Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53305

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Nicholas Rego and David Koes
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Name: 1H, 13C, and 15N chemical shift assignments of KABLE2.5 bound to 6-NBT
Published: 2025-08-21

Title:

1H, 13C, and 15N chemical shift assignments of KABLE2.5 bound to 6-NBT

Deposition date:

2025-08-07

Original release date:

2025-08-21

Authors:

Volkov, Alexander; El Yazidi Mouloud, Wael; Bhattacharya, Sagar

Citation:

Citation: Bhattacharya, Sagar; Volkov, Alexander. "Emergence of binding and catalysis from a designed generalist binding protein" .

Assembly members:

Assembly members:
entity_1, polymer, 126 residues, Formula weight is not available

Natural source:

Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: engineered protein

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: SLKEKFEEYEKFGPRILGLW QEARDAFEAGDLARVDELLR ELKEILRKDLKLAEEMKKEA EEAGNKEAVELLEEQLEGLK KIQAMFEEAVEAFRAGDRER FGELLEKIIEEGKALLPNVE KIKEAI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	392
15N chemical shifts	123
1H chemical shifts	200

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	KABLE2.5	1

Entities:

Entity 1, KABLE2.5 126 residues - Formula weight is not available

1

SER

LEU

LYS

GLU

LYS

PHE

GLU

TYR

GLU

2

LYS

PHE

GLY

PRO

ARG

ILE

LEU

GLY

LEU

TRP

3

GLN

GLU

ALA

ARG

ASP

ALA

PHE

GLU

ALA

GLY

4

ASP

LEU

ALA

ARG

VAL

ASP

GLU

LEU

ARG

5

GLU

LEU

LYS

GLU

ILE

LEU

ARG

LYS

ASP

LEU

6

LYS

LEU

ALA

GLU

MET

LYS

GLU

ALA

7

GLU

ALA

GLY

ASN

LYS

GLU

ALA

VAL

GLU

8

LEU

GLU

GLN

LEU

GLU

GLY

LEU

LYS

9

LYS

ILE

GLN

ALA

MET

PHE

GLU

ALA

VAL

10

GLU

ALA

PHE

ARG

ALA

GLY

ASP

ARG

GLU

ARG

11

PHE

GLY

GLU

LEU

GLU

LYS

ILE

GLU

12

GLU

GLY

LYS

ALA

LEU

PRO

ASN

VAL

GLU

13

LYS

ILE

LYS

GLU

ALA

ILE

Samples:

sample_1: KABLE2.5, [U-100% 13C; U-100% 15N], 2.0 mM; HEPES 20 mM; sodium chloride 100 mM; 6-NBT 8.0 mM; CD3CN, [U-100% 2H], 7.5 % v/v; D2O, [U-100% 2H], 10%

sample_conditions_1: ionic strength: 118 mM; pH: 6.9; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aliphatic	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D (H)CCH-TOCSY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_1	isotropic	sample_conditions_1
2D CB-CG	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v3.7 - collection, processing

NMRPipe - processing

CcpNMR - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker AVANCE III 800 MHz

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

BMRB Entry 53305