Statistics Calculated for Selected Chemical Shifts from Atoms in the 20 Common Amino Acids
BMRB Entries not included in the calculations for this table contained chemical shifts outside eight standard deviations
from the mean calculated for the full BMRB database or a chemical shift for at least one carbon bound proton that was
greater than 10ppm or was less than -2.5ppm. These criteria were used to eliminate from the calculations chemical shifts from paramagnetic
proteins, from proteins with aromatic prosthetic groups, and from entries where unusual chemical shift referencing was
used. Of the 5044178 possible chemical shifts in the BMRB database, 3641443 were included in calculating this table.
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: 02-08-2012
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 32279 3.53 11.48 8.20 0.60
ALA HA H 24465 0.87 6.51 4.26 0.44
ALA HB H 23130 -0.88 3.12 1.35 0.25
ALA C C 20545 164.48 187.20 177.74 2.14
ALA CA C 27666 44.22 65.52 53.14 1.98
ALA CB C 26104 0.00 38.70 19.01 1.83
ALA N N 29850 77.10 142.81 123.23 3.53
ARG H H 22224 3.57 12.69 8.24 0.61
ARG HA H 17337 1.34 6.52 4.30 0.46
ARG HB2 H 15658 -0.77 3.44 1.79 0.27
ARG HB3 H 14724 -0.86 3.32 1.76 0.28
ARG HG2 H 14068 -0.72 3.51 1.57 0.27
ARG HG3 H 12858 -0.74 3.51 1.54 0.29
ARG HD2 H 13778 0.96 4.69 3.12 0.24
ARG HD3 H 12417 0.76 4.56 3.10 0.26
ARG HE H 4317 2.99 11.88 7.39 0.65
ARG HH11 H 390 5.88 9.82 6.90 0.46
ARG HH12 H 280 5.99 10.73 6.81 0.40
ARG HH21 H 349 5.90 11.35 6.81 0.48
ARG HH22 H 272 5.97 10.18 6.76 0.39
ARG C C 13471 167.44 184.51 176.41 2.03
ARG CA C 18612 43.27 67.98 56.77 2.31
ARG CB C 17201 20.95 42.50 30.69 1.84
ARG CG C 11119 18.22 40.94 27.21 1.20
ARG CD C 11267 35.05 50.88 43.15 0.89
ARG CZ C 245 156.20 177.70 160.07 3.16
ARG N N 19951 102.78 137.60 120.79 3.68
ARG NE N 2392 67.00 99.81 84.63 1.67
ARG NH1 N 68 67.60 87.79 74.23 5.10
ARG NH2 N 56 70.10 85.28 73.27 3.29
ASP H H 25782 3.56 12.68 8.31 0.58
ASP HA H 19564 2.33 6.33 4.59 0.32
ASP HB2 H 18154 -0.39 4.58 2.72 0.26
ASP HB3 H 17377 -0.23 4.58 2.66 0.28
ASP HD2 H 4 4.65 6.03 5.25 0.58
ASP C C 16467 166.80 182.70 176.40 1.75
ASP CA C 22313 41.88 67.17 54.69 2.03
ASP CB C 20992 27.48 51.09 40.87 1.62
ASP CG C 321 170.72 186.50 179.29 1.86
ASP N N 24066 101.90 143.52 120.64 3.85
ASP OD1 O 20 177.59 180.97 179.66 0.91
ASN H H 18207 2.61 12.40 8.34 0.63
ASN HA H 14239 2.46 6.43 4.67 0.36
ASN HB2 H 13251 0.23 4.47 2.81 0.31
ASN HB3 H 12713 -0.04 4.47 2.76 0.33
ASN HD21 H 9906 3.55 10.38 7.35 0.48
ASN HD22 H 9829 3.05 10.80 7.14 0.49
ASN C C 11263 167.04 181.90 175.27 1.79
ASN CA C 15547 41.31 61.80 53.54 1.89
ASN CB C 14616 26.45 55.09 38.68 1.68
ASN CG C 1030 166.40 183.10 176.78 1.39
ASN N N 16437 101.71 137.49 118.92 4.02
ASN ND2 N 8261 99.40 133.86 112.75 2.22
