BMRB Entry 15825

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PDB ID: 2k57
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15825
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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 Putative Lipoprotein from Pseudomonas syringae Gene Locus PSPTO2350. Northeast Structural Genomics Target PsR76A.

Deposition date:

2008-06-25

Original release date:

2008-07-14

Authors:

Hang, Dehua; Aramini, James; Rossi, Paolo; Wang, Dongyan; Jiang, Mei; Maglaqui, Melissa; Xiao, Rong; Liu, Jinfeng; Baran, Michael; Acton, Thomas; Rost, Burkhard; Montelione, Gaetano

Citation:

Citation: Rossi, Paolo; Aramini, James; Hang, Dehua; Xiao, Rong; Acton, Thomas; Montelione, Gaetano. "Solution NMR Structure of Putative Lipoprotein from Pseudomonas syringae Gene Locus PSPTO2350. Northeast Structural Genomics Target PsR76A" .

Assembly members:

Assembly members:
PsR76A, polymer, 55 residues, 6340.105 Da.

Natural source:

Natural source: Common Name: Pseudomonas syringae Taxonomy ID: 317 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas syringae

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PsR76A: MASPTVITLNDGREIQAVDT PKYDEESGFYEFKQLDGKQT RINKDQVRTVKDLLE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	246
15N chemical shifts	59
1H chemical shifts	390

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PsR76A	1

Entities:

Entity 1, PsR76A 55 residues - 6340.105 Da.

truncated lipobox: MKQRTLPAAFLLALSIASLAGC M1 cloning artifact A2 is residue 23 in original sequence

1

MET

ALA

SER

PRO

THR

VAL

ILE

THR

LEU

ASN

2

ASP

GLY

ARG

GLU

ILE

GLN

ALA

VAL

ASP

THR

3

PRO

LYS

TYR

ASP

GLU

SER

GLY

PHE

TYR

4

GLU

PHE

LYS

GLN

LEU

ASP

GLY

LYS

GLN

THR

5

ARG

ILE

ASN

LYS

ASP

GLN

VAL

ARG

THR

VAL

6

LYS

ASP

LEU

GLU

Samples:

sample_1: PsR76A, [U-100% 13C; U-100% 15N], 1.07 mM; DSS 50 uM; DTT 10 mM; sodium chloride 100 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_2: PsR76A, [5% 13C; U-100% 15N], 1.07 mM; DSS 50 uM; DTT 10 mM; sodium chloride 100 mM; sodium azide 0.02%; MES 20 mM; calcium chloride 5 mM; H2O 90%; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC (aliph)	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC CT ARO	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D 1H-13C-15N SIM NOESY	sample_1	isotropic	sample_conditions_1
N15-T1	sample_1	isotropic	sample_conditions_1
N15-T2(CPMG)	sample_1	isotropic	sample_conditions_1
3J NHHA	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CC(CO)NH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H, 15N HETNOE	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC STEREO	sample_2	isotropic	sample_conditions_1

Software:

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

AutoAssign v2.4.0, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

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

TOPSPIN v2.1, Bruker Biospin - collection

SPARKY v3.113, Goddard - data analysis

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

RPF(AutoStructure) v2.2.1, Huang, Tejero, Powers and Montelione - validation

Molmol, Koradi, Billeter and Wuthrich - visualization

PSVS, Bhattacharya and Montelione - validation

PDBStat v5.0, Tejero R.; Montelione GT - validation

MolProbity, Richardson - validation

Procheck, Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho - validation

NMR spectrometers:

Varian INOVA 600 MHz
Bruker Avance 800 MHz

SWS	Q883K7_PSESM
PDB	2K57
GB	AAZ36497 ALD96182 EFH99818 EFW80354 EFW84604
REF	WP_002553129 WP_044343779 WP_054995082 WP_057446476