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 6832934 possible chemical shifts in the BMRB database, 5021474 were included in calculating this table. Last updated: 6/4/2015 Res Name Atom Count Min. Max. Avg. Std Dev ALA H H 46014 3.53 12.11 8.19 0.59 ALA HA H 33745 0.87 6.51 4.24 0.43 ALA HB H 31660 -0.83 3.12 1.36 0.25 ALA C C 29703 164.48 187.20 177.83 2.09 ALA CA C 40420 39.92 65.52 53.19 1.94 ALA CB C 37918 6.61 28.80 18.96 1.77 ALA N N 43225 98.05 142.81 123.27 3.47 ARG H H 30570 3.57 12.69 8.23 0.61 ARG HA H 22969 1.34 6.52 4.29 0.46 ARG HB2 H 20765 -0.61 3.49 1.79 0.26 ARG HB3 H 19631 -0.74 3.32 1.76 0.28 ARG HG2 H 18599 -0.64 3.51 1.57 0.27 ARG HG3 H 17164 -0.74 3.51 1.54 0.29 ARG HD2 H 18278 1.04 4.69 3.12 0.23 ARG HD3 H 16584 0.89 4.56 3.10 0.25 ARG HE H 5616 2.20 11.88 7.36 0.60 ARG HH11 H 522 5.88 10.07 6.89 0.46 ARG HH12 H 401 5.92 10.73 6.83 0.43 ARG HH21 H 457 4.85 11.35 6.80 0.48 ARG HH22 H 370 5.92 10.19 6.81 0.45 ARG C C 18570 167.44 184.51 176.48 2.01 ARG CA C 26059 43.27 67.98 56.82 2.30 ARG CB C 24284 20.78 42.50 30.64 1.82 ARG CG C 15188 18.22 39.98 27.21 1.17 ARG CD C 15390 32.50 50.88 43.15 0.90 ARG CZ C 398 145.03 179.69 160.01 2.86 ARG N N 27847 102.78 137.60 120.78 3.65 ARG NE N 3297 67.00 99.81 84.60 1.64 ARG NH1 N 93 67.60 87.79 74.25 5.11 ARG NH2 N 86 69.90 85.28 72.80 2.80 ASP H H 36255 4.06 12.68 8.30 0.57 ASP HA H 26509 2.33 6.33 4.59 0.31 ASP HB2 H 24547 -0.39 4.60 2.71 0.26 ASP HB3 H 23567 -0.23 4.58 2.66 0.27 ASP HD2 H 2 4.65 9.29 6.97 3.28 ASP C C 22996 166.80 182.70 176.45 1.72 ASP CA C 31737 41.11 67.17 54.70 2.04 ASP CB C 29933 26.50 54.95 40.86 1.61 ASP CG C 423 170.72 186.50 179.31 1.85 ASP N N 34299 101.90 143.52 120.64 3.80 ASN H H 25525 2.61 12.40 8.33 0.62 ASN HA H 19267 1.92 6.60 4.66 0.36 ASN HB2 H 17957 0.23 4.47 2.81 0.31 ASN HB3 H 17305 -0.07 4.47 2.75 0.33 ASN HD21 H 13476 2.06 10.92 7.32 0.49 ASN HD22 H 13278 2.58 10.92 7.15 0.50 ASN C C 15906 167.04 185.30 175.31 1.78 ASN CA C 22138 41.58 66.21 53.56 1.88 ASN CB C 20939 26.45 53.68 38.69 1.67 ASN CG C 1516 166.40 183.80 176.76 1.40 ASN N N 23458 101.71 137.49 118.90 3.95 ASN ND2 N 11387 99.40 134.50 112.77 2.30 CYS H H 13107 4.04 12.12 8.38 0.68 CYS HA H 11191 1.64 6.45 4.65 0.55 CYS HB2 H 10774 -0.54 4.72 2.95 0.44 CYS HB3 H 10506 -0.83 4.77 2.89 0.46 CYS HG H 109 0.10 7.39 2.03 1.23 CYS C C 6243 166.73 187.59 174.96 2.04 CYS CA C 8916 42.45 68.07 58.24 3.38 CYS CB C 8422 17.99 62.07 32.85 6.25 CYS N N 9748 4.47 135.89 120.08 4.66 GLU H H 47644 4.24 12.69 8.33 0.59 GLU HA H 35138 1.65 6.29 4.24 0.40 GLU HB2 H 31627 0.34 3.37 2.02 0.21 GLU HB3 H 29704 0.34 3.47 2.00 0.22 GLU HG2 H 29385 0.53 3.77 2.27 0.21 GLU HG3 H 27320 0.46 3.80 2.25 0.21 GLU HE2 H 3 2.73 2.93 2.82 0.10 GLU C C 31139 166.80 183.52 176.93 1.92 GLU CA C 42158 44.35 66.94 57.35 2.07 GLU CB C 39228 18.36 43.70 29.96 1.69 GLU CG C 25676 25.31 42.87 36.10 1.19 GLU CD C 458 129.75 189.46 182.46 3.08 GLU N N 45380 102.94 138.60 120.70 3.46 GLN H H 25855 3.51 12.04 8.21 0.58 GLN HA H 19322 1.57 6.34 4.26 0.43 GLN HB2 H 17449 -0.07 4.00 2.05 0.25 GLN HB3 H 16579 -0.38 4.04 2.02 0.26 GLN HG2 H 16397 -0.11 3.90 2.31 0.27 GLN HG3 H 15122 -0.41 3.90 2.29 0.28 GLN HE21 H 12279 3.39 11.11 7.21 0.45 GLN HE22 H 12206 3.59 10.35 7.04 0.44 GLN C C 16641 168.09 185.31 176.38 1.92 GLN CA C 22984 43.45 66.60 56.63 2.12 GLN CB C 21440 18.43 42.20 29.15 1.81 GLN CG C 14254 21.64 42.80 33.77 1.11 GLN CD C 1418 171.37 183.54 179.71 1.26 GLN N N 24365 103.88 139.55 119.88 3.55 GLN NE2 N 10898 97.90 125.33 111.86 1.68 GLY H H 45436 3.01 12.22 8.33 0.63 GLY HA2 H 33333 0.84 6.48 3.96 0.37 GLY HA3 H 31676 0.99 6.48 3.90 0.37 GLY C C 28797 163.27 184.89 173.90 1.86 GLY CA C 39968 33.15 57.88 45.36 1.27 GLY N N 41911 93.60 162.19 109.59 3.72 HIS H H 13042 3.97 12.39 8.24 0.68 HIS HA H 10034 1.93 8.90 4.60 0.43 HIS HB2 H 9283 -0.04 8.70 3.11 0.35 HIS HB3 H 8998 -0.39 8.70 3.05 0.38 HIS HD1 H 410 2.73 17.20 8.63 2.56 HIS HD2 H 6557 3.46 9.42 7.00 0.42 HIS HE1 H 5162 3.21 10.88 7.96 0.48 HIS HE2 H 169 6.57 16.53 9.63 2.43 HIS C C 8264 166.90 183.12 175.27 1.95 HIS CA C 11792 43.31 71.15 56.53 2.33 HIS CB C 11070 18.75 43.38 30.21 2.08 HIS CG C 92 117.54 139.56 131.91 3.37 HIS CD2 C 4253 110.52 159.95 120.44 3.42 HIS CE1 C 3261 104.67 145.42 137.64 2.29 HIS N N 12054 103.99 136.48 119.67 4.03 HIS ND1 N 214 164.31 229.14 193.20 18.30 HIS NE2 N 225 161.38 226.76 184.66 16.56 ILE H H 32155 3.43 11.87 8.26 0.68 ILE HA H 23740 1.32 6.36 4.16 0.56 ILE HB H 22235 -1.28 3.87 1.78 0.29 ILE HG12 H 20140 -2.38 2.69 1.27 0.40 ILE HG13 H 19392 -2.07 2.99 1.19 0.41 ILE HG2 H 21179 -1.47 2.20 0.78 0.27 ILE HD1 H 21592 -1.47 2.82 0.68 0.29 ILE C C 20707 166.40 187.55 175.93 1.90 ILE CA C 28400 43.84 71.86 61.67 2.69 ILE CB C 26524 22.11 51.88 38.58 1.99 ILE CG1 C 17366 11.00 39.05 27.74 1.69 ILE CG2 C 18431 3.45 29.80 17.53 1.33 ILE CD1 C 18772 2.91 29.60 13.40 1.66 ILE N N 30283 99.00 138.12 121.39 4.27 LEU H H 53396 2.15 13.22 8.22 0.64 LEU HA H 39465 1.72 6.42 4.30 0.46 LEU HB2 H 36075 -1.25 4.13 1.61 0.35 LEU HB3 H 34508 -1.45 3.23 1.52 0.36 LEU HG H 31933 -1.06 3.90 1.51 0.33 LEU HD1 H 35826 -1.73 2.36 0.75 0.28 LEU HD2 H 34421 -1.65 2.67 0.73 0.28 LEU C C 34199 167.49 189.78 177.08 1.94 LEU CA C 46899 42.69 67.88 55.70 2.12 LEU CB C 43913 26.40 53.70 42.26 1.85 LEU CG C 27245 15.30 37.70 26.78 1.09 LEU CD1 C 30178 10.95 36.85 24.68 1.59 LEU CD2 C 28749 11.71 30.40 24.07 1.69 LEU N N 50000 98.56 177.62 121.81 3.87 LYS H H 44838 4.11 12.03 8.18 0.60 LYS HA H 33803 0.68 6.17 4.26 0.43 LYS HB2 H 30077 -0.71 4.05 1.78 0.25 LYS HB3 H 28305 -0.72 3.95 1.75 0.27 LYS HG2 H 27224 -0.98 3.61 1.37 0.26 LYS HG3 H 25057 -1.16 3.61 1.35 0.27 LYS HD2 H 24195 -1.02 3.19 1.61 0.21 LYS HD3 H 21754 -1.02 3.19 1.60 0.22 LYS HE2 H 23949 1.23 4.43 2.91 0.19 LYS HE3 H 21049 1.17 4.55 2.91 0.20 LYS HZ H 889 1.95 9.90 7.41 0.66 LYS C C 28111 166.63 185.00 176.73 1.92 LYS CA C 38578 40.73 65.87 56.99 2.18 LYS CB C 35938 21.19 46.60 32.77 1.77 LYS CG C 22889 16.85 36.22 24.89 1.12 LYS CD C 21636 20.10 40.10 28.95 1.08 LYS CE C 20958 30.70 52.20 41.89 0.83 LYS N N 41431 101.10 140.30 121.03 3.71 LYS NZ N 38 29.48 43.69 33.25 2.22 MET H H 12651 4.87 12.46 8.26 0.59 MET HA H 9730 1.13 6.35 4.39 0.46 MET HB2 H 8666 -1.05 4.07 2.02 0.33 MET HB3 H 8143 -0.99 3.47 1.99 0.35 MET HG2 H 7967 -0.42 4.40 2.42 0.35 MET HG3 H 7519 -0.30 4.24 2.39 0.38 MET HE H 5770 -0.71 8.38 1.88 0.41 MET C C 8333 167.40 183.16 176.24 2.07 MET CA C 11684 43.28 66.86 56.14 2.22 MET CB C 10791 20.36 46.46 32.93 2.20 MET CG C 6598 19.06 38.58 32.03 1.24 MET CE C 5116 10.69 38.44 17.08 1.54 MET N N 11990 102.88 138.55 120.10 3.52 PHE H H 22741 3.55 12.18 8.34 0.72 PHE HA H 16644 1.78 6.87 4.61 0.57 PHE HB2 H 15431 0.16 4.46 3.00 0.37 PHE HB3 H 15050 -0.21 4.69 2.94 0.39 PHE HD1 H 12939 4.67 8.15 7.06 0.31 PHE HD2 H 11100 4.67 8.15 7.06 0.31 PHE HE1 H 11248 4.38 8.80 7.08 0.31 PHE HE2 H 9818 4.38 8.80 7.08 0.31 PHE HZ H 8022 4.32 9.50 6.99 0.42 PHE C C 14413 166.85 184.93 175.49 1.99 PHE CA C 19743 45.52 69.82 58.15 2.59 PHE CB C 18514 25.52 50.23 39.93 2.07 PHE CG C 169 127.24 144.00 138.21 2.81 PHE CD1 C 7501 116.95 143.16 131.57 1.21 PHE CD2 C 5616 118.13 138.25 131.58 1.19 PHE CE1 C 6541 114.75 139.56 130.72 1.29 PHE CE2 C 4912 114.70 139.70 130.75 1.17 PHE CZ C 5068 116.46 138.60 129.21 1.46 PHE N N 21231 102.20 139.02 120.36 4.15 PRO HA H 19055 1.04 8.08 4.39 0.33 PRO HB2 H 17624 -0.47 4.35 2.08 0.35 PRO HB3 H 17050 -0.58 3.79 2.00 0.36 PRO HG2 H 15979 -0.77 4.42 1.92 0.31 PRO HG3 H 14779 -0.90 4.42 1.90 0.33 PRO HD2 H 16357 0.63 5.36 3.65 0.35 PRO HD3 H 15755 0.34 5.36 3.61 0.38 PRO C C 15227 168.38 182.84 176.77 1.49 PRO CA C 21873 50.12 70.67 63.36 1.51 PRO CB C 20436 20.91 45.16 31.84 1.17 PRO CG C 13956 18.28 33.90 27.19 1.07 PRO CD C 13976 37.08 58.81 50.34 1.00 PRO N N 578 110.91 145.26 134.32 6.47 SER H H 38993 3.76 12.33 8.28 0.58 SER HA H 29697 1.54 6.85 