BMRB Entry 50956

Name: Side chain 1H, 13C, 15N chemical shift assignments of lysine residues in delta+PHS/V66K staphylococcal nuclease selectively labeled with SAIL Lysine
Published: 2021-06-10

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50956

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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:

Side chain 1H, 13C, 15N chemical shift assignments of lysine residues in delta+PHS/V66K staphylococcal nuclease selectively labeled with SAIL Lysine

Deposition date:

2021-05-28

Original release date:

2021-06-10

Authors:

Takeda, Mitsuhiro; Kainosho, Masatsune

Citation:

Citation: Takeda, Mitsuhiro; Miyanoiri, Yohei; Terauchi, Tsutomu; Kainosho, Masatsune. "Conformational features and ionization states of Lys side chains in a protein studied using the stereo-array isotope labeling (SAIL) method" Magn. Reson. 2, 223-237 (2021).
PubMed: 37904773

Assembly members:

Assembly members:
entity_1, polymer, 164 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET3a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MGSSHHHHHHSSGLVPRGSH MATSTKKLHKEPATLIKAID GDTVKLMYKGQPMTFRLLLV DTPEFNEKYGPEASAFTKKM KENAKKIEVEFDKGQRTDKY GRGLAYIYADGKMVNEALVR QGLAKVAYVYKGNNTHEQLL RKAEAQAKKEKLNIWSEDNA DSGQ

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	105
15N chemical shifts	21
1H chemical shifts	105

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 164 residues - Formula weight is not available

Amino acid mutations (P117G, H124L, S128A, G50F, V51N) were introduced and residue number 44 to 49 (TKHPKK) were deleted.

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

ALA

THR

SER

THR

LYS

LEU

HIS

LYS

4

GLU

PRO

ALA

THR

LEU

ILE

LYS

ALA

ILE

ASP

5

GLY

ASP

THR

VAL

LYS

LEU

MET

TYR

LYS

GLY

6

GLN

PRO

MET

THR

PHE

ARG

LEU

VAL

7

ASP

THR

PRO

GLU

PHE

ASN

GLU

LYS

TYR

GLY

8

PRO

GLU

ALA

SER

ALA

PHE

THR

LYS

MET

9

LYS

GLU

ASN

ALA

LYS

ILE

GLU

VAL

GLU

10

PHE

ASP

LYS

GLY

GLN

ARG

THR

ASP

LYS

TYR

11

GLY

ARG

GLY

LEU

ALA

TYR

ILE

TYR

ALA

ASP

12

GLY

LYS

MET

VAL

ASN

GLU

ALA

LEU

VAL

ARG

13

GLN

GLY

LEU

ALA

LYS

VAL

ALA

TYR

VAL

TYR

14

LYS

GLY

ASN

THR

HIS

GLU

GLN

LEU

15

ARG

LYS

ALA

GLU

ALA

GLN

ALA

LYS

GLU

16

LYS

LEU

ASN

ILE

TRP

SER

GLU

ASP

ASN

ALA

17

ASP

SER

GLY

GLN

Samples:

sample_1: D+PHS/V66K Nuclease, SAIL-Lysine( [U-13C,15N; b2,g2,d2,e3-D4]-Lys), 1.5 mM; D2O 100%; potassium chloride 100 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 0.17 mM; pH: 8.0; pressure: 1 atm; temperature: 303 K

Experiments:

Name	Sample	Sample state	Sample conditions
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D HE(CE)NZ	sample_1	isotropic	sample_conditions_1

Software:

SPARKY v3.110 - chemical shift assignment

NMR spectrometers:

Bruker AvanceIII 600 MHz