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Two sets of files: 1) in text format (.csv), containing precipitation records from the AEMET, CHJ, AVAMET and SISRITEL networks and meteorological station of the Torrent city council; 2) in netCDF format (.nc), containing spatial interpolations of precipitation fields. Complete list of files: **valencia_daily.csv** (daily accumulated precipitation observations); **valencia_hourly.csv** (hourly accumulated precipitation observations); **valencia_daily.nc** (daily precipitation field); **valencia_hourly_acumulated.nc** (hourly accumulated precipitation fields); **valencia_hourly.nc** (hourly precipitation fields); **valencia_hourly_intensities.nc** (fields of maximum hourly precipitation intensity)., Dos conjuntos de archivos: 1) en formato de texto (.csv), conteniendo los registros de precipitación en las redes de AEMET, CHJ, AVAMET y SISRITEL y de la estación meteorológica del Ayuntamiento de Torrent; 2) en formato netCDF (.nc), conteniendo interpolaciones espaciales de los campos de precipitación. Listado complete de archivos: valencia_daily.csv (observaciones de precipitación acumulada diaria); valencia_hourly.csv (observaciones de precipitación acumulada horaria); valencia_daily.nc (campo de precipitación diaria); valencia_hourly_acumulated.nc (campos de precipitación horaria acumulada); valencia_hourly.nc (campos de precipitación horaria); valencia_hourly_intensities.nc (campos de máxima intensidad de precipitación horaria)., Spatio-temporal reconstruction of precipitation recorded during the event of October 29, 2024, in the province of Valencia. The reconstruction process consisted of two phases: 1) Collection and curation of precipitation records obtained from various climate monitoring networks. 2) Spatial interpolation of accumulated precipitation fields and maximum intensities at different temporal intervals. The dataset includes both the observations recorded by the monitoring networks and the interpolated spatial fields., Reconstrucción espacio-temporal de la precipitación registrada durante el evento del 29 de octubre de 2024 en la provincia de Valencia. El proceso de reconstrucción constó de dos fases: 1) Recopilación y curado de registros de precipitación obtenidos en distintas redes de monitorización climática. 2) Interpolación espacial de campos de precipitación acumulada e intensidades máximas con distintos intervalos temporales. El conjunto de datos incluye tanto las observaciones registradas en las redes de monitorización como los campos espaciales interpolados., No sponsors., .csv and .nc archives, No

Supplementary Information S1: representative videos showing S. ratti L3 with indicated motility Scores, Peer reviewed

Crystal structures of Oligopeptide-Binding Proteins (OBP) of the Ami system., Peer reviewed

(A) Left panel, surface representation of the AliD:permease complex predicted by AF. Each protein is color-coded and labeled accordingly. CH: coupling helix. (B) Different configurations of the NBDs in the inward (closed, upper panel) and outward (open, lower panel) conformations. AmiF and AmiD are represented in cartoon form, and the ATP molecules are shown as spheres. (C) View corresponding to a slice located at the blue plane depicted in A, right panel. The upper panel highlights the identified hydrophobic residues that obstruct the channel in the inward, closed conformation. In contrast, the lower panel shows the location of the same residues in the outward, open conformation. The generated cavity, presumably allowing oligopeptide transport, is marked in blue and outlined with a dashed black line. Relevant residues are labeled and represented as spheres. (D) Different proteins of the Ami system and conceptual schematic model for the mechanism of oligopeptide transport., Peer reviewed

(A) Right panel, molecular electrostatic potential surface (MEPS) of AliB’s lobe 2 is shown. The three peptides complexed with AliB are depicted as capped sticks with colors orange (peptide 2), green (peptide 3) and cyan (peptide 4). The oligopeptide positions 1 to 4 and the pockets P1 to P4 are labeled. Left panel, cartoon representation corresponding to the boxed area displayed in the right panel. Conserved Aspartate (D) and Tryptophan (W) residues are depicted in capped gray sticks. The residue F521, crucial for stabilizing the lateral chain in oligopeptide position 2, is also shown as capped gray sticks. (B) Right panel, MEPS of AmiA’s lobe 2 is shown. The peptide corresponding to the AmiA:peptide 5 complex is depicted in capped sticks (colored green). The oligopeptide positions 1 to 4 and the pockets P1 to P4 are labeled. Left panel, cartoon representation corresponding to the boxed area is in the right panel is displayed. Conserved Asp (D) and Trp (W) residues are depicted as capped deep olive sticks. The residue E524, critical for stabilizing the lateral chain in oligopeptide position 2, is also shown as capped gray sticks. Polar interactions are represented with dashed black lines. R1 and R2 represent variable regions 1 and 2, respectively. The small panel between panels A and B provides a view of a typical Ami OBP with both lobes indicated. The black dashed line between the two lobes indicates the position of the slice required to obtain the view of the MEPS of lobe 2 for both panels A and B. (C) Structural superposition of lobe 2 for the five Ami OBPs is presented, with a focus on strand β20. Regions R1 and R2 are indicated. (D) Schematic cartoon representing the relevant OBP structural features involved in oligopeptide recognition (colored in pink)., Peer reviewed

