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 5188534 chemical shifts. Last updated: 5/9/2012 Res Name Atom Count Min. Max. Avg. Std Dev ALA H H 45699 0.00 123.45 8.20 0.87 ALA HA H 35664 -2.52 17.87 4.26 0.46 ALA HB H 33981 -14.04 5.48 1.35 0.30 ALA C C 28590 0.04 187.20 177.70 3.23 ALA CA C 38958 3.69 123.90 53.15 2.14 ALA CB C 37013 -40.99 99.00 19.10 2.56 ALA N N 42142 0.05 766.00 123.30 7.08 ARG H H 30913 0.00 861.00 8.27 4.94 ARG HA H 24719 0.00 12.57 4.30 0.48 ARG HB2 H 22551 -4.78 27.53 1.79 0.34 ARG HB3 H 21150 -1.13 27.53 1.76 0.35 ARG HG2 H 20291 -1.45 8.70 1.56 0.29 ARG HG3 H 18506 -1.30 8.52 1.54 0.31 ARG HD2 H 19941 -6.44 4.69 3.11 0.28 ARG HD3 H 17898 -0.49 4.79 3.09 0.30 ARG HE H 7039 0.00 118.45 8.49 10.93 ARG HH11 H 662 4.41 10.30 6.90 0.55 ARG HH12 H 486 4.41 10.73 6.84 0.52 ARG HH21 H 587 1.23 11.35 6.79 0.65 ARG HH22 H 466 1.23 10.18 6.76 0.64 ARG C C 18642 0.17 184.96 176.36 3.41 ARG CA C 25940 3.75 103.60 56.74 2.48 ARG CB C 24131 2.15 123.50 30.75 2.22 ARG CG C 16097 12.17 119.40 27.23 1.78 ARG CD C 16347 23.20 135.80 43.17 1.52 ARG CZ C 407 128.85 181.47 160.54 4.46 ARG N N 27792 0.13 177.67 120.75 4.18 ARG NE N 4375 0.00 149.11 89.79 17.37 ARG NH1 N 152 7.24 124.40 78.26 16.34 ARG NH2 N 125 66.20 128.47 79.83 16.40 ASP H H 36531 0.01 127.50 8.31 0.86 ASP HA H 28672 0.25 8.60 4.59 0.33 ASP HB2 H 26886 -0.39 37.40 2.73 0.61 ASP HB3 H 25681 -1.46 37.20 2.67 0.62 ASP HD2 H 6 1.41 12.30 5.78 3.57 ASP C C 23100 0.11 219.00 176.38 2.78 ASP CA C 31616 2.10 118.90 54.68 2.17 ASP CB C 30015 3.44 180.89 40.90 2.15 ASP CG C 622 6.71 186.50 178.27 12.54 ASP N N 34080 0.00 223.70 120.66 4.46 ASP OD1 O 20 177.59 180.97 179.66 0.91 ASN H H 25418 0.01 448.00 8.35 2.84 ASN HA H 20438 1.75 7.11 4.67 0.37 ASN HB2 H 19222 -0.64 8.74 2.81 0.33 ASN HB3 H 18438 -0.95 6.95 2.75 0.36 ASN HD21 H 14670 1.09 10.38 7.35 0.51 ASN HD22 H 14567 1.47 11.43 7.13 0.53 ASN C C 15571 0.11 184.27 175.17 4.18 ASN CA C 21657 2.20 99.00 53.53 2.02 ASN CB C 20561 1.96 99.00 38.70 2.11 ASN CG C 1583 0.00 183.10 176.40 7.35 ASN N N 22999 0.04 137.49 118.91 4.42 ASN ND2 N 12411 11.59 145.93 112.73 2.97 CYS H H 13451 3.72 12.12 8.39 0.70 CYS HA H 11845 -9.86 43.50 4.69 1.17 CYS HB2 H 11423 -39.82 363.58 3.26 8.12 CYS HB3 H 11109 -44.20 363.58 3.16 7.37 CYS HG H 136 0.25 999.00 9.41 85.50 CYS C C 6237 1.00 186.04 174.83 3.88 CYS CA C 8815 41.91 68.54 58.22 3.35 CYS CB C 8290 17.99 73.92 32.72 6.13 CYS N N 9973 -147.00 628.00 120.78 24.72 GLU H H 47049 0.00 123.45 8.34 0.89 GLU HA H 37278 0.43 31.32 4.25 0.45 GLU HB2 H 34226 -1.47 4.82 2.02 0.23 GLU HB3 H 31868 -1.63 1467.00 2.04 8.21 GLU HG2 H 31820 -0.67 4.69 2.27 0.23 GLU HG3 H 29190 -0.10 4.69 2.24 0.23 GLU HE2 H 2 2.73 11.96 7.34 6.53 GLU C C 30405 0.07 190.58 176.79 3.92 GLU CA C 41223 21.29 87.15 57.32 2.18 GLU CB C 38776 9.08 181.95 30.06 2.24 GLU CG C 27185 6.16 119.03 36.11 1.71 GLU CD C 662 36.12 189.46 181.91 6.31 GLU N N 44290 0.00 429.00 120.64 4.52 GLU OE1 O 1 184.19 184.19 184.19 0.00 GLN H H 25186 0.01 66.54 8.22 0.71 GLN HA H 20179 0.67 7.43 4.27 0.44 GLN HB2 H 18519 -1.34 5.18 2.05 0.28 GLN HB3 H 17438 -1.42 20.90 2.01 0.33 GLN HG2 H 17483 -1.76 7.50 2.31 0.29 GLN HG3 H 15921 -1.08 34.95 2.29 0.40 GLN HE21 H 13418 -3.41 111.33 7.24 1.37 GLN HE22 H 13338 1.62 113.70 7.04 1.64 GLN C C 15906 0.07 184.44 176.27 3.12 GLN CA C 21965 0.91 69.63 56.56 2.26 GLN CB C 20688 1.35 79.68 29.22 2.11 GLN CG C 14639 2.43 178.32 33.78 1.98 GLN CD C 1542 21.34 183.54 179.33 7.22 GLN N N 23427 0.08 216.50 119.84 4.16 GLN NE2 N 11855 11.96 155.00 111.85 2.42 GLY H H 45553 -15.30 128.71 8.33 1.04 GLY HA2 H 35937 -3.40 8.64 3.97 0.41 GLY HA3 H 34048 -3.40 7.58 3.89 0.42 GLY C C 28231 1.00 999.00 173.88 5.95 GLY CA C 39094 0.97 108.30 45.38 1.72 GLY N N 41453 0.00 791.00 109.86 8.72 HIS H H 13717 1.00 13.34 8.26 0.76 HIS HA H 11096 0.68 30.68 4.62 0.65 HIS HB2 H 10374 -0.05 45.90 3.20 1.33 HIS HB3 H 10045 -6.20 38.50 3.13 1.27 HIS HD1 H 686 -15.00 86.50 10.71 10.28 HIS HD2 H 7590 -25.85 67.80 7.27 4.03 HIS HE1 H 6133 -26.60 43.80 7.78 2.61 HIS HE2 H 256 -15.00 76.40 11.77 9.52 HIS C C 8341 1.00 184.20 175.18 3.73 HIS CA C 11823 11.40 176.90 56.55 2.90 HIS CB C 11159 17.80 80.78 30.29 2.43 HIS CG C 131 0.00 139.83 130.21 13.11 HIS CD2 C 4566 0.00 159.95 119.83 6.47 HIS CE1 C 3640 0.00 166.28 137.21 6.11 HIS N N 12404 1.00 159.14 119.69 4.42 HIS ND1 N 482 0.00 261.01 193.33 36.38 HIS NE2 N 457 0.00 257.57 178.65 24.01 ILE H H 32001 0.00 116.81 8.27 0.93 ILE HA H 25316 0.00 6.37 4.18 0.57 ILE HB H 23893 -2.44 38.70 1.78 0.46 ILE HG12 H 21753 -10.10 5.56 1.26 0.48 ILE HG13 H 20824 -10.10 9.71 1.19 0.52 ILE HG2 H 22782 -3.62 6.23 0.76 0.32 ILE HD1 H 22858 -4.15 8.80 0.67 0.35 ILE C C 20593 0.09 184.75 175.79 3.81 ILE CA C 27948 4.22 77.93 61.59 2.77 ILE CB C 26239 2.38 87.68 38.63 2.26 ILE CG1 C 18150 8.00 74.78 27.70 2.11 ILE CG2 C 19361 0.79 114.15 17.56 2.07 ILE CD1 C 19474 1.02 79.34 13.51 2.54 ILE N N 29788 0.05 531.00 121.48 6.31 LEU H H 52831 0.01 13.22 8.23 0.67 LEU HA H 41519 0.51 8.73 4.32 0.48 LEU HB2 H 38312 -1.52 8.02 1.61 0.37 LEU HB3 H 36446 -1.79 8.39 1.52 0.39 LEU HG H 34348 -2.08 5.70 1.50 0.35 LEU HD1 H 37635 -3.42 30.18 0.75 0.36 LEU HD2 H 36264 -3.42 24.50 0.73 0.39 LEU C C 33650 0.00 228.49 176.94 3.38 LEU CA C 45824 0.65 85.60 55.61 2.23 LEU CB C 43216 2.37 93.18 42.32 2.10 LEU CG C 28459 15.57 75.28 26.81 1.60 LEU CD1 C 31100 0.73 120.70 24.73 2.07 LEU CD2 C 29658 0.62 116.30 24.09 2.16 LEU N N 48969 0.00 627.00 122.05 10.05 LYS H H 45144 0.00 64.42 8.18 0.73 LYS HA H 35714 0.00 9.19 4.27 0.45 LYS HB2 H 32459 -1.42 35.97 1.78 0.33 LYS HB3 H 30197 -1.40 35.97 1.74 0.35 LYS HG2 H 29323 -1.45 29.88 1.36 0.32 LYS HG3 H 26567 -1.83 29.88 1.35 0.34 LYS HD2 H 26130 -1.68 119.62 1.61 0.84 LYS HD3 H 22764 -2.02 41.68 1.60 0.40 LYS HE2 H 25818 -0.49 8.37 2.91 0.22 LYS HE3 H 22013 -0.05 6.83 2.90 0.23 LYS HZ H 1087 -10.90 10.51 7.30 1.22 LYS C C 27254 0.11 999.00 176.59 8.34 LYS CA C 37613 7.01 86.72 56.92 2.28 LYS CB C 35353 -26.69 82.98 32.81 2.09 LYS CG C 23745 0.00 77.38 24.91 1.66 LYS CD C 22519 15.37 77.48 28.97 1.58 LYS CE C 21905 12.03 89.98 41.88 1.42 LYS N N 40780 0.04 1118.13 121.03 6.71 LYS NZ N 146 1.95 177.20 46.89 32.60 MET H H 12414 4.87 12.46 8.27 0.61 MET HA H 10146 -0.93 313.57 4.43 3.11 MET HB2 H 9163 -9.84 33.75 2.03 0.62 MET HB3 H 8545 -2.70 12.94 1.99 0.52 MET HG2 H 8462 -33.86 32.70 2.34 1.99 MET HG3 H 7909 -33.86 31.70 2.30 2.14 MET HE H 6103 -24.86 17.06 1.67 2.16 MET C C 8084 2.20 183.25 176.14 2.90 MET CA C 11339 36.03 85.33 56.12 2.32 MET CB C 10491 0.20 83.38 33.01 2.54 MET CG C 6914 0.00 81.18 32.02 1.81 MET CE C 5231 0.00 71.16 17.18 2.61 MET N N 11670 38.00 221.00 120.05 4.46 PHE H H 22953 0.01 12.18 8.35 0.74 PHE HA H 18042 1.45 122.00 4.63 1.13 PHE HB2 H 16939 0.16 7.98 2.99 0.39 PHE HB3 H 16468 -0.21 12.72 2.93 0.41 PHE HD1 H 14528 0.00 9.76 7.03 0.43 PHE HD2 H 11940 0.00 9.76 7.03 0.45 PHE HE1 H 12890 -2.84 14.08 7.05 0.52 PHE HE2 H 10753 0.00 12.90 7.05 0.52 PHE HZ H 9381 -7.14 130.37 7.00 1.52 PHE C C 14420 0.00 187.61 175.39 3.91 PHE CA C 19646 2.06 73.43 58.09 2.69 PHE CB C 18547 7.00 137.00 40.00 2.44 PHE CG C 227 7.00 152.84 135.54 18.25 PHE CD1 C 8238 11.74 143.45 131.34 4.21 PHE CD2 C 5718 19.15 138.70 131.42 3.66 PHE CE1 C 7257 7.90 139.56 130.46 4.11 PHE CE2 C 5049 7.90 139.70 130.55 3.67 PHE CZ C 5572 7.10 138.60 128.93 5.02 PHE N N 21162 0.07 229.00 120.42 4.73 PRO H2 H 1 8.51 8.51 8.51 0.00 PRO HA H 20607 0.00 8.51 4.39 0.36 PRO HB2 H 19375 -1.50 7.30 2.07 0.38 PRO HB3 H 18645 -3.48 6.45 1.99 0.39 PRO HG2 H 17628 -2.35 8.78 1.92 0.35 PRO HG3 H 16166 -1.52 4.92 1.89 0.36 PRO HD2 H 18149 -6.56 7.67 3.63 0.49 PRO HD3 H 17412 -6.56 6.30 3.59 0.51 PRO C C 15318 0.05 999.00 176.65 8.25 PRO CA C 22008 2.05 176.83 63.31 2.36 PRO CB C 20751 2.12 81.08 31.88 1.87 PRO CG C 14877 18.28 76.28 27.24 1.89 PRO CD C 15036 4.99 98.58 50.30 2.04 PRO N N 641 1.00 430.00 138.31 41.88 SER H H 38623 -15.30 112.72 8.28 0.82 SER HA H 31408 1.43 58.74 4.49 0.52 SER HB2 H 29020 0.61 8.02 3.87 0.28 SER HB3 H 26573 0.61 5.93 3.84 0.29 SER HG H 482 0.00 999.00 7.52 45.27 SER C C 24767 0.25 197.10 174.60 2.48 SER CA C 34152 2.86 175.20 58.70 2.25 SER CB C 31853 0.00 171.73 63.75 2.29 SER N N 35333 0.03 196.20 116.29 3.97 THR H H 34338 0.00 12.20 8.24 0.64 THR HA H 27104 -1.50 6.67 4.46 0.49 THR HB H 25112 0.00 73.47 4.18 0.91 THR HG1 H 998 0.32 11.01 5.04 1.73 THR HG2 H 24830 -12.10 22.21 1.14 0.36 THR C C 21137 60.89 185.92 174.51 2.41 THR CA C 29252 1.96 92.66 62.23 2.71 THR CB C 27294 1.06 629.21 69.62 4.38 THR CG2 C 19629 11.70 175.60 21.60 2.13 THR N N 31567 3.15 402.00 115.56 7.25 TRP H H 7775 1.79 17.32 8.29 0.80 TRP HA H 6145 2.24 11.41 4.70 0.55 TRP HB2 H 5816 0.34 5.35 3.18 0.36 TRP HB3 H 5626 0.31 7.88 3.12 0.37 TRP HD1 H 5243 4.69 127.79 7.15 1.71 TRP HE1 H 5585 -1.28 18.00 10.07 0.75 TRP HE3 H 4660 1.34 10.44 7.28 0.57 TRP HZ2 H 4979 0.96 10.81 7.26 0.46 TRP HZ3 H 4493 0.76 8.90 6.83 0.54 TRP HH2 H 4620 1.09 10.90 6.94 0.51 TRP C C 4590 57.52 184.30 176.11 2.66 TRP CA C 6265 2.19 87.02 57.66 2.75 TRP CB C 5892 1.60 112.01 30.13 2.88 TRP CG C 165 83.60 116.53 110.50 3.55 TRP CD1 C 3129 30.24 158.33 126.26 4.24 TRP CD2 C 113 120.20 139.10 127.99 1.97 TRP CE2 C 133 113.89 177.71 138.30 7.48 TRP CE3 C 2678 40.14 155.09 120.19 3.98 TRP CZ2 C 2991 6.84 144.03 113.99 4.75 TRP CZ3 C 2684 6.76 161.54 121.15 4.19 TRP CH2 C 2817 47.65 160.82 123.57 3.96 TRP N N 6865 0.00 207.70 121.67 5.02 TRP NE1 N 4408 0.53 249.50 129.26 3.78 TYR H H 19702 2.58 118.49 8.32 1.08 TYR HA H 15665 0.44 7.95 4.62 0.58 TYR HB2 H 14714 -21.23 23.28 2.90 0.51 TYR HB3 H 14350 -21.23 23.28 2.83 0.53 TYR HD1 H 12992 0.19 9.39 6.91 0.40 TYR HD2 H 10712 0.92 10.50 6.91 0.41 TYR HE1 H 12389 0.08 11.80 6.69 0.34 TYR HE2 H 10307 0.43 11.70 6.69 0.35 TYR HH H 280 3.07 31.00 9.17 2.30 TYR C C 11646 2.20 184.78 175.35 3.41 TYR CA C 16276 2.20 67.48 58.11 2.65 TYR CB C 15242 10.05 175.51 39.36 3.01 TYR CG C 215 6.80 174.59 127.33 16.15 TYR CD1 C 7434 19.59 141.57 132.43 4.79 TYR CD2 C 4882 19.59 137.80 132.43 4.57 TYR CE1 C 7380 40.44 159.57 117.68 4.06 TYR CE2 C 4833 47.30 154.10 117.76 2.98 TYR CZ C 163 6.50 162.70 152.65 24.27 TYR N N 17680 4.89 818.00 121.06 15.99 VAL H H 41932 0.00 15.05 8.28 0.69 VAL HA H 33271 -2.83 54.97 4.18 0.67 VAL HB H 31484 -27.48 31.75 1.97 0.51 VAL HG1 H 30748 -27.20 24.20 0.82 0.37 VAL HG2 H 30122 -27.20 24.20 0.80 0.39 VAL C C 26826 1.00 185.04 175.61 2.47 VAL CA C 36513 29.56 91.71 62.50 2.91 VAL CB C 34366 17.21 83.58 32.75 2.03 VAL CG1 C 25360 -7.40 117.16 21.52 2.00 VAL CG2 C 24469 -5.65 121.47 21.32 2.15 VAL N N 39210 12.39 1116.40 121.32 10.24