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 6051591 possible chemical shifts in the BMRB database, 4425378 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: 09-12-2013
Amino Atom Atom Number Minimum Maximum Average Standard
Acid Name Type of Shifts Shift Shift Shift Deviation
ALA H H 39801 3.53 12.11 8.19 0.60
ALA HA H 29581 0.87 6.51 4.25 0.43
ALA HB H 28092 -0.88 3.12 1.36 0.25
ALA C C 25545 164.48 187.20 177.80 2.12
ALA CA C 34669 44.22 65.52 53.20 1.96
ALA CB C 32851 9.79 28.80 18.98 1.78
ALA N N 37261 98.05 142.81 123.21 3.49
ARG H H 26906 3.57 12.69 8.23 0.61
ARG HA H 20630 1.34 6.52 4.29 0.46
ARG HB2 H 18670 -0.61 3.49 1.79 0.26
ARG HB3 H 17619 -0.86 3.32 1.76 0.28
ARG HG2 H 16767 -0.64 3.51 1.57 0.27
ARG HG3 H 15386 -0.74 3.51 1.54 0.29
ARG HD2 H 16434 1.04 4.69 3.12 0.24
ARG HD3 H 14891 0.89 4.56 3.10 0.26
ARG HE H 5064 2.99 11.88 7.39 0.63
ARG HH11 H 449 5.88 9.82 6.90 0.45
ARG HH12 H 326 5.92 10.73 6.82 0.40
ARG HH21 H 401 4.85 11.35 6.80 0.47
ARG HH22 H 308 5.92 10.18 6.78 0.39
ARG C C 16380 167.44 184.51 176.46 2.02
ARG CA C 22804 43.27 67.98 56.82 2.31
ARG CB C 21212 20.95 42.50 30.65 1.82
ARG CG C 13595 18.22 39.98 27.21 1.18
ARG CD C 13738 35.05 50.88 43.16 0.89
ARG CZ C 342 156.49 179.69 160.11 2.97
ARG N N 24408 102.78 137.60 120.76 3.65
ARG NE N 2885 67.00 99.81 84.59 1.63
ARG NH1 N 82 67.60 87.79 74.03 4.96
ARG NH2 N 74 69.90 85.28 72.89 2.98
ASP H H 31676 4.06 12.68 8.30 0.57
ASP HA H 23600 2.33 6.33 4.59 0.32
ASP HB2 H 22004 -0.39 4.58 2.72 0.26
ASP HB3 H 21068 -0.23 4.58 2.66 0.28
ASP HD2 H 2 4.65 9.29 6.97 3.28
ASP C C 20194 166.80 182.70 176.44 1.74
ASP CA C 27585 41.11 67.17 54.71 2.05
ASP CB C 26079 27.48 54.95 40.88 1.61
ASP CG C 404 170.72 186.50 179.31 1.83
ASP N N 29848 101.90 143.52 120.63 3.82
ASN H H 22343 2.61 12.40 8.33 0.62
ASN HA H 17155 1.92 6.43 4.66 0.36
ASN HB2 H 16052 0.18 4.47 2.81 0.32
ASN HB3 H 15414 -0.07 4.47 2.75 0.33
ASN HD21 H 12033 3.55 10.38 7.33 0.48
ASN HD22 H 11837 3.05 10.80 7.15 0.49
ASN C C 13836 167.04 185.30 175.30 1.80
ASN CA C 19216 44.78 66.21 53.57 1.89
ASN CB C 18209 26.45 48.78 38.69 1.66
ASN CG C 1300 166.40 183.10 176.76 1.41
ASN N N 20439 101.71 137.49 118.89 3.98
ASN ND2 N 10146 99.40 134.50 112.77 2.32
CYS H H 11635 4.73 12.12 8.38 0.67
CYS HA H 9997 1.64 6.45 4.64 0.55
CYS HB2 H 9620 -0.54 4.72 2.95 0.44
CYS HB3 H 9371 -0.83 4.77 2.89 0.46
CYS HG H 90 0.10 7.39 1.96 1.30
CYS C C 5554 166.73 182.73 174.98 2.03
CYS CA C 7785 42.45 67.64 58.31 3.38
CYS CB C 7313 17.99 62.07 32.65 6.11
CYS N N 8594 100.48 135.89 120.11 4.53
GLU H H 41240 4.31 12.69 8.33 0.59
GLU HA H 31141 1.65 6.29 4.25 0.41
GLU HB2 H 28444 0.34 3.37 2.02 0.21
GLU HB3 H 26584 0.34 3.47 2.00 0.22
GLU HG2 H 26450 0.53 3.77 2.27 0.21
GLU HG3 H 24452 0.56 3.80 2.25 0.21
GLU HE2 H 1 2.73 2.73 2.73 0.00
GLU C C 26966 166.80 183.52 176.93 1.94
GLU CA C 36393 44.35 65.06 57.37 2.08
GLU CB C 34145 18.71 46.75 29.98 1.70
GLU CG C 22984 25.31 44.34 36.11 1.18
GLU CD C 440 173.41 189.46 182.60 1.79
GLU N N 39215 104.54 138.60 120.65 3.47
GLN H H 22491 3.51 12.04 8.21 0.58
GLN HA H 17182 1.57 6.34 4.26 0.43
GLN HB2 H 15695 -0.07 4.00 2.05 0.25
GLN HB3 H 14839 -0.35 4.04 2.02 0.27
GLN HG2 H 14793 0.04 3.66 2.32 0.26
GLN HG3 H 13529 -0.41 3.66 2.29 0.28
GLN HE21 H 11046 3.39 11.11 7.22 0.45
GLN HE22 H 10985 3.59 10.35 7.03 0.44
GLN C C 14382 168.09 182.63 176.37 1.95
GLN CA C 19885 43.45 66.60 56.63 2.14
GLN CB C 18679 20.27 42.20 29.16 1.81
GLN CG C 12715 21.64 42.80 33.76 1.10
GLN CD C 1230 171.37 183.54 179.73 1.25
GLN N N 21083 103.88 139.55 119.84 3.56
GLN NE2 N 9772 97.90 125.33 111.87 1.68
GLY H H 39296 3.01 12.22 8.33 0.64
GLY HA2 H 29563 0.84 6.43 3.97 0.37
GLY HA3 H 27941 1.01 6.39 3.90 0.37
GLY C C 24827 163.27 184.32 173.88 1.89
GLY CA C 34303 35.78 57.88 45.37 1.27
GLY N N 36083 93.60 162.19 109.60 3.78
HIS H H 11531 3.97 12.39 8.24 0.68
HIS HA H 8998 1.93 8.90 4.60 0.43
HIS HB2 H 8355 0.17 8.70 3.11 0.35
HIS HB3 H 8077 -0.39 8.70 3.05 0.38
HIS HD1 H 384 3.79 17.20 8.69 2.57
HIS HD2 H 5930 3.46 9.01 7.00 0.42
HIS HE1 H 4673 3.21 10.88 7.95 0.49
HIS HE2 H 149 6.57 16.53 9.65 2.51
HIS C C 7309 166.90 183.12 175.28 1.97
HIS CA C 10297 46.01 66.98 56.55 2.33
HIS CB C 9689 18.75 43.38 30.22 2.07
HIS CG C 88 117.54 139.56 131.87 3.43
HIS CD2 C 3801 111.30 159.95 120.46 3.42
HIS CE1 C 2897 104.67 145.42 137.67 2.23
HIS N N 10646 104.96 136.48 119.66 4.01
HIS ND1 N 189 164.31 229.14 193.59 18.33
HIS NE2 N 195 161.70 226.29 184.09 15.75
ILE H H 28109 3.43 11.69 8.27 0.68
ILE HA H 21155 1.32 6.36 4.17 0.56
ILE HB H 19864 -1.28 3.87 1.78 0.29
ILE HG12 H 18020 -2.38 2.69 1.28 0.40
ILE HG13 H 17310 -2.07 2.99 1.19 0.41
ILE HG2 H 18893 -1.33 2.20 0.77 0.27
ILE HD1 H 19084 -1.31 2.82 0.68 0.29
ILE C C 18279 167.00 183.40 175.90 1.92
ILE CA C 24743 51.07 71.86 61.68 2.69
ILE CB C 23142 22.11 51.88 38.59 1.99
ILE CG1 C 15338 13.16 39.05 27.74 1.68
ILE CG2 C 16322 3.45 29.80 17.54 1.34
ILE CD1 C 16487 4.94 29.60 13.43 1.66
ILE N N 26363 99.00 138.12 121.39 4.28
LEU H H 46785 4.08 13.22 8.22 0.64
LEU HA H 35082 1.93 6.42 4.31 0.47
LEU HB2 H 32229 -1.25 3.18 1.61 0.34
LEU HB3 H 30723 -1.47 3.18 1.52 0.36
LEU HG H 28589 -1.06 3.90 1.51 0.33
LEU HD1 H 31777 -1.73 2.36 0.76 0.28
LEU HD2 H 30557 -1.65 2.67 0.73 0.28
LEU C C 30103 167.49 189.78 177.05 1.96
LEU CA C 40980 46.36 67.40 55.70 2.12
LEU CB C 38487 26.40 53.70 42.27 1.85
LEU CG C 24292 15.30 37.70 26.79 1.09
LEU CD1 C 26671 10.95 36.85 24.70 1.58
LEU CD2 C 25374 11.71 30.40 24.07 1.68
LEU N N 43750 98.56 177.62 121.79 3.88
LYS H H 39173 4.11 12.03 8.17 0.60
LYS HA H 29953 1.30 6.17 4.26 0.43
LYS HB2 H 27057 -0.75 4.05 1.78 0.25
LYS HB3 H 25311 -0.72 3.95 1.75 0.27
LYS HG2 H 24456 -0.98 3.13 1.37 0.26
LYS HG3 H 22346 -1.16 3.03 1.35 0.27
LYS HD2 H 21764 -0.92 7.71 1.61 0.22
LYS HD3 H 19360 -1.02 3.19 1.60 0.22
LYS HE2 H 21579 1.23 4.43 2.92 0.19
LYS HE3 H 18722 1.17 4.55 2.91 0.20
LYS HZ H 819 1.95 9.90 7.40 0.68
LYS C C 24441 166.63 185.00 176.71 1.95
LYS CA C 33380 40.73 65.87 57.00 2.19
LYS CB C 31359 21.19 46.60 32.78 1.76
LYS CG C 20402 16.85 36.22 24.91 1.13
LYS CD C 19339 20.10 40.10 28.96 1.09
LYS CE C 18669 30.48 52.20 41.90 0.83
LYS N N 35975 101.10 140.30 121.00 3.74
LYS NZ N 31 29.48 43.69 33.36 2.29
MET H H 11106 4.87 12.46 8.25 0.60
MET HA H 8737 1.13 6.35 4.40 0.47
MET HB2 H 7866 -1.05 3.87 2.03 0.33
MET HB3 H 7349 -0.99 3.47 1.99 0.35
MET HG2 H 7218 -0.42 4.40 2.42 0.35
MET HG3 H 6788 -0.30 4.24 2.39 0.38
MET HE H 5137 -0.21 8.38 1.88 0.40
MET C C 7283 167.40 183.16 176.24 2.09
MET CA C 10220 43.28 66.86 56.16 2.24
MET CB C 9454 20.98 46.46 32.96 2.20
MET CG C 5958 19.06 38.58 32.02 1.25
MET CE C 4513 10.69 32.10 17.07 1.41
MET N N 10479 102.88 138.55 120.05 3.52
PHE H H 19906 3.55 12.18 8.35 0.72
PHE HA H 14869 1.78 6.87 4.62 0.57
PHE HB2 H 13850 0.16 4.46 3.00 0.37
PHE HB3 H 13487 -0.21 4.69 2.94 0.39
PHE HD1 H 11658 4.97 8.15 7.06 0.31
PHE HD2 H 9876 4.97 8.15 7.06 0.31
PHE HE1 H 10177 4.38 8.80 7.08 0.31
PHE HE2 H 8758 4.38 8.80 7.08 0.32
PHE HZ H 7362 4.32 9.50 7.00 0.42
PHE C C 12672 166.85 184.93 175.48 2.00
PHE CA C 17147 47.31 69.82 58.16 2.58
PHE CB C 16141 25.52 50.23 39.95 2.06
PHE CG C 154 127.24 144.00 138.26 2.66
PHE CD1 C 6745 116.95 136.73 131.59 1.18
PHE CD2 C 4937 118.13 138.25 131.61 1.15
PHE CE1 C 5916 114.75 139.56 130.73 1.29
PHE CE2 C 4324 114.70 139.70 130.77 1.14
PHE CZ C 4597 116.46 138.60 129.22 1.45
PHE N N 18493 102.20 139.02 120.38 4.17
PRO HA H 16935 1.04 8.08 4.39 0.33
PRO HB2 H 15858 -0.31 4.35 2.08 0.35
PRO HB3 H 15307 -0.58 3.79 2.00 0.36
PRO HG2 H 14406 -0.77 4.42 1.93 0.31
PRO HG3 H 13297 -0.90 4.42 1.90 0.32
PRO HD2 H 14764 0.63 5.36 3.65 0.35
PRO HD3 H 14181 -0.26 5.36 3.61 0.39
PRO C C 13293 168.38 182.84 176.77 1.51
PRO CA C 18984 50.12 70.67 63.36 1.51
PRO CB C 17851 23.33 45.16 31.85 1.17
PRO CG C 12490 18.28 33.90 27.19 1.07
PRO CD C 12531 40.05 58.69 50.34 0.98
PRO N N 506 110.91 145.26 134.32 6.54
SER H H 34076 3.76 12.33 8.28 0.58
SER HA H 26429 1.54 6.85 4.47 0.40
