BMRB Entry 18468

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PDB ID: 2lte
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18468
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution NMR structure of the specialized acyl carrier protein PA3334 (apo) from Pseudomonas aeruginosa. Northeast Structural Genomics Consortium Target PaT415.

Deposition date:

2012-05-16

Original release date:

2012-07-11

Authors:

Ramelot, Theresa; Cort, John; Yang, Yunhuang; Garcia, Maite; Yee, Adelinda; Arrowsmith, Cheryl; Kennedy, Michael

Citation:

Citation: Ramelot, Theresa; Cort, John; Yang, Yunhuang; Garcia, Maite; Yee, Adelinda; Arrowsmith, Cheryl; Kennedy, Michael. "Solution NMR structure of the specialized acyl carrier protein PA3334 (apo) from Pseudomonas aeruginosa. Northeast Structural Genomics Consortium Target PaT415." .

Assembly members:

Assembly members:
PaT415, polymer, 103 residues, 12.2 Da.

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 297 Superkingdom: Bacteria Kingdom: not available Genus/species: Pseudomonas aeruginosa

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: p11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
PaT415: MGSSHDHHHHSSGRENLYFQ GHMPNDMEDHLLTVLSVASG VPKEEISRDSRMEDLAFDSL VVSELSLKLRKEFGVTGVDD ELDLLETVDELFQLVEKHRA AGS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	370
15N chemical shifts	76
1H chemical shifts	596

Time Domain Data

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	PaT415	1

Entities:

Entity 1, PaT415 103 residues - 12.2 Da.

1

MET

GLY

SER

HIS

ASP

HIS

2

SER

GLY

ARG

GLU

ASN

LEU

TYR

PHE

GLN

3

GLY

HIS

MET

PRO

ASN

ASP

MET

GLU

ASP

HIS

4

LEU

THR

VAL

LEU

SER

VAL

ALA

SER

GLY

5

VAL

PRO

LYS

GLU

ILE

SER

ARG

ASP

SER

6

ARG

MET

GLU

ASP

LEU

ALA

PHE

ASP

SER

LEU

7

VAL

SER

GLU

LEU

SER

LEU

LYS

LEU

ARG

8

LYS

GLU

PHE

GLY

VAL

THR

GLY

VAL

ASP

9

GLU

LEU

ASP

LEU

GLU

THR

VAL

ASP

GLU

10

LEU

PHE

GLN

LEU

VAL

GLU

LYS

HIS

ARG

ALA

11

ALA

GLY

SER

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	anisotropic	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
4D 1H-13C-13C-1H NOESY in D2O	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY in D2O	sample_1	isotropic	sample_conditions_1

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

BMRB Entry 18468

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: