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 3614722 chemical shifts.
In the table, the highlighted residue codes provide a link to a gif image of the amino acid with its atom nomenclature.
Jump to amino acid: Ala Arg Asn Asp Cys Gln Glu Gly His Ile
Leu Lys Met Phe Pro Ser Thr Trp Tyr Val
Last updated: 11-04-2009
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 32799 0.95 14.80 8.19 0.62
ALA HA H 26029 -2.52 8.62 4.26 0.45
ALA HB H 24726 -14.04 5.48 1.35 0.29
ALA C C 19044 49.30 187.20 177.71 2.66
ALA CA C 26747 17.01 99.00 53.14 2.12
ALA CB C 25142 -40.99 99.00 19.05 2.28
ALA N N 29405 8.63 766.00 123.37 8.01
ARG H H 21891 0.00 861.00 8.28 5.81
ARG HA H 17787 0.00 12.57 4.30 0.49
ARG HB2 H 16089 -4.78 27.53 1.79 0.35
ARG HB3 H 14968 -1.13 27.53 1.76 0.36
ARG HG2 H 14379 -1.45 4.20 1.56 0.29
ARG HG3 H 12994 -0.91 5.47 1.54 0.30
ARG HD2 H 14062 -6.44 4.69 3.11 0.28
ARG HD3 H 12444 -0.49 4.66 3.10 0.29
ARG HE H 5397 0.00 118.45 8.82 12.46
ARG HH11 H 554 4.41 10.30 6.87 0.52
ARG HH12 H 406 4.41 10.73 6.81 0.50
ARG HH21 H 496 1.23 11.35 6.77 0.64
ARG HH22 H 394 1.23 10.18 6.74 0.65
ARG C C 12352 2.20 184.51 176.39 3.23
ARG CA C 17647 8.37 103.60 56.75 2.48
ARG CB C 16180 20.95 123.50 30.74 2.28
ARG CG C 10626 12.17 119.40 27.26 2.00
ARG CD C 10839 23.20 135.80 43.18 1.73
ARG CZ C 302 128.85 180.80 160.73 4.93
ARG N N 19081 7.83 176.86 120.79 3.95
ARG NE N 3051 7.19 149.11 90.40 19.23
ARG NH1 N 111 7.24 112.50 75.49 14.15
ARG NH2 N 95 66.20 128.47 76.77 12.40
ASP H H 25898 3.56 12.61 8.32 0.59
ASP HA H 20691 0.25 8.60 4.60 0.33
ASP HB2 H 19309 -0.39 37.40 2.73 0.71
ASP HB3 H 18314 -1.46 37.20 2.68 0.72
ASP HD2 H 2 1.41 12.30 6.85 7.70
ASP C C 15446 52.77 219.00 176.42 2.15
ASP CA C 21594 36.57 86.07 54.68 2.13
ASP CB C 20241 9.70 180.89 40.92 2.32
ASP CG C 463 27.50 183.94 178.59 10.26
ASP N N 23579 8.49 223.70 120.75 4.27
ASN H H 18144 2.61 448.00 8.37 3.33
ASN HA H 14829 1.75 7.11 4.67 0.38
ASN HB2 H 13897 -0.64 5.58 2.81 0.33
ASN HB3 H 13263 -0.69 5.14 2.75 0.36
ASN HD21 H 10302 2.06 10.24 7.36 0.50
ASN HD22 H 10227 3.00 11.43 7.13 0.52
ASN C C 10393 2.20 184.27 175.26 2.64
ASN CA C 14781 2.20 99.00 53.53 2.06
ASN CB C 13824 1.96 99.00 38.73 2.23
ASN CG C 1154 27.61 181.20 176.54 5.31
ASN N N 15925 101.71 137.49 118.99 4.10
ASN ND2 N 8291 32.20 133.86 112.79 2.83
CYS H H 10096 3.72 12.12 8.40 0.70
CYS HA H 9007 -9.86 43.50 4.73 1.29
CYS HB2 H 8652 -39.82 363.58 3.23 6.97
CYS HB3 H 8413 -44.20 363.58 3.15 6.43
CYS HG H 94 0.25 10.70 2.14 1.77
CYS C C 4106 1.00 186.04 174.74 4.53
CYS CA C 5923 41.91 68.54 58.04 3.37
CYS CB C 5457 17.99 73.92 33.25 6.44
CYS N N 6974 -147.00 628.00 121.14 29.40
GLU H H 33676 4.24 64.68 8.34 0.74
