BMRB Entry 16935

Title:
Solution structure of the PECAM-1 cytoplasmic tail with DPC
Deposition date:
2010-05-14
Original release date:
2011-04-12
Authors:
Lytle, B.; Peterson, F.; Volkman, B.; Paddock, C.; Newman, D.
Citation:

Citation: Paddock, Cathy; Lytle, Betsy; Peterson, Francis; Holyst, Trudy; Newman, Peter; Volkman, Brian; Newman, Debra. "Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation."  Blood 117, 6012-6023 (2011).
PubMed: 21464369

Assembly members:

Assembly members:
PECAM-1, polymer, 55 residues, 5988.425 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: pQE30T

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts186
15N chemical shifts47
1H chemical shifts246

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PECAM-11

Entities:

Entity 1, PECAM-1 55 residues - 5988.425 Da.

The N-terminal GS dipeptide is a cloning artifact.

1   GLYSERSERASPVALGLNTYRTHRGLUVAL
2   GLNVALSERSERALAGLUSERHISLYSASP
3   LEUGLYLYSLYSASPTHRGLUTHRVALTYR
4   SERGLUVALARGLYSALAVALPROASPALA
5   VALGLUSERARGTYRSERARGTHRGLUGLY
6   SERLEUASPGLYTHR

Samples:

sample_1: PECAM-1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 20 mM; sodium chloride 50 mM; DTT 2 mM; DPC, [U-100% 2H], 600 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 52 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESY (AROMATIC)sample_1isotropicsample_conditions_1

Software:

X-PLOR NIH v2.9.3, SCHWIETERS,C.D.,KUSZEWSKI,J.J.,TJANDRA,N.,CLORE,G.M. - refinement

TOPSPIN v2.1, Bruker - collection

NMRPipe v2009, Delagio,F. et al. - processing

XEASY v1.3, Eccles, C., Guntert, P., Billeter, M., Wuthrich, K. - data analysis

GARANT v2.1, C. Bartels - data analysis

CYANA v2.1, Guntert, P. - structural calculation

NMR spectrometers:

  • Bruker Avance III 500 MHz

Related Database Links:

PDB
DBJ BAF83381 BAH14084 BAH14122 BAJ20571
GB AAA36186 AAA36429 AAA60057 AAF91446 AAF91447
REF NP_000433 XP_003262683 XP_003811413 XP_004041267 XP_005276939
SP P16284
AlphaFold P16284

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks