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 15766

Title: human calpastatin Domain 1   PubMed: 18537264

Authors: Kiss, Robert

Citation: Kiss, Robert; Kovacs, D.; Tompa, P.; Perczel, Andras. "Local Structural Preferences of Calpastatin, the Intrinsically Unstructured Protein Inhibitor of Calpain"  Biochemistry 47, 6936-6945 (2008).

Assembly members:
hCSD1, polymer, 141 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
hCSD1: AVPVESKPDKPSGKSGMDAA LDDLIDTLGGPEETEEENTT YTGPEVSDPMSSTYIEELGK REVTIPPKYRELLAKKEGIT GPPADSSKPIGPDDAIDALS SDFTCGSPTAAGKKTEKEES TEVLKAQSAGTVRSAAPPQE K

Data sets:
Data typeCount
13C chemical shifts256
15N chemical shifts122
1H chemical shifts249
T1 relaxation values90
T2 relaxation values90

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hCSD11

Entities:

Entity 1, hCSD1 141 residues - Formula weight is not available

1   ALAVALPROVALGLUSERLYSPROASPLYS
2   PROSERGLYLYSSERGLYMETASPALAALA
3   LEUASPASPLEUILEASPTHRLEUGLYGLY
4   PROGLUGLUTHRGLUGLUGLUASNTHRTHR
5   TYRTHRGLYPROGLUVALSERASPPROMET
6   SERSERTHRTYRILEGLUGLULEUGLYLYS
7   ARGGLUVALTHRILEPROPROLYSTYRARG
8   GLULEULEUALALYSLYSGLUGLYILETHR
9   GLYPROPROALAASPSERSERLYSPROILE
10   GLYPROASPASPALAILEASPALALEUSER
11   SERASPPHETHRCYSGLYSERPROTHRALA
12   ALAGLYLYSLYSTHRGLULYSGLUGLUSER
13   THRGLUVALLEULYSALAGLNSERALAGLY
14   THRVALARGSERALAALAPROPROGLNGLU
15   LYS

Samples:

sample_1: hCSD1, [U-99% 13C; U-99% 15N], 1 mM

sample_conditions_1: ionic strength: 10 M; pH: 6.07; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker DRX 500 MHz

Related Database Links:

DBJ BAH14064
GB AAA52753 AAA52759 AAB59398
SP P49342