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 2716048 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: 04-23-2008
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 25720 0.95 14.80 8.19 0.63
ALA HA H 20393 -2.52 8.62 4.25 0.45
ALA HB H 19162 -2.29 5.48 1.36 0.28
ALA C C 14325 49.30 187.20 177.73 2.64
ALA CA C 20326 17.29 99.00 53.18 2.09
ALA CB C 18940 -40.99 99.00 19.01 2.37
ALA N N 22703 8.63 766.00 123.34 8.92
ARG H H 16949 0.00 12.73 8.24 0.65
ARG HA H 13649 0.00 12.57 4.29 0.48
ARG HB2 H 12139 -4.78 4.77 1.80 0.29
ARG HB3 H 11129 -1.13 3.64 1.77 0.29
ARG HG2 H 10669 -1.45 4.20 1.57 0.29
ARG HG3 H 9473 -0.91 5.47 1.55 0.30
ARG HD2 H 10370 -6.44 4.69 3.11 0.28
ARG HD3 H 9012 -0.49 4.66 3.10 0.29
ARG HE H 4174 0.00 118.45 9.24 14.14
ARG HH11 H 439 4.41 10.30 6.88 0.53
ARG HH12 H 318 4.41 10.73 6.83 0.52
ARG HH21 H 393 3.87 9.70 6.79 0.50
ARG HH22 H 313 3.87 10.18 6.78 0.58
ARG C C 9053 2.20 184.51 176.40 3.59
ARG CA C 13171 8.37 70.69 56.80 2.48
ARG CB C 11897 20.95 82.18 30.69 2.28
ARG CG C 7320 12.17 76.58 27.26 1.96
ARG CD C 7507 23.20 91.28 43.17 1.68
ARG CZ C 180 128.85 177.70 159.76 3.85
ARG N N 14423 67.14 176.86 120.78 3.87
ARG NE N 2146 7.19 145.60 89.93 21.03
ARG NH1 N 86 7.41 112.50 74.61 11.76
ARG NH2 N 75 66.20 123.30 76.38 11.16
ASP H H 20187 3.56 12.61 8.32 0.59
ASP HA H 16139 0.25 8.60 4.60 0.33
ASP HB2 H 14853 -0.39 37.40 2.74 0.79
ASP HB3 H 14011 -1.46 37.20 2.69 0.80
ASP HD2 H 1 12.30 12.30 12.30 0.00
ASP C C 11603 52.77 219.00 176.43 2.28
ASP CA C 16378 39.80 68.47 54.67 2.11
ASP CB C 15175 9.70 180.89 40.88 2.45
ASP CG C 387 27.50 183.94 178.41 11.20
ASP N N 18059 8.49 223.70 120.76 4.33
ASN H H 14269 2.61 448.00 8.38 3.74
ASN HA H 11613 1.75 7.11 4.67 0.38
ASN HB2 H 10788 -0.64 5.58 2.81 0.34
ASN HB3 H 10276 -0.69 5.14 2.76 0.37
ASN HD21 H 7760 2.06 10.10 7.35 0.51
ASN HD22 H 7699 2.20 11.43 7.14 0.53
ASN C C 7790 2.20 184.22 175.28 2.88
ASN CA C 11233 2.20 99.00 53.53 2.08
ASN CB C 10404 1.96 99.00 38.72 2.38
ASN CG C 887 27.61 181.20 176.46 6.01
ASN N N 12239 103.70 137.49 119.01 4.12
ASN ND2 N 5952 32.20 133.86 112.78 3.05
CYS H H 8178 3.72 12.12 8.40 0.70
CYS HA H 7285 -2.78 43.50 4.75 1.40
CYS HB2 H 6956 -39.82 134.60 3.14 3.55
CYS HB3 H 6743 -44.20 125.00 3.08 3.72
CYS HG H 81 0.25 10.70 2.22 1.89
CYS C C 2945 2.20 184.37 174.70 4.08
CYS CA C 4331 41.91 68.54 57.95 3.41
CYS CB C 3913 19.12 73.92 33.36 6.52
CYS N N 5246 -147.00 628.00 121.44 33.79
GLU H H 25977 4.31 64.68 8.34 0.77
GLU HA H 20868 1.77 31.32 4.25 0.46
GLU HB2 H 18686 -0.22 4.82 2.03 0.23
GLU HB3 H 17003 -0.79 3.76 2.01 0.23
GLU HG2 H 17040 0.00 4.69 2.28 0.23
GLU HG3 H 15214 -0.10 4.69 2.26 0.23
GLU HE2 H 1 11.96 11.96 11.96 0.00
GLU C C 15275 8.22 190.58 176.89 3.17
GLU CA C 21408 28.80 82.05 57.37 2.19
GLU CB C 19614 9.08 181.95 30.04 2.57
GLU CG C 13152 6.16 119.03 36.09 2.12
GLU CD C 426 0.00 189.46 181.20 11.73
GLU N N 23579 0.00 429.00 120.69 4.65
GLN H H 13782 4.24 13.17 8.21 0.61
GLN HA H 11191 1.60 7.43 4.27 0.44
GLN HB2 H 10011 -1.34 5.18 2.05 0.28
GLN HB3 H 9220 -1.42 20.90 2.02 0.36
GLN HG2 H 9283 -1.76 3.66 2.31 0.29
GLN HG3 H 8204 -1.08 34.95 2.30 0.48
GLN HE21 H 6707 2.21 111.33 7.24 1.86
GLN HE22 H 6663 2.10 113.70 7.07 2.28
GLN C C 7830 7.24 184.44 176.32 2.82
GLN CA C 11275 4.10 69.63 56.55 2.24
GLN CB C 10354 20.27 79.68 29.18 2.16
GLN CG C 6925 2.43 125.57 33.76 1.98
GLN CD C 879 171.70 183.54 179.58 1.52
GLN N N 12318 82.60 216.50 119.87 3.84
GLN NE2 N 5511 11.96 155.00 111.78 3.00
GLY H H 25007 -15.30 128.71 8.34 1.28
GLY HA2 H 19825 -3.40 8.64 3.97 0.42
GLY HA3 H 18577 -3.40 7.58 3.89 0.45
GLY C C 13489 2.20 187.28 173.88 3.90
GLY CA C 19449 2.20 108.30 45.37 1.87
GLY N N 21550 8.65 791.00 110.08 11.41
HIS H H 7643 4.45 13.34 8.27 0.78
HIS HA H 6128 0.68 11.38 4.64 0.67
HIS HB2 H 5617 -0.05 45.90 3.27 1.73
HIS HB3 H 5394 -6.20 38.50 3.19 1.62
HIS HD1 H 490 -15.00 86.50 11.68 11.96
HIS HD2 H 4003 -25.85 67.80 7.56 5.48
HIS HE1 H 3312 -26.60 43.80 7.73 3.46
HIS HE2 H 190 -15.00 76.40 12.57 10.89
HIS C C 4171 2.20 183.83 175.17 3.66
HIS CA C 6068 23.91 118.60 56.51 2.79
HIS CB C 5609 17.80 80.78 30.25 2.56
HIS CG C 88 71.30 139.83 130.91 7.51
HIS CD2 C 1790 7.19 159.95 119.30 7.34
HIS CE1 C 1336 8.27 144.54 136.43 7.51
HIS N N 6602 105.00 137.80 119.62 4.18
HIS ND1 N 291 64.90 256.60 191.32 34.99
HIS NE2 N 282 8.40 249.96 178.06 24.34
ILE H H 17651 0.00 11.69 8.27 0.72
ILE HA H 14188 0.00 6.37 4.18 0.58
ILE HB H 13132 -2.44 38.70 1.79 0.55
ILE HG12 H 11713 -10.10 5.56 1.26 0.54
ILE HG13 H 11002 -10.10 9.71 1.21 0.60
ILE HG2 H 12429 -3.62 6.23 0.77 0.35
ILE HD1 H 12346 -4.15 8.80 0.67 0.39
ILE C C 10293 130.51 184.03 175.84 2.11
ILE CA C 14500 30.90 77.93 61.55 2.74
ILE CB C 13292 20.94 87.68 38.65 2.45
ILE CG1 C 8713 8.00 74.78 27.67 2.48
ILE CG2 C 9448 0.79 83.57 17.61 2.43
ILE CD1 C 9476 1.02 78.64 13.60 3.03
ILE N N 15766 36.90 531.00 121.61 7.30
LEU H H 28798 0.09 13.22 8.22 0.68
LEU HA H 22854 0.51 8.73 4.31 0.48
LEU HB2 H 20501 -1.52 8.02 1.62 0.38
LEU HB3 H 19195 -1.79 8.39 1.54 0.39
LEU HG H 18174 -2.08 5.70 1.50 0.36
LEU HD1 H 20042 -3.42 7.50 0.75 0.35
LEU HD2 H 19139 -3.42 22.11 0.73 0.39
LEU C C 16655 22.96 228.49 176.98 2.48
LEU CA C 23467 44.60 85.60 55.64 2.17
LEU CB C 21617 16.38 93.18 42.28 2.19
LEU CG C 13324 15.57 75.28 26.78 1.89
LEU CD1 C 14881 0.73 73.88 24.66 2.27
LEU CD2 C 14011 6.00 73.48 24.12 2.30
LEU N N 25721 8.24 627.00 122.25 13.18
LYS H H 25818 0.00 12.62 8.18 0.63
LYS HA H 20505 0.00 8.60 4.27 0.46
LYS HB2 H 18186 -0.84 10.94 1.78 0.28
LYS HB3 H 16582 -0.97 9.43 1.76 0.29
LYS HG2 H 15986 -1.45 6.70 1.38 0.28
LYS HG3 H 14061 -1.83 4.18 1.36 0.30
LYS HD2 H 13899 -1.68 119.62 1.62 1.08
LYS HD3 H 11699 -2.02 29.05 1.60 0.36
LYS HE2 H 13584 -0.49 8.37 2.92 0.23
LYS HE3 H 11218 -0.05 6.83 2.91 0.23
LYS HZ H 857 -10.90 9.90 7.30 1.26
LYS C C 13658 32.87 996.25 176.72 7.45
LYS CA C 19691 43.10 82.05 56.95 2.24
LYS CB C 18017 -26.69 82.98 32.78 2.24
LYS CG C 11406 0.00 77.38 24.95 1.96
LYS CD C 10746 20.62 77.48 28.96 1.95
LYS CE C 10315 12.03 89.98 41.88 1.72
LYS N N 22164 101.10 217.00 121.04 4.17
LYS NZ N 71 1.95 132.80 48.50 34.58
MET H H 6893 4.87 11.89 8.26 0.62
MET HA H 5715 -0.93 313.57 4.45 4.12
MET HB2 H 5046 -9.84 33.75 2.04 0.77
MET HB3 H 4642 -2.70 12.94 2.01 0.63
MET HG2 H 4594 -33.86 32.70 2.28 2.67
MET HG3 H 4232 -33.86 31.70 2.24 2.90
MET HE H 3040 -24.86 17.06 1.46 3.01
MET C C 4074 2.20 183.16 176.16 3.51
MET CA C 5925 45.50 72.49 56.15 2.32
MET CB C 5337 0.20 83.38 33.03 2.65
MET CG C 3348 2.30 81.18 32.05 1.99
MET CE C 2293 0.00 68.10 17.33 3.07
MET N N 6232 38.95 221.00 120.03 4.67
PHE H H 12776 4.06 12.03 8.36 0.74
PHE HA H 10115 1.45 122.00 4.63 1.42
PHE HB2 H 9355 0.17 7.98 2.99 0.40
PHE HB3 H 9009 0.30 12.72 2.94 0.41
PHE HD1 H 7921 2.02 8.70 7.01 0.50
PHE HD2 H 6066 2.02 8.70 7.01 0.54
PHE HE1 H 7013 0.74 12.90 7.04 0.58
PHE HE2 H 5483 0.84 12.90 7.04 0.62
PHE HZ H 5023 -7.14 43.62 7.01 1.02
PHE C C 7157 124.30 187.61 175.51 2.27
PHE CA C 10192 4.92 73.43 58.11 2.71
PHE CB C 9427 21.40 88.78 39.96 2.49
PHE CG C 101 36.75 141.50 136.28 10.50
PHE CD1 C 3374 19.15 138.12 131.10 5.10
PHE CD2 C 2002 19.15 137.20 131.05 5.47
PHE CE1 C 2837 7.90 135.60 130.19 5.53
PHE CE2 C 1662 7.90 134.50 130.21 5.91
PHE CZ C 2049 9.28 138.60 128.75 5.74
PHE N N 11273 102.20 229.00 120.59 4.51
PRO H2 H 1 8.51 8.51 8.51 0.00
PRO HA H 10995 0.00 8.51 4.39 0.38
PRO HB2 H 10106 -0.78 5.25 2.06 0.39
PRO HB3 H 9574 -3.48 6.10 2.01 0.41
PRO HG2 H 8940 -2.35 4.92 1.92 0.37
PRO HG3 H 8040 -1.29 4.92 1.90 0.38
PRO HD2 H 9271 -6.56 7.67 3.62 0.58
PRO HD3 H 8791 -6.56 6.30 3.59 0.58
PRO C C 7504 117.05 182.30 176.66 2.23
PRO CA C 10866 26.45 73.44 63.29 1.83
PRO CB C 9949 25.44 81.08 31.89 2.22
PRO CG C 6545 19.31 76.28 27.31 2.46
PRO CD C 6666 4.99 98.58 50.32 2.67
PRO N N 325 31.27 430.00 146.24 54.47
SER H H 20752 -15.30 13.13 8.28 0.65
SER HA H 16822 1.43 7.37 4.49 0.43
SER HB2 H 15163 0.61 5.70 3.87 0.29
SER HB3 H 13630 0.61 5.52 3.85 0.31
SER HG H 303 0.00 999.00 8.73 57.09
SER C C 11502 128.34 197.10 174.65 2.12
SER CA C 16776 24.40 76.07 58.70 2.19
SER CB C 15173 0.00 171.73 63.78 2.10
SER N N 18011 1.68 196.20 116.29 4.06
THR H H 19068 0.00 12.20 8.25 0.65
THR HA H 15338 -1.50 6.67 4.46 0.50
THR HB H 13935 0.00 68.14 4.17 0.85
THR HG1 H 540 0.32 11.01 5.30 1.63
THR HG2 H 13794 -12.10 16.30 1.14 0.34
THR C C 10376 60.89 185.33 174.51 2.74
THR CA C 15012 50.94 82.16 62.20 2.69
THR CB C 13653 7.00 629.21 69.63 5.42
THR CG2 C 9465 11.70 108.98 21.59 2.31
THR N N 16700 6.83 402.00 115.76 8.76
TRP H H 4333 4.49 11.67 8.29 0.80
TRP HA H 3435 2.28 7.05 4.70 0.55
TRP HB2 H 3205 0.42 5.35 3.18 0.36
TRP HB3 H 3076 0.55 4.49 3.13 0.38
TRP HD1 H 2869 4.69 8.93 7.13 0.36
TRP HE1 H 3087 5.00 18.00 10.11 0.65
TRP HE3 H 2566 1.85 10.09 7.28 0.63
TRP HZ2 H 2746 2.63 10.81 7.25 0.53
TRP HZ3 H 2514 0.76 8.90 6.82 0.61
TRP HH2 H 2556 2.84 10.90 6.93 0.59
TRP C C 2253 57.52 181.89 176.06 3.19
TRP CA C 3193 33.74 69.76 57.63 2.62
TRP CB C 2947 1.60 112.01 30.14 3.40
TRP CG C 120 83.60 114.60 109.94 3.86
TRP CD1 C 1319 30.24 136.11 126.10 4.93
TRP CD2 C 89 120.20 131.20 127.61 1.56
TRP CE2 C 99 118.37 177.71 137.80 6.86
TRP CE3 C 1095 40.14 138.50 120.07 4.76
TRP CZ2 C 1244 6.84 134.70 113.77 5.72
TRP CZ3 C 1112 6.76 138.39 121.03 5.17
TRP CH2 C 1163 47.65 133.10 123.23 4.87
TRP N N 3604 25.80 207.70 121.81 4.91
TRP NE1 N 2188 0.53 249.50 129.39 4.58
TYR H H 11084 4.39 11.96 8.32 0.75
TYR HA H 8859 1.20 6.83 4.62 0.57
TYR HB2 H 8234 0.30 23.28 2.91 0.45
TYR HB3 H 7954 -0.19 23.28 2.86 0.46
TYR HD1 H 7384 0.73 9.39 6.91 0.44
TYR HD2 H 5723 0.92 10.50 6.90 0.48
TYR HE1 H 7059 0.08 11.80 6.69 0.39
TYR HE2 H 5508 0.43 11.70 6.68 0.43
TYR HH H 184 3.07 31.00 9.19 2.62
TYR C C 5651 2.20 182.92 175.35 4.06
TYR CA C 8307 2.20 65.80 58.10 2.68
TYR CB C 7570 28.82 175.51 39.36 3.25
TYR CG C 123 36.60 138.70 128.30 8.77
TYR CD1 C 3219 19.59 138.70 132.16 6.38
TYR CD2 C 1808 19.59 137.80 131.95 7.09
TYR CE1 C 3166 40.44 159.57 117.53 5.26
TYR CE2 C 1788 51.50 154.10 117.59 4.33
TYR CZ C 101 31.30 162.70 154.03 17.24
TYR N N 9356 100.09 818.00 121.66 21.60
VAL H H 22786 0.00 11.81 8.28 0.71
VAL HA H 18374 -2.83 54.97 4.18 0.72
VAL HB H 17072 -18.50 31.75 1.98 0.44
VAL HG1 H 16632 -27.20 24.20 0.83 0.42
VAL HG2 H 16133 -27.20 24.20 0.80 0.44
VAL C C 12972 130.51 185.04 175.64 2.24
VAL CA C 18454 43.00 78.44 62.45 2.91
VAL CB C 16936 20.24 83.58 32.73 2.18
VAL CG1 C 12051 7.97 117.16 21.55 2.47
VAL CG2 C 11483 -5.65 121.47 21.38 2.61
VAL N N 20383 12.39 529.00 121.49 11.61
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