CYS H H 9625 4.73 12.12 8.39 0.67
CYS HA H 8355 1.64 6.43 4.65 0.55
CYS HB2 H 8002 -0.54 4.72 2.96 0.44
CYS HB3 H 7805 -0.83 4.69 2.89 0.46
CYS HG H 72 0.25 7.39 1.98 1.38
CYS C C 4503 166.73 182.73 174.95 2.07
CYS CA C 6174 42.45 67.64 58.32 3.33
CYS CB C 5754 17.99 62.07 32.42 5.97
CYS N N 6934 100.48 175.10 120.17 4.64
GLU H H 33853 4.20 12.17 8.33 0.59
GLU HA H 25988 1.39 6.29 4.25 0.41
GLU HB2 H 23681 0.34 3.37 2.02 0.21
GLU HB3 H 22080 -0.49 3.33 1.99 0.23
GLU HG2 H 22005 0.53 3.77 2.27 0.21
GLU HG3 H 20284 0.56 3.80 2.25 0.22
GLU HE2 H 1 2.73 2.73 2.73 0.00
GLU C C 22155 166.80 183.52 176.87 1.95
GLU CA C 29660 44.35 64.60 57.32 2.09
GLU CB C 27723 18.71 43.70 30.00 1.72
GLU CG C 18690 25.31 44.34 36.10 1.20
GLU CD C 368 173.41 189.46 182.54 1.91
GLU N N 31984 104.54 138.60 120.67 3.48
GLU OE1 O 1 184.19 184.19 184.19 0.00
GLN H H 18391 3.51 12.04 8.22 0.59
GLN HA H 14350 1.57 6.34 4.27 0.43
GLN HB2 H 13067 -0.11 4.00 2.05 0.25
GLN HB3 H 12324 -0.58 4.04 2.01 0.27
GLN HG2 H 12309 0.09 3.66 2.32 0.27
GLN HG3 H 11218 -0.55 3.66 2.29 0.29
GLN HE21 H 9289 3.39 11.11 7.23 0.45
GLN HE22 H 9236 3.59 10.35 7.02 0.44
GLN C C 11720 168.09 182.22 176.32 1.96
GLN CA C 16010 47.87 66.60 56.58 2.14
GLN CB C 14964 20.27 42.20 29.18 1.82
GLN CG C 10308 21.64 42.80 33.75 1.12
GLN CD C 984 171.37 183.54 179.72 1.29
GLN N N 17092 104.10 139.55 119.88 3.59
GLN NE2 N 8149 97.90 124.30 111.86 1.71
GLY H H 32523 3.01 12.22 8.33 0.65
GLY HA2 H 25001 0.84 6.43 3.97 0.37
GLY HA3 H 23614 1.01 6.39 3.90 0.37
GLY C C 20398 163.27 184.32 173.88 1.89
GLY CA C 28033 35.78 58.67 45.35 1.34
GLY N N 29550 42.65 162.19 109.66 3.86
HIS H H 9616 5.12 12.39 8.24 0.68
HIS HA H 7539 1.93 8.90 4.60 0.43
HIS HB2 H 6972 0.17 8.70 3.10 0.36
HIS HB3 H 6744 0.06 8.70 3.04 0.38
HIS HD1 H 319 3.79 17.20 8.68 2.61
HIS HD2 H 4997 3.46 9.01 7.01 0.43
HIS HE1 H 4049 3.21 10.88 7.95 0.48
HIS HE2 H 133 6.57 16.53 9.64 2.60
HIS C C 6059 166.90 182.80 175.25 1.98
HIS CA C 8438 46.01 66.98 56.53 2.32
HIS CB C 7918 18.75 43.30 30.24 2.08
HIS CG C 89 122.67 137.19 131.59 3.28
HIS CD2 C 3150 112.07 159.95 120.48 3.43
HIS CE1 C 2484 104.67 144.54 137.71 2.12
HIS N N 8838 105.00 136.48 119.68 3.99
HIS ND1 N 155 162.04 229.14 194.76 18.54
HIS NE2 N 168 161.70 226.29 182.25 14.19
ILE H H 23121 3.43 11.69 8.28 0.68
ILE HA H 17757 1.32 6.36 4.18 0.56
ILE HB H 16628 -1.28 3.87 1.78 0.29
ILE HG12 H 15114 -2.38 2.69 1.28 0.40
ILE HG13 H 14489 -2.04 2.99 1.19 0.41
ILE HG2 H 15833 -1.33 2.20 0.77 0.27
ILE HD1 H 15967 -1.08 2.82 0.68 0.29
ILE C C 15085 167.00 183.40 175.86 1.93
ILE CA C 20143 51.15 71.86 61.63 2.68
ILE CB C 18778 20.94 51.88 38.61 2.02
ILE CG1 C 12544 12.90 39.05 27.72 1.68
ILE CG2 C 13376 3.45 29.80 17.53 1.36
ILE CD1 C 13522 2.70 29.60 13.42 1.67
ILE N N 21492 99.00 138.12 121.45 4.27
LEU H H 38006 4.08 13.22 8.23 0.65
