Chemical shift table

Amino
Acid		 Atom
Name		 Atom type Number
of Shifts		 Minimum Maximum Average Standard
Deviation
ALA H H 12913 3.53 11.58 8.18 0.60
ALA HA H 10794 1.50 6.51 4.26 0.44
ALA HB H 9980 -0.83 2.70 1.37 0.25
ALA C C 6685 164.48 185.42 177.78 2.23
ALA CA C 9643 43.00 65.52 53.19 2.02
ALA CB C 8811 0.00 32.99 18.94 1.85
ALA N N 10773 99.44 142.81 123.15 3.65
ARG H H 8876 4.92 12.02 8.23 0.61
ARG HA H 7410 1.34 6.44 4.29 0.45
ARG HB2 H 6490 -0.42 3.29 1.80 0.27
ARG HB3 H 5906 -0.20 3.29 1.78 0.28
ARG HG2 H 5710 -0.64 3.35 1.58 0.27
ARG HG3 H 5055 -0.40 3.35 1.56 0.28
ARG HD2 H 5500 0.83 4.69 3.12 0.24
ARG HD3 H 4784 1.22 4.28 3.12 0.24
ARG HE H 2420 3.08 11.88 7.35 0.57
ARG HH11 H 293 5.82 9.45 6.83 0.39
ARG HH12 H 210 5.82 8.76 6.77 0.34
ARG HH21 H 271 4.59 9.70 6.79 0.40
ARG HH22 H 219 4.59 9.21 6.75 0.38
ARG C C 4406 167.44 184.51 176.49 2.09
ARG CA C 6464 45.00 67.98 56.86 2.39
ARG CB C 5654 22.00 42.14 30.61 1.83
ARG CG C 3323 18.22 37.83 27.26 1.31
ARG CD C 3398 28.62 49.06 43.15 1.00
ARG CZ C 96 156.49 160.60 159.18 0.95
ARG N N 7064 103.60 137.60 120.75 3.83
ARG NE N 1040 7.28 145.60 92.84 14.92
ARG NH1 N 44 70.10 112.50 73.35 6.17
ARG NH2 N 39 70.10 111.90 73.84 6.64
ASP H H 10170 4.34 12.61 8.32 0.57
ASP HA H 8473 2.59 6.34 4.60 0.32
ASP HB2 H 7639 -0.39 6.60 2.73 0.27
ASP HB3 H 7253 0.60 4.58 2.69 0.29
ASP C C 5510 166.80 182.70 176.45 1.81
ASP CA C 7822 39.80 62.49 54.64 2.09
ASP CB C 7078 29.51 48.80 40.81 1.66
ASP CG C 155 170.72 182.66 179.10 1.66
ASP N N 8736 105.33 143.52 120.76 4.00
ASN H H 7589 3.61 12.40 8.35 0.63
ASN HA H 6323 2.61 6.39 4.68 0.37
ASN HB2 H 5769 0.10 4.47 2.81 0.33
ASN HB3 H 5527 -0.19 4.77 2.77 0.35
ASN HD21 H 4109 3.33 9.62 7.32 0.50
ASN HD22 H 4077 3.05 10.33 7.16 0.51
ASN C C 3769 168.23 181.00 175.36 1.82
ASN CA C 5484 41.31 62.13 53.50 1.96
ASN CB C 4966 28.64 55.09 38.64 1.75
ASN CG C 455 170.70 181.20 176.79 1.33
ASN N N 6116 103.70 137.49 119.02 4.18
ASN ND2 N 2871 102.33 133.59 112.85 2.44
CYS H H 4935 4.73 12.12 8.40 0.67
CYS HA H 4539 1.64 6.43 4.69 0.56
CYS HB2 H 4312 -0.25 4.65 2.96 0.45
CYS HB3 H 4200 -0.83 4.65 2.92 0.49
CYS HG H 20 0.25 7.39 2.36 2.08
CYS C C 1497 168.50 182.73 174.83 2.05
CYS CA C 2160 42.45 68.54 57.71 3.43
CYS CB C 1888 20.10 62.07 34.01 6.63
CYS N N 2629 100.48 135.89 119.99 4.63
GLU H H 13211 4.31 12.17 8.33 0.61
GLU HA H 11007 1.77 6.29 4.25 0.41
GLU HB2 H 9706 0.25 3.33 2.04 0.22
GLU HB3 H 8854 0.34 3.33 2.02 0.22
GLU HG2 H 8732 0.57 3.77 2.30 0.22
GLU HG3 H 7784 0.45 3.68 2.28 0.22
GLU C C 7360 166.80 182.99 177.01 2.03
GLU CA C 10368 46.80 66.60 57.45 2.13
GLU CB C 9274 21.70 40.60 29.98 1.76
GLU CG C 6018 25.10 51.92 36.04 1.34
GLU CD C 153 173.41 185.20 181.20 3.47
GLU N N 11475 104.54 138.60 120.69 3.66
GLN H H 7186 5.41 11.94 8.21 0.59
GLN HA H 6036 2.33 6.23 4.27 0.43
GLN HB2 H 5309 -0.14 4.00 2.05 0.26
GLN HB3 H 4861 -0.52 4.04 2.03 0.28
GLN HG2 H 4899 0.06 3.66 2.32 0.29
GLN HG3 H 4290 0.05 3.66 2.31 0.29
GLN HE21 H 3484 3.39 11.11 7.20 0.48
GLN HE22 H 3465 3.59 9.79 7.04 0.47
GLN C C 3734 169.03 182.22 176.36 1.98
GLN CA C 5467 46.82 65.58 56.58 2.17
GLN CB C 4908 21.00 41.94 29.18 1.91
GLN CG C 3204 21.64 41.70 33.74 1.18
GLN CD C 399 171.70 183.50 179.71 1.24
GLN N N 6073 105.26 139.55 119.86 3.77
GLN NE2 N 2659 92.49 133.30 111.89 1.98
GLY H H 12739 3.01 12.22 8.34 0.69
GLY HA2 H 10511 0.94 7.31 3.96 0.38
GLY HA3 H 9893 1.27 6.01 3.91 0.38
GLY C C 6291 165.80 183.00 174.04 1.90
GLY CA C 9243 35.50 55.41 45.35 1.33
GLY N N 10231 88.30 135.66 109.71 4.12
HIS H H 3628 4.60 11.03 8.23 0.69
HIS HA H 3049 1.95 8.90 4.62 0.47
HIS HB2 H 2732 0.37 8.70 3.10 0.39
HIS HB3 H 2613 0.52 8.70 3.07 0.40
HIS HD1 H 188 3.79 17.20 8.97 2.86
HIS HD2 H 2057 3.46 9.01 7.06 0.49
HIS HE1 H 1799 3.21 10.26 8.03 0.55
HIS HE2 H 96 6.62 16.53 9.99 2.77
HIS C C 1895 166.90 180.80 175.35 2.08
HIS CA C 2790 45.80 66.98 56.52 2.46
HIS CB C 2532 23.40 43.30 30.23 2.16
HIS CG C 49 122.67 136.80 130.81 3.25
HIS CD2 C 744 94.17 138.85 119.71 2.80
HIS CE1 C 546 115.52 144.00 137.00 2.32
HIS N N 2985 105.00 136.48 119.47 4.23
HIS ND1 N 95 106.60 256.60 194.68 34.78
HIS NE2 N 107 114.71 231.50 175.85 18.81
ILE H H 9020 3.75 11.49 8.28 0.70
ILE HA H 7555 1.03 6.30 4.19 0.56
ILE HB H 6900 -1.28 3.01 1.80 0.30
ILE HG12 H 6035 -2.02 2.69 1.28 0.39
ILE HG13 H 5690 -2.04 2.99 1.23 0.41
ILE HG2 H 6450 -2.07 1.77 0.80 0.27
ILE HD1 H 6384 -1.22 2.96 0.69 0.30
ILE C C 4946 167.00 182.70 175.88 1.98
ILE CA C 6971 51.15 71.70 61.59 2.77
ILE CB C 6322 20.94 46.97 38.59 2.06
ILE CG1 C 4030 9.80 38.39 27.67 1.96
ILE CG2 C 4395 7.30 29.80 17.51 1.56
ILE CD1 C 4365 3.20 23.00 13.46 1.77
ILE N N 7670 99.00 138.12 121.53 4.42
LEU H H 14714 4.89 13.22 8.21 0.65
LEU HA H 12036 1.58 6.24 4.31 0.47
LEU HB2 H 10587 -1.44 3.18 1.63 0.35
LEU HB3 H 9921 -1.21 3.18 1.55 0.37
LEU HG H 9334 -1.06 3.90 1.52 0.34
LEU HD1 H 10282 -1.76 2.36 0.77 0.27
LEU HD2 H 9827 -1.16 2.78 0.74 0.29
LEU C C 7923 167.49 189.78 177.00 2.06
LEU CA C 11229 44.60 65.83 55.68 2.19
LEU CB C 10098 29.70 51.29 42.24 1.90
LEU CG C 6002 15.57 41.22 26.72 1.26
LEU CD1 C 6822 10.95 31.83 24.59 1.71
LEU CD2 C 6351 12.50 30.40 24.11 1.76
LEU N N 12487 100.60 144.55 121.79 3.99
LYS H H 13291 3.63 11.67 8.19 0.62
LYS HA H 11057 0.68 6.04 4.27 0.44
LYS HB2 H 9691 -0.18 4.05 1.78 0.25
LYS HB3 H 8818 -0.58 3.95 1.76 0.27
LYS HG2 H 8451 -0.82 3.01 1.38 0.26
LYS HG3 H 7459 -0.98 2.99 1.36 0.28
LYS HD2 H 7314 -0.61 7.71 1.61 0.24
LYS HD3 H 6163 -0.10 3.61 1.60 0.24
LYS HE2 H 7121 1.09 4.32 2.92 0.20
LYS HE3 H 5900 1.03 4.32 2.92 0.21
LYS HZ H 645 2.82 9.90 7.49 0.43
LYS C C 6682 121.16 185.00 176.68 2.15
LYS CA C 9662 46.10 63.14 56.96 2.25
LYS CB C 8670 21.00 46.60 32.73 1.84
LYS CG C 5307 17.30 40.50 24.90 1.24
LYS CD C 4974 21.20 42.60 28.87 1.24
LYS CE C 4748 25.98 56.00 41.81 0.97
LYS N N 10883 101.10 140.30 121.04 3.92
LYS NZ N 9 32.09 131.04 65.83 46.43
MET H H 3557 4.87 11.89 8.25 0.60
MET HA H 3038 1.86 6.35 4.39 0.48
MET HB2 H 2635 -0.99 4.07 2.04 0.33
MET HB3 H 2443 -0.99 3.15 2.01 0.35
MET HG2 H 2360 -0.36 4.40 2.44 0.35
MET HG3 H 2186 -0.47 4.24 2.41 0.39
MET HE H 1531 -0.21 3.30 1.88 0.39
MET C C 1903 168.20 181.47 176.31 2.08
MET CA C 2882 47.70 63.76 56.20 2.25
MET CB C 2562 24.86 46.46 33.02 2.24
MET CG C 1536 20.83 37.96 32.03 1.33
MET CE C 1071 0.00 42.57 17.27 2.65
MET N N 3068 106.30 134.80 120.05 3.64
PHE H H 6547 5.21 12.03 8.38 0.72
PHE HA H 5404 2.13 6.56 4.61 0.58
PHE HB2 H 4948 0.17 4.32 2.99 0.38
PHE HB3 H 4744 0.30 4.31 2.96 0.39
PHE HD1 H 4200 2.46 8.08 7.06 0.33
PHE HD2 H 3249 2.46 8.15 7.06 0.33
PHE HE1 H 3781 4.10 8.80 7.10 0.33
PHE HE2 H 2996 4.10 8.80 7.10 0.32
PHE HZ H 2815 4.53 9.50 7.03 0.43
PHE C C 3499 167.70 181.96 175.56 2.02
PHE CA C 4956 47.31 69.82 58.23 2.68
PHE CB C 4495 25.52 50.40 39.93 2.10
PHE CG C 34 127.84 140.40 136.82 3.31
PHE CD1 C 1521 118.50 135.90 131.44 1.36
PHE CD2 C 903 119.10 137.20 131.44 1.28
PHE CE1 C 1258 114.75 133.90 130.57 1.58
PHE CE2 C 742 121.30 133.90 130.67 1.09
PHE CZ C 935 117.51 138.60 129.22 1.80
PHE N N 5513 102.76 139.02 120.66 4.25
PRO H2 H 1 8.51 8.51 8.51 0.00
PRO HA H 5771 1.63 6.05 4.39 0.34
PRO HB2 H 5265 -0.78 4.02 2.06 0.36
PRO HB3 H 5009 -0.36 3.79 2.02 0.37
PRO HG2 H 4614 -0.93 4.92 1.93 0.34
PRO HG3 H 4166 -0.90 4.92 1.91 0.36
PRO HD2 H 4832 0.63 5.36 3.64 0.36
PRO HD3 H 4555 -0.26 5.36 3.62 0.39
PRO C C 3509 170.50 182.30 176.75 1.56
PRO CA C 5201 50.12 72.28 63.31 1.62
PRO CB C 4620 25.48 50.25 31.78 1.26
PRO CG C 2855 19.31 33.79 27.20 1.16
PRO CD C 2913 26.96 66.22 50.32 1.15
PRO N N 149 104.39 145.26 131.17 9.61
SER H H 10722 2.96 13.13 8.29 0.60
SER HA H 9073 1.43 6.46 4.49 0.42
SER HB2 H 7995 1.53 5.41 3.88 0.27
SER HB3 H 7223 1.49 5.01 3.86 0.29
