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YOLOv7 surpasses all known object detectors in both speed and accuracy in the range from 5 FPS to 160 FPS and has the highest accuracy 56.8% AP among all known real-time object detectors with 30 FPS or higher on GPU V100. YOLOv7-E6 object detector (56 FPS V100, 55.9% AP) outperforms both transformer-based detector SWIN-L Cascade-Mask R-CNN (9.2 FPS A100, 53.9% AP) by 509% in speed and 2% in accuracy, and convolutionalbased detector ConvNeXt-XL Cascade-Mask R-CNN (8.6 FPS A100, 55.2% AP) by 551% in speed and 0.7% AP in accuracy, as well as YOLOv7 outperforms: YOLOR, YOLOX, Scaled-YOLOv4, YOLOv5, DETR, Deformable DETR, DINO-5scale-R50, ViT-Adapter-B and many other object detectors in speed and accuracy. Moreover, we train YOLOv7 only on MS COCO dataset from scratch without using any other datasets or pre-trained weights. Source code is released in https:// github.com/ WongKinYiu/ yolov7.

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We investigated the correlation between the Shannon information entropy, 'sequence entropy', with respect to the local flexibility of native globular proteins as described by inverse packing density. These are determined at each residue position for a total set of 130 query proteins, where sequence entropies are calculated from each set of aligned residues. For the accompanying aggregate set of 130 alignments, a strong linear correlation is observed between the calculated sequence entropy and the corresponding inverse packing density determined at an associated residue position. This region of linearity spans the range of C(alpha) packing densities from 12 to 25 amino acids within a sphere of 9 angstrom radius. Three different hydrophobicity scales all mimic the behavior of the sequence entropies. This confirms the idea that the ability to accommodate mutations is strongly dependent on the available space and on the propensity for each amino acid type to be buried. Future applications of these types of methods may prove useful in identifying both core and flexible residues within a protein.