BMRB Entry 6398

Name: Sulfolobus Solfataricus Acylphosphatase 1H chemical shift assignment
Published: 2006-02-20

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PDB ID: 1y9o
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR6398
MolProbity Validation Chart

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Sulfolobus Solfataricus Acylphosphatase 1H chemical shift assignment

Deposition date:

2004-11-23

Original release date:

2006-02-20

Authors:

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

Citation:

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).
PubMed: 16287076

Assembly members:

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

Natural source:

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

Experimental source:

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

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- chem_shift_list_1
coupling_constants
- J_coupling_list_1

Data type	Count
1H chemical shifts	546
15N chemical shifts	100
coupling constants	60

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sulfolobus solfataricus acylphosphatase	1

Entities:

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

1

GLY

SER

MET

LYS

TRP

SER

ASP

THR

GLU

2

VAL

PHE

GLU

MET

LEU

LYS

ARG

MET

TYR

ALA

3

ARG

VAL

TYR

GLY

LEU

VAL

GLN

GLY

VAL

GLY

4

PHE

ARG

LYS

PHE

VAL

GLN

ILE

HIS

ALA

ILE

5

ARG

LEU

GLY

ILE

LYS

GLY

TYR

ALA

LYS

ASN

6

LEU

PRO

ASP

GLY

SER

VAL

GLU

VAL

ALA

7

GLU

GLY

TYR

GLU

ALA

LEU

SER

LYS

LEU

8

LEU

GLU

ARG

ILE

LYS

GLN

GLY

PRO

ALA

9

ALA

GLU

VAL

GLU

LYS

VAL

ASP

TYR

SER

PHE

10

SER

GLU

TYR

LYS

GLY

GLU

PHE

GLU

ASP

PHE

11

GLU

THR

TYR

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:

Name	Sample	Sample state	Sample conditions
COSY	sample_1	not available	not available
TOCSY	sample_1	not available	not available
NOESY	sample_1	not available	not available
1H_15N_HSQC	sample_2	not available	not available
1H_15N_NOESY-HSQC	sample_2	not available	not available

Software:

felix v2000, Accelrys - assignment

NMR spectrometers:

Bruker Avance 500 MHz

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
AlphaFold	Q97ZL0