BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16569

Title: Solution NMR structure of the N-terminal domain of cg2496 protein from Corynebacterium glutamicum. Northeast Structural Genomics Consortium Target CgR26A

Authors: Eletsky, Alexander; Sathyamoorthy, Bharathwaj; Sukumaran, Dinesh; Wang, Dongyan; Buchwald, Willam; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Sathyamoorthy, Bharathwaj; Sukumaran, Dinesh; Wang, Dongyan; Buchwald, Willam; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of the N-terminal domain of cg2496 protein from Corynebacterium glutamicum"  Proteins: Struct. Funct. Genet. ., .-..

Assembly members:
cgr26a, polymer, 148 residues, 15831.934 Da.

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

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

Entity Sequences (FASTA):
cgr26a: TETYVLAESPEFYQDNVTDY TGQISSSDITNIQAAIDDVK ASEQKVIFVVFLSSFDGVDP ETWTQQALQANGGGNVLIYA LAPEERQYGIQGGTQWTDAE LDAANNAAFQALSQEDWAGS ALALAESVGSSSSSSSGSSS LEHHHHHH

Data sets:
Data typeCount
13C chemical shifts573
15N chemical shifts155
1H chemical shifts909

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1cgr26a1

Entities:

Entity 1, cgr26a 148 residues - 15831.934 Da.

Residues 181-188 represent a non-native affinity tag

1   THRGLUTHRTYRVALLEUALAGLUSERPRO
2   GLUPHETYRGLNASPASNVALTHRASPTYR
3   THRGLYGLNILESERSERSERASPILETHR
4   ASNILEGLNALAALAILEASPASPVALLYS
5   ALASERGLUGLNLYSVALILEPHEVALVAL
6   PHELEUSERSERPHEASPGLYVALASPPRO
7   GLUTHRTRPTHRGLNGLNALALEUGLNALA
8   ASNGLYGLYGLYASNVALLEUILETYRALA
9   LEUALAPROGLUGLUARGGLNTYRGLYILE
10   GLNGLYGLYTHRGLNTRPTHRASPALAGLU
11   LEUASPALAALAASNASNALAALAPHEGLN
12   ALALEUSERGLNGLUASPTRPALAGLYSER
13   ALALEUALALEUALAGLUSERVALGLYSER
14   SERSERSERSERSERSERGLYSERSERSER
15   LEUGLUHISHISHISHISHISHIS

Samples:

sample_1: cgr26a, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_2: cgr26a, [U-100% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_3: cgr26a, [U-5% 13C; U-100% 15N], 0.9 mM; MES 20 mM; sodium chloride 200 mM; calcium chloride 5 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 225 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticsample_2isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D (H)CCH-COSY aliphaticsample_1isotropicsample_conditions_1
3D (H)CCH-COSY aromaticsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSY aliphaticsample_1isotropicsample_conditions_1
1D 15N T1sample_1isotropicsample_conditions_1
1D 15N T2sample_1isotropicsample_conditions_1
3D 1H-15N/13C NOESYsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HE aromaticsample_2isotropicsample_conditions_1
2D 1H-13C CT-HSQC methyl 28mssample_3isotropicsample_conditions_1
2D 1H-13C CT-HSQC methyl 56mssample_3isotropicsample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

TOPSPIN v2.1, Bruker Biospin - collection, processing

PROSA v6.4, Guntert - processing

XEASY v1.3.13, Bartels et al. - data analysis

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - structure solution, structure validation

PSVS v1.4, Bhattacharya and Montelione - structure validation

CNS v1.2.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAB99668 BAF55148
EMBL CAF20617 CCH25415
GB AGN19771 AGN22796 AGT06004 AIK85704 AIK88489
REF NP_601475 WP_003857041 WP_003859550 WP_006287490 WP_011015004