BMRB Entry 5031
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5031
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: Sequence-specific 1H, 13C and 15N resonance assignments of the N-terminal, 135-residue domain of KaiA, a clock protein from Synechococcus elongatus
Deposition date: 2001-05-24 Original release date: 2003-01-13
Authors: Vakonakis, Ioannis; Risinger, Aaron; Latham, Michael; Williams, Stanly; Golden, Susan; LiWang, Andy
Citation: Vakonakis, Ioannis; Risinger, Aaron; Latham, Michael; Williams, Stanly; Golden, Susan; LiWang, Andy. "Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the N-terminal, 135-residue domain of KaiA, a clock protein from Synechococcus elongatus" J. Biomol. NMR 21, 179-180 (2001).
Assembly members:
KaiA, polymer, 135 residues, 15066 Da.
Natural source: Common Name: Synechococcus elongatus Taxonomy ID: 32046 Superkingdom: Eubacteria Kingdom: not available Genus/species: Synechococcus elongatus
Experimental source: Production method: recombinant technology Host organism: coli
Entity Sequences (FASTA):
KaiA: MLSQIAICIWVESTAILQDC
QRALSADRYQLQVCESGEML
LEYAQTHRDQIDCLILVAAN
PSFRAVVQQLCFEGVVVPAI
VVGDRDSEDPDEPAKEQLYH
SAELHLGIHQLEQLPYQVDA
ALAEFLRLAPVETMA
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 959 |
| 13C chemical shifts | 596 |
| 15N chemical shifts | 147 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | KaiA N-terminus | 1 |
Entities:
Entity 1, KaiA N-terminus 135 residues - 15066 Da.
| 1 | MET | LEU | SER | GLN | ILE | ALA | ILE | CYS | ILE | TRP | ||||
| 2 | VAL | GLU | SER | THR | ALA | ILE | LEU | GLN | ASP | CYS | ||||
| 3 | GLN | ARG | ALA | LEU | SER | ALA | ASP | ARG | TYR | GLN | ||||
| 4 | LEU | GLN | VAL | CYS | GLU | SER | GLY | GLU | MET | LEU | ||||
| 5 | LEU | GLU | TYR | ALA | GLN | THR | HIS | ARG | ASP | GLN | ||||
| 6 | ILE | ASP | CYS | LEU | ILE | LEU | VAL | ALA | ALA | ASN | ||||
| 7 | PRO | SER | PHE | ARG | ALA | VAL | VAL | GLN | GLN | LEU | ||||
| 8 | CYS | PHE | GLU | GLY | VAL | VAL | VAL | PRO | ALA | ILE | ||||
| 9 | VAL | VAL | GLY | ASP | ARG | ASP | SER | GLU | ASP | PRO | ||||
| 10 | ASP | GLU | PRO | ALA | LYS | GLU | GLN | LEU | TYR | HIS | ||||
| 11 | SER | ALA | GLU | LEU | HIS | LEU | GLY | ILE | HIS | GLN | ||||
| 12 | LEU | GLU | GLN | LEU | PRO | TYR | GLN | VAL | ASP | ALA | ||||
| 13 | ALA | LEU | ALA | GLU | PHE | LEU | ARG | LEU | ALA | PRO | ||||
| 14 | VAL | GLU | THR | MET | ALA |
Samples:
sample_KaiA-135: KaiA, [U-99% 13C; U-99% 15N], 2.9 – 3.4 mM
Ex-cond_1: pH: 6.4; temperature: 298 K; ionic strength: 0.22 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 15N HSQC | not available | not available | not available |
| HNHA | not available | not available | not available |
| CBCA(CO)NH | not available | not available | not available |
| CBCANH | not available | not available | not available |
| C(CO)NH | not available | not available | not available |
| H(CCO)NH | not available | not available | not available |
| HBHACONH | not available | not available | not available |
| HCCH-COSY | not available | not available | not available |
Software:
NMRPipe v1.8 rev 2001.030.21.27 - NMR data processing
PIPP v4.2.6 - Spectra visualization
STAPP v4.2.6 - Spin system creation, partial sequence specific assignments
NMR spectrometers:
- Varian Inova 600 MHz
Related Database Links:
| PDB | |
| DBJ | BAA37101 BAD78522 |
| GB | AAM82684 ABB57248 AJD58238 |
| REF | WP_011242646 WP_011377921 YP_171042 YP_400235 |
| SP | Q79PF6 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts