BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15517

Title: 1H, 13C, and 15N Chemical Shift Assignments for ca-free rat alpha-parvalbumin   PubMed: 18218708

Deposition date: 2007-10-10 Original release date: 2008-06-26

Authors: Henzl, Michael

Citation: Henzl, Michael; Tanner, John. "Solution structure of Ca2+-free rat alpha-parvalbumin"  Protein Sci. 17, 431-438 (2008).

Assembly members:
parvalbumin, polymer, 109 residues, Formula weight is not available

Natural source:   Common Name: rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11

Entity Sequences (FASTA):
parvalbumin: SMTDLLSAEDIKKAIGAFTA ADSFDHKKFFQMVGLKKKSA DDVKKVFHILDKDKSGFIEE DELGSILKGFSSDARDLSAK ETKTLMAAGDKDGDGKIGVE EFSTLVAES

Data sets:
Data typeCount
13C chemical shifts438
15N chemical shifts108
1H chemical shifts726

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1subunit 11

Entities:

Entity 1, subunit 1 109 residues - Formula weight is not available

1   SERMETTHRASPLEULEUSERALAGLUASP
2   ILELYSLYSALAILEGLYALAPHETHRALA
3   ALAASPSERPHEASPHISLYSLYSPHEPHE
4   GLNMETVALGLYLEULYSLYSLYSSERALA
5   ASPASPVALLYSLYSVALPHEHISILELEU
6   ASPLYSASPLYSSERGLYPHEILEGLUGLU
7   ASPGLULEUGLYSERILELEULYSGLYPHE
8   SERSERASPALAARGASPLEUSERALALYS
9   GLUTHRLYSTHRLEUMETALAALAGLYASP
10   LYSASPGLYASPGLYLYSILEGLYVALGLU
11   GLUPHESERTHRLEUVALALAGLUSER

Samples:

sample_1: alpha-parvalbumin, [U-100% 15N], 3 ± 0.3 mM; MES 10 ± 0.1 mM; sodium chloride 150 ± 1 mM; EDTA 5 ± .05 mM; sodium azide 0.1 ± 0.001 %; H2O 90%; D2O 10%

sample_2: alpha-parvalbumin, [U-98% 13C; U-98% 15N], 3 ± 0.3 mM; MES 10 ± 0.1 mM; sodium chloride 150 ± 1 mM; EDTA 5 ± .05 mM; sodium azide 0.1 ± 0.001 %; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 170 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

VNMR, Varian - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Varian INOVA 600 MHz

Related Database Links:

PDB
GB AAA41799 AAA41800 AAI26091 EDM15886 EDM15887
REF NP_071944 XP_006241991
SP P02625
AlphaFold P02625

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