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NMR processing:
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Structure from NMR restraints:
Ab initio:
GeNMR
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Fragment-based:
BMRB CS-Rosetta
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Template-based:
GeNMR
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Refinement:
Amber
Structure from chemical shifts:
Fragment-based:
WeNMR CS-Rosetta
BMRB CS-Rosetta
Homology-based:
CS23D
Simshift
Torsion angles from chemical shifts:
Preditor
TALOS
Promega- Proline
Secondary structure from chemical shifts:
CSI (via RCI server)
TALOS
MICS caps, β-turns
d2D
PECAN
Flexibility from chemical shifts:
RCI
Interactions from chemical shifts:
HADDOCK
Chemical shifts re-referencing:
Shiftcor
UNIO Shiftinspector
LACS
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RefDB
NMR model quality:
NOEs, other restraints:
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RPF scores
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Chemical shifts:
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Vasco
iCing
RDCs:
DC
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Pseudocontact shifts:
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Protein geomtery:
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What-If
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SAVES2 or SAVES4
Vadar
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MetaMQAPII
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NMR spectrum prediction:
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V-NMR
Flexibility from structure:
Backbone S2
Methyl S2
B-factor
Molecular dynamics:
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Amber
Antechamber
Chemical shifts prediction:
From structure:
Shiftx2
Sparta+
Camshift
CH3shift- Methyl
ArShift- Aromatic
ShiftS
Proshift
PPM
CheShift-2- Cα
From sequence:
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Camcoil
Poulsen_rc_CS
Disordered proteins:
MAXOCC
Format conversion & validation:
CCPN
From NMR-STAR 3.1
Validate NMR-STAR 3.1
NMR sample preparation:
Protein disorder:
DisMeta
Protein solubility:
camLILA
ccSOL
Camfold
camGroEL
Zyggregator
Isotope labeling:
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Solid-state NMR:
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Unread 08-16-2005, 06:32 AM
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There are several reasons mentioned on the SEASCAPE website why there is no much of a SEASCAPE web site (see below).
  • I've got the site. I just forgot it at home.
  • The dog ate my homework.
  • The phase of the moon isn't just right.
  • Aliens have been experimenting on me.
  • It's here. You just can't see it.
  • My computer is solar powered and it's been cloudy.
  • I didn't know anyone would *actually* look at this page.
  • I'll have it tomorrow.
  • I can't release it until it's checked by the National Security Agency.
  • What site?
But the most important thing, a link to SEASCAPE program, is there on the web site.

Reference

Assignment of protein backbone resonances using connectivity, torsion angles and 13Calpha chemical shifts.

Morris LC, Valafar H, Prestegard JH.
Complex Carbohydrate Research Center, University of Georgia, 220 Riverbend Road, Athens, GA 30602-4712, U.S.A.
J Biomol NMR. 2004 May;29(1):1-9.

Abstract:

A program is presented which will return the most probable sequence location for a short connected set of residues in a protein given just (13)C(alpha) chemical shifts (delta((13)C(alpha))) and data restricting the phi and psi backbone angles. Data taken from both the BioMagResBank and the Protein Data Bank were used to create a probability density function (PDF) using a multivariate normal distribution in delta((13)C(alpha)), phi, and psi space for each amino acid residue. Extracting and combining probabilities for particular amino acid residues in a short proposed sequence yields a score indicative of the correctness of the proposed assignment. The program is illustrated using several proteins for which structure and (13)C(alpha) chemical shift data are available
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