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- PDB-8qaj: NMR solution structure of C-terminal domain of CDNF -

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Basic information

Entry
Database: PDB / ID: 8qaj
TitleNMR solution structure of C-terminal domain of CDNF
ComponentsCerebral dopamine neurotrophic factor
KeywordsSIGNALING PROTEIN / neurotrophic factor
Function / homology
Function and homology information


dopaminergic neuron differentiation / growth factor activity / neuron projection development / endoplasmic reticulum / extracellular space
Similarity search - Function
ARMET, C-terminal / ARMET, N-terminal / ARMET-like / ARMET, C-terminal / ARMET, N-terminal / SAP domain superfamily
Similarity search - Domain/homology
Cerebral dopamine neurotrophic factor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing / molecular dynamics
AuthorsTossavainen, H. / Permi, P.
Funding support Finland, 1items
OrganizationGrant numberCountry
Academy of Finland Finland
CitationJournal: To Be Published
Title: NMR solution structure of C-terminal domain of CDNF
Authors: Tossavainen, H. / Permi, P.
History
DepositionAug 22, 2023Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 11, 2024Provider: repository / Type: Initial release
Revision 1.1Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Cerebral dopamine neurotrophic factor


Theoretical massNumber of molelcules
Total (without water)7,4731
Polymers7,4731
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: NMR Distance Restraints, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 300structures with the least restraint violations
RepresentativeModel #1fewest violations

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Components

#1: Protein Cerebral dopamine neurotrophic factor / ARMET-like protein 1 / Conserved dopamine neurotrophic factor


Mass: 7472.620 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: GSHM expression artefact / Source: (gene. exp.) Homo sapiens (human) / Gene: CDNF, ARMETL1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q49AH0
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
111isotropic32D 1H-15N HSQC
121isotropic32D 1H-13C HSQC aliphatic
131isotropic32D 1H-13C HSQC aromatic
141isotropic13D HN(COCA)CB
161isotropic13D HN(CA)CB
171isotropic13D HNCA
181isotropic13D HN(CO)CA
191isotropic13D HNCO
1101isotropic33D HCACO
1111isotropic13D C(CO)NH
1121isotropic13D H(CCO)NH
1131isotropic12D (HB)CB(CGCD)HD
1141isotropic12D (HB)CB(CGCDCE)HE
1151isotropic33D (H)CCH-COSY
1161isotropic33D HCCmHm-TOCSY
1171isotropic33D 1H-13C NOESY
1181isotropic33D 1H-15N NOESY

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Sample preparation

DetailsType: solution
Contents: 1 mM [U-13C; U-15N] C-CDNF, 20 mM sodium phosphate, 50 mM sodium chloride, 93% H2O/7% D2O
Label: sample1 / Solvent system: 93% H2O/7% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
1 mMC-CDNF[U-13C; U-15N]1
20 mMsodium phosphatenatural abundance1
50 mMsodium chloridenatural abundance1
Sample conditionsIonic strength: 0.15 M / Label: conditions1 / pH: 6.5 / Pressure: ambient atm / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA6001
Varian INOVAVarianINOVA8003

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Processing

NMR software
NameDeveloperClassification
TopSpinBruker Biospincollection
CcpNmr AnalysisCCPNdata analysis
CYANAGuntert, Mumenthaler and Wuthrichstructure calculation
AmberCase, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollmanrefinement
Refinement
MethodSoftware ordinal
simulated annealing3
molecular dynamics4
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 300 / Conformers submitted total number: 20

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