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 18202

Title: Backbone and partial sidechain assignment (13C only) of hNaa50p assignment   PubMed: 22311970

Deposition date: 2012-01-19 Original release date: 2012-05-02

Authors: Brenner, Annette; Lillehaug, Johan; Evjenth, Rune; Froeystein, Nils Aage; Thompson, Paul; Arnesen, Thomas

Citation: Evjenth, Rune; Brenner, Annette; Thompson, Paul; Arnesen, Thomas; Frystein, Nils Age; Lillehaug, Johan. "Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study."  J. Biol. Chem. 287, 10081-10088 (2012).

Assembly members:
hNaa50p, polymer, 173 residues, 19576.8 Da.
ACETYL COENZYME *A, non-polymer, 809.571 Da.

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   Vector: pETM-30

Entity Sequences (FASTA):
hNaa50p: GAMVMKGSRIELGDVTPHNI KQLKRLNQVIFPVSYNDKFY KDVLEVGELAKLAYFNDIAV GAVCCRVDHSQNQKRLYIXT LGCLAPYRRLGIGTKXLNHV LNICEKDGTFDNIYLHVQIS NESAIDFYRKFGFEIIETKK NYYKRIEPADAHVLQKNLKV PSGQNADVQKTDN

Data sets:
Data typeCount
13C chemical shifts544
15N chemical shifts140
1H chemical shifts140

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hNaa50p1
2Acetyl-coenzyme A2

Entities:

Entity 1, hNaa50p 173 residues - 19576.8 Da.

Residues 1-4 are remains from the AcTev cleavage site

1   GLYALAMETVALMETLYSGLYSERARGILE
2   GLULEUGLYASPVALTHRPROHISASNILE
3   LYSGLNLEULYSARGLEUASNGLNVALILE
4   PHEPROVALSERTYRASNASPLYSPHETYR
5   LYSASPVALLEUGLUVALGLYGLULEUALA
6   LYSLEUALATYRPHEASNASPILEALAVAL
7   GLYALAVALCYSCYSARGVALASPHISSER
8   GLNASNGLNLYSARGLEUTYRILEMSETHR
9   LEUGLYCYSLEUALAPROTYRARGARGLEU
10   GLYILEGLYTHRLYSMSELEUASNHISVAL
11   LEUASNILECYSGLULYSASPGLYTHRPHE
12   ASPASNILETYRLEUHISVALGLNILESER
13   ASNGLUSERALAILEASPPHETYRARGLYS
14   PHEGLYPHEGLUILEILEGLUTHRLYSLYS
15   ASNTYRTYRLYSARGILEGLUPROALAASP
16   ALAHISVALLEUGLNLYSASNLEULYSVAL
17   PROSERGLYGLNASNALAASPVALGLNLYS
18   THRASPASN

Entity 2, Acetyl-coenzyme A - C23 H38 N7 O17 P3 S - 809.571 Da.

1   ACO

Samples:

sample_1: hNaa50p, [U-98% 13C; U-98% 15N], 0.2 ± 0.02 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 7.4; pressure: 1 atm; temperature: 310 K

Experiments:

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

Software:

xwinnmr, Keller and Wuthrich - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Varian INOVA 800 MHz

Related Database Links:

PDB
DBJ BAB14397 BAB14490 BAB27439 BAE22602 BAE26378
EMBL CAG30965 CAH89629
GB AAH12731 AAH57117 AAI22618 ABM84090 ABM87460
REF NP_001025949 NP_001069218 NP_001124730 NP_001231736 NP_001248300
SP Q0IIJ0 Q5RF28 Q6PGB6 Q9GZZ1
TPG DAA33506

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