BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 19682

Title: Solution NMR Structure of PHD Type 1 Zinc Finger Domain 1 of Lysine-specific Demethylase Lid from Drosophila melanogaster, Northeast Structural Genomics Consortium (NESG) Target FR824J

Deposition date: 2013-12-13 Original release date: 2014-01-22

Authors: Xu, Xianzhong; Eletsky, Alexander; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Sukumaran, Dinesh; Montelione, Gaetano; Szyperski, Thomas

Citation: Xu, Xianzhong; Eletsky, Alexander; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Sukumaran, Dinesh; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of PHD Type 1 Zinc Finger Domain 1 from Lysine-specific Demethylase Lid from Drosophila melanogaster, Northeast Structural Genomics Consortium (NESG) Target FR824J"  To be published ., .-..

Assembly members:
FR824J, polymer, 94 residues, 10196.379 Da.
entity_ZN, non-polymer, 65.409 Da.

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):
FR824J: SHMSGGSPLATGTTANTRGA SQKKGGEPPALIVDPLMKYI CHICNRGDVEESMLLCDGCD DSYHTFCLLPPLTSIPKGEW LCPRCVVEEVSKPQ

Data sets:
Data typeCount
13C chemical shifts392
15N chemical shifts95
1H chemical shifts628

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1FR824J1
2Zn-12
3Zn-22

Entities:

Entity 1, FR824J 94 residues - 10196.379 Da.

Residues 1-3 represent a non-native affinity tag remainder after his tag cleavage.

1   SERHISMETSERGLYGLYSERPROLEUALA
2   THRGLYTHRTHRALAASNTHRARGGLYALA
3   SERGLNLYSLYSGLYGLYGLUPROPROALA
4   LEUILEVALASPPROLEUMETLYSTYRILE
5   CYSHISILECYSASNARGGLYASPVALGLU
6   GLUSERMETLEULEUCYSASPGLYCYSASP
7   ASPSERTYRHISTHRPHECYSLEULEUPRO
8   PROLEUTHRSERILEPROLYSGLYGLUTRP
9   LEUCYSPROARGCYSVALVALGLUGLUVAL
10   SERLYSPROGLN

Entity 2, Zn-1 - Zn - 65.409 Da.

1   ZN

Samples:

FR824J.004: FR824J 0.321 mM

FR824J.003: FR824J 0.321 mM

sample_conditions_1: pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCFR824J.003isotropicsample_conditions_1
3D HNCOFR824J.003isotropicsample_conditions_1
3D CBCA(CO)NHFR824J.003isotropicsample_conditions_1
3D HNCACBFR824J.003isotropicsample_conditions_1
3D HBHA(CO)NHFR824J.003isotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYFR824J.003isotropicsample_conditions_1
2D 1H-13C ct HSQC aliphaticFR824J.003isotropicsample_conditions_1
2D 1H-13C ct HSQC aromaticFR824J.003isotropicsample_conditions_1
3D HN(CA)COFR824J.003isotropicsample_conditions_1
3D (H)CCH-COSY-aliFR824J.003isotropicsample_conditions_1
3D (H)CCH-COSY aroFR824J.003isotropicsample_conditions_1
3D (H)CCH-TOCSY aliFR824J.003isotropicsample_conditions_1
2D gNfHSQC_HisFR824J.004isotropicsample_conditions_1
2D 1H-15N HSQCFR824J.004isotropicsample_conditions_1
2D 1H-13C ct-HSQC(28ms)FR824J.004isotropicsample_conditions_1
2D 1H-13C ct- HSQC(42ms)FR824J.004isotropicsample_conditions_1
2D 1H-13C ct-HSQC(56ms)FR824J.004isotropicsample_conditions_1
2D J-modulation HSQCFR824J.004isotropicsample_conditions_1

Software:

CNS, Brunger, Adams, Clore, Gros, Nilges and Read, David Wishart,Leigh Willard,Tim Jellard,Brian Sykes, Guntert, Keller and Wuthrich - data analysis, processing, refinemen, structure solution, geometry optimization

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - refinement, geometry optimization, structure solution

AutoStructure v2.1, Huang, Tejero, Powers and Montelione - data analysis, refinement

AutoAssign v2.1, Zimmerman, Moseley, Kulikowski and Montelione - data analysis, chemical shift assignment

XEASY, Bartels et al. - data analysis

VNMRJ, Varian - collection

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PSVS, Bhattacharya, Montelione - structure validation

NMR spectrometers:

  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz

Related Database Links:

UNP Q9VMJ7
PDB
GB AAF52319 AAM11379 AAN10569 AFH03582 AFH03583
REF NP_001245908 NP_001245909 NP_001245910 NP_001285649 NP_523486
SP Q9VMJ7

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts