BMRB Entry 5054
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5054
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Title: The Structure of Ap4A Hydrolase Complexed with ATP-MgFx Reveals the Basis of Substrate Binding PubMed: 11839306
Deposition date: 2001-06-13 Original release date: 2002-04-05
Authors: Fletcher, Jamie; Swarbrick, James; Maksel, Danuta; Gayler, Kenwyn; Gooley, Paul
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).
Assembly members:
Ap4A hydrolase, polymer, 165 residues, 18815.2 Da.
ADENOSINE-5'-TRIPHOSPHATE, non-polymer, Formula weight is not available
Natural source: Common Name: narrow leafed lupin Taxonomy ID: 3871 Superkingdom: Eukaryota Kingdom: Viridiplantae Genus/species: Lupinus angustifolius
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Ap4A hydrolase: GPLGSMDSPPEGYRRNVGIC
LMNNDKKIFAASRLDIPDAW
QMPQGGIDEGEDPRNAAIRE
LREETGVTSAEVIAEVPYWL
TYDFPPKVREKLNIQWGSDW
KGQAQKWFLFKFTGQDQEIN
LLGDGSEKPEFGEWSWVTPE
QLIDLTVEFKKPVYKEVLSV
FAPHL
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 752 |
| 1H chemical shifts | 1208 |
| 15N chemical shifts | 177 |
Additional metadata:
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