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PDB ID: 7xx8
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR36490
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry

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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Name: Solution structure of RRM1 of Human SART3
Published: 2026-03-30

Title:

Solution structure of RRM1 of Human SART3

Deposition date:

2022-05-29

Original release date:

2026-03-30

Authors:

Kim, I.; Bang, K.; Park, C.; Kim, N.; Suh, J.

Citation:

Citation: Kim, Iktae; Bang, Kyeong-Mi; An, So Young; Park, Changkon; Shin, Ji-Yeon; Kim, Youngim; Song, Hyun Kyu; Suh, Jeong-Yong; Kim, Nak-Kyoon. "Structural investigation of human U6 snRNA recognition by spliceosomal recycling factor SART3 RNA recognition motifs" FEBS J. 293, 1323-1340 (2026).
PubMed: 41046346

Assembly members:

Assembly members:
Squamous cell carcinoma antigen recognized by T-cells 3, polymer, 94 residues, 10738.19 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Squamous cell carcinoma antigen recognized by T-cells 3: GSHMHDSSKDSITVFVSNLP YSMQEPDTKLRPLFEACGEV VQIRPIFSNRGDFRGYCYVE FKEEKSALQALEMDRKSVEG RPMFVSPCVDKSKN

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	366
15N chemical shifts	87
1H chemical shifts	588

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 94 residues - 10738.19 Da.

1

GLY

SER

HIS

MET

HIS

ASP

SER

LYS

ASP

2

SER

ILE

THR

VAL

PHE

VAL

SER

ASN

LEU

PRO

3

TYR

SER

MET

GLN

GLU

PRO

ASP

THR

LYS

LEU

4

ARG

PRO

LEU

PHE

GLU

ALA

CYS

GLY

GLU

VAL

5

VAL

GLN

ILE

ARG

PRO

ILE

PHE

SER

ASN

ARG

6

GLY

ASP

PHE

ARG

GLY

TYR

CYS

TYR

VAL

GLU

7

PHE

LYS

GLU

LYS

SER

ALA

LEU

GLN

ALA

8

LEU

GLU

MET

ASP

ARG

LYS

SER

VAL

GLU

GLY

9

ARG

PRO

MET

PHE

VAL

SER

PRO

CYS

VAL

ASP

10

LYS

SER

LYS

ASN

Samples:

sample_1: RRM1 of Human SART3, [U-100% 13C; U-100% 15N], 0.8 mM; DTT 1 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%

sample_conditions_1: ionic strength: 20 mM; pH: 6.5; pressure: 1 atm; temperature: 298 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 HBHA(CO)NH	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
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRFAM-SPARKY, NMRFAM-SPARKY - chemical shift assignment

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TopSpin, Bruker Biospin - collection

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation

NMR spectrometers:

Bruker ascend 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 36490