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 3614722 possible chemical shifts in the BMRB database, 2561457 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: 11-04-2009
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 23514 3.53 11.48 8.19 0.60
ALA HA H 17979 1.24 6.51 4.26 0.44
ALA HB H 16967 -0.83 3.12 1.36 0.25
ALA C C 13981 164.48 187.20 177.77 2.15
ALA CA C 19336 44.22 65.52 53.16 1.97
ALA CB C 18021 9.79 28.40 18.98 1.81
ALA N N 21222 77.10 142.81 123.23 3.57
ARG H H 16016 3.64 12.69 8.24 0.61
ARG HA H 12588 1.34 6.10 4.30 0.46
ARG HB2 H 11245 -0.77 3.29 1.80 0.27
ARG HB3 H 10478 -0.74 3.29 1.77 0.28
ARG HG2 H 10003 -0.64 3.51 1.57 0.26
ARG HG3 H 9014 -0.67 3.51 1.55 0.28
ARG HD2 H 9745 0.89 4.69 3.12 0.23
ARG HD3 H 8616 0.89 4.29 3.11 0.25
ARG HE H 3342 2.99 11.88 7.38 0.62
ARG HH11 H 345 5.88 9.82 6.90 0.45
ARG HH12 H 254 6.01 10.73 6.83 0.41
ARG HH21 H 313 5.90 11.35 6.81 0.48
ARG HH22 H 244 5.97 10.18 6.76 0.40
ARG C C 9089 167.44 184.51 176.44 2.04
ARG CA C 12895 43.27 67.98 56.78 2.31
ARG CB C 11699 20.95 42.50 30.68 1.84
ARG CG C 7325 18.22 37.83 27.23 1.18
ARG CD C 7457 35.05 49.06 43.17 0.86
ARG CZ C 179 156.20 177.70 160.09 3.29
ARG N N 13930 103.60 137.60 120.81 3.73
ARG NE N 1598 75.15 99.81 84.67 1.63
ARG NH1 N 53 67.60 87.07 73.64 4.11
ARG NH2 N 49 70.10 85.28 73.43 3.49
ASP H H 18616 4.06 12.61 8.31 0.58
ASP HA H 14277 2.33 6.33 4.60 0.32
ASP HB2 H 13181 -0.39 4.58 2.72 0.27
ASP HB3 H 12525 0.02 4.58 2.67 0.28
ASP C C 11243 166.80 182.70 176.44 1.76
ASP CA C 15559 44.81 62.49 54.68 2.04
ASP CB C 14431 27.48 51.09 40.87 1.64
ASP CG C 260 170.72 183.94 179.27 1.83
ASP N N 16998 101.90 143.52 120.68 3.91
ASN H H 13199 2.61 12.40 8.35 0.63
ASN HA H 10377 1.75 6.43 4.67 0.37
ASN HB2 H 9615 0.23 4.47 2.81 0.31
ASN HB3 H 9174 -0.07 4.47 2.76 0.33
ASN HD21 H 6971 3.55 9.60 7.35 0.48
ASN HD22 H 6915 3.08 10.80 7.14 0.49
ASN C C 7626 167.04 181.90 175.31 1.81
ASN CA C 10754 41.31 61.80 53.55 1.90
ASN CB C 9957 28.64 55.09 38.68 1.68
ASN CG C 756 166.40 181.20 176.78 1.38
ASN N N 11570 101.71 137.49 118.96 4.03
ASN ND2 N 5477 99.40 133.86 112.79 2.27
CYS H H 7392 4.73 12.12 8.40 0.67
CYS HA H 6501 1.64 6.43 4.67 0.56
CYS HB2 H 6207 -0.54 4.65 2.95 0.45
CYS HB3 H 6039 -0.83 4.69 2.90 0.47
CYS HG H 53 0.25 7.39 1.90 1.46
CYS C C 2957 166.73 182.73 174.87 2.06
CYS CA C 4218 42.45 67.64 58.16 3.37
CYS CB C 3837 17.99 62.07 32.90 6.29
CYS N N 4932 100.48 135.89 120.16 4.62
GLU H H 24647 4.24 12.17 8.34 0.60
GLU HA H 19075 1.77 6.29 4.25 0.41
GLU HB2 H 17240 0.34 3.44 2.03 0.21
GLU HB3 H 15842 0.34 3.44 2.00 0.22
GLU HG2 H 15902 0.57 3.77 2.28 0.21
GLU HG3 H 14415 0.56 3.83 2.26 0.21
GLU HE2 H 1 2.73 2.73 2.73 0.00
GLU C C 15377 166.80 183.52 176.93 1.97
GLU CA C 21019 44.35 64.60 57.35 2.09
GLU CB C 19374 18.71 42.33 30.00 1.73
GLU CG C 12844 25.50 50.28 36.10 1.22
GLU CD C 283 173.41 189.46 182.58 1.98
GLU N N 22896 104.54 138.60 120.69 3.51
GLN H H 13068 5.18 12.04 8.22 0.59
GLN HA H 10207 1.60 6.23 4.26 0.43
GLN HB2 H 9190 -0.12 4.00 2.05 0.25
GLN HB3 H 8546 -0.52 4.04 2.02 0.27
GLN HG2 H 8600 0.04 3.66 2.32 0.28
GLN HG3 H 7688 -1.08 3.66 2.30 0.29
GLN HE21 H 6268 3.69 11.11 7.24 0.46
GLN HE22 H 6232 3.59 9.79 7.02 0.45
GLN C C 7898 168.09 182.22 176.36 1.96
GLN CA C 11048 47.87 66.60 56.60 2.14
GLN CB C 10151 20.27 42.20 29.17 1.83
GLN CG C 6817 21.64 41.95 33.78 1.12
GLN CD C 719 171.70 183.54 179.67 1.37
GLN N N 11910 104.10 139.55 119.86 3.63
GLN NE2 N 5300 92.49 124.30 111.87 1.80
GLY H H 23412 3.01 12.22 8.33 0.66
GLY HA2 H 17950 0.86 6.43 3.97 0.38
GLY HA3 H 16827 1.04 6.39 3.90 0.38
GLY C C 13589 163.27 183.16 173.93 1.87
GLY CA C 19199 35.78 58.67 45.36 1.29
GLY N N 20638 94.07 162.19 109.68 3.87
HIS H H 7015 5.24 12.39 8.24 0.69
HIS HA H 5485 1.93 8.90 4.61 0.44
HIS HB2 H 5045 0.18 8.70 3.11 0.36
HIS HB3 H 4864 0.39 8.70 3.05 0.39
HIS HD1 H 261 3.79 17.20 8.79 2.72
HIS HD2 H 3532 3.46 9.01 7.03 0.45
HIS HE1 H 2924 3.21 10.26 7.98 0.51
HIS HE2 H 124 6.58 16.53 9.79 2.62
HIS C C 4223 166.90 182.80 175.28 1.98
HIS CA C 5970 46.01 66.98 56.49 2.33
HIS CB C 5526 18.75 43.30 30.21 2.09
HIS CG C 77 122.67 137.19 131.49 3.33
HIS CD2 C 1932 112.07 159.95 120.48 3.46
HIS CE1 C 1498 104.67 144.54 137.55 2.41
HIS N N 6328 105.00 136.48 119.62 4.05
HIS ND1 N 127 164.64 229.14 195.73 18.04
HIS NE2 N 146 161.70 226.29 182.19 14.39
ILE H H 16773 3.43 11.69 8.28 0.69
ILE HA H 12968 1.32 6.36 4.18 0.56
ILE HB H 12095 -1.28 3.87 1.79 0.29
ILE HG12 H 10854 -2.38 2.69 1.27 0.40
ILE HG13 H 10281 -2.04 2.99 1.21 0.41
ILE HG2 H 11448 -1.14 1.87 0.78 0.27
ILE HD1 H 11490 -1.08 2.82 0.68 0.29
ILE C C 10362 167.00 183.40 175.88 1.95
ILE CA C 14133 51.15 71.70 61.63 2.70
ILE CB C 13005 20.94 51.88 38.62 2.04
ILE CG1 C 8548 12.90 39.05 27.74 1.75
ILE CG2 C 9175 3.45 29.80 17.54 1.41
ILE CD1 C 9233 2.70 29.60 13.47 1.68
ILE N N 15284 99.00 138.12 121.50 4.33
LEU H H 27318 3.01 13.22 8.22 0.65
LEU HA H 21077 1.93 6.24 4.31 0.47
LEU HB2 H 19128 -1.21 3.18 1.62 0.34
LEU HB3 H 18009 -1.29 3.18 1.53 0.36
LEU HG H 16884 -1.06 3.90 1.51 0.33
LEU HD1 H 18763 -1.73 2.36 0.76 0.28
LEU HD2 H 17990 -1.65 2.78 0.74 0.28
LEU C C 16647 167.49 189.78 177.02 2.00
LEU CA C 22923 46.36 65.83 55.66 2.14
LEU CB C 21200 26.40 53.70 42.29 1.87
LEU CG C 13244 15.57 39.56 26.80 1.15
LEU CD1 C 14667 10.95 31.83 24.69 1.61
LEU CD2 C 13869 11.71 30.40 24.10 1.69
LEU N N 24836 40.20 144.55 121.86 3.97
LYS H H 23983 5.09 12.03 8.19 0.61
LYS HA H 18568 1.30 6.17 4.26 0.44
LYS HB2 H 16635 -0.84 4.05 1.78 0.25
LYS HB3 H 15339 -0.97 3.95 1.75 0.27
LYS HG2 H 14873 -1.16 2.99 1.37 0.26
LYS HG3 H 13336 -1.11 2.99 1.35 0.28
LYS HD2 H 13040 -1.68 8.50 1.61 0.23
LYS HD3 H 11278 -1.02 3.61 1.60 0.23
LYS HE2 H 12915 1.25 4.36 2.92 0.19
LYS HE3 H 10956 1.24 4.55 2.91 0.19
LYS HZ H 666 2.41 9.90 7.42 0.64
LYS C C 13765 167.21 185.00 176.68 1.98
LYS CA C 19170 46.60 63.38 56.96 2.20
LYS CB C 17668 21.19 46.60 32.78 1.78
LYS CG C 11265 18.20 36.22 24.93 1.15
LYS CD C 10691 21.20 42.26 28.96 1.15
LYS CE C 10305 30.48 52.20 41.91 0.81
LYS N N 21211 101.10 140.30 121.09 3.80
LYS NZ N 13 31.00 43.69 33.96 3.04
MET H H 6570 4.87 12.46 8.26 0.60
MET HA H 5267 1.13 6.35 4.41 0.47
MET HB2 H 4710 -1.05 3.87 2.03 0.34
MET HB3 H 4349 -0.99 3.20 2.00 0.34
MET HG2 H 4272 -0.36 4.40 2.43 0.36
MET HG3 H 3986 -0.30 4.24 2.40 0.38
MET HE H 2824 -0.21 17.06 1.88 0.48
MET C C 4108 167.40 183.16 176.20 2.10
MET CA C 5820 45.50 66.56 56.13 2.25
MET CB C 5261 20.98 46.46 32.99 2.24
MET CG C 3249 20.46 38.58 32.04 1.26
MET CE C 2296 0.00 40.77 17.17 1.94
MET N N 6043 87.60 135.66 120.09 3.58
PHE H H 11906 4.81 12.18 8.36 0.72
PHE HA H 9112 1.78 6.57 4.62 0.56
PHE HB2 H 8447 0.17 4.46 3.00 0.37
PHE HB3 H 8169 0.42 4.31 2.95 0.38
PHE HD1 H 7053 4.72 8.08 7.06 0.30
PHE HD2 H 5630 4.72 8.15 7.07 0.30
PHE HE1 H 6209 4.10 8.80 7.09 0.31
PHE HE2 H 5042 4.10 8.80 7.08 0.32
PHE HZ H 4422 4.53 9.50 7.00 0.42
PHE C C 7092 166.85 183.77 175.47 1.99
PHE CA C 9794 47.31 69.82 58.13 2.56
PHE CB C 9060 25.52 48.53 39.94 2.10
PHE CG C 104 128.30 152.84 138.34 2.35
PHE CD1 C 3504 118.50 138.70 131.55 1.20
PHE CD2 C 2198 118.50 138.70 131.61 1.14
PHE CE1 C 2995 114.75 135.60 130.68 1.43
PHE CE2 C 1897 118.00 139.70 130.77 1.19
PHE CZ C 2221 116.46 138.60 129.23 1.54
PHE N N 10707 102.20 139.02 120.49 4.15
PRO HA H 10146 1.63 6.05 4.40 0.33
PRO HB2 H 9442 -0.28 4.02 2.07 0.35
PRO HB3 H 8986 -1.07 3.79 2.01 0.36
PRO HG2 H 8475 -0.39 4.42 1.93 0.31
PRO HG3 H 7703 -0.90 4.42 1.91 0.33
PRO HD2 H 8714 0.63 5.36 3.65 0.36
PRO HD3 H 8297 -0.26 5.36 3.62 0.38
PRO C C 7427 168.43 182.30 176.73 1.53
PRO CA C 10714 50.12 70.67 63.34 1.55
PRO CB C 9868 24.69 43.70 31.85 1.19
PRO CG C 6674 18.28 33.90 27.21 1.09
PRO CD C 6723 40.05 58.30 50.36 0.98
PRO N N 266 111.56 145.26 133.97 6.60
SER H H 19909 3.76 13.13 8.28 0.59
SER HA H 15776 1.66 6.44 4.48 0.41
SER HB2 H 14288 1.74 5.41 3.88 0.26
SER HB3 H 12950 1.51 5.01 3.85 0.28
SER HG H 237 0.00 8.97 5.32 1.03
SER C C 11775 164.47 184.88 174.69 1.75
SER CA C 16688 45.13 68.40 58.76 2.10
SER CB C 15174 52.61 73.90 63.80 1.49
SER N N 17674 100.85 133.68 116.29 3.59
THR H H 17848 5.32 11.73 8.24 0.62
THR HA H 13811 0.87 6.36 4.46 0.48
THR HB H 12548 0.92 8.35 4.17 0.33
THR HG1 H 407 0.32 8.21 5.01 1.54
THR HG2 H 12454 -1.19 4.07 1.14 0.23
THR C C 10285 165.50 184.43 174.58 1.77
THR CA C 14508 51.61 72.80 62.23 2.63
THR CB C 13225 33.00 80.22 69.70 1.69
THR CG2 C 8936 11.70 36.73 21.56 1.11
THR N N 15893 97.70 138.27 115.46 4.77
TRP H H 3770 4.49 11.67 8.30 0.79
TRP HA H 2875 2.28 6.52 4.68 0.52
TRP HB2 H 2676 0.42 4.54 3.19 0.36
TRP HB3 H 2563 0.77 4.44 3.13 0.36
TRP HD1 H 2390 4.90 10.75 7.15 0.35
TRP HE1 H 2558 5.80 12.92 10.10 0.54
TRP HE3 H 2140 4.89 8.79 7.32 0.40
TRP HZ2 H 2261 4.90 8.27 7.29 0.32
TRP HZ3 H 2063 3.88 8.90 6.87 0.40
TRP HH2 H 2091 4.53 10.90 6.99 0.39
TRP C C 2042 168.17 181.89 176.14 2.02
TRP CA C 2890 44.69 69.76 57.67 2.57
TRP CB C 2662 21.10 43.02 29.98 2.02
TRP CG C 103 105.30 116.53 110.65 1.88
TRP CD1 C 1210 108.45 132.35 126.48 1.94
TRP CD2 C 79 120.20 130.10 127.48 1.40
TRP CE2 C 70 118.50 177.71 138.63 6.80
TRP CE3 C 1028 111.86 137.60 120.51 1.72
TRP CZ2 C 1142 81.81 129.97 114.23 1.55
TRP CZ3 C 1032 113.32 138.39 121.42 1.58
TRP CH2 C 1065 91.62 131.54 123.81 1.84
TRP N N 3184 106.44 138.11 121.64 4.17
TRP NE1 N 1825 107.64 139.20 129.39 1.93
TYR H H 10015 4.16 11.98 8.32 0.74
TYR HA H 7799 1.20 6.73 4.63 0.56
TYR HB2 H 7231 0.49 4.70 2.91 0.37
TYR HB3 H 7011 -0.19 4.70 2.85 0.39
TYR HD1 H 6459 4.98 8.53 6.94 0.30
TYR HD2 H 5243 4.20 8.50 6.94 0.30
TYR HE1 H 6191 2.78 7.86 6.71 0.23
TYR HE2 H 5077 3.13 8.50 6.71 0.24
TYR HH H 116 5.99 13.75 9.30 1.42
TYR C C 5477 167.86 182.92 175.41 2.00
TYR CA C 7845 49.08 65.99 58.13 2.55
TYR CB C 7177 28.82 57.73 39.30 2.15
TYR CG C 95 117.70 174.59 129.76 5.25
TYR CD1 C 3164 116.44 138.65 132.76 1.25
TYR CD2 C 1930 113.00 136.70 132.71 1.45
TYR CE1 C 3136 110.70 134.01 117.93 1.23
TYR CE2 C 1922 113.10 134.01 117.92 1.33
TYR CZ C 79 153.54 162.70 156.63 2.11
TYR N N 8610 100.09 144.96 120.63 4.26
VAL H H 21582 3.98 12.59 8.29 0.68
VAL HA H 16782 0.97 6.30 4.19 0.58
VAL HB H 15684 -0.54 3.32 1.99 0.32
VAL HG1 H 15331 -1.12 2.57 0.83 0.26
VAL HG2 H 14882 -2.32 2.78 0.80 0.28
VAL C C 13067 165.65 183.69 175.66 1.90
VAL CA C 18060 50.16 70.02 62.49 2.88
VAL CB C 16652 20.55 45.33 32.72 1.80
VAL CG1 C 11805 13.53 32.27 21.51 1.38
VAL CG2 C 11244 13.58 30.46 21.29 1.57
VAL N N 19690 97.95 143.29 121.13 4.59
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