BIOMOLECULAR NMR ASSIGNMENTS 提供了一个论坛，用于发布蛋白质和核酸的序列特异性共振分配作为分配说明。大分子中 NMR 活性核的化学位移包含有关分子构象和性质的详细信息。在 BIOMOLECULAR NMR ASSIGNMENTS 中发布共振分配可确保将这些数据存入 BIOMAGRESBANK (BMRB; HTTP://WWW.BMRB.WISC 的公共数据库中.EDU/)，可供其他研究人员使用。覆盖范围包括蛋白质和核酸；作业笔记被处理为快速在线发布，并在六月和十二月以半年一次的在线版本发布。

Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments of proteins and nucleic acids. The chemical shifts of NMR-active nuclei in macromolecules contain detailed information about molecular conformation and properties. Resonance assignments published in Biomolecular NMR Assignments will be deposited in the public database BIOMAGRESBANK (BMRB; http://www.bmrb.wisc.edu/) for use by other researchers. The scope includes proteins and nucleic acids; assignment notes are processed for rapid online publication and released biannually in June and December.

《Biomolecular NMR Assignments》是一个专门发布蛋白质和核酸序列特异性共振分配的论坛。大分子中 NMR 活性核的化学位移提供了关于分子构象和性质的详细信息。在《Biomolecular NMR Assignments》上发布的共振分配数据将被存入公共数据库 BIOMAGRESBANK (BMRB; http://www.bmrb.wisc.edu/)，供其他研究人员使用。期刊涵盖蛋白质和核酸领域，作业笔记会被快速在线发布，并在每年的六月和十二月以半年一次的在线版本发布。

Biomolecular NMR Assignments

The backbone and side chain resonance assignments of human ACS (approximately 22 KD), apoptosis-associated speck-like protein containing a caspase recruitment domain and a pyrin domain, have been determined by triple-resonance NMR techniques.

Eva de Alba

1H, 15N and 13C backbone and side chain chemical shifts of human ASC (apoptosis-associated speck-like protein containing a CARD domain)

人ASC（含CARD域的凋亡相关斑点样蛋白）的1H、15N和13C主链及侧链化学位移

Porcine reproductive and respiratory syndrome virus (PRRSV) is the causative agent of porcine reproductive and respiratory syndrome, a destructive disease of swine. PRRSV has a single strand positive-sense RNA genome which contains at least ten open reading frames, of these, ORF1a and ORF1b encode polyproteins pp1a and pp1ab. Subsequently, pp1a is cleaved into ten nonstructural proteins, including nonstructural protein 7α and 7β (nsp7α and 7β), the internal cleavage products of a conserved nonstructural protein nsp7. Nsp7 plays a role in provoking the humoral immune system into producing anti-nsp7 antibodies which can be highly and persistently expressed in PRRSV-infected swine. However, the functions of nsp7α and 7β remain unknown. Western blot and radioimmunoprecipitation analysis of the two proteins showed that only cleaved nsp7α was detectable and cleaved nsp7β was not detected in the infected cells. Here, we reported the (1)H, (13)C and (15)N resonance assignment of nsp7α from PRRSV as a basis for further structural and functional studies.

Jiaping Chen

Xiaodong Xu

Hu Tao

Yuanyuan Wang

Hongying Chen

Biomolecular NMR assignments

Biomol NMR Assign

Chemical shift assignments of nsp7α from porcine reproductive and respiratory syndrome virus.

