   METASNTRPPROPROGLY

Samples:

sample_1: HINT1, [U-98% 13C; U-98% 15N], 0.2 mM; D2O, [U-99% 2H], 10%; H2O 90%; sodium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 7.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DMX 600 MHz
  • Varian Unity 500 MHz

Related Database Links:

DBJ BAB22484 BAB28235
GB AAC71076 AAH70415 AAH80296 AAI68732 EDL33521
REF NP_001103077 NP_032274 XP_005350115
SP P62959 P70349

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts