Score distillation sampling (SDS) demonstrates a powerful capability for text-conditioned 2D image and 3D object generation by distilling the knowledge from learned score functions. However, SDS often suffers from blurriness caused by noisy gradients. When SDS meets the image editing, such degradations can be reduced by adjusting bias shifts using reference pairs, but the de-biasing techniques are still corrupted by erroneous gradients. To this end, we introduce Identity-preserving Distillation Sampling (IDS), which compensates for the gradient leading to undesired changes in the results. Based on the analysis that these errors come from the text-conditioned scores, a new regularization technique, called fixed-point iterative regularization (FPR), is proposed to modify the score itself, driving the preservation of the identity even including poses and structures. Thanks to a self-correction by FPR, the proposed method provides clear and unambiguous representations corresponding to the given prompts in image-to-image editing and editable neural radiance field (NeRF). The structural consistency between the source and the edited data is obviously maintained compared to other state-of-the-art methods. Our code is https://github.com/shhh0620/IDS

MOTIVATION: Predicting protein structures with high accuracy is a critical challenge for the broad community of life sciences and industry. Despite progress made by deep neural networks like AlphaFold2, there is a need for further improvements in the quality of detailed structures, such as side-chains, along with protein backbone structures. RESULTS: Building upon the successes of AlphaFold2, the modifications we made include changing the losses of side-chain torsion angles and frame aligned point error, adding loss functions for side chain confidence and secondary structure prediction, and replacing template feature generation with a new alignment method based on conditional random fields. We also performed re-optimization by conformational space annealing using a molecular mechanics energy function which integrates the potential energies obtained from distogram and side-chain prediction. In the CASP15 blind test for single protein and domain modeling (109 domains), DeepFold ranked fourth among 132 groups with improvements in the details of the structure in terms of backbone, side-chain, and Molprobity. In terms of protein backbone accuracy, DeepFold achieved a median GDT-TS score of 88.64 compared with 85.88 of AlphaFold2. For TBM-easy/hard targets, DeepFold ranked at the top based on Z-scores for GDT-TS. This shows its practical value to the structural biology community, which demands highly accurate structures. In addition, a thorough analysis of 55 domains from 39 targets with publicly available structures indicates that DeepFold shows superior side-chain accuracy and Molprobity scores among the top-performing groups. AVAILABILITY AND IMPLEMENTATION: DeepFold tools are open-source software available at https://github.com/newtonjoo/deepfold.