BMRB Entry 5794

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5794

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Title:
1H, 13C, 15N Chemical Shift Assignments for the SH3-SH2 domain pair of the tyrosin kinase Lck
Deposition date:
2003-05-10
Original release date:
2003-10-16
Authors:
Schweimer, Kristian; Kiessling, Anke; Bauer, Finn; Hor, Simon; Hoffmann, Silke; Roesch, Paul; Sticht, Heinrich
Citation:

Citation: Schweimer, Kristian; Kiessling, Anke; Bauer, Finn; Hor, Simon; Hoffmann, Silke; Roesch, Paul; Sticht, Heinrich. "Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the SH3-SH2 domain pair of the human tyrosine kinase Lck "  J. Biomol. NMR 27, 405-406 (2003).
PubMed: 14512743

Assembly members:

Assembly members:
Tyrosine kinase, polymer, 169 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):
Tyrosine kinase: ASPLQDNLVIALHSYEPSHD GDLGFEKGEQLRILEQSGEW WKAQSLTTGQEGFIPFNFVA KANSLEPEPWFFKNLSRKDA ERQLLAPGNTHGSFLIRESE STAGSFSLSVRDFDQNQGEV VKHYKIRNLDNGGFYISPRI TFPGLHELVRHYTNASDGLC TRLSRPCQT

Data sets:
Data typeCount
1H chemical shifts981
13C chemical shifts618
15N chemical shifts156

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1LckSH321

Entities:

Entity 1, LckSH32 169 residues - Formula weight is not available

1   ALASERPROLEUGLNASPASNLEUVALILE
2   ALALEUHISSERTYRGLUPROSERHISASP
3   GLYASPLEUGLYPHEGLULYSGLYGLUGLN
4   LEUARGILELEUGLUGLNSERGLYGLUTRP
5   TRPLYSALAGLNSERLEUTHRTHRGLYGLN
6   GLUGLYPHEILEPROPHEASNPHEVALALA
7   LYSALAASNSERLEUGLUPROGLUPROTRP
8   PHEPHELYSASNLEUSERARGLYSASPALA
9   GLUARGGLNLEULEUALAPROGLYASNTHR
10   HISGLYSERPHELEUILEARGGLUSERGLU
11   SERTHRALAGLYSERPHESERLEUSERVAL
12   ARGASPPHEASPGLNASNGLNGLYGLUVAL
13   VALLYSHISTYRLYSILEARGASNLEUASP
14   ASNGLYGLYPHETYRILESERPROARGILE
15   THRPHEPROGLYLEUHISGLULEUVALARG
16   HISTYRTHRASNALASERASPGLYLEUCYS
17   THRARGLEUSERARGPROCYSGLNTHR

Samples:

sample_1: Tyrosine kinase, [U-95% 13C; U-95% 15N], 0.5 – 0.7 mM

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

Experiments:

NameSampleSample stateSample conditions
1H-15N HSQCnot availablenot availablenot available
1H-13C constant time HSQCnot availablenot availablenot available
HNCOnot availablenot availablenot available
HNCAnot availablenot availablenot available
HNCACBnot availablenot availablenot available
CBCA(CO)NHnot availablenot availablenot available
CCCONH-TOCSYnot availablenot availablenot available
HBHA(CO)NHnot availablenot availablenot available
HCCH-COSYnot availablenot availablenot available
HCCH-TOCSYnot availablenot availablenot available

Software:

NMRView v5.0.4 - visual analysis of the NMR spectra

home written software - processing of the NMR raw data, automatic assignment of the backbone resonances

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
DBJ BAC40086 BAG64189 BAI45973
EMBL CAA27234 CAA31884 CAA32211 CAC38871 CAC44027
GB AAA18225 AAA59502 AAB59674 AAC50287 AAF34794
PRF 1203381A 2201317A
REF NP_001036236 NP_001094179 NP_001155904 NP_001155905 NP_005347
SP P06239 P06240 Q01621 Q5PXS1 Q95KR7
TPE CAD55807
AlphaFold P06239 P06240 Q01621 Q5PXS1 Q95KR7

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