1ERF

CONFORMATIONAL MAPPING OF THE N-TERMINAL FUSION PEPTIDE OF HIV-1 GP41 USING 13C-ENHANCED FOURIER TRANSFORM INFRARED SPECTROSCOPY (FTIR)

INFRARED SPECTROSCOPY

NMR Experiment
Experiment	Type	Sample Contents	Solvent	Ionic Strength	pH	Pressure	Temperature (K)	Spectrometer
1	13-C isotope enhanced FTIR	THIS STRUCTURE WAS DETERMINED USING 13-C ISOTOPE ENHANCED FTIR SPECTROSCOPY ON A FAMILY OF SELECTIVELY LABELED CHEMICALLY SYNTHESIZED PEPTIDES. 13-C CARBONYL LABELS INCLUDED RESIDUES 519,521,523,524,525,526,527,528,529,530,531,532,533,534,538,539.	70% hexafluoroisopropanol (HFIP), 29.9% water, 0.1% formic acid (v/v)	0	7.0	1 atm	298

NMR Spectrometer Information
Spectrometer	Manufacturer	Model	Field Strength
1	Mattson FTIR	Research Series

NMR Refinement
Method	Details	Software
molecular dynamics, simulated annealing	Molecular dynamics (simulated annealing) was used to generate an ensemble of conformers consistent with the FTIR data.	Winfirst

NMR Ensemble Information
Conformer Selection Criteria	structures with acceptable covalent geometry
Conformers Calculated Total Number	31
Conformers Submitted Total Number	17
Representative Model	9 (closest to the average)

Additional NMR Experimental Information
Details	The coordinates in this entry were generated from 13-C induced spectral shifts which give residue-specific secondary structure information.

Computation: NMR Software
#	Classification	Version	Software Name	Author
1	data analysis	Winfirst	FTIR curve fitting software	Kauppine et al.
2	refinement	DISCOVER	2.9.7	Molecular Simulations, Inc. (San Diego, CA)

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.