BMRB Entry 27988

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for C-terminal tail of human CRY1
Published: 2020-10-15

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27988

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for C-terminal tail of human CRY1

Deposition date:

2019-07-24

Original release date:

2020-10-15

Authors:

Lee, Hsiau-Wei; Parico, Gian Carlo; Partch, Carrie

Citation:

Citation: Parico, Gian Carlo; Perez, Ivette; Fribourgh, Jennifer; Hernandez, Britney; Lee, Hsiau-Wei; Partch, Carrie. "The CRY1 tail controls circadian timing by regulating its association with CLOCK:BMAL1" Proc. Natl. Acad. Sci. U. S. A. 117, 27971-27979 (2020).
PubMed: 33106415

Assembly members:

Assembly members:
CRY1, polymer, 98 residues, Formula weight is not available

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: pET22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CRY1: gamdpefGLGLLASVPSNPN GNGGFMGYSAENIPGCSSSG SCSQGSGILHYAHGDSQQTH LLKQGRSSMGTGLSGGKRPS QEEDTQSIGPKVQRQSTN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts

Data type	Count
13C chemical shifts	260
15N chemical shifts	96
1H chemical shifts	87

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CRY1	1

Entities:

Entity 1, CRY1 98 residues - Formula weight is not available

1

GLY

ALA

MET

ASP

PRO

GLU

PHE

GLY

LEU

GLY

2

LEU

ALA

SER

VAL

PRO

SER

ASN

PRO

ASN

3

GLY

ASN

GLY

PHE

MET

GLY

TYR

SER

ALA

4

GLU

ASN

ILE

PRO

GLY

CYS

SER

GLY

5

SER

CYS

SER

GLN

GLY

SER

GLY

ILE

LEU

HIS

6

TYR

ALA

HIS

GLY

ASP

SER

GLN

THR

HIS

7

LEU

LYS

GLN

GLY

ARG

SER

MET

GLY

8

THR

GLY

LEU

SER

GLY

LYS

ARG

PRO

SER

9

GLN

GLU

ASP

THR

GLN

SER

ILE

GLY

PRO

10

LYS

VAL

GLN

ARG

GLN

SER

THR

ASN

Samples:

sample_1: CRY1, [U-100% 13C; U-100% 15N], 120 uM; MES 20 mM; sodium chloride 100 mM; EDTA 1 mM; TCEP 4 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

SPARKY, Goddard - chemical shift assignment

CccpNMR v2.4.2, CCPN - chemical shift assignment, data analysis

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

NMR spectrometers:

Bruker Avance 800 MHz
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