SER HB2 H 24315 1.74 5.41 3.88 0.25
SER HB3 H 22319 1.55 5.27 3.85 0.27
SER HG H 381 0.13 8.97 5.46 1.04
SER C C 21947 164.47 184.88 174.65 1.74
SER CA C 30331 45.13 68.40 58.76 2.08
SER CB C 28202 31.40 76.39 63.79 1.51
SER N N 31499 95.97 133.68 116.27 3.52
THR H H 29703 5.32 11.73 8.24 0.62
THR HA H 22438 1.65 6.63 4.45 0.48
THR HB H 20586 0.92 8.35 4.17 0.33
THR HG1 H 671 0.32 8.21 5.21 1.13
THR HG2 H 20418 -1.19 3.40 1.14 0.22
THR C C 18545 165.50 184.43 174.57 1.75
THR CA C 25624 51.61 72.80 62.28 2.61
THR CB C 23862 29.97 81.53 69.71 1.74
THR CG2 C 16465 11.70 36.73 21.56 1.09
THR N N 27567 95.77 138.27 115.36 4.74
TRP H H 6421 5.16 11.76 8.28 0.77
TRP HA H 4769 2.24 6.55 4.66 0.52
TRP HB2 H 4464 0.42 4.54 3.19 0.35
TRP HB3 H 4323 0.31 4.44 3.12 0.36
TRP HD1 H 3973 4.90 8.93 7.14 0.35
TRP HE1 H 4353 5.12 13.49 10.08 0.64
TRP HE3 H 3482 4.89 9.95 7.32 0.41
TRP HZ2 H 3742 4.90 8.56 7.28 0.32
TRP HZ3 H 3373 3.88 8.90 6.86 0.39
TRP HH2 H 3433 4.37 10.17 6.97 0.38
TRP C C 3810 168.17 182.60 176.20 2.01
TRP CA C 5212 44.69 69.76 57.72 2.58
TRP CB C 4908 21.10 43.02 29.98 1.99
TRP CG C 120 107.50 116.53 110.92 1.84
TRP CD1 C 2411 108.45 133.49 126.55 1.82
TRP CD2 C 90 120.20 132.62 127.72 1.61
TRP CE2 C 85 113.89 177.71 138.68 7.06
TRP CE3 C 2040 93.34 137.60 120.45 1.75
TRP CZ2 C 2309 103.18 132.03 114.26 1.17
TRP CZ3 C 2071 98.61 138.39 121.37 1.56
TRP CH2 C 2151 112.43 131.54 123.86 1.39
TRP N N 5722 101.97 138.11 121.58 4.12
TRP NE1 N 3432 107.64 139.20 129.29 2.03
TYR H H 16786 4.16 12.01 8.30 0.73
TYR HA H 12774 1.19 6.73 4.61 0.56
TYR HB2 H 11901 -0.49 4.70 2.90 0.37
TYR HB3 H 11607 -0.19 4.70 2.84 0.39
TYR HD1 H 10403 4.68 8.53 6.93 0.30
TYR HD2 H 8964 4.43 8.50 6.93 0.30
TYR HE1 H 9871 4.58 7.83 6.70 0.23
TYR HE2 H 8592 4.56 8.50 6.70 0.23
TYR HH H 182 5.99 13.75 9.30 1.27
TYR C C 10070 167.86 184.78 175.45 2.00
TYR CA C 14083 44.64 69.56 58.20 2.54
TYR CB C 13169 28.82 47.30 39.27 2.14
TYR CG C 136 117.70 174.59 129.68 4.52
TYR CD1 C 6052 115.30 141.57 132.75 1.31
TYR CD2 C 4284 113.00 138.29 132.71 1.46
TYR CE1 C 6015 110.70 134.01 117.93 1.21
TYR CE2 C 4224 106.55 135.82 117.90 1.27
TYR CZ C 110 105.25 160.45 156.26 5.13
TYR N N 15171 39.20 144.96 120.45 4.27
VAL H H 36547 3.98 12.59 8.28 0.67
VAL HA H 27680 0.97 6.30 4.17 0.58
VAL HB H 26054 -1.22 3.32 1.98 0.32
VAL HG1 H 25554 -1.13 2.57 0.83 0.26
VAL HG2 H 24951 -2.32 2.78 0.80 0.28
VAL C C 23630 165.65 183.95 175.68 1.90
VAL CA C 32096 50.16 70.34 62.57 2.89
VAL CB C 30101 20.55 45.33 32.71 1.78
VAL CG1 C 21452 13.53 32.27 21.51 1.36
VAL CG2 C 20636 13.26 30.46 21.29 1.54
VAL N N 34435 97.22 143.29 121.08 4.53
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