BMRB Entry 16647

Name: Solution NMR structure of SH3 domain from CPF_0587 (fragment 415-479) from Clostridium perfringens. Northeast Structural Genomics Consortium (NESG) Target CpR74A.
Published: 2010-01-06

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PDB ID: 2krs
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16647
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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of SH3 domain from CPF_0587 (fragment 415-479) from Clostridium perfringens. Northeast Structural Genomics Consortium (NESG) Target CpR74A.

Deposition date:

2009-12-22

Original release date:

2010-01-06

Authors:

Ramelot, Theresa; Cort, John; Maglaqui, Melissa; Ciccosanti, Colleen; Janjua, Haleema; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Cort, John; Maglaqui, Melissa; Ciccosanti, Colleen; Janjua, Haleema; Nair, R; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of SH3 domain from CPF_0587 (fragment 415-479) from Clostridium perfringens. Northeast Structural Genomics Consortium (NESG) Target CpR74A." .

Assembly members:

Assembly members:
CPF_0587-SH3, polymer, 74 residues, 8300 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: pET21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
CPF_0587-SH3: MQGVVKVNSALNMRSGPGSN YGVIGTLRNNDKVEIIKEVD GWYEIRFNGKVGYASKSYIT IVNEGSLEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	307
15N chemical shifts	76
1H chemical shifts	482

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	CPF_0587-SH3	1

Entities:

Entity 1, CPF_0587-SH3 74 residues - 8300 Da.

1 non-native residue at the C-term (M). 8 non-native residues at C-terminus (LEHHHHHH)

1

MET

GLN

GLY

VAL

LYS

VAL

ASN

SER

ALA

2

LEU

ASN

MET

ARG

SER

GLY

PRO

GLY

SER

ASN

3

TYR

GLY

VAL

ILE

GLY

THR

LEU

ARG

ASN

4

ASP

LYS

VAL

GLU

ILE

LYS

GLU

VAL

ASP

5

GLY

TRP

TYR

GLU

ILE

ARG

PHE

ASN

GLY

LYS

6

VAL

GLY

TYR

ALA

SER

LYS

SER

TYR

ILE

THR

7

ILE

VAL

ASN

GLU

GLY

SER

LEU

GLU

HIS

8

HIS

Samples:

NC_sample: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 0.8 ± .05 mM

NC_sample_in_D2O: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; protein, [U-100% 13C; U-100% 15N], 0.8 ± .05 mM

NC5: MES 20 ± 1 mM; sodium chloride 100 ± 10 mM; calcium chloride 5 ± .25 mM; DTT 10 ± .5 mM; sodium azide 0.02 ± .001 %; protein, [U-5% 13C; U-100% 15N], 0.9 ± .05 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; 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	NC_sample	isotropic	sample_conditions_1
3D 1H-15N NOESY	NC_sample	isotropic	sample_conditions_1
3D 1H-13C NOESY aliph	NC_sample	isotropic	sample_conditions_1
3D HNCO	NC_sample	isotropic	sample_conditions_1
3D HN(CO)CA	NC_sample	isotropic	sample_conditions_1
3D CBCA(CO)NH	NC_sample	isotropic	sample_conditions_1
3D HNCACB	NC_sample	isotropic	sample_conditions_1
3D HBHA(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 HCCH NOESY	NC_sample_in_D2O	isotropic	sample_conditions_1
3D 1H-13C NOESY arom	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC swN	NC_sample	isotropic	sample_conditions_1
2D 1H-15N HSQC NH2 only	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC_sample	isotropic	sample_conditions_1
T1 1D array	NC_sample	isotropic	sample_conditions_1
T1 rho 1D array	NC_sample	isotropic	sample_conditions_1
3D (H)CCONH	NC_sample	isotropic	sample_conditions_1
3D CCONH	NC_sample	isotropic	sample_conditions_1
2D 1H-13C HSQC in D2O	NC_sample_in_D2O	isotropic	sample_conditions_1
2D 1H-13C HSQC long ct	NC5	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

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

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

NMR spectrometers:

Varian INOVA 600 MHz
Bruker AvanceIII 850 MHz