(A) Crystal structure of the AliD:peptide 1 complex. Left, ribbon representation of the AliD:peptide 1 complex (ligand shown in yellow caped sticks). Domains I, II, and III are labeled and colored green, light orange and blue; respectively. Right, a magnified view (corresponding to the boxed area shown in the left panel) highlighting amino acid residues engaged in the recognition of peptide 1 by AliD. Polar interactions are indicated by dotted black lines. The sequence of peptide 1 (FPPQNV) is illustrated in yellow capital letters. (B) The crystal structure of AliB in complex with peptides 2, 3 and 4. AliB, as observed in the AliB:peptide 2 complex, is depicted as a white cartoon. The substrates are represented with their secondary structure elements and are color-coded as yellow (peptide 2), green (peptide 3) and blue (peptide 4). (C) Stereo view illustrating polar interactions between AliB (white sticks) and peptide 2 (yellow sticks). (D) Stereo view showcasing polar interactions between AliB (white sticks) and peptide 3 (green sticks). (E) Stereo view illustrating polar interactions between AliB (white sticks) and peptide 4 (blue sticks). (F) Ribbon representation of AmiA in complex with peptide 4 (depicted as yellow capped sticks). (G) Stereo view providing specific details of peptide 4 recognition by AmiA. The relevant residues and crystallographic water molecules are depicted as gray-capped sticks and red spheres, respectively. Residues participating in hydrophobic interactions have been omitted for clarity. P1 to P6, pocket 1 to pocket 6. Pockets beyond substrate position 6 have been omitted for clarity., Peer reviewed

(A) Molecular surface and topology of AliD. The upper panel illustrates the molecular surface representation of AliD, with each domain color-coded. In the lower panel, a topological diagram depicts the secondary structure elements of AliD, labeled and numbered. The color code spans from blue (N-terminus) to red (C-terminus), portraying α-helices as cylinders and β-strands as arrows. (B) Overall cartoon representation of AliD monomer structure. The structure is presented in two orientations spaced 180° apart. Domains I, II, and III are labeled and colored green, light orange, and blue, respectively. The dimensions of the peptide-binding cavity (~16 Å in width and ~45 Å in height) are specified. The C-terminal α-helix (α19) is highlighted in red and labeled. N, amino-terminus; C, Carboxy-terminus., Peer reviewed

(A) Schematic representation illustrating the different elements composing the lipoproteins of the Ami system. Distinctive coloring is applied to each domain. (B) Alignment of sequences encompassing the signal peptide (in yellow), the lipobox (in red) and the linker region (in gray) in the five lipoproteins of the Ami system. The cysteine residue designated for lipidation is denoted by a black arrow., Peer reviewed

5 files, This dataset contains the OVIDE 2018 qualified measurements of the hydrographic CTD-02 (genuine netCDF and zipped text files in WHP format), bottle data (WHP format with traditionnal headers), Ship Acoustic Doppler Current Profilers (OS 38kHz and 150 kHz, CASCADE netCDF format), and Lowered Acoustic Doppler Current Profilers (WH150 downlooking and WH300 uplooking, zipped ascii format from LDEO software), We acknowledge the LEFE program funded by CNRS, the European project AtlantOS, the Spanish Ministry of Economy and Competitiveness. This work was also supported by the ISblue project, Interdisciplinary graduate school for the blue plante (ANR-17-EURE-0015) and "Laboratoire d'Excellence" LabexMER (ANR-10-LABX-19) and co-funded by a grant from the French government under the program "Investissements d'Avenir", Peer reviewed

The structure of AliD is presented in a cartoon oval representation. Domain I, II and III are color-coded as green, pale brown and blue, respectively. Peptide 1 is represented as yellow capped sticks. Hydrophobic residues, forming a hydrophobic patch that encloses the ligand when the protein adopts a closed conformation, are also visualized in capped sticks. (MPG), Peer reviewed