BMRB Entry 17505

Title:
1H, 13C, and 15N Chemical Shift Assignments for human muscle Acylphosphatase   PubMed: 21643968
Deposition date:
2011-03-03
Original release date:
2011-06-07
Authors:
Fusco, Giuliana; Hsu, Shang-Te; Bemporad, Francesco; Vendruscolo, Michele; Chiti, Fabrizio; Dobson, Christopher
Citation:

Citation: Fusco, Giuliana; De Simone, Alfonso; Hsu, Shang-Te Danny; Bemporad, Francesco; Vendruscolo, Michele; Chiti, Fabrizio; Dobson, Christopher. "(1)H, (13)C and (15)N resonance assignments of human muscle acylphosphatase."  Biomol. NMR Assignments 6, 27-29 (2012).

Assembly members:

Assembly members:
human_muscle_acylphosphatase_polypeptide, polymer, 99 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:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-2t

Experimental source:

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pGEX-2t

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts386
15N chemical shifts103
1H chemical shifts588

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human muscle acylphosphatase polypeptide1

Entities:

Entity 1, human muscle acylphosphatase polypeptide 99 residues - Formula weight is not available

1   METSERTHRALAGLNSERLEULYSSERVAL
2   ASPTYRGLUVALPHEGLYARGVALGLNGLY
3   VALSERPHEARGMETTYRTHRGLUASPGLU
4   ALAARGLYSILEGLYVALVALGLYTRPVAL
5   LYSASNTHRSERLYSGLYTHRVALTHRGLY
6   GLNVALGLNGLYPROGLUASPLYSVALASN
7   SERMETLYSSERTRPLEUSERLYSVALGLY
8   SERPROSERSERARGILEASPARGTHRASN
9   PHESERASNGLULYSTHRILESERLYSLEU
10   GLUTYRSERASNPHESERILEARGTYR

Samples:

sample_1: human muscle acylphosphatase polypeptide, [U-95% 13C; U-95% 15N], 250 uM; sodium phosphate 50 mM; H2O 90%; D2O 10%

sample_conditions_1: pH: 5.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

SPARKY, Bruker Biospin, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

EMBL CAA58988
GB AAH12290 AAY14721 AIC48219 EAX00154
PRF 2122227B
REF NP_612457 XP_003262429 XP_003830881 XP_004029284 XP_009440741
SP P14621
AlphaFold P14621

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts