ISDA: 1CFF

SOLUTION NMR

NMR Experiment

Experiment	Type	Sample Contents	Ionic Strength	Solvent	pH	Pressure	Temprature (K)
1	HNCO	90% H2O/10% D2O, 100% D2O	0.115	?	6.5	1	303
2	HNCA	90% H2O/10% D2O, 100% D2O	0.115	?	6.5	1	303
3	CBCACONH	90% H2O/10% D2O, 100% D2O	0.115	?	6.5	1	303
4	CBCANH	90% H2O/10% D2O, 100% D2O	0.115	?	6.5	1	303
5	HCCCONH	90% H2O/10% D2O, 100% D2O	0.115	?	6.5	1	303
6	HCCH-TOCSY	90% H2O/10% D2O, 100% D2O	0.115	?	6.5	1	303
7	NOESY-HSQC	90% H2O/10% D2O, 100% D2O	0.115	?	6.5	1	303

NMR Spectrometer Information

Spectrometer	Manufacturer	Model	Field Strength

NMR Refinement

Method	Details	Software
simulated annealing	REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. IT IS IMPOSSIBLE TO SUPERIMPOSE THE N- AND C-TERMINAL DOMAIN OF CAM SIMULTANEOUSLY DUE TO THE LACK OF NOES BETWEEN BOTH DOMAINS. THEREFOR THE 26 STRUCTURES ARE SUPERIMPOSED ONLY OVER THE BACKBONE ATOMS OF THE C-TERMINAL DOMAIN OF CAM AND THE PEPTIDE C20W. RMSD VALUES OF THE N-TERMINAL DOMAIN OF CAM (LEU A 4 - ALA A 73) ARE 0.85 (BACKBONE) AND 1.27 (HEAVY ATOMS) ANGSTROMS. RMSD VALUE FOR THE C- TERMINAL DOMAIN OF CAM AND THE PEPTIDE C20W (ILE A 85 - MET A 145, GLY B 4 - GLN B 16) ARE 0.57 (BACKBONE) AND 1.08 (HEAVY ATOMS) ANGSTROMS. RESIDUES ALA A 1 - GLN A 3, ARG A 74 - GLU A 84, THR A 146 - LYS A 148 OF CAM AND RESIDUES LEU B 1 - ARG B 3, THR B 17 - LYS B 20 OF THE PEPTIDE C20W ARE DISORDERED.	1

NMR Ensemble Information

Conformer Selection Criteria	LOWEST ENERGY
Conformers Calculated Total Number	200
Conformers Submitted Total Number	26
Representative Model	()

Computation: NMR Software

#	Classification	Version	Software Name	Author
1	refinement	3.851	X-PLOR	BRUNGER
2	structure solution	?	XPLOR	?