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Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules

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Statistics menu

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 8302997 possible chemical shifts in the BMRB database, 6268939 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: 10-04-2018
Amino   Atom    Atom     Number     Minimum     Maximum    Average    Standard    
Acid    Name    Type    of Shifts    Shift       Shift      Shift     Deviation   

ALA     H        H        59047        3.53        12.11       8.19       0.58       
ALA     HA       H        40823        0.87         6.51       4.24       0.43       
ALA     HB       H        38566       -0.83         3.12       1.36       0.24       
ALA     C        C        38858      164.48       187.20     177.81       2.06       
ALA     CA       C        52858       39.92        67.02      53.18       1.93       
ALA     CB       C        49574        6.61        43.14      18.97       1.78       
ALA     N        N        56274       98.05       142.81     123.31       3.46       

ARG     H        H        39279        3.57        12.69       8.23       0.61       
ARG     HA       H        27691        1.29         6.62       4.29       0.45       
ARG     HB2      H        24958       -0.61         3.74       1.80       0.26       
ARG     HB3      H        23631       -0.74         3.74       1.77       0.27       
ARG     HG2      H        22273       -0.64         3.51       1.57       0.26       
ARG     HG3      H        20679       -0.74         3.51       1.55       0.28       
ARG     HD2      H        21855        1.04         4.85       3.12       0.23       
ARG     HD3      H        19932        0.85         4.69       3.10       0.25       
ARG     HE       H        6612         2.20        11.88       7.36       0.58       
ARG     HH11     H        588          5.88        10.07       6.90       0.46       
ARG     HH12     H        455          5.92        10.73       6.86       0.48       
ARG     HH21     H        508          4.85        11.35       6.81       0.48       
ARG     HH22     H        410          5.92        10.19       6.82       0.49       
ARG     C        C        24350      167.44       184.51     176.48       2.00       
ARG     CA       C        34045       35.70        67.98      56.81       2.30       
ARG     CB       C        31591       20.78        42.50      30.64       1.80       
ARG     CG       C        18651       18.22        49.39      27.22       1.21       
ARG     CD       C        18828       27.12        50.88      43.15       0.92       
ARG     CZ       C        494        113.28       179.92     160.01       3.76       
ARG     N        N        36346      102.43       137.60     120.82       3.63       
ARG     NE       N        3961        67.00        99.81      84.60       1.63       
ARG     NH1      N        120         67.60        87.82      74.30       5.15       
ARG     NH2      N        107         69.26        87.83      72.73       2.99       

ASP     H        H        46493        4.06        12.68       8.30       0.56       
ASP     HA       H        32126        2.33         6.67       4.58       0.31       
ASP     HB2      H        29764       -0.39         4.60       2.71       0.26       
ASP     HB3      H        28553       -0.23         4.58       2.66       0.27       
ASP     HD2      H        2            4.65         9.29       6.97       3.28       
ASP     C        C        29820      166.80       182.70     176.44       1.70       
ASP     CA       C        41256       41.11        67.17      54.69       2.02       
ASP     CB       C        38863       26.50        58.51      40.88       1.61       
ASP     CG       C        500        170.72       186.50     179.33       1.81       
ASP     N        N        44465      101.90       143.52     120.70       3.79       

ASN     H        H        32684        3.46        12.68       8.32       0.61       
ASN     HA       H        23124        2.04         6.60       4.66       0.35       
ASN     HB2      H        21527        0.22         4.47       2.80       0.31       
ASN     HB3      H        20718       -0.07         4.77       2.75       0.33       
ASN     HD21     H        15901        2.06        10.92       7.32       0.48       
ASN     HD22     H        15677        2.58        10.92       7.15       0.50       
ASN     C        C        20744      167.75       185.30     175.30       1.76       
ASN     CA       C        28973       41.20        66.21      53.55       1.86       
ASN     CB       C        27338       23.16        57.35      38.69       1.66       
ASN     CG       C        1767       166.40       183.80     176.79       1.38       
ASN     N        N        30520      101.71       137.49     118.92       3.92       
ASN     ND2      N        13621       99.40       134.50     112.76       2.27       

CYS     H        H        16422        4.38        12.66       8.38       0.68       
CYS     HA       H        13422        1.64         6.45       4.65       0.54       
CYS     HB2      H        12902       -0.54         4.72       2.95       0.44       
CYS     HB3      H        12579       -0.83         4.77       2.89       0.45       
CYS     HG       H        165         -1.83         7.39       1.96       1.20       
CYS     C        C        8080       166.73       187.59     174.89       2.04       
CYS     CA       C        11724       41.51        68.07      58.14       3.43       
CYS     CB       C        11107       17.99        63.89      33.13       6.39       
CYS     N        N        12782      100.48       138.68     120.12       4.47       

GLU     H        H        60770        4.29        12.69       8.33       0.58       
GLU     HA       H        42249        1.39         6.32       4.24       0.40       
GLU     HB2      H        37935        0.34         3.37       2.02       0.21       
GLU     HB3      H        35649        0.27         3.47       2.00       0.21       
GLU     HG2      H        34966        0.53         3.77       2.27       0.21       
GLU     HG3      H        32599        0.56         3.83       2.25       0.21       
GLU     HE2      H        3            2.73         2.93       2.82       0.10       
GLU     C        C        39796      166.80       183.52     176.94       1.90       
GLU     CA       C        54127       41.96        70.38      57.34       2.07       
GLU     CB       C        50291       18.36        49.56      29.97       1.70       
GLU     CG       C        31139       25.06        54.83      36.11       1.20       
GLU     CD       C        572        173.41       189.46     182.28       2.43       
GLU     N        N        58445      101.34       138.60     120.74       3.44       

GLN     H        H        33728        3.51        12.22       8.22       0.57       
GLN     HA       H        23520        1.57         6.44       4.26       0.43       
GLN     HB2      H        21222       -0.12         4.00       2.05       0.25       
GLN     HB3      H        20202       -0.56         4.04       2.01       0.26       
GLN     HG2      H        19741       -0.21         4.44       2.31       0.26       
GLN     HG3      H        18270       -0.41         4.44       2.29       0.28       
GLN     HE21     H        14648        3.39        11.11       7.22       0.44       
GLN     HE22     H        14575        3.59        10.35       7.04       0.43       
GLN     C        C        21978      168.09       185.31     176.36       1.91       
GLN     CA       C        30351       43.45        66.60      56.59       2.10       
GLN     CB       C        28276       18.43        43.65      29.17       1.80       
GLN     CG       C        17463       21.64        51.08      33.78       1.11       
GLN     CD       C        1694       171.37       183.54     179.72       1.22       
GLN     N        N        32170      103.88       139.55     119.95       3.54       
GLN     NE2      N        13128       92.49       133.30     111.86       1.68       

GLY     H        H        58480        3.34        12.22       8.33       0.63       
GLY     HA2      H        39744        0.84         6.98       3.96       0.37       
GLY     HA3      H        37811        0.74         6.98       3.90       0.37       
GLY     C        C        37658      163.27       184.89     173.90       1.83       
GLY     CA       C        52373       33.15        60.91      45.37       1.30       
GLY     N        N        54841       93.60       162.19     109.59       3.68       

HIS     H        H        16507        3.97        12.39       8.24       0.67       
HIS     HA       H        11918        1.93         8.90       4.60       0.43       
HIS     HB2      H        11012       -0.04         8.70       3.11       0.35       
HIS     HB3      H        10680       -0.39         8.70       3.05       0.37       
HIS     HD1      H        490          2.73        17.20       8.55       2.45       
HIS     HD2      H        7690         3.65         9.42       7.00       0.41       
HIS     HE1      H        6007         3.21        10.88       7.96       0.48       
HIS     HE2      H        197          6.57        16.53       9.53       2.35       
HIS     C        C        10516      166.90       183.12     175.26       1.95       
HIS     CA       C        15076       43.31        77.56      56.51       2.31       
HIS     CB       C        14078       18.75        54.90      30.25       2.11       
HIS     CG       C        123        117.54       139.56     131.92       3.22       
HIS     CD2      C        5086       110.52       159.95     120.38       3.36       
HIS     CE1      C        3924       104.67       145.42     137.64       2.24       
HIS     N        N        15461      103.99       136.48     119.70       4.02       
HIS     ND1      N        286        162.88       229.14     193.49      18.79       
HIS     NE2      N        293        161.10       226.76     185.42      17.16       

ILE     H        H        40964        3.42        11.87       8.26       0.68       
ILE     HA       H        28587        1.32         6.36       4.16       0.55       
ILE     HB       H        26774       -1.28         3.87       1.78       0.29       
ILE     HG12     H        24201       -2.12         2.85       1.28       0.40       
ILE     HG13     H        23240       -2.07         2.99       1.20       0.41       
ILE     HG2      H        25447       -1.47         2.20       0.78       0.27       
ILE     HD1      H        26251       -1.47         2.82       0.68       0.28       
ILE     C        C        26612      166.40       187.55     175.93       1.90       
ILE     CA       C        36606       43.84        71.86      61.68       2.68       
ILE     CB       C        34034       18.10        51.88      38.56       2.00       
ILE     CG1      C        21345        8.77        42.09      27.75       1.70       
ILE     CG2      C        22570        3.45        37.01      17.53       1.34       
ILE     CD1      C        23296        4.94        29.60      13.41       1.66       
ILE     N        N        38996       99.00       138.12     121.42       4.22       

LEU     H        H        68213        4.08        13.22       8.22       0.63       
LEU     HA       H        47301        1.72         6.42       4.30       0.46       
LEU     HB2      H        43226       -1.21         4.13       1.61       0.34       
LEU     HB3      H        41408       -1.41         3.23       1.52       0.36       
LEU     HG       H        38049       -1.06         3.90       1.51       0.33       
LEU     HD1      H        43092       -1.73         2.36       0.75       0.27       
LEU     HD2      H        41361       -1.92         2.15       0.73       0.28       
LEU     C        C        44202      166.22       189.78     177.08       1.93       
LEU     CA       C        60732       42.69        67.88      55.69       2.11       
LEU     CB       C        56556       26.88        53.70      42.25       1.85       
LEU     CG       C        33187       15.30        38.62      26.78       1.09       
LEU     CD1      C        37015       10.95        36.85      24.66       1.59       
LEU     CD2      C        35234        9.86        32.52      24.07       1.69       
LEU     N        N        64708       98.56       177.62     121.84       3.85       

LYS     H        H        57087        4.11        12.03       8.18       0.60       
LYS     HA       H        40712        0.68         6.25       4.26       0.43       
LYS     HB2      H        36200       -0.25         3.82       1.78       0.24       
LYS     HB3      H        34225       -0.45         3.82       1.75       0.26       
LYS     HG2      H        32709       -0.69         3.13       1.37       0.25       
LYS     HG3      H        30254       -0.87         3.05       1.35       0.27       
LYS     HD2      H        29024       -1.68         3.19       1.61       0.21       
LYS     HD3      H        26237       -0.53         3.19       1.60       0.21       
LYS     HE2      H        28733        0.67         4.43       2.91       0.20       
LYS     HE3      H        25382        1.17         4.55       2.91       0.20       
LYS     HZ       H        1016         1.95         9.90       7.38       0.66       
LYS     C        C        35906      166.63       185.00     176.72       1.91       
LYS     CA       C        49658       40.73        65.87      56.97       2.17       
LYS     CB       C        46113       21.19        46.60      32.76       1.77       
LYS     CG       C        28078       16.85        40.50      24.90       1.13       
LYS     CD       C        26493       15.37        42.70      28.96       1.11       
LYS     CE       C        25542       25.24        56.00      41.88       0.88       
LYS     N        N        53320      101.10       140.30     121.04       3.69       
LYS     NZ       N        70          29.48        35.90      33.08       1.14       

MET     H        H        16288        4.87        12.46       8.25       0.58       
MET     HA       H        11782        1.13         6.35       4.39       0.46       
MET     HB2      H        10484       -1.05         4.07       2.02       0.33       
MET     HB3      H        9845        -0.99         3.47       1.99       0.34       
MET     HG2      H        9586        -0.42         4.40       2.42       0.35       
MET     HG3      H        9070        -0.47         4.24       2.39       0.38       
MET     HE       H        7075        -0.71         8.38       1.89       0.40       
MET     C        C        10844      167.40       183.16     176.27       2.05       
MET     CA       C        15225       43.28        66.86      56.17       2.20       
MET     CB       C        14008       20.36        46.46      32.93       2.17       
MET     CG       C        8090        15.94        51.70      32.03       1.28       
MET     CE       C        6375         9.70        44.10      17.09       1.67       
MET     N        N        15630      102.80       138.55     120.10       3.48       

PHE     H        H        29092        3.55        12.18       8.34       0.71       
PHE     HA       H        19911        1.33         6.87       4.61       0.56       
PHE     HB2      H        18409        0.16         4.46       3.00       0.37       
PHE     HB3      H        17990       -0.19         4.69       2.94       0.39       
PHE     HD1      H        15223        4.47         8.15       7.06       0.31       
PHE     HD2      H        13058        4.47         8.15       7.06       0.31       
PHE     HE1      H        13187        4.38         8.80       7.08       0.31       
PHE     HE2      H        11475        4.38         8.80       7.08       0.31       
PHE     HZ       H        9305         4.32         9.50       6.99       0.41       
PHE     C        C        18512      166.85       184.93     175.50       1.97       
PHE     CA       C        25582       36.03        69.82      58.14       2.57       
PHE     CB       C        23863       25.52        56.74      39.93       2.06       
PHE     CG       C        235        127.24       152.84     138.46       2.80       
PHE     CD1      C        9081       116.95       143.16     131.58       1.22       
PHE     CD2      C        6660       115.55       138.70     131.57       1.23       
PHE     CE1      C        7882       114.75       139.56     130.73       1.32       
PHE     CE2      C        5776       114.70       139.70     130.75       1.21       
PHE     CZ       C        6009       115.10       139.13     129.21       1.48       
PHE     N        N        27483      101.47       139.02     120.37       4.12       

PRO     HA       H        22923        1.04         8.08       4.39       0.33       
PRO     HB2      H        21167       -0.75         4.59       2.08       0.34       
PRO     HB3      H        20556       -0.58         3.79       2.00       0.35       
PRO     HG2      H        18965       -0.77         4.42       1.93       0.31       
PRO     HG3      H        17613       -0.73         4.42       1.90       0.32       
PRO     HD2      H        19398        0.63         5.36       3.65       0.35       
PRO     HD3      H        18720        0.34         5.36       3.62       0.38       
PRO     C        C        19886      168.38       182.84     176.77       1.47       
PRO     CA       C        28290       48.56        72.28      63.35       1.51       
PRO     CB       C        26324       20.91        56.76      31.85       1.18       
PRO     CG       C        17054       18.28        50.75      27.20       1.10       
PRO     CD       C        17029       26.92        58.81      50.34       1.05       
PRO     N        N        1164       110.49       145.74     135.36       5.44       

SER     H        H        50108        3.76        12.52       8.28       0.58       
SER     HA       H        35502        1.28         6.85       4.47       0.40       
SER     HB2      H        32314        1.70         5.45       3.87       0.25       
SER     HB3      H        29903        1.12         5.45       3.84       0.27       
SER     HG       H        560          0.13         8.97       5.36       1.06       
SER     C        C        32557      164.47       197.10     174.65       1.72       
SER     CA       C        45525       45.13        73.19      58.73       2.07       
SER     CB       C        41990       31.40        76.39      63.80       1.51       
SER     N        N        47254       95.97       133.68     116.29       3.48       

THR     H        H        44103        5.32        11.80       8.24       0.62       
THR     HA       H        30775        1.65         7.47       4.45       0.47       
THR     HB       H        27890        0.92         8.35       4.16       0.32       
THR     HG1      H        951         -1.78         9.01       5.08       1.29       
THR     HG2      H        27592       -0.97         3.28       1.14       0.22       
THR     C        C        28091      165.50       184.43     174.58       1.72       
THR     CA       C        39011       43.39        72.80      62.25       2.58       
THR     CB       C        35990       29.97        81.53      69.71       1.73       
THR     CG2      C        23073       11.70        36.73      21.55       1.10       
THR     N        N        41794       95.77       138.27     115.35       4.71       

