BMRB Entry 18555

Name: NMR solution structure of PA1075 from Pseudomonas Aeruginosa
Published: 2013-06-28

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PDB ID: 2lv5
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR18555
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

NMR solution structure of PA1075 from Pseudomonas Aeruginosa

Deposition date:

2012-06-29

Original release date:

2013-06-28

Authors:

Sunnerhagen, Maria; Schnell, Robert; Andresen, Cecilia; Moshref, Ahmad; Schneider, Gunter

Citation:

Citation: Sunnerhagen, Maria. "NMR solution structure of PA1075, an essential protein in Pseudomonas Aeruginosa" .

Assembly members:

Assembly members:
entity, polymer, 108 residues, 11629.234 Da.

Natural source:

Natural source: Common Name: Pseudomonas aeruginosa Taxonomy ID: 287 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GSHMTEQTSTLYAKLLGETA VISWAELQPFFARGALLQVD AALDLVEVAEALAGDDREKV AAWLSGGGLSKVGEDAAKDF LERDPTLWAVVVAPWVVIQE RAEKATLH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	429
15N chemical shifts	105
1H chemical shifts	692

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PA1075	1

Entities:

Entity 1, PA1075 108 residues - 11629.234 Da.

1

GLY

SER

HIS

MET

THR

GLU

GLN

THR

SER

THR

2

LEU

TYR

ALA

LYS

LEU

GLY

GLU

THR

ALA

3

VAL

ILE

SER

TRP

ALA

GLU

LEU

GLN

PRO

PHE

4

PHE

ALA

ARG

GLY

ALA

LEU

GLN

VAL

ASP

5

ALA

LEU

ASP

LEU

VAL

GLU

VAL

ALA

GLU

6

ALA

LEU

ALA

GLY

ASP

ARG

GLU

LYS

VAL

7

ALA

TRP

LEU

SER

GLY

LEU

SER

8

LYS

VAL

GLY

GLU

ASP

ALA

LYS

ASP

PHE

9

LEU

GLU

ARG

ASP

PRO

THR

LEU

TRP

ALA

VAL

10

VAL

ALA

PRO

TRP

VAL

ILE

GLN

GLU

11

ARG

ALA

GLU

LYS

ALA

THR

LEU

HIS

Samples:

sample_1: PA1075, [U-100% 13C; U-100% 15N], 0.5-0.7 mM; TRIS 12.5 mM; sodium chloride 75 mM

sample_conditions_1: ionic strength: 165 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D CCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

SPARKY, Goddard - data analysis

ABACUS, Lemak and Arrowsmith - chemical shift assignment, data analysis, structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

MDD, Orekhov - collection, processing

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks