BMRB Entry 19143

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR19143
MolProbity Validation Chart

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Title:
Solution structure of the Escherichia coli apo ferric enterobactin binding protein
Deposition date:
2013-04-05
Original release date:
2014-04-28
Authors:
Chu, Byron; Otten, Renee; Krewulak, Karla; Mulder, Frans; Vogel, Hans
Citation:

Citation: Chu, Byron; Otten, Renee; Krewulak, Karla; Mulder, Frans; Vogel, Hans. "The structure, binding properties, and dynamics of the 34 kDa bacterial siderophore binding protein FepB in solution."  .

Assembly members:

Assembly members:
FepB, polymer, 315 residues, 31590.873 Da.

Natural source:

Natural source:   Common Name: Eenterobacteria   Taxonomy ID: 562   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-19

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FepB: MGHHHHHHHHHHSGHIDDDD KHMADWPRQITDSRGTHTLE SQPQRIVSTSVTLTGSLLAI DAPVIASGATTPNNRVADDQ GFLRQWSKVAKERKLQRLYI GEPSAEAVAAQMPDLILISA TGGDSALALYDQLSTIAPTL IINYDDKSWQSLLTQLGEIT GHEKQAAERIAQFDKQLAAA KEQIKLPPQPVTAIVYTAAA HSANLWTPESAQGQMLEQLG FTLAKLPAGLNASQSQGKRH DIIQLGGENLAAGLNGESLF LFAGDQKDADAIYANPLLAH LPAVQNKQVYALGTETFRLD YYSAMQVLDRLKALF

Data sets:
Data typeCount
13C chemical shifts860
15N chemical shifts268
1H chemical shifts268

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FepB1

Entities:

Entity 1, FepB 315 residues - 31590.873 Da.

1   METGLYHISHISHISHISHISHISHISHIS
2   HISHISSERGLYHISILEASPASPASPASP
3   LYSHISMETALAASPTRPPROARGGLNILE
4   THRASPSERARGGLYTHRHISTHRLEUGLU
5   SERGLNPROGLNARGILEVALSERTHRSER
6   VALTHRLEUTHRGLYSERLEULEUALAILE
7   ASPALAPROVALILEALASERGLYALATHR
8   THRPROASNASNARGVALALAASPASPGLN
9   GLYPHELEUARGGLNTRPSERLYSVALALA
10   LYSGLUARGLYSLEUGLNARGLEUTYRILE
11   GLYGLUPROSERALAGLUALAVALALAALA
12   GLNMETPROASPLEUILELEUILESERALA
13   THRGLYGLYASPSERALALEUALALEUTYR
14   ASPGLNLEUSERTHRILEALAPROTHRLEU
15   ILEILEASNTYRASPASPLYSSERTRPGLN
16   SERLEULEUTHRGLNLEUGLYGLUILETHR
17   GLYHISGLULYSGLNALAALAGLUARGILE
18   ALAGLNPHEASPLYSGLNLEUALAALAALA
19   LYSGLUGLNILELYSLEUPROPROGLNPRO
20   VALTHRALAILEVALTYRTHRALAALAALA
21   HISSERALAASNLEUTRPTHRPROGLUSER
22   ALAGLNGLYGLNMETLEUGLUGLNLEUGLY
23   PHETHRLEUALALYSLEUPROALAGLYLEU
24   ASNALASERGLNSERGLNGLYLYSARGHIS
25   ASPILEILEGLNLEUGLYGLYGLUASNLEU
26   ALAALAGLYLEUASNGLYGLUSERLEUPHE
27   LEUPHEALAGLYASPGLNLYSASPALAASP
28   ALAILETYRALAASNPROLEULEUALAHIS
29   LEUPROALAVALGLNASNLYSGLNVALTYR
30   ALALEUGLYTHRGLUTHRPHEARGLEUASP
31   TYRTYRSERALAMETGLNVALLEUASPARG
32   LEULYSALALEUPHE

Samples:

sample_1: FepB mM; H2O 93%; D2O 7%

sample_2: FepB mM; H2O 93%; D2O 7%

sample_3: FepB mM; H2O 93%; D2O 7%

sample_conditions: ionic strength: 0 M; pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions
3D 1H-13C NOESYsample_2isotropicsample_conditions
3D HNCACBsample_3isotropicsample_conditions
3D CBCA(CO)NHsample_3isotropicsample_conditions
3D HNCOsample_3isotropicsample_conditions
3D HN(CO)CAsample_3isotropicsample_conditions
3D HNCAsample_3isotropicsample_conditions
2D 1H-15N HSQCsample_3isotropicsample_conditions

Software:

No software information available

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Varian INOVA 600 MHz

Related Database Links:

PDB
DBJ BAB34054 BAE76347 BAG76183 BAI23996 BAI29464
EMBL CAP75093 CAQ31065 CAQ89998 CAQ97446 CAR01973
GB AAA83853 AAB40791 AAC73693 AAG54927 AAN42155
REF NP_308658 NP_415124 NP_706448 WP_000948435 WP_001234290
SP P0AEL6 P0AEL7
AlphaFold P0AEL6 P0AEL7

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