BMRB Entry 18725

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18725
MolProbity Validation Chart

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Title:
Structure of Faap24 residues 141-215
Deposition date:
2012-09-18
Original release date:
2013-04-29
Authors:
Wienk, Hans; Slootweg, Jack; Kaptein, Robert; Boelens, Rolf; Folkers, Gert
Citation:

Citation: Wienk, Hans; Slootweg, Jack; Speerstra, Sietske; Kaptein, Robert; Boelens, Rolf; Folkers, Gert. "The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition."  Nucleic Acids Res. 41, 6739-6749 (2013).
PubMed: 23661679

Assembly members:

Assembly members:
Faap24, polymer, 95 residues, 10411.190 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: pLICHIS

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Faap24: MGSSHHHHHHSSHMLVPRGS SKNPLLGKKRALLLSEPSLL RTVQQIPGVGKVKAPLLLQK FPSIQQLSNASIGELEQVVG QAVAQQIHAFFTQPR

Data sets:
Data typeCount
13C chemical shifts341
15N chemical shifts79
1H chemical shifts560

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Faap241

Entities:

Entity 1, Faap24 95 residues - 10411.190 Da.

1   METGLYSERSERHISHISHISHISHISHIS
2   SERSERHISMETLEUVALPROARGGLYSER
3   SERLYSASNPROLEULEUGLYLYSLYSARG
4   ALALEULEULEUSERGLUPROSERLEULEU
5   ARGTHRVALGLNGLNILEPROGLYVALGLY
6   LYSVALLYSALAPROLEULEULEUGLNLYS
7   PHEPROSERILEGLNGLNLEUSERASNALA
8   SERILEGLYGLULEUGLUGLNVALVALGLY
9   GLNALAVALALAGLNGLNILEHISALAPHE
10   PHETHRGLNPROARG

Samples:

sample_1: FAAP24, [U-100% 13C; U-100% 15N], 0.2 mM; sodium phosphate 50 mM; sodium chloride 100 mM; PMSF 0.2 mM; D2O 7%; H2O 93%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

ProcheckNMR, Laskowski and MacArthur - data analysis

WhatIF, Vriend - data analysis

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz

Related Database Links:

BMRB 19303
PDB
DBJ BAG54708
GB AAH03535 AAH10170 AAH20247 ADQ32151 AIC52732
REF NP_001287907 NP_689479 XP_002762034 XP_003780763 XP_003816251
SP Q9BTP7
AlphaFold Q9BTP7

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