BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18547

Title: Solution NMR Structure of CalU16 from Micromonospora echinospora, Northeast Structural Genomics Consortium (NESG) Target MiR12

Authors: Ramelot, Theresa; Yang, Yunhuang; Lee, Hsiau-Wei; Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Wrobel, Russel; Bingman, Craig; Singh, Shanteri; Thorson, Jon; Prestegard, James; Montelione, Gaetano; Phillips Jr., George; Kennedy, Michael

Citation: Ramelot, Theresa; Yang, Yunhuang; Lee, Hsiau-Wei; Pederson, Kari; Lee, Dan; Kohan, Eitan; Janjua, Haleema; Xiao, Rong; Acton, Thomas; Everett, John; Wrobel, Russel; Bingman, Craig; Singh, Shanteri; Thorson, Jon; Prestegard, James; Montelione, Gaetano; Phillips Jr., George; Kennedy, Michael. "Solution NMR Structure of CalU16 from Micromonospora echinospora, Northeast Structural Genomics Consortium (NESG) Target MiR12"  To be published ., .-..

Assembly members:
MiR12, polymer, 192 residues, 21347.8 Da.

Natural source:   Common Name: high GC Gram+   Taxonomy ID: 1877   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Micromonospora echinospora

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

Entity Sequences (FASTA):
MiR12: MGHHHHHHSHMASGQATERA LGRRTIPAGEARSIIIRQRY DAPVDEVWSACTDPNRINRW FIEPKGDLREGGNFALQGNA SGDILRCEPPRRLTISWVYE GKPDSEVELRLSEEGDGTLL ELEHATTSEQMLVEVGVGWE MALDFLGMFIRGDLPGGPVP EDAAEEFEPSPEMMRISQER GEAWAALVHSGS

Data sets:
Data typeCount
13C chemical shifts783
15N chemical shifts201
1H chemical shifts1258

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1MiR121

Entities:

Entity 1, MiR12 192 residues - 21347.8 Da.

1   METGLYHISHISHISHISHISHISSERHIS
2   METALASERGLYGLNALATHRGLUARGALA
3   LEUGLYARGARGTHRILEPROALAGLYGLU
4   ALAARGSERILEILEILEARGGLNARGTYR
5   ASPALAPROVALASPGLUVALTRPSERALA
6   CYSTHRASPPROASNARGILEASNARGTRP
7   PHEILEGLUPROLYSGLYASPLEUARGGLU
8   GLYGLYASNPHEALALEUGLNGLYASNALA
9   SERGLYASPILELEUARGCYSGLUPROPRO
10   ARGARGLEUTHRILESERTRPVALTYRGLU
11   GLYLYSPROASPSERGLUVALGLULEUARG
12   LEUSERGLUGLUGLYASPGLYTHRLEULEU
13   GLULEUGLUHISALATHRTHRSERGLUGLN
14   METLEUVALGLUVALGLYVALGLYTRPGLU
15   METALALEUASPPHELEUGLYMETPHEILE
16   ARGGLYASPLEUPROGLYGLYPROVALPRO
17   GLUASPALAALAGLUGLUPHEGLUPROSER
18   PROGLUMETMETARGILESERGLNGLUARG
19   GLYGLUALATRPALAALALEUVALHISSER
20   GLYSER

Samples:

mir12.006: mir12.006, [U-100% 13C; U-100% 15N], 0.9 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

mir12.006_d2o: mir12.006, [U-100% 13C; U-100% 15N], 0.9 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 100%; DSS 50 uM

mir12.011: mir12.011, [U-100% 13C; U-100% 15N], 0.9 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

mir12.008_NC5: mir12.008, [U-100% 15N], 5% 13C stereo, 0.9 mM; NaN3 0.02%; DTT 10 mM; CaCL2 5 mM; NaCL 100 mM; Proteinase Inhibitors 1 x; MES pH 6.5 20 mM; D2O 10%; DSS 50 uM; H2O 90%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCmir12.006isotropicsample_conditions_1
2D 1H-13C HSQCmir12.006isotropicsample_conditions_1
3D HNCOmir12.006isotropicsample_conditions_1
3D CBCA(CO)NHmir12.006isotropicsample_conditions_1
3D HNCACBmir12.006isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticmir12.006isotropicsample_conditions_1
3D 1H-13C NOESY aromaticmir12.006isotropicsample_conditions_1
3D HCCH-TOCSYmir12.006isotropicsample_conditions_1
3D (H)CCH-TOCSYmir12.006_d2oisotropicsample_conditions_1
2D 1H-13C HSQCmir12.008_NC5isotropicsample_conditions_1
4D CC-NOESYmir12.006_d2oisotropicsample_conditions_1
3D HBHA(CO)NHmir12.006isotropicsample_conditions_1
3D HCCH-COSYmir12.006isotropicsample_conditions_1
3D C(CO)NHmir12.006isotropicsample_conditions_1
3D H(CCO)NHmir12.006isotropicsample_conditions_1
NUS 3D 1H-13C NOESY aliphaticmir12.011isotropicsample_conditions_1
NUS 3D 1H-15N NOESYmir12.011isotropicsample_conditions_1
3D 1H-15N NOESYmir12.006isotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - refinemen,structure solution,geometry optimization

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

AutoStruct vASDP-1.0, Huang, Tejero, Powers and Montelione - data analysis,refinement

NMRPipe v2008 linux9, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

TOPSPIN v2.1.4 and 3.1, Bruker Biospin - collection

VNMRJ v1.1 D, Varian - collection

PINE, Bahrami, Markley, Assadi, and Eghbalnia - chemical shift assignment

SPARKY v3.113, Goddard - data analysis

TALOS+, Shen, Cornilescu, Delaglio and Bax - geometry optimization

PALES, PALES (Zweckstetter, Bax) - geometry optimization

PSVS v1.5, Bhattacharya, Montelione - structure validation

FMCGUI, Alex Lemak, Cheryl Arrowsmith, University of Toronto - refinement

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Varian INOVA 600 MHz
  • Bruker AvanceIII 600 MHz

Related Database Links:

UNP Q8KNE9
PDB
GB AAM70339