BMRB Entry 15203

Name: NMR Structure of Clostridium Perfringens Protein CPE0013. Northeast Structural Genomics Target CpR31.
Published: 2007-05-04

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PDB ID: 2jov
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15203
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR Structure of Clostridium Perfringens Protein CPE0013. Northeast Structural Genomics Target CpR31.

Deposition date:

2007-04-04

Original release date:

2007-05-04

Authors:

Ding, Keyang; Ramelot, Theresa; Anklin, Clemens; Wang, Huang; Nwosu, Chioma; Cunningham, Kellie; Ma, Li-Chung; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, Gurla; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Ding, Keyang; Ramelot, Theresa; Wang, Huang; Nwosu, Chioma; Montelione, Gaetano; Kennedy, Michael. "NMR structure of Clostridium perfringens protein CPE0013." .

Assembly members:

Assembly members:
CPE0013, polymer, 85 residues, 9683.400 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CPE0013: MHKDIFTSVVRVRGSKKYNV VPVKSNKPVEISKWIDFSNV LSRLYVGVPTKSGNVVCKNI MNTGVDIICTKNLPKDSLEH HHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	347
15N chemical shifts	80
1H chemical shifts	569

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CPE0013	1

Entities:

Entity 1, CPE0013 85 residues - 9683.400 Da.

The full sequence is cloned with his-tag LEHHHHHH added at the C-terminal.

1

MET

HIS

LYS

ASP

ILE

PHE

THR

SER

VAL

2

ARG

VAL

ARG

GLY

SER

LYS

TYR

ASN

VAL

3

VAL

PRO

VAL

LYS

SER

ASN

LYS

PRO

VAL

GLU

4

ILE

SER

LYS

TRP

ILE

ASP

PHE

SER

ASN

VAL

5

LEU

SER

ARG

LEU

TYR

VAL

GLY

VAL

PRO

THR

6

LYS

SER

GLY

ASN

VAL

CYS

LYS

ASN

ILE

7

MET

ASN

THR

GLY

VAL

ASP

ILE

CYS

THR

8

LYS

ASN

LEU

PRO

LYS

ASP

SER

LEU

GLU

HIS

9

HIS

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1

PDB	2JOV
DBJ	BAB79719
EMBL	CUO73046
GB	ABG83544 ABG87799 ALG47387 EDS80569 EDT15029
REF	WP_003450903

BMRB Entry 15203

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers:

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