SOLUTION NMR STRUCTURE OF THE IBETA SUBDOMAIN OF THE MU END DNA BINDING DOMAIN OF PHAGE MU TRANSPOSASE, REGULARIZED MEAN STRUCTURE
Solution structure of the Mu end DNA-binding ibeta subdomain of phage Mu transposase: modular DNA recognition by two tethered domains.
MIARPTLEAHDYDREALWSKWDNASDSQRRLAEKWLPAVQAADEMLNQGISTKTAFATVAGHYQVSASTLRDKYYQVQKF AKPDWAAALVDGRGASRRN
TRIPLE RESONANCE FOR ASSIGNMENT OF PROTEIN: CBCA(CO)NH
15N-SEPARATED HOHAHA; QUANTITATIVE J CORRELATION FOR COUPLING CONSTANTS; 3D 15N-SEPARATED NOE
THE 3D STRUCTURE OF THE IBETA SUBDOMAIN OF MU A TRANSPOSASE WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR NMR AND IS BASED ON 1446 EXPERIMENTAL NMR RESTRAINTS: 255 SEQUENTIAL (|I- J|=1), 220 MEDIUM RANGE (1 < |I-J| <=5) AND 252 LONG RANGE (|I-J| >5) INTERRESIDUES AND 234 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 52 DISTANCE RESTRAINTS FOR 26 BACKBONE H-BONDS;. 153 TORSION ANGLE RESTRAINTS (94 PHI, 8 PSI, 36 CHI1 AND 15 CHI2); 58 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; AND 180 (92 CALPHA AND 88 CBETA) 13C SHIFT RESTRAINTS. THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136 USING THE PROGRAM X-PLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J. MAGN. RESON. SERIES B 104, 99-103) AND CARBON CHEMICAL SHIFT (KUSZEWSKI ET AL. (1995) J. MAGN. RESON. SERIES B 106, 92-96) RESTRAINTS, AND A CONFORMATIONAL DATABASE POTENTIAL (KUSZEWSKI ET AL.(1996) PROTEIN SCI. 5, 1067-1080; KUSZEWSKI ET AL. (1997) J. MAGN. RESON 125, 171-177). THE RESTRAINED REGULARIZED MEAN STRUCTURE IS PRESENTED IN ENTRY 2EZK AND 29 STRUCTURES ARE PRESENTED IN ENTRY 2EZL, AND THE EXPERIMENTAL RESTRAINTS IN R2EZKMR. IN THE RESTRAINED REGULARIZED MEAN COORDINATES (2EZK) THE LAST COLUMN REPRESENTS THE AVERAGE RMS DIFFERENCE BETWEEN THE INDIVIDUAL SIMULATED ANNEALING STRUCTURES AND THE MEAN COORDINATE POSITIONS. THE LAST COLUMN IN THE INDIVIDUAL SA THE STRUCTURES (2EZI) HAS NO MEANING. BEST FITTING TO GENERATE AVERAGE STRUCTURE IS WITH RESPECT TO RESIDUES 89 - 166. RESIDUES 76 - 88 AND 167 - 174 AT THE N- AND C-TERMINI ARE POORLY DEFINED BY THE EXPERIMENTAL DATA. NOTE THE OCCUPANCY FIELD HAS NO MEANING. RMSD IN BONDS,ANGLES,IMPROPERS,CDIH,NOE,COUP: 2808E-03,0.871524,1.02906,0.295155,2.337017E-02,0.902726 SHIFTS RMS A, B: 1.04343, 1.11143
DNA-BINDING PROTEIN, TRANSPOSITION, TRANSPOSABLE ELEMENT, DNA BINDING PROTEIN
MELWVSPKECANLPGLPKTSAGVIYVAKKQGWQNRTRAGVKGGKAIEYNANSLPVEAKAALLLRQGEIETSLGYFEIARP TLEAHDYDREALWSKWDNASDSQRRLAEKWLPAVQAADEMLNQGISTKTAFATVAGHYQVSASTLRDKYYQVQKFAKPDW AAALVDGRGASRRNVHKSEFDEDAWQFLIADYLRPEKPAFRKCYERLELAAREHGWSIPSRATAFRRIQQLDEAMVVACR EGEHALMHLIPAQQRTVEHLDAMQWINGDGYLHNVFVRWFNGDVIRPKTWFWQDVKTRKILGWRCDVSENIDSIRLSFMD VVTRYGIPEDFHITIDNTRGAANKWLTGGAPNRYRFKVKEDDPKGLFLLMGAKMHWTSVVAGKGWGQAKPVERAFGVGGL EEYVDKHPALAGAYTGPNPQAKPDNYGDRAVDAELFLKTLAEGVAMFNARTGRETEMCGGKLSFDDVFEREYARTIVRKP TEEQKRMLLLPAEAVNVSRKGEFTLKVGGSLKGAKNVYYNMALMNAGVKKVVVRFDPQQLHSTVYCYTLDGRFICEAECL APVAFNDAAAGREYRRRQKQLKSATKAAIKAQKQMDALEVAELLPQIAEPAAPESRIVGIFRPSGNTERVKNQERDDEYE TERDEYLNHSLDILEQNRRKKAI