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 5188534 possible chemical shifts in the BMRB database, 3754614 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: 05-09-2012
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 33519 3.53 11.48 8.19 0.60
ALA HA H 25220 0.87 6.51 4.25 0.44
ALA HB H 23858 -0.88 3.12 1.35 0.25
ALA C C 21365 164.48 187.20 177.75 2.13
ALA CA C 28725 44.22 65.52 53.15 1.98
ALA CB C 27153 0.00 38.70 19.00 1.83
ALA N N 31064 77.10 142.81 123.22 3.53
ARG H H 22933 3.57 12.69 8.24 0.61
ARG HA H 17763 1.34 6.52 4.30 0.46
ARG HB2 H 16033 -0.77 3.49 1.80 0.27
ARG HB3 H 15080 -0.86 3.32 1.76 0.28
ARG HG2 H 14398 -0.72 3.51 1.57 0.27
ARG HG3 H 13155 -0.74 3.51 1.54 0.29
ARG HD2 H 14110 0.96 4.69 3.12 0.24
ARG HD3 H 12712 0.89 4.56 3.10 0.26
ARG HE H 4395 2.99 11.88 7.39 0.65
ARG HH11 H 394 5.88 9.82 6.90 0.46
ARG HH12 H 282 5.99 10.73 6.82 0.41
ARG HH21 H 351 5.90 11.35 6.81 0.48
ARG HH22 H 272 5.97 10.18 6.76 0.39
ARG C C 13867 167.44 184.51 176.41 2.03
ARG CA C 19199 43.27 67.98 56.77 2.31
ARG CB C 17768 20.95 42.50 30.68 1.84
ARG CG C 11416 18.22 40.94 27.21 1.20
ARG CD C 11576 35.05 50.88 43.15 0.89
ARG CZ C 251 156.20 177.70 160.11 3.26
ARG N N 20621 102.78 137.60 120.79 3.68
ARG NE N 2427 67.00 99.81 84.63 1.66
ARG NH1 N 70 67.60 87.79 74.33 5.10
ARG NH2 N 56 70.10 85.28 73.27 3.29
ASP H H 26724 3.56 12.68 8.30 0.58
ASP HA H 20136 2.33 6.33 4.59 0.32
ASP HB2 H 18676 -0.39 4.58 2.72 0.26
ASP HB3 H 17878 -0.23 4.58 2.66 0.28
ASP HD2 H 4 4.65 6.03 5.25 0.58
ASP C C 17105 166.80 182.70 176.41 1.75
ASP CA C 23170 41.88 67.17 54.69 2.04
ASP CB C 21841 27.48 51.09 40.87 1.63
ASP CG C 337 170.72 186.50 179.30 1.82
ASP N N 25002 101.90 143.52 120.64 3.84
ASP OD1 O 20 177.59 180.97 179.66 0.91
ASN H H 18884 2.61 12.40 8.34 0.63
ASN HA H 14651 2.46 6.43 4.67 0.36
ASN HB2 H 13640 0.23 4.47 2.81 0.31
ASN HB3 H 13083 -0.04 4.47 2.75 0.33
ASN HD21 H 10196 3.55 10.38 7.35 0.48
ASN HD22 H 10119 3.05 10.80 7.14 0.49
ASN C C 11698 167.04 181.90 175.27 1.79
ASN CA C 16134 41.31 61.80 53.54 1.89
ASN CB C 15206 26.45 55.09 38.68 1.68
ASN CG C 1067 166.40 183.10 176.77 1.40
ASN N N 17101 101.71 137.49 118.92 4.01
ASN ND2 N 8525 99.40 133.86 112.75 2.23
CYS H H 9941 4.73 12.12 8.39 0.67
CYS HA H 8625 1.64 6.43 4.65 0.55
CYS HB2 H 8265 -0.54 4.72 2.95 0.44
CYS HB3 H 8051 -0.83 4.69 2.89 0.46
CYS HG H 79 0.25 7.39 1.98 1.33
CYS C C 4639 166.73 182.73 174.95 2.07
CYS CA C 6422 42.45 67.64 58.31 3.36
CYS CB C 5993 17.99 62.07 32.48 6.01
CYS N N 7195 100.48 175.10 120.15 4.63
GLU H H 34929 4.20 12.17 8.33 0.59
GLU HA H 26675 1.39 6.29 4.25 0.41
GLU HB2 H 24291 0.34 3.37 2.02 0.21
GLU HB3 H 22651 -0.49 3.33 1.99 0.23
GLU HG2 H 22565 0.53 3.77 2.27 0.21
GLU HG3 H 20790 0.56 3.80 2.25 0.22
GLU HE2 H 1 2.73 2.73 2.73 0.00
GLU C C 22903 166.80 183.52 176.88 1.95
GLU CA C 30664 44.35 64.60 57.33 2.09
GLU CB C 28703 18.71 46.75 30.00 1.73
GLU CG C 19286 25.31 44.34 36.10 1.20
GLU CD C 389 173.41 189.46 182.56 1.87
GLU N N 33044 104.54 138.60 120.67 3.47
GLU OE1 O 1 184.19 184.19 184.19 0.00
GLN H H 18998 3.51 12.04 8.22 0.58
GLN HA H 14738 1.57 6.34 4.27 0.43
GLN HB2 H 13409 -0.10 4.00 2.05 0.25
GLN HB3 H 12666 -0.58 4.04 2.02 0.27
GLN HG2 H 12642 0.09 3.66 2.32 0.27
GLN HG3 H 11528 -0.55 3.66 2.29 0.29
GLN HE21 H 9537 -1.96 11.11 7.23 0.46
GLN HE22 H 9481 3.59 10.35 7.02 0.44
GLN C C 12137 168.09 182.22 176.33 1.96
GLN CA C 16588 47.87 66.60 56.59 2.14
GLN CB C 15526 20.27 42.20 29.17 1.82
GLN CG C 10654 21.64 42.80 33.76 1.12
GLN CD C 1032 171.37 183.54 179.71 1.29
GLN N N 17694 104.10 139.55 119.86 3.58
GLN NE2 N 8386 97.90 124.30 111.86 1.73
GLY H H 33548 3.01 12.22 8.33 0.65
GLY HA2 H 25633 0.84 6.43 3.97 0.37
GLY HA3 H 24177 1.01 6.39 3.90 0.37
GLY C C 21053 163.27 184.32 173.87 1.89
GLY CA C 28959 35.78 58.67 45.35 1.34
GLY N N 30557 42.65 162.19 109.65 3.85
HIS H H 9924 5.12 12.39 8.24 0.68
HIS HA H 7763 1.93 8.90 4.61 0.43
HIS HB2 H 7179 0.17 8.70 3.11 0.35
HIS HB3 H 6942 0.06 8.70 3.04 0.38
HIS HD1 H 328 3.79 17.20 8.67 2.59
HIS HD2 H 5122 3.46 9.01 7.01 0.43
HIS HE1 H 4146 3.21 10.88 7.95 0.48
HIS HE2 H 134 6.57 16.53 9.62 2.60
HIS C C 6271 166.90 183.12 175.25 1.98
HIS CA C 8724 46.01 66.98 56.52 2.32
HIS CB C 8200 18.75 43.30 30.23 2.08
HIS CG C 89 122.67 137.19 131.59 3.28
HIS CD2 C 3221 112.07 159.95 120.46 3.41
HIS CE1 C 2529 104.67 144.54 137.70 2.11
HIS N N 9122 105.00 136.48 119.68 3.99
HIS ND1 N 160 162.04 229.14 194.80 18.58
HIS NE2 N 172 161.70 226.29 182.09 14.07
ILE H H 23941 3.43 11.69 8.27 0.68
ILE HA H 18234 1.32 6.36 4.18 0.56
ILE HB H 17086 -1.28 3.87 1.78 0.29
ILE HG12 H 15503 -2.38 2.69 1.28 0.40
ILE HG13 H 14887 -2.04 2.99 1.19 0.41
ILE HG2 H 16260 -1.33 2.20 0.77 0.27
ILE HD1 H 16407 -1.08 2.82 0.68 0.29
ILE C C 15635 167.00 183.40 175.86 1.93
ILE CA C 20898 51.07 71.86 61.63 2.69
ILE CB C 19510 22.11 51.88 38.60 2.02
ILE CG1 C 12963 12.90 39.05 27.72 1.69
ILE CG2 C 13803 3.45 29.80 17.53 1.36
ILE CD1 C 13962 2.70 29.60 13.43 1.67
ILE N N 22300 99.00 138.12 121.44 4.26
LEU H H 39316 4.08 13.22 8.22 0.65
LEU HA H 29903 1.58 6.42 4.32 0.47
LEU HB2 H 27454 -1.25 3.18 1.61 0.34
LEU HB3 H 26073 -1.47 3.18 1.52 0.36
LEU HG H 24381 -1.06 3.90 1.51 0.33
LEU HD1 H 26992 -1.73 2.36 0.75 0.28
LEU HD2 H 26043 -1.65 2.78 0.73 0.29
LEU C C 25369 167.49 189.78 177.00 1.98
LEU CA C 34146 46.36 65.83 55.64 2.13
LEU CB C 32045 26.40 53.70 42.29 1.88
LEU CG C 20364 15.57 37.70 26.78 1.11
LEU CD1 C 22343 10.95 31.83 24.71 1.59
LEU CD2 C 21329 11.71 30.40 24.04 1.70
LEU N N 36534 98.56 144.55 121.84 3.90
LYS H H 33434 4.11 12.03 8.18 0.60
LYS HA H 25612 1.30 6.54 4.26 0.44
LYS HB2 H 23121 -0.75 4.05 1.78 0.25
LYS HB3 H 21555 -0.97 3.95 1.74 0.27
LYS HG2 H 20886 -1.11 3.13 1.37 0.26
LYS HG3 H 19030 -1.16 3.03 1.35 0.28
LYS HD2 H 18609 -0.67 7.71 1.61 0.22
LYS HD3 H 16418 -1.02 3.61 1.60 0.22
LYS HE2 H 18464 1.25 4.36 2.92 0.19
LYS HE3 H 15934 1.13 4.55 2.91 0.20
LYS HZ H 729 1.95 9.90 7.41 0.67
LYS C C 20726 121.16 185.00 176.66 2.00
LYS CA C 28107 40.73 64.57 56.96 2.20
LYS CB C 26308 21.19 46.60 32.77 1.79
LYS CG C 16967 12.11 36.22 24.89 1.15
LYS CD C 16111 21.24 40.10 28.95 1.09
LYS CE C 15656 31.57 52.20 41.88 0.82
LYS N N 30436 101.10 140.30 121.03 3.76
LYS NZ N 27 29.48 43.69 33.45 2.43
MET H H 9339 4.87 12.46 8.26 0.60
MET HA H 7375 1.13 6.35 4.40 0.47
MET HB2 H 6620 -1.05 3.87 2.03 0.34
MET HB3 H 6155 -0.99 3.22 1.98 0.34
MET HG2 H 6075 -0.36 4.40 2.42 0.35
MET HG3 H 5693 -0.30 4.24 2.39 0.38
MET HE H 4306 -0.21 17.06 1.89 0.46
MET C C 6078 167.40 183.16 176.19 2.09
MET CA C 8458 45.50 66.56 56.11 2.24
MET CB C 7781 20.98 46.46 32.97 2.24
MET CG C 4911 20.46 38.58 32.01 1.26
MET CE C 3717 0.00 37.40 17.07 1.58
MET N N 8759 87.60 135.66 120.06 3.57
PHE H H 16845 4.81 12.18 8.35 0.72
PHE HA H 12749 1.78 6.87 4.62 0.57
PHE HB2 H 11881 0.16 4.46 3.00 0.37
PHE HB3 H 11538 -0.21 4.69 2.93 0.39
PHE HD1 H 10035 4.97 8.15 7.06 0.31
PHE HD2 H 8449 4.97 8.15 7.06 0.31
PHE HE1 H 8814 4.38 8.80 7.08 0.31
PHE HE2 H 7538 4.38 8.80 7.08 0.32
PHE HZ H 6471 4.32 9.50 7.00 0.42
PHE C C 10705 166.85 184.16 175.44 2.00
PHE CA C 14399 47.31 69.82 58.12 2.58
PHE CB C 13499 25.52 48.53 39.96 2.09
PHE CG C 142 23.48 144.00 137.68 9.85
PHE CD1 C 5752 116.95 136.73 131.58 1.19
PHE CD2 C 4122 120.00 138.25 131.61 1.15
PHE CE1 C 5043 114.75 139.56 130.71 1.31
PHE CE2 C 3637 114.70 139.70 130.75 1.13
PHE CZ C 3936 116.46 138.60 129.21 1.43
PHE N N 15544 102.20 139.02 120.42 4.17
PRO HA H 14761 1.63 6.05 4.40 0.33
PRO HB2 H 13811 -0.28 4.35 2.08 0.34
PRO HB3 H 13328 -0.62 3.79 2.00 0.35
PRO HG2 H 12552 -0.47 4.42 1.93 0.31
PRO HG3 H 11559 -0.90 4.42 1.90 0.32
PRO HD2 H 12882 0.63 5.36 3.65 0.35
PRO HD3 H 12334 -0.26 5.36 3.61 0.38
PRO C C 11536 168.38 182.84 176.76 1.51
PRO CA C 16293 50.12 70.67 63.34 1.52
PRO CB C 15242 23.33 43.70 31.85 1.18
PRO CG C 10636 18.28 33.90 27.17 1.09
PRO CD C 10699 40.05 58.30 50.32 0.99
PRO N N 376 110.91 145.26 133.62 7.22
SER H H 29004 2.32 13.13 8.28 0.58
SER HA H 22851 1.58 6.85 4.48 0.40
SER HB2 H 20977 1.74 5.41 3.88 0.25
SER HB3 H 19218 1.60 5.27 3.85 0.27
SER HG H 294 0.00 8.97 5.37 1.01
SER C C 18666 164.47 184.88 174.62 1.73
SER CA C 25583 45.13 68.40 58.73 2.08
SER CB C 23709 46.69 76.39 63.80 1.48
SER N N 26553 95.97 133.68 116.28 3.52
THR H H 25322 5.54 11.73 8.24 0.62
THR HA H 19247 0.87 6.63 4.46 0.48
THR HB H 17623 0.92 8.35 4.17 0.33
THR HG1 H 581 0.32 8.95 4.91 1.59
THR HG2 H 17458 -1.19 3.54 1.14 0.23
THR C C 15727 165.50 184.43 174.54 1.76
THR CA C 21531 51.61 72.80 62.22 2.59
THR CB C 19943 43.10 81.53 69.72 1.68
THR CG2 C 13699 11.70 36.73 21.55 1.11
THR N N 23270 95.77 138.27 115.41 4.76
TRP H H 5426 5.16 11.76 8.29 0.78
TRP HA H 4093 2.24 6.55 4.68 0.52
TRP HB2 H 3832 0.42 4.54 3.19 0.35
TRP HB3 H 3698 0.31 4.44 3.12 0.36
TRP HD1 H 3428 4.90 10.75 7.14 0.35
TRP HE1 H 3688 5.12 14.39 10.08 0.65
TRP HE3 H 3027 4.89 8.92 7.31 0.41
TRP HZ2 H 3222 4.90 8.60 7.28 0.33
TRP HZ3 H 2923 3.88 8.90 6.86 0.40
TRP HH2 H 2973 4.39 10.90 6.98 0.39
TRP C C 3233 168.17 182.30 176.14 2.01
TRP CA C 4389 44.69 69.76 57.68 2.58
TRP CB C 4105 21.10 43.02 30.00 2.01
TRP CG C 110 105.30 116.53 110.60 1.87
TRP CD1 C 2032 108.45 132.35 126.52 1.84
TRP CD2 C 87 120.20 132.62 127.61 1.57
TRP CE2 C 79 113.89 177.71 138.31 6.98
TRP CE3 C 1731 93.34 137.60 120.43 1.78
TRP CZ2 C 1929 109.10 125.70 114.27 1.12
TRP CZ3 C 1746 98.61 138.39 121.35 1.52
TRP CH2 C 1810 112.43 131.54 123.85 1.42
TRP N N 4787 101.97 138.11 121.67 4.16
TRP NE1 N 2853 107.64 144.36 129.31 2.09
TYR H H 14296 4.16 12.01 8.31 0.73
TYR HA H 11032 1.20 6.73 4.62 0.56
TYR HB2 H 10272 0.31 4.70 2.91 0.37
TYR HB3 H 10000 -0.19 4.70 2.84 0.39
TYR HD1 H 9021 4.82 8.53 6.93 0.30
TYR HD2 H 7672 4.97 8.50 6.93 0.30
TYR HE1 H 8595 4.58 7.86 6.70 0.23
TYR HE2 H 7391 4.56 8.50 6.70 0.23
TYR HH H 149 5.99 13.75 9.28 1.35
TYR C C 8505 167.86 184.78 175.41 2.00
TYR CA C 11834 49.08 66.43 58.14 2.52
TYR CB C 11026 28.82 57.73 39.30 2.16
TYR CG C 119 117.70 174.59 129.75 4.71
TYR CD1 C 5148 116.44 141.57 132.76 1.18
TYR CD2 C 3572 113.00 137.80 132.72 1.32
TYR CE1 C 5115 110.70 135.80 117.92 1.20
TYR CE2 C 3531 112.58 134.01 117.90 1.19
TYR CZ C 101 153.54 162.70 156.83 1.93
TYR N N 12790 100.09 144.96 120.51 4.19
VAL H H 31086 3.98 12.59 8.29 0.67
VAL HA H 23816 0.97 6.30 4.18 0.58
VAL HB H 22355 -1.22 3.32 1.98 0.32
VAL HG1 H 21927 -1.12 2.57 0.83 0.26
VAL HG2 H 21417 -1.98 2.78 0.80 0.28
VAL C C 20101 165.65 183.95 175.63 1.90
VAL CA C 27009 50.16 70.34 62.50 2.87
VAL CB C 25305 20.55 45.33 32.72 1.79
VAL CG1 C 18038 13.53 32.27 21.49 1.36
VAL CG2 C 17373 13.58 30.46 21.26 1.55
VAL N N 29074 97.22 143.29 121.12 4.54
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