TRP     H        H        9230         5.16        11.76       8.27       0.77       
TRP     HA       H        6311         2.04         6.58       4.66       0.52       
TRP     HB2      H        5914         0.68         4.54       3.19       0.34       
TRP     HB3      H        5739         0.26         4.44       3.12       0.36       
TRP     HD1      H        5235         4.60         8.93       7.14       0.34       
TRP     HE1      H        5823         4.69        13.49      10.07       0.64       
TRP     HE3      H        4523         4.89         9.95       7.32       0.41       
TRP     HZ2      H        4876         4.66         8.56       7.28       0.32       
TRP     HZ3      H        4371         3.88         8.90       6.87       0.37       
TRP     HH2      H        4489         4.37        10.17       6.98       0.36       
TRP     C        C        5572       168.17       182.60     176.20       1.98       
TRP     CA       C        7773        43.50        81.00      57.72       2.53       
TRP     CB       C        7236        18.63        52.30      29.97       1.99       
TRP     CG       C        143        107.50       116.53     111.06       1.79       
TRP     CD1      C        3260       108.45       135.60     126.55       1.85       
TRP     CD2      C        114        120.00       132.62     127.77       1.88       
TRP     CE2      C        117        113.89       177.71     138.11       6.95       
TRP     CE3      C        2715        93.34       137.60     120.47       1.83       
TRP     CZ2      C        3106        81.81       134.70     114.26       1.44       
TRP     CZ3      C        2752        98.61       138.39     121.37       1.59       
TRP     CH2      C        2900        91.62       131.54     123.81       1.57       
TRP     N        N        8368       101.97       138.11     121.57       4.07       
TRP     NE1      N        4686       106.00       139.73     129.28       2.06       

TYR     H        H        24516        4.16        12.34       8.30       0.72       
TYR     HA       H        17038        1.19         6.83       4.60       0.56       
TYR     HB2      H        15721       -0.49         4.70       2.90       0.37       
TYR     HB3      H        15362       -0.19         4.70       2.84       0.39       
TYR     HD1      H        13533        4.68         8.54       6.93       0.29       
TYR     HD2      H        11795        4.43         8.54       6.93       0.29       
TYR     HE1      H        12844        4.58         7.85       6.70       0.22       
TYR     HE2      H        11275        4.56         8.50       6.70       0.23       
TYR     HH       H        236         -0.79        13.75       9.13       1.60       
TYR     C        C        15101      167.86       184.78     175.51       1.95       
TYR     CA       C        21085       44.64        69.56      58.19       2.49       
TYR     CB       C        19493       25.32        57.73      39.27       2.14       
TYR     CG       C        214        117.70       144.30     129.56       2.51       
TYR     CD1      C        8111       115.30       141.57     132.72       1.35       
TYR     CD2      C        5779       113.00       139.47     132.69       1.52       
TYR     CE1      C        8049       110.70       137.42     117.94       1.28       
TYR     CE2      C        5692       106.55       135.82     117.91       1.29       
TYR     CZ       C        155        153.54       160.45     156.82       1.47       
TYR     N        N        22644      100.09       144.96     120.49       4.09       

VAL     H        H        53730        3.98        12.59       8.27       0.66       
VAL     HA       H        37522        0.97         6.30       4.16       0.57       
VAL     HB       H        34712       -1.24         3.76       1.98       0.31       
VAL     HG1      H        34401       -1.13         2.57       0.83       0.26       
VAL     HG2      H        33671       -2.32         3.32       0.80       0.28       
VAL     C        C        35130      165.65       183.95     175.72       1.85       
VAL     CA       C        47938       44.98        70.34      62.56       2.84       
VAL     CB       C        44161       18.97        45.33      32.70       1.77       
VAL     CG1      C        29797       12.07        32.27      21.52       1.36       
VAL     CG2      C        28711       11.38        33.12      21.29       1.53       
VAL     N        N        51456       97.22       143.29     121.09       4.44