BMRB Entry 17943

Title:
1H, 13C and 15N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase.
Deposition date:
2011-09-15
Original release date:
2012-03-23
Authors:
Nogaret, Sophie; Guittet, Eric; Birlirakis, Nicolas
Citation:

Citation: Nogaret, Sophie; Guittet, Eric; Birlirakis, Nicolas. "(1)H, (13)C and (15)N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase."  Biomol. NMR Assignments 7, 1-4 (2013).
PubMed: 22419055

Assembly members:

Assembly members:
CGC-19, polymer, 127 residues, 13790 Da.

Natural source:

Natural source:   Common Name: Streptomyces ambofaciens   Taxonomy ID: 1889   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces ambofaciens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET151/D-TOPO

Data sets:
Data typeCount
13C chemical shifts540
15N chemical shifts135
1H chemical shifts829

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CGC-19 major form1
2CGC-19 minor form1

Entities:

Entity 1, CGC-19 major form 127 residues - 13790 Da.

Residues 1-6 originate from a non-native extended affinity tag

1   GLYILEASPPROPHETHRMETTHRASNHIS
2   ALAASPASNPROTHRTHRHISVALTRPALA
3   THRLEUALAASPARGGLUALAGLUHISLEU
4   THRGLYASPALAGLUALAALAALAGLUVAL
5   VALARGGLYILETRPALAGLUVALLEUGLU
6   ALAASPALAGLUSERILEASPVALHISARG
7   GLYASPPHEPHEGLULEUGLYGLYTYRSER
8   LEULEUALALEUGLNALAILEGLYARGILE
9   LEUTHRGLUTYRGLYVALGLYGLUVALGLU
10   SERVALGLUTRPGLUGLYGLULEULEUASN
11   ARGLEUPHEGLUASNALATHRPROMETGLY
12   GLNALAGLUPHELEUALAGLULYSGLYTYR
13   GLYARGPROASNGLUTHRPRO

Samples:

sample_CGC-19: CGC-19, [U-13C; U-15N], 0.5 mM

sample_CGC-19a: CGC-19, [U-13C; U-15N], 0.5 mM

CGC-19_sample_conditions: ionic strength: 90 mM; pH: 5.6; pressure: 1 atm; temperature: 298 K

CGC-19a_sample_conditions: ionic strength: 90 mM; pH: 5.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_CGC-19isotropicCGC-19_sample_conditions
2D 1H-13C HSQCsample_CGC-19aisotropicCGC-19a_sample_conditions
3D HNCOsample_CGC-19isotropicCGC-19_sample_conditions
3D HN(CA)COsample_CGC-19isotropicCGC-19_sample_conditions
3D HNCAsample_CGC-19isotropicCGC-19_sample_conditions
3D HN(CO)CAsample_CGC-19isotropicCGC-19_sample_conditions
3D HNCACBsample_CGC-19isotropicCGC-19_sample_conditions
3D CBCA(CO)NHsample_CGC-19isotropicCGC-19_sample_conditions
3D HNHAsample_CGC-19isotropicCGC-19_sample_conditions
3D HBHA(CO)NHsample_CGC-19isotropicCGC-19_sample_conditions
3D H(CCO)NHsample_CGC-19isotropicCGC-19_sample_conditions
3D (H)C(CO)NHsample_CGC-19isotropicCGC-19_sample_conditions
3D HCCH-TOCSYsample_CGC-19aisotropicCGC-19a_sample_conditions
3D 1H-15N NOESYsample_CGC-19isotropicCGC-19_sample_conditions
3D 1H-13C NOESY aliphaticsample_CGC-19aisotropicCGC-19a_sample_conditions

Software:

SPARKY v3.114, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance III 800 MHz

Related Database Links:

EMBL CAJ88609
GB AKZ59720
REF WP_053140600

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