BMRB Entry 51406

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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/BMR51406
MolProbity Validation Chart

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Title:
1H, 13C, and 15N Chemical Shift Assignments for amyloidogenic SEM1(68-107) peptide
Deposition date:
2022-04-21
Original release date:
2022-04-26
Authors:
Blokhin, Dmitriy; Sanchugova, Daria; Klochkov, Vladimir
Citation:

Citation: Sanchugova, Daria; Kusova, Aleksandra; Bikmullin, Aydar; Yulmetov, Aydar; Mukhametzyanov, Timur; Klochkov, Vladimir; Blokhin, Dmitriy. "Conformational ensemble of amyloid-forming semenogelin 1 peptide SEM1(68-107) by NMR spectroscopy and MD simulations"  J. Struct. Biol. 214, 107900-107900 (2022).
PubMed: 36191746

Assembly members:

Assembly members:
entity_1, polymer, 40 residues, 4941.3959 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   Vector: pET-GB1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: TYHVDANDHDQSRKSQQYDL NALHKTTKSQRHLGGSQQLL

Data typeCount
13C chemical shifts109
15N chemical shifts22
1H chemical shifts99

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1SEM1(68-107) peptide1

Entities:

Entity 1, SEM1(68-107) peptide 40 residues - 4941.3959 Da.

1   THRTYRHISVALASPALAASNASPHISASP
2   GLNSERARGLYSSERGLNGLNTYRASPLEU
3   ASNALALEUHISLYSTHRTHRLYSSERGLN
4   ARGHISLEUGLYGLYSERGLNGLNLEULEU

Samples:

sample_1: Molecule 1, [U-100% 13C; U-100% 15N], 0.3 mM

sample_conditions_1: pH: 8.8; temperature: 278 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC/HMQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
CC(CO)NH (HNco_C.relayed)sample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
HN(CA)CO (H[N[ca[CO]]])sample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
HNHA (H{[N]+[HA]})sample_1isotropicsample_conditions_1
3D HNHBsample_1isotropicsample_conditions_1

Software:

CcpNmr Analysis v2.5 - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

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