猪繁殖与呼吸综合征病毒nsp7α的化学位移归属。

Natural macrocyclic peptides produced by microorganisms serve as valuable resources for therapeutic compounds, including antibiotics, anticancer agents, and immune suppressive agents. Nonribosomal peptide synthetases (NRPSs) are responsible for the biosynthesis of macrocyclic peptides. NRPSs are large multimodular enzymes, and each module recognizes and incorporates one specific amino acid into the polypeptide product. In the final biosynthetic step, the mature linear peptide precursor is subject to head-to-tail cyclization by the thioesterase (TE) domain in the C-terminal module. Since the TE domains can autonomously catalyze the cyclization of diverse linear peptide substrates, isolated TE domains can be used to produce natural product derivatives. To understand the mechanism of TE domains in NRPSs as a base for therapeutic applications, we investigated the TE domain (residues 6236-6486) of tyrocidine synthetase TycC by NMR. Tyrocidine is a cyclic decapeptide with antibiotic activity, and TycC-TE catalyzes the cyclization of the linear decapeptide precursor. Here, we report the backbone resonance assignments of TycC-TE. The assignments of TycC-TE provide the basis for NMR investigations of the structure and substrate-recognition mode of the TE domain in NRPS.

Mitsuhiro Takeda

Rino Saito

Sho Konno

Takayuki Nagae

Hiroshi Aoyama

Sosuke Yoshinaga

Hiroaki Terasawa

Akihiro Taguchi

Atsuhiko Taniguchi

Yoshio Hayashi

Masaki Mishima

Backbone resonance assignments of the C-terminal thioesterase domain of tyrocidine synthetase C

环孢菌素合成酶C的C端硫酯酶结构域的主链共振归属

It has been shown that human seminal fluid is a major factor in enhancing HIV activity. The SEM2(49-107) peptide is a product of cleavage after ejaculation by internal prostheses of the semenogelin 2 protein, expressed in seminal vesicles. It is established that the peptide SEM2(49-107) forms amyloid fibrils, which increase probability of contracting HIV infection. In this nuclear magnetic resonance (NMR) study, we present almost complete (86%) resonance assignments for the 1H 15N and 13C atoms of the backbone and side-chain of the SEM2(49-107) peptide (BioMagResBank accession number 52356). The secondary structure of SEM2(49-107) peptide was estimated by using two approaches, secondary chemical shifts analysis (CSI) and TALOS-N prediction. Analysis of the secondary structure of the SEM2(49-107) peptide using both methods revealed that the peptide contains helical segments at the C-terminus. Also in this work, we used phase-sensitive 2D HSQC 1H- 15N experiments measuring longitudinal T1 and transverse T2 NMR relaxation times to report predicted secondary structure and backbone dynamics of the SEM2(49-107) peptide. This resonance assignment will form the basis of future NMR research, contributing to a better understanding of the peptide structure and internal dynamics of the molecule.

Anastasia A Troshkina

Vladimir V Klochkov

Aydar G Bikmullin

Evelina A Klochkova

Dmitriy S Blokhin

1H, 13C, and 15N resonance assignments of the amyloidogenic peptide SEM2(49–107) by NMR spectroscopy

通过核磁共振波谱法测定的淀粉样蛋白原性肽SEM2(49–107)的1H、13C和15N共振归属

Zika virus has raised global concerns due to its link to microcephaly and Guillain-Barré syndrome in adults. One of viral nonstructural proteins-NS4B, an integral membrane protein, plays crucial roles in viral replication by interacting with both viral and host proteins, rendering it an attractive drug target for antiviral development. We purified the N-terminal region of ZIKV NS4B (NS4B NTD) and reconstituted it into detergent micelles. Here, we report the assignments of the backbone resonances of NS4B NTD in detergent micelles. The available assignment is useful for understanding its structure and ligand binding to provide useful information for developing NS4B inhibitors.

