BMRB Entry 18467

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18467
MolProbity Validation Chart

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Title:
FAS1-4, R555W
Deposition date:
2012-05-16
Original release date:
2013-08-15
Authors:
Underhaug, Jarl; Nielsen, Niels Chr.; Runager, Kasper
Citation:

Citation: Underhaug, Jarl; Kolds, Heidi; Runager, Kasper; Nielsen, Jakob Toudahl; Srensen, Charlotte; Kristensen, Torsten; Otzen, Daniel; Karring, Henrik; Malmendal, Anders; Schitt, Birgit; Enghild, Jan; Nielsen, Niels Chr. "Mutation in transforming growth factor beta induced protein associated with granular corneal dystrophy type 1 reduces the proteolytic susceptibility through local structural stabilization."  Biochim. Biophys. Acta 1834, 2812-2822 (2013).
PubMed: 24129074

Assembly members:

Assembly members:
FAS1-4_R555W, polymer, 135 residues, 14484.779 Da.

Natural source:

Natural source:   Common Name: Humans   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 SUMO

Entity Sequences (FASTA):

Entity Sequences (FASTA):
FAS1-4_R555W: AGMGTVMDVLKGDNRFSMLV AAIQSAGLTETLNREGVYTV FAPTNEAFRALPPREWSRLL GDAKELANILKYHIGDEILV SGGIGALVRLKSLQGDKLEV SLKNNVVSVNKEPVAEPDIM ATNGVVHVITNVLQA

Data sets:
Data typeCount
13C chemical shifts514
15N chemical shifts132
1H chemical shifts855

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FAS1-4_R555W1

Entities:

Entity 1, FAS1-4_R555W 135 residues - 14484.779 Da.

1   ALAGLYMETGLYTHRVALMETASPVALLEU
2   LYSGLYASPASNARGPHESERMETLEUVAL
3   ALAALAILEGLNSERALAGLYLEUTHRGLU
4   THRLEUASNARGGLUGLYVALTYRTHRVAL
5   PHEALAPROTHRASNGLUALAPHEARGALA
6   LEUPROPROARGGLUTRPSERARGLEULEU
7   GLYASPALALYSGLULEUALAASNILELEU
8   LYSTYRHISILEGLYASPGLUILELEUVAL
9   SERGLYGLYILEGLYALALEUVALARGLEU
10   LYSSERLEUGLNGLYASPLYSLEUGLUVAL
11   SERLEULYSASNASNVALVALSERVALASN
12   LYSGLUPROVALALAGLUPROASPILEMET
13   ALATHRASNGLYVALVALHISVALILETHR
14   ASNVALLEUGLNALA

Samples:

sample_1: FAS1-4, R555W, [U-99% 13C; U-99% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; DSS 0.5 mM; sodium azide 0.5%; arginine 50 mM; glutamate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D CBCANHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 15N-TOCSY-HSQCsample_1isotropicsample_conditions_1
3D 13C-NOESY-HSQCsample_1isotropicsample_conditions_1
3D 15N-NOESY-HSQCsample_1isotropicsample_conditions_1
2D NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - peak picking

TALOS, Cornilescu, Delaglio and Bax - data analysis

REDCAT, Valafar, Homayoun, and James H. Prestegard - data analysis

ARIA, Linge, O'Donoghue and Nilges - structure solution

CNSSOLVE, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 11311 18466 25425
PDB
GB AAC24944

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