BMRB Entry 30481

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30481
MolProbity Validation Chart

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Title:
Recombinant melittin
Deposition date:
2018-06-14
Original release date:
2019-04-03
Authors:
Ramirez, L.; Pande, J.; Shekhtman, A.
Citation:

Citation: Ramirez, L.; Pande, J.; Shekhtman, A.; Ramirez, L.; Shekhtman, A.; Pande, J.. "Nuclear Magnetic Resonance-Based Structural Characterization and Backbone Dynamics of Recombinant Bee Venom Melittin."  Biochemistry 57, 2775-2785 (2018).
PubMed: 29668274

Assembly members:

Assembly members:
Melittin, polymer, 26 residues, 2852.487 Da.

Natural source:

Natural source:   Common Name: Honeybee   Taxonomy ID: 7460   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Apis mellifera

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Melittin: GIGAVLKVLTTGLPALISWI KRKRQQ

Data sets:
Data typeCount
13C chemical shifts93
15N chemical shifts26
1H chemical shifts202

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 26 residues - 2852.487 Da.

1   GLYILEGLYALAVALLEULYSVALLEUTHR
2   THRGLYLEUPROALALEUILESERTRPILE
3   LYSARGLYSARGGLNGLN

Samples:

sample_1: melittin, [U-95% 13C; U-95% 15N], 0.05 mM; glycerol, [U-2H], 10 % v/v; potassium phosphate buffer 10 mM

sample_2: Melittin, [U-95% 13C; U-95% 15N], 0.050 mM; potassium phosphate buffer 10 mM

sample_conditions_1: ionic strength: 10 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 10 mM; pH: 7; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_2
3D 1H-13C NOESYsample_1isotropicsample_conditions_2
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_2
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1

Software:

CYANA v3.98, Guntert, Mumenthaler and Wuthrich - structure calculation

YASARA v18.4.24, Krieger and Vriend - refinement

CARA v1.9.1, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AvanceII 700 MHz
  • Bruker AvanceIII 600 MHz

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