BMRB Entry 51003

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR51003

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Title:
Role of active site loop dynamics in ligand release from E. coli dihydrofolate reductase
Deposition date:
2021-07-01
Original release date:
2021-07-09
Authors:
Singh, Amrinder; Fenwick, Robert; Dyson, Helen; Wright, Peter
Citation:

Citation: Singh, Amrinder; Fenwick, Robert; Dyson, Helen; Wright, Peter. "Role of Active Site Loop Dynamics in Mediating Ligand Release from E. coli Dihydrofolate Reductase"  Biochemistry 60, 2663-2671 (2021).
PubMed: 34428034

Assembly members:

Assembly members:
entity_1, polymer, 160 residues, Formula weight is not available
entity_DDF, non-polymer, 443.453 Da.
entity_NAP, non-polymer, 743.405 Da.

Natural source:

Natural source:   Common Name: E. coli   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: pET21b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MISLIAALAVDRVIGMENAM PWPPLPADLAWFKRNTLNKP VIMGRHTWESIGRPLPGRKN IILSSQPGTDDRVTWVKSVD EAIAACGDVPEIMVIGGGRV YEQFLPKAQKLYLTHIDAEV EGDTHFPDYEPDDWESVFSE FHDADAQNAHSYCFEILERR

Data sets:
Data typeCount
15N chemical shifts147
1H chemical shifts147

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1N23PPS148A E.coli DHFR1
2ddTHF2
3NADP3

Entities:

Entity 1, N23PPS148A E.coli DHFR 160 residues - Formula weight is not available

1   METILESERLEUILEALAALALEUALAVAL
2   ASPARGVALILEGLYMETGLUASNALAMET
3   PROTRPPROPROLEUPROALAASPLEUALA
4   TRPPHELYSARGASNTHRLEUASNLYSPRO
5   VALILEMETGLYARGHISTHRTRPGLUSER
6   ILEGLYARGPROLEUPROGLYARGLYSASN
7   ILEILELEUSERSERGLNPROGLYTHRASP
8   ASPARGVALTHRTRPVALLYSSERVALASP
9   GLUALAILEALAALACYSGLYASPVALPRO
10   GLUILEMETVALILEGLYGLYGLYARGVAL
11   TYRGLUGLNPHELEUPROLYSALAGLNLYS
12   LEUTYRLEUTHRHISILEASPALAGLUVAL
13   GLUGLYASPTHRHISPHEPROASPTYRGLU
14   PROASPASPTRPGLUSERVALPHESERGLU
15   PHEHISASPALAASPALAGLNASNALAHIS
16   SERTYRCYSPHEGLUILELEUGLUARGARG

Entity 2, ddTHF - C21 H25 N5 O6 - 443.453 Da.

1   DDF

Entity 3, NADP - C21 H28 N7 O17 P3 - 743.405 Da.

1   NAP

Samples:

sample_1: N23PPS148A E. coli DHFR, [U-100% 13C; U-100% 15N], 500 uM

sample_conditions_1: ionic strength: 0.075 M; pH: 7.6; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCACONHsample_1isotropicsample_conditions_1

Software:

CcpNMR - chemical shift assignment

NMR spectrometers:

  • Bruker AVANCE III 800 MHz

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