BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15166

Title: Pac1-Rshort N-terminal EC domain Pacap(6-38) complex   PubMed: 17470806

Deposition date: 2007-03-08 Original release date: 2008-02-07

Authors: Olejniczak, Edward; 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

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).

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

Entity Sequences (FASTA):
pac1-R_N-terminal_EC_domain: MGSMAHSDGIFKKEQAMCLE KIQRANELMGFNDSSPGCPG MWDNITCWKPAHVGEMVLVS CPELFRIFNPDQDMGVVSRN CTEDGWSEPFPHYFDACGFD EYESET
PACAP_(6-38): FTDSYSRYRKQMAVKKYLAA VLGKRYKQRVKNK

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts83
1H chemical shifts512

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1pac1r Nterm ec1
2pacap(6-38)2

Entities:

Entity 1, pac1r Nterm ec 106 residues - 16015.379 Da.

1   METGLYSERMETALAHISSERASPGLYILE
2   PHELYSLYSGLUGLNALAMETCYSLEUGLU
3   LYSILEGLNARGALAASNGLULEUMETGLY
4   PHEASNASPSERSERPROGLYCYSPROGLY
5   METTRPASPASNILETHRCYSTRPLYSPRO
6   ALAHISVALGLYGLUMETVALLEUVALSER
7   CYSPROGLULEUPHEARGILEPHEASNPRO
8   ASPGLNASPMETGLYVALVALSERARGASN
9   CYSTHRGLUASPGLYTRPSERGLUPROPHE
10   PROHISTYRPHEASPALACYSGLYPHEASP
11   GLUTYRGLUSERGLUTHR

Entity 2, pacap(6-38) 32 residues - 4036.852 Da.

1   PHETHRASPSERTYRSERARGTYRARGLYS
2   GLNMETALAVALLYSLYSTYRLEUALAALA
3   VALLEUGLYLYSARGTYRLYSGLNARGVAL
4   LYSASNLYS

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:

NameSampleSample stateSample conditions
3D 1H-13C NOESYsample_1isotropicsample_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

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts