BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules 		Member of WWPDB

BMRB Entry 17404

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17404

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Title: Backbone (H,N,CA,HA,CB,HB) assignment of the Escherichia coli peptidyl-tRNA hydrolase   PubMed: 21718701

Deposition date: 2011-01-11 Original release date: 2011-07-07

Authors: Giorgi, Laurent; Plateau, Pierre; Aubard, Caroline; Fromant, Michel; Blanquet, Sylvain; Bontems, Francois

Citation: Giorgi, Laurent; Plateau, Pierre; Aubard, Gavin; Fromant, Caroline; Thureau, Michel; Grtli, Aurelien; Blanquet, Morten; Bontems, Sylvain. "NMR-based substrate analog docking to Escherichia coli peptidyl-tRNA hydrolase."  J. Mol. Biol. 412, 619-633 (2011).

Assembly members:
PTH-HA20, polymer, 214 residues, Formula weight is not available

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

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

Entity Sequences (FASTA):
PTH-HA20: MGSSHHHHHHSSGLVPRGSH MTIKLIVGLANPGAEYAATR ANAGAWFVDLLAERLRAPLR EEAKFFGYTSRVTLGGEDVR LLVPTTFMNLSGKAVAAMAS FFRINPDEILVAHDELDLPP GVAKFKLGGGHGGHNGLKDI ISKLGNNPNFHRLRIGIGHP GDKNKVVGFVLGKPPVSEQK LIDEAIDEAARCTEMWFTDG LTKATNRLHAFKAQ

Data sets:
Data typeCount
13C chemical shifts541
15N chemical shifts183
1H chemical shifts679

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PTH-HA20 solution1

Entities:

Entity 1, PTH-HA20 solution 214 residues - Formula weight is not available

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERGLYLEUVALPROARGGLYSERHIS
3   METTHRILELYSLEUILEVALGLYLEUALA
4   ASNPROGLYALAGLUTYRALAALATHRARG
5   ALAASNALAGLYALATRPPHEVALASPLEU
6   LEUALAGLUARGLEUARGALAPROLEUARG
7   GLUGLUALALYSPHEPHEGLYTYRTHRSER
8   ARGVALTHRLEUGLYGLYGLUASPVALARG
9   LEULEUVALPROTHRTHRPHEMETASNLEU
10   SERGLYLYSALAVALALAALAMETALASER
11   PHEPHEARGILEASNPROASPGLUILELEU
12   VALALAHISASPGLULEUASPLEUPROPRO
13   GLYVALALALYSPHELYSLEUGLYGLYGLY
14   HISGLYGLYHISASNGLYLEULYSASPILE
15   ILESERLYSLEUGLYASNASNPROASNPHE
16   HISARGLEUARGILEGLYILEGLYHISPRO
17   GLYASPLYSASNLYSVALVALGLYPHEVAL
18   LEUGLYLYSPROPROVALSERGLUGLNLYS
19   LEUILEASPGLUALAILEASPGLUALAALA
20   ARGCYSTHRGLUMETTRPPHETHRASPGLY
21   LEUTHRLYSALATHRASNARGLEUHISALA
22   PHELYSALAGLN

Samples:

sample_1: PTH-HA20, [U-98% 13C; U-98% 15N], 0.5-0.7 mM; sodium acetate 50 mM; sodium chloride 200 mM

sample_2: PTH-HA20, [U-98% 13C; U-98% 15N], 0.5-0.7 mM; sodium acetate 50 mM; sodium chloride 200 mM

sample_conditions_1: ionic strength: 250 mM; pH: 6.0; pressure: 1 atm; temperature: 290 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
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 950 MHz

Related Database Links:

PDB
DBJ BAA36062 BAB35132 BAG76778 BAI25016 BAI30140
EMBL CAA43945 CAP75743 CAQ31706 CAQ98084 CAR02598
GB AAC74288 AAG56062 AAN42820 AAN80127 AAP16706
PRF 2104267B
REF NP_309736 NP_415722 NP_707113 WP_000152925 WP_000152927
SP A7ZKX7 A7ZZE0 B1IU89 B1LH96 B1XAP5

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