BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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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   PubMed: 8181064

Authors: Forman-Kay, Julie

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).

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

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

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