BMRB Entry 16688

Name: Solution NMR structure of the CPE1231(468-535) protein from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR82B.
Published: 2010-02-25

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PDB ID: 2kt8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16688
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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:

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:

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

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET 21-23C

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	327
15N chemical shifts	81
1H chemical shifts	504

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CpR82B	1

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

ALA

GLU

LYS

THR

GLY

ILE

VAL

ASN

VAL

SER

2

SER

LEU

ASN

VAL

ARG

GLU

GLY

ALA

SER

3

THR

SER

LYS

VAL

ILE

GLY

SER

LEU

SER

4

GLY

ASN

THR

LYS

VAL

THR

ILE

VAL

GLY

GLU

5

GLU

GLY

ALA

PHE

TYR

LYS

ILE

GLU

TYR

LYS

6

GLY

SER

HIS

GLY

TYR

VAL

ALA

LYS

GLU

TYR

7

ILE

LYS

ASP

ILE

LYS

ASP

GLU

VAL

LEU

GLU

8

HIS

Samples:

NC_sample: CPE1231(468-535) protein, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

NC5_sample: CPE1231(468-535) protein, [U-5% 13C; U-100% 15N], 1 ± 0.1 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

NC_sample_in_D2O: CPE1231(468-535) protein, [U-100% 13C; U-100% 15N], 1.0 ± 0.1 mM; ammonium acetate 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; D2O 100%

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

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC_CT	NC5_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HNCA	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
3D HBHA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D H(CCO)NH	NC_sample	isotropic	sample_conditions_1
3D C(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HCCH-TOCSY	NC_sample	isotropic	sample_conditions_1
3D HCCH-COSY	NC_sample	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	NC_sample_in_D2O	isotropic	sample_conditions_1
4D CC NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-15N HSQC_swN150ppm	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC_HiRes	NC5_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC_HiRes	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC	NC5_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC_no_CT	NC5_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY_arom	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC_HiRes	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC_NH2only	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC_D2O	NC_sample_in_D2O	isotropic	sample_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