4.47 0.40 SER HB2 H 27098 1.70 5.45 3.87 0.25 SER HB3 H 25054 1.54 5.45 3.85 0.27 SER HG H 418 0.13 8.97 5.44 1.01 SER C C 25061 164.47 184.88 174.66 1.73 SER CA C 34875 45.13 73.19 58.75 2.09 SER CB C 32354 31.40 76.39 63.78 1.52 SER N N 36194 95.97 133.68 116.26 3.51 THR H H 34133 5.32 11.82 8.23 0.62 THR HA H 25298 1.65 7.47 4.45 0.48 THR HB H 22923 0.92 8.35 4.16 0.32 THR HG1 H 748 0.32 8.21 5.17 1.15 THR HG2 H 22714 -1.19 3.40 1.14 0.22 THR C C 21309 165.50 184.43 174.59 1.72 THR CA C 29576 48.01 72.80 62.27 2.60 THR CB C 27357 29.97 81.53 69.71 1.73 THR CG2 C 18437 11.70 36.73 21.56 1.10 THR N N 31835 95.77 138.27 115.36 4.72 TRP H H 7344 5.16 11.76 8.27 0.76 TRP HA H 5368 2.24 6.55 4.66 0.52 TRP HB2 H 5038 0.42 4.54 3.19 0.35 TRP HB3 H 4892 0.26 4.44 3.12 0.37 TRP HD1 H 4495 4.90 8.93 7.14 0.35 TRP HE1 H 4945 5.12 13.49 10.08 0.64 TRP HE3 H 3940 4.89 9.95 7.32 0.41 TRP HZ2 H 4228 4.66 8.56 7.28 0.32 TRP HZ3 H 3816 3.88 8.90 6.87 0.38 TRP HH2 H 3889 4.37 10.17 6.98 0.37 TRP C C 4347 168.17 182.60 176.23 2.00 TRP CA C 6010 44.69 69.76 57.74 2.56 TRP CB C 5657 18.63 52.30 29.96 2.00 TRP CG C 126 107.50 116.53 110.98 1.84 TRP CD1 C 2766 108.45 133.49 126.55 1.82 TRP CD2 C 96 120.20 132.62 127.78 1.60 TRP CE2 C 91 113.89 177.71 138.35 7.21 TRP CE3 C 2330 93.34 137.60 120.43 1.74 TRP CZ2 C 2639 81.81 132.03 114.25 1.39 TRP CZ3 C 2367 98.61 138.39 121.35 1.58 TRP CH2 C 2462 91.62 131.54 123.81 1.56 TRP N N 6557 101.97 138.11 121.59 4.07 TRP NE1 N 3913 107.31 139.20 129.29 2.06 TYR H H 19183 4.16 12.01 8.30 0.73 TYR HA H 14316 1.19 6.77 4.61 0.56 TYR HB2 H 13212 -0.49 4.70 2.90 0.37 TYR HB3 H 12907 -0.19 4.70 2.84 0.39 TYR HD1 H 11527 3.93 8.53 6.93 0.30 TYR HD2 H 10054 4.03 8.50 6.93 0.30 TYR HE1 H 10967 4.58 7.83 6.70 0.23 TYR HE2 H 9668 4.56 8.50 6.70 0.23 TYR HH H 195 -0.79 13.75 9.23 1.62 TYR C C 11560 167.86 184.78 175.47 1.97 TYR CA C 16209 44.64 69.56 58.19 2.52 TYR CB C 15052 25.32 47.30 39.26 2.14 TYR CG C 152 117.70 174.59 129.71 4.49 TYR CD1 C 6728 31.06 141.57 132.71 2.05 TYR CD2 C 4836 31.06 138.29 132.67 2.10 TYR CE1 C 6700 110.70 137.42 117.93 1.25 TYR CE2 C 4796 106.55 135.82 117.89 1.25 TYR CZ C 117 105.25 160.45 156.39 5.01 TYR N N 17413 39.20 144.96 120.47 4.26 VAL H H 42364 3.98 12.59 8.28 0.67 VAL HA H 31402 0.97 6.30 4.16 0.57 VAL HB H 29018 -1.24 3.32 1.98 0.32 VAL HG1 H 28676 -1.13 2.57 0.83 0.26 VAL HG2 H 28080 -2.32 2.78 0.80 0.28 VAL C C 27385 165.65 183.95 175.71 1.87 VAL CA C 37272 49.18 70.34 62.58 2.86 VAL CB C 34462 20.29 45.33 32.70 1.78 VAL CG1 C 24305 13.53 32.27 21.51 1.37 VAL CG2 C 23385 13.26 30.46 21.29 1.55 VAL N N 40068 97.22 143.29 121.08 4.48