BMRB Entry 52737

Name: SERBP1 1-149
Published: 2025-11-19

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52737

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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:

SERBP1 1-149

Deposition date:

2024-12-02

Original release date:

2025-11-19

Authors:

Baudin, Antoine; Dinh, Hoang; Xu, Xiaoping; Libich, David

Citation:

Citation: Baudin, Antoine; Dinh, Hoang; Xu, Xiaoping; Libich, David. "The 1H, 15N and 13C backbone resonance assignments of the N-terminal (1-149) domain of Serpine mRNA Binding Protein 1 (SERBP1)" Biomol. NMR Assign. 19, 101-107 (2025).
PubMed: 40153110

Assembly members:

Assembly members:
entity_1, polymer, 149 residues, Formula weight is not available

Natural source:

Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pAG8Ha-SERBP1(1-149)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MPGHLQEGFGCVVTNRFDQL FDDESDPFEVLKAAENKKKE AGGGGVGGPGAKSAAQAAAQ TNSNAAGKQLRKESQKDRKN PLPPSVGVVDKKEETQPPVA LKKEGIRRVGRRPDQQLQGE GKIIDRRPERRPPRERRFEK PLEEKGEGG

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	406
15N chemical shifts	129
1H chemical shifts	271

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SERBP1	1

Entities:

Entity 1, SERBP1 149 residues - Formula weight is not available

1

MET

PRO

GLY

HIS

LEU

GLN

GLU

GLY

PHE

GLY

2

CYS

VAL

THR

ASN

ARG

PHE

ASP

GLN

LEU

3

PHE

ASP

GLU

SER

ASP

PRO

PHE

GLU

VAL

4

LEU

LYS

ALA

GLU

ASN

LYS

GLU

5

ALA

GLY

VAL

GLY

PRO

GLY

6

ALA

LYS

SER

ALA

GLN

ALA

GLN

7

THR

ASN

SER

ASN

ALA

GLY

LYS

GLN

LEU

8

ARG

LYS

GLU

SER

GLN

LYS

ASP

ARG

LYS

ASN

9

PRO

LEU

PRO

SER

VAL

GLY

VAL

ASP

10

LYS

GLU

THR

GLN

PRO

VAL

ALA

11

LEU

LYS

GLU

GLY

ILE

ARG

VAL

GLY

12

ARG

PRO

ASP

GLN

LEU

GLN

GLY

GLU

13

GLY

LYS

ILE

ASP

ARG

PRO

GLU

ARG

14

ARG

PRO

ARG

GLU

ARG

PHE

GLU

LYS

15

PRO

LEU

GLU

LYS

GLY

GLU

GLY

Samples:

sample_1: SERBP1 1-149, [U-13C; U-15N], 400 uM; Na2HPO4 20 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.8; pressure: 1 atm; temperature: 278 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	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 HNHA	sample_1	isotropic	sample_conditions_1

Software:

CcpNMR v3 - chemical shift assignment

NMR spectrometers:

Bruker AVANCE NEO 700 MHz

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