1WJE

SOLUTION STRUCTURE OF H12C MUTANT OF THE N-TERMINAL ZN BINDING DOMAIN OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM, NMR, MINIMIZED AVERAGE STRUCTURE

SOLUTION NMR

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DMX600	500
2	Bruker	DMX500	600

NMR Refinement
Method	Details	Software
simulated annealing	THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136, USING THE PROGRAM XPLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J. MAGN RESON. SERIES B 104, 99-103), 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 AND (1997) J. MAGN. RESON. 125, 171-177). THE 3D STRUCTURE OF THE N-TERMINAL DOMAIN OF THE H12C MUTANT OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR IS BASED ON 757 EXPERIMENTAL RESTRAINTS (PER MONOMER): (A) INTRASUBUNIT: 203 SEQUENTIAL (\|I-J\|=1), 161 MEDIUM RANGE (1 < \|I-J\| >=5) AND 82 LONG RANGE (\|I-J\| >5) INTERRESIDUE, AND 5 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 16 DISTANCE RESTRAINTS FOR 8 HYDROGEN BONDS; 117 TORSION ANGLE (45 PHI, 35 PSI, 26 CHI1, 10 CHI2 AND 1 CHI3) RESTRAINTS; 47 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; 99 (50 CALPHA AND 49 CBETA) 13C SHIFT RESTRAINTS. (B) 20 INTERSUBUNIT INTERPROTON DISTANCE RESTRAINTS. (C) 7 AMBIGUOUS INTERPROTON DISTANCE RESTRAINTS THAT CAN ARISE FROM INTRA AND/OR INTERSUBUNIT INTERACTIONS. THE STRUCTURES WERE CALCULATED USING THE SIMULATED ANNEALING PROTOCOL OF NILGES ET AL. (1988) FEBS LETT. 229, 129-136, USING THE PROGRAM XPLOR 3.1 (BRUNGER) MODIFIED TO INCORPORATE COUPLING CONSTANT (GARRETT ET AL. (1984) J. MAGN RESON. SERIES B 104, 99-103), 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 AND (1997) J. MAGN. RESON. 125, 171-177). THE 3D STRUCTURE OF THE N-TERMINAL DOMAIN OF THE H12C MUTANT OF HIV-1 INTEGRASE COMPLEXED TO CADMIUM WAS SOLVED BY MULTI-DIMENSIONAL HETERONUCLEAR-EDITED AND -FILTERED NMR IS BASED ON 757 EXPERIMENTAL RESTRAINTS (PER MONOMER): (A) INTRASUBUNIT: 203 SEQUENTIAL (\|I-J\|=1), 161 MEDIUM RANGE (1 < \|I-J\| >=5) AND 82 LONG RANGE (\|I-J\| >5) INTERRESIDUE, AND 5 INTRARESIDUE APPROXIMATE INTERPROTON DISTANCE RESTRAINTS; 16 DISTANCE RESTRAINTS FOR 8 HYDROGEN BONDS; 117 TORSION ANGLE (45 PHI, 35 PSI, 26 CHI1, 10 CHI2 AND 1 CHI3) RESTRAINTS; 47 THREE-BOND HN-HA COUPLING CONSTANT RESTRAINTS; 99 (50 CALPHA AND 49 CBETA) 13C SHIFT RESTRAINTS. (B) 20 INTERSUBUNIT INTERPROTON DISTANCE RESTRAINTS. (C) 7 AMBIGUOUS INTERPROTON DISTANCE RESTRAINTS THAT CAN ARISE FROM INTRA AND/OR INTERSUBUNIT INTERACTIONS.	CNS

NMR Ensemble Information
Conformer Selection Criteria	REGULARIZED MEAN STRUCTURE
Conformers Calculated Total Number	40
Conformers Submitted Total Number	1

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	CNS		BRUNGER,ADAMS,CLORE,DELANO,GROS, GROSSE-KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,READ,RICE,SIMONSON,WARREN
2	structure solution	CNS MODIFIED	MODIFIED

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.