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 2729098 possible chemical shifts in the BMRB database, 2144558 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: 05-23-2008
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 20143 3.53 11.58 8.19 0.61
ALA HA H 15747 1.24 6.51 4.26 0.44
ALA HB H 14793 -0.76 3.12 1.36 0.26
ALA C C 11759 164.48 187.20 177.74 2.21
ALA CA C 16297 43.00 65.52 53.15 2.01
ALA CB C 15180 9.79 32.99 18.96 1.86
ALA N N 18064 77.10 142.81 123.19 3.60
ARG H H 13595 4.15 12.69 8.24 0.62
ARG HA H 10800 1.34 6.44 4.29 0.46
ARG HB2 H 9542 -0.45 3.29 1.80 0.27
ARG HB3 H 8745 -0.35 3.29 1.77 0.28
ARG HG2 H 8376 -0.64 3.24 1.57 0.27
ARG HG3 H 7423 -0.75 3.39 1.55 0.28
ARG HD2 H 8101 0.90 4.69 3.12 0.24
ARG HD3 H 7046 0.89 4.29 3.11 0.25
ARG HE H 3135 2.99 11.88 7.39 0.65
ARG HH11 H 324 5.82 9.82 6.88 0.46
ARG HH12 H 237 5.82 10.73 6.82 0.43
ARG HH21 H 295 4.59 9.21 6.79 0.38
ARG HH22 H 234 4.59 10.18 6.78 0.47
ARG C C 7492 167.44 184.51 176.45 2.09
ARG CA C 10670 45.00 67.98 56.80 2.34
ARG CB C 9612 20.95 42.50 30.64 1.88
ARG CG C 5821 18.22 37.83 27.21 1.25
ARG CD C 5975 35.05 49.06 43.14 0.95
ARG CZ C 125 156.20 175.90 159.77 2.99
ARG N N 11681 103.60 137.60 120.80 3.74
ARG NE N 1578 7.28 136.16 91.65 13.84
ARG NH1 N 57 7.41 112.50 74.50 13.24
ARG NH2 N 56 70.10 112.56 76.15 9.78
ASP H H 15919 4.16 12.61 8.32 0.58
ASP HA H 12498 2.33 6.34 4.60 0.32
ASP HB2 H 11458 -0.39 4.58 2.72 0.27
ASP HB3 H 10844 0.02 4.58 2.68 0.28
ASP C C 9429 166.80 182.70 176.44 1.80
ASP CA C 13064 39.80 62.49 54.65 2.08
ASP CB C 12093 28.00 51.09 40.82 1.67
ASP CG C 228 170.72 183.94 179.15 1.91
ASP N N 14410 101.90 143.52 120.73 3.95
ASN H H 11363 2.61 12.92 8.35 0.64
ASN HA H 9077 1.75 6.39 4.67 0.37
ASN HB2 H 8409 0.18 4.47 2.81 0.31
ASN HB3 H 8031 -0.09 4.47 2.77 0.34
ASN HD21 H 6071 3.34 9.66 7.34 0.49
ASN HD22 H 6023 3.05 10.80 7.14 0.50
ASN C C 6388 168.23 181.90 175.32 1.85
ASN CA C 9048 41.31 62.13 53.53 1.93
ASN CB C 8375 28.64 55.09 38.65 1.74
ASN CG C 696 166.40 181.20 176.78 1.35
ASN N N 9855 103.70 137.49 118.99 4.07
ASN ND2 N 4725 104.35 133.86 112.80 2.34
CYS H H 6409 4.73 12.12 8.40 0.67
CYS HA H 5672 1.64 6.43 4.68 0.56
CYS HB2 H 5395 -0.54 4.65 2.95 0.46
CYS HB3 H 5239 -0.83 4.69 2.90 0.49
CYS HG H 48 0.25 7.39 1.95 1.52
CYS C C 2364 166.73 182.73 174.80 2.10
CYS CA C 3436 42.45 66.85 57.98 3.40
CYS CB C 3088 19.12 62.07 33.22 6.45
CYS N N 4116 100.48 135.89 120.22 4.65
GLU H H 20734 4.31 12.17 8.34 0.60
GLU HA H 16431 1.77 6.29 4.25 0.41
GLU HB2 H 14676 0.34 3.44 2.03 0.21
GLU HB3 H 13337 0.34 3.44 2.01 0.22
GLU HG2 H 13403 0.57 3.77 2.28 0.22
