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 5210967 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: 05-18-2012
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 45893 0.00 123.45 8.20 0.86
ALA HA H 35819 -2.52 17.87 4.26 0.46
ALA HB H 34112 -14.04 5.48 1.35 0.29
ALA C C 28695 0.04 187.20 177.70 3.23
ALA CA C 39154 3.69 123.90 53.15 2.14
ALA CB C 37195 -40.99 99.00 19.10 2.56
ALA N N 42336 0.05 766.00 123.30 7.07
ARG H H 31022 0.00 861.00 8.27 4.93
ARG HA H 24820 0.00 12.57 4.30 0.48
ARG HB2 H 22650 -4.78 27.53 1.79 0.34
ARG HB3 H 21249 -1.13 27.53 1.76 0.35
ARG HG2 H 20383 -1.45 8.70 1.56 0.29
ARG HG3 H 18595 -1.30 8.52 1.54 0.31
ARG HD2 H 20027 -6.44 4.69 3.11 0.28
ARG HD3 H 17982 -0.49 4.79 3.09 0.30
ARG HE H 7053 0.00 118.45 8.49 10.92
ARG HH11 H 662 4.41 10.30 6.90 0.55
ARG HH12 H 486 4.41 10.73 6.84 0.52
ARG HH21 H 588 1.23 11.35 6.80 0.65
ARG HH22 H 467 1.23 10.18 6.76 0.63
ARG C C 18703 0.17 184.96 176.36 3.41
ARG CA C 26035 3.75 103.60 56.74 2.48
ARG CB C 24219 2.15 123.50 30.75 2.22
ARG CG C 16166 12.17 119.40 27.23 1.78
ARG CD C 16416 23.20 135.80 43.17 1.52
ARG CZ C 407 128.85 181.47 160.54 4.46
ARG N N 27885 0.13 177.67 120.75 4.18
ARG NE N 4386 0.00 149.11 89.80 17.36
ARG NH1 N 152 7.24 124.40 78.26 16.34
ARG NH2 N 125 66.20 128.47 79.83 16.40
ASP H H 36701 0.01 127.50 8.31 0.86
ASP HA H 28829 0.25 8.60 4.59 0.33
ASP HB2 H 27038 -0.39 37.40 2.73 0.61
ASP HB3 H 25828 -1.46 37.20 2.67 0.62
ASP HD2 H 6 1.41 12.30 5.78 3.57
ASP C C 23190 0.11 219.00 176.38 2.77
ASP CA C 31777 2.10 118.90 54.68 2.17
ASP CB C 30157 3.44 180.89 40.90 2.15
ASP CG C 622 6.71 186.50 178.27 12.54
ASP N N 34243 0.00 223.70 120.66 4.45
ASP OD1 O 20 177.59 180.97 179.66 0.91
ASN H H 25531 0.01 448.00 8.35 2.83
ASN HA H 20541 1.75 7.11 4.67 0.37
ASN HB2 H 19326 -0.64 8.74 2.81 0.33
ASN HB3 H 18539 -0.95 6.95 2.75 0.36
ASN HD21 H 14728 1.09 10.38 7.35 0.51
ASN HD22 H 14625 1.47 11.43 7.14 0.53
ASN C C 15640 0.11 184.27 175.18 4.18
ASN CA C 21764 2.20 99.00 53.53 2.02
ASN CB C 20661 1.96 99.00 38.70 2.11
ASN CG C 1586 0.00 183.10 176.40 7.34
ASN N N 23106 0.04 137.49 118.91 4.42
ASN ND2 N 12463 11.59 145.93 112.73 2.96
CYS H H 13500 3.72 12.12 8.39 0.70
CYS HA H 11895 -9.86 43.50 4.69 1.17
CYS HB2 H 11473 -39.82 363.58 3.26 8.10
CYS HB3 H 11158 -44.20 363.58 3.16 7.35
CYS HG H 136 0.25 999.00 9.41 85.50
CYS C C 6256 1.00 186.04 174.83 3.87
CYS CA C 8840 41.91 68.54 58.21 3.35
CYS CB C 8317 17.99 73.92 32.73 6.13
CYS N N 9998 -147.00 628.00 120.78 24.69
GLU H H 47258 0.00 123.45 8.34 0.89
GLU HA H 37469 0.43 31.32 4.25 0.45
GLU HB2 H 34413 -1.47 4.82 2.02 0.23
GLU HB3 H 32045 -1.63 1467.00 2.04 8.19
GLU HG2 H 31995 -0.67 4.69 2.27 0.23
GLU HG3 H 29363 -0.10 4.69 2.24 0.23
GLU HE2 H 2 2.73 11.96 7.34 6.53
GLU C C 30521 0.07 190.58 176.79 3.92
GLU CA C 41430 21.29 87.15 57.31 2.18
GLU CB C 38956 9.08 181.95 30.06 2.23
GLU CG C 27312 6.16 119.03 36.11 1.71
GLU CD C 662 36.12 189.46 181.91 6.31
GLU N N 44494 0.00 429.00 120.64 4.52
GLU OE1 O 1 184.19 184.19 184.19 0.00
GLN H H 25279 0.01 66.54 8.22 0.71
GLN HA H 20255 0.67 7.43 4.27 0.44
GLN HB2 H 18592 -1.34 5.18 2.04 0.28
GLN HB3 H 17509 -1.42 20.90 2.01 0.33
GLN HG2 H 17553 -1.76 7.50 2.31 0.29
GLN HG3 H 15988 -1.08 34.95 2.29 0.40
GLN HE21 H 13454 -3.41 111.33 7.24 1.37
GLN HE22 H 13374 1.62 113.70 7.05 1.64
GLN C C 15952 0.07 184.44 176.27 3.12
GLN CA C 22057 0.91 69.63 56.56 2.26
GLN CB C 20772 1.35 79.68 29.22 2.11
GLN CG C 14696 2.43 178.32 33.78 1.98
GLN CD C 1543 21.34 183.54 179.33 7.22
GLN N N 23519 0.08 216.50 119.84 4.16
GLN NE2 N 11889 11.96 155.00 111.85 2.42
GLY H H 45736 -15.30 128.71 8.33 1.04
GLY HA2 H 36086 -3.40 8.64 3.97 0.41
GLY HA3 H 34198 -3.40 7.58 3.89 0.42
GLY C C 28336 1.00 999.00 173.88 5.94
GLY CA C 39271 0.97 108.30 45.37 1.71
GLY N N 41624 0.00 791.00 109.86 8.71
HIS H H 13768 1.00 13.34 8.26 0.76
HIS HA H 11147 0.68 30.68 4.62 0.65
HIS HB2 H 10421 -0.05 45.90 3.20 1.32
HIS HB3 H 10093 -6.20 38.50 3.13 1.27
HIS HD1 H 686 -15.00 86.50 10.71 10.28
HIS HD2 H 7617 -25.85 67.80 7.27 4.02
HIS HE1 H 6152 -26.60 43.80 7.78 2.61
HIS HE2 H 257 -15.00 76.40 11.77 9.50
HIS C C 8372 1.00 184.20 175.18 3.72
HIS CA C 11871 11.40 176.90 56.55 2.90
HIS CB C 11205 17.80 80.78 30.29 2.43
HIS CG C 131 0.00 139.83 130.21 13.11
HIS CD2 C 4583 0.00 159.95 119.83 6.46
HIS CE1 C 3652 0.00 166.28 137.21 6.10
HIS N N 12449 1.00 159.14 119.70 4.42
HIS ND1 N 482 0.00 261.01 193.33 36.38
HIS NE2 N 457 0.00 257.57 178.65 24.01
ILE H H 32116 0.00 116.81 8.27 0.93
ILE HA H 25424 0.00 6.37 4.18 0.57
ILE HB H 24000 -2.44 38.70 1.78 0.45
ILE HG12 H 21842 -10.10 5.56 1.26 0.48
ILE HG13 H 20911 -10.10 9.71 1.19 0.52
ILE HG2 H 22873 -3.62 6.23 0.76 0.32
ILE HD1 H 22953 -4.15 8.80 0.67 0.35
ILE C C 20662 0.09 184.75 175.79 3.80
ILE CA C 28060 4.22 77.93 61.59 2.77
ILE CB C 26340 2.38 87.68 38.63 2.26
ILE CG1 C 18231 8.00 74.78 27.70 2.10
ILE CG2 C 19445 0.79 114.15 17.56 2.07
ILE CD1 C 19557 1.02 79.34 13.50 2.54
ILE N N 29898 0.05 531.00 121.48 6.31
LEU H H 53025 0.01 13.22 8.23 0.67
LEU HA H 41686 0.51 8.73 4.32 0.48
LEU HB2 H 38476 -1.52 8.02 1.61 0.37
LEU HB3 H 36611 -1.79 8.39 1.52 0.38
LEU HG H 34481 -2.08 5.70 1.50 0.35
LEU HD1 H 37768 -3.42 30.18 0.75 0.36
LEU HD2 H 36395 -3.42 24.50 0.73 0.39
LEU C C 33752 0.00 228.49 176.94 3.37
LEU CA C 46019 0.65 85.60 55.61 2.22
LEU CB C 43397 2.37 93.18 42.32 2.10
LEU CG C 28565 15.57 75.28 26.81 1.60
LEU CD1 C 31211 0.73 120.70 24.73 2.07
LEU CD2 C 29765 0.62 116.30 24.09 2.16
LEU N N 49158 0.00 627.00 122.05 10.04
LYS H H 45315 0.00 64.42 8.18 0.73
LYS HA H 35886 0.00 9.19 4.27 0.45
LYS HB2 H 32628 -1.42 35.97 1.78 0.33
LYS HB3 H 30361 -1.40 35.97 1.74 0.35
LYS HG2 H 29472 -1.45 29.88 1.36 0.32
LYS HG3 H 26710 -1.83 29.88 1.35 0.34
LYS HD2 H 26260 -1.68 119.62 1.61 0.84
LYS HD3 H 22891 -2.02 41.68 1.60 0.40
LYS HE2 H 25927 -0.49 8.37 2.91 0.22
LYS HE3 H 22118 -0.05 6.83 2.90 0.23
LYS HZ H 1090 -10.90 10.51 7.30 1.22
LYS C C 27373 0.11 999.00 176.59 8.32
LYS CA C 37786 7.01 86.72 56.92 2.28
LYS CB C 35512 -26.69 82.98 32.81 2.09
LYS CG C 23866 0.00 77.38 24.91 1.65
LYS CD C 22636 15.37 77.48 28.97 1.59
LYS CE C 22017 12.03 89.98 41.88 1.42
LYS N N 40941 0.04 1118.13 121.03 6.71
LYS NZ N 146 1.95 177.20 46.89 32.60
MET H H 12486 4.87 12.46 8.27 0.61
MET HA H 10210 -0.93 313.57 4.43 3.10
MET HB2 H 9225 -9.84 33.75 2.03 0.62
MET HB3 H 8604 -2.70 12.94 1.99 0.52
MET HG2 H 8515 -33.86 32.70 2.34 1.98
MET HG3 H 7962 -33.86 31.70 2.30 2.13
MET HE H 6129 -24.86 17.06 1.67 2.15
MET C C 8118 2.20 183.25 176.15 2.90
MET CA C 11409 36.03 85.33 56.12 2.32
MET CB C 10548 0.20 83.38 33.00 2.54
MET CG C 6953 0.00 81.18 32.02 1.80
MET CE C 5253 0.00 71.16 17.19 2.61
MET N N 11739 38.00 221.00 120.05 4.45
PHE H H 23038 0.01 12.18 8.35 0.74
PHE HA H 18126 1.45 122.00 4.63 1.13
PHE HB2 H 17020 0.16 7.98 2.99 0.39
PHE HB3 H 16548 -0.21 12.72 2.93 0.41
PHE HD1 H 14589 0.00 9.76 7.03 0.43
PHE HD2 H 11998 0.00 9.76 7.03 0.45
PHE HE1 H 12934 -2.84 14.08 7.05 0.52
PHE HE2 H 10792 0.00 12.90 7.05 0.52
PHE HZ H 9410 -7.14 130.37 7.01 1.52
PHE C C 14469 0.00 187.61 175.39 3.90
PHE CA C 19729 2.06 73.43 58.09 2.69
PHE CB C 18619 7.00 137.00 40.00 2.44
PHE CG C 227 7.00 152.84 135.54 18.25
PHE CD1 C 8268 11.74 143.45 131.34 4.20
PHE CD2 C 5744 19.15 138.70 131.42 3.65
PHE CE1 C 7280 7.90 139.56 130.46 4.10
PHE CE2 C 5068 7.90 139.70 130.55 3.66
PHE CZ C 5579 7.10 138.60 128.93 5.02
PHE N N 21243 0.07 229.00 120.42 4.73
PRO H2 H 1 8.51 8.51 8.51 0.00
PRO HA H 20668 0.00 8.51 4.39 0.36
PRO HB2 H 19434 -1.50 7.30 2.07 0.38
PRO HB3 H 18702 -3.48 6.45 1.99 0.39
PRO HG2 H 17673 -2.35 8.78 1.92 0.35
PRO HG3 H 16211 -1.52 4.92 1.89 0.36
PRO HD2 H 18196 -6.56 7.67 3.63 0.49
PRO HD3 H 17457 -6.56 6.30 3.59 0.51
PRO C C 15360 0.05 999.00 176.65 8.24
PRO CA C 22076 2.05 176.83 63.31 2.35
PRO CB C 20819 2.12 81.08 31.88 1.87
PRO CG C 14918 18.28 76.28 27.24 1.89
PRO CD C 15077 4.99 98.58 50.30 2.04
PRO N N 641 1.00 430.00 138.31 41.88
SER H H 38767 -15.30 112.72 8.28 0.82
SER HA H 31526 1.43 58.74 4.49 0.52
SER HB2 H 29137 0.61 8.02 3.87 0.28
SER HB3 H 26692 0.61 5.93 3.84 0.29
SER HG H 483 0.00 999.00 7.52 45.22
SER C C 24852 0.25 197.10 174.60 2.48
SER CA C 34295 2.86 175.20 58.70 2.25
SER CB C 31991 0.00 171.73 63.75 2.28
SER N N 35472 0.03 196.20 116.29 3.96
THR H H 34491 0.00 12.20 8.24 0.64
THR HA H 27237 -1.50 6.67 4.46 0.49
THR HB H 25241 0.00 73.47 4.18 0.90
THR HG1 H 998 0.32 11.01 5.04 1.73
THR HG2 H 24944 -12.10 22.21 1.14 0.36
THR C C 21217 60.89 185.92 174.51 2.41
THR CA C 29406 1.96 92.66 62.23 2.71
THR CB C 27435 1.06 629.21 69.62 4.37
THR CG2 C 19732 11.70 175.60 21.60 2.13
THR N N 31717 3.15 402.00 115.56 7.24
TRP H H 7793 1.79 17.32 8.29 0.80
TRP HA H 6163 2.24 11.41 4.70 0.55
TRP HB2 H 5833 0.34 5.35 3.18 0.36
TRP HB3 H 5644 0.31 7.88 3.12 0.37
TRP HD1 H 5258 4.69 127.79 7.15 1.70
TRP HE1 H 5601 -1.28 18.00 10.07 0.75
TRP HE3 H 4673 1.34 10.44 7.28 0.57
TRP HZ2 H 4991 0.96 10.81 7.26 0.46
TRP HZ3 H 4506 0.76 8.90 6.83 0.54
TRP HH2 H 4631 1.09 10.90 6.94 0.51
TRP C C 4600 57.52 184.30 176.12 2.66
TRP CA C 6279 2.19 87.02 57.66 2.75
TRP CB C 5909 1.60 112.01 30.13 2.87
TRP CG C 165 83.60 116.53 110.50 3.55
TRP CD1 C 3136 30.24 158.33 126.26 4.24
TRP CD2 C 113 120.20 139.10 127.99 1.97
TRP CE2 C 133 113.89 177.71 138.30 7.48
TRP CE3 C 2683 40.14 155.09 120.19 3.98
TRP CZ2 C 2998 6.84 144.03 113.99 4.74
TRP CZ3 C 2691 6.76 161.54 121.15 4.19
TRP CH2 C 2824 47.65 160.82 123.57 3.95
TRP N N 6880 0.00 207.70 121.68 5.02
TRP NE1 N 4421 0.53 249.50 129.26 3.77
TYR H H 19787 2.58 118.49 8.32 1.08
TYR HA H 15751 0.44 7.95 4.62 0.58
TYR HB2 H 14795 -21.23 23.28 2.90 0.51
TYR HB3 H 14431 -21.23 23.28 2.83 0.53
TYR HD1 H 13060 0.19 9.39 6.91 0.40
TYR HD2 H 10779 0.92 10.50 6.91 0.41
TYR HE1 H 12447 0.08 11.80 6.69 0.34
TYR HE2 H 10367 0.43 11.70 6.69 0.35
TYR HH H 280 3.07 31.00 9.17 2.30
TYR C C 11712 2.20 184.78 175.35 3.41
TYR CA C 16356 2.20 67.48 58.11 2.65
TYR CB C 15319 10.05 175.51 39.36 3.01
TYR CG C 215 6.80 174.59 127.33 16.15
TYR CD1 C 7472 19.59 141.57 132.43 4.78
TYR CD2 C 4922 19.59 137.80 132.43 4.55
TYR CE1 C 7421 40.44 159.57 117.69 4.05
TYR CE2 C 4876 47.30 154.10 117.77 2.97
TYR CZ C 163 6.50 162.70 152.65 24.27
TYR N N 17760 4.89 818.00 121.06 15.95
VAL H H 42117 0.00 15.05 8.28 0.69
VAL HA H 33441 -2.83 54.97 4.18 0.67
VAL HB H 31652 -27.48 31.75 1.97 0.51
VAL HG1 H 30917 -27.20 24.20 0.82 0.37
VAL HG2 H 30289 -27.20 24.20 0.80 0.39
VAL C C 26944 1.00 185.04 175.61 2.46
VAL CA C 36696 29.56 91.71 62.50 2.91
VAL CB C 34538 17.21 83.58 32.75 2.03
VAL CG1 C 25493 -7.40 117.16 21.52 2.00
VAL CG2 C 24600 -5.65 121.47 21.32 2.14
VAL N N 39390 12.39 1116.40 121.32 10.22
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