GLU HA H 27077 1.09 31.32 4.26 0.45
GLU HB2 H 24659 -1.47 4.82 2.02 0.23
GLU HB3 H 22694 -1.63 3.76 2.00 0.23
GLU HG2 H 22808 -0.67 4.69 2.27 0.23
GLU HG3 H 20616 -0.10 4.69 2.25 0.23
GLU HE2 H 2 2.73 11.96 7.34 6.53
GLU C C 20632 1.00 190.58 176.86 3.13
GLU CA C 28569 21.29 87.15 57.33 2.21
GLU CB C 26520 9.08 181.95 30.07 2.38
GLU CG C 18466 6.16 119.03 36.12 1.90
GLU CD C 512 0.00 189.46 181.50 10.73
GLU N N 31056 0.00 429.00 120.70 4.40
GLN H H 17697 4.24 13.17 8.22 0.61
GLN HA H 14358 1.60 7.43 4.28 0.45
GLN HB2 H 13054 -1.34 5.18 2.05 0.28
GLN HB3 H 12143 -1.42 20.90 2.02 0.34
GLN HG2 H 12244 -1.76 7.50 2.31 0.29
GLN HG3 H 10972 -1.08 34.95 2.30 0.44
GLN HE21 H 9116 2.21 111.33 7.25 1.61
GLN HE22 H 9062 2.10 113.70 7.05 1.97
GLN C C 10510 7.24 184.44 176.31 2.62
GLN CA C 14891 4.10 69.63 56.57 2.22
GLN CB C 13822 20.27 79.68 29.22 2.08
GLN CG C 9658 2.43 178.32 33.80 2.29
GLN CD C 1103 171.70 183.54 179.63 1.43
GLN N N 16102 82.60 216.50 119.87 3.81
GLN NE2 N 7783 11.96 155.00 111.84 2.69
GLY H H 32457 -15.30 128.71 8.33 1.17
GLY HA2 H 25806 -3.40 8.64 3.97 0.41
GLY HA3 H 24373 -3.40 7.58 3.89 0.44
GLY C C 18630 1.00 187.28 173.87 3.69
GLY CA C 26447 2.20 108.30 45.38 1.76
GLY N N 28632 8.65 791.00 110.00 10.11
HIS H H 9892 1.00 13.34 8.26 0.77
HIS HA H 8049 0.68 30.68 4.63 0.69
HIS HB2 H 7500 -0.05 45.90 3.23 1.52
HIS HB3 H 7263 -6.20 38.50 3.15 1.42
HIS HD1 H 565 -15.00 86.50 11.25 11.21
HIS HD2 H 5447 -25.85 67.80 7.40 4.72
HIS HE1 H 4489 -26.60 43.80 7.78 3.00
HIS HE2 H 231 -15.00 76.40 12.07 9.96
HIS C C 5693 1.00 184.20 175.18 4.02
HIS CA C 8212 11.40 118.60 56.53 2.81
HIS CB C 7656 17.80 80.78 30.27 2.49
HIS CG C 105 71.30 139.83 131.11 6.97
HIS CD2 C 2899 7.19 159.95 119.86 6.29
HIS CE1 C 2311 8.27 166.28 137.00 6.07
HIS N N 8733 1.00 159.14 119.65 4.62
HIS ND1 N 374 64.90 256.60 192.35 35.02
HIS NE2 N 367 8.40 253.92 179.13 23.41
ILE H H 22705 0.00 11.69 8.28 0.71
ILE HA H 18273 0.00 6.37 4.19 0.58
ILE HB H 17143 -2.44 38.70 1.79 0.50
ILE HG12 H 15503 -10.10 5.56 1.26 0.51
ILE HG13 H 14663 -10.10 9.71 1.20 0.56
ILE HG2 H 16313 -3.62 6.23 0.77 0.34
ILE HD1 H 16263 -4.15 8.80 0.67 0.37
ILE C C 13738 1.00 184.75 175.79 3.75
ILE CA C 19105 30.90 77.93 61.58 2.73
ILE CB C 17728 20.94 87.68 38.66 2.34
ILE CG1 C 12213 8.00 74.78 27.71 2.28
ILE CG2 C 13111 0.79 114.15 17.59 2.34
ILE CD1 C 13117 1.02 79.34 13.59 2.87
ILE N N 20639 36.90 531.00 121.59 6.70
LEU H H 37322 0.09 13.22 8.23 0.67
LEU HA H 29880 0.51 8.73 4.32 0.48
LEU HB2 H 27274 -1.52 8.02 1.62 0.37
LEU HB3 H 25769 -1.79 8.39 1.53 0.38
LEU HG H 24413 -2.08 5.70 1.51 0.35
LEU HD1 H 26759 -3.42 30.18 0.75 0.38
LEU HD2 H 25671 -3.42 23.45 0.73 0.40
LEU C C 22377 22.96 228.49 176.97 2.35
LEU CA C 31198 14.37 85.60 55.61 2.25
LEU CB C 29087 16.38 93.18 42.33 2.12
LEU CG C 18995 15.57 75.28 26.83 1.78
LEU CD1 C 20904 0.73 120.70 24.73 2.27
LEU CD2 C 19807 6.00 116.30 24.15 2.34
LEU N N 33777 8.24 627.00 122.20 11.67
LYS H H 32918 0.00 58.72 8.19 0.69
LYS HA H 26412 0.00 8.60 4.27 0.46
LYS HB2 H 23813 -1.42 35.97 1.78 0.35
LYS HB3 H 21949 -1.40 35.97 1.75 0.37
LYS HG2 H 21286 -1.45 29.88 1.37 0.34
LYS HG3 H 19057 -1.83 29.88 1.35 0.36
LYS HD2 H 18751 -1.68 119.62 1.62 0.98
LYS HD3 H 16117 -2.02 41.68 1.60 0.45
LYS HE2 H 18479 -0.49 8.37 2.91 0.22
LYS HE3 H 15575 -0.05 6.83 2.91 0.22
LYS HZ H 963 -10.90 9.90 7.29 1.23
LYS C C 18432 32.87 996.25 176.66 6.60
LYS CA C 26125 22.02 86.72 56.92 2.29
LYS CB C 24219 -26.69 82.98 32.82 2.14
LYS CG C 16220 0.00 77.38 24.95 1.81
LYS CD C 15386 15.37 77.48 28.98 1.74
LYS CE C 14862 12.03 89.98 41.90 1.52
LYS N N 28902 8.10 1118.13 121.13 7.21
LYS NZ N 95 1.95 132.80 49.98 34.90
MET H H 8796 4.87 12.46 8.26 0.61
MET HA H 7310 -0.93 313.57 4.45 3.65
MET HB2 H 6575 -9.84 33.75 2.03 0.69
MET HB3 H 6093 -2.70 12.94 2.01 0.58
MET HG2 H 6033 -33.86 32.70 2.31 2.34
MET HG3 H 5608 -33.86 31.70 2.27 2.53
MET HE H 4112 -24.86 17.06 1.57 2.60
MET C C 5455 2.20 183.16 176.14 3.21
MET CA C 7805 36.03 85.33 56.14 2.35
MET CB C 7110 0.20 83.38 33.05 2.58
MET CG C 4634 2.30 81.18 32.05 1.89
MET CE C 3301 0.00 71.16 17.28 3.03
MET N N 8098 38.00 221.00 120.09 4.53
PHE H H 16443 4.06 12.18 8.36 0.73
PHE HA H 13100 1.45 122.00 4.64 1.27
PHE HB2 H 12237 0.17 7.98 2.99 0.39
PHE HB3 H 11873 0.09 12.72 2.94 0.41
PHE HD1 H 10468 0.00 9.76 7.02 0.47
PHE HD2 H 8230 0.00 9.76 7.02 0.49
PHE HE1 H 9325 0.00 14.08 7.05 0.54
PHE HE2 H 7475 0.00 12.90 7.04 0.57
PHE HZ H 6662 -7.14 130.37 7.01 1.77
PHE C C 9649 124.30 187.61 175.44 2.20
PHE CA C 13506 4.92 73.43 58.06 2.67
PHE CB C 12623 21.40 137.00 40.01 2.54
PHE CG C 156 7.00 152.84 134.61 19.89
PHE CD1 C 5217 11.74 143.45 131.30 4.48
PHE CD2 C 3237 19.15 138.70 131.34 4.36
PHE CE1 C 4535 7.90 135.60 130.40 4.45
PHE CE2 C 2807 7.90 139.70 130.45 4.63
PHE CZ C 3352 7.10 138.60 128.80 6.20
PHE N N 14748 102.20 229.00 120.53 4.41
PRO H2 H 1 8.51 8.51 8.51 0.00
PRO HA H 14482 0.00 8.51 4.39 0.37
PRO HB2 H 13556 -0.78 5.25 2.07 0.38
PRO HB3 H 12917 -3.48 6.10 2.00 0.40
PRO HG2 H 12199 -2.35 4.92 1.92 0.35
PRO HG3 H 11122 -1.35 4.92 1.90 0.37
PRO HD2 H 12581 -6.56 7.67 3.62 0.53
PRO HD3 H 12046 -6.56 6.30 3.59 0.54
PRO C C 10065 3.19 183.52 176.62 3.68
PRO CA C 14713 26.45 176.83 63.33 2.59
PRO CB C 13706 24.08 81.08 31.91 2.07
PRO CG C 9614 18.28 76.28 27.28 2.19
PRO CD C 9740 4.99 98.58 50.31 2.38
PRO N N 438 31.27 430.00 142.26 48.58
SER H H 27071 -15.30 13.13 8.28 0.63
SER HA H 22193 1.43 58.74 4.49 0.56
SER HB2 H 20294 0.61 5.70 3.87 0.28
SER HB3 H 18456 0.61 5.52 3.84 0.30
SER HG H 388 0.00 999.00 8.02 50.46
SER C C 16007 128.34 197.10 174.66 2.00
SER CA C 22796 24.40 89.55 58.72 2.16
SER CB C 20939 0.00 171.73 63.80 1.98
SER N N 24041 1.68 196.20 116.33 3.93
THR H H 24598 0.00 12.20 8.25 0.65
THR HA H 19781 -1.50 6.67 4.46 0.49
THR HB H 18200 0.00 73.47 4.18 1.05
THR HG1 H 736 0.32 11.01 5.12 1.73
THR HG2 H 18015 -12.10 22.21 1.14 0.39
THR C C 14085 60.89 185.92 174.52 2.51
THR CA C 20056 41.95 92.66 62.22 2.68
THR CB C 18493 1.06 629.21 69.65 4.84
THR CG2 C 13201 11.70 108.98 21.61 2.09
THR N N 21949 6.83 402.00 115.69 7.98
TRP H H 5541 4.49 11.67 8.30 0.80
TRP HA H 4420 2.28 7.05 4.70 0.54
TRP HB2 H 4160 0.42 5.35 3.18 0.36
TRP HB3 H 3999 0.55 4.49 3.13 0.37
TRP HD1 H 3729 4.69 127.79 7.17 2.01
TRP HE1 H 3995 -1.28 18.00 10.10 0.67
TRP HE3 H 3355 1.85 10.44 7.29 0.59
TRP HZ2 H 3566 2.63 10.81 7.26 0.49
TRP HZ3 H 3227 0.76 8.90 6.83 0.57
TRP HH2 H 3316 2.84 10.90 6.94 0.55
TRP C C 2962 57.52 181.89 176.08 2.96
TRP CA C 4206 33.74 87.02 57.63 2.69
TRP CB C 3916 1.60 112.01 30.16 3.16
TRP CG C 136 83.60 116.53 110.28 3.78
TRP CD1 C 1929 30.24 158.33 126.23 4.29
TRP CD2 C 96 120.20 131.20 127.68 1.57
TRP CE2 C 113 118.37 177.71 138.21 7.16
TRP CE3 C 1651 40.14 155.09 120.24 4.08
TRP CZ2 C 1838 6.84 144.03 113.98 4.84
TRP CZ3 C 1659 6.76 161.54 121.19 4.43
TRP CH2 C 1730 47.65 160.82 123.51 4.17
TRP N N 4688 25.80 207.70 121.76 4.75
TRP NE1 N 2947 0.53 249.50 129.37 4.18
TYR H H 14048 2.58 11.98 8.32 0.75
TYR HA H 11295 0.44 6.83 4.63 0.57
TYR HB2 H 10566 -21.23 23.28 2.90 0.49
TYR HB3 H 10280 -21.23 23.28 2.85 0.51
TYR HD1 H 9465 0.19 9.39 6.91 0.42
TYR HD2 H 7492 0.92 10.50 6.91 0.45
TYR HE1 H 9070 0.08 121.90 6.70 1.26
TYR HE2 H 7244 0.43 121.90 6.70 1.41
TYR HH H 220 3.07 31.00 9.27 2.47
TYR C C 7628 2.20 183.93 175.32 3.65
TYR CA C 10961 2.20 65.99 58.09 2.68
TYR CB C 10127 28.82 175.51 39.38 3.01
TYR CG C 154 6.80 174.59 126.44 19.01
TYR CD1 C 4758 19.59 138.70 132.37 5.29
TYR CD2 C 2772 19.59 137.80 132.26 5.79
TYR CE1 C 4710 40.44 159.57 117.67 4.38
TYR CE2 C 2756 51.50 154.10 117.73 3.59
TYR CZ C 127 6.50 162.70 151.18 27.34
TYR N N 12147 100.09 818.00 121.43 19.06
VAL H H 29636 0.00 15.05 8.29 0.70
VAL HA H 23935 -2.83 54.97 4.19 0.70
VAL HB H 22535 -27.48 31.75 1.98 0.50
VAL HG1 H 21950 -27.20 24.20 0.82 0.40
VAL HG2 H 21388 -27.20 24.20 0.80 0.41
VAL C C 17776 44.78 185.04 175.63 2.37
VAL CA C 24831 29.56 91.71 62.45 2.92
VAL CB C 23074 20.24 83.58 32.77 2.10
VAL CG1 C 17006 -7.40 117.16 21.54 2.24
VAL CG2 C 16276 -5.65 121.47 21.36 2.37
VAL N N 27038 12.39 1116.40 121.45 11.97
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