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 34304

Title: A computationally designed dRP lyase domain reconstructed from two heterologous fragments   PubMed: 30558718

Deposition date: 2018-07-24 Original release date: 2018-12-05

Authors: ElGamacy, M.; Coles, M.; Lupas, A.

Citation: ElGamacy, M.; Coles, M.; Lupas, A.. "Asymmetric protein design from conserved supersecondary structures"  J. Struct. Biol. 204, 380-387 (2018).

Assembly members:
entity_1, polymer, 121 residues, 13443.259 Da.

Natural source:   Common Name: not available   Taxonomy ID: 32630   Superkingdom: not available   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli BL21(DE3)

Entity Sequences (FASTA):
entity_1: MKHHHHHHPMSDYDIPTTEN LYFQGAMGGQETLNGALVNM LKEEGNKALSVGNIDDALQY YAAAITLDKYPHKIKSGAEA KKLPGVGTKIAEKIDEFLAT GKLRKLEKIRQDDTSSSINF L

Data sets:
Data typeCount
13C chemical shifts257
15N chemical shifts61
1H chemical shifts430

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 121 residues - 13443.259 Da.

1   METLYSHISHISHISHISHISHISPROMET
2   SERASPTYRASPILEPROTHRTHRGLUASN
3   LEUTYRPHEGLNGLYALAMETGLYGLYGLN
4   GLUTHRLEUASNGLYALALEUVALASNMET
5   LEULYSGLUGLUGLYASNLYSALALEUSER
6   VALGLYASNILEASPASPALALEUGLNTYR
7   TYRALAALAALAILETHRLEUASPLYSTYR
8   PROHISLYSILELYSSERGLYALAGLUALA
9   LYSLYSLEUPROGLYVALGLYTHRLYSILE
10   ALAGLULYSILEASPGLUPHELEUALATHR
11   GLYLYSLEUARGLYSLEUGLULYSILEARG
12   GLNASPASPTHRSERSERSERILEASNPHE
13   LEU

Samples:

sample_1: polb4, [U-15N], 500 uM; potassium phosphate 150 mM

sample_2: polb4, [U-13C; U-15N], 500 uM; potassium phosphate 150 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 7.1; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D 15N-HSQC NOESYsample_1isotropicsample_conditions_1
3D 13C-HSQC NOESYsample_2isotropicsample_conditions_1
3D CNH-NOESYsample_2isotropicsample_conditions_1
3D NNH-NOESYsample_1isotropicsample_conditions_1
3D CCH-TOCSYsample_2isotropicsample_conditions_1
2D 15N-filtered NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - data analysis

X-PLOR, Brunger - structure calculation

Shine, Riss, M. and Coles, M. - refinement

NMR spectrometers:

  • Bruker AvanceIII 600 MHz
  • Bruker AvanceIII 800 MHz

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