BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16556

Title: Solution NMR structure of Streptomyces coelicolor SCO3027 modelled with Zn+2 bound. Northeast Structural Genomics Consortium Target RR58.

Deposition date: 2009-10-15 Original release date: 2009-11-18

Authors: Ramelot, Theresa; Cort, John; Garcia, Maite; Yee, Adelinda; Arrowmith, Cheryl; Montelione, Gaetano; Kennedy, Michael

Citation: Ramelot, Theresa; Cort, John; Garcia, Maite; Yee, Adelinda; Arrowmith, Cheryl; Montelione, Gaetano; Kennedy, Michael. "Solution NMR structure of Streptomyces coelicolor SCO3027 modelled with Zn+2 bound. Northeast Structural Genomics Consortium Target RR58."  .

Assembly members:
RR58, polymer, 56 residues, 6000 Da.

Natural source:   Common Name: not available   Taxonomy ID: 1902   Superkingdom: 1   Kingdom: not available   Genus/species: not available not available

Experimental source:   Production method: recombinant technology' 'Escherichia coli' . . . Escherichia coli 'BL21(DE3) gold pMGK   Vector: 16556

Entity Sequences (FASTA):
RR58: MPLEAGLLEILACPACHAPL EERDAELICTGQDCGLAYPV RDGIPVLLVDEARRPE

Data sets:
Data typeCount
13C chemical shifts234
15N chemical shifts51
1H chemical shifts384

Time Domain Data

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RR581

Entities:

Entity 1, RR58 56 residues - 6000 Da.

1   METPROLEUGLUALAGLYLEULEUGLUILE
2   LEUALACYSPROALACYSHISALAPROLEU
3   GLUGLUARGASPALAGLULEUILECYSTHR
4   GLYGLNASPCYSGLYLEUALATYRPROVAL
5   ARGASPGLYILEPROVALLEULEUVALASP
6   GLUALAARGARGPROGLU

Samples:

NC_sample: Tris 10 ± 0.5 mM; sodium chloride' 'natural abundance 30; .mM – .5; .mM – .5; . %; ., 1, mM

NC_sample_in_D2O: Tris 10 ± 0.5 mM; sodium chloride' 'natural abundance 30; .mM – .5; .mM – .5; . %; ., 1, mM

NC7_sample: Tris 10 ± 0.5 mM; sodium chloride' 'natural abundance 30; .mM – .5; .mM – .5; . %; ., 1, mM

sample_conditions_1: ionic strength: 200 mM; pH: 7.0; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC aromNC_sampleisotropicsample_conditions_1
3D 1H-15N NOESYNC_sampleisotropicsample_conditions_1
3D 1H-13C NOESY aliphNC_sampleisotropicsample_conditions_1
3D HNCONC_sampleisotropicsample_conditions_1
3D CBCA(CO)NHNC_sampleisotropicsample_conditions_1
3D HNCACBNC_sampleisotropicsample_conditions_1
3D HBHA(CO)NHNC_sampleisotropicsample_conditions_1
3D HCCH-TOCSYNC_sampleisotropicsample_conditions_1
3D (H)CCH-TOCSYNC_sampleisotropicsample_conditions_1
4D HCCH NOESYNC_sample_in_D2Oisotropicsample_conditions_1
3D C(CO)NHNC_sampleisotropicsample_conditions_1
3D H(CCO)NHNC_sampleisotropicsample_conditions_1
2D 1H-13C HSQC ctNC7_sampleisotropicsample_conditions_1
2D 1H-15N HSQC fastNC_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

SPARKY v3.113, Goddard - data analysis

PSVS v1.3, Bhattacharya and Montelione - structure validation

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

PDBStat v5.0, (PDBStat) R. Tejero, G.T. Montelione - data analysis

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

NMR spectrometers:

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

Related Database Links:

PDB
EMBL CAB88911 CQR63713
GB AIJ15443 AIR98739 AKZ56116 EFD68867
REF NP_627249 WP_003975784

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