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 17414

Title: Structure of an engineered splicing intein mutant based on Mycobacterium tuberculosis RecA   PubMed: 21604815

Deposition date: 2011-01-19 Original release date: 2012-01-04

Authors: Du, Zhenming; Wang, Chunyu

Citation: Du, Zhenming; Zheng, Yuchuan; Liu, Yangzhong; Belfort, Marlene; Wang, Chunyu. "pK(a) coupling at the intein active site: implications for the coordination mechanism of protein splicing with a conserved aspartate"  J. Am. Chem. Soc. 133, 10275-10282 (2011).

Assembly members:
RecA, polymer, 139 residues, 15365.621 Da.

Natural source:   Common Name: high GC Gram+   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

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

Entity Sequences (FASTA):
RecA: CLAEGTRIFDPVTGTTHRIE DVVGGRKPIHVVAAAKDGTL HARPVVSWFDQGTRDVIGLR IAGGAILWATPDHKVLTEYG WRAAGELRKGDRVAVRDVET GELRYSVIREVLPTRRARTF DLEVEELHTLVAEGVVVHN

Data sets:
Data typeCount
13C chemical shifts288
15N chemical shifts137
1H chemical shifts904

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1RecA1

Entities:

Entity 1, RecA 139 residues - 15365.621 Da.

1   CYSLEUALAGLUGLYTHRARGILEPHEASP
2   PROVALTHRGLYTHRTHRHISARGILEGLU
3   ASPVALVALGLYGLYARGLYSPROILEHIS
4   VALVALALAALAALALYSASPGLYTHRLEU
5   HISALAARGPROVALVALSERTRPPHEASP
6   GLNGLYTHRARGASPVALILEGLYLEUARG
7   ILEALAGLYGLYALAILELEUTRPALATHR
8   PROASPHISLYSVALLEUTHRGLUTYRGLY
9   TRPARGALAALAGLYGLULEUARGLYSGLY
10   ASPARGVALALAVALARGASPVALGLUTHR
11   GLYGLULEUARGTYRSERVALILEARGGLU
12   VALLEUPROTHRARGARGALAARGTHRPHE
13   ASPLEUGLUVALGLUGLULEUHISTHRLEU
14   VALALAGLUGLYVALVALVALHISASN

Samples:

sample_1: sodium phosphate 50 mM; sodium chloride 100 mM; sodium azide 1 mM; entity, [U-98% 13C; U-98% 15N], 0.15 – 0.2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 150 mM; pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D HCCH-COSYsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment

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

NMR spectrometers:

  • Bruker ARX 800 MHz
  • Bruker ARX 600 MHz

Related Database Links:

BMRB 15560 16634
PDB
EMBL CFR77613 CMM98736
GB EPZ65824 KAM73204
REF WP_049963343

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