BMRB Entry 19851

Title:
NMR structure of the protein YP_001712342.1 from Acinetobacter baumannii
Deposition date:
2014-03-14
Original release date:
2014-04-22
Authors:
Proudfoot, Andrew; Serrano, Pedro; Geralt, Michael; Wuthrich, Kurt
Citation:

Citation: Proudfoot, Andrew; Wuthrich, Kurt; Serrano, Pedro; Geralt, Michael; Dutta, Samit. "NMR structure of the protein YP_002937094.1 from Eubacterium rectale"  .

Assembly members:

Assembly members:
entity, polymer, 107 residues, 12156.859 Da.

Natural source:

Natural source:   Common Name: Acinetobacter baumannii   Taxonomy ID: 470   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Acinetobacter baumannii

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts362
15N chemical shifts115
1H chemical shifts750

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 107 residues - 12156.859 Da.

1   GLYTHRASPPHEGLYTHRTHRASNASNPHE
2   VALSERPROASNLEUGLNLEULYSGLNASN
3   VALLEUPROPROTHRPROLYSASNILEPRO
4   LEUPROALAPHEGLYGLNARGILEILEGLY
5   TRPGLYTHRGLYALAGLUGLYALAARGGLN
6   ARGLEUGLUASNILEGLNPROALAASPVAL
7   SERMETILELYSLYSGLNGLYTHRTHRLEU
8   GLUMETILETHRALATRPGLNASPPHETYR
9   GLUGLNGLUGLNGLNARGASNGLUASNASN
10   PROTHRALALYSTYRARGALAARGLEUMET
11   LYSLYSILEALAASPLEUTRP

Samples:

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

sample_conditions_1: ionic strength: 0.220 M; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

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

Software:

CYANA, Bruker Biospin, Guntert P. - chemical shift assignment, collection, processing, refinement

UNIO, Herrmann and Wuthrich - chemical shift assignment, structure solution

Opalp, Luginbuhl, Guntert, Billeter and Wuthrich - refinement

CARA, Keller and Wuthrich - chemical shift assignment, refinement

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

MDDNMR, Maxim Mayzel, Vladislav Orekhov - processing

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAN88776 BAP67935
EMBL CAM87951 CAP02179 CDG77613 CQR69588 CQR89098
GB ABS89932 ACJ40142 ACJ58428 ADX02293 ADX91089
REF WP_000266118 WP_000266120 WP_000266121 WP_000266122 WP_000266123

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