BMRB Entry 15604

Name: Solution NMR structure of Ssl0352 protein from Synechocystis sp. - Northeast Structural Genomics Consortium target SgR42
Published: 2008-03-07

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PDB ID: 2jz2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15604
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of Ssl0352 protein from Synechocystis sp. - Northeast Structural Genomics Consortium target SgR42

Deposition date:

2007-12-22

Original release date:

2008-03-07

Authors:

Eletsky, Alexander; Sukumaran, Dinesh; Wang, Dongyan; Hamilton, Keith; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano; Szyperski, Thomas

Citation:

Citation: Eletsky, Alexander; Sukumaran, Dinesh; Wang, Dongyan; Hamilton, Keith; Foote, Erica; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Swapna, G.V.T; Rost, Burkhard; Acton, Thomas; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR structure of Ssl0352 protein from Synechocystis sp." Proteins: Struct. Funct. Genet. ., .-..

Assembly members:

Assembly members:
SgR42_protein, polymer, 66 residues, 7657.740 Da.

Natural source:

Natural source: Common Name: Synechocystis sp. Taxonomy ID: 1143 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis sp.

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SgR42_protein: MIFPGATVRVTNVDDTYYRF EGLVQRVSDGKAAVLFENGN WDKLVTFRLSELEAVKPILE HHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	268
15N chemical shifts	66
1H chemical shifts	446

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SgR42_protein	1

Entities:

Entity 1, SgR42_protein 66 residues - 7657.740 Da.

C-terminal His-tag LEHHHHHH

1

MET

ILE

PHE

PRO

GLY

ALA

THR

VAL

ARG

VAL

2

THR

ASN

VAL

ASP

THR

TYR

ARG

PHE

3

GLU

GLY

LEU

VAL

GLN

ARG

VAL

SER

ASP

GLY

4

LYS

ALA

VAL

LEU

PHE

GLU

ASN

GLY

ASN

5

TRP

ASP

LYS

LEU

VAL

THR

PHE

ARG

LEU

SER

6

GLU

LEU

GLU

ALA

VAL

LYS

PRO

ILE

LEU

GLU

7

HIS

Samples:

NC: SgR42 protein, [U-100% 13C; U-100% 15N], 1.17 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.03%

NC5: SgR42 protein, [U-5% 13C; U-100% 15N], 1.17 mM; calcium chloride 5 mM; sodium chloride 100 mM; ammonium acetate 20 mM; DTT 10 mM; sodium azide 0.03%

sample_conditions_1: ionic strength: 135 mM; pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aliphatic	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC aromatic	NC	isotropic	sample_conditions_1
3D HNCO	NC	isotropic	sample_conditions_1
(4,3)D GFT CABCA(CO)NHN	NC	isotropic	sample_conditions_1
(4,3)D GFT HNNCABCA	NC	isotropic	sample_conditions_1
(4,3)D GFT HABCAB(CO)NHN	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY aliphatic	NC	isotropic	sample_conditions_1
3D HCCH-TOCSY aliphatic	NC	isotropic	sample_conditions_1
(4,3)D GFT HCCH-COSY aromatic	NC	isotropic	sample_conditions_1
3D 1H-15N,13C NOESY	NC	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC 28ms methyl	NC5	isotropic	sample_conditions_1
2D 1H-13C CT-HSQC 56ms methyl	NC5	isotropic	sample_conditions_1

Software:

VNMRJ v2.1B, Varian - collection

PROSA v6.0.2, Guntert - processing

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, peak picking

CSI v2.0, Wishart and Sykes - data analysis

TALOS, Cornilescu, Delaglio and Bax - data analysis

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AutoStruct v2.1.1, Huang, Tejero, Powers and Montelione - structure solution

AutoAssign v1.15.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

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

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

NMR spectrometers:

Varian INOVA 750 MHz
Varian INOVA 600 MHz

PDB	2JZ2 3C4S
DBJ	BAA10423 BAK51208 BAL30206 BAL33375 BAL36544
GB	AGF52715