The combinatorial distance geometry method for the calculation of molecular conformation. I. A new approach to an old problem.

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Protein 3D Structure Computed from Evolutionary Sequence Variation (2011, neutral): “magnetic resonance (NMR) spectroscopy [52] (Text S1).”
Protein structure prediction from sequence variation (2012, methodology): “P E R S P E C T I V E n p g riance scores using a standard distance geometry algorithm, first pio-neered and then ubiquitously used to solve three-dimensional structures with experimental constraints deduced from NMR spectroscopy data 41 .”
3D Protein Structure Predicted from Sequence (2011, unknown): “the family (Table S1) we used well-‐established distance geometry algorithms, as used for structure determination by NMR spectroscopy [50] (Box 1, Text S1).”
GeoMol: Torsional Geometric Generation of Molecular 3D Conformer Ensembles (2021, background): “Subsequently, the corresponding 3D atom coordinates are learned to approximately match these predicted distances [Havel et al., 1983b,a, Crippen et al., 1988, Havel, 1998, Lagorce et al., 2009, Riniker and Landrum, 2015].”
A topology‐constrained distance network algorithm for protein structure determination from NOESY data (2005, unknown): “30–32 The process of determining sequence-speciﬁc resonance assignments provide a set R of protein nuclei resonance frequencies assigned to speciﬁc atoms of the protein structure [ R (cid”