BMRB Entry 51827

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for FASP peptide of hPER2
Published: 2023-02-13

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51827

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for FASP peptide of hPER2

Deposition date:

2023-02-08

Original release date:

2023-02-13

Authors:

Philpott, Jonathan; Hunt, Sabrina; Partch, Carrie

Citation:

Citation: Philpott, Jonathan; Freeberg, Alfred; Park, Jiyoung; Lee, Kwangiun; Ricci, Clarisse; Hunt, Sabrina; Narasimamurthy, Rajesh; Segal, David; Robles, Rafael; Cai, Yao; Tripathi, Sarvind; McCammon, J. Andrew; Virshup, David; Chiu, Joanna; Lee, Choogon; Partch, Carrie. "PERIOD phosphorylation leads to feedback inhibition of CK1 activity to control circadian period" Mol. Cell 83, 1677-1692 (2023).
PubMed: 37207626

Assembly members:

Assembly members:
entity_1, polymer, 55 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMDPEFWRKKKTGVGTHLT SLALPGKAESVASLTSQCSY SSTIVHVGDKKPQPE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	150
15N chemical shifts	48
1H chemical shifts	48

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hPER2 FASP	1

Entities:

Entity 1, hPER2 FASP 55 residues - Formula weight is not available

Residues 1-12 represent non-native sequence. Residues 13-55 correspond to hPER2 residues 645-687.

1

GLY

ALA

MET

ASP

PRO

GLU

PHE

TRP

ARG

LYS

2

LYS

THR

GLY

VAL

GLY

THR

HIS

LEU

THR

3

SER

LEU

ALA

LEU

PRO

GLY

LYS

ALA

GLU

SER

4

VAL

ALA

SER

LEU

THR

SER

GLN

CYS

SER

TYR

5

SER

THR

ILE

VAL

HIS

VAL

GLY

ASP

LYS

6

LYS

PRO

GLN

PRO

GLU

Samples:

sample_1: hPER2 FASP, [U-13C; U-15N], 0.5 mM; MES 25 mM; sodium chloride 50 mM; TCEP 2 mM; EDTA 1 mM; Pierce protease inhibitor tablet 1 tablet/50mL; ATP 2.5 mM; D2O, [U-2H], 10%

sample_conditions_1: pH: 7.0; pressure: 1 atm; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe - processing

NMRDraw - processing

CcpNMR_Analysis - chemical shift assignment, data analysis, peak picking

hmsIST - data reconstruction

NMR spectrometers:

Varian INOVA 600 MHz

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