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 3623767 possible chemical shifts in the BMRB database, 2568844 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: 11-17-2009
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 23592 3.53 11.48 8.20 0.60
ALA HA H 18028 1.24 6.51 4.26 0.44
ALA HB H 17017 -0.83 3.12 1.36 0.25
ALA C C 14038 164.48 187.20 177.77 2.15
ALA CA C 19393 44.22 65.52 53.16 1.97
ALA CB C 18102 9.79 28.40 18.98 1.81
ALA N N 21300 77.10 142.81 123.23 3.57
ARG H H 16069 3.64 12.69 8.24 0.61
ARG HA H 12628 1.34 6.10 4.30 0.46
ARG HB2 H 11283 -0.77 3.29 1.80 0.27
ARG HB3 H 10513 -0.74 3.29 1.77 0.28
ARG HG2 H 10034 -0.64 3.51 1.57 0.26
ARG HG3 H 9040 -0.67 3.51 1.55 0.28
ARG HD2 H 9777 0.89 4.69 3.12 0.23
ARG HD3 H 8645 0.89 4.29 3.11 0.25
ARG HE H 3346 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 9120 167.44 184.51 176.44 2.04
ARG CA C 12941 43.27 67.98 56.78 2.31
ARG CB C 11750 20.95 42.50 30.67 1.84
ARG CG C 7355 18.22 37.83 27.23 1.19
ARG CD C 7489 35.05 49.06 43.17 0.86
ARG CZ C 179 156.20 177.70 160.09 3.29
ARG N N 13983 103.60 137.60 120.81 3.72
ARG NE N 1602 75.15 99.81 84.68 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 18668 4.06 12.61 8.31 0.58
ASP HA H 14306 2.33 6.33 4.60 0.32
ASP HB2 H 13209 -0.39 4.58 2.72 0.27
ASP HB3 H 12552 0.02 4.58 2.67 0.28
ASP C C 11284 166.80 182.70 176.44 1.76
ASP CA C 15593 44.81 62.49 54.68 2.04
ASP CB C 14484 27.48 51.09 40.86 1.64
ASP CG C 260 170.72 183.94 179.27 1.83
ASP N N 17050 101.90 143.52 120.68 3.91
ASN H H 13233 2.61 12.40 8.35 0.63
ASN HA H 10395 1.75 6.43 4.67 0.37
ASN HB2 H 9633 0.23 4.47 2.81 0.31
ASN HB3 H 9191 -0.07 4.47 2.76 0.33
ASN HD21 H 6984 3.55 9.60 7.35 0.48
ASN HD22 H 6928 3.08 10.80 7.14 0.49
ASN C C 7649 167.04 181.90 175.31 1.81
ASN CA C 10781 41.31 61.80 53.55 1.90
ASN CB C 9991 28.64 55.09 38.68 1.68
ASN CG C 757 166.40 181.20 176.77 1.38
ASN N N 11604 101.71 137.49 118.96 4.03
ASN ND2 N 5490 99.40 133.86 112.79 2.27
CYS H H 7396 4.73 12.12 8.40 0.67
CYS HA H 6504 1.64 6.43 4.67 0.56
CYS HB2 H 6210 -0.54 4.65 2.95 0.45
CYS HB3 H 6042 -0.83 4.69 2.90 0.47
CYS HG H 53 0.25 7.39 1.90 1.46
CYS C C 2959 166.73 182.73 174.87 2.06
CYS CA C 4222 42.45 67.64 58.17 3.37
CYS CB C 3841 17.99 62.07 32.91 6.29
CYS N N 4936 100.48 135.89 120.16 4.62
GLU H H 24703 4.24 12.17 8.34 0.60
GLU HA H 19108 1.77 6.29 4.25 0.41
GLU HB2 H 17271 0.34 3.44 2.03 0.21
GLU HB3 H 15873 0.34 3.44 2.00 0.22
GLU HG2 H 15931 0.57 3.77 2.28 0.21
GLU HG3 H 14443 0.56 3.83 2.26 0.21
GLU HE2 H 1 2.73 2.73 2.73 0.00
GLU C C 15424 166.80 183.52 176.93 1.97
GLU CA C 21063 44.35 64.60 57.35 2.09
GLU CB C 19433 18.71 42.33 30.00 1.73
GLU CG C 12874 25.50 50.28 36.10 1.22
GLU CD C 284 173.41 189.46 182.58 1.97
GLU N N 22952 104.54 138.60 120.69 3.51
GLN H H 13124 5.18 12.04 8.22 0.59
GLN HA H 10247 1.60 6.23 4.26 0.43
GLN HB2 H 9226 -0.12 4.00 2.05 0.25
GLN HB3 H 8581 -0.52 4.04 2.02 0.27
GLN HG2 H 8636 0.04 3.66 2.32 0.27
GLN HG3 H 7721 -1.08 3.66 2.30 0.29
GLN HE21 H 6286 3.69 11.11 7.24 0.46
GLN HE22 H 6245 3.59 9.79 7.02 0.45
GLN C C 7947 168.09 182.22 176.36 1.96
GLN CA C 11097 47.87 66.60 56.60 2.14
GLN CB C 10209 20.27 42.20 29.17 1.83
GLN CG C 6855 21.64 41.95 33.78 1.12
GLN CD C 719 171.70 183.54 179.67 1.37
GLN N N 11966 104.10 139.55 119.86 3.63
GLN NE2 N 5318 92.49 124.30 111.87 1.80
GLY H H 23513 3.01 12.22 8.33 0.66
GLY HA2 H 18020 0.86 6.43 3.97 0.38
GLY HA3 H 16897 1.04 6.39 3.90 0.38
GLY C C 13671 163.27 183.16 173.93 1.87
GLY CA C 19293 35.78 58.67 45.35 1.29
GLY N N 20739 94.07 162.19 109.68 3.86
HIS H H 7032 5.24 12.39 8.24 0.69
HIS HA H 5497 1.93 8.90 4.61 0.44
HIS HB2 H 5057 0.18 8.70 3.11 0.36
HIS HB3 H 4876 0.39 8.70 3.05 0.39
HIS HD1 H 262 3.79 17.20 8.79 2.71
HIS HD2 H 3534 3.46 9.01 7.03 0.45
HIS HE1 H 2925 3.21 10.26 7.98 0.51
HIS HE2 H 124 6.58 16.53 9.79 2.62
HIS C C 4239 166.90 182.80 175.28 1.98
HIS CA C 5987 46.01 66.98 56.49 2.33
HIS CB C 5546 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 6345 105.00 136.48 119.62 4.04
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 16824 3.43 11.69 8.28 0.69
ILE HA H 12991 1.32 6.36 4.18 0.56
ILE HB H 12117 -1.28 3.87 1.79 0.29
ILE HG12 H 10874 -2.38 2.69 1.27 0.40
ILE HG13 H 10302 -2.04 2.99 1.21 0.41
ILE HG2 H 11468 -1.14 1.87 0.78 0.27
ILE HD1 H 11512 -1.08 2.82 0.68 0.29
ILE C C 10401 167.00 183.40 175.88 1.95
ILE CA C 14169 51.15 71.70 61.63 2.69
ILE CB C 13058 20.94 51.88 38.62 2.04
ILE CG1 C 8570 12.90 39.05 27.74 1.75
ILE CG2 C 9199 3.45 29.80 17.54 1.41
ILE CD1 C 9257 2.70 29.60 13.47 1.68
ILE N N 15335 99.00 138.12 121.50 4.33
LEU H H 27402 3.01 13.22 8.22 0.65
LEU HA H 21123 1.93 6.24 4.31 0.47
LEU HB2 H 19175 -1.21 3.18 1.62 0.34
LEU HB3 H 18054 -1.29 3.18 1.53 0.36
LEU HG H 16926 -1.06 3.90 1.51 0.33
LEU HD1 H 18806 -1.73 2.36 0.76 0.28
LEU HD2 H 18027 -1.65 2.78 0.74 0.28
LEU C C 16702 167.49 189.78 177.02 2.00
LEU CA C 22974 46.36 65.83 55.66 2.14
LEU CB C 21272 26.40 53.70 42.29 1.87
LEU CG C 13274 15.57 39.56 26.80 1.15
LEU CD1 C 14699 10.95 31.83 24.68 1.61
LEU CD2 C 13894 11.71 30.40 24.10 1.69
LEU N N 24920 40.20 144.55 121.85 3.96
LYS H H 24057 5.09 12.03 8.19 0.61
LYS HA H 18613 1.30 6.17 4.26 0.44
LYS HB2 H 16677 -0.84 4.05 1.78 0.25
LYS HB3 H 15383 -0.97 3.95 1.75 0.27
LYS HG2 H 14910 -1.16 2.99 1.37 0.26
LYS HG3 H 13371 -1.11 2.99 1.35 0.28
LYS HD2 H 13075 -1.68 8.50 1.61 0.23
LYS HD3 H 11312 -1.02 3.61 1.60 0.23
LYS HE2 H 12948 1.25 4.36 2.92 0.19
LYS HE3 H 10988 1.24 4.55 2.91 0.19
LYS HZ H 666 2.41 9.90 7.42 0.64
LYS C C 13823 167.21 185.00 176.68 1.97
LYS CA C 19226 46.60 63.38 56.96 2.20
LYS CB C 17741 21.19 46.60 32.78 1.78
LYS CG C 11299 18.20 36.22 24.93 1.15
LYS CD C 10714 21.20 42.26 28.96 1.15
LYS CE C 10328 30.48 52.20 41.91 0.81
LYS N N 21285 101.10 140.30 121.09 3.80
LYS NZ N 13 31.00 43.69 33.96 3.04
MET H H 6595 4.87 12.46 8.26 0.60
MET HA H 5287 1.13 6.35 4.41 0.48
MET HB2 H 4729 -1.05 3.87 2.03 0.34
MET HB3 H 4368 -0.99 3.20 2.00 0.34
MET HG2 H 4290 -0.36 4.40 2.43 0.36
MET HG3 H 4003 -0.30 4.24 2.40 0.38
MET HE H 2834 -0.21 17.06 1.88 0.48
MET C C 4125 167.40 183.16 176.21 2.09
MET CA C 5843 45.50 66.56 56.13 2.25
MET CB C 5286 20.98 46.46 32.99 2.24
MET CG C 3264 20.46 38.58 32.04 1.26
MET CE C 2301 0.00 40.77 17.17 1.94
MET N N 6068 87.60 135.66 120.10 3.58
PHE H H 11931 4.81 12.18 8.36 0.72
PHE HA H 9125 1.78 6.57 4.62 0.56
PHE HB2 H 8460 0.17 4.46 3.00 0.37
PHE HB3 H 8182 0.42 4.31 2.95 0.38
PHE HD1 H 7062 4.72 8.08 7.06 0.30
PHE HD2 H 5638 4.72 8.15 7.07 0.30
PHE HE1 H 6215 4.10 8.80 7.09 0.31
PHE HE2 H 5048 4.10 8.80 7.08 0.32
PHE HZ H 4426 4.53 9.50 7.00 0.42
PHE C C 7108 166.85 183.77 175.48 1.99
PHE CA C 9812 47.31 69.82 58.13 2.56
PHE CB C 9086 25.52 48.53 39.93 2.10
PHE CG C 104 128.30 152.84 138.34 2.35
PHE CD1 C 3509 118.50 138.70 131.55 1.20
PHE CD2 C 2200 118.50 138.70 131.61 1.14
PHE CE1 C 2998 114.75 135.60 130.68 1.43
PHE CE2 C 1899 118.00 139.70 130.77 1.19
PHE CZ C 2225 116.46 138.60 129.24 1.54
PHE N N 10732 102.20 139.02 120.49 4.15
PRO HA H 10175 1.63 6.05 4.40 0.33
PRO HB2 H 9469 -0.28 4.02 2.07 0.35
PRO HB3 H 9012 -1.07 3.79 2.01 0.36
PRO HG2 H 8496 -0.39 4.42 1.93 0.31
PRO HG3 H 7721 -0.90 4.42 1.91 0.33
PRO HD2 H 8735 0.63 5.36 3.65 0.36
PRO HD3 H 8317 -0.26 5.36 3.62 0.38
PRO C C 7467 168.43 182.30 176.73 1.53
PRO CA C 10753 50.12 70.67 63.34 1.55
PRO CB C 9916 24.69 43.70 31.85 1.19
PRO CG C 6692 18.28 33.90 27.21 1.09
PRO CD C 6741 40.05 58.30 50.36 0.98
PRO N N 266 111.56 145.26 133.97 6.60
SER H H 19972 3.76 13.13 8.28 0.59
SER HA H 15812 1.66 6.44 4.48 0.41
SER HB2 H 14322 1.74 5.41 3.88 0.26
SER HB3 H 12983 1.51 5.01 3.85 0.28
SER HG H 237 0.00 8.97 5.32 1.03
SER C C 11819 164.47 184.88 174.69 1.75
SER CA C 16738 45.13 68.40 58.76 2.10
SER CB C 15232 52.61 73.90 63.80 1.49
SER N N 17737 100.85 133.68 116.29 3.59
THR H H 17903 5.32 11.73 8.24 0.62
THR HA H 13855 0.87 6.36 4.46 0.48
THR HB H 12592 0.92 8.35 4.17 0.33
THR HG1 H 407 0.32 8.21 5.01 1.54
THR HG2 H 12498 -1.19 4.07 1.14 0.23
THR C C 10324 165.50 184.43 174.58 1.77
THR CA C 14559 51.61 72.80 62.23 2.63
THR CB C 13281 33.00 80.22 69.70 1.69
THR CG2 C 8976 11.70 36.73 21.56 1.11
THR N N 15948 97.70 138.27 115.45 4.76
TRP H H 3788 4.49 11.67 8.30 0.79
TRP HA H 2886 2.28 6.52 4.68 0.52
TRP HB2 H 2686 0.42 4.54 3.19 0.36
TRP HB3 H 2573 0.77 4.44 3.13 0.36
TRP HD1 H 2397 4.90 10.75 7.15 0.35
TRP HE1 H 2566 5.80 12.92 10.10 0.54
TRP HE3 H 2146 4.89 8.79 7.32 0.40
TRP HZ2 H 2268 4.90 8.27 7.29 0.32
TRP HZ3 H 2069 3.88 8.90 6.87 0.40
TRP HH2 H 2099 4.53 10.90 6.99 0.39
TRP C C 2051 168.17 181.89 176.15 2.02
TRP CA C 2906 44.69 69.76 57.66 2.58
TRP CB C 2680 21.10 43.02 29.98 2.02
TRP CG C 103 105.30 116.53 110.65 1.88
TRP CD1 C 1212 108.45 132.35 126.47 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 1029 111.86 137.60 120.51 1.72
TRP CZ2 C 1144 81.81 129.97 114.23 1.55
TRP CZ3 C 1032 113.32 138.39 121.42 1.58
TRP CH2 C 1067 91.62 131.54 123.81 1.84
TRP N N 3202 106.44 138.11 121.63 4.17
TRP NE1 N 1833 107.64 139.20 129.36 2.05
TYR H H 10047 4.16 11.98 8.32 0.74
TYR HA H 7821 1.20 6.73 4.63 0.56
TYR HB2 H 7253 0.49 4.70 2.91 0.37
TYR HB3 H 7033 -0.19 4.70 2.85 0.39
TYR HD1 H 6473 4.98 8.53 6.94 0.30
TYR HD2 H 5255 4.20 8.50 6.94 0.30
TYR HE1 H 6204 2.78 7.86 6.71 0.23
TYR HE2 H 5089 3.13 8.50 6.71 0.24
TYR HH H 116 5.99 13.75 9.30 1.42
TYR C C 5494 167.86 182.92 175.41 1.99
TYR CA C 7872 49.08 65.99 58.13 2.55
TYR CB C 7207 28.82 57.73 39.30 2.15
TYR CG C 95 117.70 174.59 129.76 5.25
TYR CD1 C 3165 116.44 138.65 132.76 1.25
TYR CD2 C 1930 113.00 136.70 132.71 1.45
TYR CE1 C 3137 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 8642 100.09 144.96 120.63 4.26
VAL H H 21624 3.98 12.59 8.29 0.68
VAL HA H 16806 0.97 6.30 4.19 0.58
VAL HB H 15708 -0.54 3.32 1.99 0.32
VAL HG1 H 15354 -1.12 2.57 0.83 0.26
VAL HG2 H 14905 -2.32 2.78 0.80 0.28
VAL C C 13095 165.65 183.69 175.66 1.90
VAL CA C 18088 50.16 70.02 62.49 2.88
VAL CB C 16694 20.55 45.33 32.72 1.80
VAL CG1 C 11828 13.53 32.27 21.50 1.38
VAL CG2 C 11267 13.58 30.46 21.29 1.57
VAL N N 19732 97.95 143.29 121.13 4.59
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