BMRB Entry 15232

Name: proline-free mutant of SNase V8
Published: 2007-10-29

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PDB ID: 2pqe
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15232
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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:

proline-free mutant of SNase V8

Deposition date:

2007-05-02

Original release date:

2007-10-29

Authors:

Shan, Lu

Citation:

Citation: Shan, Lu; Tong, Yufeng; Xie, Tao; Wang, Min; Wang, Jinfeng. "Restricted backbone conformational and motional flexibilities of loops containing peptidyl-proline bonds dominate the enzyme activity of staphylococcal nuclease(,)." Biochemistry 46, 11504-11513 (2007).
PubMed: 17887731

Assembly members:

Assembly members:
v8pf, polymer, 149 residues, 16678.268 Da.

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Bacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: PET3D

Entity Sequences (FASTA):

Entity Sequences (FASTA):
v8pf: ATSTKKLHKEAATLIKAIDG DTVKLMYKGQAMTFRLLLVD TAETKHTKKGVEKYGAEASA FTKKMVENAKKIEVEFDKGQ RTDKYGRGLAYIYADGKMVN EALVRQGLAKVAYVYKGNNT HEQLLRKSEAQAKKEKLNIW SEDNADSGQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	371
15N chemical shifts	127
1H chemical shifts	666

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	v8pf	1

Entities:

Entity 1, v8pf 149 residues - 16678.268 Da.

1

ALA

THR

SER

THR

LYS

LEU

HIS

LYS

GLU

2

ALA

THR

LEU

ILE

LYS

ALA

ILE

ASP

GLY

3

ASP

THR

VAL

LYS

LEU

MET

TYR

LYS

GLY

GLN

4

ALA

MET

THR

PHE

ARG

LEU

VAL

ASP

5

THR

ALA

GLU

THR

LYS

HIS

THR

LYS

GLY

6

VAL

GLU

LYS

TYR

GLY

ALA

GLU

ALA

SER

ALA

7

PHE

THR

LYS

MET

VAL

GLU

ASN

ALA

LYS

8

LYS

ILE

GLU

VAL

GLU

PHE

ASP

LYS

GLY

GLN

9

ARG

THR

ASP

LYS

TYR

GLY

ARG

GLY

LEU

ALA

10

TYR

ILE

TYR

ALA

ASP

GLY

LYS

MET

VAL

ASN

11

GLU

ALA

LEU

VAL

ARG

GLN

GLY

LEU

ALA

LYS

12

VAL

ALA

TYR

VAL

TYR

LYS

GLY

ASN

THR

13

HIS

GLU

GLN

LEU

ARG

LYS

SER

GLU

ALA

14

GLN

ALA

LYS

GLU

LYS

LEU

ASN

ILE

TRP

15

SER

GLU

ASP

ASN

ALA

ASP

SER

GLY

GLN

Samples:

sample_1: entity, [U-100% 13C; U-100% 15N], 1 mM; KCL 100 mM; D2O 10%; H2O 90%; acetate 59 mM

sample_conditions_1: ionic strength: 100 mM; pH: 5.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1

Software:

FELIX v98, Accelrys Software Inc. - data analysis

NMR spectrometers:

Bruker DMX 600 MHz