SER HG H 147 0.00 8.97 5.33 1.08
SER C C 5402 165.00 182.20 174.66 1.78
SER CA C 7912 45.13 68.40 58.69 2.19
SER CB C 6960 55.50 73.90 63.81 1.56
SER N N 8638 102.60 133.10 116.25 3.76
THR H H 9874 5.54 11.39 8.25 0.63
THR HA H 8215 0.87 6.36 4.47 0.48
THR HB H 7324 0.92 8.35 4.17 0.34
THR HG1 H 293 0.32 8.21 4.74 1.76
THR HG2 H 7222 -0.83 4.07 1.15 0.24
THR C C 4898 165.50 182.02 174.60 1.79
THR CA C 7195 51.61 72.80 62.18 2.73
THR CB C 6411 30.16 81.53 69.63 1.86
THR CG2 C 4268 11.70 38.90 21.48 1.26
THR N N 8150 97.70 134.00 115.52 4.93
TRP H H 2111 4.49 11.09 8.29 0.80
TRP HA H 1748 2.28 6.75 4.70 0.54
TRP HB2 H 1601 0.42 4.54 3.21 0.36
TRP HB3 H 1533 0.77 4.49 3.15 0.36
TRP HD1 H 1479 4.90 8.93 7.15 0.35
TRP HE1 H 1491 5.16 12.14 10.10 0.56
TRP HE3 H 1339 4.89 8.98 7.35 0.41
TRP HZ2 H 1404 4.90 8.60 7.30 0.33
TRP HZ3 H 1302 3.88 8.20 6.87 0.44
TRP HH2 H 1315 4.92 10.90 7.00 0.42
TRP C C 1005 169.63 181.83 176.14 1.99
TRP CA C 1449 44.69 69.76 57.67 2.64
TRP CB C 1321 22.48 43.02 30.03 2.03
TRP CG C 86 102.53 114.60 110.21 1.84
TRP CD1 C 542 109.30 132.35 126.39 2.11
TRP CD2 C 73 120.20 130.70 127.46 1.36
TRP CE2 C 57 118.37 177.71 137.67 6.64
TRP CE3 C 453 113.97 137.60 120.60 2.25
TRP CZ2 C 510 81.81 123.76 114.13 2.02
TRP CZ3 C 455 114.90 138.39 121.37 1.84
TRP CH2 C 468 91.62 130.07 123.60 2.21
TRP N N 1609 101.75 134.89 121.65 4.50
TRP NE1 N 905 106.75 139.96 129.45 2.30
TYR H H 5799 4.39 11.92 8.33 0.74
TYR HA H 4865 1.20 6.73 4.62 0.57
TYR HB2 H 4470 0.31 4.70 2.91 0.37
TYR HB3 H 4286 0.34 4.70 2.88 0.38
TYR HD1 H 4145 4.98 8.53 6.95 0.30
TYR HD2 H 3293 4.43 10.50 6.95 0.31
TYR HE1 H 4023 4.58 7.86 6.71 0.23
TYR HE2 H 3213 4.56 8.50 6.71 0.24
TYR HH H 94 5.31 13.75 9.13 1.56
TYR C C 2663 168.37 182.40 175.45 2.03
TYR CA C 4004 45.20 65.80 58.10 2.61
TYR CB C 3567 28.95 57.73 39.27 2.18
TYR CG C 69 120.94 138.70 129.02 2.82
TYR CD1 C 1439 116.44 136.70 132.66 1.34
TYR CD2 C 794 113.00 136.70 132.47 1.74
TYR CE1 C 1412 110.70 133.31 117.84 1.43
TYR CE2 C 785 114.58 133.31 117.86 1.66
TYR CZ C 64 153.54 162.70 156.47 2.25
TYR N N 4484 103.60 144.96 120.72 4.46
VAL H H 11522 3.98 11.63 8.28 0.70
VAL HA H 9584 0.97 6.24 4.17 0.58
VAL HB H 8706 -0.56 3.42 1.99 0.32
VAL HG1 H 8494 -1.09 2.56 0.84 0.26
VAL HG2 H 8178 -2.32 3.32 0.82 0.29
VAL C C 6084 168.50 181.72 175.69 1.94
VAL CA C 8752 51.10 70.02 62.49 2.95
VAL CB C 7847 22.04 42.84 32.66 1.82
VAL CG1 C 5467 11.60 29.00 21.45 1.46
VAL CG2 C 5167 11.30 31.10 21.32 1.63
VAL N N 9833 96.29 143.29 121.06 4.78

Chemical shifts

1H
13C
15N

Contents