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 4448

Title: 1H, 13C and 15N backbone assignment and secondary structure of the 19 kDa diadenosine 5',5'''-P1,P4 tetraphosphate hydrolase from Lupinus angustifolius L.

Deposition date: 1999-11-01 Original release date: 2000-05-09

Authors: Swarbrick, James; Bashtannyk, Tanya; Maksel, Danuta; Gayler, Kenwyn; Pau, Richard; Gooley, Paul

Citation: Swarbrick, James; Bashtannyk, Tanya; Maksel, Danuta; Gayler, Kenwyn; Pau, Richard; Gooley, Paul. "Letter to the Editor: 1H, 13C and 15N backbone assignment and secondary structure of the 19 kDa diadenosine 5', 5'''-P1, P4-tetraphosphate hydrolase from Lupinus angustifolius L"  J. Biomol. NMR 16, 269-270 (2000).

Assembly members:
Ap4a hydrolase, polymer, 165 residues, 18815.2 Da.

Natural source:   Common Name: lupin   Taxonomy ID: 3871   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Lupinus angustifolius

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-6P-3

Entity Sequences (FASTA):
Ap4a hydrolase: GPLGSMDSPPEGYRRNVGIC LMNNDKKIFAASRLDIPDAW QMPQGGIDEGEDPRNAAIRE LREETGVTSAEVIAEVPYWL TYDFPPKVREKLNIQWGSDW KGQAQKWFLFKFTGQDQEIN LLGDGSEKPEFGEWSWVTPE QLIDLTVEFKKPVYKEVLSV FAPHL

Data sets:
Data typeCount
1H chemical shifts1014
13C chemical shifts612
15N chemical shifts162

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Ap4a hydrolase monomer1

Entities:

Entity 1, Ap4a hydrolase monomer 165 residues - 18815.2 Da.

1   GLYPROLEUGLYSERMETASPSERPROPRO
2   GLUGLYTYRARGARGASNVALGLYILECYS
3   LEUMETASNASNASPLYSLYSILEPHEALA
4   ALASERARGLEUASPILEPROASPALATRP
5   GLNMETPROGLNGLYGLYILEASPGLUGLY
6   GLUASPPROARGASNALAALAILEARGGLU
7   LEUARGGLUGLUTHRGLYVALTHRSERALA
8   GLUVALILEALAGLUVALPROTYRTRPLEU
9   THRTYRASPPHEPROPROLYSVALARGGLU
10   LYSLEUASNILEGLNTRPGLYSERASPTRP
11   LYSGLYGLNALAGLNLYSTRPPHELEUPHE
12   LYSPHETHRGLYGLNASPGLNGLUILEASN
13   LEULEUGLYASPGLYSERGLULYSPROGLU
14   PHEGLYGLUTRPSERTRPVALTHRPROGLU
15   GLNLEUILEASPLEUTHRVALGLUPHELYS
16   LYSPROVALTYRLYSGLUVALLEUSERVAL
17   PHEALAPROHISLEU

Samples:

sample_1: Ap4a hydrolase, [U-95% 13C; U-95% 15N], 0.8 mM; Sodium phosphate 45 mM; EDTA 2 mM; DTT 1.5 mM

sample_2: Ap4a hydrolase, [U-95% 15N], 0.8 – 1.2 mM; Sodium phosphate 45 mM; EDTA 2 mM; DTT 1.5 mM

cond_set_1: pH*: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-15N NOESYnot availablenot availablenot available
1H-15N TOCSYnot availablenot availablenot available
HNHanot availablenot availablenot available
HNHbnot availablenot availablenot available
CbCaNHnot availablenot availablenot available
CbCa(CO)NHnot availablenot availablenot available
HNCOnot availablenot availablenot available
(HCa)CO(Ca)HNnot availablenot availablenot available
HCACOnot availablenot availablenot available
C(CO)TOCSYnot availablenot availablenot available
HCCH TOCSYnot availablenot availablenot available
H(CCP)TOCSYnot availablenot availablenot available
(Hb)Cb(CgCd)Hdnot availablenot availablenot available
(Hb)Cb(CgCdCe)Henot availablenot availablenot available
13C-1H NOESYnot availablenot availablenot available

Software:

NMRPipe - Processing

XEASY v1.13 - Analysis

NMR spectrometers:

  • Varian Inova 600 MHz

Related Database Links:

PDB
GB AAC49902

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