BMRB Entry 5310

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:
Data typeCount
1H chemical shifts781
13C chemical shifts460
15N chemical shifts133

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1PLCC SH2 domain1
2phosphopeptide ligand2

Entities:

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

1   GLYSERPROGLYILEHISGLUSERLYSGLU
2   TRPTYRHISALASERLEUTHRARGALAGLN
3   ALAGLUHISMETLEUMETARGVALPROARG
4   ASPGLYALAPHELEUVALARGLYSARGASN
5   GLUPROASNSERTYRALAILESERPHEARG
6   ALAGLUGLYLYSILELYSHISCYSARGVAL
7   GLNGLNGLUGLYGLNTHRVALMETLEUGLY
8   ASNSERGLUPHEASPSERLEUVALASPLEU
9   ILESERTYRTYRGLULYSHISPROLEUTYR
10   ARGLYSMETLYSLEUARGTYRPROILEASN
11   GLUGLUASNSERSER

Entity 2, phosphopeptide ligand 12 residues - 261.168 Da.

1   ASPASNASPPTRILEILEPROLEUPROASP
2   PROLYS

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:

NameSampleSample stateSample conditions
3D 13C- or 15N-edited NOESY-HSQCsample_1not availablecondition_1
3D 15N-edited TOCSY-HSQCsample_1not availablecondition_1
CN NOESY-HSQCsample_1not availablecondition_1
HBCBCA(CO)NNHsample_1not availablecondition_1
HNCACBsample_1not availablecondition_1
(HB)CB(CGCD)HDsample_1not availablecondition_1
(HB)CB(CGCDCE)HEsample_1not availablecondition_1
HMQC Jsample_1not availablecondition_1

Software:

X-PLOR - combined distance geometry-simulated annealing calculations

STEREOSEARCH - extraction of torsion angle restraint values

NMR spectrometers:

  • Varian UNITY 500 MHz

Related Database Links:

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
BMRB 5318

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