Table 3 Side-chain 3JHαHβ-coupling values (58) in Hz derived and stereo-specifically assigned based on NMR measurements (set sc1) and from four unrestrained MD simulations starting from four X-ray crystal structures, and the mean of the latter four values and the root-mean-square deviation (RMSD) from it

From: On the use of 3J-coupling NMR data to derive structural information on proteins

Residue Expt value MD simulation (X-ray crystal)
2VB1 4LZT 1IEE 1AKI Mean RMSD
Val 2 10.8 9.3 (12.9) 10.0 (12.9) 9.8 (12.9) 9.3 (12.9) 9.6 (12.9) 0.3 (0.0)
Cys 6        
β2 11.5 12.6 (12.7) 12.6 (12.8) 8.9 (12.7) 12.3 (12.5) 11.6 (12.7) 1.6 (0.1)
β3 3.5 3.4 (2.5) 3.1 (2.7) 5.3 (2.5) 2.8 (2.3) 3.6 (2.5) 1.0 (0.1)
His 15        
β2 11.2 11.9 (12.9) 12.3 (12.5) 12.0 (12.6) 11.0 (11.4) 11.8 (12.4) 0.5 (0.6)
β3 2.6 2.4 (3.1) 2.6 (2.2) 2.5 (2.4) 3.1 (1.8) 2.6 (2.4) 0.3 (0.5)
Asp 18        
β2 4.2 5.1 (3.2) 2.9 (2.3) 3.2 (1.9) 3.4 (2.1) 3.7 (2.4) 0.9 (0.5)
β3 11.0 7.5 (12.9) 11.1 (12.5) 10.0 (12.0) 8.0 (12.3) 9.2 (12.4) 1.5 (0.3)
Tyr 20        
β2 2.3 7.2 (3.0) 5.7 (3.2) 9.9 (2.4) 8.7 (2.3) 7.9 (2.7) 1.6 (0.4)
β3 11.7 6.9 (12.9) 9.6 (12.9) 5.0 (12.6) 5.4 (12.5) 6.7 (12.7) 1.8 (0.2)
Tyr 23        
β2 10.9 12.6 (12.5) 7.1(12.7) 12.0 (12.5) 11.8(12.7) 10.9 (12.6) 2.2 (0.1)
β3 2.7 3.1 (2.2) 5.8 (2.5) 3.5 (2.3) 3.3 (2.5) 3.9 (2.4) 1.1 (0.1)
Asn 27        
β2 10.3 3.6 (11.6) 12.2 (12.2) 12.1 (11.6) 12.3 (12.2) 10.0 (11.9) 3.7 (0.3)
β3 2.4 4.3 (1.8) 3.3 (2.0) 3.4 (1.8) 4.3 (2.0) 3.8 (1.9) 0.5 (0.1)
Val 29 11.1 10.1 (12.8) 10.5 (12.9) 9.5 (12.8) 7.9 (12.9) 9.5 (12.8) 1.0 (0.0)
Cys 30        
β2 5.3 3.2 (3.0) 3.5 (2.9) 3.1 (2.7) 3.5 (2.4) 3.3 (2.7) 0.2 (0.2)
β3 10.8 12.6 (12.9) 12.6 (12.8) 12.6 (12.8) 12.7 (12.6) 12.6 (12.8) 0.0 (0.1)
Phe 34        
β2 10.7 10.7 (12.8) 11.3 (12.7) 11.8 (12.9) 4.2 (12.5) 9.5 (12.7) 3.1 (0.1)
β3 5.0 3.5 (2.6) 2.2 (2.6) 2.2 (2.9) 10.1 (2.3) 4.5 (2.6) 3.3 (0.2)
Asn 39        
β2 4.5 2.5 (2.6) 2.6 (2.8) 2.8 (2.6) 2.5 (2.1) 2.6 (2.5) 0.1 (0.3)
β3 10.8 12.0 (12.7) 12.1 (12.8) 11.9 (12.8) 11.9 (12.3) 12.0 (12.6) 0.1 (0.2)
Thr 40 4.5 2.7 (3.5) 2.9 (4.0) 2.9 (4.2) 2.8 (6.2) 2.8 (4.5) 0.1 (1.0)
Thr 43 3.7 3.4 (3.0) 3.0 (3.3) 2.9 (3.8) 3.9 (4.1) 3.3 (3.5) 0.4 (0.4)
Asn 46        
β2 11.2 2.6 (12.9) 8.4 (12.9) 11.8 (12.9) 4.6 (12.9) 6.8 (12.9) 3.5 (0.0)
β3 4.7 9.2 (3.4) 6.0 (3.7) 3.9 (3.4) 8.3 (3.6) 6.8 (3.5) 2.1 (0.1)
Thr 47 2.6 3.0 (3.6) 2.9 (4.2) 3.0 (3.9) 2.9 (5.1) 2.9 (4.2) 0.1 (0.5)
Asp 48        
β2 2.6 4.2 (5.3) 4.2 (4.7) 4.3 (4.3) 4.2 (5.5) 4.2 (4.9) 0.0 (0.5)
β3 3.7 2.9 (2.1) 2.9 (2.4) 2.9 (2.6) 3.5 (2.0) 3.1 (2.3) 0.3 (0.2)
Thr 51 9.3 5.6 (12.9) 9.6 (12.9) 10.7 (12.9) 8.7 (12.8) 8.7 (12.9) 1.9 (0.1)
Asp 52        
