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 3443106 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: 06-30-2009
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 31348 0.95 14.80 8.19 0.62
ALA HA H 24822 -2.52 8.62 4.26 0.45
ALA HB H 23505 -14.04 5.48 1.35 0.29
ALA C C 18198 49.30 187.20 177.71 2.66
ALA CA C 25457 17.01 99.00 53.15 2.10
ALA CB C 23889 -40.99 99.00 19.04 2.27
ALA N N 28083 8.63 766.00 123.37 8.16
ARG H H 20981 0.00 12.73 8.24 0.64
ARG HA H 17013 0.00 12.57 4.29 0.49
ARG HB2 H 15338 -4.78 27.53 1.79 0.36
ARG HB3 H 14240 -1.13 27.53 1.76 0.37
ARG HG2 H 13689 -1.45 4.20 1.56 0.29
ARG HG3 H 12345 -0.91 5.47 1.54 0.30
ARG HD2 H 13350 -6.44 4.69 3.11 0.29
ARG HD3 H 11797 -0.49 4.66 3.10 0.30
ARG HE H 5204 0.00 118.45 8.87 12.69
ARG HH11 H 528 4.41 10.30 6.89 0.53
ARG HH12 H 383 4.41 10.73 6.81 0.51
ARG HH21 H 468 1.23 11.35 6.77 0.64
ARG HH22 H 374 1.23 10.18 6.73 0.67
ARG C C 11793 2.20 184.51 176.39 3.28
ARG CA C 16832 8.37 103.60 56.76 2.47
ARG CB C 15391 20.95 123.50 30.73 2.30
ARG CG C 10025 12.17 119.40 27.25 2.01
ARG CD C 10232 23.20 135.80 43.18 1.77
ARG CZ C 299 128.85 180.80 160.75 4.95
ARG N N 18226 64.79 176.86 120.79 3.86
ARG NE N 2926 7.19 149.11 90.31 19.42
ARG NH1 N 110 7.24 112.50 75.49 14.21
ARG NH2 N 94 66.20 128.47 76.79 12.46
ASP H H 24737 3.56 12.61 8.32 0.59
ASP HA H 19776 0.25 8.60 4.60 0.33
ASP HB2 H 18386 -0.39 37.40 2.74 0.72
ASP HB3 H 17426 -1.46 37.20 2.68 0.73
ASP HD2 H 2 1.41 12.30 6.85 7.70
ASP C C 14725 52.77 219.00 176.42 2.17
ASP CA C 20533 39.80 86.07 54.68 2.12
ASP CB C 19207 9.70 180.89 40.92 2.35
ASP CG C 438 27.50 183.94 178.53 10.54
ASP N N 22477 8.49 223.70 120.77 4.28
ASN H H 17377 2.61 448.00 8.37 3.40
ASN HA H 14234 1.75 7.11 4.67 0.38
ASN HB2 H 13311 -0.64 5.58 2.81 0.33
ASN HB3 H 12712 -0.69 5.14 2.75 0.37
ASN HD21 H 9837 2.06 10.24 7.36 0.50
ASN HD22 H 9768 3.00 11.43 7.13 0.52
ASN C C 9934 2.20 184.27 175.25 2.68
ASN CA C 14109 2.20 99.00 53.53 2.03
ASN CB C 13172 1.96 99.00 38.73 2.25
ASN CG C 1084 27.61 181.20 176.52 5.47
ASN N N 15211 101.71 137.49 119.00 4.10
ASN ND2 N 7862 32.20 133.86 112.79 2.87
CYS H H 9729 3.72 12.12 8.40 0.70
CYS HA H 8674 -9.86 43.50 4.73 1.31
CYS HB2 H 8317 -39.82 363.58 3.24 7.11
CYS HB3 H 8087 -44.20 363.58 3.16 6.56
CYS HG H 90 0.25 10.70 2.15 1.80
CYS C C 3921 1.00 186.04 174.72 4.61
CYS CA C 5643 41.91 68.54 58.02 3.37
CYS CB C 5177 17.99 73.92 33.23 6.46
CYS N N 6639 -147.00 628.00 121.19 30.11
GLU H H 32147 4.24 64.68 8.34 0.74
GLU HA H 25859 1.77 31.32 4.26 0.46
GLU HB2 H 23457 -1.47 4.82 2.02 0.23
GLU HB3 H 21566 -1.63 3.76 2.00 0.23
GLU HG2 H 21649 -0.67 4.69 2.27 0.23
GLU HG3 H 19538 -0.10 4.69 2.25 0.23
GLU HE2 H 1 11.96 11.96 11.96 0.00
GLU C C 19666 1.00 190.58 176.86 3.18
GLU CA C 27147 21.29 87.15 57.34 2.20
GLU CB C 25161 9.08 181.95 30.07 2.41
GLU CG C 17414 6.16 119.03 36.11 1.94
GLU CD C 492 0.00 189.46 181.45 10.94
GLU N N 29587 0.00 429.00 120.70 4.44
GLN H H 16979 4.24 13.17 8.22 0.61
GLN HA H 13751 1.60 7.43 4.28 0.44
GLN HB2 H 12467 -1.34 5.18 2.05 0.28
GLN HB3 H 11587 -1.42 20.90 2.02 0.34
GLN HG2 H 11675 -1.76 7.50 2.31 0.29
GLN HG3 H 10442 -1.08 34.95 2.30 0.45
GLN HE21 H 8682 2.21 111.33 7.25 1.65
GLN HE22 H 8633 2.10 113.70 7.06 2.01
GLN C C 10047 7.24 184.44 176.31 2.65
GLN CA C 14232 4.10 69.63 56.57 2.21
GLN CB C 13177 20.27 79.68 29.21 2.09
GLN CG C 9138 2.43 178.32 33.80 2.34
GLN CD C 1064 171.70 183.54 179.62 1.44
GLN N N 15431 82.60 216.50 119.87 3.81
GLN NE2 N 7375 11.96 155.00 111.84 2.74
GLY H H 31011 -15.30 128.71 8.33 1.18
GLY HA2 H 24665 -3.40 8.64 3.97 0.41
GLY HA3 H 23274 -3.40 7.58 3.89 0.44
GLY C C 17737 1.00 187.28 173.87 3.75
GLY CA C 25124 2.20 108.30 45.38 1.77
GLY N N 27287 8.65 791.00 110.00 10.32
HIS H H 9410 1.00 13.34 8.26 0.77
HIS HA H 7645 0.68 30.68 4.63 0.70
HIS HB2 H 7092 -0.05 45.90 3.23 1.55
HIS HB3 H 6870 -6.20 38.50 3.16 1.45
HIS HD1 H 551 -15.00 86.50 11.29 11.34
HIS HD2 H 5146 -25.85 67.80 7.42 4.85
HIS HE1 H 4253 -26.60 43.80 7.77 3.08
HIS HE2 H 220 -15.00 76.40 12.19 10.18
HIS C C 5415 1.00 184.20 175.17 4.10
HIS CA C 7769 11.40 118.60 56.52 2.81
HIS CB C 7240 17.80 80.78 30.26 2.52
HIS CG C 98 71.30 139.83 130.99 7.16
HIS CD2 C 2698 7.19 159.95 119.82 6.39
HIS CE1 C 2149 8.27 166.28 136.92 6.26
HIS N N 8298 1.00 159.14 119.60 4.63
HIS ND1 N 355 64.90 256.60 192.37 34.65
HIS NE2 N 351 8.40 250.20 179.14 23.55
ILE H H 21661 0.00 11.69 8.28 0.71
ILE HA H 17464 0.00 6.37 4.19 0.57
ILE HB H 16324 -2.44 38.70 1.79 0.51
ILE HG12 H 14747 -10.10 5.56 1.26 0.52
ILE HG13 H 13952 -10.10 9.71 1.20 0.57
ILE HG2 H 15519 -3.62 6.23 0.77 0.34
ILE HD1 H 15462 -4.15 8.80 0.67 0.37
ILE C C 13082 1.00 184.75 175.79 3.81
ILE CA C 18161 30.90 77.93 61.58 2.71
ILE CB C 16832 20.94 87.68 38.66 2.36
ILE CG1 C 11524 8.00 74.78 27.69 2.30
ILE CG2 C 12392 0.79 114.15 17.59 2.37
ILE CD1 C 12393 1.02 79.34 13.57 2.85
ILE N N 19639 36.90 531.00 121.60 6.79
LEU H H 35606 0.09 13.22 8.23 0.67
LEU HA H 28458 0.51 8.73 4.32 0.48
LEU HB2 H 25888 -1.52 8.02 1.62 0.37
LEU HB3 H 24472 -1.79 8.39 1.53 0.38
LEU HG H 23133 -2.08 5.70 1.51 0.35
LEU HD1 H 25370 -3.42 7.50 0.75 0.33
LEU HD2 H 24344 -3.42 22.11 0.73 0.37
LEU C C 21342 22.96 228.49 176.97 2.36
LEU CA C 29695 14.37 85.60 55.63 2.19
LEU CB C 27655 16.38 93.18 42.33 2.14
LEU CG C 17901 15.57 75.28 26.81 1.74
LEU CD1 C 19709 0.73 120.70 24.70 2.24
LEU CD2 C 18663 6.00 116.30 24.13 2.28
LEU N N 32211 8.24 627.00 122.21 11.92
LYS H H 31463 0.00 12.62 8.18 0.63
LYS HA H 25235 0.00 8.60 4.27 0.46
LYS HB2 H 22668 -1.42 35.97 1.78 0.36
LYS HB3 H 20901 -1.40 35.97 1.75 0.37
LYS HG2 H 20224 -1.45 29.88 1.37 0.34
LYS HG3 H 18079 -1.83 29.88 1.36 0.36
LYS HD2 H 17738 -1.68 119.62 1.62 1.01
LYS HD3 H 15239 -2.02 41.68 1.60 0.46
LYS HE2 H 17492 -0.49 8.37 2.92 0.22
LYS HE3 H 14732 -0.05 6.83 2.91 0.22
LYS HZ H 937 -10.90 9.90 7.30 1.24
LYS C C 17595 32.87 996.25 176.67 6.68
LYS CA C 24850 22.02 86.72 56.93 2.26
LYS CB C 22997 -26.69 82.98 32.82 2.16
LYS CG C 15318 0.00 77.38 24.93 1.79
LYS CD C 14519 15.37 77.48 28.98 1.77
LYS CE C 14029 12.03 89.98 41.90 1.55
LYS N N 27552 101.10 1118.13 121.11 7.26
LYS NZ N 92 1.95 132.80 48.63 33.82
MET H H 8423 4.87 12.46 8.26 0.61
MET HA H 6990 -0.93 313.57 4.45 3.73
MET HB2 H 6262 -9.84 33.75 2.03 0.71
MET HB3 H 5801 -2.70 12.94 2.01 0.59
MET HG2 H 5742 -33.86 32.70 2.31 2.40
MET HG3 H 5330 -33.86 31.70 2.27 2.59
MET HE H 3908 -24.86 17.06 1.55 2.67
MET C C 5213 2.20 183.16 176.14 3.25
MET CA C 7445 45.50 85.33 56.14 2.34
MET CB C 6764 0.20 83.38 33.05 2.60
MET CG C 4384 2.30 81.18 32.04 1.92
MET CE C 3111 0.00 71.16 17.30 3.09
MET N N 7734 38.00 221.00 120.07 4.57
PHE H H 15735 4.06 12.18 8.36 0.73
PHE HA H 12545 1.45 122.00 4.64 1.29
PHE HB2 H 11691 0.17 7.98 2.99 0.39
PHE HB3 H 11338 0.09 12.72 2.94 0.41
PHE HD1 H 9997 0.00 9.76 7.02 0.47
PHE HD2 H 7834 0.00 9.76 7.02 0.50
PHE HE1 H 8898 0.00 14.08 7.05 0.55
PHE HE2 H 7115 0.00 12.90 7.04 0.57
PHE HZ H 6366 -7.14 130.37 7.02 1.81
PHE C C 9212 124.30 187.61 175.44 2.21
PHE CA C 12854 4.92 73.43 58.07 2.66
PHE CB C 12009 21.40 137.00 40.00 2.56
PHE CG C 150 7.00 152.84 134.36 20.25
PHE CD1 C 4868 19.15 143.45 131.30 4.30
PHE CD2 C 3034 19.15 138.70 131.31 4.49
PHE CE1 C 4217 7.90 135.60 130.38 4.60
PHE CE2 C 2626 7.90 139.70 130.43 4.77
PHE CZ C 3138 7.10 138.60 128.78 6.40
PHE N N 14066 102.20 229.00 120.55 4.42
PRO H2 H 1 8.51 8.51 8.51 0.00
PRO HA H 13829 0.00 8.51 4.39 0.37
PRO HB2 H 12893 -0.78 5.25 2.07 0.38
PRO HB3 H 12283 -3.48 6.10 2.00 0.40
PRO HG2 H 11589 -2.35 4.92 1.92 0.36
PRO HG3 H 10549 -1.35 4.92 1.90 0.37
PRO HD2 H 11965 -6.56 7.67 3.62 0.54
PRO HD3 H 11451 -6.56 6.30 3.59 0.55
PRO C C 9637 3.19 183.52 176.62 3.70
PRO CA C 14034 26.45 176.83 63.34 2.58
PRO CB C 13027 24.69 81.08 31.91 2.11
PRO CG C 9076 18.28 76.28 27.27 2.18
PRO CD C 9189 4.99 98.58 50.33 2.36
PRO N N 422 31.27 430.00 142.57 49.45
SER H H 26020 -15.30 13.13 8.29 0.63
SER HA H 21317 1.43 58.74 4.49 0.56
SER HB2 H 19431 0.61 5.70 3.87 0.29
SER HB3 H 17644 0.61 5.52 3.84 0.30
SER HG H 373 0.00 999.00 8.13 51.46
SER C C 15353 128.34 197.10 174.65 2.02
SER CA C 21823 24.40 89.55 58.71 2.16
SER CB C 20007 0.00 171.73 63.80 2.00
SER N N 23048 1.68 196.20 116.34 3.94
THR H H 23544 0.00 12.20 8.24 0.65
THR HA H 18931 -1.50 6.67 4.46 0.49
THR HB H 17378 0.00 73.47 4.18 1.07
THR HG1 H 668 0.32 11.01 5.18 1.68
THR HG2 H 17165 -12.10 22.21 1.14 0.39
THR C C 13484 60.89 185.92 174.52 2.54
THR CA C 19125 50.94 92.66 62.22 2.66
THR CB C 17598 1.06 629.21 69.67 4.90
THR CG2 C 12499 11.70 108.98 21.60 2.09
THR N N 20992 6.83 402.00 115.69 8.10
TRP H H 5307 4.49 11.67 8.29 0.80
TRP HA H 4218 2.28 7.05 4.70 0.54
TRP HB2 H 3964 0.42 5.35 3.18 0.36
TRP HB3 H 3809 0.55 4.49 3.13 0.37
TRP HD1 H 3558 4.69 127.79 7.17 2.06
TRP HE1 H 3828 -1.28 18.00 10.10 0.68
TRP HE3 H 3197 1.85 10.09 7.28 0.59
TRP HZ2 H 3398 2.63 10.81 7.26 0.49
TRP HZ3 H 3075 0.76 8.90 6.83 0.58
TRP HH2 H 3162 2.84 10.90 6.94 0.55
TRP C C 2835 57.52 181.89 176.08 2.99
TRP CA C 4004 33.74 87.02 57.63 2.64
TRP CB C 3721 1.60 112.01 30.15 3.19
TRP CG C 131 83.60 114.60 110.15 3.76
TRP CD1 C 1823 30.24 158.33 126.25 4.37
TRP CD2 C 94 120.20 131.20 127.70 1.58
TRP CE2 C 110 118.37 177.71 138.22 7.25
TRP CE3 C 1554 40.14 155.09 120.24 4.18
TRP CZ2 C 1733 6.84 144.03 113.96 4.95
TRP CZ3 C 1562 6.76 161.54 121.17 4.54
TRP CH2 C 1627 47.65 160.82 123.49 4.28
TRP N N 4483 25.80 207.70 121.75 4.79
TRP NE1 N 2811 0.53 249.50 129.39 4.23
TYR H H 13489 2.58 11.96 8.32 0.75
TYR HA H 10834 0.44 6.83 4.62 0.57
TYR HB2 H 10132 -21.23 23.28 2.90 0.50
TYR HB3 H 9851 -21.23 23.28 2.85 0.51
TYR HD1 H 9078 0.19 9.39 6.91 0.42
TYR HD2 H 7176 0.92 10.50 6.91 0.45
TYR HE1 H 8702 0.08 11.80 6.69 0.37
TYR HE2 H 6936 0.43 11.70 6.69 0.39
TYR HH H 214 3.07 31.00 9.25 2.49
TYR C C 7304 2.20 183.93 175.33 3.71
TYR CA C 10489 2.20 65.99 58.08 2.68
TYR CB C 9655 28.82 175.51 39.38 3.05
TYR CG C 150 6.80 138.70 126.06 18.85
TYR CD1 C 4496 19.59 138.70 132.35 5.44
TYR CD2 C 2623 19.59 137.80 132.23 5.94
TYR CE1 C 4454 40.44 159.57 117.67 4.47
TYR CE2 C 2606 51.50 154.10 117.74 3.63
TYR CZ C 126 6.50 162.70 151.11 27.44
TYR N N 11645 100.09 818.00 121.46 19.44
VAL H H 28345 0.00 15.05 8.29 0.70
VAL HA H 22851 -2.83 54.97 4.19 0.70
VAL HB H 21452 -27.48 31.75 1.98 0.50
VAL HG1 H 20893 -27.20 24.20 0.82 0.40
VAL HG2 H 20349 -27.20 24.20 0.80 0.42
VAL C C 16944 44.78 185.04 175.62 2.39
VAL CA C 23635 30.42 91.71 62.45 2.91
VAL CB C 21917 20.24 83.58 32.76 2.12
VAL CG1 C 16049 -7.40 117.16 21.53 2.27
VAL CG2 C 15350 -5.65 121.47 21.35 2.40
VAL N N 25796 12.39 1116.40 121.46 12.22
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