Full Chemical Shift Statistics Statistics Calculated for All Chemical Shifts from Atoms in the 20 Common Amino Acids The statistics presented in this table were calculated from the full BMRB database. This includes paramagnetic proteins, proteins with aromatic prosthetic groups, and entries where chemical shifts are reported relative to uncommon chemical shift references. The calculated statistics are drived from a total of 6832934 chemical shifts. Last updated: 6/4/2015 Res Name Atom Count Min. Max. Avg. Std Dev ALA H H 61351 0.00 69.23 8.19 0.66 ALA HA H 46318 -2.52 17.87 4.25 0.45 ALA HB H 43933 -14.04 5.48 1.35 0.29 ALA C C 39029 0.04 187.20 177.74 3.61 ALA CA C 53540 17.01 123.90 53.17 2.08 ALA CB C 50629 -40.99 99.00 19.05 2.40 ALA N N 57495 0.05 766.00 123.29 6.51 ARG H H 40744 0.01 12.73 8.24 0.63 ARG HA H 31529 1.21 12.57 4.29 0.48 ARG HB2 H 28727 -4.78 27.53 1.79 0.32 ARG HB3 H 27130 -1.13 27.53 1.76 0.33 ARG HG2 H 25837 -1.45 4.20 1.56 0.29 ARG HG3 H 23836 -1.30 5.47 1.54 0.30 ARG HD2 H 25407 -6.44 4.69 3.11 0.27 ARG HD3 H 23037 -0.69 4.79 3.09 0.30 ARG HE H 8781 2.20 116.66 7.47 3.15 ARG HH11 H 821 4.41 10.68 6.91 0.56 ARG HH12 H 628 4.41 10.73 6.85 0.50 ARG HH21 H 707 1.23 11.35 6.80 0.67 ARG HH22 H 583 1.23 60.14 6.88 2.30 ARG C C 24723 0.17 184.96 176.39 3.38 ARG CA C 34819 8.37 103.60 56.77 2.44 ARG CB C 32543 17.74 123.50 30.72 2.16 ARG CG C 21145 12.17 119.40 27.23 1.67 ARG CD C 21426 18.94 135.80 43.17 1.54 ARG CZ C 571 43.20 181.47 160.14 6.51 ARG N N 37151 0.13 177.67 120.74 4.32 ARG NE N 5580 7.22 149.11 90.58 13.48 ARG NH1 N 213 67.60 124.79 79.75 13.75 ARG NH2 N 189 66.20 128.47 79.52 15.23 ASP H H 48693 -0.35 17.50 8.30 0.60 ASP HA H 36799 -3.75 8.66 4.59 0.33 ASP HB2 H 34441 -5.20 37.40 2.72 0.56 ASP HB3 H 33056 -1.46 37.20 2.67 0.57 ASP HD2 H 9 1.16 12.30 5.31 3.63 ASP C C 30820 0.11 219.00 176.36 3.82 ASP CA C 42585 5.63 118.90 54.68 2.15 ASP CB C 40406 9.70 180.89 40.89 2.03 ASP CG C 753 2.64 186.50 177.65 16.29 ASP N N 45995 0.06 223.70 120.64 4.55 ASN H H 33906 0.01 448.00 8.35 2.55 ASN HA H 26360 1.75 7.11 4.66 0.37 ASN HB2 H 24799 -0.77 8.88 2.80 0.34 ASN HB3 H 23919 -0.95 5.14 2.74 0.37 ASN HD21 H 19003 1.09 111.32 7.34 0.91 ASN HD22 H 18786 1.47 111.32 7.15 0.93 ASN C C 20978 0.11 185.30 175.23 3.24 ASN CA C 29442 2.20 99.00 53.53 1.99 ASN CB C 27966 1.96 99.00 38.70 2.02 ASN CG C 2170 0.00 183.80 176.41 7.10 ASN N N 31208 0.04 208.90 118.89 4.48 ASN ND2 N 16282 21.04 1114.29 112.88 11.44 CYS H H 17440 3.72 12.40 8.38 0.70 CYS HA H 15122 -9.86 43.50 4.68 1.06 CYS HB2 H 14633 -39.82 363.58 3.19 7.18 CYS HB3 H 14261 -44.20 363.58 3.10 6.51 CYS HG H 172 0.10 10.70 2.08 1.45 CYS C C 8229 1.00 187.59 174.85 3.53 CYS CA C 12047 30.67 82.30 58.13 3.40 CYS CB C 11449 17.99 73.92 33.07 6.33 CYS N N 13260 -147.00 628.00 120.56 21.59 GLU H H 63083 0.01 64.68 8.33 0.69 GLU HA H 48018 0.43 31.32 4.25 0.44 GLU HB2 H 43682 -1.47 4.82 2.02 0.22 GLU HB3 H 40994 -1.63 4.08 1.99 0.23 GLU HG2 H 40692 -0.67 4.69 2.26 0.22 GLU HG3 H 37747 -0.10 4.69 2.24 0.23 GLU HE2 H 7 2.73 11.96 5.94 3.42 GLU C C 40942 0.07 190.58 176.82 3.97 GLU CA C 55766 3.77 87.15 57.32 2.17 GLU CB C 52176 9.08 181.95 30.02 2.13 GLU CG C 35589 6.16 181.20 36.11 1.78 GLU CD C 769 27.25 198.61 181.60 9.60 GLU N N 59943 0.04 429.00 120.65 4.55 GLN H H 33810 0.01 66.54 8.22 0.68 GLN HA H 26014 1.57 7.43 4.27 0.44 GLN HB2 H 23722 -1.34 5.18 2.04 0.27 GLN HB3 H 22512 -1.42 20.90 2.01 0.32 GLN HG2 H 22332 -1.76 33.60 2.31 0.35 GLN HG3 H 20623 -1.40 34.95 2.29 0.38 GLN HE21 H 17102 -3.41 23.89 7.21 0.51 GLN HE22 H 17004 2.10 113.70 7.04 0.96 GLN C C 21620 0.07 1756.00 176.38 11.21 GLN CA C 30008 4.10 69.63 56.59 2.18 GLN CB C 28167 17.41 79.68 29.20 2.09 GLN CG C 19355 2.29 178.32 33.78 1.82 GLN CD C 2066 6.79 183.54 179.26 7.86 GLN N N 31879 0.08 216.50 119.86 3.98 GLN NE2 N 15279 33.90 155.00 111.86 2.14 GLY H H 60849 -15.30 112.83 8.33 0.93 GLY HA2 H 45996 -3.40 8.64 3.96 0.40 GLY HA3 H 43867 -3.40 7.69 3.89 0.41 GLY C C 38244 1.00 189.53 173.83 3.94 GLY CA C 53317 2.20 108.30 45.38 1.62 GLY N N 56204 0.20 791.00 109.74 7.94 HIS H H 17778 -0.30 13.34 8.26 0.75 HIS HA H 14082 0.68 30.68 4.62 0.62 HIS HB2 H 13153 -0.05 45.90 3.17 1.19 HIS HB3 H 12789 -6.20 38.50 3.11 1.14 HIS HD1 H 848 -15.00 86.50 10.36 9.32 HIS HD2 H 9496 -25.85 67.80 7.21 3.61 HIS HE1 H 7544 -26.60 134.81 7.82 2.79 HIS HE2 H 334 -15.00 76.40 11.37 8.43 HIS C C 10983 1.00 184.20 175.12 4.85 HIS CA C 15789 11.40 176.90 56.53 2.83 HIS CB C 14894 17.80 80.78 30.29 2.43 HIS CG C 169 60.97 139.83 131.21 8.02 HIS CD2 C 5963 7.19 159.95 119.91 5.91 HIS CE1 C 4694 8.20 166.28 137.25 5.74 HIS N N 16306 0.20 159.14 119.62 4.89 HIS ND1 N 650 64.90 261.01 193.25 33.58 HIS NE2 N 609 17.00 257.57 180.74 21.27 ILE H H 42547 0.01 174.75 8.27 1.07 ILE HA H 32471 -9.00 173.54 4.18 1.10 ILE HB H 30643 -2.44 38.70 1.78 0.42 ILE HG12 H 27925 -10.10 5.56 1.26 0.47 ILE HG13 H 26866 -10.10 9.71 1.19 0.50 ILE HG2 H 29317 -3.62 6.23 0.77 0.31 ILE HD1 H 29835 -4.15 13.89 0.67 0.35 ILE C C 27277 0.09 187.55 175.79 4.56 ILE CA C 37667 30.90 77.93 61.61 2.75 ILE CB C 35365 18.10 87.68 38.60 2.21 ILE CG1 C 24094 8.00 225.84 27.71 2.40 ILE CG2 C 25625 0.79 114.15 17.56 1.99 ILE CD1 C 26078 2.70 79.34 13.47 2.48 ILE N N 40134 0.00 531.00 121.42 6.25 LEU H H 70225 -0.30 125.18 8.22 0.79 LEU HA H 53383 0.51 119.41 4.31 0.69 LEU HB2 H 49150 -1.52 8.02 1.61 0.37 LEU HB3 H 47082 -1.79 8.39 1.52 0.38 LEU HG H 43937 -2.08 5.70 1.50 0.35 LEU HD1 H 48931 -3.42 30.18 0.75 0.34 LEU HD2 H 47045 -3.42 24.50 0.72 0.37 LEU C C 44872 0.07 228.49 176.98 3.64 LEU CA C 61856 14.37 158.32 55.65 2.25 LEU CB C 58145 16.38 93.18 42.29 2.04 LEU CG C 37337 15.30 75.28 26.81 1.52 LEU CD1 C 41395 0.68 120.70 24.70 2.03 LEU CD2 C 39514 0.28 116.30 24.10 2.11 LEU N N 65936 0.04 627.00 122.00 8.94 LYS H H 59776 0.00 64.42 8.18 0.66 LYS HA H 46075 0.27 32.65 4.26 0.47 LYS HB2 H 41531 -1.42 35.97 1.77 0.32 LYS HB3 H 38983 -1.43 35.97 1.74 0.33 LYS HG2 H 37640 -1.45 29.88 1.36 0.31 LYS HG3 H 34510 -1.83 29.88 1.35 0.33 LYS HD2 H 33529 -1.68 119.62 1.61 0.75 LYS HD3 H 29837 -2.02 41.68 1.60 0.37 LYS HE2 H 33023 -0.49 8.37 2.91 0.22 LYS HE3 H 28830 -0.05 6.83 2.90 0.22 LYS HZ H 1293 -10.90 10.51 7.32 1.15 LYS C C 36670 0.11 996.25 176.59 6.38 LYS CA C 50925 22.02 86.72 56.94 2.27 LYS CB C 47640 -26.69 229.20 32.81 2.22 LYS CG C 31493 2.90 77.38 24.91 1.61 LYS CD C 29749 15.37 77.48 28.97 1.51 LYS CE C 28863 12.03 89.98 41.89 1.45 LYS N N 54888 0.04 217.00 121.00 4.34 LYS NZ N 211 1.95 177.20 47.93 30.24 MET H H 16652 -0.21 19.97 8.26 0.62 MET HA H 13161 -0.93 313.57 4.42 2.74 MET HB2 H 11818 -27.31 33.75 2.02 0.63 MET HB3 H 11141 -27.31 12.94 1.99 0.56 MET HG2 H 10926 -33.86 32.70 2.35 1.76 MET HG3 H 10299 -33.86 31.70 2.32 1.88 MET HE H 8084 -24.86 10.20 1.71 1.92 MET C C 10950 2.20 183.25 176.14 3.83 MET CA C 15407 4.37 85.33 56.13 2.34 MET CB C 14288 0.20 83.38 32.98 2.50 MET CG C 9145 2.30 81.18 32.04 1.70 MET CE C 7119 8.90 88.20 17.20 2.72 MET N N 15835 0.20 222.50 120.06 4.90 PHE H H 30523 -0.50 175.07 8.35 1.21 PHE HA H 23117 1.45 59.70 4.62 0.68 PHE HB2 H 21640 0.16 7.98 2.99 0.38 PHE HB3 H 21095 -0.21 12.72 2.93 0.41 PHE HD1 H 18401 0.60 12.15 7.03 0.42 PHE HD2 H 15507 0.60 12.15 7.03 0.43 PHE HE1 H 16150 -2.84 14.08 7.05 0.48 PHE HE2 H 13823 0.14 12.90 7.05 0.47 PHE HZ H 11550 -7.14 43.62 6.99 0.77 PHE C C 19232 0.09 187.61 175.44 3.41 PHE CA C 26515 4.92 73.43 58.11 2.65 PHE CB C 25017 21.40 137.00 39.97 2.34 PHE CG C 285 7.23 152.84 137.23 12.27 PHE CD1 C 10612 7.16 731.37 131.38 7.38 PHE CD2 C 7759 7.16 731.37 131.39 8.26 PHE CE1 C 9268 0.00 144.99 130.47 4.34 PHE CE2 C 6788 7.47 139.70 130.53 3.99 PHE CZ C 7134 7.35 138.60 129.04 3.74 PHE N N 28518 0.07 229.00 120.36 5.00 PRO HA H 26224 0.74 135.80 4.39 0.89 PRO HB2 H 24428 -1.50 5.63 2.07 0.37 PRO HB3 H 23621 -3.48 6.10 1.99 0.39 PRO HG2 H 22196 -2.35 4.92 1.92 0.35 PRO HG3 H 20534 -1.52 4.92 1.89 0.36 PRO HD2 H 22840 -6.56 7.67 3.63 0.47 PRO HD3 H 22011 -6.56 6.30 3.60 0.49 PRO C C 20108 0.05 183.52 176.67 3.72 PRO CA C 29227 4.19 177.79 63.35 2.90 PRO CB C 27467 6.11 81.08 31.87 1.75 PRO CG C 19330 18.28 76.28 27.24 1.79 PRO CD C 19463 4.99 98.58 50.31 1.88 PRO N N 961 31.27 430.00 135.93 35.56 SER H H 51261 -15.30 13.13 8.28 0.61 SER HA H 40273 1.43 58.74 4.48 0.50 SER HB2 H 36967 0.61 8.20 3.87 0.28 SER HB3 H 34231 0.61 7.77 3.84 0.30 SER HG H 682 0.13 11.36 5.50 1.21 SER C C 32971 0.00 197.10 174.60 3.19 SER CA C 46094 24.40 175.20 58.71 2.22 SER CB C 42974 -939.28 171.73 63.71 5.34 SER N N 47647 0.00 227.50 116.27 4.07 THR H H 45579 0.02 175.50 8.24 1.13 THR HA H 34886 -1.50 54.90 4.46 0.56 THR HB H 32139 0.09 73.47 4.17 0.83 THR HG1 H 1239 0.27 11.01 5.30 1.34 THR HG2 H 31856 -12.10 22.21 1.14 0.33 THR C C 28346 11.85 185.92 174.47 4.22 THR CA C 39587 34.44 92.66 62.25 2.66 THR CB C 36864 -939.28 629.21 69.60 6.55 THR CG2 C 26041 10.91 175.60 21.59 1.98 THR N N 42567 0.00 402.00 115.47 6.90 TRP H H 10362 5.13 59.40 8.28 0.93 TRP HA H 7908 2.24 11.41 4.68 0.54 TRP HB2 H 7499 0.42 5.35 3.17 0.36 TRP HB3 H 7289 -0.38 4.49 3.11 0.38 TRP HD1 H 6733 2.43 10.75 7.13 0.37 TRP HE1 H 7309 -1.28 18.00 10.07 0.72 TRP HE3 H 5928 1.85 10.82 7.28 0.54 TRP HZ2 H 6374 2.63 10.81 7.26 0.43 TRP HZ3 H 5732 0.76 8.90 6.84 0.50 TRP HH2 H 5875 2.84 10.90 6.94 0.48 TRP C C 6180 10.35 184.30 176.13 3.87 TRP CA C 8531 28.74 177.91 57.71 2.98 TRP CB C 8062 1.60 123.64 30.11 2.93 TRP CG C 205 25.21 116.53 109.96 8.96 TRP CD1 C 4187 30.24 158.33 126.28 4.32 TRP CD2 C 141 120.20 155.17 128.39 2.94 TRP CE2 C 180 113.89 177.71 138.23 6.95 TRP CE3 C 3541 -10.87 174.81 120.13 5.19 TRP CZ2 C 4017 7.38 144.03 114.01 4.50 TRP CZ3 C 3573 -8.70 161.54 121.10 4.84 TRP CH2 C 3732 -6.33 160.82 123.51 5.04 TRP N N 9293 25.80 224.60 121.65 4.94 TRP NE1 N 5896 0.53 249.50 129.18 3.99 TYR H H 26253 0.02 12.01 8.31 0.74 TYR HA H 20083 0.44 7.16 4.61 0.57 TYR HB2 H 18771 -21.23 23.28 2.89 0.49 TYR HB3 H 18355 -21.23 23.28 2.83 0.50 TYR HD1 H 16413 0.19 9.39 6.91 0.39 TYR HD2 H 13899 0.55 10.50 6.91 0.39 TYR HE1 H 15609 0.08 11.80 6.69 0.32 TYR HE2 H 13353 0.43 11.70 6.69 0.33 TYR HH H 361 -0.79 31.00 9.13 2.21 TYR C C 15794 2.20 184.78 175.32 4.68 TYR CA C 22158 2.20 69.56 58.13 2.62 TYR CB C 20674 18.38 175.51 39.32 2.72 TYR CG C 266 7.11 174.59 128.24 11.83 TYR CD1 C 9670 19.59 733.91 132.86 16.86 TYR CD2 C 6673 19.59 733.91 133.05 20.02 TYR CE1 C 9589 40.44 177.72 117.74 3.78 TYR CE2 C 6616 34.12 154.10 117.78 3.01 TYR CZ C 218 6.84 165.72 155.02 15.96 TYR N N 23967 0.20 818.00 120.87 13.97 VAL H H 56233 -0.41 15.05 8.28 0.69 VAL HA H 42952 -2.83 54.97 4.17 0.65 VAL HB H 40195 -27.48 31.75 1.98 0.47 VAL HG1 H 39782 -27.20 24.20 0.82 0.35 VAL HG2 H 39037 -27.20 56.56 0.80 0.46 VAL C C 36193 1.00 205.70 175.64 3.23 VAL CA C 49640 29.56 91.71 62.53 2.90 VAL CB C 46214 17.10 175.75 32.74 2.10 VAL CG1 C 33912 -7.40 117.16 21.53 1.89 VAL CG2 C 32715 -5.65 121.47 21.32 2.04 VAL N N 53283 0.20 529.00 121.19 8.18