BMRB Entry 15086

Title:
Solution NMR structure of Hypothetical Protein Cgl2762 from Corynebacterium Glutamicum: Northeast Structural Genomics Consortium Target CgR3
Deposition date:
2006-12-28
Original release date:
2007-02-23
Authors:
Singarapu, Kiran Kumar; sukumaran, Dinesh; Parish, David; Chen, Chen; Kellie, Cunningham; Rong, Xiao; G V T, Swapna; Montelione, Gaetano; Szyperski, Thomas
Citation:

Citation: Singarapu, Kiran Kumar; Xiao, Rong; Sukumaran, Dinesh; Acton, Thomas; Montelione, Gaetano; Szyperski, Thomas. "NMR structure of protein Cgl2762 from Corynebacterium glutamicum implicated in DNA transposition reveals a helix-turn-helix motif attached to a flexibly disordered leucine zipper."  Proteins 70, 1650-1654 (2008).
PubMed: 18175328

Assembly members:

Assembly members:
hypothetical_protein_Cgl2762, polymer, 97 residues, 11048.383 Da.

Natural source:

Natural source:   Common Name: Corynebacterium glutamicum   Taxonomy ID: 1718   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Corynebacterium glutamicum

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts411
15N chemical shifts108
1H chemical shifts671

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hypothetical protein Cgl27621

Entities:

Entity 1, hypothetical protein Cgl2762 97 residues - 11048.383 Da.

1   METPROTHRLYSTHRTYRSERGLUGLUPHE
2   LYSARGASPALAVALALALEUTYRGLUASN
3   SERASPGLYALASERLEUGLNGLNILEALA
4   ASNASPLEUGLYILEASNARGVALTHRLEU
5   LYSASNTRPILEILELYSTYRGLYSERASN
6   HISASNVALGLNGLYTHRTHRPROSERALA
7   ALAVALSERGLUALAGLUGLNILEARGGLN
8   LEULYSLYSGLUASNALALEUGLNARGALA
9   ARGTHRARGHISPROALAGLUSERCYSLEU
10   GLUHISHISHISHISHISHIS

Samples:

sample_1: hypothetical protein Cgl2762, [U-100% 13C; U-100% 15N], 1.2 ± 0.2 mM

sample_conditions_1: ionic strength: 100 mM; pH: 4.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
4,3D GFT HNNCABCAsample_1isotropicsample_conditions_1
4,3D GFT CABCACONNHsample_1isotropicsample_conditions_1
4,3D GFT HABCABCONNHsample_1isotropicsample_conditions_1
4,3D GFT HCCH TOCSYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 13C,15N simulatanious NOESYsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1

Software:

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

DYANA v1.5, Guntert, Braun and Wuthrich - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement

AutoStruct v2.0, Huang, Swapana, Rajan, Ke, Xia, Shukla, Inouye and Montelione - data analysis

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR, Varian - collection

NMR spectrometers:

  • Varian INOVA 750 MHz

Related Database Links:

PDB
DBJ BAC00156
EMBL CAF20784 CCH25886
GB AGT06475
REF NP_601957 WP_011015358

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