BMRB Entry 53473

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53473

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Title:
Resonance assignments of 2-14 domains fragment of human tropoelastin (hTE)
Deposition date:
2025-12-09
Original release date:
2026-02-06
Authors:
Reichheld, Sean; Sharpe, Simon
Citation:

Citation: Reichheld, Sean; Muiznieks, Lisa; Liu, Zi Hao; Payliss, Brandon; Keeley, Fred; Sharpe, Simon. "A free energy landscape screen reveals the disordered conformational ensemble of tropoelastin"  .

Assembly members:

Assembly members:
entity_1, polymer, 221 residues, Formula weight is not available

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: pet32b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GVPGAIPGGVPGGVFYPGAG LGALGGGALGPGGKPLKPVP GGLAGAGLGAGLGAFPAVTF PGALVPGGVADAAAAYKAAK AGAGLGGVPGVGGLGVSAGA VVPQPGAGVKPGKVPGVGLP GVYPGGVLPGARFPGVGVLP GVPTGAGVKPKAPGVGGAFA GIPGVGPFGGPQPGVPLGYP IKAPKLPGGYGLPYTTGKLP YGYGPGGVAGAAGKAGYPTG T

Data sets:
Data typeCount
13C chemical shifts431
15N chemical shifts179
1H chemical shifts396

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1hTE_2-141

Entities:

Entity 1, hTE_2-14 221 residues - Formula weight is not available

1   GLYVALPROGLYALAILEPROGLYGLYVAL
2   PROGLYGLYVALPHETYRPROGLYALAGLY
3   LEUGLYALALEUGLYGLYGLYALALEUGLY
4   PROGLYGLYLYSPROLEULYSPROVALPRO
5   GLYGLYLEUALAGLYALAGLYLEUGLYALA
6   GLYLEUGLYALAPHEPROALAVALTHRPHE
7   PROGLYALALEUVALPROGLYGLYVALALA
8   ASPALAALAALAALATYRLYSALAALALYS
9   ALAGLYALAGLYLEUGLYGLYVALPROGLY
10   VALGLYGLYLEUGLYVALSERALAGLYALA
11   VALVALPROGLNPROGLYALAGLYVALLYS
12   PROGLYLYSVALPROGLYVALGLYLEUPRO
13   GLYVALTYRPROGLYGLYVALLEUPROGLY
14   ALAARGPHEPROGLYVALGLYVALLEUPRO
15   GLYVALPROTHRGLYALAGLYVALLYSPRO
16   LYSALAPROGLYVALGLYGLYALAPHEALA
17   GLYILEPROGLYVALGLYPROPHEGLYGLY
18   PROGLNPROGLYVALPROLEUGLYTYRPRO
19   ILELYSALAPROLYSLEUPROGLYGLYTYR
20   GLYLEUPROTYRTHRTHRGLYLYSLEUPRO
21   TYRGLYTYRGLYPROGLYGLYVALALAGLY
22   ALAALAGLYLYSALAGLYTYRPROTHRGLY
23   THR

Samples:

sample_1: hTE fragment domains 2-14 monomer, [U-100% 13C; U-100% 15N], 1.3 mM; sodium phosphate 50 mM; sodium chloride 200 mM

sample_conditions_1: ionic strength: 0.25 M; pH: 7.0; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D NOESY-HSQCsample_1isotropicsample_conditions_1
3D HSQC-TOCSYsample_1isotropicsample_conditions_1
3D HCANsample_1isotropicsample_conditions_1
3D HNNsample_1isotropicsample_conditions_1
3D HN(CO)Nsample_1isotropicsample_conditions_1

Software:

TOPSPIN - collection

CcpNMR - chemical shift assignment

NMRPipe - processing

NMR spectrometers:

  • Bruker AVANCE III 600 MHz
  • Bruker AVANCE III 700 MHz

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