Solution NMR Structure of Kazal-1 Domain of Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.
Northeast Structural Genomics Consortium (NESG)
Follistatin-like 3, Follistatin-related gene protein
Northeast Structural Genomics Consortium
MONOMER BY GEL FILTRATION CHROMATOGRAPHY/LIGHT SCATTERING AND BY NMR. T1/T2(CPMG) (MS) = 516.1/136.2, TAUC = 3.94(NS). CONSISTENT WITH MOLECULAR WEIGHT. STRUCTURE DETERMINED BY TRIPLE RESONANCE NMR SPECTROSCOPY. NOESY ASSIGNMENTS BY CYANA2.1. 20 OF 100 STRUCTURES LOWEST TARGET FUNCTION SELECTED WITH CYANA-2.1. SELECTED MODELS ARE FURTHER REFINED USING CNS IN EXPLICIT WATER SHELL (NILGES PROTOCOL WITH PARAM19). ASSIGNMENT STATS (EXCLUDING C-TERM TAG): BACKBONE 98.10%, SIDECHAIN 88.50%, AROMATIC (SC) 75.00%. STRUCTURE BASED ON 912 NOE, 65 DIHE. MAX NOE VIOLATION: 0.19 A (1MODEL); MAX DIHE VIOLATION: 5.4 DEG. 6 TOTAL CLOSE CONTACTS PER 20 MODELS. STRUCTURE QUALITY FACTOR (PSVS 1.3): ORDERED RESIDUES RANGES: 4-9, 13-27, 33-34, 37-58, 61-69, 72-73 FOR [S(PHI)+S(PSI)] > 1.8. SECONDARY STRUCTURE - ALPHA HELICES: 50-60, BETA STRANDS: 13-18, 21-26, 46-47, 39-41, 66-69. RMSD 1.3 BACKBONE, 1.8 ALL HEAVY ATOMS. RAMA. DISTRIBUTION: 92.1/7.8/0.1/0.0. PROCHECK (PSI-PHI): -0.34/-1.02 (RAW/Z), PROCHECK (ALL): -0.33/-1.95 (RAW/Z), MOLPROBITY CLASH: 19.69/-1.85 (RAW/Z). RPF SCORES ALL ASSIGNED RESIDUES (FIT OF NOESY PEAKLISTS TO STRUCTURE): RECALL: 0.99, PRECISION: 0.85, F-MEASURE: 0.91, DP-SCORE: 0.82.
Brunger, Adams, Clore, Gros, Nilges and Read
Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax
Laskowski, MacArthur, Smith, Jones, Hutchinson, Morris, Moss and Tho
Kazal-1, Follistatin, Chromosomal rearrangement, Glycoprotein, Nucleus, Proto-oncogene, Secreted, Structural Genomics, PSI-2, Protein Structure Initiative, Northeast Structural Genomics Consortium, NESG, unknown function, NUCLEOTIDE-BINDING PROTEIN