GLU HG3 H 11972 0.44 3.80 2.27 0.22
GLU C C 12576 166.80 183.52 176.94 2.03
GLU CA C 17322 44.35 66.60 57.35 2.13
GLU CB C 15869 18.71 49.56 29.97 1.78
GLU CG C 10452 25.10 51.92 36.03 1.31
GLU CD C 247 173.41 189.46 182.36 2.22
GLU N N 19088 104.54 138.60 120.71 3.58
GLN H H 11053 5.18 12.04 8.22 0.59
GLN HA H 8801 1.60 6.23 4.27 0.43
GLN HB2 H 7841 -0.14 4.00 2.05 0.26
GLN HB3 H 7238 -0.52 4.04 2.02 0.28
GLN HG2 H 7277 0.06 3.66 2.31 0.28
GLN HG3 H 6402 -1.08 3.66 2.30 0.29
GLN HE21 H 5231 3.39 11.11 7.22 0.48
GLN HE22 H 5195 3.59 9.79 7.02 0.47
GLN C C 6492 168.09 182.22 176.34 2.01
GLN CA C 9166 46.82 66.60 56.55 2.16
GLN CB C 8388 20.27 42.20 29.14 1.88
GLN CG C 5527 21.64 41.95 33.73 1.18
GLN CD C 687 171.70 183.54 179.61 1.45
GLN N N 9978 105.26 139.55 119.93 3.70
GLN NE2 N 4352 92.49 133.30 111.85 1.93
GLY H H 19591 3.01 12.22 8.34 0.67
GLY HA2 H 15247 0.86 6.17 3.97 0.38
GLY HA3 H 14264 1.27 6.39 3.90 0.38
GLY C C 10908 163.27 183.16 173.95 1.91
GLY CA C 15510 35.50 55.80 45.33 1.32
GLY N N 17035 94.07 135.80 109.70 3.99
HIS H H 5848 5.24 11.39 8.25 0.68
HIS HA H 4604 1.93 8.90 4.62 0.45
HIS HB2 H 4153 0.37 8.70 3.11 0.37
HIS HB3 H 3978 0.52 8.70 3.05 0.39
HIS HD1 H 263 3.79 17.64 9.16 2.86
HIS HD2 H 2853 3.46 9.01 7.05 0.48
HIS HE1 H 2354 3.21 10.26 7.98 0.54
HIS HE2 H 122 6.58 16.53 10.08 2.80
HIS C C 3425 166.90 182.80 175.24 2.03
HIS CA C 4832 45.80 66.98 56.45 2.39
HIS CB C 4468 18.75 43.30 30.19 2.12
HIS CG C 63 122.67 137.19 131.21 3.45
HIS CD2 C 1333 112.07 159.95 119.87 2.99
HIS CE1 C 965 115.52 144.54 137.15 2.29
HIS N N 5207 105.00 136.48 119.55 4.10
HIS ND1 N 185 110.10 256.60 193.81 33.68
HIS NE2 N 184 114.71 247.15 178.26 18.77
ILE H H 14206 3.43 11.69 8.28 0.70
ILE HA H 11213 1.32 6.37 4.19 0.56
ILE HB H 10389 -1.28 3.87 1.79 0.29
ILE HG12 H 9244 -2.12 2.69 1.28 0.40
ILE HG13 H 8695 -2.04 2.99 1.21 0.41
ILE HG2 H 9835 -1.14 1.87 0.78 0.27
ILE HD1 H 9798 -1.18 2.82 0.68 0.30
ILE C C 8594 167.00 183.40 175.85 1.98
ILE CA C 11797 51.15 71.70 61.57 2.72
ILE CB C 10809 20.94 51.88 38.59 2.08
ILE CG1 C 6973 9.80 39.05 27.66 1.85
ILE CG2 C 7561 3.45 29.80 17.51 1.50
ILE CD1 C 7622 2.70 29.60 13.44 1.74
ILE N N 12813 99.00 138.12 121.51 4.38
LEU H H 23029 4.89 13.22 8.22 0.66
LEU HA H 17960 1.58 6.24 4.32 0.47
LEU HB2 H 16116 -1.31 3.18 1.62 0.35
LEU HB3 H 15075 -1.51 3.18 1.54 0.37
LEU HG H 14152 -1.06 3.90 1.51 0.34
LEU HD1 H 15758 -1.65 2.36 0.76 0.28
LEU HD2 H 15037 -1.65 2.78 0.73 0.29
LEU C C 13772 167.49 189.78 177.00 2.05
LEU CA C 18992 44.60 67.11 55.64 2.17
LEU CB C 17496 26.40 53.70 42.24 1.90
LEU CG C 10617 15.57 41.22 26.74 1.23
