BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 5309

Title: 1H, 15N and 13C assignments of FLIN4, an intramolecular LMO4:ldb1 complex   PubMed: 12153047

Deposition date: 2002-03-04 Original release date: 2002-08-22

Authors: Deane, Janet; Visvader, Jane; Mackay, Joel; Matthews, Jacqueline

Citation: Deane, Janet; Visvader, Jane; Mackay, Joel; Matthews, Jacqueline. "Letter to the Editor: 1H, 15N and 13C assignments of FLIN4, an intramolecular LMO4:ldb1 complex"  J. Biomol. NMR 23, 165-166 (2002).

Assembly members:
engineered intramolecular protein complex, polymer, 122 residues, 13004 Da.
ZN, non-polymer, 65.409 Da.

Natural source:   Common Name: mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

Experimental source:   Production method: recombinant technology

Entity Sequences (FASTA):
engineered intramolecular protein complex: GSLSWKRCAGCGGKIADRFL LYAMDSYWHSRCLKCSSCQA QLGDIGTSSYTKSGMILCRN DYIRLFGNSGAGGSGGHMGS GGDVMVVGEPTLMGGEFGDE DERLITRLENTQFDAANGID DE

Data sets:
Data typeCount
13C chemical shifts393
15N chemical shifts116
1H chemical shifts693

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1flin41
2Zinc ion, I2
3Zinc ion, II2

Entities:

Entity 1, flin4 122 residues - 13004 Da.

1   GLYSERLEUSERTRPLYSARGCYSALAGLY
2   CYSGLYGLYLYSILEALAASPARGPHELEU
3   LEUTYRALAMETASPSERTYRTRPHISSER
4   ARGCYSLEULYSCYSSERSERCYSGLNALA
5   GLNLEUGLYASPILEGLYTHRSERSERTYR
6   THRLYSSERGLYMETILELEUCYSARGASN
7   ASPTYRILEARGLEUPHEGLYASNSERGLY
8   ALAGLYGLYSERGLYGLYHISMETGLYSER
9   GLYGLYASPVALMETVALVALGLYGLUPRO
10   THRLEUMETGLYGLYGLUPHEGLYASPGLU
11   ASPGLUARGLEUILETHRARGLEUGLUASN
12   THRGLNPHEASPALAALAASNGLYILEASP
13   ASPGLU

Entity 2, Zinc ion, I - Zn - 65.409 Da.

1   ZN

Samples:

sample_1: engineered intramolecular protein complex0.3 – 0.8 mM

sample_2: engineered intramolecular protein complex, [U-95% 15N], 0.3 – 0.8 mM

sample_3: engineered intramolecular protein complex, [U-95% 13C; U-95% 15N], 0.3 – 0.8 mM

cond_1: ionic strength: 0.22 M; pH: 7.0 na; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
1H TOCSYnot availablenot availablecond_1
1H NOESYnot availablenot availablecond_1
1H DQF-COSYnot availablenot availablecond_1
1H-15N HSQCnot availablenot availablecond_1
HNHAnot availablenot availablecond_1
HNCAnot availablenot availablecond_1
HN(CO)CAnot availablenot availablecond_1
HNCACBnot availablenot availablecond_1
CBCA(CO)NHnot availablenot availablecond_1
HNCOnot availablenot availablecond_1
HN(CA)COnot availablenot availablecond_1
CC(CO)NH-TOCSYnot availablenot availablecond_1
HCC(CO)NH-TOCSYnot availablenot availablecond_1
HCCH-TOCSYnot availablenot availablecond_1
15N-NOESY-HSQCnot availablenot availablecond_1

Software:

xwinnmr - data aquisition, processing

XEASY - assignments

NMR spectrometers:

  • BRUKER DMX 600 MHz

Related Database Links:

PDB

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts