BMRB Entry 6837

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR6837

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Title:
NMR Assignments of L27 Heterodimer From C. Elegans Lin-7 and H. Sapiens Lin-2 Scaffold Proteins
Deposition date:
2005-09-26
Original release date:
2006-10-02
Authors:
Petrosky, Keiko; Loehr, Frank; Doetsch, Volker
Citation:

Citation: Petrosky, Keiko; Loehr, Frank; Doetsch, Volker. "NMR Assignment of the L27 Heterodimer from LIN-2 and LIN-7 Scaffold Proteins"  J. Biomol. NMR 36, 15-15 (2006).
PubMed: 16721631

Assembly members:

Assembly members:
construct, polymer, 164 residues, 18302.2 Da.

Natural source:

Natural source:   Common Name: Caenorhabditis elegans   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

Experimental source:

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):

Entity Sequences (FASTA):
construct: MGHHHHHHDYDIPTTENLYE QGSLNLERDVQRILELMEHV QKTGEVNNAKLASLQQVLQS EFFGAVREVYETVYESIDAD TTPEIKAAAGSGSGSGSNLP SDAVQRAKEVLEEISCYPEN NDAKELKRILTQPHFMALLQ THDVVAHEVYSDEALRVTPP PTSP

Data sets:
Data typeCount
13C chemical shifts549
15N chemical shifts146
1H chemical shifts851

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1L27 Heterodimer From Lin-7 and Lin-2 Scaffold Proteins1

Entities:

Entity 1, L27 Heterodimer From Lin-7 and Lin-2 Scaffold Proteins 164 residues - 18302.2 Da.

1   METGLYHISHISHISHISHISHISASPTYR
2   ASPILEPROTHRTHRGLUASNLEUTYRGLU
3   GLNGLYSERLEUASNLEUGLUARGASPVAL
4   GLNARGILELEUGLULEUMETGLUHISVAL
5   GLNLYSTHRGLYGLUVALASNASNALALYS
6   LEUALASERLEUGLNGLNVALLEUGLNSER
7   GLUPHEPHEGLYALAVALARGGLUVALTYR
8   GLUTHRVALTYRGLUSERILEASPALAASP
9   THRTHRPROGLUILELYSALAALAALAGLY
10   SERGLYSERGLYSERGLYSERASNLEUPRO
11   SERASPALAVALGLNARGALALYSGLUVAL
12   LEUGLUGLUILESERCYSTYRPROGLUASN
13   ASNASPALALYSGLULEULYSARGILELEU
14   THRGLNPROHISPHEMETALALEULEUGLN
15   THRHISASPVALVALALAHISGLUVALTYR
16   SERASPGLUALALEUARGVALTHRPROPRO
17   PROTHRSERPRO

Samples:

sample_1: construct 2 mM

sample_2: construct, [U-15N], 2 mM

sample_3: construct, [U-13C], 2 mM

sample_4: construct, [U-13C; U-15N], 2 mM; HEPES 20 mM; TCEP 0.5 mM

conditions_1: ionic strength: 20 mM; pH: 8; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H15N_HSQCsample_1not availableconditions_1
HNCOsample_1not availableconditions_1
HN(CO)CACBsample_1not availableconditions_1
HNCACBsample_1not availableconditions_1
CCCONHsample_1not availableconditions_1
HCCCONHsample_1not availableconditions_1
sample_1-NOESY-TROSYsample_1not availableconditions_1
13C-NOESY-HSQCsample_2not availableconditions_1

Software:

xwinnmr -

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 500 MHz

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