PMID- 19436955
OWN - NLM
STAT- MEDLINE
DCOM- 20090831
LR  - 20211020
IS  - 1573-5001 (Electronic)
IS  - 0925-2738 (Print)
IS  - 0925-2738 (Linking)
VI  - 44
IP  - 2
DP  - 2009 Jun
TI  - Empirical correlation between protein backbone 15N and 13C secondary chemical 
      shifts and its application to nitrogen chemical shift re-referencing.
PG  - 95-9
LID - 10.1007/s10858-009-9324-0 [doi]
AB  - The linear analysis of chemical shifts (LACS) has provided a robust method for 
      identifying and correcting 13C chemical shift referencing problems in data from 
      protein NMR spectroscopy. Unlike other approaches, LACS does not require prior 
      knowledge of the three-dimensional structure or inference of the secondary 
      structure of the protein. It also does not require extensive assignment of the 
      NMR data. We report here a way of extending the LACS approach to 15N NMR data 
      from proteins, so as to enable the detection and correction of inconsistencies in 
      chemical shift referencing for this nucleus. The approach is based on our finding 
      that the secondary 15N chemical shift of the backbone nitrogen atom of residue i 
      is strongly correlated with the secondary chemical shift difference (experimental 
      minus random coil) between the alpha and beta carbons of residue i-1. Thus once 
      alpha and beta 13C chemical shifts are available (their difference is referencing 
      error-free), the 15N referencing can be validated, and an appropriate offset 
      correction can be derived. This approach can be implemented prior to a structure 
      determination and can be used to analyze potential referencing problems in 
      database data not associated with three-dimensional structure. Application of the 
      LACS algorithm to the current BMRB protein chemical shift database, revealed that 
      nearly 35% of the BMRB entries have delta 15N values mis-referenced by over 0.7 
      ppm and over 25% of them have delta 1HN values mis-referenced by over 0.12 ppm. 
      One implication of the findings reported here is that a backbone 15N chemical 
      shift provides a better indicator of the conformation of the preceding residue 
      than of the residue itself.
FAU - Wang, Liya
AU  - Wang L
AD  - Cold Spring Harbor Laboratory, Williams 5, 1 Bungtown Rd, Cold Spring Harbor, NY 
      11724, USA.
FAU - Markley, John L
AU  - Markley JL
LA  - eng
GR  - P41 RR002301/RR/NCRR NIH HHS/United States
GR  - U54 GM074901-03/GM/NIGMS NIH HHS/United States
GR  - P41RR02301/RR/NCRR NIH HHS/United States
GR  - U54 GM074901/GM/NIGMS NIH HHS/United States
GR  - 1U54 GM074901/GM/NIGMS NIH HHS/United States
GR  - P41 RR002301-22/RR/NCRR NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
DEP - 20090513
PL  - Netherlands
TA  - J Biomol NMR
JT  - Journal of biomolecular NMR
JID - 9110829
RN  - 0 (Amino Acids)
RN  - 0 (Carbon Isotopes)
RN  - 0 (Nitrogen Isotopes)
RN  - 0 (Proteins)
SB  - IM
MH  - Algorithms
MH  - Amino Acids/chemistry
MH  - Carbon Isotopes/*chemistry
MH  - *Models, Chemical
MH  - Nitrogen Isotopes/*chemistry
MH  - *Nuclear Magnetic Resonance, Biomolecular
MH  - Proteins/*chemistry
PMC - PMC2782637
MID - NIHMS151250
EDAT- 2009/05/14 09:00
MHDA- 2009/09/01 06:00
PMCR- 2010/06/01
CRDT- 2009/05/14 09:00
PHST- 2009/04/13 00:00 [received]
PHST- 2009/04/22 00:00 [accepted]
PHST- 2009/05/14 09:00 [entrez]
PHST- 2009/05/14 09:00 [pubmed]
PHST- 2009/09/01 06:00 [medline]
PHST- 2010/06/01 00:00 [pmc-release]
AID - 10.1007/s10858-009-9324-0 [doi]
PST - ppublish
SO  - J Biomol NMR. 2009 Jun;44(2):95-9. doi: 10.1007/s10858-009-9324-0. Epub 2009 May 
      13.