Rinaldelli Mauro, Carlon Azzurra, Ravera Enrico, Parigi Giacomo, Luchinat Claudio
CERM and Department of Chemistry "Ugo Schiff", University of Florence, via Sacconi 6, Sesto Fiorentino, Florence, Italy.
J Biomol NMR. 2015 Jan;61(1):21-34. doi: 10.1007/s10858-014-9877-4. Epub 2014 Nov 22.
Pseudocontact shifts (PCSs) and residual dipolar couplings (RDCs) arising from the presence of paramagnetic metal ions in proteins as well as RDCs due to partial orientation induced by external orienting media are nowadays routinely measured as a part of the NMR characterization of biologically relevant systems. PCSs and RDCs are becoming more and more popular as restraints (1) to determine and/or refine protein structures in solution, (2) to monitor the extent of conformational heterogeneity in systems composed of rigid domains which can reorient with respect to one another, and (3) to obtain structural information in protein-protein complexes. The use of both PCSs and RDCs proceeds through the determination of the anisotropy tensors which are at the origin of these NMR observables. A new user-friendly web tool, called FANTEN (Finding ANisotropy TENsors), has been developed for the determination of the anisotropy tensors related to PCSs and RDCs and has been made freely available through the WeNMR ( http://fanten-enmr.cerm.unifi.it:8080 ) gateway. The program has many new features not available in other existing programs, among which the possibility of a joint analysis of several sets of PCS and RDC data and the possibility to perform rigid body minimizations.
由于蛋白质中存在顺磁性金属离子而产生的伪接触位移（PCSs）和残余偶极耦合（RDCs），以及由于外部定向介质诱导的部分取向而产生的RDCs，如今已作为生物相关系统核磁共振表征的一部分进行常规测量。PCSs和RDCs作为约束条件正变得越来越受欢迎，用于（1）确定和/或优化溶液中的蛋白质结构，（2）监测由可相互重新取向的刚性结构域组成的系统中构象异质性的程度，以及（3）获取蛋白质-蛋白质复合物中的结构信息。PCSs和RDCs的使用都需要通过确定作为这些核磁共振可观测量起源的各向异性张量来进行。一个名为FANTEN（查找各向异性张量）的新的用户友好型网络工具已被开发出来，用于确定与PCSs和RDCs相关的各向异性张量，并已通过WeNMR（http://fanten-enmr.cerm.unifi.it:8080）网关免费提供。该程序具有许多其他现有程序所没有的新功能，其中包括对多组PCS和RDC数据进行联合分析的可能性以及进行刚体最小化的可能性。
