BMRB Entry 5202

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR5202
MolProbity Validation Chart

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

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).
PubMed: 11885989

Assembly members:

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

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

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
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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 nucleotide 3'-phosphodiesterase, [U-13C; U-15N; U-90% 2H], 1.0 mM; NaCl 0.15 M

sample_2: 2',3'-cyclic nucleotide 3'-phosphodiesterase, [U-15N], 1.0 – 2.0 mM; NaCl 0.15 M

sample_3: 2',3'-cyclic nucleotide 3'-phosphodiesterase, [U-13C; U-15N], 1.0 mM; NaCl 0.15 M

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
AlphaFold P13233

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CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks