BMRB Entry 5054

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5054
MolProbity Validation Chart

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Title:
The Structure of Ap4A Hydrolase Complexed with ATP-MgFx Reveals the Basis of Substrate Binding
Deposition date:
2001-06-13
Original release date:
2002-04-05
Authors:
Fletcher, Jamie; Swarbrick, James; Maksel, Danuta; Gayler, Kenwyn; Gooley, Paul
Citation:

Citation: Fletcher, Jamie; Swarbrick, James; Maksel, Danuta; Gayler, Kenwyn; Gooley, Paul. "The Structure of Ap(4)A Hydrolase Complexed with ATP-MgF(x) Reveals the Basis of Substrate Binding"  Structure 10, 205-213 (2002).
PubMed: 11839306

Assembly members:

Assembly members:
Ap4A hydrolase, polymer, 165 residues, 18815.2 Da.
ADENOSINE-5'-TRIPHOSPHATE, non-polymer, Formula weight is not available

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Ap4A hydrolase: GPLGSMDSPPEGYRRNVGIC LMNNDKKIFAASRLDIPDAW QMPQGGIDEGEDPRNAAIRE LREETGVTSAEVIAEVPYWL TYDFPPKVREKLNIQWGSDW KGQAQKWFLFKFTGQDQEIN LLGDGSEKPEFGEWSWVTPE QLIDLTVEFKKPVYKEVLSV FAPHL

Data sets:
Data typeCount
13C chemical shifts752
1H chemical shifts1208
15N chemical shifts177

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Ap4A hydrolase monomer1
2adenosine triphosphate2

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

Entity 2, adenosine triphosphate 1 residues - C10 H16 N5 O13 P3 - Formula weight is not available

1   ATP

Samples:

sample_1: Ap4A hydrolase, [U-95% 13C; U-95% 15N], 1.6 mM; ADENOSINE-5'-TRIPHOSPHATE 1.6 mM; Imidazole, [U-100% 2H], 20 mM; NaF 32 mM; MgCl2 20 mM; NaN3 0.02%

Ex-cond_1: pH*: 6.5; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
15N-HSQCnot availablenot availablenot available
[13C,1H]-HSQCnot availablenot availablenot available
1H TOCSY-relayed ct-[13C,1H]-COSYnot availablenot availablenot available
CBCANHnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
C(CO)NH-TOCSYnot availablenot availablenot available
H(CCO)NH-TOCSYnot availablenot availablenot available
HNCOnot availablenot availablenot available
HNHBnot availablenot availablenot available
HACACOnot availablenot availablenot available
HACAHBnot availablenot availablenot available
HCCH-COSYnot availablenot availablenot available
15N NOESY-HSQCnot availablenot availablenot available
13C NOESY-HSQCnot availablenot availablenot available
2D doubly-tuned [13C,15N]-filtered TOCSYnot availablenot availablenot available
2D doubly-tuned [13C,15N]-filtered NOESYnot availablenot availablenot available

Software:

NMRPipe v1.1 - spectral processing

XEASY v1.4 - analysis and assignment

NMR spectrometers:

  • Varian Inova 600 MHz

Related Database Links:

BMRB 4448
PDB
GB AAC49902

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