BMRB Entry 15166
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15166
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Sun, Chaohong; Song, Danying; Davis-taber, Rachel; Barrett, Leo; Scott, Victoria; Richardson, Paul; Pereda-lopez, Ana; Uchic, Marie; Solomon, Larry; Lake, Marc; Walter, Karl; Hajduk, Philip; Olejniczak, Edward. "Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS" Proc. Natl. Acad. Sci. U.S.A. 104, 7875-7880 (2007).
PubMed: 17470806
Assembly members:
pac1-R_N-terminal_EC_domain, polymer, 106 residues, 16015.379 Da.
PACAP_(6-38), polymer, 32 residues, 4036.852 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: not applicable
Entity Sequences (FASTA):
pac1-R_N-terminal_EC_domain: MGSMAHSDGIFKKEQAMCLE
KIQRANELMGFNDSSPGCPG
MWDNITCWKPAHVGEMVLVS
CPELFRIFNPDQDMGVVSRN
CTEDGWSEPFPHYFDACGFD
EYESET
PACAP_(6-38): FTDSYSRYRKQMAVKKYLAA
VLGKRYKQRVKNK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 380 |
| 15N chemical shifts | 83 |
| 1H chemical shifts | 512 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | pac1r Nterm ec | 1 |
| 2 | pacap(6-38) | 2 |
Entities:
Entity 1, pac1r Nterm ec 106 residues - 16015.379 Da.
| 1 | MET | GLY | SER | MET | ALA | HIS | SER | ASP | GLY | ILE | ||||
| 2 | PHE | LYS | LYS | GLU | GLN | ALA | MET | CYS | LEU | GLU | ||||
| 3 | LYS | ILE | GLN | ARG | ALA | ASN | GLU | LEU | MET | GLY | ||||
| 4 | PHE | ASN | ASP | SER | SER | PRO | GLY | CYS | PRO | GLY | ||||
| 5 | MET | TRP | ASP | ASN | ILE | THR | CYS | TRP | LYS | PRO | ||||
| 6 | ALA | HIS | VAL | GLY | GLU | MET | VAL | LEU | VAL | SER | ||||
| 7 | CYS | PRO | GLU | LEU | PHE | ARG | ILE | PHE | ASN | PRO | ||||
| 8 | ASP | GLN | ASP | MET | GLY | VAL | VAL | SER | ARG | ASN | ||||
| 9 | CYS | THR | GLU | ASP | GLY | TRP | SER | GLU | PRO | PHE | ||||
| 10 | PRO | HIS | TYR | PHE | ASP | ALA | CYS | GLY | PHE | ASP | ||||
| 11 | GLU | TYR | GLU | SER | GLU | THR |
Entity 2, pacap(6-38) 32 residues - 4036.852 Da.
| 1 | PHE | THR | ASP | SER | TYR | SER | ARG | TYR | ARG | LYS | ||||
| 2 | GLN | MET | ALA | VAL | LYS | LYS | TYR | LEU | ALA | ALA | ||||
| 3 | VAL | LEU | GLY | LYS | ARG | TYR | LYS | GLN | ARG | VAL | ||||
| 4 | LYS | ASN | LYS |
Samples:
sample_1: pac1-R N-terminal EC domain, [U-100% 13C; U-100% 15N], 0.5 – 1 mM; PACAP (6-38)0.5 – 1 mM
sample_conditions_1: ionic strength: 100 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker DRX 800 MHz
Related Database Links:
| PDB | |
| REF | NP_001186566 XP_001166687 XP_003833436 XP_004045318 XP_007979874 NP_001001291 NP_001001544 NP_001009776 NP_001040020 NP_001081947 |
| BMRB | 11059 |
| DBJ | BAA28355 BAC37673 BAE22234 BAG35881 BAH11708 |
| EMBL | CAA42962 CAA56564 CAG29646 CDQ56897 CDQ74600 |
| GB | AAA31575 AAA41791 AAB20402 AAB21469 AAB21470 |
| SP | O70176 P0DJ95 P13589 P16613 P18509 |
| TPG | DAA15829 |
| AlphaFold | O70176 P0DJ95 P13589 P16613 P18509 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks