BMRB Entry 6398
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6398
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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
- assigned_chemical_shifts
- coupling_constants
Data type | Count |
1H chemical shifts | 546 |
15N chemical shifts | 100 |
coupling constants | 60 |
Additional metadata:
Related Database Links:
PDB | 1Y9O 2BJD 2BJE 4OIX 4OJ1 4OJ3 4OJG 4OJH |
GB | AAK41170 ACP35428 ACP38087 ACP45594 ACP48618 |
REF | NP_342380 WP_009992301 WP_010923147 WP_012711338 WP_015581176 |
SP | Q97ZL0 |
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