LEU CD1 C 11913 10.95 31.83 24.61 1.66
LEU CD2 C 11193 12.50 30.40 24.08 1.73
LEU N N 20808 98.56 144.55 121.84 3.95
LYS H H 20375 3.63 12.46 8.19 0.61
LYS HA H 15921 1.42 6.17 4.27 0.44
LYS HB2 H 14080 -0.18 3.77 1.78 0.25
LYS HB3 H 12860 -0.45 3.77 1.76 0.26
LYS HG2 H 12421 -0.82 3.01 1.38 0.26
LYS HG3 H 10974 -0.87 2.99 1.36 0.28
LYS HD2 H 10768 -1.68 7.71 1.61 0.23
LYS HD3 H 9147 -1.02 3.61 1.60 0.24
LYS HE2 H 10584 1.17 4.36 2.92 0.19
LYS HE3 H 8817 1.13 4.55 2.92 0.20
LYS HZ H 645 2.25 9.90 7.40 0.74
LYS C C 11245 121.16 185.00 176.70 2.08
LYS CA C 15851 46.10 63.38 56.96 2.22
LYS CB C 14550 21.19 46.60 32.75 1.85
LYS CG C 8999 17.30 36.22 24.89 1.21
LYS CD C 8501 21.20 42.60 28.90 1.27
LYS CE C 8183 29.22 52.20 41.85 0.92
LYS N N 17843 101.10 140.30 121.04 3.84
LYS NZ N 22 31.00 131.04 67.27 43.20
MET H H 5580 4.87 11.89 8.25 0.60
MET HA H 4555 1.81 6.35 4.40 0.48
MET HB2 H 4014 -1.05 3.87 2.04 0.34
MET HB3 H 3704 -0.99 3.15 2.00 0.35
MET HG2 H 3629 -0.41 4.40 2.43 0.36
MET HG3 H 3369 -0.47 4.24 2.40 0.39
MET HE H 2330 -0.21 17.06 1.89 0.49
MET C C 3368 168.20 183.16 176.21 2.11
MET CA C 4822 45.50 66.56 56.12 2.24
MET CB C 4342 21.40 46.46 32.98 2.27
MET CG C 2656 20.46 38.58 32.01 1.29
MET CE C 1791 0.00 40.77 17.21 2.08
MET N N 5056 87.60 134.80 120.05 3.62
PHE H H 10183 4.81 11.78 8.36 0.72
PHE HA H 7921 1.78 6.56 4.61 0.57
PHE HB2 H 7302 0.17 4.32 2.99 0.37
PHE HB3 H 7036 0.30 4.31 2.95 0.39
PHE HD1 H 6030 4.97 8.08 7.06 0.31
PHE HD2 H 4630 4.97 8.15 7.07 0.30
PHE HE1 H 5314 5.18 8.80 7.09 0.32
PHE HE2 H 4140 5.18 8.80 7.09 0.32
PHE HZ H 3756 4.53 9.50 7.02 0.42
PHE C C 5873 166.85 183.77 175.52 2.04
PHE CA C 8189 47.31 69.82 58.15 2.63
PHE CB C 7554 25.52 50.40 39.90 2.10
PHE CG C 61 128.30 141.34 137.90 2.08
PHE CD1 C 2614 118.50 135.90 131.46 1.29
PHE CD2 C 1551 120.00 137.20 131.47 1.23
PHE CE1 C 2160 114.75 135.60 130.61 1.55
PHE CE2 C 1274 118.03 134.10 130.69 1.25
PHE CZ C 1557 116.46 138.60 129.19 1.73
PHE N N 9069 102.20 139.02 120.58 4.19
PRO H2 H 1 8.51 8.51 8.51 0.00
PRO HA H 8567 1.63 6.05 4.39 0.34
PRO HB2 H 7856 -0.78 4.02 2.07 0.35
PRO HB3 H 7460 -0.58 3.79 2.02 0.36
PRO HG2 H 6931 -0.93 3.90 1.93 0.33
PRO HG3 H 6244 -0.90 3.90 1.91 0.34
PRO HD2 H 7167 0.08 5.36 3.65 0.36
PRO HD3 H 6780 -0.26 5.36 3.62 0.39
PRO C C 6128 168.43 182.30 176.71 1.59
PRO CA C 8744 50.12 70.67 63.31 1.59
PRO CB C 7970 25.44 43.70 31.81 1.25
PRO CG C 5152 19.31 33.39 27.20 1.15
PRO CD C 5232 40.05 57.09 50.34 1.03
PRO N N 207 31.27 145.26 131.97 10.84
SER H H 16715 3.76 13.13 8.29 0.60
SER HA H 13340 1.91 6.46 4.49 0.41
SER HB2 H 11988 1.62 5.41 3.88 0.27
