BMRB Entry 53123

Name: Backbone assignment of the designed protein TFD-EE bound to Lanthanum.
Published: 2025-11-06

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR53123

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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 assignment of the designed protein TFD-EE bound to Lanthanum.

Deposition date:

2025-05-06

Original release date:

2025-11-06

Authors:

Delhommel, Florent; Wagner Egea, Paula; Zeymer, Cathleen; Sattler, Michael

Citation:

Citation: Wagner Egea, Paula; Delhommel, Florent; Ghulam, Mustafa; Leiss-Maier, Florian; Klimper, Lisa; Badmann, Thomas; Heider, Anna; Wille, Idoai; Groll, Michael; Sattler, Michael; Zeymer, Cathleen. "Modular protein scaffold architecture and AI-guided sequence optimization facilitate de novo metalloenzyme engineering" Structure ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 172 residues, Formula weight is not available
entity_LA, non-polymer, 138.905 Da.

Natural source:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GAMGDILIVWAKDVDEMLKQ VEILRRLGAKQIAVESSDWR ILQEALKKGGDILIVNGGGM TITFRGDDLEALLKAAIEMI KQALKFGATITLSLDGNDLN INITGVPEQVRKELAKEAER LAKEFGITVTRTGGGDVDEM LKQVEILRRLGAKQIAVESD DWRILQEALKKG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	479
15N chemical shifts	164
1H chemical shifts	164

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	TFD-EE	1
2	La	2

Entities:

Entity 1, TFD-EE 172 residues - Formula weight is not available

1

GLY

ALA

MET

GLY

ASP

ILE

LEU

ILE

VAL

TRP

2

ALA

LYS

ASP

VAL

ASP

GLU

MET

LEU

LYS

GLN

3

VAL

GLU

ILE

LEU

ARG

LEU

GLY

ALA

LYS

4

GLN

ILE

ALA

VAL

GLU

SER

ASP

TRP

ARG

5

ILE

LEU

GLN

GLU

ALA

LEU

LYS

GLY

6

ASP

ILE

LEU

ILE

VAL

ASN

GLY

MET

7

THR

ILE

THR

PHE

ARG

GLY

ASP

LEU

GLU

8

ALA

LEU

LYS

ALA

ILE

GLU

MET

ILE

9

LYS

GLN

ALA

LEU

LYS

PHE

GLY

ALA

THR

ILE

10

THR

LEU

SER

LEU

ASP

GLY

ASN

ASP

LEU

ASN

11

ILE

ASN

ILE

THR

GLY

VAL

PRO

GLU

GLN

VAL

12

ARG

LYS

GLU

LEU

ALA

LYS

GLU

ALA

GLU

ARG

13

LEU

ALA

LYS

GLU

PHE

GLY

ILE

THR

VAL

THR

14

ARG

THR

GLY

ASP

VAL

ASP

GLU

MET

15

LEU

LYS

GLN

VAL

GLU

ILE

LEU

ARG

LEU

16

GLY

ALA

LYS

GLN

ILE

ALA

VAL

GLU

SER

ASP

17

ASP

TRP

ARG

ILE

LEU

GLN

GLU

ALA

LEU

LYS

18

LYS

GLY

Entity 2, La - La - 138.905 Da.

1

LA

Samples:

sample_1: TFD-EE, [U-100% 13C; U-100% 15N], 2 mM; Lanthanum 1 mM; HEPES 25 mM; sodium chloride 25 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D CBCACONH	sample_1	isotropic	sample_conditions_1
3D HN(CA)CO	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v2.4.2 - chemical shift assignment

NMRPipe - processing

TOPSPIN - collection

NMR spectrometers:

Bruker AVANCE III 900 MHz

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