BMRB Entry 34657

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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/BMR34657
MolProbity Validation Chart

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Title:
Structure of Insulin-like growth factor 1 receptor's transmembrane domain
Deposition date:
2021-08-18
Original release date:
2022-09-02
Authors:
Bershatsky, Y.; Nadezhdin, K.; Bocharova, O.; Bocharov, E.
Citation:

Citation: Bershatsky, Yaroslav; Kuznetsov, Andrey; Idiatullina, Aisha; Bocharova, Olga; Dolotova, Sofya; Gavrilenkova, Alina; Serova, Oxana; Deyev, Igor; Rakitina, Tatiana; Zangieva, Olga; Pavlov, Konstantin; Batishchev, Oleg; Britikov, Vladimir; Usanov, Sergey; Arseniev, Alexander; Efremov, Roman; Bocharov, Eduard. "Diversity of Structural, Dynamic, and Environmental Effects Explain a Distinctive Functional Role of Transmembrane Domains in the Insulin Receptor Subfamily"  Int. J. Mol. Sci. 24, 3906-3906 (2023).
PubMed: 36835322

Assembly members:

Assembly members:
entity_1, polymer, 30 residues, 3455.314 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 BL21(DE3)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: NIAKIIIGPLIFVFLFSVVI GSIYLFLRKR

Data sets:
Data typeCount
13C chemical shifts157
15N chemical shifts29
1H chemical shifts255

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1unit_11

Entities:

Entity 1, unit_1 30 residues - 3455.314 Da.

1   ASNILEALALYSILEILEILEGLYPROLEU
2   ILEPHEVALPHELEUPHESERVALVALILE
3   GLYSERILETYRLEUPHELEUARGLYSARG

Samples:

sample_1: InsRtm, [U-100% 13C; U-100% 15N], 0.5 mM; DPC, [U-99% 2H], 100 mM; sodium azide 0.3 mM; KH2PO4 30 mM; K2HPO4 20 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.7; pressure: 1 atm; temperature: 313 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-1H TROSYsample_1isotropicsample_conditions_1
2D 1H-13C CT HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1anisotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1anisotropicsample_conditions_1
3D HCCH-TOCSYsample_1anisotropicsample_conditions_1
3D CBCA(CO)NHsample_1anisotropicsample_conditions_1
3D HN(CO)CAsample_1anisotropicsample_conditions_1
3D HNCOsample_1anisotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1anisotropicsample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure calculation

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

TopSpin, Bruker Biospin - collection

TALOS, Cornilescu, Delaglio and Bax - processing

NMR spectrometers:

  • Bruker AVANCE 600 MHz

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