BMRB Entry 17035

Title:
NMR Solution Structure of asr4154 from Nostoc sp. PCC7120 Northeast Structural Genomics Consortium target ID Nsr143
Deposition date:
2010-06-30
Original release date:
2011-12-15
Authors:
Feldmann, Erik; Yang, Yunhuang; Ramelot, Theresa; Cort, John; Janjua, Haleema; Ciccosanti, Colleen; Lee, Dan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael
Citation:

Citation: Feldmann, Erik; Yang, Yunhuang; Ramelot, Theresa; Cort, John; Janjua, Haleema; Ciccosanti, Colleen; Lee, Dan; Acton, Thomas; Xiao, Rong; Everett, John; Montelione, Gaetano; Kennedy, Michael. "NMR Solution Structure of asr4154 from Nostoc sp. PCC7120 Northeast Structural Genomics target ID Nsr143"  .

Assembly members:

Assembly members:
Hypothetical_protein_asr4154_from_Nostoc_sp._PCC7120, polymer, 62 residues, 7352 Da.

Natural source:

Natural source:   Common Name: Nostoc sp. PCC 7120   Taxonomy ID: 103690   Superkingdom: Bacteria   Kingdom: Nostoc   Genus/species: not available Nostoc sp. PCC 7120

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET 21-23C

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Hypothetical_protein_asr4154_from_Nostoc_sp._PCC7120: MNLRWTSEAKTKLKNIPFFA RSQAKARIEQLARQAEQDIV TPELVEQARLEFGQLEHHHH HH

Data typeCount
13C chemical shifts254
15N chemical shifts67
1H chemical shifts414

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1asr41541

Entities:

Entity 1, asr4154 62 residues - 7352 Da.

Native asr4154 protein followed by 8 non-native C-terminal residues (LEHHHHHH)

1   METASNLEUARGTRPTHRSERGLUALALYS
2   THRLYSLEULYSASNILEPROPHEPHEALA
3   ARGSERGLNALALYSALAARGILEGLUGLN
4   LEUALAARGGLNALAGLUGLNASPILEVAL
5   THRPROGLULEUVALGLUGLNALAARGLEU
6   GLUPHEGLYGLNLEUGLUHISHISHISHIS
7   HISHIS

Samples:

NC_sample: Hypothetical protein asr4154 from Nostoc sp. PCC7120, [U-100% 13C; U-100% 15N], 0.9 ± 0.09 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

NC5_sample: Hypothetical protein asr4154 from Nostoc sp. PCC7120, [U-5% 13C; U-100% 15N], 0.82 ± 0.08 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; H2O 90%; D2O 10%

NC_sample_in_D2O: Hypothetical protein asr4154 from Nostoc sp. PCC7120, [U-100% 13C; U-100% 15N], 0.9 ± 0.09 mM; MES 20 ± 1 mM; sodium chloride 100 ± 5 mM; calcium chloride 5 ± 0.2 mM; DTT 10 ± 0.5 mM; sodium azide 0.02 ± 0.001 %; D2O 100%

sample_conditions_1: ionic strength: 0.2 M; pH: 6.5; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC_CTNC5_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESYNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D HNCANC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HN(CO)CANC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D HCCH-COSYNC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYNC_sample_in_D2Oisotropicsample_conditions_1
4D CC NOESYNC_sample_in_D2Oisotropicsample_conditions_1
2D 1H-15N HSQC_swN150ppmNC_sampleisotropicsample_conditions_1

Software:

NMRPipe v2008, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

VNMR v6.1C, Varian - collection

TOPSPIN v2.1.4, Bruker Biospin - collection

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

X-PLOR NIH v2.20, Schwieters, Kuszewski, Tjandra and Clore - structure solution

CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY v3.113, Goddard - data analysis

PSVS v1.4, Bhattacharya and Montelione - refinement

AutoAssign v2.30, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

PDBStat v5.1, (PdbStat)-Roberto Tejero and Gaetano T. Montelione - structure solution

PINE v1.0, Bahrami, A., Assadi, A., Markley, J. L. & Eghbalnia, H. - autoassignment

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

NMR spectrometers:

  • Varian INOVA 600 MHz
  • Bruker AvanceIII 850 MHz
  • Varian INOVA 500 MHz

Related Database Links:

PDB
DBJ BAB75853
GB ABA20375
REF WP_010998293

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