β2 11.6 12.6 (12.6) 12.5 (12.8) 12.4 (12.4) 12.5 (12.9) 12.5 (12.7) 0.1 (0.2)
β3 3.6 3.8 (4.7) 4.0 (4.0) 3.6 (2.2) 3.8 (3.9) 3.8 (3.7) 0.1 (0.9)
Tyr 53        
β2 10.4 12.1 (12.7) 12.2 (12.7) 12.0 (12.8) 12.2 (12.7) 12.1 (12.7) 0.1 (0.1)
β3 3.0 2.4 (2.5) 2.4 (2.6) 2.3 (2.9) 2.4 (2.5) 2.4 (2.6) 0.1 (0.2)
Asn 59        
β2 5.4 2.3 (2.8) 2.3 (2.9) 2.2 (1.9) 2.2 (2.6) 2.3 (2.5) 0.1 (0.4)
β3 11.3 12.3 (12.8) 12.2 (12.8) 12.2 (11.9) 12.2 (12.8) 12.2(12.6) 0.1 (0.4)
Arg 61        
β2 5.7 5.5 (2.6) 5.6 (2.4) 5.3 (2.9) 7.9 (1.8) 6.1 (2.4) 1.1 (0.4)
β3 10.8 8.4 (12.7) 7.7 (12.6) 7.9 (12.8) 5.6 (11.8) 7.4 (12.5) 1.1 (0.4)
Asp 66        
β2 5.1 3.2 (4.5) 3.2 (4.6) 3.0 (4.1) 3.0 (4.6) 3.1 (4.4) 0.1 (0.2)
β3 4.5 11.5 (2.5) 9.7 (2.4) 10.8 (2.7) 12.1 (2.4) 11.0 (2.5) 0.9 (0.1)
Thr 69 9.3 6.1 (12.9) 9.1 (12.9) 9.4 (12.7) 6.3 (12.8) 7.7 (12.8) 1.5 (0.1)
Leu 75        
β2 12.4 11.5 (12.9) 12.0 (12.9) 11.5 (12.9) 12.1 (12.5) 11.8 (12.8) 0.3 (0.2)
β3 2.1 3.0 (3.1) 2.8 (3.3) 2.9 (3.0) 4.8 (2.3) 3.4 (2.9) 0.8 (0.4)
Asp 87        
β2 5.1 3.3 (4.1) 2.7 (5.2) 3.3 (2.9) 3.2 (3.8) 3.1 (4.0) 0.3 (0.8)
β3 11.5 12.2 (12.8) 12.1 (12.4) 11.8 (12.9) 12.0 (12.9) 12.0(12.7) 0.1 (0.2)
Ile 88 4.5 4.3 (4.5) 2.8 (4.4) 4.8 (4.9) 2.8 (4.8) 3.7 (4.6) 0.9 (0.2)
Thr 89 9.5 4.8 (12.8) 4.2 (12.7) 5.2 (12.9) 4.9 (12.8) 4.8 (12.8) 0.4 (0.1)
Val 92 10.1 9.6 (12.5) 12.2 (12.4) 7.5 (12.7) 10.3 (12.3) 9.9 (12.5) 1.7 (0.1)
Cys 94        
β2 4.0 2.6 (2.9) 2.3 (2.9) 2.5 (2.7) 2.6 (2.7) 2.5 (2.8) 0.1 (0.1)
β3 12.2 12.4 (12.8) 12.0 (12.8) 12.3 (12.8) 12.4 (12.8) 12.3 (12.8) 0.2 (0.0)
Val 99 6.3 3.0 (12.8) 3.3 (12.8) 6.0 (2.2) 4.5 (2.4) 4.2 (7.6) 1.2 (5.3)
Val 109 8.0 9.0 (3.2) 6.8 (12.9) 5.8 (12.4) 8.2 (3.7) 7.4 (8.1) 1.2 (4.6)
Thr 118 4.2 2.9 (5.2) 3.1 (5.4) 3.0 (5.3) 3.1 (6.1) 3.0 (5.5) 0.1 (0.3)
Asp 119        
β2 4.9 4.5 (3.1) 2.8 (4.7) 2.9 (3.8) 3.0 (3.2) 3.3 (3.7) 0.7 (0.7)
β3 11.7 10.1(12.9) 12.3 (12.6) 12.1 (12.9) 12.2 (12.9) 11.7 (12.8) 0.9 (0.1)
Trp 123        
β2 10.6 12.2(11.9) 11.6 (12.5) 10.3 (12.6) 11.2 (12.8) 11.3 (12.4) 0.7 (0.3)
β3 2.9 3.7 (1.9) 2.9 (2.3) 5.8 (2.4) 4.4 (2.8) 4.2 (2.3) 1.1 (0.3)
Ile 124 4.6 4.1 (4.4) 5.7 (4.3) 4.2 (3.7) 3.6 (4.6) 4.4 (4.2) 0.8 (0.4)
Cys 127        
β2 11.6 12.6 (12.9) 11.6 (12.9) 4.4 (12.9) 12.4 (12.9) 10.3 (12.9) 3.4 (0.0)
β3 4.8 3.2 (3.3) 3.8 (3.4) 5.8 (3.8) 3.2 (3.7) 4.0 (3.5) 1.1 (0.2)
  1. Experimental values from Tables III and IV of Smith et al. (1991). The values within brackets in the six “MD simulation (X-ray crystal)” columns represent the 3JHαHβ-couplings calculated from the four X-ray crystal structures, their mean and RMSD from it. MD or X-ray values differing more than 2 Hz from the experimental value are denoted using italics