BMRB Entry 16123

Name: Backbone 1H, 13C, and 15N Chemical Shift Assignments for d+PHS/V66K SNase
Published: 2012-08-07

Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR16123

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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:

Backbone 1H, 13C, and 15N Chemical Shift Assignments for d+PHS/V66K SNase

Deposition date:

2009-01-16

Original release date:

2012-08-07

Authors:

Chimenti, Michael

Citation:

Citation: Chimenti, Michael; Castaneda, Carlos; Majumdar, Ananya; Garcia-Moreno, Bertrand. "Structural origins of high apparent dielectric constants experienced by ionizable groups in the hydrophobic core of a protein" J. Mol. Biol. 405, 361-377 (2011).
PubMed: 21059359

Assembly members:

Assembly members:
D+PHS-V66K_Nuclease, polymer, 143 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET24a+

Entity Sequences (FASTA):

Entity Sequences (FASTA):
D+PHS-V66K_Nuclease: ATSTKKLHKEPATLIKAIDG DTVKLMYKGQPMTFRLLLVD TPEFNEKYGPEASAFTKKMK ENAKKIEVEFDKGQRTDKYG RGLAYIYADGKMVNEALVRQ GLAKVAYVYKGNNTHEQLLR KAEAQAKKEKLNIWSEDNAD SGQ

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	243
15N chemical shifts	130
1H chemical shifts	130

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	D+PHS/V66K	1

Entities:

Entity 1, D+PHS/V66K 143 residues - Formula weight is not available

Residues 44-49 (an active site loop) were deleted from the protein; the original numbering scheme was kept.

1

ALA

THR

SER

THR

LYS

LEU

HIS

LYS

GLU

2

PRO

ALA

THR

LEU

ILE

LYS

ALA

ILE

ASP

GLY

3

ASP

THR

VAL

LYS

LEU

MET

TYR

LYS

GLY

GLN

4

PRO

MET

THR

PHE

ARG

LEU

VAL

ASP

5

THR

PRO

GLU

PHE

ASN

GLU

LYS

TYR

GLY

PRO

6

GLU

ALA

SER

ALA

PHE

THR

LYS

MET

LYS

7

GLU

ASN

ALA

LYS

ILE

GLU

VAL

GLU

PHE

8

ASP

LYS

GLY

GLN

ARG

THR

ASP

LYS

TYR

GLY

9

ARG

GLY

LEU

ALA

TYR

ILE

TYR

ALA

ASP

GLY

10

LYS

MET

VAL

ASN

GLU

ALA

LEU

VAL

ARG

GLN

11

GLY

LEU

ALA

LYS

VAL

ALA

TYR

VAL

TYR

LYS

12

GLY

ASN

THR

HIS

GLU

GLN

LEU

ARG

13

LYS

ALA

GLU

ALA

GLN

ALA

LYS

GLU

LYS

14

LEU

ASN

ILE

TRP

SER

GLU

ASP

ASN

ALA

ASP

15

SER

GLY

GLN

Samples:

sample_1: D+PHS/V66K Nuclease, [U-99% 15N], 1 mM; D2O 10%; H2O 90%; sodium chloride 100 mM; sodium phosphate 25 mM

sample_conditions_1: ionic strength: 0.17 mM; pH: 6.7; pressure: 1 atm; temperature: 298 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

Software:

SPARKY v3.110, Goddard - chemical shift assignment

NMR spectrometers:

Varian INOVA 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks