Statistics Calculated for All Chemical Shifts from Atoms in the 20 Common Amino Acids
The statistics presented in this table were calculated from the full BMRB database. This includes paramagnetic proteins,
proteins with aromatic prosthetic groups, and entries where chemical shifts are reported relative to uncommon chemical
shift references. The calculated statistics are drived from a total of 6051591 chemical shifts.
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: 09-12-2013
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 53400 0.00 69.23 8.19 0.67
ALA HA H 41079 -2.52 17.87 4.25 0.45
ALA HB H 39240 -14.04 5.48 1.35 0.29
ALA C C 33799 0.04 187.20 177.73 3.13
ALA CA C 46241 17.01 123.90 53.18 2.10
ALA CB C 43998 -40.99 99.00 19.07 2.45
ALA N N 49729 0.05 766.00 123.28 6.68
ARG H H 35977 0.01 12.73 8.24 0.63
ARG HA H 28431 1.21 12.57 4.30 0.48
ARG HB2 H 25955 -4.78 27.53 1.79 0.33
ARG HB3 H 24463 -1.13 27.53 1.76 0.34
ARG HG2 H 23386 -1.45 4.20 1.56 0.29
ARG HG3 H 21467 -1.30 5.47 1.54 0.30
ARG HD2 H 22962 -6.44 4.69 3.11 0.28
ARG HD3 H 20771 -0.69 4.79 3.09 0.30
ARG HE H 7936 2.28 116.66 7.49 3.30
ARG HH11 H 732 4.41 10.30 6.90 0.54
ARG HH12 H 544 4.41 10.73 6.83 0.50
ARG HH21 H 640 1.23 11.35 6.79 0.67
ARG HH22 H 513 1.23 10.18 6.78 0.62
ARG C C 21951 0.17 184.96 176.39 3.13
ARG CA C 30592 8.37 103.60 56.77 2.42
ARG CB C 28568 17.74 123.50 30.73 2.20
ARG CG C 18937 12.17 119.40 27.23 1.72
ARG CD C 19169 18.94 135.80 43.18 1.58
ARG CZ C 486 128.85 181.47 160.49 4.25
ARG N N 32609 0.13 177.67 120.75 4.06
ARG NE N 4978 7.28 149.11 90.98 13.82
ARG NH1 N 168 67.60 124.40 79.24 13.92
ARG NH2 N 145 66.20 128.47 79.20 15.81
ASP H H 42677 -0.35 17.50 8.30 0.61
ASP HA H 32960 -3.75 8.60 4.59 0.33
ASP HB2 H 30998 -5.20 37.40 2.72 0.58
ASP HB3 H 29691 -1.46 37.20 2.67 0.59
ASP HD2 H 7 1.41 12.30 6.29 3.52
ASP C C 27115 0.11 219.00 176.40 2.58
ASP CA C 37152 36.57 118.90 54.69 2.13
ASP CB C 35312 9.70 180.89 40.90 2.06
ASP CG C 710 6.71 186.50 178.23 12.86
ASP N N 40092 0.06 223.70 120.65 4.45
ASN H H 29786 0.01 448.00 8.35 2.63
ASN HA H 23616 1.75 7.11 4.66 0.37
ASN HB2 H 22283 -0.77 8.88 2.80 0.34
ASN HB3 H 21436 -0.95 5.14 2.74 0.36
ASN HD21 H 17070 1.09 10.38 7.34 0.51
ASN HD22 H 16855 1.47 11.43 7.14 0.53
ASN C C 18390 0.11 185.30 175.23 2.96
ASN CA C 25646 2.20 99.00 53.55 2.00
ASN CB C 24423 1.96 99.00 38.70 2.04
ASN CG C 1921 0.00 183.10 176.45 6.69
ASN N N 27231 0.04 137.49 118.90 4.35
ASN ND2 N 14580 21.04 145.93 112.76 2.82
CYS H H 15545 3.72 12.40 8.38 0.70
CYS HA H 13585 -9.86 43.50 4.68 1.11
CYS HB2 H 13140 -39.82 363.58 3.21 7.57
CYS HB3 H 12792 -44.20 363.58 3.13 6.87
CYS HG H 151 0.10 10.70 2.07 1.52
CYS C C 7384 1.00 186.04 174.86 3.65
CYS CA C 10539 41.91 82.30 58.21 3.37
CYS CB C 9962 17.99 73.92 32.85 6.22
CYS N N 11726 -147.00 628.00 120.65 22.86
GLU H H 54931 0.01 64.68 8.33 0.70
GLU HA H 42904 0.43 31.32 4.25 0.44
GLU HB2 H 39488 -1.47 4.82 2.02 0.22
GLU HB3 H 36944 -1.63 4.08 1.99 0.23
GLU HG2 H 36794 -0.67 4.69 2.27 0.22
GLU HG3 H 33963 -0.10 4.69 2.24 0.23
GLU HE2 H 5 2.73 11.96 7.17 3.30
GLU C C 35700 0.07 190.58 176.84 3.33
GLU CA C 48453 3.77 87.15 57.34 2.18
GLU CB C 45654 9.08 181.95 30.04 2.18
GLU CG C 31877 6.16 119.03 36.12 1.63
GLU CD C 728 36.12 189.46 181.81 7.74
GLU N N 52001 0.04 429.00 120.64 4.48
GLN H H 29553 0.01 66.54 8.22 0.70
GLN HA H 23273 1.57 7.43 4.27 0.44
GLN HB2 H 21411 -1.34 5.18 2.04 0.27
GLN HB3 H 20243 -1.42 20.90 2.01 0.32
GLN HG2 H 20206 -1.76 33.60 2.31 0.35
GLN HG3 H 18503 -1.40 34.95 2.29 0.39
GLN HE21 H 15393 -3.41 23.89 7.22 0.51
GLN HE22 H 15308 2.10 113.70 7.04 0.99
GLN C C 18804 0.07 184.44 176.31 2.94
GLN CA C 26076 4.10 69.63 56.60 2.19
GLN CB C 24615 17.41 79.68 29.21 2.09
GLN CG C 17245 2.43 178.32 33.78 1.87
GLN CD C 1818 21.34 183.54 179.40 6.67
GLN N N 27682 0.08 216.50 119.84 4.01
GLN NE2 N 13687 33.90 155.00 111.86 2.16
GLY H H 52995 -15.30 112.83 8.33 0.85
GLY HA2 H 41141 -3.40 8.64 3.97 0.40
GLY HA3 H 39051 -3.40 7.69 3.89 0.42
GLY C C 33283 1.00 187.39 173.85 3.10
GLY CA C 46084 2.20 108.30 45.39 1.65
GLY N N 48633 0.20 791.00 109.79 8.18
HIS H H 15813 -0.30 13.34 8.26 0.75
HIS HA H 12734 0.68 30.68 4.62 0.63
HIS HB2 H 11931 -0.05 45.90 3.18 1.24
HIS HB3 H 11572 -6.20 38.50 3.12 1.19
HIS HD1 H 786 -15.00 86.50 10.51 9.65
HIS HD2 H 8677 -25.85 67.80 7.23 3.77
HIS HE1 H 6920 -26.60 43.80 7.79 2.47
HIS HE2 H 289 -15.00 76.40 11.53 9.00
HIS C C 9746 1.00 184.20 175.16 4.26
HIS CA C 13875 11.40 176.90 56.55 2.83
HIS CB C 13108 17.80 80.78 30.29 2.41
HIS CG C 146 71.30 139.83 131.42 6.16
HIS CD2 C 5355 7.19 159.95 119.93 5.77
HIS CE1 C 4199 8.27 166.28 137.29 5.36
HIS N N 14406 0.20 159.14 119.68 4.51
HIS ND1 N 583 64.90 261.01 193.40 34.28
HIS NE2 N 537 17.00 257.57 180.36 21.66
ILE H H 37231 0.01 11.69 8.27 0.70
ILE HA H 29025 -9.00 6.37 4.17 0.58
ILE HB H 27452 -2.44 38.70 1.78 0.44
ILE HG12 H 25020 -10.10 7.74 1.26 0.48
ILE HG13 H 24024 -10.10 9.71 1.19 0.51
ILE HG2 H 26180 -3.62 6.23 0.77 0.32
ILE HD1 H 26337 -4.15 8.80 0.67 0.34
ILE C C 24119 0.09 184.75 175.83 3.35
ILE CA C 32858 30.90 77.93 61.63 2.75
ILE CB C 30875 18.10 87.68 38.62 2.22
ILE CG1 C 21244 8.00 74.78 27.71 2.06
ILE CG2 C 22624 0.79 114.15 17.57 2.01
ILE CD1 C 22775 1.02 79.34 13.50 2.47
ILE N N 34923 0.05 531.00 121.44 6.07
LEU H H 61754 -0.30 13.22 8.22 0.66
LEU HA H 47764 0.51 119.41 4.31 0.71
LEU HB2 H 44157 -1.52 8.02 1.61 0.37
LEU HB3 H 42160 -1.79 8.39 1.52 0.38
LEU HG H 39565 -2.08 5.70 1.51 0.35
LEU HD1 H 43518 -3.42 30.18 0.75 0.35
LEU HD2 H 41884 -3.42 24.50 0.73 0.38
LEU C C 39595 0.07 228.49 176.99 2.93
LEU CA C 54206 14.37 158.32 55.66 2.24
LEU CB C 51096 16.38 93.18 42.30 2.05
LEU CG C 33354 15.30 75.28 26.81 1.56
LEU CD1 C 36506 0.73 120.70 24.73 2.03
LEU CD2 C 34802 0.62 116.30 24.10 2.10
LEU N N 57751 0.04 627.00 122.01 9.32
LYS H H 52391 0.00 64.42 8.18 0.67
LYS HA H 41213 0.27 8.60 4.26 0.45
LYS HB2 H 37553 -1.42 35.97 1.77 0.32
LYS HB3 H 35060 -1.40 35.97 1.74 0.34
LYS HG2 H 33969 -1.45 29.88 1.36 0.32
LYS HG3 H 30928 -1.83 29.88 1.35 0.33
LYS HD2 H 30297 -1.68 119.62 1.61 0.78
LYS HD3 H 26692 -2.02 41.68 1.60 0.38
LYS HE2 H 29861 -0.49 8.37 2.91 0.22
LYS HE3 H 25752 -0.05 6.83 2.90 0.22
LYS HZ H 1189 -10.90 10.51 7.30 1.19
LYS C C 32114 0.11 996.25 176.64 5.74
LYS CA C 44308 22.02 86.72 56.95 2.25
LYS CB C 41774 -26.69 229.20 32.81 2.26
LYS CG C 28106 2.90 77.38 24.92 1.60
LYS CD C 26614 15.37 77.48 28.97 1.54
LYS CE C 25759 12.03 89.98 41.90 1.49
LYS N N 47799 0.04 217.00 121.00 4.31
LYS NZ N 157 1.95 177.20 48.41 34.05
MET H H 14632 -0.21 19.97 8.26 0.63
MET HA H 11864 -0.93 313.57 4.43 2.88
MET HB2 H 10746 -9.84 33.75 2.03 0.59
MET HB3 H 10085 -2.70 12.94 1.99 0.50
MET HG2 H 9916 -33.86 32.70 2.35 1.84
MET HG3 H 9312 -33.86 31.70 2.32 1.98
MET HE H 7176 -24.86 10.20 1.69 2.03
MET C C 9620 2.20 183.25 176.18 2.79
MET CA C 13521 36.03 85.33 56.15 2.31
MET CB C 12557 0.20 83.38 33.00 2.48
MET CG C 8238 2.30 81.18 32.04 1.72
MET CE C 6249 8.90 71.16 17.19 2.48
MET N N 13834 0.20 221.00 120.01 4.78
PHE H H 26796 -0.50 12.18 8.35 0.74
PHE HA H 20750 1.45 59.70 4.62 0.70
PHE HB2 H 19477 0.16 7.98 2.99 0.39
PHE HB3 H 18971 -0.21 12.72 2.93 0.41
PHE HD1 H 16613 2.02 9.76 7.03 0.42
PHE HD2 H 13820 2.02 9.76 7.03 0.43
PHE HE1 H 14657 -2.84 14.08 7.05 0.49
PHE HE2 H 12367 0.14 12.90 7.05 0.49
PHE HZ H 10578 -7.14 43.62 6.99 0.79
PHE C C 16999 0.09 187.61 175.45 2.85
PHE CA C 23147 4.92 73.43 58.12 2.65
PHE CB C 21906 21.40 137.00 39.99 2.37
PHE CG C 250 7.23 152.84 136.94 13.01
PHE CD1 C 9515 19.15 143.45 131.35 4.07
PHE CD2 C 6781 19.15 138.70 131.39 3.89
PHE CE1 C 8369 51.32 139.56 130.49 3.80
PHE CE2 C 5957 51.32 139.70 130.58 3.33
PHE CZ C 6424 7.35 138.60 129.03 3.91
PHE N N 24898 0.07 229.00 120.41 4.59
PRO HA H 23511 0.74 135.80 4.39 0.93
PRO HB2 H 22107 -1.50 5.63 2.07 0.37
PRO HB3 H 21321 -3.48 6.10 1.99 0.39
PRO HG2 H 20130 -2.35 4.92 1.92 0.35
PRO HG3 H 18561 -1.52 4.92 1.89 0.36
PRO HD2 H 20730 -6.56 7.67 3.63 0.47
PRO HD3 H 19935 -6.56 6.30 3.59 0.50
PRO C C 17708 0.05 183.52 176.66 3.74
PRO CA C 25563 4.19 176.83 63.32 2.26
PRO CB C 24158 6.11 81.08 31.88 1.78
PRO CG C 17343 18.28 76.28 27.24 1.79
PRO CD C 17487 4.99 98.58 50.31 1.93
PRO N N 799 31.27 430.00 138.47 36.65
SER H H 45087 -15.30 13.13 8.28 0.62
SER HA H 36104 1.43 58.74 4.48 0.51
SER HB2 H 33411 0.61 8.20 3.87 0.28
SER HB3 H 30730 0.61 5.93 3.84 0.29
SER HG H 605 0.00 11.36 5.52 1.25
SER C C 29107 0.25 197.10 174.62 2.37
SER CA C 40298 24.40 175.20 58.73 2.21
SER CB C 37647 -939.28 171.73 63.72 5.62
SER N N 41667 0.03 196.20 116.29 3.89
THR H H 40002 0.02 115.48 8.24 0.84
THR HA H 31270 -1.50 7.23 4.46 0.49
THR HB H 29075 0.09 73.47 4.17 0.85
THR HG1 H 1098 0.32 11.01 5.34 1.32
THR HG2 H 28789 -12.10 22.21 1.14 0.34
THR C C 24909 60.89 185.92 174.52 2.32
THR CA C 34581 41.04 92.66 62.26 2.65
THR CB C 32370 -939.28 629.21 69.61 6.91
THR CG2 C 23256 11.70 175.60 21.59 2.01
THR N N 37132 0.20 402.00 115.51 6.95
TRP H H 9161 5.13 17.32 8.28 0.79
TRP HA H 7110 2.24 11.41 4.69 0.54
TRP HB2 H 6740 0.42 5.35 3.18 0.35
TRP HB3 H 6536 0.31 4.49 3.11 0.37
TRP HD1 H 6048 4.69 10.75 7.13 0.37
TRP HE1 H 6531 -1.28 18.00 10.08 0.73
TRP HE3 H 5340 1.85 10.82 7.28 0.55
TRP HZ2 H 5735 2.63 10.81 7.26 0.44
TRP HZ3 H 5169 0.76 8.90 6.83 0.51
TRP HH2 H 5303 2.84 10.90 6.94 0.49
TRP C C 5476 57.52 184.30 176.15 2.58
TRP CA C 7468 33.74 87.02 57.68 2.65
TRP CB C 7059 1.60 112.01 30.12 2.80
TRP CG C 193 27.38 116.53 110.29 6.89
TRP CD1 C 3711 30.24 158.33 126.30 4.07
TRP CD2 C 130 120.20 139.10 128.17 1.92
TRP CE2 C 165 113.89 177.71 138.38 7.04
TRP CE3 C 3157 40.14 155.09 120.22 3.82
TRP CZ2 C 3565 7.38 144.03 114.05 4.10
TRP CZ3 C 3190 50.12 161.54 121.20 3.44
TRP CH2 C 3335 47.65 160.82 123.63 3.67
TRP N N 8187 25.80 207.70 121.64 4.52
TRP NE1 N 5245 0.53 249.50 129.26 3.55
TYR H H 23026 0.02 12.01 8.31 0.74
TYR HA H 18014 0.44 7.16 4.62 0.57
TYR HB2 H 16935 -21.23 23.28 2.89 0.50
TYR HB3 H 16545 -21.23 23.28 2.83 0.51
TYR HD1 H 14852 0.19 9.39 6.91 0.39
TYR HD2 H 12438 0.92 10.50 6.91 0.40
TYR HE1 H 14127 0.08 11.80 6.69 0.33
TYR HE2 H 11932 0.43 11.70 6.69 0.34
TYR HH H 323 3.07 31.00 9.18 2.18
TYR C C 13855 2.20 184.78 175.37 3.35
TYR CA C 19313 2.20 69.56 58.13 2.63
TYR CB C 18115 18.38 175.51 39.33 2.78
TYR CG C 243 7.11 174.59 128.54 10.49
TYR CD1 C 8657 19.59 141.57 132.43 4.82
TYR CD2 C 5845 19.59 138.29 132.43 4.74
TYR CE1 C 8590 40.44 159.57 117.72 3.89
TYR CE2 C 5782 42.40 154.10 117.79 2.99
TYR CZ C 187 6.84 162.70 154.70 17.19
TYR N N 20873 0.20 818.00 120.94 14.83
VAL H H 48916 -0.41 15.05 8.28 0.70
VAL HA H 38279 -2.83 54.97 4.18 0.66
VAL HB H 36329 -27.48 31.75 1.98 0.49
VAL HG1 H 35557 -27.20 24.20 0.82 0.36
VAL HG2 H 34805 -27.20 56.56 0.80 0.48
VAL C C 31520 1.00 185.04 175.64 2.40
VAL CA C 43085 29.56 91.71 62.53 2.92
VAL CB C 40563 17.21 83.58 32.75 2.00
VAL CG1 C 29892 -7.40 117.16 21.54 1.91
VAL CG2 C 28837 -5.65 121.47 21.33 2.06
VAL N N 46096 0.20 529.00 121.23 8.50
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