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Biological Magnetic Resonance Data Bank


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BMRB Entry 19299

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19299
MolProbity Validation Chart

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Title: Analysis of target DNA binding sites through NMR structural analysis of the MLV IN CTD and homology modeling of the CCD domains.

Deposition date: 2013-06-12 Original release date: 2013-12-16

Authors: Aiyer, Sriram; Schneider, William; Chander, Ashwin; Roth, Monica; Montelione, Gaetano; Genomics Consortium, Northeast Structural; Rossi, Paolo

Citation: Aiyer, Sriram; Schneider, William; Chander, Ashwin; Montelione, Gaetano; Roth, Monica; Rossi, Paolo. "Analysis of target DNA binding sites through NMR structural analysis of the MLV IN CTD and homology modeling of the CCD domains."  Not known ., .-..

Assembly members:
OR41A-15.1, polymer, 91 residues, 10239.74 Da.

Natural source:   Common Name: Murine leukemia virus   Taxonomy ID: 11786   Superkingdom: Viruses   Kingdom: not available   Genus/species: Gammaretrovirus Murine leukemia virus

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

Entity Sequences (FASTA):
OR41A-15.1: MGHHHHHHSHMVGDTVWVRR HQTKNLEPRWKGPYTVLLTT PTALKVDGIAAWIHAAHVKA ADPGGGPSSRLTWRVQRSQN PLKIRLTREAP

Data sets:
Data typeCount
13C chemical shifts334
15N chemical shifts74
1H chemical shifts492

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1MLV CTD IN1

Entities:

Entity 1, MLV CTD IN 91 residues - 10239.74 Da.

The sequence used to solve the structure is a construct (329-408 amino acids) of the the full length Moloney murine leukemia virus integrase protein (IN)(408 amino acids). The construct has a non-cleavable tag at the N terminus (M G H H H H H H S H M) that is used for purification.

1   METGLYHISHISHISHISHISHISSERHIS
2   METVALGLYASPTHRVALTRPVALARGARG
3   HISGLNTHRLYSASNLEUGLUPROARGTRP
4   LYSGLYPROTYRTHRVALLEULEUTHRTHR
5   PROTHRALALEULYSVALASPGLYILEALA
6   ALATRPILEHISALAALAHISVALLYSALA
7   ALAASPPROGLYGLYGLYPROSERSERARG
8   LEUTHRTRPARGVALGLNARGSERGLNASN
9   PROLEULYSILEARGLEUTHRARGGLUALA
10   PRO

Samples:

sample_1: MLV IN CTD, [U-100% 13C; U-100% 15N], 0.5 mM; NaCl 100 mM; potassium glutamate 50 mM; MES 20 mM; DSS 50 uM

sample_2: MLV IN CTD, [U-10% 13C; U-100% 15N], 0.5 mM; NaCl 100 mM; potassium glutamate 50 mM; MES 20 mM; DSS 50 uM

sample_conditions_2: ionic strength: 150 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

sample_conditions_1: ionic strength: 150 mM; 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
3D HNCOsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HBHA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 13C-edited_NOESYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 13C-edited_NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
2D 1H-13C HSQCsample_2isotropicsample_conditions_2

Software:

AutoAssign v2.2.1, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - chemical shift assignment, structure solution

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

CNS v2.0.6, Brunger, Adams, Clore, Gros, Nilges and Read - geometry optimization, refinement

SPARKY v2.1, Goddard - peak picking

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

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Download simulated HSQC data in one of the following formats:
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