BMRB Entry 6456

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6456
MolProbity Validation Chart

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Title:
NMR STRUCTURE OF THE SH3 DOMAIN OF HUMAN LYN TYROSINE KINASE
Deposition date:
2005-01-12
Original release date:
2005-10-17
Authors:
Bauer, Finn; Schweimer, Kristian; Hoffmann, Silke; Roesch, Paul; Sticht, Heinrich
Citation:

Citation: Bauer, Finn; Schweimer, Kristian; Meiselbach, Heike; Hoffmann, Silke; Roesch, Paul; Sticht, Heinrich. "Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity"  Protein Sci. 14, 2487-2498 (2005).
PubMed: 16155203

Assembly members:

Assembly members:
SH3 domain of the Lyn kinase, polymer, 68 residues, Formula weight is not available
Tyrosine kinase interacting protein, polymer, 23 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SH3 domain of the Lyn kinase: GPLGSPEEQGDIVVALYPYD GIHPDDLSFKKGEKMKVLEE HGEWWKAKSLLTKKEGFIPS NYVAKLNT
Tyrosine kinase interacting protein: TWDPGMPTPPLPPRPANLGE RQA

Data sets:
Data typeCount
1H chemical shifts642
13C chemical shifts321
15N chemical shifts84

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1LynSH3 monomer1
2TIP monomer2

Entities:

Entity 1, LynSH3 monomer 68 residues - Formula weight is not available

1   GLYPROLEUGLYSERPROGLUGLUGLNGLY
2   ASPILEVALVALALALEUTYRPROTYRASP
3   GLYILEHISPROASPASPLEUSERPHELYS
4   LYSGLYGLULYSMETLYSVALLEUGLUGLU
5   HISGLYGLUTRPTRPLYSALALYSSERLEU
6   LEUTHRLYSLYSGLUGLYPHEILEPROSER
7   ASNTYRVALALALYSLEUASNTHR

Entity 2, TIP monomer 23 residues - Formula weight is not available

1   THRTRPASPPROGLYMETPROTHRPROPRO
2   LEUPROPROARGPROALAASNLEUGLYGLU
3   ARGGLNALA

Samples:

sample_1: SH3 domain of the Lyn kinase, [U-99% 13C; U-98% 15N], 1.5 mM; Tyrosine kinase interacting protein 3.4 mM

sample_2: SH3 domain of the Lyn kinase, [U-99% 13C; U-98% 15N], 1.5 mM

sample_3: SH3 domain of the Lyn kinase 3.3 mM; Tyrosine kinase interacting protein, [U-99% 13C; U-98% 15N], 1.5 mM

Ex-cond_1: pH: 6.4; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H-13C NOESYnot availablenot availablenot available
1H-15N NOESYnot availablenot availablenot available
CBCACONHnot availablenot availablenot available
HNCAnot availablenot availablenot available
HNCACBnot availablenot availablenot available
HNCOnot availablenot availablenot available
CCONHnot availablenot availablenot available
HNHAnot availablenot availablenot available
HCCHTOCSYnot availablenot availablenot available

Software:

NMRview v5.0.4 -

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
EMBL CAC84294 CAC84987 CAC84987 CAC84294
GB AAA72928
PIR A34770 A34770
SP P22575
SWISS-PROT P22575
GenBank AAA72928
AlphaFold P22575

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