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 3443106 possible chemical shifts in the BMRB database, 2448162 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: 06-30-2009
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 22522 3.53 11.48 8.19 0.60
ALA HA H 17215 1.24 6.51 4.26 0.44
ALA HB H 16190 -0.83 3.12 1.36 0.25
ALA C C 13408 164.48 187.20 177.77 2.16
ALA CA C 18423 44.22 65.52 53.16 1.98
ALA CB C 17147 9.79 28.40 18.98 1.81
ALA N N 20307 77.10 142.81 123.22 3.57
ARG H H 15381 3.64 12.69 8.24 0.61
ARG HA H 12075 1.34 6.10 4.29 0.46
ARG HB2 H 10748 -0.77 3.29 1.80 0.27
ARG HB3 H 9988 -0.74 3.29 1.77 0.28
ARG HG2 H 9546 -0.64 3.51 1.57 0.27
ARG HG3 H 8573 -0.67 3.51 1.55 0.29
ARG HD2 H 9281 0.87 4.69 3.12 0.23
ARG HD3 H 8174 0.89 4.29 3.11 0.25
ARG HE H 3236 2.99 11.88 7.38 0.62
ARG HH11 H 332 5.88 9.82 6.91 0.46
ARG HH12 H 244 6.01 10.73 6.85 0.43
ARG HH21 H 299 5.90 11.35 6.81 0.46
ARG HH22 H 235 5.97 10.18 6.77 0.42
ARG C C 8714 167.44 184.51 176.44 2.05
ARG CA C 12315 43.27 67.98 56.80 2.32
ARG CB C 11142 20.95 42.50 30.66 1.83
ARG CG C 6915 18.22 37.83 27.23 1.19
ARG CD C 7056 29.71 49.06 43.17 0.88
ARG CZ C 178 156.20 177.70 160.09 3.30
ARG N N 13337 103.60 137.60 120.80 3.72
ARG NE N 1544 75.15 98.77 84.68 1.59
ARG NH1 N 52 67.60 87.07 73.62 4.15
ARG NH2 N 48 70.10 85.28 73.41 3.52
ASP H H 17846 4.06 12.61 8.31 0.57
ASP HA H 13726 2.33 6.33 4.60 0.31
ASP HB2 H 12624 -0.39 4.58 2.72 0.27
ASP HB3 H 11992 0.02 4.58 2.67 0.28
ASP C C 10766 166.80 182.70 176.44 1.77
ASP CA C 14839 44.81 62.49 54.68 2.04
ASP CB C 13740 27.48 51.09 40.87 1.64
ASP CG C 236 170.72 183.94 179.24 1.85
ASP N N 16277 101.90 143.52 120.70 3.92
ASN H H 12656 2.61 12.40 8.35 0.62
ASN HA H 10000 1.75 6.43 4.67 0.37
ASN HB2 H 9252 0.23 4.47 2.81 0.31
ASN HB3 H 8831 -0.07 4.47 2.76 0.33
ASN HD21 H 6704 3.55 9.60 7.35 0.48
ASN HD22 H 6650 3.14 10.80 7.14 0.49
ASN C C 7321 167.04 181.90 175.31 1.82
ASN CA C 10287 41.31 61.80 53.55 1.90
ASN CB C 9508 28.64 55.09 38.68 1.68
ASN CG C 715 166.40 181.20 176.77 1.39
ASN N N 11072 101.71 137.49 118.97 4.03
ASN ND2 N 5234 99.60 133.86 112.80 2.29
CYS H H 7093 4.73 12.12 8.40 0.67
CYS HA H 6237 1.64 6.43 4.68 0.56
CYS HB2 H 5946 -0.54 4.65 2.95 0.45
CYS HB3 H 5782 -0.83 4.69 2.90 0.47
CYS HG H 51 0.25 7.39 1.89 1.48
CYS C C 2799 166.73 182.73 174.84 2.06
CYS CA C 3985 42.45 67.64 58.16 3.38
CYS CB C 3606 17.99 62.07 32.83 6.29
CYS N N 4674 100.48 135.89 120.17 4.61
GLU H H 23619 4.24 12.17 8.34 0.60
GLU HA H 18328 1.77 6.29 4.25 0.41
GLU HB2 H 16501 0.34 3.44 2.03 0.21
GLU HB3 H 15141 0.34 3.44 2.00 0.22
GLU HG2 H 15190 0.57 3.77 2.28 0.21
GLU HG3 H 13746 0.45 3.83 2.26 0.21
GLU C C 14734 166.80 183.52 176.93 1.98
GLU CA C 20055 44.35 64.60 57.36 2.10
GLU CB C 18473 18.71 42.33 30.00 1.73
GLU CG C 12207 25.50 50.28 36.09 1.23
GLU CD C 263 173.41 189.46 182.58 2.02
GLU N N 21911 104.54 138.60 120.69 3.51
GLN H H 12577 5.18 12.04 8.22 0.59
GLN HA H 9815 1.60 6.23 4.26 0.43
GLN HB2 H 8816 -0.12 4.00 2.05 0.25
GLN HB3 H 8184 -0.52 4.04 2.02 0.27
GLN HG2 H 8236 0.04 3.66 2.32 0.27
GLN HG3 H 7339 -1.08 3.66 2.30 0.29
GLN HE21 H 6004 3.69 11.11 7.23 0.46
GLN HE22 H 5969 3.59 9.79 7.02 0.45
GLN C C 7587 168.09 182.22 176.36 1.97
GLN CA C 10589 47.87 66.60 56.60 2.14
GLN CB C 9705 20.27 42.20 29.16 1.84
GLN CG C 6486 21.64 41.95 33.77 1.12
GLN CD C 698 171.70 183.54 179.67 1.39
GLN N N 11457 104.65 139.55 119.86 3.63
GLN NE2 N 5051 92.49 124.30 111.87 1.81
GLY H H 22374 3.01 12.22 8.33 0.66
GLY HA2 H 17190 0.86 6.43 3.97 0.38
GLY HA3 H 16090 1.04 6.39 3.90 0.37
GLY C C 12964 163.27 183.16 173.93 1.87
GLY CA C 18234 35.78 58.67 45.36 1.29
GLY N N 19681 94.07 162.19 109.67 3.88
HIS H H 6672 5.24 12.39 8.23 0.69
HIS HA H 5211 1.93 8.90 4.61 0.45
HIS HB2 H 4770 0.37 8.70 3.11 0.36
HIS HB3 H 4596 0.39 8.70 3.05 0.39
HIS HD1 H 255 3.79 17.20 8.83 2.73
HIS HD2 H 3326 3.46 9.01 7.03 0.45
HIS HE1 H 2775 3.21 10.26 7.98 0.51
HIS HE2 H 117 6.58 16.53 9.77 2.66
HIS C C 4009 166.90 182.80 175.28 1.99
HIS CA C 5632 46.01 66.98 56.49 2.35
HIS CB C 5214 18.75 43.30 30.19 2.10
HIS CG C 70 122.67 137.19 131.36 3.35
HIS CD2 C 1791 112.07 159.95 120.40 3.41
HIS CE1 C 1392 104.67 144.54 137.49 2.44
HIS N N 6000 105.00 136.48 119.54 4.04
HIS ND1 N 121 164.64 229.14 195.39 18.23
HIS NE2 N 139 161.70 226.29 182.50 14.67
ILE H H 16000 3.43 11.69 8.28 0.69
ILE HA H 12415 1.32 6.36 4.18 0.56
ILE HB H 11533 -1.28 3.87 1.79 0.29
ILE HG12 H 10344 -2.38 2.69 1.27 0.40
ILE HG13 H 9802 -2.04 2.99 1.21 0.41
ILE HG2 H 10902 -1.14 1.87 0.78 0.27
ILE HD1 H 10929 -1.08 2.82 0.68 0.29
ILE C C 9886 167.00 183.40 175.88 1.95
ILE CA C 13431 51.15 71.70 61.63 2.70
ILE CB C 12350 20.94 51.88 38.62 2.04
ILE CG1 C 8076 12.90 38.39 27.73 1.76
ILE CG2 C 8682 3.45 29.80 17.53 1.42
ILE CD1 C 8729 2.70 29.60 13.46 1.68
ILE N N 14546 99.00 138.12 121.51 4.32
LEU H H 26192 3.01 13.22 8.22 0.65
LEU HA H 20217 1.93 6.24 4.31 0.47
LEU HB2 H 18297 -1.21 3.18 1.62 0.34
LEU HB3 H 17208 -1.21 3.18 1.54 0.36
LEU HG H 16124 -1.06 3.90 1.51 0.33
LEU HD1 H 17907 -1.73 2.36 0.76 0.28
LEU HD2 H 17170 -1.65 2.78 0.74 0.28
LEU C C 15940 167.49 189.78 177.01 2.01
LEU CA C 21905 46.36 65.83 55.66 2.14
LEU CB C 20245 26.40 53.70 42.29 1.88
LEU CG C 12571 15.57 39.56 26.79 1.16
LEU CD1 C 13923 10.95 31.83 24.67 1.62
LEU CD2 C 13155 11.71 30.40 24.10 1.70
LEU N N 23782 40.20 144.55 121.85 3.97
LYS H H 22987 5.11 11.84 8.19 0.61
LYS HA H 17827 1.30 6.17 4.26 0.44
LYS HB2 H 15920 -0.84 4.05 1.78 0.25
LYS HB3 H 14667 -0.97 3.95 1.75 0.27
LYS HG2 H 14205 -1.16 2.99 1.37 0.26
LYS HG3 H 12707 -1.11 4.18 1.36 0.28
LYS HD2 H 12398 -1.68 8.50 1.61 0.23
LYS HD3 H 10693 -1.02 3.61 1.60 0.23
LYS HE2 H 12287 1.25 4.36 2.92 0.19
LYS HE3 H 10410 1.24 4.55 2.91 0.19
LYS HZ H 649 2.41 9.90 7.42 0.65
LYS C C 13175 167.21 185.00 176.68 1.98
LYS CA C 18288 46.60 63.38 56.97 2.20
LYS CB C 16836 21.19 46.60 32.77 1.78
LYS CG C 10699 18.20 36.22 24.92 1.15
LYS CD C 10148 15.37 42.60 28.96 1.18
LYS CE C 9797 30.48 52.20 41.90 0.82
LYS N N 20295 101.10 140.30 121.06 3.79
LYS NZ N 12 31.00 43.69 34.01 3.17
MET H H 6327 4.87 12.46 8.26 0.60
MET HA H 5075 1.13 6.35 4.41 0.47
MET HB2 H 4524 -1.05 3.87 2.03 0.35
MET HB3 H 4173 -0.99 3.20 2.00 0.35
MET HG2 H 4104 -0.36 4.40 2.43 0.36
MET HG3 H 3821 -0.30 4.24 2.40 0.39
MET HE H 2717 -0.21 17.06 1.88 0.48
MET C C 3953 168.20 183.16 176.21 2.09
MET CA C 5580 45.50 66.56 56.14 2.26
MET CB C 5033 20.98 46.46 32.99 2.24
MET CG C 3107 20.46 38.58 32.03 1.26
MET CE C 2196 0.00 41.37 17.19 2.01
MET N N 5802 87.60 134.80 120.08 3.57
PHE H H 11446 4.81 12.18 8.36 0.72
PHE HA H 8790 1.78 6.57 4.61 0.57
PHE HB2 H 8134 0.17 4.46 3.00 0.37
PHE HB3 H 7854 0.53 4.31 2.95 0.38
PHE HD1 H 6781 4.72 8.08 7.06 0.30
PHE HD2 H 5387 4.72 8.15 7.06 0.30
PHE HE1 H 5970 4.10 8.80 7.09 0.31
PHE HE2 H 4828 4.10 8.80 7.09 0.32
PHE HZ H 4265 4.53 9.50 7.01 0.42
PHE C C 6820 166.85 183.77 175.48 1.99
PHE CA C 9359 47.31 69.82 58.14 2.57
PHE CB C 8662 25.52 48.53 39.92 2.09
PHE CG C 98 128.30 152.84 138.19 2.30
PHE CD1 C 3307 118.50 138.70 131.53 1.21
PHE CD2 C 2085 118.50 138.70 131.59 1.15
PHE CE1 C 2818 114.75 135.60 130.67 1.43
PHE CE2 C 1799 118.00 139.70 130.76 1.21
PHE CZ C 2105 116.46 138.60 129.23 1.56
PHE N N 10257 102.20 139.02 120.51 4.14
PRO HA H 9721 1.63 6.05 4.40 0.33
PRO HB2 H 9006 -0.28 4.02 2.07 0.35
PRO HB3 H 8573 -0.58 3.79 2.02 0.36
PRO HG2 H 8082 -0.39 4.42 1.93 0.31
PRO HG3 H 7333 -0.90 4.42 1.91 0.33
PRO HD2 H 8313 0.63 5.36 3.65 0.36
PRO HD3 H 7913 -0.26 5.36 3.62 0.38
PRO C C 7107 168.43 182.30 176.72 1.55
PRO CA C 10244 50.12 70.67 63.33 1.56
PRO CB C 9399 24.69 43.70 31.84 1.19
PRO CG C 6330 18.28 33.90 27.21 1.09
PRO CD C 6369 40.05 58.30 50.36 0.99
PRO N N 254 111.56 145.26 133.85 6.70
SER H H 19154 3.76 13.13 8.28 0.59
SER HA H 15192 1.66 6.44 4.48 0.41
SER HB2 H 13708 1.66 5.41 3.88 0.26
SER HB3 H 12402 1.49 5.01 3.85 0.28
SER HG H 230 0.00 8.97 5.32 1.04
SER C C 11318 164.47 184.88 174.68 1.76
SER CA C 15975 45.13 68.40 58.74 2.10
SER CB C 14503 52.61 73.90 63.79 1.49
SER N N 16956 100.85 133.68 116.30 3.59
THR H H 17138 5.32 11.73 8.24 0.62
THR HA H 13281 0.87 6.36 4.46 0.48
THR HB H 12041 0.92 8.35 4.17 0.33
THR HG1 H 379 0.32 8.21 5.07 1.48
THR HG2 H 11913 -1.19 4.07 1.14 0.23
THR C C 9905 165.50 184.43 174.58 1.77
THR CA C 13873 51.61 72.80 62.23 2.63
THR CB C 12624 33.00 80.22 69.70 1.69
THR CG2 C 8500 11.70 36.73 21.55 1.12
THR N N 15259 97.70 166.48 115.45 4.79
TRP H H 3607 4.49 11.67 8.29 0.79
TRP HA H 2738 2.28 6.52 4.68 0.52
TRP HB2 H 2544 0.42 4.54 3.19 0.36
TRP HB3 H 2435 0.77 4.44 3.14 0.36
TRP HD1 H 2277 4.90 10.75 7.15 0.36
TRP HE1 H 2447 5.80 13.29 10.10 0.55
TRP HE3 H 2040 4.89 8.79 7.33 0.39
TRP HZ2 H 2154 4.90 8.18 7.29 0.32
TRP HZ3 H 1968 3.88 8.90 6.87 0.40
TRP HH2 H 1993 4.53 10.90 6.99 0.39
TRP C C 1949 168.17 181.89 176.14 2.01
TRP CA C 2748 44.69 69.76 57.68 2.58
TRP CB C 2527 21.10 43.02 29.97 2.01
TRP CG C 98 105.30 114.60 110.48 1.70
TRP CD1 C 1145 109.30 132.35 126.49 1.88
TRP CD2 C 77 120.20 130.10 127.50 1.41
TRP CE2 C 67 118.50 177.71 138.66 6.93
TRP CE3 C 969 111.86 137.60 120.51 1.72
TRP CZ2 C 1077 81.81 124.10 114.21 1.51
TRP CZ3 C 973 113.32 138.39 121.39 1.53
TRP CH2 C 1002 91.62 131.54 123.81 1.86
TRP N N 3045 106.44 138.11 121.63 4.18
TRP NE1 N 1737 107.64 139.96 129.39 1.96
TYR H H 9622 4.16 11.96 8.32 0.74
TYR HA H 7491 1.20 6.73 4.62 0.56
TYR HB2 H 6946 0.49 4.70 2.91 0.37
TYR HB3 H 6726 -0.19 4.70 2.85 0.38
TYR HD1 H 6211 4.98 8.53 6.94 0.30
TYR HD2 H 5036 5.12 8.50 6.94 0.30
TYR HE1 H 5960 4.58 7.86 6.71 0.23
TYR HE2 H 4877 4.56 8.50 6.71 0.23
TYR HH H 113 5.99 13.75 9.29 1.41
TYR C C 5266 167.86 182.92 175.42 2.00
TYR CA C 7512 49.08 65.99 58.13 2.55
TYR CB C 6846 28.82 57.73 39.30 2.15
TYR CG C 91 117.70 138.70 129.29 2.49
TYR CD1 C 3001 116.44 138.65 132.76 1.27
TYR CD2 C 1833 113.00 136.70 132.71 1.48
TYR CE1 C 2978 110.70 134.01 117.94 1.25
TYR CE2 C 1823 113.10 134.01 117.93 1.35
TYR CZ C 78 153.54 162.70 156.59 2.09
TYR N N 8268 100.09 144.96 120.63 4.27
VAL H H 20714 3.98 12.59 8.29 0.68
VAL HA H 16088 0.97 6.24 4.18 0.58
VAL HB H 14993 -0.54 3.32 1.99 0.32
VAL HG1 H 14660 -1.09 2.56 0.83 0.26
VAL HG2 H 14223 -2.32 2.78 0.81 0.28
VAL C C 12523 165.65 183.21 175.65 1.90
VAL CA C 17244 50.16 70.02 62.49 2.89
VAL CB C 15874 20.55 45.33 32.71 1.81
VAL CG1 C 11210 13.53 32.27 21.50 1.39
VAL CG2 C 10671 13.58 30.46 21.30 1.59
VAL N N 18856 97.95 143.29 121.13 4.59
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