BMRB Entry 6261

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6261
MolProbity Validation Chart

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Title:
NMR STRUCTURE OF THE SH3 DOMAIN OF HUMAN LYN TYROSINE KINASE
Deposition date:
2004-07-13
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

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

Data sets:
Data typeCount
1H chemical shifts495
13C chemical shifts275
15N chemical shifts67

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1LynSH3 monomer1

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

Samples:

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

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

Experiments:

NameSampleSample stateSample conditions
1H-13C NOESYsample_1not availableEx-cond_1
1H-15N NOESYsample_1not availableEx-cond_1
CBCACONHsample_1not availableEx-cond_1
HNCAsample_1not availableEx-cond_1
HNCACBsample_1not availableEx-cond_1
HNCOsample_1not availableEx-cond_1
CCONHsample_1not availableEx-cond_1
HNHAsample_1not availableEx-cond_1
HCCHTOCSYsample_1not availableEx-cond_1

Software:

NMRview v5.0.4 -

NMR spectrometers:

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

Related Database Links:

PDB
DBJ BAF83183 BAG60841 BAI45692
GB AAA59540 AAB50019 AAH59394 AAH68551 AAH75001
PRF 2006286C
REF NP_001104567 NP_002341 XP_001087049 XP_002805388 XP_002805389
SP P07948
AlphaFold P07948

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