BMRB Entry 4060

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4060

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Title:
Multinuclear Backbone NMR Resonance Assignments and the Secondary Structure of Escherichia coli Thioesterase/Protease I - A Member of a New Subclass of Lipolytic Enzymes
Deposition date:
1997-09-20
Original release date:
2002-07-17
Authors:
Lin, Ta-Hsien; Chen, Chinpan; Huang, Rong-Fong; Lee, Ya-Lin; Shaw, Jei-Fu; Huang, Tai-huang
Citation:

Citation: Lin, Ta-Hsien; Chen, Chinpan; Huang, Rong-Fong; Lee, Ya-Lin; Shaw, Jei-Fu; Huang, Tai-huang. "Multinuclear Backbone NMR Resonance Assignments and the Secondary Structure of Escherichia coli Thioesterase/Protease I - A Member of a New Subclass of Lipolytic Enzymes"  .

Assembly members:

Assembly members:
thioesterase/protease_I, polymer, 189 residues, 21000 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
thioesterase/protease_I: MADTLLILGDSLSAGYRMSA SAAWPALLNDKWQSKTSVVN ASISGDTSQQGLARLPALLK QHQPRWVLVELGGNDGLRGF QPQQTEQTLRQILQDVKAAN AEPLLMQIRLPANYGRRYNE AFSAIYPKLAKEFDVPLLPF FMEEVYLKPQWMQDDGIHPN RDAQPFIADWMAKQLQPLVN HDSHHHHHH

Data sets:
Data typeCount
13C chemical shifts506
15N chemical shifts161
1H chemical shifts579

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1thioesterase/protease_I1

Entities:

Entity 1, thioesterase/protease_I 189 residues - 21000 Da.

1   METALAASPTHRLEULEUILELEUGLYASP
2   SERLEUSERALAGLYTYRARGMETSERALA
3   SERALAALATRPPROALALEULEUASNASP
4   LYSTRPGLNSERLYSTHRSERVALVALASN
5   ALASERILESERGLYASPTHRSERGLNGLN
6   GLYLEUALAARGLEUPROALALEULEULYS
7   GLNHISGLNPROARGTRPVALLEUVALGLU
8   LEUGLYGLYASNASPGLYLEUARGGLYPHE
9   GLNPROGLNGLNTHRGLUGLNTHRLEUARG
10   GLNILELEUGLNASPVALLYSALAALAASN
11   ALAGLUPROLEULEUMETGLNILEARGLEU
12   PROALAASNTYRGLYARGARGTYRASNGLU
13   ALAPHESERALAILETYRPROLYSLEUALA
14   LYSGLUPHEASPVALPROLEULEUPROPHE
15   PHEMETGLUGLUVALTYRLEULYSPROGLN
16   TRPMETGLNASPASPGLYILEHISPROASN
17   ARGASPALAGLNPROPHEILEALAASPTRP
18   METALALYSGLNLEUGLNPROLEUVALASN
19   HISASPSERHISHISHISHISHISHIS

Samples:

sample_one: thioesterase/protease_I, [U-15N], 2 mM; phosphate buffer 50 mM

sample_two: thioesterase/protease_I, [U-13C], 2 mM; phosphate buffer 50 mM

sample_three: thioesterase/protease_I, [U-13C;U-15N], 2 mM; phosphate buffer 50 mM

sample_conditions_one: pH: 3.5; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
not availablenot availablenot availablesample_conditions_one

Software:

No software information available

NMR spectrometers:

  • unknown unknown 0 MHz

Related Database Links:

PDB
DBJ BAA02475 BAB33980 BAE76273 BAG76043 BAI23868
EMBL CAP75030 CAQ30967 CAQ88099 CAQ97369 CAR01845
GB AAA24664 AAB40248 AAC73596 AAG54851 AAN79092
REF NP_308584 NP_415027 WP_001295836 WP_001297298 WP_001301605
SP P0ADA1 P0ADA2
AlphaFold P0ADA1 P0ADA2

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