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 2729098 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: 05-23-2008
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 25830 0.95 14.80 8.19 0.63
ALA HA H 20488 -2.52 8.62 4.25 0.45
ALA HB H 19259 -2.29 5.48 1.36 0.28
ALA C C 14406 49.30 187.20 177.71 2.81
ALA CA C 20421 17.29 99.00 53.18 2.09
ALA CB C 19027 -40.99 99.00 19.01 2.37
ALA N N 22789 8.63 766.00 123.34 8.90
ARG H H 17004 0.00 12.73 8.24 0.65
ARG HA H 13705 0.00 12.57 4.29 0.48
ARG HB2 H 12197 -4.78 4.77 1.80 0.29
ARG HB3 H 11184 -1.13 3.64 1.77 0.29
ARG HG2 H 10720 -1.45 4.20 1.57 0.29
ARG HG3 H 9523 -0.91 5.47 1.55 0.30
ARG HD2 H 10418 -6.44 4.69 3.11 0.28
ARG HD3 H 9058 -0.49 4.66 3.10 0.28
ARG HE H 4183 0.00 118.45 9.24 14.12
ARG HH11 H 439 4.41 10.30 6.88 0.53
ARG HH12 H 318 4.41 10.73 6.83 0.52
ARG HH21 H 393 3.87 9.70 6.79 0.50
ARG HH22 H 313 3.87 10.18 6.78 0.58
ARG C C 9095 2.20 184.51 176.40 3.59
ARG CA C 13221 8.37 70.69 56.80 2.48
ARG CB C 11945 20.95 82.18 30.69 2.28
ARG CG C 7359 12.17 76.58 27.26 1.96
ARG CD C 7548 23.20 91.28 43.17 1.68
ARG CZ C 181 128.85 177.70 159.85 4.03
ARG N N 14472 67.14 176.86 120.78 3.87
ARG NE N 2152 7.19 145.60 89.91 21.01
ARG NH1 N 86 7.41 112.50 74.61 11.76
ARG NH2 N 75 66.20 123.30 76.38 11.16
ASP H H 20261 3.56 12.61 8.32 0.59
ASP HA H 16209 0.25 8.60 4.60 0.33
ASP HB2 H 14925 -0.39 37.40 2.74 0.79
ASP HB3 H 14082 -1.46 37.20 2.69 0.80
ASP HD2 H 1 12.30 12.30 12.30 0.00
ASP C C 11669 52.77 219.00 176.43 2.28
ASP CA C 16451 39.80 68.47 54.67 2.10
ASP CB C 15249 9.70 180.89 40.88 2.45
ASP CG C 387 27.50 183.94 178.41 11.20
ASP N N 18133 8.49 223.70 120.76 4.35
ASN H H 14334 2.61 448.00 8.38 3.73
ASN HA H 11669 1.75 7.11 4.67 0.38
ASN HB2 H 10844 -0.64 5.58 2.81 0.34
ASN HB3 H 10332 -0.69 5.14 2.76 0.37
ASN HD21 H 7807 2.06 10.10 7.35 0.51
ASN HD22 H 7746 2.20 11.43 7.14 0.53
ASN C C 7836 2.20 184.22 175.28 2.87
ASN CA C 11299 2.20 99.00 53.53 2.08
ASN CB C 10469 1.96 99.00 38.72 2.37
ASN CG C 895 27.61 181.20 176.47 5.99
ASN N N 12302 103.70 137.49 119.00 4.12
ASN ND2 N 5995 32.20 133.86 112.78 3.04
CYS H H 8210 3.72 12.12 8.40 0.70
CYS HA H 7317 -2.78 43.50 4.75 1.40
CYS HB2 H 6988 -39.82 134.60 3.14 3.54
CYS HB3 H 6774 -44.20 125.00 3.08 3.71
CYS HG H 81 0.25 10.70 2.22 1.89
CYS C C 2963 2.20 184.37 174.71 4.07
CYS CA C 4361 41.91 68.54 57.95 3.41
CYS CB C 3943 19.12 73.92 33.34 6.50
CYS N N 5275 -147.00 628.00 121.44 33.70
GLU H H 26100 4.31 64.68 8.34 0.77
GLU HA H 20988 1.77 31.32 4.25 0.46
GLU HB2 H 18804 -0.22 4.82 2.03 0.23
GLU HB3 H 17119 -0.79 3.76 2.01 0.23
GLU HG2 H 17155 0.00 4.69 2.28 0.23
GLU HG3 H 15327 -0.10 4.69 2.26 0.23
GLU HE2 H 1 11.96 11.96 11.96 0.00
GLU C C 15372 8.22 190.58 176.89 3.16
GLU CA C 21526 28.80 82.05 57.37 2.19
GLU CB C 19723 9.08 181.95 30.04 2.56
GLU CG C 13217 6.16 119.03 36.09 2.12
GLU CD C 426 0.00 189.46 181.20 11.73
GLU N N 23693 0.00 429.00 120.70 4.64
GLN H H 13839 4.24 13.17 8.21 0.61
GLN HA H 11234 1.60 7.43 4.27 0.44
GLN HB2 H 10052 -1.34 5.18 2.05 0.28
GLN HB3 H 9262 -1.42 20.90 2.02 0.36
GLN HG2 H 9323 -1.76 3.66 2.31 0.29
GLN HG3 H 8243 -1.08 34.95 2.30 0.47
GLN HE21 H 6732 2.21 111.33 7.24 1.86
GLN HE22 H 6688 2.10 113.70 7.07 2.27
GLN C C 7868 7.24 184.44 176.31 2.82
GLN CA C 11333 4.10 69.63 56.55 2.24
GLN CB C 10410 20.27 79.68 29.18 2.16
GLN CG C 6954 2.43 125.57 33.76 1.97
GLN CD C 881 171.70 183.54 179.58 1.51
GLN N N 12373 82.60 216.50 119.88 3.84
GLN NE2 N 5532 11.96 155.00 111.78 3.00
GLY H H 25115 -15.30 128.71 8.34 1.28
GLY HA2 H 19915 -3.40 8.64 3.97 0.42
GLY HA3 H 18670 -3.40 7.58 3.89 0.45
GLY C C 13565 2.20 187.28 173.88 3.89
GLY CA C 19548 2.20 108.30 45.37 1.87
GLY N N 21646 8.65 791.00 110.08 11.39
HIS H H 7669 4.45 13.34 8.27 0.78
HIS HA H 6154 0.68 11.38 4.64 0.67
HIS HB2 H 5643 -0.05 45.90 3.27 1.73
HIS HB3 H 5420 -6.20 38.50 3.19 1.62
HIS HD1 H 490 -15.00 86.50 11.68 11.96
HIS HD2 H 4024 -25.85 67.80 7.56 5.47
HIS HE1 H 3325 -26.60 43.80 7.73 3.46
HIS HE2 H 192 -15.00 76.40 12.52 10.84
HIS C C 4188 2.20 183.83 175.17 3.66
HIS CA C 6094 23.91 118.60 56.51 2.79
HIS CB C 5635 17.80 80.78 30.25 2.56
HIS CG C 88 71.30 139.83 130.91 7.51
HIS CD2 C 1800 7.19 159.95 119.32 7.33
HIS CE1 C 1346 8.27 144.54 136.44 7.49
HIS N N 6627 105.00 137.80 119.63 4.18
HIS ND1 N 293 64.90 256.60 191.53 35.02
HIS NE2 N 284 8.40 249.96 178.03 24.26
ILE H H 17714 0.00 11.69 8.27 0.72
ILE HA H 14250 0.00 6.37 4.18 0.58
ILE HB H 13194 -2.44 38.70 1.79 0.55
ILE HG12 H 11772 -10.10 5.56 1.26 0.54
ILE HG13 H 11061 -10.10 9.71 1.21 0.60
ILE HG2 H 12486 -3.62 6.23 0.77 0.35
ILE HD1 H 12406 -4.15 8.80 0.67 0.39
ILE C C 10345 130.51 184.03 175.84 2.11
ILE CA C 14557 30.90 77.93 61.56 2.74
ILE CB C 13350 20.94 87.68 38.65 2.44
ILE CG1 C 8750 8.00 74.78 27.67 2.47
ILE CG2 C 9502 0.79 83.57 17.60 2.43
ILE CD1 C 9530 1.02 78.64 13.60 3.02
ILE N N 15824 36.90 531.00 121.60 7.29
LEU H H 28910 0.09 13.22 8.22 0.67
LEU HA H 22961 0.51 8.73 4.31 0.48
LEU HB2 H 20604 -1.52 8.02 1.62 0.38
LEU HB3 H 19297 -1.79 8.39 1.54 0.39
LEU HG H 18264 -2.08 5.70 1.50 0.36
LEU HD1 H 20143 -3.42 7.50 0.75 0.35
LEU HD2 H 19242 -3.42 22.11 0.73 0.39
LEU C C 16744 22.96 228.49 176.99 2.48
LEU CA C 23577 44.60 85.60 55.64 2.17
LEU CB C 21730 16.38 93.18 42.28 2.19
LEU CG C 13380 15.57 75.28 26.79 1.89
LEU CD1 C 14951 0.73 73.88 24.66 2.26
LEU CD2 C 14075 6.00 73.48 24.12 2.30
LEU N N 25833 8.24 627.00 122.25 13.16
LYS H H 25934 0.00 12.62 8.18 0.63
LYS HA H 20616 0.00 8.60 4.27 0.46
LYS HB2 H 18294 -0.84 10.94 1.78 0.28
LYS HB3 H 16688 -0.97 9.43 1.76 0.29
LYS HG2 H 16082 -1.45 6.70 1.38 0.28
LYS HG3 H 14153 -1.83 4.18 1.36 0.30
LYS HD2 H 13981 -1.68 119.62 1.62 1.07
LYS HD3 H 11775 -2.02 29.05 1.60 0.36
LYS HE2 H 13651 -0.49 8.37 2.92 0.23
LYS HE3 H 11281 -0.05 6.83 2.91 0.23
LYS HZ H 857 -10.90 9.90 7.30 1.26
LYS C C 13739 32.87 996.25 176.72 7.43
LYS CA C 19798 43.10 82.05 56.95 2.24
LYS CB C 18123 -26.69 82.98 32.78 2.25
LYS CG C 11463 0.00 77.38 24.95 1.95
LYS CD C 10801 20.62 77.48 28.96 1.95
LYS CE C 10371 12.03 89.98 41.88 1.72
LYS N N 22269 101.10 217.00 121.04 4.16
LYS NZ N 71 1.95 132.80 48.50 34.58
MET H H 6926 4.87 11.89 8.26 0.62
MET HA H 5750 -0.93 313.57 4.45 4.11
MET HB2 H 5079 -9.84 33.75 2.04 0.76
MET HB3 H 4675 -2.70 12.94 2.01 0.63
MET HG2 H 4626 -33.86 32.70 2.28 2.66
MET HG3 H 4263 -33.86 31.70 2.24 2.89
MET HE H 3060 -24.86 17.06 1.47 3.00
MET C C 4099 2.20 183.16 176.15 3.50
MET CA C 5958 45.50 72.49 56.15 2.32
MET CB C 5367 0.20 83.38 33.03 2.65
MET CG C 3367 2.30 81.18 32.05 1.98
MET CE C 2308 0.00 68.10 17.33 3.06
MET N N 6261 38.95 221.00 120.04 4.67
PHE H H 12825 4.06 12.03 8.36 0.74
PHE HA H 10165 1.45 122.00 4.63 1.41
PHE HB2 H 9405 0.17 7.98 2.99 0.40
PHE HB3 H 9059 0.30 12.72 2.94 0.41
PHE HD1 H 7967 0.00 8.70 7.01 0.51
PHE HD2 H 6099 0.00 8.70 7.01 0.54
PHE HE1 H 7053 0.00 12.90 7.04 0.59
PHE HE2 H 5511 0.00 12.90 7.04 0.63
PHE HZ H 5052 -7.14 43.62 7.00 1.02
PHE C C 7203 124.30 187.61 175.50 2.27
PHE CA C 10242 4.92 73.43 58.11 2.71
PHE CB C 9476 21.40 88.78 39.96 2.48
PHE CG C 101 36.75 141.50 136.28 10.50
PHE CD1 C 3394 19.15 138.12 131.11 5.09
PHE CD2 C 2010 19.15 137.20 131.06 5.46
PHE CE1 C 2855 7.90 135.60 130.20 5.52
PHE CE2 C 1668 7.90 134.50 130.21 5.90
PHE CZ C 2062 9.28 138.60 128.76 5.72
PHE N N 11321 102.20 229.00 120.59 4.51
PRO H2 H 1 8.51 8.51 8.51 0.00
PRO HA H 11027 0.00 8.51 4.39 0.38
PRO HB2 H 10138 -0.78 5.25 2.06 0.39
PRO HB3 H 9606 -3.48 6.10 2.01 0.41
PRO HG2 H 8968 -2.35 4.92 1.92 0.37
PRO HG3 H 8065 -1.29 4.92 1.90 0.38
PRO HD2 H 9303 -6.56 7.67 3.62 0.58
PRO HD3 H 8821 -6.56 6.30 3.59 0.58
PRO C C 7540 117.05 182.30 176.66 2.23
PRO CA C 10906 26.45 73.44 63.29 1.83
PRO CB C 9989 25.44 81.08 31.89 2.25
PRO CG C 6567 19.31 76.28 27.31 2.46
PRO CD C 6688 4.99 98.58 50.32 2.67
PRO N N 328 31.27 430.00 146.02 54.27
SER H H 20837 -15.30 13.13 8.28 0.65
SER HA H 16893 1.43 7.37 4.49 0.43
SER HB2 H 15233 0.61 5.70 3.87 0.29
SER HB3 H 13699 0.61 5.52 3.85 0.31
SER HG H 304 0.00 999.00 8.72 57.00
SER C C 11568 128.34 197.10 174.65 2.12
SER CA C 16859 24.40 76.07 58.70 2.19
SER CB C 15255 0.00 171.73 63.78 2.10
SER N N 18092 1.68 196.20 116.30 4.06
THR H H 19154 0.00 12.20 8.25 0.65
THR HA H 15409 -1.50 6.67 4.46 0.50
THR HB H 14004 0.00 68.14 4.17 0.85
THR HG1 H 542 0.32 11.01 5.30 1.63
THR HG2 H 13865 -12.10 16.30 1.14 0.34
THR C C 10439 60.89 185.33 174.51 2.73
THR CA C 15094 50.94 82.16 62.19 2.69
THR CB C 13734 7.00 629.21 69.63 5.40
THR CG2 C 9509 11.70 108.98 21.59 2.31
THR N N 16781 6.83 402.00 115.76 8.74
TRP H H 4346 4.49 11.67 8.29 0.80
TRP HA H 3448 2.28 7.05 4.70 0.55
TRP HB2 H 3218 0.42 5.35 3.18 0.36
TRP HB3 H 3089 0.55 4.49 3.13 0.38
TRP HD1 H 2883 4.69 8.93 7.13 0.37
TRP HE1 H 3100 5.00 18.00 10.11 0.64
TRP HE3 H 2577 1.85 10.09 7.28 0.63
TRP HZ2 H 2758 2.63 10.81 7.25 0.53
TRP HZ3 H 2524 0.76 8.90 6.82 0.61
TRP HH2 H 2566 2.84 10.90 6.93 0.59
TRP C C 2259 57.52 181.89 176.06 3.19
TRP CA C 3203 33.74 69.76 57.64 2.62
TRP CB C 2957 1.60 112.01 30.14 3.39
TRP CG C 120 83.60 114.60 109.94 3.86
TRP CD1 C 1323 30.24 136.11 126.10 4.92
TRP CD2 C 89 120.20 131.20 127.61 1.56
TRP CE2 C 99 118.37 177.71 137.80 6.86
TRP CE3 C 1099 40.14 138.50 120.07 4.75
TRP CZ2 C 1248 6.84 134.70 113.77 5.71
TRP CZ3 C 1116 6.76 138.39 121.03 5.17
TRP CH2 C 1167 47.65 133.10 123.24 4.86
TRP N N 3614 25.80 207.70 121.81 4.91
TRP NE1 N 2198 0.53 249.50 129.39 4.57
TYR H H 11126 4.39 11.96 8.32 0.75
TYR HA H 8899 1.20 6.83 4.62 0.57
TYR HB2 H 8274 0.30 23.28 2.91 0.45
TYR HB3 H 7994 -0.19 23.28 2.86 0.46
TYR HD1 H 7424 0.73 9.39 6.91 0.44
TYR HD2 H 5750 0.92 10.50 6.90 0.48
TYR HE1 H 7092 0.08 11.80 6.69 0.39
TYR HE2 H 5532 0.43 11.70 6.68 0.43
TYR HH H 184 3.07 31.00 9.19 2.62
TYR C C 5680 2.20 182.92 175.35 4.05
TYR CA C 8343 2.20 65.80 58.10 2.68
TYR CB C 7606 28.82 175.51 39.36 3.25
TYR CG C 123 36.60 138.70 128.30 8.77
TYR CD1 C 3231 19.59 138.70 132.16 6.37
TYR CD2 C 1811 19.59 137.80 131.95 7.09
TYR CE1 C 3178 40.44 159.57 117.53 5.25
TYR CE2 C 1791 51.50 154.10 117.59 4.33
TYR CZ C 101 31.30 162.70 154.03 17.24
TYR N N 9391 100.09 818.00 121.66 21.56
VAL H H 22868 0.00 11.81 8.28 0.71
VAL HA H 18448 -2.83 54.97 4.18 0.72
VAL HB H 17145 -18.50 31.75 1.98 0.44
VAL HG1 H 16706 -27.20 24.20 0.83 0.42
VAL HG2 H 16206 -27.20 24.20 0.80 0.44
VAL C C 13032 130.51 185.04 175.63 2.24
VAL CA C 18534 43.00 78.44 62.45 2.91
VAL CB C 17016 20.24 83.58 32.73 2.18
VAL CG1 C 12109 7.97 117.16 21.55 2.46
VAL CG2 C 11537 -5.65 121.47 21.38 2.61
VAL N N 20464 12.39 529.00 121.49 11.60
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