1PMX

INSULIN-LIKE GROWTH FACTOR-I BOUND TO A PHAGE-DERIVED PEPTIDE

SOLUTION NMR

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	3D_15N-SEPARATED_NOESY	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313
2	HNHA	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313
3	D-HNHB	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313
4	3D 15N-SEPARATED LOW MIXING TIME TOCSY	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313
5	2D-15N-FILTERED NOESY	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313
6	3D_13C-SEPARATED_NOESY	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313
7	3D-13_FILTERED	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313
8	13C-EDITED NOESY	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313
9	2D-13C-FILTERED NOESY	1.4 MM IGF-I (15N), 2.0 MM PEPTIDE, 25 MM SODIUM ACETATE		25 mM	5.1	1 atm	313

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Bruker	DRX	600
2	Bruker	DRX	800

NMR Refinement
Method	Details	Software
TORSION ANGLE DYNAMICS, SIMULATED ANNEALING	THE COMPLEX WAS DETERMINED USING A TOTAL OF 905 NOE DISTANCE RESTRAINTS (146 INTRA RESIDUE, 203 SEQUENTIAL, 232 MEDIUM RANGE, 237 LONG-RANGE AND 87 INTERMOLECULAR), 24 HYDROGEN BOND RESTRAINTS, 139 DIHEDRAL ANGLE RESTRAINTS (72 PHI, 44 PSI AND 23 CHI-1). THE BEST 20 CONFORMERS (OF 100) HAD NO DISTANCE VIOLATIONS GREATER THAN 0.11A AND NO DIHEDRAL ANGLE VIOLATIONS GREATER THAN 1.5 DEGREES. RMSD FROM EXPERIMENTAL DISTANCE RESTRAINTS WAS 0.0049+/-0.0008. THE MEAN BACKBONE RMSD FROM THE MEAN STRUCTURE WAS 0.35 +/- 0.06 A FOR N, CA AND C ATOMS OF RESIDUES 3-26, 42-63 of IGF-I AND RESIDUES 3-15 OF THE PEPTIDE. 82% (17%) OF RESIDUES WERE IN THE MOST FAVOURED (ALLOWED) REGION OF PHI/PSI SPACE; NO RESIDUES WERE CONSISTENTLY IN THE DISALLOWED REGION.	CNS

NMR Ensemble Information
Conformer Selection Criteria	LEAST VIOLATION OF EXPERIMENTAL RESTRAINTS
Conformers Calculated Total Number	100
Conformers Submitted Total Number	20
Representative Model	1 (closest to the average, fewest violations)

Additional NMR Experimental Information
Details	THE RESONANCE ASSIGNMENTS WERE DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	refinement	CNS	2000.1	ACCELRYS
2	structure solution	XwinNMR	3.1	ACCELRYS
3	structure solution	Felix	98	ACCELRYS

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.