BMRB Entry 19541

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR19541
MolProbity Validation Chart

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Title:
Structure of the Nucleoplasmin-like N-terminal domain of Drosophila FKBP39
Deposition date:
2013-10-08
Original release date:
2014-10-27
Authors:
Artero, J.; Forsyth, T.; Callow, P.; Watson, A.; Zhang, W.; Laue, E.; EDLICH-MUTH, CHRISTIAN; Przewloka, M.; Edlich- muth, C.
Citation:

Citation: EDLICH-MUTH, CHRISTIAN. "Structure of the Nucleoplasmin-like N-terminal domain of FKBP39"  To BE Published ., .-..

Assembly members:

Assembly members:
39_KDA_FK506-BINDING_NUCLEAR_PROTEIN, polymer, 98 residues, 10810.4264 Da.

Natural source:

Natural source:   Common Name: fruit fly   Taxonomy ID: 7227   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Drosophila melanogaster

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: undefined   Vector: na

Entity Sequences (FASTA):

Entity Sequences (FASTA):
39_KDA_FK506-BINDING_NUCLEAR_PROTEIN: FQGAMAMFWGLNMKPERKYS QTIIKSFHISGVALDKGQEA KLYLAAEKQEYIVATVTKAI PQVALDLNFSKGDRIMFYTA GDASVSLLGYLHDIDSGS

Data typeCount
13C chemical shifts503
15N chemical shifts294
1H chemical shifts1382

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
139 KDA FK506-BINDING NUCLEAR PROTEIN, 11
239 KDA FK506-BINDING NUCLEAR PROTEIN, 21
339 KDA FK506-BINDING NUCLEAR PROTEIN, 31
439 KDA FK506-BINDING NUCLEAR PROTEIN, 41
539 KDA FK506-BINDING NUCLEAR PROTEIN, 51

Entities:

Entity 1, 39 KDA FK506-BINDING NUCLEAR PROTEIN, 1 98 residues - 10810.4264 Da.

1   PHEGLNGLYALAMETALAMETPHETRPGLY
2   LEUASNMETLYSPROGLUARGLYSTYRSER
3   GLNTHRILEILELYSSERPHEHISILESER
4   GLYVALALALEUASPLYSGLYGLNGLUALA
5   LYSLEUTYRLEUALAALAGLULYSGLNGLU
6   TYRILEVALALATHRVALTHRLYSALAILE
7   PROGLNVALALALEUASPLEUASNPHESER
8   LYSGLYASPARGILEMETPHETYRTHRALA
9   GLYASPALASERVALSERLEULEUGLYTYR
10   LEUHISASPILEASPSERGLYSER

Samples:

sample_1: 39 KDA FK506-BINDING NUCLEAR PROTEIN, [U-13C; U-15N], 0.5 mM; MgCl2 25 mM

sample_conditions_1: ionic strength: 50.000 mM; pH: 6.000; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1solutionsample_conditions_1
3D 1H-13C NOESYsample_1solutionsample_conditions_1
3D 1H-15N NOESYsample_1solutionsample_conditions_1
3D 1H-13C NOESYsample_1solutionsample_conditions_1
2D 1H-1H NOESYsample_1solutionsample_conditions_1
3D 1H-13C NOESYsample_1solutionsample_conditions_1
3D 1H-15N NOESYsample_1solutionsample_conditions_1
2Dsample_1solutionsample_conditions_1
S2_CNOEsample_1solutionsample_conditions_1
S3_NNOEsample_1solutionsample_conditions_1
C13_D2Osample_1solutionsample_conditions_1
M0sample_1solutionsample_conditions_1
N15sample_1solutionsample_conditions_1
NOE2H15Nsample_1solutionsample_conditions_1

Software:

ARIA2 v2.1, Linge, O'Donoghue and Nilges - chemical shift assignment

AutoDep v4.3, PDBe - chemical shift assignment

ANALYSIS v2.0, CCPN - chemical shift assignment

DANGLE v1.1, na - chemical shift assignment

NMRDraw vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

NMRPipe vany, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment

nmrView_any vany, Johnson, One Moon Scientific - chemical shift assignment

ARIA vany, Linge, O'Donoghue and Nilges - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

UNP FKB39_DROME
PDB
EMBL CAA86996
GB AAF55171 AAM11167 ACL85568 ACL90444 EDV48997
REF NP_524364 XP_001980039 XP_002031083 XP_002097757 XP_002103335
SP P54397
AlphaFold Q9VF88 P54397

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