BMRB Entry 18204

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18204

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Title:
Backbone 1H, 13C, and 15N Chemical Shift Assignments for human PEBP1
Deposition date:
2012-01-20
Original release date:
2012-03-02
Authors:
Karsisiotis, Andreas; Tavel, Laurette; Damblon, Christian
Citation:

Citation: Tavel, Laurette; Jaquillard, Lucie; Karsisiotis, Andreas; Saab, Fabienne; Jouvensal, Laurence; Brans, Alain; Delmas, Agnes; Schoentgen, Francoise; Cadene, Martine; Damblon, Christian. "Ligand binding study of human PEBP1/RKIP: interaction with nucleotides and Raf-1 peptides evidenced by NMR and mass spectrometry."  PLoS ONE 7, .-. (2012).
PubMed: 22558375

Assembly members:

Assembly members:
hPEBP1, polymer, 187 residues, 20924 Da.

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET31B

Entity Sequences (FASTA):

Entity Sequences (FASTA):
hPEBP1: MPVDLSKWSGPLSLQEVDEQ PQHPLHVTYAGAAVDELGKV LTPTQVKNRPTSISWDGLDS GKLYTLVLTDPDAPSRKDPK YREWHHFLVVNMKGNDISSG TVLSDYVGSGPPKGTGLHRY VWLVYEQDRPLKCDEPILSN RSGDHRGKFKVASFRKKYEL RAPVAGTCYQAEWDDYVPKL YEQLSGK

Data sets:
Data typeCount
13C chemical shifts531
15N chemical shifts167
1H chemical shifts167

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hPEBP11

Entities:

Entity 1, hPEBP1 187 residues - 20924 Da.

1   METPROVALASPLEUSERLYSTRPSERGLY
2   PROLEUSERLEUGLNGLUVALASPGLUGLN
3   PROGLNHISPROLEUHISVALTHRTYRALA
4   GLYALAALAVALASPGLULEUGLYLYSVAL
5   LEUTHRPROTHRGLNVALLYSASNARGPRO
6   THRSERILESERTRPASPGLYLEUASPSER
7   GLYLYSLEUTYRTHRLEUVALLEUTHRASP
8   PROASPALAPROSERARGLYSASPPROLYS
9   TYRARGGLUTRPHISHISPHELEUVALVAL
10   ASNMETLYSGLYASNASPILESERSERGLY
11   THRVALLEUSERASPTYRVALGLYSERGLY
12   PROPROLYSGLYTHRGLYLEUHISARGTYR
13   VALTRPLEUVALTYRGLUGLNASPARGPRO
14   LEULYSCYSASPGLUPROILELEUSERASN
15   ARGSERGLYASPHISARGGLYLYSPHELYS
16   VALALASERPHEARGLYSLYSTYRGLULEU
17   ARGALAPROVALALAGLYTHRCYSTYRGLN
18   ALAGLUTRPASPASPTYRVALPROLYSLEU
19   TYRGLUGLNLEUSERGLYLYS

Samples:

sample_1: hPEBP1, [U-100% 13C; U-100% 15N], 0.5 ± 0.1 mM; H2O 90%; D2O 10%; MES 10 mM

sample_conditions_1: ionic strength: 0.01 M; pH: 6.5; 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 HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

BMRB 16992 17382
PDB
DBJ BAA03684 BAE88027 BAE88359 BAG34868 BAG61396
EMBL CAA51652 CAA53031 CAA59404 CAH93256
GB AAB32876 AAD14234 AAH08714 AAH17396 AAH31102
PRF 2117380B
REF NP_001126915 NP_001233128 NP_002558 XP_002753109 XP_004054017
SP P30086 P48737 Q5R4R0
AlphaFold P30086 P48737 Q5R4R0

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