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Biological Magnetic Resonance Data Bank


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BMRB Entry 17359

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17359
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Title: Solution NMR Structure of protein CD1104.2 from Clostridium difficile, Northeast Structural Genomics Consortium Target CfR130

Deposition date: 2010-12-13 Original release date: 2011-01-05

Authors: Pulavarti, Surya Venkata SRK; Eletsky, Alexander; Mills, Jeffrey; Sukumaran, Dinesh; Wang, Huang; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation: Pulavarti, Surya Venkata SRK; Eletsky, Alexander; Mills, Jeffrey; Sukumaran, Dinesh; Wang, Huang; Ciccosanti, Colleen; Janjua, Haleema; Acton, Thomas; Xiao, Rong; Everett, John; Lee, Hsiau-Wei; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of protein CD1104.2 from Clostridium difficile, Northeast Structural Genomics Consortium Target CfR130"  To be published ., .-..

Assembly members:
CfR130, polymer, 76 residues, 8751.025 Da.

Natural source:   Common Name: Clostridium difficile   Taxonomy ID: 1496   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Clostridium difficile

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

Entity Sequences (FASTA):
CfR130: MIRLTIEETNLLSIYNEGGK RGLMENINAALPFMDEDMRE LAKRTLAKIAPLTENEYAEL AIFAADEVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts314
15N chemical shifts74
1H chemical shifts523

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CfR1301

Entities:

Entity 1, CfR130 76 residues - 8751.025 Da.

1   METILEARGLEUTHRILEGLUGLUTHRASN
2   LEULEUSERILETYRASNGLUGLYGLYLYS
3   ARGGLYLEUMETGLUASNILEASNALAALA
4   LEUPROPHEMETASPGLUASPMETARGGLU
5   LEUALALYSARGTHRLEUALALYSILEALA
6   PROLEUTHRGLUASNGLUTYRALAGLULEU
7   ALAILEPHEALAALAASPGLUVALLEUGLU
8   HISHISHISHISHISHIS

Samples:

sample_4: CfR130, [U-5% 13C; U-100% 15N], 1.68 mM; MES 20 mM; sodium chloride 100 mM; sodium azide 0.02%; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; D2O 10%; H2O 90%; Pf1 phage 13.2 mg/ml

sample_1: CfR130, [U-100% 13C; U-100% 15N], 1.61 mM; MES 20 mM; sodium chloride 100 mM; sodium azide 0.02%; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; D2O 5%; H2O 95%

sample_2: CfR130, [U-5% 13C; U-100% 15N], 1.68 mM; MES 20 mM; sodium chloride 100 mM; sodium azide 0.02%; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; D2O 5%; H2O 95%

sample_3: CfR130, [U-5% 13C; U-100% 15N], 1.68 mM; MES 20 mM; sodium chloride 100 mM; sodium azide 0.02%; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; D2O 10%; H2O 90%; PEG 4%

sample_conditions_1: ionic strength: 0.11 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
(4,3)D GFT-HNCACBCAsample_1isotropicsample_conditions_1
(4,3)D GFT-CBCACA(CO)NHNsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D GFT HCCH-COSY-alisample_1isotropicsample_conditions_1
3D GFT HCCH-COSY-arosample_1isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSY-alisample_1isotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticsample_2isotropicsample_conditions_1
(4,3)D GFT-HABCAB(CO)NHNsample_1isotropicsample_conditions_1
2D 1H-15N J-modulated HSQCsample_3anisotropicsample_conditions_1
2D 1H-15N J-modulated HSQCsample_4anisotropicsample_conditions_1

Software:

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

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

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

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

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

VNMRJ, Varian - collection

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

CARA v1.8.4, Keller and Wuthrich - data analysis

PROSA v6.4, Guntert - processing

PSVS, Bhattacharya and Montelione - analysis of structure

NMR spectrometers:

  • Varian INOVA 500 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz

Related Database Links:

PDB
EMBL CAJ67952 CCL09941 CCL67833 CCL71552 CCL94504
GB AJP10794 EQE02915
REF WP_011861106 WP_021361577 WP_032509728 YP_001087591

Download simulated HSQC data in one of the following formats:
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