BMRB Entry 30079

Name: NMR structure of Uncharacterized protein from Pseudomonas aeruginosa PAO1
Published: 2016-06-09

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PDB ID: 5jtk
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30079
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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:

NMR structure of Uncharacterized protein from Pseudomonas aeruginosa PAO1

Deposition date:

2016-05-09

Original release date:

2016-06-09

Authors:

Barnwal, R.; Varani, G.; Seattle Structural Genomics Center for Infectious Disease (SSGCID), SSGCID

Citation:

Citation: Barnwal, R.; Varani, G.. "NMR structure of Uncharacterized protein from Pseudomonas aeruginosa PAO1" .

Assembly members:

Assembly members:
Uncharacterized protein, polymer, 94 residues, 10693.325 Da.

Natural source:

Natural source: Common Name: g-proteobacteria Taxonomy ID: 208964 Superkingdom: Bacteria Kingdom: not available Genus/species: not available not available

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Uncharacterized protein: MTPIEYIDRALALVVDRLAR YPGYEVLLSAEKQLQYIRSV LLDRSLDRSALHRLTLGSIA VKEFDETDPELSRALKDAYY VGIRTGRGLKVDLP

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1
spectral_peak_list

Data type	Count
13C chemical shifts	413
15N chemical shifts	91
1H chemical shifts	622

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 94 residues - 10693.325 Da.

1

MET

THR

PRO

ILE

GLU

TYR

ILE

ASP

ARG

ALA

2

LEU

ALA

LEU

VAL

ASP

ARG

LEU

ALA

ARG

3

TYR

PRO

GLY

TYR

GLU

VAL

LEU

SER

ALA

4

GLU

LYS

GLN

LEU

GLN

TYR

ILE

ARG

SER

VAL

5

LEU

ASP

ARG

SER

LEU

ASP

ARG

SER

ALA

6

LEU

HIS

ARG

LEU

THR

LEU

GLY

SER

ILE

ALA

7

VAL

LYS

GLU

PHE

ASP

GLU

THR

ASP

PRO

GLU

8

LEU

SER

ARG

ALA

LEU

LYS

ASP

ALA

TYR

9

VAL

GLY

ILE

ARG

THR

GLY

ARG

GLY

LEU

LYS

10

VAL

ASP

LEU

PRO

Samples:

sample_1: Uncharacterized protein, [U-98% 13C; U-98% 15N], 1.1 mM; H2O 95%; D2O 5%; NaCl 100 mM; MES 20 mM

sample_conditions_1: ionic strength: 100 mM; pH: 6.0; 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	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment, peak picking

TOPSPIN, Bruker Biospin - collection, processing

CYANA v3.97, GUNTERT, MUMENTHALER AND WUTHRICH - refinement, structure calculation

NMR spectrometers:

Bruker AvanceII 600 MHz
Bruker AvanceIII 800 MHz

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