BMRB Entry 19632

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:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: SpeedET

Experimental source:

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

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts241
15N chemical shifts73
1H chemical shifts514

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 84921

Entities:

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

1   GLYALAASPASPASPALAPROSERGLYGLU
2   PROASPVALTHRILEARGGLNGLUGLYASP
3   LYSTHRILEGLNGLUTYRARGVALASNGLY
4   PHELEUTYRALAILELYSVALVALPROLYS
5   HISGLYLYSPROTYRPHELEUVALARGALA
6   ASPGLYSERASPGLYASNPHEILEARGSER
7   ASPGLNPROASPLYSLEUILEPROGLNTRP
8   GLUILEPHESERTRP

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:

NameSampleSample stateSample conditions
APSY 4D-HACANHsample_1isotropicsample_conditions_1
APSY 5D-HACACONHsample_1isotropicsample_conditions_1
APSY 5D-CBCACONHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_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

Related Database Links:

PDB
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

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