BMRB Entry 19632

Name: NMR structure of protein NP_254181.1 from Pseudomonas aeruginosa PA01
Published: 2013-12-20

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PDB ID: 2mhg
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19632
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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 protein NP_254181.1 from Pseudomonas aeruginosa PA01

Deposition date:

2013-11-22

Original release date:

2013-12-20

Authors:

Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt

Citation:

Citation: Dutta, Samit; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt. "NMR structure of protein NP_254181.1 from Pseudomonas aeruginosa PA01" .

Assembly members:

Assembly members:
entity, polymer, 75 residues, 7154.342 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: SpeedET

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GADDDAPSGEPDVTIRQEGD KTIQEYRVNGFLYAIKVVPK HGKPYFLVRADGSDGNFIRS DQPDKLIPQWEIFSW

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	241
15N chemical shifts	73
1H chemical shifts	514

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492	1

Entities:

Entity 1, hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492 75 residues - 7154.342 Da.

1

GLY

ALA

ASP

ALA

PRO

SER

GLY

GLU

2

PRO

ASP

VAL

THR

ILE

ARG

GLN

GLU

GLY

ASP

3

LYS

THR

ILE

GLN

GLU

TYR

ARG

VAL

ASN

GLY

4

PHE

LEU

TYR

ALA

ILE

LYS

VAL

PRO

LYS

5

HIS

GLY

LYS

PRO

TYR

PHE

LEU

VAL

ARG

ALA

6

ASP

GLY

SER

ASP

GLY

ASN

PHE

ILE

ARG

SER

7

ASP

GLN

PRO

ASP

LYS

LEU

ILE

PRO

GLN

TRP

8

GLU

ILE

PHE

SER

TRP

Samples:

sample_1: entity, [U-99% 13C; U-98% 15N], 1.2 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM

sample_2: entity, [U-99% 13C; U-98% 15N], 0.6 mM; sodium phosphate 20 mM; sodium chloride 50 mM; sodium azide 5 mM; entity, [U-15N; U-2H], 0.6 mM

sample_conditions_1: ionic strength: 0.0798 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
APSY 4D-HACANH	sample_1	isotropic	sample_conditions_1
APSY 5D-HACACONH	sample_1	isotropic	sample_conditions_1
APSY 5D-CBCACONH	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
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1

Software:

CNS, Bruker Biospin, Brunger A. T. et.al. - collection, processing, refinement

CARA, Keller and Wuthrich - chemical shift assignment, data analysis

j-UNIO, Herrmann, Guntert and Wuthrich - chemical shift assignment, data analysis, peak picking

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - collection

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2MHG
DBJ	BAK93077 BAP25407 BAP54205 BAQ43445 BAR70992
EMBL	CAW30644 CCQ84532 CDH74259 CDH80608 CDI94117
GB	AAG08879 AAT49351 ABJ14880 ABR84127 AEO78092
REF	NP_254181 WP_003096984 WP_003155462 WP_003161101 WP_017002432