SER HB3 H 10767 1.49 5.01 3.85 0.29
SER HG H 214 0.00 9.36 5.31 1.09
SER C C 9483 164.47 184.88 174.66 1.82
SER CA C 13590 45.13 68.40 58.71 2.16
SER CB C 12284 52.61 73.90 63.77 1.55
SER N N 14644 100.85 133.68 116.27 3.66
THR H H 15195 5.54 11.57 8.25 0.62
THR HA H 12011 0.87 6.36 4.47 0.49
THR HB H 10882 0.92 5.90 4.17 0.33
THR HG1 H 361 0.32 8.21 5.17 1.39
THR HG2 H 10796 -0.84 3.54 1.14 0.23
THR C C 8481 165.50 184.43 174.57 1.82
THR CA C 12046 51.61 72.80 62.18 2.67
THR CB C 10939 29.97 80.22 69.65 1.82
THR CG2 C 7406 11.70 38.90 21.52 1.21
THR N N 13402 97.70 134.00 115.49 4.85
TRP H H 3194 4.49 11.67 8.31 0.79
TRP HA H 2486 2.28 6.52 4.69 0.53
TRP HB2 H 2311 0.42 4.54 3.19 0.36
TRP HB3 H 2207 0.77 4.44 3.14 0.37
TRP HD1 H 2075 4.69 8.93 7.14 0.36
TRP HE1 H 2229 5.16 13.29 10.10 0.57
TRP HE3 H 1834 4.89 8.79 7.32 0.41
TRP HZ2 H 1956 4.90 8.18 7.29 0.33
TRP HZ3 H 1794 3.88 8.90 6.87 0.42
TRP HH2 H 1804 4.92 10.90 6.99 0.41
TRP C C 1725 168.17 181.89 176.09 2.02
TRP CA C 2412 44.69 69.76 57.65 2.60
TRP CB C 2223 21.10 43.02 29.98 2.04
TRP CG C 89 105.30 114.60 110.28 1.61
TRP CD1 C 959 109.30 132.35 126.40 2.06
TRP CD2 C 74 120.20 130.10 127.39 1.37
TRP CE2 C 62 118.37 177.71 138.28 7.65
TRP CE3 C 793 107.68 137.60 120.51 2.18
TRP CZ2 C 904 81.81 124.10 114.13 1.71
TRP CZ3 C 805 113.32 138.39 121.38 1.78
TRP CH2 C 831 91.62 131.54 123.66 2.08
TRP N N 2687 106.44 134.89 121.77 4.29
TRP NE1 N 1588 106.75 147.43 129.39 2.28
TYR H H 8629 5.06 11.96 8.33 0.74
TYR HA H 6828 1.20 6.73 4.63 0.57
TYR HB2 H 6314 0.68 4.70 2.90 0.37
TYR HB3 H 6082 -0.19 4.70 2.86 0.39
TYR HD1 H 5688 4.98 8.53 6.94 0.30
TYR HD2 H 4461 5.12 10.50 6.94 0.30
TYR HE1 H 5446 4.58 7.86 6.71 0.23
TYR HE2 H 4300 4.56 8.50 6.71 0.24
TYR HH H 118 5.99 13.75 9.20 1.47
TYR C C 4538 167.86 182.92 175.43 2.02
TYR CA C 6575 45.20 65.80 58.10 2.58
TYR CB C 6002 28.82 57.73 39.27 2.20
TYR CG C 77 117.70 138.70 129.25 2.63
TYR CD1 C 2490 116.44 138.65 132.69 1.36
TYR CD2 C 1435 113.00 136.70 132.60 1.61
TYR CE1 C 2436 110.70 134.01 117.89 1.40
TYR CE2 C 1411 113.10 134.01 117.88 1.55
TYR CZ C 66 153.54 162.70 156.43 2.23
TYR N N 7319 100.09 144.96 120.66 4.32
VAL H H 18192 3.98 11.66 8.29 0.69
VAL HA H 14385 0.97 6.24 4.19 0.58
VAL HB H 13344 -0.56 3.63 1.98 0.32
VAL HG1 H 13051 -1.09 2.56 0.83 0.26
VAL HG2 H 12602 -2.32 3.32 0.81 0.29
VAL C C 10631 165.65 183.21 175.63 1.95
VAL CA C 14873 44.98 70.02 62.42 2.91
VAL CB C 13665 20.55 42.84 32.69 1.84
VAL CG1 C 9581 11.60 32.27 21.44 1.44
VAL CG2 C 9085 11.30 31.10 21.29 1.61
VAL N N 16425 97.95 143.29 121.14 4.67
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