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Biological Magnetic Resonance Data Bank


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BMRB Entry 17965

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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/BMR17965
MolProbity Validation Chart

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Title: Solution NMR structure of Alr2454 protein from Nostoc sp. strain PCC 7120, Northeast Structural Genomics Consortium Target NsR264

Deposition date: 2011-09-30 Original release date: 2011-10-24

Authors: Aramini, James; Lee, Dong yup; Ciccosanti, Colleen; Janjua, Haleema; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano

Citation: Aramini, James; Lee, Dong yup; Ciccosanti, Colleen; Janjua, Haleema; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano. "Solution NMR structure of Alr2454 protein from Nostoc sp. strain PCC 7120, Northeast Structural Genomics Consortium Target NsR264"  To be published ., .-..

Assembly members:
NsR264, polymer, 110 residues, 12163.996 Da.

Natural source:   Common Name: Nostoc sp.   Taxonomy ID: 1180   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Nostoc sp.

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

Entity Sequences (FASTA):
NsR264: MTGQELRQLLLDKWGYSYDV QFRRTQGKIFLQVMWKYLEQ ASFPMNETEYQEHLDSVANY LHALGGAVQVKTFITQTKER PRLGKAVSIPLDLGERASEW IILEHHHHHH

Data sets:
Data typeCount
13C chemical shifts500
15N chemical shifts119
1H chemical shifts790

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1NsR2641

Entities:

Entity 1, NsR264 110 residues - 12163.996 Da.

C-terminal LEHHHHHH purification tag

1   METTHRGLYGLNGLULEUARGGLNLEULEU
2   LEUASPLYSTRPGLYTYRSERTYRASPVAL
3   GLNPHEARGARGTHRGLNGLYLYSILEPHE
4   LEUGLNVALMETTRPLYSTYRLEUGLUGLN
5   ALASERPHEPROMETASNGLUTHRGLUTYR
6   GLNGLUHISLEUASPSERVALALAASNTYR
7   LEUHISALALEUGLYGLYALAVALGLNVAL
8   LYSTHRPHEILETHRGLNTHRLYSGLUARG
9   PROARGLEUGLYLYSALAVALSERILEPRO
10   LEUASPLEUGLYGLUARGALASERGLUTRP
11   ILEILELEUGLUHISHISHISHISHISHIS

Samples:

NsR264_007: NsR264, [U-100% 13C; U-100% 15N], 1.01 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; H2O 90%; D2O 10%

NsR264_008: NsR264, [U-5% 13C; U-100% 15N], 0.567 mM; ammonium acetate 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; sodium azide 0.02%; DSS 50 uM; H2O 90%; D2O 10%

sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNsR264_007isotropicsample_conditions_1
2D 1H-13C HSQCNsR264_007isotropicsample_conditions_1
3D 1H-15N NOESYNsR264_007isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticNsR264_007isotropicsample_conditions_1
3D 1H-13C NOESY aromaticNsR264_007isotropicsample_conditions_1
2D 1H-13C HSQC high resolution (L/V methyl stereoassignment)NsR264_008isotropicsample_conditions_1
3D HNCONsR264_007isotropicsample_conditions_1
3D HN(CA)CONsR264_007isotropicsample_conditions_1
3D HNCANsR264_007isotropicsample_conditions_1
3D HN(CO)CANsR264_007isotropicsample_conditions_1
3D CBCA(CO)NHNsR264_007isotropicsample_conditions_1
3D HNCACBNsR264_007isotropicsample_conditions_1
3D HBHA(CO)NHNsR264_007isotropicsample_conditions_1
3D HCCH-TOCSYNsR264_007isotropicsample_conditions_1
3D CCH-TOCSYNsR264_007isotropicsample_conditions_1
3D HCCH COSYNsR264_007isotropicsample_conditions_1
1D 15N T1 and T2NsR264_007isotropicsample_conditions_1
2D 1H-15N hetNOENsR264_007isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

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

AutoStruct v2.2.1, Huang, Tejero, Powers and Montelione - RPF analysis

NMRPipe v2.3, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1, Bruker Biospin - collection, data analysis

PINE v1.0, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY v3.112, Goddard - data analysis, peak picking

TALOS+, Shen, Cornilescu, Delaglio and Bax - dihedral angle constraints, geometry optimization

PSVS v1.4, Bhattacharya and Montelione - structure quality analysis

MolProbity v3.18, Richardson - structure quality analysis

PDBStat v5.4, Tejero & Montelione - PDB coordinate analysis

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker Avance 600 MHz

Related Database Links:

PDB
DBJ BAB74153
GB ABA20012
REF WP_010996610

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