BMRB Entry 5310

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PDB ID: 2pld
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR5310
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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 and Sidechain 1H, 13C and 15N resonance assignments for PLC-gamma 1 C-terminal SH2 domain complexed with a PDGFR-derived phosphopeptide

Deposition date:

2002-03-04

Original release date:

2008-07-17

Authors:

Forman-Kay, Julie

Citation:

Citation: Pascal, Steve; Singer, Alex; Gish, Gerry; Yamazaki, Toshio; Shoelson, Steven; Pawson, Tony; Kay, Lewis; Forman-Kay, Julie. "Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide " Cell 77, 461-472 (1994).
PubMed: 8181064

Assembly members:

Assembly members:
PLCC SH2, polymer, 105 residues, Formula weight is not available
PDGFR-derived phosphopeptide, residues 1018 to 1029, polymer, 12 residues, 261.168 Da.
PTR, non-polymer, 261.168 Da.

Natural source:

Natural source: Common Name: Cow Taxonomy ID: 9913 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Bos taurus

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PLCC SH2: GSPGIHESKEWYHASLTRAQ AEHMLMRVPRDGAFLVRKRN EPNSYAISFRAEGKIKHCRV QQEGQTVMLGNSEFDSLVDL ISYYEKHPLYRKMKLRYPIN EENSS
PDGFR-derived phosphopeptide, residues 1018 to 1029: DNDXIIPLPDPK

Data sets:

assigned_chemical_shifts
- shift_set_1
- shift_set_2

Data type	Count
1H chemical shifts	781
13C chemical shifts	460
15N chemical shifts	133

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PLCC SH2 domain	1
2	phosphopeptide ligand	2

Entities:

Entity 1, PLCC SH2 domain 105 residues - Formula weight is not available

1

GLY

SER

PRO

GLY

ILE

HIS

GLU

SER

LYS

GLU

2

TRP

TYR

HIS

ALA

SER

LEU

THR

ARG

ALA

GLN

3

ALA

GLU

HIS

MET

LEU

MET

ARG

VAL

PRO

ARG

4

ASP

GLY

ALA

PHE

LEU

VAL

ARG

LYS

ARG

ASN

5

GLU

PRO

ASN

SER

TYR

ALA

ILE

SER

PHE

ARG

6

ALA

GLU

GLY

LYS

ILE

LYS

HIS

CYS

ARG

VAL

7

GLN

GLU

GLY

GLN

THR

VAL

MET

LEU

GLY

8

ASN

SER

GLU

PHE

ASP

SER

LEU

VAL

ASP

LEU

9

ILE

SER

TYR

GLU

LYS

HIS

PRO

LEU

TYR

10

ARG

LYS

MET

LYS

LEU

ARG

TYR

PRO

ILE

ASN

11

GLU

ASN

SER

Entity 2, phosphopeptide ligand 12 residues - 261.168 Da.

1

ASP

ASN

ASP

PTR

ILE

PRO

LEU

PRO

ASP

2

PRO

LYS

Samples:

sample_1: PLCC SH2, [U-99% 13C; U-99% 15N], 1.5 mM; PDGFR-derived phosphopeptide, residues 1018 to 1029 1.5 mM

condition_1: pH: 6.4; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D 13C- or 15N-edited NOESY-HSQC	sample_1	not available	condition_1
3D 15N-edited TOCSY-HSQC	sample_1	not available	condition_1
CN NOESY-HSQC	sample_1	not available	condition_1
HBCBCA(CO)NNH	sample_1	not available	condition_1
HNCACB	sample_1	not available	condition_1
(HB)CB(CGCD)HD	sample_1	not available	condition_1
(HB)CB(CGCDCE)HE	sample_1	not available	condition_1
HMQC J	sample_1	not available	condition_1

Software:

X-PLOR - combined distance geometry-simulated annealing calculations

STEREOSEARCH - extraction of torsion angle restraint values

NMR spectrometers:

Varian UNITY 500 MHz

SWISS-PROT	Q62077 P08487 P19174 P10686
REF	XP_514650.2 XP_001500255.1 XP_001087295.1 NP_002651.2 XP_542998.2
PRF	1404383A
GenBank	EDL96615.1 ABK42331.1 EDL96614.1 EAW75989.1 EAW75993.1
EMBL	CAM23068.1 CAM28260.1 CAA68406.1 CAM23067.1 CAA18537.1
DBJ	BAE06110.1 BAG10236.1 BAE21990.1
PDB	2PLE 2PLD 2FCI
BMRB	5318