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 25536

Title: MDMX-057

Deposition date: 2015-03-17 Original release date: 2016-01-25

Authors: Grace, Christy; Kriwacki, Richard

Citation: Grace, Christy; Kriwacki, Richard. "Monitoring ligand induced protein ordering in drug discovery"  J. Mol. Biol. ., .-..

Assembly members:
entity_1, polymer, 89 residues, 10160.976 Da.
entity_CM7, non-polymer, 628.705 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity_1: QINQVRPKLPLLKILHAAGA QGEMFTVKEVMHYLGQYIMV KQLYDQQEQHMVYCGGDLLG ELLGRQSFSVKDPSPLYDML RKNLVTLAT

Data sets:
Data typeCount
13C chemical shifts413
15N chemical shifts95
1H chemical shifts704

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 89 residues - 10160.976 Da.

1   GLNILEASNGLNVALARGPROLYSLEUPRO
2   LEULEULYSILELEUHISALAALAGLYALA
3   GLNGLYGLUMETPHETHRVALLYSGLUVAL
4   METHISTYRLEUGLYGLNTYRILEMETVAL
5   LYSGLNLEUTYRASPGLNGLNGLUGLNHIS
6   METVALTYRCYSGLYGLYASPLEULEUGLY
7   GLULEULEUGLYARGGLNSERPHESERVAL
8   LYSASPPROSERPROLEUTYRASPMETLEU
9   ARGLYSASNLEUVALTHRLEUALATHR

Entity 2, entity_2 - C32 H35 F3 N4 O4 S - 628.705 Da.

1   CM7

Samples:

sample_1: entity_1, [U-100% 13C; U-100% 15N], 0.5 mM; entity_2 0.6 mM; NaCl 200 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection, processing

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

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