## 1 Introduction  
Liquid-state nuclear magnetic resonance (NMR) spectroscopy provides detailed information about the structure and dynamics of biomolecules in solution, such as proteins, nucleic acids, and carbohydrates. However, some biomolecules, such as membrane proteins, amyloid fibrils, and large macromolecular assemblies, are challenging to study using liquid-state NMR due to their low solubility and structural complexity. Therefore, magic angle spinning (MAS) solid-state NMR (ssNMR) spectroscopy has become a powerful alternative for studying such systems, as it enables the investigation of complex biomolecules [1, 2, 3, 4]. Recent advances in MAS ssNMR have improved the ability to study complex biomolecular systems at atomic resolution. For instance, techniques for solvent suppression, hydrogen/deuterium (H/D) exchange, and deuterium spectroscopy have been developed to improve spectral quality [5]. The use of perdeuterated and labeled proteins combined with ultrafast MAS has demonstrated remarkable improvements in spectral resolution [6]. Additionally, deuterium quadrupolar interactions have enabled site-specific characterization of molecular motions without the need for proton decoupling [7]. Furthermore, the emergence of proton-detected multidimensional experiments under ultrafast MAS conditions has opened new possibilities for studying protein structure and dynamics, even in the absence of complete deuteration [8, 9]. These methodological innovations, together with the application of hybrid structural approaches, have contributed to the high-resolution structure determination of different biomolecule complexes [10, 11, 12]. Often, this investigation involves multidimensional NMR techniques, and the pulse sequences have been actively developed to observe different aspects and responses of proteins. The number of pulse sequences is increasing rapidly [2; 13; 14; 15; 16]; however, the analysis of the resulting multidimensional NMR spectra remains a significant challenge. Once NMR spectra are acquired from a protein sample, most tasks are performed on computers. Therefore, lack of user-friendly software tools for automation would be a huge drawback, which is partly true with biomolecular ssNMR spectroscopy. Considering the potential of ssNMR on challenging and complex biomolecules described above, it is important to develop critical tools analogous to existing in solution NMR. Tasks in solution NMR are more streamlined than in ssNMR. For example, the POKY suite provides all-in-one features for routinely conducted analytical activities, which is a great advancement compared to its ancestor, NMRFAM-SPARKY [17; 18]. Initially, the APES plugin (two-letter-code _ae_) automates peak picking, cross-validates between them and filters out noise peaks [19]. Subsequently, the I-PINE webserver and the PINE-SPARKY.2 plugin (two-letter-code _ep_) provide automated chemical shift assignments for both backbone and sidechain atoms using the identified peaks as inputs. They support twenty-nine solution NMR experiments and versions, including the POKY capability of integrating artificial intelligence + three-dimensional structure (AI-based 3D-structure methods) and chemical prediction methods in the assignment. Additionally, the PONDEROSA plugin (two-letter-code _c3_) offers combined automated peak picking, assignment of NOESY spectra and calculation of 3D structure, requiring near-complete backbone and sidechain chemical shifts to run optimally. Moreover, the user can intervene in any of these steps to improve the quality of results, and the existence of these automation tools in the POKY suite provides seamless user experience of the Integrative NMR research platform unlike other automation programs. This kind of streamlined routine automation tool has focused more on data from solution NMR despite ssNMR's potential in challenging systems. The large number of peaks and complex coupling patterns in these spectra make it difficult to assign the signals to specific atomic sites and extract meaningful structural information.