BMRB Entry 6053
Click here to enlarge.
PDB ID: 1adn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6053
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H, 13C and 15N resonance assignments of the N-terminal 16kDa domain of Escherichia coli Ada Protein PubMed: 15213462
Deposition date: 2003-12-18 Original release date: 2004-07-06
Authors: Takinowaki, Hiroto; Matsuda, Yasuhiro; Yoshida, Takuya; Kobayashi, Yuji; Ohkubo, Tadayasu
Citation: Takinowaki, Hiroto; Matsuda, Yasuhiro; Yoshida, Takuya; Kobayashi, Yuji; Ohkubo, Tadayasu. "Letter to the Editer: 1H, 13C and 15N resonance assignments of the N-terminal 16 kDa domain of Escherichia coli Ada Protein " J. Biomol. NMR 29, 447-448 (2004).
Assembly members:
Escherichia coli Ada Protein, polymer, 146 residues, Formula weight is not available
ZN, non-polymer, 65.409 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Escherichia coli Ada Protein: MKKATCLTDDQRWQSVLARD
PNADGEFVFAVRTTGIFCRP
SCRARHALRENVSFYANASE
ALAAGFRPCKRCQPEKANAQ
QHRLDKITHACRLLEQETPV
TLEALADQVAMSPFHLHRLF
KATTGMTPKAWQQAWRARRL
RESLAK
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 948 |
| 13C chemical shifts | 586 |
| 15N chemical shifts | 145 |
Additional metadata:
Related Database Links:
| SWISS-PROT | P06134 |
| REF | YP_001724427 NP_416717 NP_311129 NP_288793 AP_002809 |
| GenBank | ACA77100 AAG57348 AAC75273 AAA23412 AAA16408 |
| DBJ | BAB36525 BAA15996 |
| PDB | 1WPK |
| BMRB | 6054 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts