Selected Chemical Shift Statistics Statistics Calculated for Selected Chemical Shifts from Atoms in the 20 Common Amino Acids BMRB Entries not included in the calculations for this table contained chemical shifts outside eight standard deviations from the mean calculated for the full BMRB database or a chemical shift for at least one carbon bound proton that was greater than 10ppm or was less than -2.5ppm. These criteria were used to eliminate from the calculations chemical shifts from paramagnetic proteins, from proteins with aromatic prosthetic groups, and from entries where unusual chemical shift referencing was used. Of the 9046374 possible chemical shifts in the BMRB database, 6854642 were included in calculating this table. Last updated: 8/13/2020 Res Name Atom Count Min. Max. Avg. Std Dev ALA H H 66020 3.53 12.11 8.19 0.58 ALA HA H 43760 0.87 6.57 4.24 0.42 ALA HB H 41469 -0.83 3.12 1.36 0.24 ALA C C 43294 164.48 187.20 177.81 2.05 ALA CA C 58950 39.92 72.25 53.17 1.94 ALA CB C 55321 6.61 43.14 18.96 1.78 ALA N N 63335 98.05 142.81 123.32 3.45 ARG H H 43988 3.57 12.69 8.23 0.61 ARG HA H 29790 1.29 6.62 4.29 0.45 ARG HB2 H 26776 -0.61 3.74 1.80 0.26 ARG HB3 H 25358 -0.74 3.74 1.77 0.27 ARG HG2 H 23788 -0.64 3.51 1.57 0.26 ARG HG3 H 22095 -0.74 3.51 1.55 0.28 ARG HD2 H 23333 1.04 4.85 3.12 0.23 ARG HD3 H 21271 0.89 4.69 3.10 0.25 ARG HE H 6990 2.20 11.88 7.36 0.58 ARG HH11 H 609 5.88 10.11 6.91 0.48 ARG HH12 H 465 5.92 10.73 6.87 0.51 ARG HH21 H 524 4.85 11.35 6.81 0.48 ARG HH22 H 422 5.92 10.19 6.83 0.50 ARG C C 27158 167.44 184.51 176.49 1.99 ARG CA C 38100 35.70 74.48 56.80 2.29 ARG CB C 35336 20.78 43.39 30.64 1.80 ARG CG C 20174 18.22 49.39 27.22 1.20 ARG CD C 20325 27.12 50.88 43.16 0.92 ARG CZ C 518 113.28 179.92 160.05 3.78 ARG N N 40993 102.43 137.60 120.85 3.62 ARG NE N 4179 67.00 99.81 84.60 1.62 ARG NH1 N 137 67.60 87.82 74.32 5.13 ARG NH2 N 120 69.26 87.83 72.78 2.97 ASP H H 51989 4.06 12.68 8.30 0.56 ASP HA H 34396 2.33 6.67 4.58 0.31 ASP HB2 H 31758 -0.39 4.60 2.71 0.26 ASP HB3 H 30495 -0.23 4.58 2.66 0.27 ASP HD2 H 9 4.58 12.12 7.19 2.89 ASP C C 33397 166.80 182.70 176.43 1.69 ASP CA C 46041 41.11 67.17 54.69 2.01 ASP CB C 43357 26.50 58.51 40.87 1.60 ASP CG C 590 169.68 186.50 179.25 1.86 ASP N N 50039 101.90 143.52 120.71 3.76 ASN H H 36515 2.61 12.68 8.32 0.61 ASN HA H 24694 2.04 6.60 4.66 0.35 ASN HB2 H 22910 0.22 4.47 2.80 0.31 ASN HB3 H 22075 -0.04 4.77 2.75 0.33 ASN HD21 H 16772 2.06 10.92 7.32 0.48 ASN HD22 H 16543 2.58 10.92 7.15 0.50 ASN C C 23024 166.80 185.30 175.29 1.76 ASN CA C 32233 41.20 68.56 53.54 1.86 ASN CB C 30450 23.16 57.35 38.69 1.66 ASN CG C 1912 166.40 183.80 176.78 1.38 ASN N N 34346 101.71 137.49 118.93 3.88 ASN ND2 N 14433 99.40 134.50 112.76 2.26 CYS H H 18002 4.38 12.66 8.38 0.68 CYS HA H 14417 1.64 6.45 4.65 0.54 CYS HB2 H 13811 -0.54 4.72 2.95 0.44 CYS HB3 H 13469 -0.83 4.77 2.89 0.45 CYS HG H 178 -1.83 7.39 1.95 1.17 CYS C C 8825 166.73 187.59 174.87 2.02 CYS CA C 12895 41.51 68.07 58.10 3.43 CYS CB C 12240 17.99 63.89 33.22 6.43 CYS N N 14173 100.48 138.68 120.13 4.43 GLU H H 68326 4.29 12.69 8.33 0.58 GLU HA H 45461 1.39 6.32 4.24 0.40 GLU HB2 H 40668 0.34 3.37 2.02 0.21 GLU HB3 H 38268 0.27 3.47 2.00 0.21 GLU HG2 H 37388 0.56 3.77 2.27 0.21 GLU HG3 H 34892 0.56 3.83 2.25 0.21 GLU HE2 H 6 2.73 2.93 2.82 0.07 GLU C C 44626 166.80 183.52 176.94 1.89 GLU CA C 60569 41.96 71.16 57.33 2.07 GLU CB C 56324 18.36 49.56 29.96 1.69 GLU CG C 33667 25.06 54.83 36.11 1.19 GLU CD C 686 173.41 189.46 182.31 2.29 GLU N N 66023 101.34 138.60 120.75 3.42 GLN H H 37741 3.51 12.22 8.22 0.57 GLN HA H 25187 1.57 6.44 4.26 0.42 GLN HB2 H 22686 -0.11 4.00 2.05 0.25 GLN HB3 H 21626 -0.52 4.04 2.01 0.26 GLN HG2 H 21067 -0.21 4.44 2.31 0.26 GLN HG3 H 19540 -0.41 4.44 2.29 0.28 GLN HE21 H 15524 3.39 11.08 7.22 0.44 GLN HE22 H 15439 3.59 10.35 7.04 0.43 GLN C C 24341 168.09 185.31 176.36 1.91 GLN CA C 33725 43.45 66.60 56.58 2.10 GLN CB C 31432 18.43 43.65 29.16 1.79 GLN CG C 18767 21.64 51.08 33.78 1.10 GLN CD C 1836 171.37 183.93 179.70 1.25 GLN N N 36232 103.88 139.55 119.99 3.51 GLN NE2 N 13967 92.49 133.30 111.87 1.68 GLY H H 65220 3.01 12.22 8.33 0.63 GLY HA2 H 42465 0.86 6.98 3.96 0.36 GLY HA3 H 40441 0.74 6.98 3.89 0.36 GLY C C 41697 163.27 184.89 173.90 1.82 GLY CA C 58225 33.15 61.28 45.36 1.30 GLY N N 61538 93.60 162.19 109.57 3.64 HIS H H 18169 3.97 12.39 8.24 0.67 HIS HA H 12692 1.93 8.90 4.60 0.43 HIS HB2 H 11711 -0.04 8.70 3.10 0.35 HIS HB3 H 11364 -0.39 8.70 3.05 0.37 HIS HD1 H 515 2.73 17.20 8.51 2.41 HIS HD2 H 8058 3.65 9.42 7.00 0.41 HIS HE1 H 6253 3.21 10.88 7.95 0.48 HIS HE2 H 205 6.57 16.53 9.56 2.33 HIS C C 11576 166.90 183.12 175.26 1.94 HIS CA C 16548 43.31 77.56 56.49 2.31 HIS CB C 15458 18.75 54.90 30.26 2.11 HIS CG C 163 117.54 139.56 132.12 3.10 HIS CD2 C 5379 110.52 159.95 120.35 3.32 HIS CE1 C 4130 104.67 145.42 137.62 2.24 HIS N N 17144 103.99 136.48 119.70 4.01 HIS ND1 N 322 162.83 229.14 194.62 19.10 HIS NE2 N 333 161.10 226.76 184.29 16.64 ILE H H 45757 3.42 11.87 8.26 0.68 ILE HA H 30682 1.32 6.36 4.16 0.55 ILE HB H 28632 -1.28 3.87 1.78 0.29 ILE HG12 H 25788 -2.12 2.85 1.27 0.40 ILE HG13 H 24783 -2.07 2.99 1.20 0.41 ILE HG2 H 27267 -1.47 2.20 0.78 0.27 ILE HD1 H 28653 -1.47 2.82 0.68 0.28 ILE C C 29511 166.40 187.55 175.94 1.90 ILE CA C 40600 39.56 71.86 61.67 2.69 ILE CB C 37714 18.10 51.88 38.55 1.99 ILE CG1 C 23085 8.77 42.09 27.75 1.70 ILE CG2 C 24402 3.45 37.01 17.52 1.33 ILE CD1 C 25722 4.94 29.60 13.40 1.65 ILE N N 43762 83.33 138.12 121.42 4.21 LEU H H 76154 4.08 13.22 8.22 0.63 LEU HA H 50714 1.72 6.42 4.30 0.45 LEU HB2 H 46246 -1.20 4.13 1.61 0.34 LEU HB3 H 44345 -1.41 3.23 1.53 0.36 LEU HG H 40511 -1.06 3.90 1.51 0.33 LEU HD1 H 46753 -1.73 2.36 0.76 0.27 LEU HD2 H 44938 -1.92 2.35 0.73 0.28 LEU C C 49114 166.22 189.78 177.09 1.93 LEU CA C 67535 42.69 67.88 55.68 2.11 LEU CB C 62876 26.88 54.44 42.24 1.85 LEU CG C 35740 15.30 37.80 26.78 1.09 LEU CD1 C 40486 10.95 36.85 24.64 1.59 LEU CD2 C 38617 9.86 32.52 24.08 1.68 LEU N N 72582 84.66 177.62 121.84 3.84 LYS H H 63967 3.26 12.03 8.18 0.59 LYS HA H 43712 1.30 6.25 4.26 0.43 LYS HB2 H 38805 -0.30 3.82 1.78 0.24 LYS HB3 H 36698 -0.45 3.82 1.75 0.26 LYS HG2 H 34977 -0.69 3.13 1.37 0.25 LYS HG3 H 32400 -0.85 3.05 1.35 0.26 LYS HD2 H 31000 -1.02 3.19 1.61 0.21 LYS HD3 H 28058 -0.53 3.19 1.60 0.21 LYS HE2 H 30579 0.67 4.43 2.91 0.19 LYS HE3 H 27058 1.17 4.55 2.91 0.20 LYS HZ H 1063 1.95 9.90 7.39 0.65 LYS C C 40024 166.63 185.00 176.73 1.91 LYS CA C 55362 40.73 75.50 56.97 2.17 LYS CB C 51493 21.19 46.60 32.75 1.76 LYS CG C 30369 16.85 40.50 24.90 1.13 LYS CD C 28579 15.37 42.87 28.96 1.10 LYS CE C 27505 25.24 56.00 41.89 0.87 LYS N N 60097 101.10 140.30 121.06 3.68 LYS NZ N 76 29.48 35.90 33.02 1.20 MET H H 17976 4.87 12.46 8.25 0.58 MET HA H 12527 1.13 6.35 4.39 0.46 MET HB2 H 11109 -1.05 4.07 2.03 0.32 MET HB3 H 10443 -0.99 3.47 1.99 0.34 MET HG2 H 10144 -0.42 4.40 2.42 0.35 MET HG3 H 9608 -0.47 4.24 2.39 0.37 MET HE H 7579 -0.71 8.38 1.89 0.39 MET C C 11955 167.40 183.16 176.26 2.05 MET CA C 16790 43.28 66.86 56.16 2.19 MET CB C 15467 20.36 46.46 32.93 2.16 MET CG C 8682 15.94 51.70 32.03 1.30 MET CE C 6905 0.00 44.10 17.11 1.71 MET N N 17354 102.80 138.55 120.09 3.46 PHE H H 32246 3.55 12.18 8.34 0.71 PHE HA H 21177 1.33 6.87 4.61 0.56 PHE HB2 H 19532 0.16 4.46 3.00 0.36 PHE HB3 H 19096 -0.14 4.69 2.94 0.38 PHE HD1 H 15988 4.47 8.15 7.06 0.31 PHE HD2 H 13769 4.47 8.15 7.06 0.31 PHE HE1 H 13838 4.38 8.80 7.08 0.31 PHE HE2 H 12081 4.38 8.80 7.08 0.31 PHE HZ H 9694 4.32 9.50 6.99 0.41 PHE C C 20425 166.85 184.93 175.49 1.97 PHE CA C 28309 36.03 69.82 58.12 2.57 PHE CB C 26379 25.52 56.74 39.92 2.06 PHE CG C 280 127.24 152.84 138.31 2.73 PHE CD1 C 9671 116.95 143.16 131.57 1.25 PHE CD2 C 7009 115.55 140.31 131.58 1.22 PHE CE1 C 8375 114.75 139.56 130.72 1.34 PHE CE2 C 6057 114.70 139.70 130.75 1.20 PHE CZ C 6315 115.10 139.13 129.22 1.48 PHE N N 30646 101.47 139.02 120.38 4.09 PRO HA H 24455 1.04 8.08 4.39 0.32 PRO HB2 H 22509 -0.75 4.59 2.08 0.34 PRO HB3 H 21861 -0.58 3.79 2.00 0.35 PRO HG2 H 20064 -0.60 4.42 1.93 0.30 PRO HG3 H 18653 -0.73 4.42 1.90 0.32 PRO HD2 H 20550 0.63 5.36 3.65 0.34 PRO HD3 H 19827 0.34 5.36 3.62 0.37 PRO C C 22134 168.38 182.84 176.76 1.47 PRO CA C 31243 48.56 72.28 63.35 1.51 PRO CB C 28992 20.91 50.25 31.84 1.16 PRO CG C 18268 18.28 50.75 27.20 1.10 PRO CD C 18229 26.92 58.81 50.34 1.04 PRO N N 1374 110.49 145.74 135.33 5.31 SER H H 55775 2.96 13.13 8.28 0.57 SER HA H 37783 1.28 6.85 4.47 0.40 SER HB2 H 34345 1.70 5.45 3.87 0.25 SER HB3 H 31833 1.16 5.45 3.85 0.27 SER HG H 614 0.13 8.97 5.37 1.05 SER C C 36177 164.47 197.10 174.65 1.72 SER CA C 50669 45.13 73.19 58.72 2.06 SER CB C 46747 31.40 76.39 63.80 1.50 SER N N 53021 95.97 133.68 116.30 3.47 THR H H 49222 5.32 11.80 8.23 0.61 THR HA H 32904 1.65 7.47 4.45 0.47 THR HB H 29729 0.92 8.35 4.16 0.32 THR HG1 H 1027 -1.78 9.01 5.07 1.29 THR HG2 H 29484 -0.97 3.28 1.14 0.21 THR C C 31159 165.50 184.43 174.57 1.71 THR CA C 43394 40.74 72.80 62.23 2.57 THR CB C 40009 27.09 81.53 69.70 1.72 THR CG2 C 24896 11.70 35.09 21.55 1.09 THR N N 46922 95.26 138.27 115.34 4.71 TRP H H 10190 5.16 11.76 8.27 0.76 TRP HA H 6690 2.04 6.58 4.66 0.52 TRP HB2 H 6255 0.68 4.54 3.19 0.34 TRP HB3 H 6068 0.26 4.44 3.12 0.36 TRP HD1 H 5508 4.60 8.93 7.14 0.34 TRP HE1 H 6234 4.69 13.49 10.08 0.64 TRP HE3 H 4748 4.89 10.00 7.32 0.41 TRP HZ2 H 5126 4.66 8.60 7.28 0.32 TRP HZ3 H 4584 3.88 8.90 6.87 0.37 TRP HH2 H 4718 4.37 10.17 6.98 0.36 TRP C C 6141 168.17 182.60 176.20 1.98 TRP CA C 8599 43.50 81.00 57.71 2.53 TRP CB C 7948 18.63 52.30 29.94 1.98 TRP CG C 158 105.80 116.53 111.05 1.82 TRP CD1 C 3455 108.45 135.60 126.55 1.86 TRP CD2 C 118 120.00 132.62 127.82 1.90 TRP CE2 C 121 113.89 177.71 138.05 6.84 TRP CE3 C 2868 93.34 137.60 120.48 1.83 TRP CZ2 C 3293 81.81 134.70 114.26 1.44 TRP CZ3 C 2912 98.61 138.39 121.37 1.60 TRP CH2 C 3074 91.62 131.54 123.81 1.55 TRP N N 9312 101.97 138.11 121.56 4.07 TRP NE1 N 5038 106.00 139.73 129.28 2.04 TYR H H 27183 4.16 12.34 8.29 0.73 TYR HA H 18104 1.19 6.83 4.60 0.55 TYR HB2 H 16653 -0.49 4.70 2.91 0.37 TYR HB3 H 16272 -0.19 4.70 2.84 0.39 TYR HD1 H 14202 4.68 8.54 6.93 0.29 TYR HD2 H 12434 4.43 8.54 6.93 0.29 TYR HE1 H 13462 4.58 8.04 6.70 0.22 TYR HE2 H 11874 4.56 8.50 6.70 0.23 TYR HH H 244 -0.79 13.75 9.14 1.58 TYR C C 16727 167.86 184.78 175.51 1.95 TYR CA C 23306 44.64 69.56 58.18 2.49 TYR CB C 21537 25.32 57.73 39.26 2.13 TYR CG C 246 117.70 144.30 129.64 2.51 TYR CD1 C 8619 115.30 141.57 132.71 1.40 TYR CD2 C 6128 113.00 139.47 132.69 1.52 TYR CE1 C 8526 92.49 137.42 117.95 1.38 TYR CE2 C 6025 106.55 135.82 117.92 1.28 TYR CZ C 156 153.54 160.45 156.82 1.47 TYR N N 25313 61.07 144.96 120.48 4.09 VAL H H 59751 3.98 12.59 8.27 0.66 VAL HA H 40003 0.97 6.30 4.16 0.57 VAL HB H 36866 -1.24 3.76 1.99 0.31 VAL HG1 H 37069 -1.13 2.57 0.83 0.26 VAL HG2 H 36283 -2.32 3.32 0.80 0.28 VAL C C 38921 165.65 183.95 175.72 1.85 VAL CA C 53133 39.65 77.15 62.55 2.85 VAL CB C 48950 18.97 45.33 32.68 1.78 VAL CG1 C 32442 12.07 32.27 21.51 1.37 VAL CG2 C 31254 11.38 33.12 21.30 1.52 VAL N N 57509 93.76 143.29 121.08 4.41