BMRB Entry 6354
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6354
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 and 15N-1H residual dipolar couplings for NECAP1 protein PubMed: 17762867
Deposition date: 2004-10-13 Original release date: 2008-07-01
Authors: Denisov, Alexei; Gehring, Kalle
Citation: Ritter, Brigitte; Denisov, Alexey; Philie, Jacynthe; Allaire, Patrick; Legendre-Guillemin, Valerie; Zylbergold, Peter; Gehring, Kalle; McPherson, Peter. "Solution structure of NECAP1 protein" EMBO J. 26, 4066-4077 (2007).
Assembly members:
NECAP1 protein, polymer, 133 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
NECAP1 protein: MAAELEYESVLCVKPDVSVY
RIPPRASNRGYRASDWKLDQ
PDWTGRLRITSKGKIAYIKL
EDKVSGELFAQAPVEQYPGI
AVETVTDSSRYFVIRIQDGT
GRSAFIGIGFTDRGDAFDFN
VSLQDHFKWVKQE
- assigned_chemical_shifts
- RDCs
| Data type | Count |
| 1H chemical shifts | 645 |
| 13C chemical shifts | 498 |
| 15N chemical shifts | 124 |
| residual dipolar couplings | 121 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | NECAP1 monomer | 1 |
Entities:
Entity 1, NECAP1 monomer 133 residues - Formula weight is not available
| 1 | MET | ALA | ALA | GLU | LEU | GLU | TYR | GLU | SER | VAL | ||||
| 2 | LEU | CYS | VAL | LYS | PRO | ASP | VAL | SER | VAL | TYR | ||||
| 3 | ARG | ILE | PRO | PRO | ARG | ALA | SER | ASN | ARG | GLY | ||||
| 4 | TYR | ARG | ALA | SER | ASP | TRP | LYS | LEU | ASP | GLN | ||||
| 5 | PRO | ASP | TRP | THR | GLY | ARG | LEU | ARG | ILE | THR | ||||
| 6 | SER | LYS | GLY | LYS | ILE | ALA | TYR | ILE | LYS | LEU | ||||
| 7 | GLU | ASP | LYS | VAL | SER | GLY | GLU | LEU | PHE | ALA | ||||
| 8 | GLN | ALA | PRO | VAL | GLU | GLN | TYR | PRO | GLY | ILE | ||||
| 9 | ALA | VAL | GLU | THR | VAL | THR | ASP | SER | SER | ARG | ||||
| 10 | TYR | PHE | VAL | ILE | ARG | ILE | GLN | ASP | GLY | THR | ||||
| 11 | GLY | ARG | SER | ALA | PHE | ILE | GLY | ILE | GLY | PHE | ||||
| 12 | THR | ASP | ARG | GLY | ASP | ALA | PHE | ASP | PHE | ASN | ||||
| 13 | VAL | SER | LEU | GLN | ASP | HIS | PHE | LYS | TRP | VAL | ||||
| 14 | LYS | GLN | GLU |
Samples:
sample_1: NECAP1 protein, [U-99% 13C; U-99% 15N], 1.4 mM; sodium phosphate buffer 25 mM; NaCl 75 mM
sample_2: NECAP1 protein, [U-99% 15N], 1.4 mM; sodium phosphate buffer 25 mM; NaCl 75 mM
sample_3: NECAP1 protein, [U-99% 15N], 0.6 mM; sodium phosphate buffer 25 mM; NaCl 75 mM; Pf1 phage 8.0 mg/mL
Ex-cond_1: pH: 7.2; temperature: 303 K; ionic strength: 0.10 M
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| IPAP-HSQC | not available | not available | Ex-cond_1 |
Software:
XWINNMR v3.5 - collection, processing
XEASY v1.3.13 - data analysis
NMR spectrometers:
- Bruker DRX 600 MHz
Related Database Links:
| tpg|DAA01433.1| | DAA01433 |
| SWISS-PROT | Q9CR95 Q8NC96 Q5R630 P69682 |
| REF | XP_001113344 XP_001113313 NP_080543 NP_056324 NP_001025090 |
| GenBank | AAI20842 AAI19134 AAI10877 AAH97496 AAH11466 |
| EMBL | CAH92786 CAH92713 |
| DBJ | BAC11296 BAC11264 BAC11250 BAB23915 BAB23577 |
| PDB |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts