BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 6398

Title: Sulfolobus Solfataricus Acylphosphatase 1H chemical shift assignment   PubMed: 16287076

Deposition date: 2004-11-23 Original release date: 2006-02-20

Authors: Corazza, Alessandra; Pagano, Katiuscia; Viglino, Paolo; Esposito, Gennaro

Citation: Corazza, Alessandra; Rosano, Camillo; Pagano, Katiuscia; Alverdi, V.; Esposito, Gennaro; Capanni, Cristina; Bemporad, Francesco; Plakoutsi, Georgia; Stefani, Massimo; Chiti, Fabrizio; Zuccotti, Simone; Bolognesi, Martino; Viglino, Paolo. "Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus"  Proteins 62, 64-79 (2006).

Assembly members:
Sso AcP, polymer, 103 residues, Formula weight is not available

Natural source:   Common Name: Sulfolobus solfataricus   Taxonomy ID: 2287   Superkingdom: Archaea   Kingdom: not available   Genus/species: Sulfolobus solfataricus

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
Sso AcP: GSMKKWSDTEVFEMLKRMYA RVYGLVQGVGFRKFVQIHAI RLGIKGYAKNLPDGSVEVVA EGYEEALSKLLERIKQGPPA AEVEKVDYSFSEYKGEFEDF ETY

Data sets:
Data typeCount
1H chemical shifts546
15N chemical shifts100
coupling constants60

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sulfolobus solfataricus acylphosphatase1

Entities:

Entity 1, Sulfolobus solfataricus acylphosphatase 103 residues - Formula weight is not available

1   GLYSERMETLYSLYSTRPSERASPTHRGLU
2   VALPHEGLUMETLEULYSARGMETTYRALA
3   ARGVALTYRGLYLEUVALGLNGLYVALGLY
4   PHEARGLYSPHEVALGLNILEHISALAILE
5   ARGLEUGLYILELYSGLYTYRALALYSASN
6   LEUPROASPGLYSERVALGLUVALVALALA
7   GLUGLYTYRGLUGLUALALEUSERLYSLEU
8   LEUGLUARGILELYSGLNGLYPROPROALA
9   ALAGLUVALGLULYSVALASPTYRSERPHE
10   SERGLUTYRLYSGLYGLUPHEGLUASPPHE
11   GLUTHRTYR

Samples:

sample_1: Sso AcP 0.4 mM; sodium phosphate buffer 50 mM; NaCl 50 mM

sample_2: Sso AcP, [U-15N], 0.7 mM; sodium phosphate buffer 50 mM; NaCl 50 mM

conditions_1: pH: 5.6; temperature: 310 K

conditions_2: pH: 5.79; temperature: 310 K

Experiments:

NameSampleSample stateSample conditions
COSYsample_1not availablenot available
TOCSYsample_1not availablenot available
NOESYsample_1not availablenot available
1H_15N_HSQCsample_2not availablenot available
1H_15N_NOESY-HSQCsample_2not availablenot available

Software:

felix v2000, Accelrys - assignment

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
GB AAK41170 ACP35428 ACP38087 ACP45594 ACP48618
REF NP_342380 WP_009992301 WP_010923147 WP_012711338 WP_015581176
SP Q97ZL0

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