BMRB Entry 34548

Name: Structure of the cis-(Tyr39-Pro40) form of the Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1)
Published: 2021-01-06

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PDB ID: 6zzf
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34548
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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:

Structure of the cis-(Tyr39-Pro40) form of the Human Secreted Ly-6/uPAR Related Protein-1 (SLURP-1)

Deposition date:

2020-08-04

Original release date:

2021-01-06

Authors:

Paramonov, A.; Lyukmanova, E.; Shenkarev, Z.

Citation:

Citation: Shulepko, Mikhail; Bychkov, Maxim; Shenkarev, Zakhar; Kulbatskii, Dmitrii; Makhonin, Alexey; Paramonov, Alexander; Chugunov, Anton; Kirpichnikov, Mikhail; Lyukmanova, Ekaterina. "Biochemical Basis of Skin Disease Mal de Meleda: SLURP-1 Mutants Differently Affect Keratinocyte Proliferation and Apoptosis" J. Invest. Dermatol. 141, 2229-2237 (2021).
PubMed: 33741389

Assembly members:

Assembly members:
entity_1, polymer, 82 residues, 8992.360 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 BL21(DE3) Vector: pET-22b(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: MLKCYTCKEPMTSASCRTIT RCKPEDTACMTTLVTVEAEY PFNQSPVVTRSCSSSCVATD PDSIGAAHLIFCCFRDLCNS EL

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	319
15N chemical shifts	82
1H chemical shifts	535

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	unit_1	1

Entities:

Entity 1, unit_1 82 residues - 8992.360 Da.

1

MET

LEU

LYS

CYS

TYR

THR

CYS

LYS

GLU

PRO

2

MET

THR

SER

ALA

SER

CYS

ARG

THR

ILE

THR

3

ARG

CYS

LYS

PRO

GLU

ASP

THR

ALA

CYS

MET

4

THR

LEU

VAL

THR

VAL

GLU

ALA

GLU

TYR

5

PRO

PHE

ASN

GLN

SER

PRO

VAL

THR

ARG

6

SER

CYS

SER

CYS

VAL

ALA

THR

ASP

7

PRO

ASP

SER

ILE

GLY

ALA

HIS

LEU

ILE

8

PHE

CYS

PHE

ARG

ASP

LEU

CYS

ASN

SER

9

GLU

LEU

Samples:

sample_1: SLURP-1, [U-15N], 0.3 ± 0.03 mM

sample_2: SLURP-1, [U-13C; U-15N], 0.3 ± 0.03 mM

sample_3: SLURP-1, [U-13C; U-15N], 0.3 ± 0.03 mM

sample_conditions_1: ionic strength: 10 mM; pH: 4.7; pressure: 1 atm; temperature: 310 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1

Software:

CYANA v3.98.13, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA v1.8, Keller and Wuthrich - chemical shift assignment

TopSpin, Bruker Biospin - collection

MddNMR, V. Orekhov, V. Jaravine, M. Mayzel, K. Kazimierczuk, Swedish NMR Center, University of Gothenburg - processing

CARA, Keller and Wuthrich - peak picking

NMR spectrometers:

Bruker AVANCE III 800 MHz
Bruker AVANCE 700 MHz

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