BMRB Entry 36383

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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/BMR36383
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

Title:
NERP-2 in a HFIP solution
Deposition date:
2020-09-13
Original release date:
2025-10-24
Authors:
Park, O.; Cheong, C.; Jeon, Y.
Citation:

Citation: Park, One-Sung; Bang, Jeong Kyu; Ryu, Kyoung-Seok; Hwang, Eunha; Hong, Kwan Soo; Byun, Youngjoo; Cheong, Chaejoon; Jeon, Young Ho. "Structure of neuroendocrine regulatory peptide-2 in membrane-mimicking environments."  Peptide Science ., .-. (2020).

Assembly members:

Assembly members:
Neurosecretory protein VGF, polymer, 39 residues, 4173.605 Da.

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Neurosecretory protein VGF: SQAEATRQAAAQEERLADLA SDLLLQYLLQGGARQRGLG

Data sets:
Data typeCount
13C chemical shifts111
15N chemical shifts47
1H chemical shifts199

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 39 residues - 4173.605 Da.

1   SERGLNALAGLUALATHRARGGLNALAALA
2   ALAGLNGLUGLUARGLEUALAASPLEUALA
3   SERASPLEULEULEUGLNTYRLEULEUGLN
4   GLYGLYALAARGGLNARGGLYLEUGLY

Samples:

15N_13C_sample: Neurosecretory protein VGF, [U-13C; U-15N], mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 25 mM; pH: 6.0; pressure: 1 atm; temperature: 298.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15N_13C_sampleisotropicsample_conditions_1
2D 1H-13C HSQC15N_13C_sampleisotropicsample_conditions_1
3D HNCACB15N_13C_sampleisotropicsample_conditions_1
3D CBCA(CO)NH15N_13C_sampleisotropicsample_conditions_1
3D 1H-15N TOCSY15N_13C_sampleisotropicsample_conditions_1
3D HCCH-TOCSY15N_13C_sampleisotropicsample_conditions_1
3D 1H-15N NOESY15N_13C_sampleisotropicsample_conditions_1
3D 1H-13C NOESY15N_13C_sampleisotropicsample_conditions_1

Software:

CYANA, Guntert P. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CcpNmr Analysis, CCPN - chemical shift assignment

CcpNmr Analysis, CCPN - peak picking

TopSpin, Bruker Biospin - processing

NMR spectrometers:

  • Bruker AVANCE III HD 800 MHz

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