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Biological Magnetic Resonance Data Bank


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BMRB Entry 17670

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17670
MolProbity Validation Chart

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Title: Solution NMR Structure of Protein AAur_3427 from Arthrobacter aurescens, Northeast Structural Genomics Consortium Target AaR96

Deposition date: 2011-05-27 Original release date: 2011-06-24

Authors: Eletsky, Alexander; Lee, Hsiau-Wei; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas

Citation: Eletsky, Alexander; Lee, Hsiau-Wei; Wang, Dongyan; Ciccosanti, Colleen; Janjua, Haleema; Nair, Rajesh; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of Protein AAur_3427 from Arthrobacter aurescens, Northeast Structural Genomics Consortium Target AaR96"  To be published ., .-..

Assembly members:
AaR96, polymer, 172 residues, 19625.873 Da.

Natural source:   Common Name: Arthrobacter aurescens   Taxonomy ID: 290340   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Arthrobacter aurescens

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

Entity Sequences (FASTA):
AaR96: TVVSVDKDVEALSFSIVAEF DADVKRVWAIWEDPRQLERW WGPPTWPATFETHEFTVGGK AAYYMTGPDGTKARGWWQFT TIEAPDHLEFDDGFADEHGA PVDELGVTHATVKLEPLENR TRMTIISTFESEEQMQKMAE MGMEEGMREAIEQIDAVLSE PANALEHHHHHH

Data sets:
Data typeCount
13C chemical shifts744
15N chemical shifts179
1H chemical shifts1170

Time Domain Data

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1AaR961

Entities:

Entity 1, AaR96 172 residues - 19625.873 Da.

Residues 1-164 correspond to the range 2-165 in the native protein. Residues 165-172 represent a non-native affinity tag.

1   THRVALVALSERVALASPLYSASPVALGLU
2   ALALEUSERPHESERILEVALALAGLUPHE
3   ASPALAASPVALLYSARGVALTRPALAILE
4   TRPGLUASPPROARGGLNLEUGLUARGTRP
5   TRPGLYPROPROTHRTRPPROALATHRPHE
6   GLUTHRHISGLUPHETHRVALGLYGLYLYS
7   ALAALATYRTYRMETTHRGLYPROASPGLY
8   THRLYSALAARGGLYTRPTRPGLNPHETHR
9   THRILEGLUALAPROASPHISLEUGLUPHE
10   ASPASPGLYPHEALAASPGLUHISGLYALA
11   PROVALASPGLULEUGLYVALTHRHISALA
12   THRVALLYSLEUGLUPROLEUGLUASNARG
13   THRARGMETTHRILEILESERTHRPHEGLU
14   SERGLUGLUGLNMETGLNLYSMETALAGLU
15   METGLYMETGLUGLUGLYMETARGGLUALA
16   ILEGLUGLNILEASPALAVALLEUSERGLU
17   PROALAASNALALEUGLUHISHISHISHIS
18   HISHIS

Samples:

NC: AaR96, [U-100% 13C; U-100% 15N], 0.6 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5: AaR96, [5% 13C; U-100% 15N], 1.7 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; H2O 90%; D2O 10%

NC5_PEG: AaR96, [5% 13C; U-100% 15N], 1.2 mM; MES 20 mM; sodium chloride 100 mM; calcium chloride 5 mM; DTT 10 mM; DSS 50 uM; sodium azide 0.02%; C12E5 PEG 4%; hexanol 1.3%; H2O 80%; D2O 20%

NC5_Phage: AaR96, [5% 13C; U-100% 15N], 1.1 mM; MES 13 mM; sodium chloride 70 mM; calcium chloride 3 mM; DTT 10 mM; DSS 33 uM; sodium azide 0.02%; Pf1 phage 12.5 g/l; H2O 80%; D2O 20%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aliphaticNCisotropicsample_conditions_1
3D HNCONCisotropicsample_conditions_1
3D CBCA(CO)NHNCisotropicsample_conditions_1
3D HNCACBNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC aromaticNCisotropicsample_conditions_1
3D simutaneous 13C-aromatic,13C-aliphatic,15N edited 1H-1H NOESYNCisotropicsample_conditions_1
3D (H)CCH-TOCSY aliphaticNCisotropicsample_conditions_1
3D HBHA(CO)NHNCisotropicsample_conditions_1
3D HN(CA)CONCisotropicsample_conditions_1
2D 1H-15N LR-HSQC histidineNCisotropicsample_conditions_1
2D (HB)CB(CGCDCE)HDHENCisotropicsample_conditions_1
(4,3)D GFT HCCH-COSY aliphaticNCisotropicsample_conditions_1
3D HCCH-COSY aromaticNCisotropicsample_conditions_1
2D 1H-13C CT-HSQC methylNC5isotropicsample_conditions_1
1D 15N T1NCisotropicsample_conditions_1
1D 15N T2NCisotropicsample_conditions_1
2D J-mod 1H-15N HSQCNC5isotropicsample_conditions_1
2D J-mod 1H-15N HSQCNC5_PEGisotropicsample_conditions_1
2D J-mod 1H-15N HSQCNC5_Phageisotropicsample_conditions_1

Software:

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement,structure solution,geometry optimization

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

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

AutoAssign v2.3.0, Zimmerman, Moseley, Kulikowski and Montelione - data analysis,chemical shift assignment

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

XEASY v1.3.13, Bartels et al. - data analysis

TOPSPIN v2.1, Bruker Biospin - collection, processing

VNMRJ v2.2D, Varian - collection

TALOS+ v1.2009.0721.18, Shen, Cornilescu, Delaglio and Bax - geometry optimization

CARA v1.8.4, Keller and Wuthrich - chemical shift assignment, data analysis, peak picking

PROSA v6.4, Guntert - processing

NMR spectrometers:

  • Bruker Avance 900 MHz
  • Varian INOVA 600 MHz
  • Varian INOVA 750 MHz
  • Varian INOVA 600 MHz
  • Bruker Avance 700 MHz

Related Database Links:

PDB
GB ABM10196 AFR30444
REF WP_011776048 WP_014922734

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