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 2716048 possible chemical shifts in the BMRB database, 2138079 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: 04-23-2008
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 20088 3.53 11.58 8.19 0.61
ALA HA H 15693 1.24 6.51 4.26 0.44
ALA HB H 14739 -0.76 3.12 1.36 0.26
ALA C C 11727 164.48 187.20 177.75 2.20
ALA CA C 16257 43.00 65.52 53.15 2.01
ALA CB C 15140 9.79 32.99 18.95 1.85
ALA N N 18026 77.10 142.81 123.19 3.60
ARG H H 13566 4.15 12.69 8.24 0.62
ARG HA H 10771 1.34 6.44 4.29 0.46
ARG HB2 H 9510 -0.45 3.29 1.80 0.27
ARG HB3 H 8715 -0.35 3.29 1.77 0.28
ARG HG2 H 8349 -0.64 3.24 1.57 0.27
ARG HG3 H 7395 -0.75 3.39 1.55 0.28
ARG HD2 H 8072 0.90 4.69 3.12 0.24
ARG HD3 H 7019 0.89 4.29 3.11 0.25
ARG HE H 3131 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 7474 167.44 184.51 176.45 2.09
ARG CA C 10646 45.00 67.98 56.80 2.34
ARG CB C 9589 20.95 42.50 30.64 1.87
ARG CG C 5794 18.22 37.83 27.21 1.25
ARG CD C 5947 35.05 49.06 43.14 0.95
ARG CZ C 124 156.20 175.66 159.64 2.62
ARG N N 11657 103.60 137.60 120.80 3.74
ARG NE N 1576 7.28 136.16 91.66 13.85
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 15888 4.16 12.61 8.32 0.58
ASP HA H 12469 2.33 6.34 4.60 0.32
ASP HB2 H 11427 -0.39 4.58 2.72 0.27
ASP HB3 H 10809 0.02 4.58 2.68 0.28
ASP C C 9406 166.80 182.70 176.44 1.80
ASP CA C 13033 39.80 62.49 54.65 2.08
ASP CB C 12062 28.00 51.09 40.82 1.67
ASP CG C 228 170.72 183.94 179.15 1.91
ASP N N 14379 101.90 143.52 120.73 3.95
ASN H H 11328 2.61 12.92 8.35 0.64
ASN HA H 9046 1.75 6.39 4.67 0.37
ASN HB2 H 8378 0.18 4.47 2.81 0.31
ASN HB3 H 7998 -0.09 4.47 2.77 0.34
ASN HD21 H 6043 3.34 9.66 7.34 0.49
ASN HD22 H 5995 3.05 10.80 7.14 0.50
ASN C C 6369 168.23 181.90 175.32 1.85
ASN CA C 9013 41.31 62.13 53.53 1.93
ASN CB C 8340 28.64 55.09 38.65 1.74
ASN CG C 688 166.40 181.20 176.78 1.35
ASN N N 9822 103.70 137.49 118.99 4.07
ASN ND2 N 4699 104.35 133.86 112.81 2.34
CYS H H 6393 4.73 12.12 8.40 0.67
CYS HA H 5656 1.64 6.43 4.68 0.56
CYS HB2 H 5379 -0.54 4.65 2.95 0.46
CYS HB3 H 5223 -0.83 4.69 2.90 0.49
CYS HG H 48 0.25 7.39 1.95 1.52
CYS C C 2362 166.73 182.73 174.80 2.10
CYS CA C 3423 42.45 66.85 57.98 3.40
CYS CB C 3075 19.12 62.07 33.24 6.46
CYS N N 4103 100.48 135.89 120.22 4.64
GLU H H 20678 4.31 12.17 8.34 0.60
GLU HA H 16375 1.77 6.29 4.25 0.41
GLU HB2 H 14620 0.34 3.44 2.03 0.21
GLU HB3 H 13282 0.34 3.44 2.01 0.22
GLU HG2 H 13347 0.57 3.77 2.28 0.22
GLU HG3 H 11910 0.44 3.80 2.27 0.22
GLU C C 12541 166.80 183.52 176.95 2.02
GLU CA C 17272 44.35 66.60 57.35 2.12
