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Solution structure of the Vav1 SH2 domain complexed with a Syk-derived singly phosphorylated peptide
Authors
Chen, C., Piraner, D., Gorenstein, N.M., Geahlen, R.L., Post, C.B.
Assembly
Vav1 SH2 domain complex
Entity
1. Vav1 SH2 domain complex, entity 1 (polymer), 106 monomers, 12259.94 Da Detail

HMQDLSVHLW YAGPMERAGA ESILANRSDG TFLVRQRVKD AAEFAISIKY NVEVKHIKIM TAEGLYRITE KKAFRGLTEL VEFYQQNSLK DCFKSLDTTL QFPFKE


2. Vav1 SH2 domain complex, entity 2 (polymer, Thiol state: not present), 13 monomers, 1594.478 Da Detail

DTEVYESPXA DPE


3. O-PHOSPHOTYROSINE (non-polymer), 261.168 Da
Total weight
14115.586 Da
Max. entity weight
12259.94 Da
Source organism
Homo sapiens , Mus musculus
Exptl. method
solution NMR
Refine. method
simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete1
Sequence coverage: 86.6 %, Completeness: 68.7 %, Completeness (bb): 72.3 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All68.7 % (970 of 1411)71.7 % (526 of 734)62.8 % (348 of 554)78.0 % (96 of 123)
Backbone72.3 % (506 of 700)84.0 % (199 of 237)60.7 % (212 of 349)83.3 % (95 of 114)
Sidechain67.8 % (559 of 824)65.8 % (327 of 497)72.6 % (231 of 318)11.1 % (1 of 9)
Aromatic25.4 % (34 of 134)25.4 % (17 of 67)25.8 % (17 of 66) 0.0 % (0 of 1)
Methyl92.1 % (116 of 126)92.1 % (58 of 63)92.1 % (58 of 63)

1. entity 1

HMQDLSVHLW YAGPMERAGA ESILANRSDG TFLVRQRVKD AAEFAISIKY NVEVKHIKIM TAEGLYRITE KKAFRGLTEL VEFYQQNSLK DCFKSLDTTL QFPFKE

2. entity 2

DTEVYESPXA DPE

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7


#NameIsotope labelingTypeConcentration
1entity_1[U-99% 13C; U-99% 15N]1 mM
2entity_2natural abundance1 mM
3TRISnatural abundance20 mM
4sodium chloridenatural abundance100 mM
5DTTnatural abundance1 mM
6sodium azidenatural abundance0.02 %
7H2Onatural abundance90 %
8D2Onatural abundance10 %

Chem. Shift Complete2
Sequence coverage: 28.6 %, Completeness: 43.4 %, Completeness (bb): 46.8 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All43.4 % (1224 of 2822)45.9 % (674 of 1468)38.9 % (431 of 1108)48.4 % (119 of 246)
Backbone46.8 % (655 of 1400)55.3 % (262 of 474)39.4 % (275 of 698)51.8 % (118 of 228)
Sidechain41.5 % (684 of 1648)41.4 % (412 of 994)42.6 % (271 of 636) 5.6 % (1 of 18)
Aromatic19.0 % (51 of 268)21.6 % (29 of 134)16.7 % (22 of 132) 0.0 % (0 of 2)
Methyl56.0 % (141 of 252)57.1 % (72 of 126)54.8 % (69 of 126)

1. entity 1

HMQDLSVHLW YAGPMERAGA ESILANRSDG TFLVRQRVKD AAEFAISIKY NVEVKHIKIM TAEGLYRITE KKAFRGLTEL VEFYQQNSLK DCFKSLDTTL QFPFKE

2. entity 2

DTEVYESPXA DPE

Sample

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 298 K, pH 7


#NameIsotope labelingTypeConcentration
1entity_1[U-99% 13C; U-99% 15N]1 mM
2entity_2natural abundance1 mM
3TRISnatural abundance20 mM
4sodium chloridenatural abundance100 mM
5DTTnatural abundance1 mM
6sodium azidenatural abundance0.02 %
7H2Onatural abundance90 %
8D2Onatural abundance10 %

Protein Blocks Logo
Calculated from 20 models in PDB: 2MC1, Strand ID: A, B Detail


Release date
2013-08-25
Citation
Differential recognition of syk-binding sites by each of the two phosphotyrosine-binding pockets of the Vav SH2 domain
Chen, C., Piraner, D., Gorenstein, N.M., Geahlen, R.L., Beth Post, C.
Biopolymers (2013), 99, 897-907, PubMed 23955592 , DOI 10.1002/bip.22371 ,
Related entities 1. Vav1 SH2 domain complex, entity 1, : 3 : 191 entities Detail
Related entities 2. Vav1 SH2 domain complex, entity 2, : 1 : 18 : 8 entities Detail
Interaction partners 1. Vav1 SH2 domain complex, entity 1, : 23 : 1 interactors Detail
Interaction partners 2. Vav1 SH2 domain complex, entity 2, : 1 interactors Detail
Experiments performed 10 experiments Detail
NMR combined restraints 4 contents Detail
Keywords B CELL SIGNALING PROTEIN, PHOSPHOPEPTIDE, PHOSPHORYLATED PEPTIDE, PHOSPHOTYROSINE BINDING DOMAIN, PROTEIN-PEPTIDE COMPLEX, SIGNALING PROTEIN, SYK KINASE, TYROSINE KINASE