BMRB Entry 15563

Name: Backbone 1H, 13C and 15N chemical shift assignment of N-terminal end (1-85) of human SRC
Published: 2009-06-29

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15563

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 assignment of N-terminal end (1-85) of human SRC

Deposition date:

2007-11-26

Original release date:

2009-06-29

Authors:

Perez, Yolanda; Bernad, Pau; Gair, Margarida; Pons, Miquel

Citation:

Citation: Perez, Yolanda; Gairi, Margarida; Pons, Miquel; Bernado, Pau. "Structural Characterization of the Natively Unfolded N-Terminal Domain of Human c-Src Kinase: Insights into the Role of Phosphorylation of the Unique Domain." J. Mol. Biol. 391, 136-148 (2009).
PubMed: 19520085

Assembly members:

Assembly members:
USRC, polymer, 95 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pet14a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
USRC: MASNKSKPKDASQRRRSLEP AENVHGAGGGAFPASQTPSK PASADGHRGPSAAFAPAAAE PKLFGGFNSSDTVTSPQRAG PLAGGSAWSHPQFEK

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	266
15N chemical shifts	91
1H chemical shifts	80

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	USRC	1

Entities:

Entity 1, USRC 95 residues - Formula weight is not available

1

MET

ALA

SER

ASN

LYS

SER

LYS

PRO

LYS

ASP

2

ALA

SER

GLN

ARG

SER

LEU

GLU

PRO

3

ALA

GLU

ASN

VAL

HIS

GLY

ALA

GLY

4

ALA

PHE

PRO

ALA

SER

GLN

THR

PRO

SER

LYS

5

PRO

ALA

SER

ALA

ASP

GLY

HIS

ARG

GLY

PRO

6

SER

ALA

PHE

ALA

PRO

ALA

GLU

7

PRO

LYS

LEU

PHE

GLY

PHE

ASN

SER

8

ASP

THR

VAL

THR

SER

PRO

GLN

ARG

ALA

GLY

9

PRO

LEU

ALA

GLY

SER

ALA

TRP

SER

HIS

10

PRO

GLN

PHE

GLU

LYS

Samples:

sample_1: USRC, [U-100% 13C; U-100% 15N], 0.6 mM; PMSF 0.2 mM; sodium acetate 50 mM; D2O, [U-99% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 4.5; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D COCON	sample_1	isotropic	sample_conditions_1
2D CON	sample_1	isotropic	sample_conditions_1
3D CBCACON	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v1.3, Bruker Biospin, Goddard - chemical shift assignment, collection, peak picking, processing

NMR spectrometers:

Bruker Avance 800 MHz
Bruker Avance 700 MHz

PDB	2H8H
DBJ	BAI47379
GB	AAA60584 AAH11566 AAH51270 AAX29840 ACE86438
REF	NP_001248263 NP_005408 NP_938033 XP_004062179 XP_005569018
SP	P12931
AlphaFold	P12931