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Backbone and Sidechain 1H, 13C and 15N resonance assignments for PLC-gamma 1 C-terminal SH2 domain complexed with a PDGFR-derived phosphopeptide
Authors
Forman-Kay, J.D.
Assembly
phospholipase C gamma-1 C-terminal SH2 domain
Entity
1. PLCC SH2 (polymer, Thiol state: all free), 105 monomers, 12254.75 Da Detail

GSPGIHESKE WYHASLTRAQ AEHMLMRVPR DGAFLVRKRN EPNSYAISFR AEGKIKHCRV QQEGQTVMLG NSEFDSLVDL ISYYEKHPLY RKMKLRYPIN EENSS


2. PDGFR-derived phosphopeptide, residues 1018 to 1029 (polymer, Thiol state: not present), 12 monomers, 1479.523 Da Detail

DNDXIIPLPD PK


Total weight
13734.273 Da
Max. entity weight
12254.75 Da
Source organism
Bos taurus
Exptl. method
NMR
Data set
assigned_chemical_shifts
Chem. Shift Complete1
Sequence coverage: 88.0 %, Completeness: 82.8 %, Completeness (bb): 87.9 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All82.8 % (1152 of 1392)80.2 % (591 of 737)84.7 % (454 of 536)89.9 % (107 of 119)
Backbone87.9 % (598 of 680)87.8 % (202 of 230)87.1 % (298 of 342)90.7 % (98 of 108)
Sidechain79.3 % (652 of 822)76.7 % (389 of 507)83.6 % (254 of 304)81.8 % (9 of 11)
Aromatic64.5 % (71 of 110)63.6 % (35 of 55)64.8 % (35 of 54)100.0 % (1 of 1)
Methyl87.0 % (87 of 100)86.0 % (43 of 50)88.0 % (44 of 50)

1. PLCC SH2

GSPGIHESKE WYHASLTRAQ AEHMLMRVPR DGAFLVRKRN EPNSYAISFR AEGKIKHCRV QQEGQTVMLG NSEFDSLVDL ISYYEKHPLY RKMKLRYPIN EENSS

2. PDGFR-derived phosphopeptide, residues 1018 to 1029

DNDXIIPLPD PK

Sample

Temperature 303 (±1) K, pH 6.4 (±0.2)


#NameIsotope labelingTypeConcentration
1PLCC SH2[U-99% 13C; U-99% 15N]1.5 mM
2PDGFR-derived phosphopeptide, residues 1018 to 10291.5 mM

Chem. Shift Complete2
Sequence coverage: 35.9 %, Completeness: 51.3 %, Completeness (bb): 55.2 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All51.3 % (1427 of 2784)51.8 % (764 of 1474)49.3 % (529 of 1072)56.3 % (134 of 238)
Backbone55.2 % (751 of 1360)57.8 % (266 of 460)52.9 % (362 of 684)56.9 % (123 of 216)
Sidechain48.4 % (796 of 1644)49.1 % (498 of 1014)47.2 % (287 of 608)50.0 % (11 of 22)
Aromatic34.1 % (75 of 220)35.5 % (39 of 110)32.4 % (35 of 108)50.0 % (1 of 2)
Methyl52.0 % (104 of 200)55.0 % (55 of 100)49.0 % (49 of 100)

1. PLCC SH2

GSPGIHESKE WYHASLTRAQ AEHMLMRVPR DGAFLVRKRN EPNSYAISFR AEGKIKHCRV QQEGQTVMLG NSEFDSLVDL ISYYEKHPLY RKMKLRYPIN EENSS

2. PDGFR-derived phosphopeptide, residues 1018 to 1029

DNDXIIPLPD PK

Sample

Temperature 303 (±1) K, pH 6.4 (±0.2)


#NameIsotope labelingTypeConcentration
1PLCC SH2[U-99% 13C; U-99% 15N]1.5 mM
2PDGFR-derived phosphopeptide, residues 1018 to 10291.5 mM

Protein Blocks Logo
Calculated from 1 models in PDB: 2PLD, Strand ID: A, B Detail


Release date
2008-07-16
Citation 1
Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide
Pascal, S.M., Singer, A.U., Gish, G., Yamazaki, T., Shoelson, S.E., Pawson, T., Kay, L.E., Forman-Kay, J.D.
Cell (1994), 77, 461-472, PubMed 8181064 ,
Citation 2
Sequence similarity of phospholipase C with the non-catalytic region of src
Stahl, M.L., Ferenz, C.R., Kelleher, K.L., Kriz, R.W., Knopf, J.L.
Nature (1988), 332, 269-272, PubMed 2831461 , DOI 10.1038/332269a0 ,
Citation 3
Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding
Piccione, E., Case, R.D., Domchek, S.M., Hu, P., Chaudhuri, M., Backer, J.M., Schlessinger, J., Shoelson, S.E.
Biochemistry (1993), 32, 3197-3202, PubMed 8384875 ,
Citation 4
[The history of the discovery of anesthesia. Progress is the attainment of utopia]
Miguel Giacchella, R.
Rev. Soc. Odontol. La Plata (1988), 1, 29-30, PubMed 3078736 ,
Entries sharing articles BMRB: 1, Swiss-Prot: 1 entries Detail
  BMRB: 5318 released on 2002-04-30
    Title Backbone and Sidechain 1H, 13C and 15N resonance assignments for PLC-gamma 1 C-terminal SH2 domain
  Swiss-Prot: P08487 released on 1988-08-01
    Title PLCG1_BOVIN Entity 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
Related entities 1. PLCC SH2, : 7 : 179 entities Detail
Related entities 2. PDGFR-derived phosphopeptide, residues 1018 to 1029, : 1 : 1 : 7 entities Detail
Interaction partners 1. PLCC SH2, : 28 interactors Detail
Interaction partners 2. PDGFR-derived phosphopeptide, residues 1018 to 1029, : 1 interactors Detail
Experiments performed 8 experiments Detail
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