BMRB Entry 53304

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

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53304

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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:

1H, 13C, and 15N chemical shift assignments of KABLE2.5

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, 127 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: SSLKEKFEEYEKFGPRILGL WQEARDAFEAGDLARVDELL RELKEILRKDLKLAEEMKKE AEEAGNKEAVELLEEQLEGL KKIQAMFEEAVEAFRAGDRE RFGELLEKIIEEGKALLPNV EKIKEAI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	543
15N chemical shifts	124
1H chemical shifts	805

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, KABLE2.5 127 residues - Formula weight is not available

1

SER

LEU

LYS

GLU

LYS

PHE

GLU

TYR

2

GLU

LYS

PHE

GLY

PRO

ARG

ILE

LEU

GLY

LEU

3

TRP

GLN

GLU

ALA

ARG

ASP

ALA

PHE

GLU

ALA

4

GLY

ASP

LEU

ALA

ARG

VAL

ASP

GLU

LEU

5

ARG

GLU

LEU

LYS

GLU

ILE

LEU

ARG

LYS

ASP

6

LEU

LYS

LEU

ALA

GLU

MET

LYS

GLU

7

ALA

GLU

ALA

GLY

ASN

LYS

GLU

ALA

VAL

8

GLU

LEU

GLU

GLN

LEU

GLU

GLY

LEU

9

LYS

ILE

GLN

ALA

MET

PHE

GLU

ALA

10

VAL

GLU

ALA

PHE

ARG

ALA

GLY

ASP

ARG

GLU

11

ARG

PHE

GLY

GLU

LEU

GLU

LYS

ILE

12

GLU

GLY

LYS

ALA

LEU

PRO

ASN

VAL

13

GLU

LYS

ILE

LYS

GLU

ALA

ILE

Samples:

sample_1: KABLE2.5, [U-100% 13C; U-100% 15N], 2.8 mM; HEPES 20 mM; sodium chloride 100 mM; 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
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCD)HD	sample_1	isotropic	sample_conditions_1
2D (HB)CB(CGCDCE)HE	sample_1	isotropic	sample_conditions_1
2D CB-CG	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	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