GLU CB C 15826 18.71 49.56 29.97 1.78
GLU CG C 10405 25.10 51.92 36.03 1.31
GLU CD C 247 173.41 189.46 182.36 2.22
GLU N N 19039 104.54 138.60 120.71 3.58
GLN H H 11028 5.18 12.04 8.22 0.59
GLN HA H 8779 1.60 6.23 4.27 0.43
GLN HB2 H 7820 -0.14 4.00 2.05 0.26
GLN HB3 H 7218 -0.52 4.04 2.02 0.28
GLN HG2 H 7258 0.06 3.66 2.32 0.28
GLN HG3 H 6377 -1.08 3.66 2.30 0.29
GLN HE21 H 5215 3.39 11.11 7.22 0.48
GLN HE22 H 5179 3.59 9.79 7.02 0.47
GLN C C 6486 168.09 182.22 176.34 2.00
GLN CA C 9140 46.82 66.60 56.55 2.16
GLN CB C 8363 20.27 42.20 29.14 1.88
GLN CG C 5503 21.64 41.95 33.74 1.18
GLN CD C 685 171.70 183.54 179.62 1.46
GLN N N 9955 105.26 139.55 119.93 3.69
GLN NE2 N 4336 92.49 133.30 111.85 1.93
GLY H H 19534 3.01 12.22 8.34 0.67
GLY HA2 H 15197 0.86 6.17 3.97 0.38
GLY HA3 H 14205 1.27 5.83 3.90 0.38
GLY C C 10879 163.27 183.16 173.95 1.91
GLY CA C 15462 35.50 55.80 45.33 1.32
GLY N N 16989 94.07 135.80 109.70 3.99
HIS H H 5833 5.24 11.39 8.25 0.68
HIS HA H 4588 1.93 8.90 4.62 0.45
HIS HB2 H 4136 0.37 8.70 3.11 0.37
HIS HB3 H 3961 0.52 8.70 3.05 0.39
HIS HD1 H 263 3.79 17.64 9.16 2.86
HIS HD2 H 2839 3.46 9.01 7.05 0.48
HIS HE1 H 2345 3.21 10.26 7.98 0.54
HIS HE2 H 122 6.58 16.53 10.08 2.80
HIS C C 3418 166.90 182.80 175.24 2.03
HIS CA C 4817 45.80 66.98 56.45 2.39
HIS CB C 4453 18.75 43.30 30.18 2.12
HIS CG C 63 122.67 137.19 131.21 3.45
HIS CD2 C 1327 112.07 159.95 119.87 2.98
HIS CE1 C 959 115.52 144.54 137.15 2.30
HIS N N 5193 105.00 136.48 119.55 4.10
HIS ND1 N 183 110.10 256.60 193.51 33.64
HIS NE2 N 182 114.71 247.15 178.31 18.87
ILE H H 14176 3.43 11.69 8.28 0.70
ILE HA H 11184 1.32 6.37 4.19 0.56
ILE HB H 10360 -1.28 3.87 1.79 0.29
ILE HG12 H 9216 -2.12 2.69 1.28 0.40
ILE HG13 H 8667 -2.04 2.99 1.21 0.41
ILE HG2 H 9811 -1.14 1.87 0.78 0.27
ILE HD1 H 9770 -1.18 2.82 0.68 0.30
ILE C C 8573 167.00 183.40 175.85 1.98
ILE CA C 11772 51.15 71.70 61.57 2.72
ILE CB C 10784 20.94 51.88 38.59 2.08
ILE CG1 C 6946 9.80 39.05 27.67 1.85
ILE CG2 C 7534 3.45 29.80 17.52 1.50
ILE CD1 C 7595 2.70 29.60 13.44 1.74
ILE N N 12787 99.00 138.12 121.51 4.39
LEU H H 22990 4.89 13.22 8.22 0.66
LEU HA H 17924 1.58 6.24 4.32 0.46
LEU HB2 H 16081 -1.31 3.18 1.62 0.35
LEU HB3 H 15034 -1.51 3.18 1.54 0.37
LEU HG H 14117 -1.06 3.90 1.51 0.34
LEU HD1 H 15721 -1.65 2.36 0.76 0.28
LEU HD2 H 15000 -1.65 2.78 0.73 0.29
LEU C C 13751 167.49 189.78 177.00 2.05
LEU CA C 18953 44.60 67.11 55.64 2.17
LEU CB C 17456 26.40 53.70 42.24 1.90
LEU CG C 10581 15.57 41.22 26.74 1.23
LEU CD1 C 11878 10.95 31.83 24.61 1.66
LEU CD2 C 11159 12.50 30.40 24.08 1.73
LEU N N 20769 98.56 144.55 121.84 3.95
LYS H H 20319 3.63 12.46 8.19 0.61
LYS HA H 15867 1.42 6.17 4.27 0.44
LYS HB2 H 14021 -0.18 3.77 1.78 0.25
LYS HB3 H 12808 -0.45 3.77 1.76 0.26
LYS HG2 H 12373 -0.82 3.01 1.38 0.26
LYS HG3 H 10924 -0.87 2.99 1.36 0.28
LYS HD2 H 10722 -1.68 7.71 1.61 0.24
LYS HD3 H 9105 -1.02 3.61 1.60 0.24
LYS HE2 H 10532 1.17 4.36 2.92 0.19
LYS HE3 H 8769 1.13 4.55 2.92 0.20
LYS HZ H 645 2.25 9.90 7.40 0.74
LYS C C 11216 121.16 185.00 176.70 2.08
LYS CA C 15802 46.10 63.38 56.96 2.22
LYS CB C 14502 21.19 46.60 32.75 1.85
LYS CG C 8953 17.30 36.22 24.90 1.21
LYS CD C 8457 21.20 42.60 28.90 1.27
LYS CE C 8137 29.22 52.20 41.85 0.92
LYS N N 17796 101.10 140.30 121.04 3.84
LYS NZ N 22 31.00 131.04 67.27 43.20
MET H H 5564 4.87 11.89 8.25 0.60
MET HA H 4536 1.81 6.35 4.40 0.48
MET HB2 H 3997 -1.05 3.87 2.04 0.34
MET HB3 H 3686 -0.99 3.15 2.00 0.35
MET HG2 H 3613 -0.41 4.40 2.43 0.36
MET HG3 H 3351 -0.47 4.24 2.40 0.39
MET HE H 2320 -0.21 17.06 1.89 0.49
MET C C 3358 168.20 183.16 176.21 2.11
MET CA C 4806 45.50 66.56 56.13 2.24
MET CB C 4327 21.40 46.46 32.98 2.27
MET CG C 2643 20.46 38.58 32.01 1.29
MET CE C 1781 0.00 40.77 17.21 2.08
MET N N 5043 87.60 134.80 120.05 3.62
PHE H H 10156 4.81 11.78 8.36 0.72
PHE HA H 7893 1.78 6.56 4.61 0.57
PHE HB2 H 7273 0.17 4.32 2.99 0.37
PHE HB3 H 7008 0.30 4.31 2.95 0.39
PHE HD1 H 6002 4.31 8.08 7.06 0.31
PHE HD2 H 4610 4.97 8.15 7.07 0.30
PHE HE1 H 5291 5.18 8.80 7.09 0.32
PHE HE2 H 4124 5.18 8.80 7.09 0.32
PHE HZ H 3739 4.53 9.50 7.02 0.42
PHE C C 5847 166.85 183.77 175.53 2.04
PHE CA C 8161 47.31 69.82 58.15 2.63
PHE CB C 7527 25.52 50.40 39.89 2.10
PHE CG C 61 128.30 141.34 137.90 2.08
PHE CD1 C 2599 118.50 135.90 131.46 1.29
PHE CD2 C 1543 120.00 137.20 131.47 1.23
PHE CE1 C 2147 114.75 135.60 130.60 1.55
PHE CE2 C 1268 118.03 134.10 130.69 1.25
PHE CZ C 1547 116.46 138.60 129.19 1.74
PHE N N 9042 102.20 139.02 120.58 4.19
PRO H2 H 1 8.51 8.51 8.51 0.00
PRO HA H 8549 1.63 6.05 4.39 0.34
PRO HB2 H 7836 -0.78 4.02 2.07 0.35
PRO HB3 H 7440 -0.58 3.79 2.02 0.36
PRO HG2 H 6915 -0.93 3.90 1.93 0.33
PRO HG3 H 6231 -0.90 3.90 1.91 0.34
PRO HD2 H 7147 0.08 5.36 3.65 0.36
PRO HD3 H 6762 -0.26 5.36 3.62 0.39
PRO C C 6118 168.43 182.30 176.71 1.58
PRO CA C 8725 50.12 70.67 63.31 1.59
PRO CB C 7951 25.44 43.70 31.81 1.25
PRO CG C 5136 19.31 33.39 27.20 1.15
PRO CD C 5215 40.05 57.09 50.34 1.03
PRO N N 207 31.27 145.26 131.97 10.84
SER H H 16677 3.76 13.13 8.29 0.60
SER HA H 13307 1.91 6.46 4.49 0.41
SER HB2 H 11955 1.62 5.41 3.88 0.26
