BMRB Entry 5047

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR5047
MolProbity Validation Chart

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Title:
NMR structure of the LCCL Domain and its Implications for DFNA9 Deafness Disorder
Deposition date:
2001-06-06
Original release date:
2001-11-14
Authors:
Liepinsh, Edvards; Trexler, Maria; Kaikkonen, Andrei; Weigelt, Johan; Banyai, Laszlo; Patthy, Laszlo; Otting, Gottfried
Citation:

Citation: Liepinsh, Edvards; Trexler, Maria; Kaikkonen, Andrei; Weigelt, Johan; Banyai, Laszlo; Patthy, Laszlo; Otting, Gottfried. "NMR structure of the LCCL Domain and its Implications for DFNA9 Deafness Disorder"  EMBO J. 20, 5347-5353 (2001).
PubMed: 11574466

Assembly members:

Assembly members:
Human coch-5h2 protein, polymer, 100 residues, 10467 Da.

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   Host organism: Escherichia coli   Vector: pmed23

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human coch-5h2 protein: TAPIAITCFTRGLDIRKEKA DVLCPGGCPLEEFSVYGNIV YASVSSICGAAVHRGVISNS GGPVRVYSLPGRENYSSVDA NGIQSQMLSRWSASFTVTLE

Data sets:
Data typeCount
15N chemical shifts108
1H chemical shifts685

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1LCCL domain 11

Entities:

Entity 1, LCCL domain 1 100 residues - 10467 Da.

1   THRALAPROILEALAILETHRCYSPHETHR
2   ARGGLYLEUASPILEARGLYSGLULYSALA
3   ASPVALLEUCYSPROGLYGLYCYSPROLEU
4   GLUGLUPHESERVALTYRGLYASNILEVAL
5   TYRALASERVALSERSERILECYSGLYALA
6   ALAVALHISARGGLYVALILESERASNSER
7   GLYGLYPROVALARGVALTYRSERLEUPRO
8   GLYARGGLUASNTYRSERSERVALASPALA
9   ASNGLYILEGLNSERGLNMETLEUSERARG
10   TRPSERALASERPHETHRVALTHRLEUGLU

Samples:

sample_1: Human coch-5h2 protein 1.0 mM; NaCl 0.1 M

sample_2: Human coch-5h2 protein, [U-95% 15N], 3.0 mg/mL; NaCl 0.1 M

sample_3: Human coch-5h2 protein, [U-95% 15N], 3.3 mg/mL; NaCl 0.1 M

Ex-cond_1: ionic strength: 0.1 M; pH: 4.9; temperature: 301 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H DQF-COSYnot availablenot availablenot available
2D 1H-1H HOHAHAnot availablenot availablenot available
2D 1H-1H NOESYnot availablenot availablenot available
2D 1H-1H ROESYnot availablenot availablenot available
2D 1H-15N HSQCnot availablenot availablenot available
3D 1H-1H-15N TOCSYnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available

Software:

XWINNMR - spectral processing

PROSA - spectral processing

NMR spectrometers:

  • Bruker DMX 500 MHz
  • Bruker DMX 600 MHz
  • Varian UnityPlus 800 MHz

Related Database Links:

PDB
DBJ BAF85413
GenBank AAC39545 AAH07230 AAQ89259 AAW82432 EAW65963
REF NP_004077 XP_001114738 XP_001114756 XP_001114785 XP_001114797
SWISS-PROT O43405

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