LEU HA H 29053 1.58 6.42 4.32 0.47
LEU HB2 H 26691 -1.25 3.18 1.61 0.34
LEU HB3 H 25381 -1.47 3.18 1.52 0.36
LEU HG H 23756 -1.06 3.90 1.51 0.33
LEU HD1 H 26256 -1.73 2.36 0.75 0.28
LEU HD2 H 25368 -1.65 2.78 0.73 0.29
LEU C C 24512 167.49 189.78 176.99 1.98
LEU CA C 32988 46.36 65.83 55.63 2.13
LEU CB C 30912 26.40 53.70 42.30 1.88
LEU CG C 19751 15.57 37.70 26.78 1.11
LEU CD1 C 21677 10.95 31.83 24.71 1.59
LEU CD2 C 20717 11.71 30.40 24.04 1.70
LEU N N 35287 98.56 144.55 121.85 3.90
LYS H H 32408 4.11 12.03 8.18 0.60
LYS HA H 24962 1.30 6.54 4.26 0.44
LYS HB2 H 22540 -0.75 4.05 1.78 0.25
LYS HB3 H 20995 -0.97 3.95 1.74 0.27
LYS HG2 H 20381 -1.16 3.13 1.37 0.26
LYS HG3 H 18547 -1.16 3.03 1.35 0.28
LYS HD2 H 18169 -0.67 7.71 1.61 0.22
LYS HD3 H 15990 -1.02 3.61 1.60 0.22
LYS HE2 H 18008 1.25 4.36 2.92 0.19
LYS HE3 H 15494 1.13 4.55 2.91 0.20
LYS HZ H 721 1.95 9.90 7.41 0.67
LYS C C 20002 121.16 185.00 176.64 2.00
LYS CA C 27174 40.73 64.57 56.96 2.20
LYS CB C 25407 21.19 46.60 32.78 1.78
LYS CG C 16438 12.11 36.22 24.89 1.14
LYS CD C 15618 21.24 40.10 28.95 1.08
LYS CE C 15175 30.70 52.20 41.89 0.83
LYS N N 29449 101.10 140.30 121.04 3.76
LYS NZ N 18 29.48 43.69 33.81 2.81
MET H H 9039 4.87 12.46 8.26 0.60
MET HA H 7179 1.13 6.35 4.41 0.48
MET HB2 H 6441 -1.05 3.87 2.02 0.34
MET HB3 H 5993 -0.99 3.22 1.99 0.34
MET HG2 H 5911 -0.36 4.40 2.42 0.35
MET HG3 H 5540 -0.30 4.24 2.39 0.38
MET HE H 4183 -0.21 17.06 1.89 0.46
MET C C 5873 167.40 183.16 176.18 2.09
MET CA C 8178 45.50 66.56 56.10 2.23
MET CB C 7511 20.98 46.46 32.98 2.24
MET CG C 4745 20.46 38.58 32.01 1.26
MET CE C 3602 0.00 37.40 17.08 1.58
MET N N 8467 87.60 135.66 120.08 3.57
PHE H H 16326 4.81 12.18 8.35 0.72
PHE HA H 12432 1.78 6.87 4.63 0.57
PHE HB2 H 11589 0.16 4.46 3.00 0.37
PHE HB3 H 11260 -0.21 4.69 2.93 0.40
PHE HD1 H 9821 4.97 8.15 7.06 0.30
PHE HD2 H 8236 4.97 8.15 7.06 0.31
PHE HE1 H 8634 4.38 8.80 7.08 0.31
PHE HE2 H 7361 4.38 8.80 7.08 0.32
PHE HZ H 6341 4.32 9.50 7.00 0.42
PHE C C 10361 166.85 184.16 175.42 2.00
PHE CA C 13927 47.31 69.82 58.09 2.58
PHE CB C 13037 25.52 48.53 39.97 2.10
PHE CG C 136 128.30 144.00 138.47 1.98
PHE CD1 C 5610 116.95 136.73 131.58 1.19
PHE CD2 C 3990 120.00 138.25 131.62 1.15
PHE CE1 C 4927 114.75 139.56 130.71 1.32
PHE CE2 C 3536 114.70 139.70 130.76 1.13
PHE CZ C 3867 116.46 138.60 129.21 1.43
PHE N N 15038 102.20 139.02 120.44 4.18
PRO HA H 14405 1.63 6.05 4.40 0.33
PRO HB2 H 13474 -0.28 4.35 2.08 0.35
PRO HB3 H 12994 -0.62 3.79 2.00 0.36
PRO HG2 H 12248 -0.47 4.42 1.93 0.31
PRO HG3 H 11277 -0.90 4.42 1.90 0.33
PRO HD2 H 12564 0.63 5.36 3.65 0.35
PRO HD3 H 12025 -0.26 5.36 3.62 0.39
PRO C C 11225 168.38 182.84 176.74 1.52
PRO CA C 15823 50.12 70.67 63.33 1.52
PRO CB C 14784 23.33 43.70 31.85 1.18
PRO CG C 10342 18.28 33.90 27.17 1.09
