BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 5202

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5202

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry

Title: Assignment of the 1H, 13C and 15N resonances of the catalytic domain of the rat 2',3'-cyclic nucleotide 3'-phosphodiesterase   PubMed: 11885989

Deposition date: 2001-11-06 Original release date: 2006-06-16

Authors: Kozlov, Guennadi; Lee, John; Gravel, Michel; Ekiel, Irena; Braun, Peter; Gehrin, Kalle

Citation: Kozlov, Guennadi; Lee, John; Gravel, Michel; Ekiel, Irena; Braun, Peter; Gehrin, Kalle. "Letter to the Editor: Assignment of the 1H, 13C and 15N Resonances of the Catalytic Domain of the Rat 2',3'-cyclic Nucleotide 3'-phosphodiesterase "  J. Biomol. NMR 22, 99-100 (2002).

Assembly members:
2',3'-cyclic nucleotide 3'-phosphodiesterase, polymer, 219 residues, 24218 Da.

Natural source:   Common Name: Rat   Taxonomy ID: 10116   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Rattus norvegicus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
2',3'-cyclic nucleotide 3'-phosphodiesterase: GSHMFLPLYFGWFLTKKSSE TLRKAGQVFLEELGNHKAFK KELRHFISGDEPKEKLDLVS YFGKRPPGVLHCTTKFCDYG KATGAEEYAQQDVVRRSYGK AFKLSISALFVTPKTAGAQV VLNEQELQLWPSDLDKPSSS ESLPPGSRAHVTLGCAADVQ PVQTGLDLLEILQQVKGGSQ GEEVGELPRGKLYSLGKGRW MLSLAKKMEVKAIFTGYYG

Data sets:
Data typeCount
1H chemical shifts1116
13C chemical shifts590
15N chemical shifts200

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CNP catalytic domain1

Entities:

Entity 1, CNP catalytic domain 219 residues - 24218 Da.

1   GLYSERHISMETPHELEUPROLEUTYRPHE
2   GLYTRPPHELEUTHRLYSLYSSERSERGLU
3   THRLEUARGLYSALAGLYGLNVALPHELEU
4   GLUGLULEUGLYASNHISLYSALAPHELYS
5   LYSGLULEUARGHISPHEILESERGLYASP
6   GLUPROLYSGLULYSLEUASPLEUVALSER
7   TYRPHEGLYLYSARGPROPROGLYVALLEU
8   HISCYSTHRTHRLYSPHECYSASPTYRGLY
9   LYSALATHRGLYALAGLUGLUTYRALAGLN
10   GLNASPVALVALARGARGSERTYRGLYLYS
11   ALAPHELYSLEUSERILESERALALEUPHE
12   VALTHRPROLYSTHRALAGLYALAGLNVAL
13   VALLEUASNGLUGLNGLULEUGLNLEUTRP
14   PROSERASPLEUASPLYSPROSERSERSER
15   GLUSERLEUPROPROGLYSERARGALAHIS
16   VALTHRLEUGLYCYSALAALAASPVALGLN
17   PROVALGLNTHRGLYLEUASPLEULEUGLU
18   ILELEUGLNGLNVALLYSGLYGLYSERGLN
19   GLYGLUGLUVALGLYGLULEUPROARGGLY
20   LYSLEUTYRSERLEUGLYLYSGLYARGTRP
21   METLEUSERLEUALALYSLYSMETGLUVAL
22   LYSALAILEPHETHRGLYTYRTYRGLY

Samples:

sample_1: 2, ,3'-cyclic, $CNP 1.0; 5202, 1, 0.15; 5202, 1,

sample_2: 2, ,3'-cyclic, $CNP ± 1.0 ; 5202, 2, 0.15; 5202, 2,

sample_3: 2, ,3'-cyclic, $CNP 1.0; 5202, 3, 0.15; 5202, 3,

condition_1: pH: 6.0 na; temperature: 310 K; ionic strength: 0.15 M

Experiments:

NameSampleSample stateSample conditions
3D HNCAnot availablenot availablenot available
3D HNCACBnot availablenot availablenot available
3D CBCA(CO)NHnot availablenot availablenot available
3D HNCOnot availablenot availablenot available
3D 1H-13C-1H HCCH-TOCSYnot availablenot availablenot available
3D 1H-13C-1H NOESYnot availablenot availablenot available
3D 1H-1H-15N NOESYnot availablenot availablenot available

Software:

XWINNMR v2.1 - data collection

GIFA v4.31 - data processing

XEASY v1.3.13 - data analysis

NMR spectrometers:

  • Varian UnityPlus 800 MHz
  • Bruker DRX 500 MHz

Related Database Links:

PDB
GB AAA64429 AAH98066 AIS72844 EDM06047 EDM06048
REF NP_036941 XP_006247322 XP_006247323 XP_008766170
SP P13233

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