BMRB Entry 16935

Name: Solution structure of the PECAM-1 cytoplasmic tail with DPC
Published: 2011-04-12

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PDB ID: 2ky5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16935
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
PECAM-1: GSSDVQYTEVQVSSAESHKD LGKKDTETVYSEVRKAVPDA VESRYSRTEGSLDGT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	186
15N chemical shifts	47
1H chemical shifts	246

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PECAM-1	1

Entities:

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

The N-terminal GS dipeptide is a cloning artifact.

1

GLY

SER

ASP

VAL

GLN

TYR

THR

GLU

VAL

2

GLN

VAL

SER

ALA

GLU

SER

HIS

LYS

ASP

3

LEU

GLY

LYS

ASP

THR

GLU

THR

VAL

TYR

4

SER

GLU

VAL

ARG

LYS

ALA

VAL

PRO

ASP

ALA

5

VAL

GLU

SER

ARG

TYR

SER

ARG

THR

GLU

GLY

6

SER

LEU

ASP

GLY

THR

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:

Name	Sample	Sample state	Sample conditions
3D_15N-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY	sample_1	isotropic	sample_conditions_1
3D_13C-separated_NOESY (AROMATIC)	sample_1	isotropic	sample_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

PDB	2KY5
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