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 15614

Title: Solution structure of the complex between E.coli NusA-AR2 and RNAP-aCTD

Authors: Prasch, Stefan; Schweimer, Kristian; Roesch, Paul

Citation: Prasch, Stefan; Schweimer, Kristian; Roesch, Paul. "structural basis of transcription elongation control: the NusA-aCTD complex"  . ., .-..

Assembly members:
actd, polymer, 99 residues, 9014.511 Da.
ar2, polymer, 74 residues, 7470.336 Da.

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

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

Entity Sequences (FASTA):
actd: GPDLRDVRQPEVKEEKPEFD PILLRPVDDLELTVRSANCL KAEAIHYIGDLVQRTEVELL KTPNLGKKSLTEIKDVLASR GLSLGMRLENWPPASIADE
ar2: GPSLGDNKPADDLLNLEGVD RDLAFKLAARGVCTLEDLAE QGIDDLADIEGLTDEKAGAL IMAARNICWFGDEA

Data sets:
Data typeCount
13C chemical shifts540
15N chemical shifts170
1H chemical shifts1176

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11
2entity_22

Entities:

Entity 1, entity_1 99 residues - 9014.511 Da.

1   GLYPROASPLEUARGASPVALARGGLNPRO
2   GLUVALLYSGLUGLULYSPROGLUPHEASP
3   PROILELEULEUARGPROVALASPASPLEU
4   GLULEUTHRVALARGSERALAASNCYSLEU
5   LYSALAGLUALAILEHISTYRILEGLYASP
6   LEUVALGLNARGTHRGLUVALGLULEULEU
7   LYSTHRPROASNLEUGLYLYSLYSSERLEU
8   THRGLUILELYSASPVALLEUALASERARG
9   GLYLEUSERLEUGLYMETARGLEUGLUASN
10   TRPPROPROALASERILEALAASPGLU

Entity 2, entity_2 74 residues - 7470.336 Da.

1   GLYPROSERLEUGLYASPASNLYSPROALA
2   ASPASPLEULEUASNLEUGLUGLYVALASP
3   ARGASPLEUALAPHELYSLEUALAALAARG
4   GLYVALCYSTHRLEUGLUASPLEUALAGLU
5   GLNGLYILEASPASPLEUALAASPILEGLU
6   GLYLEUTHRASPGLULYSALAGLYALALEU
7   ILEMETALAALAARGASNILECYSTRPPHE
8   GLYASPGLUALA

Samples:

sample_1: actd, [U-98% 13C; U-98% 15N], 0.7 mM; ar2 2.1 mM; potassium phosphate 10 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM

sample_2: ar2, [U-98% 13C; U-98% 15N], 0.7 mM; actd 2.1 mM; potassium phosphate 10 mM; sodium chloride 50 mM; beta-mercaptoethanol 1 mM

sample_conditions_1: pH: 6.4; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_2isotropicsample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

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

NMR spectrometers:

  • Bruker Avance 800 MHz

Related Database Links:

PDB
DBJ BAA11840 BAB37583 BAE75528 BAE77996 BAG79094 BAB37473 BAE77215 BAG78979 BAI27449 BAI32628
EMBL CAA25337 CAA26395 CAA37838 CAA37839 CAD09171 CAA25200 CAP77631 CAQ33504 CAQ90641 CAR00133
GB AAA24577 AAA27214 AAA58092 AAC76320 AAG58416 AAA57972 AAC76203 AAG58305 AAN44677 AAN82367
PIR AB1009
REF NP_312187 NP_417754 NP_458485 NP_462319 NP_709083 NP_289745 NP_312077 NP_417638 NP_708970 NP_755793
SP A0KF45 A1AGI6 A1JS01 A4SSY1 A4TH15 P0AFF6 P0AFF7 P0AFF8 P0AFF9
BMRB 5800