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Biological Magnetic Resonance Data Bank


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BMRB Entry 18989

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18989
MolProbity Validation Chart

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Title: Solution NMR structure of the Polyketide_cyc-like protein Cgl2372 from Corynebacterium glutamicum, Northeast Structural Genomics Consortium Target CgR160.

Deposition date: 2013-01-30 Original release date: 2013-02-11

Authors: Yang, Yunhuang; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Sapin, Ari; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Sapin, Ari; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the Polyketide_cyc-like protein Cgl2372 from Corynebacterium glutamicum, Northeast Structural Genomics Consortium Target CgR160."  To be published ., .-..

Assembly members:
CgR160, polymer, 163 residues, 18809.209 Da.

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

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

Entity Sequences (FASTA):
CgR160: MPKSLTFEDSINIAAPINQV YALVSDITRTGEWSPVCEKC WWDEDEGPVVGAHFTGRNVT PERTWETRSEVIVAEPNRCF GWSVTDGNVKWIYSMEPLEE GTVLTESWEFTPKGQRFFHD KFGDKSIEEIEKRRLAAITG IPETLVAIQRILEVELEHHH HHH

Data sets:
Data typeCount
13C chemical shifts643
15N chemical shifts156
1H chemical shifts1043

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CgR1601

Entities:

Entity 1, CgR160 163 residues - 18809.209 Da.

1   METPROLYSSERLEUTHRPHEGLUASPSER
2   ILEASNILEALAALAPROILEASNGLNVAL
3   TYRALALEUVALSERASPILETHRARGTHR
4   GLYGLUTRPSERPROVALCYSGLULYSCYS
5   TRPTRPASPGLUASPGLUGLYPROVALVAL
6   GLYALAHISPHETHRGLYARGASNVALTHR
7   PROGLUARGTHRTRPGLUTHRARGSERGLU
8   VALILEVALALAGLUPROASNARGCYSPHE
9   GLYTRPSERVALTHRASPGLYASNVALLYS
10   TRPILETYRSERMETGLUPROLEUGLUGLU
11   GLYTHRVALLEUTHRGLUSERTRPGLUPHE
12   THRPROLYSGLYGLNARGPHEPHEHISASP
13   LYSPHEGLYASPLYSSERILEGLUGLUILE
14   GLULYSARGARGLEUALAALAILETHRGLY
15   ILEPROGLUTHRLEUVALALAILEGLNARG
16   ILELEUGLUVALGLULEUGLUHISHISHIS
17   HISHISHIS

Samples:

sample_1: CgR160.003, [U-100% 13C; U-100% 15N], 0.76 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

sample_2: CgR160.0035, [U-5% 13C; U-100% 15N], 0.83 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C arom NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
4D CC-NOESYsample_1isotropicsample_conditions_1
3D (H)CCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQC-Histidinesample_1isotropicsample_conditions_1
2D 1H-15N HSQC NH2 onlysample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement,geometry optimization,structure solution

AutoStruct v2.1, Huang, Tejero, Powers and Montelione - data analysis,refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

XEASY, Bartels et al. - data analysis,peak picking,chemical shift assignment

TOPSPIN, Bruker Biospin - collection

VNMRJ, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Bruker Avance 850 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB99766 BAF55259
EMBL CAF21038 CCH25510
GB AGN19875 AGN22900 AGT06101 AIK85798 AIK88583
REF NP_601574 WP_003859290 WP_040967737

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