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Biological Magnetic Resonance Data Bank


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BMRB Entry 18048

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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/BMR18048
MolProbity Validation Chart

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Title: NPM1_C70   PubMed: 22707729

Deposition date: 2011-11-09 Original release date: 2012-06-19

Authors: Banci, Lucia; Bertini, Ivano; Brunori, Maurizio; Di Matteo, Adele; Federici, Luca; Gallo, Angelo; Lo Sterzo, Carlo; Mori, Mirko

Citation: Gallo, Angelo; Lo Sterzo, Carlo; Mori, Mirko; Di Matteo, Adele; Bertini, Ivano; Banci, Lucia; Brunori, Maurizio; Federici, Luca. "Structure of nucleophosmin DNA-binding domain and analysis of its complex with a G-quadruplex sequence from the c-MYC promoter."  J. Biol. Chem. 287, 26539-26548 (2012).

Assembly members:
entity, polymer, 70 residues, 8101.407 Da.

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

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

Entity Sequences (FASTA):
entity: QESFKKQEKTPKTPKGPSSV EDIKAKMQASIEKGGSLPKV EAKFINYVKNCFRMTDQEAI QDLWQWRKSL

Data sets:
Data typeCount
13C chemical shifts276
15N chemical shifts73
1H chemical shifts241

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1NPM1_C701

Entities:

Entity 1, NPM1_C70 70 residues - 8101.407 Da.

1   GLNGLUSERPHELYSLYSGLNGLULYSTHR
2   PROLYSTHRPROLYSGLYPROSERSERVAL
3   GLUASPILELYSALALYSMETGLNALASER
4   ILEGLULYSGLYGLYSERLEUPROLYSVAL
5   GLUALALYSPHEILEASNTYRVALLYSASN
6   CYSPHEARGMETTHRASPGLNGLUALAILE
7   GLNASPLEUTRPGLNTRPARGLYSSERLEU

Samples:

sample_1: NPM1_C70, [U-15N], 0.5 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_2: NPM1_C70, [U-13C; U-15N], 0.5 mM; sodium phosphate 20 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 20 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

CARA v2.1, Keller and Wuthrich - chemical shift assignment

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER v11.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

PSVS, Bhattacharya and Montelione - validation

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Bruker Avance 700 MHz
  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAC25844 BAE22562 BAE26248 BAE26667 BAE32244
EMBL CAA34809 CAH90204
GB AAA36380 AAA36385 AAA36473 AAA36474 AAA39801
REF NP_001030518 NP_001125077 NP_001164790 NP_001238905 NP_001239100
SP P06748 P13084 Q3T160 Q61937
TPG DAA18048 DAA21326 DAA21327 DAA26330 DAA26331

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