SER HB3 H 10730 1.49 5.01 3.85 0.29
SER HG H 213 0.00 9.36 5.31 1.09
SER C C 9459 164.47 184.88 174.66 1.82
SER CA C 13554 45.13 68.40 58.71 2.16
SER CB C 12248 52.61 73.90 63.77 1.55
SER N N 14608 100.85 133.68 116.27 3.66
THR H H 15157 5.54 11.57 8.25 0.62
THR HA H 11981 0.87 6.36 4.47 0.49
THR HB H 10853 0.92 5.90 4.17 0.33
THR HG1 H 359 0.32 8.21 5.17 1.39
THR HG2 H 10767 -0.84 3.54 1.14 0.23
THR C C 8458 165.50 184.43 174.57 1.82
THR CA C 12012 51.61 72.80 62.18 2.67
THR CB C 10905 29.97 80.22 69.65 1.82
THR CG2 C 7377 11.70 38.90 21.52 1.21
THR N N 13369 97.70 134.00 115.49 4.85
TRP H H 3185 4.49 11.67 8.31 0.79
TRP HA H 2477 2.28 6.52 4.69 0.53
TRP HB2 H 2302 0.42 4.54 3.19 0.36
TRP HB3 H 2198 0.77 4.44 3.14 0.37
TRP HD1 H 2066 4.69 8.93 7.14 0.36
TRP HE1 H 2220 5.16 13.29 10.10 0.57
TRP HE3 H 1827 4.89 8.79 7.32 0.41
TRP HZ2 H 1949 4.90 8.18 7.29 0.33
TRP HZ3 H 1787 3.88 8.90 6.86 0.42
TRP HH2 H 1797 4.92 10.90 6.99 0.41
TRP C C 1723 168.17 181.89 176.09 2.02
TRP CA C 2406 44.69 69.76 57.65 2.60
TRP CB C 2217 21.10 43.02 29.98 2.04
TRP CG C 89 105.30 114.60 110.28 1.61
TRP CD1 C 955 109.30 132.35 126.40 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 789 107.68 137.60 120.51 2.18
TRP CZ2 C 900 81.81 124.10 114.13 1.72
TRP CZ3 C 801 113.32 138.39 121.38 1.78
TRP CH2 C 827 91.62 131.54 123.65 2.09
TRP N N 2681 106.44 134.89 121.77 4.28
TRP NE1 N 1582 106.75 147.43 129.39 2.28
TYR H H 8604 5.06 11.96 8.33 0.74
TYR HA H 6805 1.20 6.73 4.63 0.56
TYR HB2 H 6290 0.68 4.70 2.90 0.37
TYR HB3 H 6059 -0.19 4.70 2.86 0.39
TYR HD1 H 5663 4.98 8.53 6.94 0.30
TYR HD2 H 4443 5.12 10.50 6.94 0.30
TYR HE1 H 5428 4.58 7.86 6.71 0.23
TYR HE2 H 4285 4.56 8.50 6.71 0.24
TYR HH H 118 5.99 13.75 9.20 1.47
TYR C C 4525 167.86 182.92 175.43 2.02
TYR CA C 6556 45.20 65.80 58.10 2.58
TYR CB C 5983 28.82 57.73 39.27 2.20
TYR CG C 77 117.70 138.70 129.25 2.63
TYR CD1 C 2482 116.44 138.65 132.69 1.36
TYR CD2 C 1432 113.00 136.70 132.60 1.61
TYR CE1 C 2428 110.70 134.01 117.89 1.41
TYR CE2 C 1408 113.10 134.01 117.88 1.55
TYR CZ C 66 153.54 162.70 156.43 2.23
TYR N N 7300 100.09 144.96 120.66 4.32
VAL H H 18154 3.98 11.66 8.29 0.69
VAL HA H 14350 0.97 6.24 4.19 0.58
VAL HB H 13309 -0.56 3.63 1.98 0.32
VAL HG1 H 13012 -1.09 2.56 0.83 0.26
VAL HG2 H 12567 -2.32 3.32 0.81 0.29
VAL C C 10610 165.65 183.21 175.64 1.95
VAL CA C 14836 44.98 70.02 62.42 2.91
VAL CB C 13628 20.55 42.84 32.69 1.84
VAL CG1 C 9544 11.60 32.27 21.44 1.44
VAL CG2 C 9049 11.30 31.10 21.29 1.61
VAL N N 16388 97.95 143.29 121.14 4.67
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