BMRB Entry 18269

Name: Solution Structure of N-Terminal domain of human Conserved Dopamine Neurotrophic Factor (CDNF)
Published: 2012-06-13

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PDB ID: 2lpn
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18269
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of N-Terminal domain of human Conserved Dopamine Neurotrophic Factor (CDNF)

Deposition date:

2012-02-15

Original release date:

2012-06-13

Authors:

Cristiane, Latge; Katia, Cabral; Debora, Foguel; Pires, Jose Ricardo; Almeida, Marcius

Citation:

Citation: Latge, Cristiane; Cabral, Katia; Almeida, Marcius; Foguel, Debora. "(1)H-, (13)C- and (15)N-NMR assignment of the N-terminal domain of human cerebral dopamine neurotrophic factor (CDNF)" Biomol. NMR Assign. ., .-. (2012).
PubMed: 22528768

Assembly members:

Assembly members:
entity, polymer, 105 residues, 11965.022 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 Vector: pET25b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: QEAGGRPGADCEVCKEFLNR FYKSLIDRGVNFSLDTIEKE LISFCLDTKGKENRLCYYLG ATKDAATKILSEVTRPMSVH MPAMKICEKLKKLDSQICEL KYEKT

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	360
15N chemical shifts	98
1H chemical shifts	688

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	N-terminal domain of human CDNF	1

Entities:

Entity 1, N-terminal domain of human CDNF 105 residues - 11965.022 Da.

Mature sequence of N-terminal domain.

1

GLN

GLU

ALA

GLY

ARG

PRO

GLY

ALA

ASP

2

CYS

GLU

VAL

CYS

LYS

GLU

PHE

LEU

ASN

ARG

3

PHE

TYR

LYS

SER

LEU

ILE

ASP

ARG

GLY

VAL

4

ASN

PHE

SER

LEU

ASP

THR

ILE

GLU

LYS

GLU

5

LEU

ILE

SER

PHE

CYS

LEU

ASP

THR

LYS

GLY

6

LYS

GLU

ASN

ARG

LEU

CYS

TYR

LEU

GLY

7

ALA

THR

LYS

ASP

ALA

THR

LYS

ILE

LEU

8

SER

GLU

VAL

THR

ARG

PRO

MET

SER

VAL

HIS

9

MET

PRO

ALA

MET

LYS

ILE

CYS

GLU

LYS

LEU

10

LYS

LEU

ASP

SER

GLN

ILE

CYS

GLU

LEU

11

LYS

TYR

GLU

LYS

THR

Samples:

sample_1: CDNF, [U-100% 13C; U-100% 15N], 0.7 mM; D2O, [U-2H], 10%; sodium azide 5 mM; MES 20 mM; sodium chloride 150 mM; H2O 90%

sample_conditions_1: ionic strength: 175 mM; pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCA	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 HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - peak picking, refinement, structure solution

TOPSPIN v3, Bruker Biospin - collection, processing

CARA v1.8.4.2., Keller and Wuthrich - chemical shift assignment, data analysis

CNSSOLVE v1.1., Brunger, Adams, Clore, Gros, Nilges and Read - refinement, structure solution

NMR spectrometers:

Bruker Avance III 800 MHz

BMRB	19164
PDB	2LPN 2W50 4BIT
DBJ	BAG62825
GB	AAI33043 AAI33045 AIC53868 EAW86264 EHH18900
REF	NP_001025125 NP_001180755 XP_002820588 XP_003257694 XP_003806807
SP	Q49AH0
AlphaFold	Q49AH0