BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 16688

Title: Solution NMR structure of the CPE1231(468-535) protein from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR82B.

Deposition date: 2010-01-21 Original release date: 2010-02-25

Authors: Yang, Yunhuang; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation: Yang, Yunhuang; Ramelot, Theresa; Lee, Dan; Ciccosanti, Colleen; Hamilton, Keith; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of the CPE1231(468-535) protein from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR82B."  .

Assembly members:
CpR82B, polymer, 76 residues, 8305 Da.

Natural source:   Common Name: not available   Taxonomy ID: 1502   Superkingdom: not available   Kingdom: Clostridium   Genus/species: perfringens not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21(DE3) pMGK' . . . . . . . . . . . . . . . 'pET 21-23C

Entity Sequences (FASTA):
CpR82B: AEKTGIVNVSSSLNVREGAS TSSKVIGSLSGNTKVTIVGE EGAFYKIEYKGSHGYVAKEY IKDIKDEVLEHHHHHH

Data sets:
Data typeCount
13C chemical shifts327
15N chemical shifts81
1H chemical shifts504

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1CpR82B1

Entities:

Entity 1, CpR82B 76 residues - 8305 Da.

CPE1231(468-535) protein from Clostridium perfringens, preceded by non-native N-terminal Met and followed by 8 non-native C-terminal residues (LEHHHHHH)

1   ALAGLULYSTHRGLYILEVALASNVALSER
2   SERSERLEUASNVALARGGLUGLYALASER
3   THRSERSERLYSVALILEGLYSERLEUSER
4   GLYASNTHRLYSVALTHRILEVALGLYGLU
5   GLUGLYALAPHETYRLYSILEGLUTYRLYS
6   GLYSERHISGLYTYRVALALALYSGLUTYR
7   ILELYSASPILELYSASPGLUVALLEUGLU
8   HISHISHISHISHISHIS

Samples:

NC_sample: CPE1231(468-535) protein' '[U-100% 13C; U-100% 15N] 0.1; .mM – 1; . mM; . 0.2 ± 16688 ; . 0.5 ± 16688 ; . 16688; . 16688; . 16688

NC5_sample: CPE1231(468-535) protein' '[U-5% 13C; U-100% 15N] 0.1; .mM – 1; . mM; . 0.2 ± 16688 ; . 0.5 ± 16688 ; . 16688; . 16688; . 16688

NC_sample_in_D2O: CPE1231(468-535) protein' '[U-100% 13C; U-100% 15N] 0.1; .mM – 1; . mM; . 0.2 ± 16688 ; . 0.5 ± 16688 ; . 16688; . 16688

sample_conditions_1: ionic strength: 0.2 M; pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC_CTNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC NOESYNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC_swN150ppmNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC_HiResNC5_sampleisotropicsample_conditions_1
2D 1H-13C HSQC_HiResNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQCNC5_sampleisotropicsample_conditions_1
2D 1H-13C HSQC_no_CTNC5_sampleisotropicsample_conditions_1
3D 1H-13C NOESY_aromNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC_HiResNC_sampleisotropicsample_conditions_1
2D 1H-15N HSQC_NH2onlyNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC_D2ONC_sample_in_D2Oisotropicsample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - data analysis

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, A., Assadi, A., Markley, J. L. & Eghbalnia, H. - autoassignment

Rosetta, David Baker - Performs de novo protein structure prediction

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz

Related Database Links:

PDB

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