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					[Authors: There are FOUR table templates in this document.

The first table template is a shortform version for presenting NMR structure statistics in your main
paper. Please cut and paste the table from this document into your paper.

The other three table templates are for presentation of more detailed NMR structure statistics in the
Supplementary Information that will be published online alongside the main paper. Please choose the
ONE that is most appropriate for your data.]



Table 1 NMR structure statistics

Violations (mean and s.d.)


    Distance constraints (Å)


    Dihedral angle constraints (º)


    Max. dihedral angle violation (º)


    Max. distance constraint violation (Å)


Deviations from idealized geometry


    Bond lengths (Å)


    Bond angles (º)


    Impropers (º)


Average pairwise r.m.s.d. (Å)


    Heavy


    Backbone
Table 1 NMR and refinement statistics for protein structures
                                                               Protein
NMR distance and dihedral constraints
Distance constraints
  Total NOE
  Intra-residue
  Inter-residue
   Sequential (|i-j| = 1)
   Medium-range (|i-j| < 4)
   Long-range (|i-j > 5)
   Intermolecular
  Hydrogen bonds
Total dihedral angle restraints
  phi
  psi

Structure statistics
Violations (mean and s.d.)
   Distance constraints (Å)
   Dihedral angle constraints ()
   Max. dihedral angle violation ()
   Max. distance constraint violation (Å)
Deviations from idealized geometry
   Bond lengths (Å)
   Bond angles ()
   Impropers ()
Average pairwise r.m.s.d.** (Å)
   Heavy
   Backbone
**[AUTHOR: Please indicate number of structures used in r.m.s.d. calculations.] Pairwise r.m.s.d.
was calculated among ## refined structures.
[AUTHOR: Ramachandran statistics should be in Methods section at the end of the refinement sub-
section.]
[AUTHOR: If RDC is used, please include]
Total RDCs
Qfree (%) Q and Qfree is
[Recommended in the case where there are many RDCs, often though there are not enough to make this
statistically meaningful]
Table 2 NMR and refinement statistics for nucleic acids
                                                          Structure name
NMR distance and dihedral constraints
Distance restraints
 Total NOE
 Intra-residue
 Inter-residue
   Sequential (|i-j| = 1)
   Non-sequential (|i-j| > 1 )
 Hydrogen bonds
Total dihedral angle restraints
   Base pair
   Sugar pucker
   Backbone
 Based on A-form geometry

Structure statistics
Violations (mean and s.d.)
  Distance constraints (Å)
  Dihedral angle constraints ()
  Max. dihedral angle violation ()
  Max. distance constraint violation (Å)
Deviations from idealized geometry
  Bond lengths (Å)
  Bond angles ()
  Impropers ()
Average pairwise r.m.s.d.** (Å)
  All RNA heavy
  RNA binding site
  All nucleotides
     (Special parts??) apical, tetraloop, symmetric
bulge
**[AUTHOR: Please indicate number of structures used in r.m.s.d. calculations] Pairwise r.m.s.d. was
calculated among ## refined structures.
[AUTHOR: Ramachandran statistics should be in Methods section at the end of the refinement sub-
section.]
[AUTHOR: If RDC is used, please include]
Total RDCs
Qfree (%) Q and Qfree is
[Recommended in the case where there are many RDCs, often though there are not enough to make this
statistically meaningful]
Table 3 NMR and refinement statistics for complexes
                                                             Protein             Nucleic
                                                                               acid/ligand
NMR distance and dihedral constraints
Distance restraints
  Total NOE
  Intra-residue
  Inter-residue
    Sequential (|i-j| = 1)
    Non-sequential (|i-j| > 1 )
   Hydrogen bonds
Protein–nucleic acid intermolecular
Total dihedral angle restraints
   Protein
     phi
     psi
   Nucleic acid
     Base pair
     Sugar pucker
     Backbone
   Based on A-form geometry

Structure statistics
Violations (mean and s.d.)
  Distance constraints (Å)
  Dihedral angle constraints ()
  Max. dihedral angle violation ()
  Max. distance constraint violation (Å)
Deviations from idealized geometry
  Bond lengths (Å)
  Bond angles ()
  Impropers ()
Average pairwise r.m.s.d.** (Å)
  Protein
   Heavy
   Backbone
 RNA
   All RNA heavy
   RNA binding site
   All nucleotides
      (special parts??) apical, tetraloop, symmetric
bulge
 Complex
   All complex heavy (C, N, O, P)
   Protein and nucleic acid heavy
**[AUTHOR: Please indicate number of structures used in r.m.s.d. calculations] Pairwise r.m.s.d. was
calculated among ## refined structures.
[AUTHOR: Ramachandran statistics should be in Methods section at the end of the refinement sub-
section.]
[AUTHOR: If RDC is used, please include]
 Total RDCs
Qfree (%) Q and Qfree is
[Recommended in the case where there are many RDCs, often though there are not enough to make this
statistically meaningful]