PRO CD C 10396 40.05 58.30 50.32 1.00
PRO N N 369 110.91 145.26 133.52 7.24
SER H H 28179 2.32 13.13 8.28 0.58
SER HA H 22331 1.58 6.85 4.48 0.40
SER HB2 H 20495 1.74 5.41 3.88 0.25
SER HB3 H 18783 1.55 5.27 3.85 0.27
SER HG H 292 0.00 8.97 5.37 1.02
SER C C 18106 164.47 184.88 174.62 1.73
SER CA C 24828 45.13 68.40 58.72 2.08
SER CB C 22978 46.69 76.39 63.79 1.48
SER N N 25748 99.62 133.68 116.27 3.52
THR H H 24524 5.54 11.73 8.24 0.62
THR HA H 18743 0.87 6.63 4.46 0.48
THR HB H 17158 0.92 8.35 4.17 0.33
THR HG1 H 566 0.32 8.95 4.90 1.59
THR HG2 H 17003 -1.19 3.54 1.14 0.23
THR C C 15199 165.50 184.43 174.54 1.76
THR CA C 20777 51.61 72.80 62.22 2.59
THR CB C 19208 43.10 80.22 69.72 1.63
THR CG2 C 13240 11.70 36.73 21.55 1.11
THR N N 22459 95.77 138.27 115.41 4.75
TRP H H 5217 5.16 11.76 8.29 0.78
TRP HA H 3972 2.24 6.55 4.68 0.52
TRP HB2 H 3717 0.42 4.54 3.19 0.35
TRP HB3 H 3583 0.31 4.44 3.12 0.36
TRP HD1 H 3329 4.90 10.75 7.14 0.36
TRP HE1 H 3582 5.12 14.39 10.08 0.66
TRP HE3 H 2950 4.89 8.92 7.31 0.41
TRP HZ2 H 3128 4.90 8.60 7.28 0.33
TRP HZ3 H 2856 3.88 8.90 6.86 0.40
TRP HH2 H 2900 4.39 10.90 6.98 0.39
TRP C C 3109 168.17 181.89 176.12 2.00
TRP CA C 4228 44.69 69.76 57.66 2.58
TRP CB C 3952 21.10 43.02 30.00 2.01
TRP CG C 109 105.30 116.53 110.59 1.88
TRP CD1 C 1973 108.45 132.35 126.51 1.84
TRP CD2 C 86 120.20 132.62 127.57 1.54
TRP CE2 C 78 113.89 177.71 138.31 7.02
TRP CE3 C 1682 93.34 137.60 120.43 1.80
TRP CZ2 C 1869 109.53 125.70 114.26 1.12
TRP CZ3 C 1702 98.61 138.39 121.35 1.53
TRP CH2 C 1756 112.43 131.54 123.86 1.41
TRP N N 4589 104.80 138.11 121.69 4.17
TRP NE1 N 2761 107.64 144.36 129.31 2.11
TYR H H 13817 4.16 12.01 8.32 0.73
TYR HA H 10732 1.20 6.73 4.63 0.56
TYR HB2 H 9989 0.31 4.70 2.91 0.37
TYR HB3 H 9726 -0.19 4.70 2.84 0.39
TYR HD1 H 8805 4.82 8.53 6.93 0.30
TYR HD2 H 7463 4.97 8.50 6.93 0.30
TYR HE1 H 8389 4.58 7.86 6.70 0.23
TYR HE2 H 7191 4.56 8.50 6.70 0.23
TYR HH H 148 5.99 13.75 9.29 1.35
TYR C C 8197 167.86 184.78 175.40 1.99
TYR CA C 11398 49.08 66.43 58.13 2.52
TYR CB C 10594 28.82 57.73 39.31 2.16
TYR CG C 115 117.70 174.59 129.76 4.79
TYR CD1 C 5009 116.44 141.57 132.77 1.17
TYR CD2 C 3463 113.00 137.80 132.72 1.31
TYR CE1 C 4973 110.70 135.80 117.93 1.20
TYR CE2 C 3429 112.58 134.01 117.90 1.18
TYR CZ C 99 153.54 162.70 156.81 1.93
TYR N N 12327 100.09 144.96 120.52 4.20
VAL H H 30160 3.98 12.59 8.29 0.67
VAL HA H 23201 0.97 6.30 4.18 0.58
VAL HB H 21767 -1.22 3.32 1.98 0.32
VAL HG1 H 21358 -1.12 2.57 0.83 0.26
VAL HG2 H 20864 -1.98 2.78 0.80 0.28
VAL C C 19416 165.65 183.95 175.62 1.90
VAL CA C 26119 50.16 70.34 62.49 2.86
VAL CB C 24431 20.55 45.33 32.73 1.79
VAL CG1 C 17477 13.53 32.27 21.49 1.36
VAL CG2 C 16838 13.58 30.46 21.26 1.56
VAL N N 28139 97.22 143.29 121.13 4.54
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