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 5995331 possible chemical shifts in the BMRB database, 4383107 were included in calculating this table.
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: 08-08-2013
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 39532 3.53 12.11 8.19 0.60
ALA HA H 29268 0.87 6.51 4.25 0.43
ALA HB H 27808 -0.88 3.12 1.36 0.25
ALA C C 25352 164.48 187.20 177.79 2.13
ALA CA C 34362 44.22 65.52 53.20 1.97
ALA CB C 32563 9.79 28.80 18.98 1.79
ALA N N 36966 98.05 142.81 123.21 3.50
ARG H H 26668 3.57 12.69 8.24 0.61
ARG HA H 20386 1.34 6.52 4.29 0.46
ARG HB2 H 18440 -0.76 3.49 1.79 0.27
ARG HB3 H 17400 -0.86 3.32 1.76 0.28
ARG HG2 H 16545 -0.64 3.51 1.57 0.27
ARG HG3 H 15176 -0.74 3.51 1.54 0.29
ARG HD2 H 16217 1.04 4.69 3.12 0.24
ARG HD3 H 14682 0.89 4.56 3.10 0.25
ARG HE H 5016 2.99 11.88 7.39 0.63
ARG HH11 H 449 5.88 9.82 6.90 0.45
ARG HH12 H 326 5.92 10.73 6.82 0.40
ARG HH21 H 397 4.85 11.35 6.80 0.47
ARG HH22 H 308 5.92 10.18 6.78 0.39
ARG C C 16243 167.44 184.51 176.46 2.03
ARG CA C 22574 43.27 67.98 56.81 2.31
ARG CB C 20997 20.95 42.50 30.65 1.83
ARG CG C 13438 18.22 39.98 27.21 1.18
ARG CD C 13586 35.05 50.88 43.16 0.89
ARG CZ C 335 156.49 179.69 160.11 3.00
ARG N N 24183 102.78 137.60 120.76 3.66
ARG NE N 2856 67.00 99.81 84.60 1.63
ARG NH1 N 79 67.60 87.79 73.90 4.90
ARG NH2 N 71 69.90 85.28 72.88 3.03
ASP H H 31480 4.06 12.68 8.30 0.57
ASP HA H 23380 2.33 6.33 4.59 0.32
ASP HB2 H 21800 -0.39 4.58 2.72 0.26
ASP HB3 H 20874 -0.23 4.58 2.66 0.27
ASP HD2 H 2 4.65 9.29 6.97 3.28
ASP C C 20109 166.80 182.70 176.44 1.75
ASP CA C 27395 41.11 67.17 54.71 2.04
ASP CB C 25897 27.48 54.95 40.87 1.62
ASP CG C 403 170.72 186.50 179.31 1.83
ASP N N 29657 101.90 143.52 120.63 3.82
ASN H H 22123 2.61 12.40 8.33 0.62
ASN HA H 16921 1.92 6.43 4.66 0.36
ASN HB2 H 15833 0.18 4.47 2.81 0.32
ASN HB3 H 15201 -0.07 4.47 2.75 0.33
ASN HD21 H 11882 3.55 10.38 7.33 0.48
ASN HD22 H 11688 3.05 10.80 7.14 0.49
ASN C C 13728 167.04 185.30 175.29 1.80
ASN CA C 19008 44.78 66.21 53.57 1.89
ASN CB C 18009 26.45 48.78 38.69 1.67
ASN CG C 1297 166.40 183.10 176.76 1.41
ASN N N 20231 101.71 137.49 118.89 3.99
ASN ND2 N 10030 99.40 134.50 112.77 2.33
CYS H H 11511 4.73 12.12 8.38 0.67
CYS HA H 9896 1.64 6.45 4.64 0.55
CYS HB2 H 9524 -0.54 4.72 2.95 0.44
CYS HB3 H 9277 -0.83 4.77 2.89 0.46
CYS HG H 89 0.10 7.39 1.96 1.31
CYS C C 5506 166.73 182.73 174.97 2.04
CYS CA C 7694 42.45 67.64 58.31 3.38
CYS CB C 7226 17.99 62.07 32.63 6.11
CYS N N 8511 100.48 135.89 120.10 4.53
GLU H H 40972 4.31 12.69 8.33 0.59
GLU HA H 30827 1.65 6.29 4.25 0.41
GLU HB2 H 28174 0.34 3.37 2.02 0.21
GLU HB3 H 26311 0.34 3.47 2.00 0.22
GLU HG2 H 26182 0.53 3.77 2.27 0.21
GLU HG3 H 24188 0.56 3.80 2.25 0.21
GLU HE2 H 1 2.73 2.73 2.73 0.00
GLU C C 26803 166.80 183.52 176.92 1.94
GLU CA C 36123 44.35 65.06 57.37 2.08
GLU CB C 33900 18.71 46.75 29.98 1.71
GLU CG C 22740 25.31 44.34 36.11 1.18
GLU CD C 435 173.41 189.46 182.60 1.80
GLU N N 38937 104.54 138.60 120.66 3.47
GLN H H 22325 3.51 12.04 8.21 0.58
GLN HA H 17016 1.57 6.34 4.26 0.43
GLN HB2 H 15551 -0.07 4.00 2.05 0.25
GLN HB3 H 14705 -0.35 4.04 2.02 0.26
GLN HG2 H 14654 0.04 3.66 2.32 0.26
GLN HG3 H 13387 -0.41 3.66 2.29 0.28
GLN HE21 H 10976 3.39 11.11 7.22 0.45
GLN HE22 H 10915 3.59 10.35 7.03 0.44
GLN C C 14315 168.09 182.63 176.37 1.96
GLN CA C 19713 43.45 66.60 56.63 2.14
GLN CB C 18508 20.27 42.20 29.16 1.81
GLN CG C 12581 21.64 42.80 33.76 1.11
GLN CD C 1221 171.37 183.54 179.73 1.25
GLN N N 20907 103.88 139.55 119.85 3.57
GLN NE2 N 9714 97.90 125.33 111.87 1.69
GLY H H 39025 3.01 12.22 8.33 0.64
GLY HA2 H 29252 0.84 6.43 3.97 0.37
GLY HA3 H 27628 1.01 6.39 3.90 0.37
GLY C C 24677 163.27 184.32 173.88 1.89
GLY CA C 34024 35.78 57.88 45.36 1.28
GLY N N 35818 93.60 162.19 109.60 3.79
HIS H H 11407 3.97 12.39 8.24 0.68
HIS HA H 8864 1.93 8.90 4.60 0.43
HIS HB2 H 8230 0.17 8.70 3.11 0.35
HIS HB3 H 7956 -0.39 8.70 3.05 0.38
HIS HD1 H 378 3.79 17.20 8.65 2.55
HIS HD2 H 5840 3.46 9.01 7.00 0.42
HIS HE1 H 4613 3.21 10.88 7.95 0.48
HIS HE2 H 145 6.57 16.53 9.66 2.54
HIS C C 7244 166.90 183.12 175.28 1.97
HIS CA C 10177 46.01 66.98 56.55 2.33
HIS CB C 9571 18.75 43.38 30.23 2.07
HIS CG C 97 122.67 139.56 132.01 3.27
HIS CD2 C 3747 111.30 159.95 120.45 3.41
HIS CE1 C 2861 104.67 144.54 137.66 2.22
HIS N N 10535 104.96 136.48 119.66 3.99
HIS ND1 N 182 164.31 229.14 194.22 18.32
HIS NE2 N 187 161.70 226.29 183.09 14.99
ILE H H 27934 3.43 11.69 8.27 0.68
ILE HA H 20926 1.32 6.36 4.17 0.56
ILE HB H 19656 -1.28 3.87 1.78 0.30
ILE HG12 H 17821 -2.38 2.69 1.28 0.40
ILE HG13 H 17117 -2.07 2.99 1.19 0.41
ILE HG2 H 18714 -1.33 2.20 0.77 0.27
ILE HD1 H 18884 -1.31 2.82 0.68 0.29
ILE C C 18206 167.00 183.40 175.90 1.92
ILE CA C 24577 51.07 71.86 61.68 2.70
ILE CB C 22988 22.11 51.88 38.59 2.00
ILE CG1 C 15181 13.16 39.05 27.74 1.68
ILE CG2 C 16150 3.45 29.80 17.54 1.34
ILE CD1 C 16306 4.94 29.60 13.43 1.66
ILE N N 26198 99.00 138.12 121.40 4.29
LEU H H 46318 4.08 13.22 8.22 0.64
LEU HA H 34614 1.93 6.42 4.31 0.46
LEU HB2 H 31804 -1.25 3.18 1.61 0.34
LEU HB3 H 30311 -1.47 3.18 1.52 0.36
LEU HG H 28215 -1.06 3.90 1.51 0.33
LEU HD1 H 31370 -1.73 2.36 0.75 0.28
LEU HD2 H 30161 -1.65 2.78 0.73 0.28
LEU C C 29882 167.49 189.78 177.05 1.96
LEU CA C 40582 46.36 67.40 55.70 2.13
LEU CB C 38107 26.40 53.70 42.27 1.86
LEU CG C 23990 15.30 37.70 26.79 1.09
LEU CD1 C 26349 10.95 36.85 24.70 1.58
LEU CD2 C 25074 11.71 30.40 24.07 1.69
LEU N N 43339 98.56 177.62 121.80 3.89
LYS H H 38886 4.11 12.03 8.17 0.60
LYS HA H 29608 1.30 6.17 4.26 0.43
LYS HB2 H 26758 -0.75 4.05 1.78 0.25
LYS HB3 H 25026 -0.72 3.95 1.75 0.27
LYS HG2 H 24165 -0.98 3.13 1.37 0.26
LYS HG3 H 22062 -1.16 3.03 1.35 0.27
LYS HD2 H 21491 -0.92 7.71 1.61 0.22
LYS HD3 H 19098 -1.02 3.61 1.60 0.22
LYS HE2 H 21315 1.23 4.43 2.91 0.19
LYS HE3 H 18469 1.17 4.55 2.91 0.20
LYS HZ H 812 1.95 9.90 7.39 0.68
LYS C C 24309 166.63 185.00 176.70 1.96
LYS CA C 33090 40.73 64.57 57.00 2.20
LYS CB C 31097 21.19 46.60 32.77 1.77
LYS CG C 20156 16.85 36.22 24.91 1.13
LYS CD C 19105 20.10 40.10 28.96 1.08
LYS CE C 18453 31.57 52.20 41.90 0.82
LYS N N 35703 101.10 140.30 121.00 3.74
LYS NZ N 31 29.48 43.69 33.36 2.29
MET H H 11036 4.87 12.46 8.25 0.60
MET HA H 8656 1.13 6.35 4.40 0.47
MET HB2 H 7801 -1.05 3.87 2.03 0.33
MET HB3 H 7286 -0.99 3.47 1.99 0.35
MET HG2 H 7150 -0.42 4.40 2.42 0.35
MET HG3 H 6724 -0.30 4.24 2.39 0.38
MET HE H 5094 -0.21 8.38 1.88 0.41
MET C C 7243 167.40 183.16 176.24 2.09
MET CA C 10140 43.28 66.56 56.15 2.24
MET CB C 9372 20.98 46.46 32.95 2.20
MET CG C 5897 19.06 38.58 32.03 1.25
MET CE C 4469 10.69 32.10 17.07 1.42
MET N N 10410 102.88 138.55 120.06 3.54
PHE H H 19782 3.55 12.18 8.34 0.72
PHE HA H 14728 1.78 6.87 4.62 0.57
PHE HB2 H 13723 0.16 4.46 3.00 0.37
PHE HB3 H 13362 -0.21 4.69 2.94 0.39
PHE HD1 H 11577 4.97 8.15 7.06 0.31
PHE HD2 H 9777 4.97 8.15 7.06 0.31
PHE HE1 H 10107 4.38 8.80 7.08 0.31
PHE HE2 H 8675 4.38 8.80 7.08 0.32
PHE HZ H 7324 4.32 9.50 7.00 0.42
PHE C C 12618 166.85 184.93 175.48 2.00
PHE CA C 17026 47.31 69.82 58.16 2.59
PHE CB C 16031 25.52 50.23 39.95 2.07
PHE CG C 148 128.30 144.00 138.64 1.89
PHE CD1 C 6700 116.95 136.73 131.59 1.18
PHE CD2 C 4881 118.13 138.25 131.61 1.15
PHE CE1 C 5878 114.75 139.56 130.73 1.29
PHE CE2 C 4276 114.70 139.70 130.77 1.13
PHE CZ C 4556 116.46 138.60 129.21 1.43
PHE N N 18385 102.20 139.02 120.38 4.17
PRO HA H 16737 1.04 8.08 4.39 0.33
PRO HB2 H 15689 -0.31 4.35 2.08 0.34
PRO HB3 H 15145 -0.58 3.79 2.00 0.35
PRO HG2 H 14236 -0.77 4.42 1.93 0.31
PRO HG3 H 13138 -0.90 4.42 1.90 0.32
PRO HD2 H 14592 0.63 5.36 3.65 0.35
PRO HD3 H 14014 -0.26 5.36 3.61 0.39
PRO C C 13195 168.38 182.84 176.76 1.52
PRO CA C 18825 50.12 70.67 63.36 1.51
PRO CB C 17691 23.33 45.16 31.85 1.17
PRO CG C 12332 18.28 33.90 27.19 1.07
PRO CD C 12360 40.05 58.69 50.34 0.98
PRO N N 454 110.91 145.26 133.95 6.79
SER H H 33783 3.76 12.33 8.28 0.58
SER HA H 26114 1.54 6.85 4.47 0.40
SER HB2 H 24040 1.74 5.41 3.88 0.25
SER HB3 H 22048 1.55 5.27 3.85 0.27
SER HG H 373 0.13 8.97 5.46 1.04
SER C C 21747 164.47 184.88 174.64 1.74
SER CA C 30008 45.13 68.40 58.76 2.09
SER CB C 27897 31.40 76.39 63.79 1.51
SER N N 31183 95.97 133.68 116.27 3.52
THR H H 29445 5.32 11.73 8.24 0.62
THR HA H 22160 0.87 6.63 4.46 0.48
THR HB H 20347 0.92 8.35 4.17 0.33
THR HG1 H 641 0.32 8.21 5.19 1.15
THR HG2 H 20179 -1.19 3.54 1.14 0.22
THR C C 18399 165.50 184.43 174.57 1.75
THR CA C 25374 51.61 72.80 62.27 2.61
THR CB C 23621 15.57 81.53 69.71 1.78
THR CG2 C 16233 11.70 36.73 21.56 1.10
THR N N 27323 95.77 138.27 115.37 4.76
TRP H H 6374 5.16 11.76 8.28 0.77
TRP HA H 4710 2.24 6.55 4.66 0.52
TRP HB2 H 4414 0.42 4.54 3.19 0.35
TRP HB3 H 4277 0.31 4.44 3.12 0.36
TRP HD1 H 3930 4.90 8.93 7.14 0.35
TRP HE1 H 4317 5.12 13.49 10.08 0.64
TRP HE3 H 3442 4.89 9.95 7.32 0.41
TRP HZ2 H 3698 4.90 8.56 7.28 0.33
TRP HZ3 H 3336 3.88 8.90 6.86 0.39
TRP HH2 H 3394 4.37 10.17 6.97 0.38
TRP C C 3782 168.17 182.60 176.19 2.02
TRP CA C 5160 44.69 69.76 57.72 2.58
TRP CB C 4858 21.10 43.02 29.98 2.00
TRP CG C 122 107.50 116.53 110.85 1.83
TRP CD1 C 2378 108.45 132.35 126.55 1.81
TRP CD2 C 93 120.20 132.62 127.70 1.58
TRP CE2 C 90 113.89 177.71 138.61 6.86
TRP CE3 C 2013 93.34 137.60 120.44 1.76
TRP CZ2 C 2276 103.18 124.10 114.25 1.10
TRP CZ3 C 2042 98.61 138.39 121.37 1.54
TRP CH2 C 2120 112.43 131.54 123.86 1.39
TRP N N 5681 101.97 138.11 121.58 4.12
TRP NE1 N 3406 107.64 139.20 129.29 2.03
TYR H H 16674 4.16 12.01 8.30 0.73
TYR HA H 12650 1.19 6.73 4.61 0.56
TYR HB2 H 11793 -0.49 4.70 2.90 0.37
TYR HB3 H 11505 -0.19 4.70 2.84 0.39
TYR HD1 H 10330 4.68 8.53 6.93 0.30
TYR HD2 H 8872 4.43 8.50 6.93 0.30
TYR HE1 H 9808 4.58 7.86 6.70 0.23
TYR HE2 H 8515 4.56 8.50 6.70 0.23
TYR HH H 182 5.99 13.75 9.30 1.27
TYR C C 10008 167.86 184.78 175.44 1.99
TYR CA C 13959 44.64 69.56 58.20 2.54
TYR CB C 13056 28.82 47.30 39.27 2.14
TYR CG C 129 117.70 174.59 129.67 4.61
TYR CD1 C 6005 116.44 141.57 132.76 1.20
TYR CD2 C 4245 113.00 138.29 132.73 1.32
TYR CE1 C 5974 110.70 134.01 117.93 1.21
TYR CE2 C 4191 106.55 135.82 117.90 1.27
TYR CZ C 114 105.25 162.70 156.50 5.18
TYR N N 15071 39.20 144.96 120.47 4.22
VAL H H 36291 3.98 12.59 8.28 0.67
VAL HA H 27401 0.97 6.30 4.17 0.58
VAL HB H 25796 -1.22 3.32 1.98 0.32
VAL HG1 H 25297 -1.13 2.57 0.83 0.26
VAL HG2 H 24712 -2.32 2.78 0.80 0.28
VAL C C 23514 165.65 183.95 175.67 1.90
VAL CA C 31846 50.16 70.34 62.57 2.89
VAL CB C 29872 20.55 45.33 32.71 1.78
VAL CG1 C 21239 13.53 32.27 21.51 1.36
VAL CG2 C 20441 13.26 30.46 21.29 1.54
VAL N N 34197 97.22 143.29 121.08 4.54
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