BMRB Entry 16982

Title:
Backbone assignment of the D-allose binding protein from Escherichia coli in the apo form
Deposition date:
2010-06-08
Original release date:
2010-08-19
Authors:
Millet, Oscar; Castano, David
Citation:

Citation: Castano, David; Millet, Oscar. "Backbone chemical shifts assignments of D: -allose binding protein in the free form and in complex with D: -allose."  Biomol. NMR Assignments 5, 31-34 (2011).
PubMed: 20711759

Assembly members:

Assembly members:
ALBP, polymer, 288 residues, 30385 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET11d

Data sets:
Data typeCount
13C chemical shifts775
15N chemical shifts266
1H chemical shifts266

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1D-allose binding protein1

Entities:

Entity 1, D-allose binding protein 288 residues - 30385 Da.

1   ALAALAGLUTYRALAVALVALLEULYSTHR
2   LEUSERASNPROPHETRPVALASPMETLYS
3   LYSGLYILEGLUASPGLUALALYSTHRLEU
4   GLYVALSERVALASPILEPHEALASERPRO
5   SERGLUGLYASPPHEGLNSERGLNLEUGLN
6   LEUPHEGLUASPLEUSERASNLYSASNTYR
7   LYSGLYILEALAPHEALAPROLEUSERSER
8   VALASNLEUVALMETPROVALALAARGALA
9   TRPLYSLYSGLYILETYRLEUVALASNLEU
10   ASPGLULYSILEASPMETASPASNLEULYS
11   LYSALAGLYGLYASNVALGLUALAPHEVAL
12   THRTHRASPASNVALALAVALGLYALALYS
13   GLYALASERPHEILEILEASPLYSLEUGLY
14   ALAGLUGLYGLYGLUVALALAILEILEGLU
15   GLYLYSALAGLYASNALASERGLYGLUALA
16   ARGARGASNGLYALATHRGLUALAPHELYS
17   LYSALASERGLNILELYSLEUVALALASER
18   GLNPROALAASPTRPASPARGILELYSALA
19   LEUASPVALALATHRASNVALLEUGLNARG
20   ASNPROASNILELYSALAILETYRCYSALA
21   ASNASPTHRMETALAMETGLYVALALAGLN
22   ALAVALALAASNALAGLYLYSTHRGLYLYS
23   VALLEUVALVALGLYTHRASPGLYILEPRO
24   GLUALAARGLYSMETVALGLUALAGLYGLN
25   METTHRALATHRVALALAGLNASNPROALA
26   ASPILEGLYALATHRGLYLEULYSLEUMET
27   VALASPALAGLULYSSERGLYLYSVALILE
28   PROLEUASPLYSALAPROGLUPHELYSLEU
29   VALASPSERILELEUVALTHRGLN

Samples:

sample_1: ALBP, [U-100% 13C; U-100% 15N; U-80% 2H], 800 uM; NaCl 150 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7.1; pressure: 1 atm; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1

Software:

NMRPipe, Delaglio, Zhengrong and Bax - processing

NMR spectrometers:

  • Varian DMX 500 MHz

Related Database Links:

BMRB 16984
PDB
DBJ BAE78091 BAG79910 BAI33528 BAI57509 BAJ45803
EMBL CAP78562 CAQ34437 CAR05747 CAR10927 CAR20617
GB AAA96987 AAC77049 AAN83519 ABE10091 ABG72275
REF NP_418512 WP_001046184 WP_001046185 WP_001046186 WP_001046187
SP P39265
AlphaFold P39265

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