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Biological Magnetic Resonance Data Bank


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BMRB Entry 17319

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17319
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Title: NMR solution structure of the protein NP_253742.1

Deposition date: 2010-11-23 Original release date: 2010-12-16

Authors: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt

Citation: Mohanty, Biswaranjan; Serrano, Pedro; Geralt, Michael; Horst, Reto; Wuthrich, Kurt. "NMR solution structure of the protein NP_253742.1"  Not known ., .-..

Assembly members:
NP_253742.1, polymer, 124 residues, 13726.535 Da.

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

Entity Sequences (FASTA):
NP_253742.1: GMRIPSAIQLHKASKTLTLR YGEDSYDLPAEFLRVHSPSA EVQGHGNPVLQYGKLNVGLV GVEPAGQYALKLSFDDGHDS GLFTWDYLYELATRKDQLWA DYLAELASAGKSRDPDESVV KLML

Data sets:
Data typeCount
13C chemical shifts479
15N chemical shifts126
1H chemical shifts818

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NP_253742.11

Entities:

Entity 1, NP_253742.1 124 residues - 13726.535 Da.

1   GLYMETARGILEPROSERALAILEGLNLEU
2   HISLYSALASERLYSTHRLEUTHRLEUARG
3   TYRGLYGLUASPSERTYRASPLEUPROALA
4   GLUPHELEUARGVALHISSERPROSERALA
5   GLUVALGLNGLYHISGLYASNPROVALLEU
6   GLNTYRGLYLYSLEUASNVALGLYLEUVAL
7   GLYVALGLUPROALAGLYGLNTYRALALEU
8   LYSLEUSERPHEASPASPGLYHISASPSER
9   GLYLEUPHETHRTRPASPTYRLEUTYRGLU
10   LEUALATHRARGLYSASPGLNLEUTRPALA
11   ASPTYRLEUALAGLULEUALASERALAGLY
12   LYSSERARGASPPROASPGLUSERVALVAL
13   LYSLEUMETLEU

Samples:

sample_1: sodium chloride 50 mM; sodium phosphate 20 mM; sodium azide 4.5 mM; protein-NP_253742.1, [U-98% 13C; U-98% 15N], 1.2 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 0.113 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
4D APSY-HACANHsample_1isotropicsample_conditions_1
5D APSY-HACACONHsample_1isotropicsample_conditions_1
5D APSY-CBCACONHsample_1isotropicsample_conditions_1
15N resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Cali resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
13Caro resolved [1H,1H]-NOESYsample_1isotropicsample_conditions_1
15 N {1H} - NOEsample_1isotropicsample_conditions_1

Software:

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure solution

UNIO v2.0.1, Herrmann and Wuthrich - structure solution

OPAL, Luginbuhl, Guntert, Billeter and Wuthrich - energy refinement

CARA, Keller and Wuthrich - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - Acquisition, data analysis, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAK87347 BAP24871 BAP53641 BAQ42904 BAR70520
EMBL CAA47150 CAW30199 CCQ86077 CDH73800 CDH80121
GB AAG08440 AAT49749 ABJ14439 AEO77648 AFM67617
REF NP_253742 WP_003095857 WP_003121209 WP_003125656 WP_003135779

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts