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 5995331 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: 08-08-2013
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 52879 0.00 69.23 8.19 0.67
ALA HA H 40681 -2.52 17.87 4.25 0.45
ALA HB H 38886 -14.04 5.48 1.35 0.29
ALA C C 33459 0.04 187.20 177.73 3.14
ALA CA C 45755 17.01 123.90 53.17 2.10
ALA CB C 43549 -40.99 99.00 19.07 2.46
ALA N N 49202 0.05 766.00 123.28 6.71
ARG H H 35612 0.01 861.00 8.27 4.56
ARG HA H 28156 1.21 12.57 4.30 0.48
ARG HB2 H 25717 -4.78 27.53 1.79 0.33
ARG HB3 H 24221 -1.13 27.53 1.76 0.34
ARG HG2 H 23162 -1.45 4.20 1.56 0.29
ARG HG3 H 21239 -1.30 5.47 1.54 0.30
ARG HD2 H 22743 -6.44 4.69 3.11 0.28
ARG HD3 H 20554 -0.69 4.79 3.09 0.30
ARG HE H 7877 2.28 116.66 7.49 3.32
ARG HH11 H 725 4.41 10.30 6.90 0.54
ARG HH12 H 539 4.41 10.73 6.83 0.50
ARG HH21 H 636 1.23 11.35 6.79 0.67
ARG HH22 H 512 1.23 10.18 6.77 0.62
ARG C C 21722 0.17 184.96 176.38 3.14
ARG CA C 30263 8.37 103.60 56.77 2.42
ARG CB C 28260 17.74 123.50 30.73 2.21
ARG CG C 18760 12.17 119.40 27.23 1.72
ARG CD C 18998 18.94 135.80 43.16 1.47
ARG CZ C 479 128.85 181.47 160.50 4.28
ARG N N 32261 0.13 177.67 120.75 4.06
ARG NE N 4942 7.28 149.11 91.01 13.84
ARG NH1 N 165 67.60 124.40 79.27 14.03
ARG NH2 N 142 66.20 128.47 79.32 15.95
ASP H H 42282 0.01 17.50 8.30 0.60
ASP HA H 32702 -3.75 8.60 4.59 0.33
ASP HB2 H 30767 -5.20 37.40 2.72 0.58
ASP HB3 H 29455 -1.46 37.20 2.67 0.59
ASP HD2 H 7 1.41 12.30 6.29 3.52
ASP C C 26884 0.11 219.00 176.40 2.45
ASP CA C 36810 36.57 118.90 54.69 2.13
ASP CB C 34991 9.70 180.89 40.90 2.07
ASP CG C 708 6.71 186.50 178.42 11.77
ASP N N 39713 0.06 223.70 120.66 4.46
ASN H H 29459 0.01 448.00 8.35 2.65
ASN HA H 23362 1.75 7.11 4.66 0.37
ASN HB2 H 22051 -0.77 8.88 2.80 0.34
ASN HB3 H 21201 -0.95 5.14 2.75 0.36
ASN HD21 H 16888 1.09 10.38 7.34 0.51
ASN HD22 H 16674 1.47 11.43 7.14 0.53
ASN C C 18184 0.11 185.30 175.23 2.97
ASN CA C 25353 2.20 99.00 53.54 2.01
ASN CB C 24143 1.96 99.00 38.70 2.05
ASN CG C 1918 0.00 183.10 176.45 6.70
ASN N N 26921 0.04 137.49 118.90 4.36
ASN ND2 N 14429 21.04 145.93 112.76 2.83
CYS H H 15411 3.72 12.40 8.38 0.70
CYS HA H 13475 -9.86 43.50 4.68 1.11
CYS HB2 H 13036 -39.82 363.58 3.22 7.60
CYS HB3 H 12688 -44.20 363.58 3.13 6.89
CYS HG H 150 0.10 10.70 2.07 1.53
CYS C C 7321 1.00 186.04 174.85 3.66
CYS CA C 10433 41.91 82.30 58.21 3.37
CYS CB C 9862 17.99 73.92 32.84 6.22
CYS N N 11625 -147.00 628.00 120.65 22.95
GLU H H 54454 0.01 64.68 8.33 0.70
GLU HA H 42532 0.43 31.32 4.25 0.44
GLU HB2 H 39175 -1.47 4.82 2.02 0.22
GLU HB3 H 36614 -1.63 4.08 1.99 0.23
GLU HG2 H 36488 -0.67 4.69 2.27 0.22
GLU HG3 H 33652 -0.10 4.69 2.24 0.23
GLU HE2 H 3 2.73 11.96 7.49 4.62
GLU C C 35385 0.07 190.58 176.83 3.34
GLU CA C 48019 3.77 87.15 57.33 2.18
GLU CB C 45249 9.08 181.95 30.04 2.19
GLU CG C 31592 6.16 119.03 36.12 1.64
GLU CD C 723 36.12 189.46 181.80 7.77
GLU N N 51526 0.04 429.00 120.64 4.49
GLN H H 29249 0.01 66.54 8.22 0.70
GLN HA H 23081 1.57 7.43 4.27 0.44
GLN HB2 H 21255 -1.34 5.18 2.04 0.27
GLN HB3 H 20081 -1.42 20.90 2.01 0.32
GLN HG2 H 20058 -1.76 33.60 2.31 0.36
GLN HG3 H 18341 -1.40 34.95 2.29 0.39
GLN HE21 H 15296 -3.41 23.89 7.22 0.51
GLN HE22 H 15210 2.10 113.70 7.04 1.00
GLN C C 18636 0.07 184.44 176.31 2.95
GLN CA C 25813 4.10 69.63 56.59 2.20
GLN CB C 24365 17.41 79.68 29.21 2.10
GLN CG C 17099 2.43 178.32 33.78 1.88
GLN CD C 1809 21.34 183.54 179.40 6.68
GLN N N 27374 0.08 216.50 119.84 4.02
GLN NE2 N 13596 33.90 155.00 111.86 2.17
GLY H H 52490 -15.30 112.83 8.33 0.85
GLY HA2 H 40780 -3.40 8.64 3.97 0.40
GLY HA3 H 38687 -3.40 7.69 3.89 0.42
GLY C C 32968 1.00 187.39 173.85 3.12
GLY CA C 45625 2.20 108.30 45.38 1.66
GLY N N 48150 0.20 791.00 109.80 8.21
HIS H H 15643 0.02 13.34 8.26 0.75
HIS HA H 12588 0.68 30.68 4.62 0.63
HIS HB2 H 11797 -0.05 45.90 3.18 1.25
HIS HB3 H 11438 -6.20 38.50 3.12 1.20
HIS HD1 H 779 -15.00 86.50 10.51 9.69
HIS HD2 H 8578 -25.85 67.80 7.23 3.79
HIS HE1 H 6853 -26.60 43.80 7.79 2.48
HIS HE2 H 286 -15.00 76.40 11.55 9.04
HIS C C 9644 1.00 184.20 175.15 4.28
HIS CA C 13719 11.40 176.90 56.55 2.84
HIS CB C 12956 17.80 80.78 30.29 2.41
HIS CG C 146 71.30 139.83 131.42 6.16
HIS CD2 C 5288 7.19 159.95 119.91 5.79
HIS CE1 C 4155 8.27 166.28 137.27 5.38
HIS N N 14246 0.20 159.14 119.67 4.50
HIS ND1 N 574 64.90 261.01 193.69 34.46
HIS NE2 N 529 17.00 257.57 179.95 21.48
ILE H H 36909 0.01 11.69 8.27 0.70
ILE HA H 28764 -9.00 6.37 4.18 0.58
ILE HB H 27211 -2.44 38.70 1.78 0.44
ILE HG12 H 24797 -10.10 7.74 1.26 0.48
ILE HG13 H 23813 -10.10 9.71 1.19 0.51
ILE HG2 H 25972 -3.62 6.23 0.77 0.32
ILE HD1 H 26107 -4.15 8.80 0.67 0.34
ILE C C 23938 0.09 184.75 175.84 3.02
ILE CA C 32576 30.90 77.93 61.62 2.75
ILE CB C 30617 18.10 87.68 38.61 2.22
ILE CG1 C 21058 8.00 74.78 27.71 2.06
ILE CG2 C 22430 0.79 114.15 17.57 2.02
ILE CD1 C 22567 1.02 79.34 13.50 2.48
ILE N N 34615 0.05 531.00 121.44 6.09
LEU H H 61095 0.01 13.22 8.23 0.66
LEU HA H 47261 0.51 119.41 4.32 0.71
LEU HB2 H 43714 -1.52 8.02 1.61 0.37
LEU HB3 H 41708 -1.79 8.39 1.52 0.38
LEU HG H 39149 -2.08 5.70 1.50 0.35
LEU HD1 H 43071 -3.42 30.18 0.75 0.35
LEU HD2 H 41460 -3.42 24.50 0.72 0.38
LEU C C 39214 0.07 228.49 176.98 2.94
LEU CA C 53635 14.37 85.60 55.65 2.20
LEU CB C 50563 16.38 93.18 42.30 2.06
LEU CG C 33010 15.30 75.28 26.81 1.56
LEU CD1 C 36147 0.73 120.70 24.72 2.04
LEU CD2 C 34469 0.62 116.30 24.10 2.11
LEU N N 57135 0.04 627.00 122.02 9.36
LYS H H 51904 0.00 64.42 8.18 0.67
LYS HA H 40822 0.27 8.60 4.26 0.45
LYS HB2 H 37217 -1.42 35.97 1.77 0.33
LYS HB3 H 34716 -1.40 35.97 1.74 0.34
LYS HG2 H 33654 -1.45 29.88 1.36 0.32
LYS HG3 H 30598 -1.83 29.88 1.35 0.33
LYS HD2 H 30009 -1.68 119.62 1.61 0.79
LYS HD3 H 26380 -2.02 41.68 1.60 0.38
LYS HE2 H 29571 -0.49 8.37 2.91 0.22
LYS HE3 H 25447 -0.05 6.83 2.90 0.23
LYS HZ H 1177 -10.90 10.51 7.30 1.19
LYS C C 31844 0.11 996.25 176.63 5.77
LYS CA C 43885 22.02 86.72 56.95 2.26
LYS CB C 41368 -26.69 229.20 32.81 2.27
LYS CG C 27833 2.90 77.38 24.92 1.60
LYS CD C 26360 15.37 77.48 28.97 1.54
LYS CE C 25520 12.03 89.98 41.89 1.36
LYS N N 47341 0.04 217.00 121.00 4.32
LYS NZ N 157 1.95 177.20 48.41 34.05
MET H H 14497 0.02 19.97 8.26 0.63
MET HA H 11770 -0.93 313.57 4.43 2.89
MET HB2 H 10671 -9.84 33.75 2.03 0.59
MET HB3 H 10008 -2.70 12.94 1.99 0.50
MET HG2 H 9842 -33.86 32.70 2.35 1.85
MET HG3 H 9240 -33.86 31.70 2.32 1.99
MET HE H 7115 -24.86 10.20 1.70 2.00
MET C C 9540 2.20 183.25 176.18 2.79
MET CA C 13404 36.03 85.33 56.15 2.31
MET CB C 12448 0.20 83.38 33.00 2.49
MET CG C 8176 2.30 81.18 32.04 1.73
MET CE C 6194 8.90 71.16 17.19 2.49
MET N N 13709 0.20 221.00 120.01 4.79
PHE H H 26539 0.01 12.18 8.35 0.74
PHE HA H 20578 1.45 59.70 4.62 0.70
PHE HB2 H 19329 0.16 7.98 2.99 0.39
PHE HB3 H 18822 -0.21 12.72 2.93 0.41
PHE HD1 H 16518 2.02 9.76 7.03 0.42
PHE HD2 H 13716 2.02 9.76 7.03 0.43
PHE HE1 H 14574 -2.84 14.08 7.05 0.49
PHE HE2 H 12277 0.14 12.90 7.05 0.49
PHE HZ H 10519 -7.14 43.62 6.99 0.79
PHE C C 16842 0.09 187.61 175.44 2.86
PHE CA C 22919 4.92 73.43 58.12 2.66
PHE CB C 21695 21.40 137.00 39.99 2.38
PHE CG C 250 7.23 152.84 136.94 13.01
PHE CD1 C 9471 19.15 143.45 131.35 4.08
PHE CD2 C 6731 19.15 138.70 131.38 3.90
PHE CE1 C 8332 51.32 139.56 130.49 3.81
PHE CE2 C 5915 51.32 139.70 130.57 3.34
PHE CZ C 6383 7.35 138.60 129.02 3.91
PHE N N 24659 0.07 229.00 120.41 4.60
PRO HA H 23302 0.74 135.80 4.39 0.93
PRO HB2 H 21926 -1.50 5.63 2.07 0.37
PRO HB3 H 21139 -3.48 6.10 1.99 0.39
PRO HG2 H 19952 -2.35 4.92 1.92 0.35
PRO HG3 H 18387 -1.52 4.92 1.89 0.36
PRO HD2 H 20548 -6.56 7.67 3.63 0.47
PRO HD3 H 19757 -6.56 6.30 3.59 0.50
PRO C C 17540 0.05 183.52 176.66 3.76
PRO CA C 25347 4.19 176.83 63.32 2.26
PRO CB C 23952 6.11 81.08 31.88 1.78
PRO CG C 17178 18.28 76.28 27.24 1.80
PRO CD C 17313 4.99 98.58 50.31 1.94
PRO N N 748 31.27 430.00 138.53 37.87
SER H H 44665 -15.30 13.13 8.28 0.62
SER HA H 35776 1.43 58.74 4.48 0.51
SER HB2 H 33130 0.61 8.20 3.87 0.28
SER HB3 H 30438 0.61 5.93 3.84 0.29
SER HG H 595 0.00 11.36 5.52 1.26
SER C C 28810 0.25 197.10 174.61 2.38
SER CA C 39882 24.40 175.20 58.72 2.21
SER CB C 37265 -939.28 171.73 63.72 5.66
SER N N 41222 0.00 196.20 116.29 3.94
THR H H 39603 0.02 115.48 8.24 0.85
THR HA H 30964 -1.50 7.23 4.46 0.49
THR HB H 28795 0.09 73.47 4.17 0.86
THR HG1 H 1067 0.32 11.01 5.33 1.33
THR HG2 H 28514 -12.10 22.21 1.14 0.34
THR C C 24667 60.89 185.92 174.52 2.33
THR CA C 34228 41.04 92.66 62.25 2.65
THR CB C 32035 -939.28 629.21 69.61 6.94
THR CG2 C 23019 11.70 175.60 21.59 2.02
THR N N 36747 0.20 402.00 115.52 6.97
TRP H H 9065 5.13 17.32 8.28 0.79
TRP HA H 7035 2.24 11.41 4.69 0.54
TRP HB2 H 6678 0.42 5.35 3.18 0.35
TRP HB3 H 6477 0.31 4.49 3.11 0.37
TRP HD1 H 5991 4.69 10.75 7.13 0.37
TRP HE1 H 6479 -1.28 18.00 10.07 0.73
TRP HE3 H 5292 1.85 10.44 7.28 0.55
TRP HZ2 H 5682 2.63 10.81 7.26 0.44
TRP HZ3 H 5123 0.76 8.90 6.83 0.51
TRP HH2 H 5256 2.84 10.90 6.94 0.49
TRP C C 5411 57.52 184.30 176.15 2.59
TRP CA C 7379 33.74 87.02 57.68 2.66
TRP CB C 6973 1.60 112.01 30.12 2.81
TRP CG C 193 27.38 116.53 110.29 6.89
TRP CD1 C 3669 30.24 158.33 126.31 3.99
TRP CD2 C 129 120.20 139.10 128.17 1.93
TRP CE2 C 165 113.89 177.71 138.38 7.04
TRP CE3 C 3125 40.14 155.09 120.23 3.74
TRP CZ2 C 3527 7.38 144.03 114.05 4.01
TRP CZ3 C 3156 50.12 161.54 121.21 3.34
TRP CH2 C 3301 47.65 160.82 123.62 3.69
TRP N N 8104 25.80 207.70 121.64 4.51
TRP NE1 N 5204 0.53 249.50 129.26 3.56
TYR H H 22820 0.02 12.01 8.31 0.74
TYR HA H 17872 0.44 7.16 4.62 0.57
TYR HB2 H 16819 -21.23 23.28 2.89 0.50
TYR HB3 H 16429 -21.23 23.28 2.83 0.51
TYR HD1 H 14772 0.19 9.39 6.91 0.39
TYR HD2 H 12350 0.92 10.50 6.91 0.40
TYR HE1 H 14056 0.08 11.80 6.69 0.33
TYR HE2 H 11854 0.43 11.70 6.69 0.34
TYR HH H 322 3.07 31.00 9.18 2.18
TYR C C 13723 2.20 184.78 175.36 3.36
TYR CA C 19130 2.20 69.56 58.13 2.63
TYR CB C 17947 18.38 175.51 39.33 2.79
TYR CG C 243 7.11 174.59 128.54 10.49
TYR CD1 C 8616 19.59 141.57 132.43 4.83
TYR CD2 C 5816 19.59 138.29 132.43 4.75
TYR CE1 C 8549 40.44 159.57 117.71 3.90
TYR CE2 C 5753 42.40 154.10 117.78 3.00
TYR CZ C 187 6.84 162.70 154.70 17.19
TYR N N 20685 0.20 818.00 120.95 14.89
VAL H H 48460 0.02 15.05 8.28 0.69
VAL HA H 37956 -2.83 54.97 4.18 0.66
VAL HB H 36025 -27.48 31.75 1.98 0.49
VAL HG1 H 35247 -27.20 24.20 0.82 0.36
VAL HG2 H 34525 -27.20 56.56 0.80 0.48
VAL C C 31286 1.00 185.04 175.63 2.40
VAL CA C 42714 29.56 91.71 62.53 2.92
VAL CB C 40227 17.21 83.58 32.75 2.00
VAL CG1 C 29643 -7.40 117.16 21.53 1.92
VAL CG2 C 28612 -5.65 121.47 21.33 2.07
VAL N N 45676 0.20 529.00 121.23 8.53
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