The Protein database is a collection of sequences from several sources, including translations from annotated coding regions in GenBank, RefSeq and TPA, as well as records from SwissProt, PIR, PRF, and PDB. Protein sequences are the fundamental determinants of biological structure and function.

A computer algorithm that identifies similar protein 3-dimensional structures. Structure neighbors for every structure in MMDB are pre-computed and accessible via links on the MMDB Structure Summary pages.

Gene integrates information from a wide range of species. A record may include nomenclature, Reference Sequences (RefSeqs), maps, pathways, variations, phenotypes, and links to genome-, phenotype-, and locus-specific resources worldwide.

● 데이터 키워드 - 유전체, 유전자, NGS, DNA ● 데이터 상품 정보 - 본 상품은 자생종 유전체 분석을 통해 얻어진 유전자의 유전자군 발현확률 정보를 제공합니다. - 기능 도메인에 대해 기능별 유용성, 효소, 단백질, 병 저항성 유전자군 분류 가공 - 데이터 comparative analysis를 통해 유전자군별 발현 확률 및 계통 확률 계산 ● 컬럼 정보 - fasta format ● 활용 예제 - 본 데이터 상품을 활용하여 사용자는 다음과 같은 정보를 확인할 수 있습니다. 1) 신약 및 기능성 식품, 화장품 개발 관련 분야 기초자료 ● 기간 및 범위 - 2019년 7월 ~ 2019년 12월 [원본 데이터](https://www.bigdata-forest.kr/product/GNM201201)는 로그인 후 구매하여 다운로드 하십시오.

CDTree is a stand-alone application for classifying protein sequences and investigating their evolutionary relationships. CDTree can import, analyze and update existing Conserved Domain (CDD) records and hierarchies, and also allows users to create their own.

Three dimensional structures provide a wealth of information on the biological function and the evolutionary history of macromolecules. They can be used to examine sequence-structure-function relationships, interactions, active sites, and more.

NIST peptide libraries are comprehensive, annotated mass spectral reference collections from various organisms and proteins useful for the rapid matching and identification of acquired MS/MS spectra. Spectra were produced by tandem mass spectrometers using liquid chromatographic separations followed by electrospray ionization. Unlike the NIST small molecule electron ionization library which contains one spectrum per molecular structure, there are several different modes of fragmentation (ion trap and ?beam-type? collision cells are currently the most commonly used fragmentation devices) that result in spectra with different, energy dependent, patterns. These result in multiple spectral libraries, distinguished by ionization mode, each of which may contain several spectra per peptide. Different libraries have also been assembled for iTRAQ-4 derivatized peptides and for phosphorylated peptides. Separating libraries by animal species reduces search time, although investigators may elect to include several species in their searches.

A comprehensive, integrated, non-redundant, well-annotated set of reference sequences including genomic, transcript, and protein.

Data file for "Vliet SMF, Hazemi M, Blatz D, Jensen M, Mayasich S, Transue TR, Simmons C, Wilkinson A, LaLone CA. Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation. J Vis Exp. 2023 Feb 10;(192). doi: 10.3791/63970. PMID: 36847398.". This dataset is associated with the following publication: Vliet, S., M. Hazemi, D. Blatz, M. Jensen, S. Mayasich, T. Transue, C. Simmons, A. Wilkinson, and C. Lalone. Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation. Journal of Visualized Experiments. JoVE, Somerville, MA, USA, 192, (2023).

Data file for "Vliet SMF, Hazemi M, Blatz D, Jensen M, Mayasich S, Transue TR, Simmons C, Wilkinson A, LaLone CA. Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation. J Vis Exp. 2023 Feb 10;(192). doi: 10.3791/63970. PMID: 36847398.". This dataset is associated with the following publication: Vliet, S., M. Hazemi, D. Blatz, M. Jensen, S. Mayasich, T. Transue, C. Simmons, A. Wilkinson, and C. Lalone. Demonstration of the Sequence Alignment to Predict Across Species Susceptibility Tool for Rapid Assessment of Protein Conservation. Journal of Visualized Experiments. JoVE, Somerville, MA, USA, 192, (2023).