BMRB Entry 5314

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5314

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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:

Assignment of 1H, 13C, and 15N Resonances of the SH2 Domain of Human Grb14 and Chemical Shift Changes upon Binding a phosphorylated decapeptide

Deposition date:

2002-03-08

Original release date:

2002-12-23

Authors:

Scharf, Paul; Lyons, Barbara

Citation:

Citation: Scharf, Paul; Lyons, Barbara. "Letter to the editor: Assignment of backbone 1H, 13C, and 15N Resonances of the SH2 Domain of Human Grb14" J. Biomol. NMR 24, 275-276 (2002).

Assembly members:

Assembly members:
Grb14, polymer, 117 residues, Formula weight is not available
pY-766, polymer, 11 residues, 1356 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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Grb14: GSSSATNMAIHRSQPWFHHK ISRDEAQRLIIQQGLVDGVF LVRDSQSNPKTFVLSMSHGQ KIKHFQIIPVEDDGEMFHTL DDGHTRFTDLIQLVEFYQLN KGVLPCKLKHYCARIAL
pY-766: TSNQEXLDLSM

Data sets:

assigned_chemical_shifts
- Shift_set_1

Data type	Count
1H chemical shifts	726
13C chemical shifts	232
15N chemical shifts	112

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Grb14 SH2 domain	1
2	phosphorylated peptide	2

Entities:

Entity 1, Grb14 SH2 domain 117 residues - Formula weight is not available

1

GLY

SER

ALA

THR

ASN

MET

ALA

ILE

2

HIS

ARG

SER

GLN

PRO

TRP

PHE

HIS

LYS

3

ILE

SER

ARG

ASP

GLU

ALA

GLN

ARG

LEU

ILE

4

ILE

GLN

GLY

LEU

VAL

ASP

GLY

VAL

PHE

5

LEU

VAL

ARG

ASP

SER

GLN

SER

ASN

PRO

LYS

6

THR

PHE

VAL

LEU

SER

MET

SER

HIS

GLY

GLN

7

LYS

ILE

LYS

HIS

PHE

GLN

ILE

PRO

VAL

8

GLU

ASP

GLY

GLU

MET

PHE

HIS

THR

LEU

9

ASP

GLY

HIS

THR

ARG

PHE

THR

ASP

LEU

10

ILE

GLN

LEU

VAL

GLU

PHE

TYR

GLN

LEU

ASN

11

LYS

GLY

VAL

LEU

PRO

CYS

LYS

LEU

LYS

HIS

12

TYR

CYS

ALA

ARG

ILE

ALA

LEU

Entity 2, phosphorylated peptide 11 residues - 1356 Da.

1

THR

SER

ASN

GLN

GLU

PTR

LEU

ASP

LEU

SER

2

MET

Samples:

Sample_1: Grb14, [U-98% 13C; U-98% 15N], 0.8 mM; pY-766 0.8 mM; sodium acetate 50 mM; NaCl 100 mM

Experimental_Conditions_I: pH: 5.5; temperature: 298 K; ionic strength: 0.15 M

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCA	Sample_1	not available	Experimental_Conditions_I
3D HN(CO)CA	Sample_1	not available	Experimental_Conditions_I
3D CBCA(CO)NH	Sample_1	not available	Experimental_Conditions_I
3D CBCANH	Sample_1	not available	Experimental_Conditions_I
3D C(CO)NH	Sample_1	not available	Experimental_Conditions_I
N HSQC TOCSY	Sample_1	not available	Experimental_Conditions_I
N HSQC NOESY	Sample_1	not available	Experimental_Conditions_I

Software:

ANSIG v3.3 - data processing, assignment, analysis

NMR spectrometers:

Varian INOVA 500 MHz

SWISS-PROT	Q14449 Q5ICW4
REF	XP_001151613 XP_001151683 NP_004481 XP_001151426 NP_001011681
GenBank	ACE86896 AAW47246 AAY24176 AAC15861 AAH53559
PDB	2AUG
DBJ	BAG35971