Yan Li

Ying Ru Loh

Qingxin Li

Dahai Luo

CongBao Kang

1H, 15N and 13C backbone resonance assignment of the N-terminal region of Zika virus NS4B protein in detergent micelles

Zika病毒NS4B蛋白N端区域在去污剂微粒中的1H、15N和13C骨架共振归属

The Rho GTPase (Ras homolog GTPases) system is a crucial signal transducer that regulates various cellular processes, including cell cycle and migration, genetic transcription, and apoptosis. In this study, we investigated the unfolded state of the first FF domain (FF1) of P190A RhoGAP, which features four tandem FF domains. For signal transduction, FF1 is phosphorylated at tyrosine 308 (Y308), which is buried in the hydrophobic core and is inaccessible to kinases in the folded domain. It was proposed, therefore, that the phosphorylation occurs in a transiently populated unfolded state of FF1. To probe the folding pathway of the RhoGAP FF1 domain, here we have performed a nearly complete backbone resonance assignments of a putative partially unfolded state of FF1 in 5 M urea and its fully unfolded state in 8 M urea.

Aarão Camilo-Ramos

Dmitry M. Korzhnev

Ramon Pinheiro-Aguiar

Fabio C. L. Almeida

Backbone 1H, 15N, and 13C resonance assignments of the FF1 domain from P190A RhoGAP in 5 and 8 M urea

P190A RhoGAP中FF1域在5和8 M尿素中的骨架1H、15N和13C共振分配

Abstract Transfer RNAs (tRNAs) are an essential component of the protein synthesis machinery. In order to accomplish their cellular functions, tRNAs go through a highly controlled biogenesis process leading to the production of correctly folded tRNAs. tRNAs in solution adopt the characteristic L-shape form, a stable tertiary conformation imperative for the cellular stability of tRNAs, their thermotolerance, their interaction with protein and RNA complexes and their activity in the translation process. The introduction of post-transcriptional modifications by modification enzymes, the global conformation of tRNAs, and their cellular stability are highly interconnected. We aim to further investigate this existing link by monitoring the maturation of bacterial tRNAs in E. coli extracts using NMR. Here, we report on the 1 H, 15 N chemical shift assignment of the imino groups and some amino groups of unmodified and modified E. coli tRNA Asp , tRNA Val and tRNA Phe , which are essential for characterizing their maturation process using NMR spectroscopy.

Marcel-Joseph Yared

Carine Chagneau

Pierre Barraud

Imino chemical shift assignments of tRNAAsp, tRNAVal and tRNAPhe from Escherichia coli

大肠杆菌tRNAAsp、tRNAVal和tRNAPhe的亚胺化学位移指派

Abbreviation	Biomol. NMR Assign.
Journal Impact	0.84
Quartiles(Global)	SPECTROSCOPY(Q4)

ISSN	1874-270X, 1874-2718
h-index	19

Publication Information	Publisher: Springer Netherlands，Publishing cycle: Semiannual，Journal Type: journal，Open Access Journals: No
Basic data	Year of publication: 2007，Proportion of original research papers: 100.00%，Self Citation Rate:12.50%， Gold OA Rate: 35.33%
Average review cycle	网友分享经验：较慢,6-12周
Average recruitment ratio	网友分享经验：容易

Biomolecular NMR Assignments

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1H, 15N and 13C backbone and side chain chemical shifts of human ASC (apoptosis-associated speck-like protein containing a CARD domain)

Chemical shift assignments of nsp7α from porcine reproductive and respiratory syndrome virus.

Backbone resonance assignments of the C-terminal thioesterase domain of tyrocidine synthetase C

1H, 13C, and 15N resonance assignments of the amyloidogenic peptide SEM2(49–107) by NMR spectroscopy

1H, 15N and 13C backbone resonance assignment of the N-terminal region of Zika virus NS4B protein in detergent micelles

Backbone resonance assignments of the C-terminal thioesterase domain of tyrocidine synthetase C

1H, 13C, and 15N resonance assignments of the amyloidogenic peptide SEM2(49–107) by NMR spectroscopy

1H, 15N and 13C backbone resonance assignment of the N-terminal region of Zika virus NS4B protein in detergent micelles

Backbone 1H, 15N, and 13C resonance assignments of the FF1 domain from P190A RhoGAP in 5 and 8 M urea

Imino chemical shift assignments of tRNAAsp, tRNAVal and tRNAPhe from Escherichia coli