Table 1
Solution structure and basis for functional activity of stromal cell-derived factor-1; dissociation of CXCR4 activation from binding and inhibition of HIV-1
Matthew P. Crump, Jiang-Hong Gong, Pius Loetscher, Krishna Rajarathnam, Ali Amara, Fernando Arenzana-Seisdedos, Jean-Louis Virelizier, Marco Baggiolini, Brian D. Sykes and Ian Clark-Lewis
- The EMBO Journal (1997) 16, 6996 - 7007
- doi:10.1093/emboj/16.23.6996
| All (796)a | 0.027  0.001 |
| Inter-residue (centre averaged)a | |
Short (1 < |i-j|  5) | 0.039 0.015 |
| Sequential (|i-j| = 1) | 0.024 0.003 |
| Long (|i-j| > 5) | 0.029 0.015 |
| Inter-residue (R-6 averaged)a | |
| Long | 0.025 0.008 |
| Intra-residue (centre averaged)a | 0.020 0.002 |
| i = j | 0.020 0.008 |
| ENOE (kcal/mol)b | 29.0 1.9 |
| EDIHE (kcal/mol)b | 1.49 0.3 |
| EREPEL (kcal/mol)b | 0.06 0.05 |
| Deviations from idealized geometryc | |
| Bonds (Å) | 0.0031 0.0001 |
| Angles (°) | 0.530 0.008 |
| Improper (°) | 0.368 0.007 |
| Atomic r.m.s. differences (Å)d | |
| Backbone atoms (9–65) | 0.35 0.1 |
| Heavy atoms (9–65) | 0.96 0.09 |
| aThe r.m.s. deviation of the experimental restraints (Å) is calculated with respect to the upper and lower limits of the input restraints. | |
| bThe values for ENOE and EDIHE are calculated from a square well potential with a force constant of 50 kcal mol-1 Å2 and 200 kcal mol-1 rad-2. EREPEL is calculated with a force constant of 4 kcal mol-1 Å-4 and the final van der Waal's radii were set to 0.75 times the value used in the CHARMM force field. | |
| cThe values for bonds, angles and impropers show the deviation from ideal values based on perfect stereochemistry. | |
| dR.m.s. differences of the 30 final simulated annealing structures superimposed on the average structure. | |
