BMRB Entry 11059

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR11059

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Title:
Chemical shift assignment of PACAP27 bound to phospholipid membranes by magic angle spinning solid-state NMR
Deposition date:
2008-11-25
Original release date:
2009-03-18
Authors:
Komi, Nobuyasu; Okawa, Kayo; Tateishi, Yukihiro; Shirakawa, Masahiro; Fujiwara, Toshimichi; Akutsu, Hideo
Citation:

Citation: Komi, Nobuyasu; Okawa, Kayo; Tateishi, Yukihiro; Shirakawa, Masahiro; Fujiwara, Toshimichi; Akutsu, Hideo. "Structural analysis of pituitary adenylate cyclase-activating polypeptides bound to phospholipid membranes by magic angle spinning solid-state NMR."  Biochim. Biophys. Acta 1768, 3001-3011 (2007).
PubMed: 17996724

Assembly members:

Assembly members:
PACAP27, polymer, 28 residues, 3146.4 Da.

Natural source:

Natural source:   Common Name: human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PACAP27: HSDGIFTDSYSRYRKQMAVK KYLAAVLX

Data sets:
Data typeCount
13C chemical shifts131
15N chemical shifts21

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PACAP271

Entities:

Entity 1, PACAP27 28 residues - 3146.4 Da.

1   HISSERASPGLYILEPHETHRASPSERTYR
2   SERARGTYRARGLYSGLNMETALAVALLYS
3   LYSTYRLEUALAALAVALLEUNH2

Samples:

sample_1: PACAP27, [U-13C; U-15N], 4 mg; DMPC, [U-98% 2H], 25.4 uM

sample_conditions_233K: pressure: 1 atm; temperature: 233 K

sample_conditions_273K: pressure: 1 atm; temperature: 273 K

sample_conditions_213K: pressure: 1 atm; temperature: 213 K

Experiments:

NameSampleSample stateSample conditions
2D 13C-13C DARRsample_1isotropicsample_conditions_233K
2D 13C-13C RFDRsample_1isotropicsample_conditions_233K
2D 13C-13C SPC-5sample_1isotropicsample_conditions_273K
2D 15N-13Csample_1isotropicsample_conditions_273K
2D 15N-13C RFDRsample_1isotropicsample_conditions_273K
2D CA-CA DARRsample_1isotropicsample_conditions_213K

Software:

FELIX v2002, Accelrys Software Inc. - processing

NMR spectrometers:

  • Varian Infinity-plus 500 MHz
  • Varian Infinity-plus 600 MHz
  • Varian Infinity-plus 700 MHz

Related Database Links:

BMRB 11058
PDB
DBJ BAA28355 BAC21153 BAC21154 BAC21155 BAC21156
EMBL CAA42962 CAA51705 CAA55684 CAA56564 CAG10213
GB AAA31575 AAA41791 AAB20402 AAB21469 AAB21470
PRF 2107317A
REF NP_001001544 NP_001009776 NP_001040020 NP_001081947 NP_001093203
SP O70176 P0DJ95 P13589 P16613 P18509
TPG DAA15829
AlphaFold O70176 P0DJ95 P13589 P16613 P18509