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

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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 3623767 possible chemical shifts in the BMRB database, 2568844 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: 11-17-2009
Amino   Atom    Atom     Number     Minimum     Maximum    Average    Standard    
Acid    Name    Type    of Shifts    Shift       Shift      Shift     Deviation   

ALA     H        H        23592        3.53        11.48       8.20       0.60       
ALA     HA       H        18028        1.24         6.51       4.26       0.44       
ALA     HB       H        17017       -0.83         3.12       1.36       0.25       
ALA     C        C        14038      164.48       187.20     177.77       2.15       
ALA     CA       C        19393       44.22        65.52      53.16       1.97       
ALA     CB       C        18102        9.79        28.40      18.98       1.81       
ALA     N        N        21300       77.10       142.81     123.23       3.57       

ARG     H        H        16069        3.64        12.69       8.24       0.61       
ARG     HA       H        12628        1.34         6.10       4.30       0.46       
ARG     HB2      H        11283       -0.77         3.29       1.80       0.27       
ARG     HB3      H        10513       -0.74         3.29       1.77       0.28       
ARG     HG2      H        10034       -0.64         3.51       1.57       0.26       
ARG     HG3      H        9040        -0.67         3.51       1.55       0.28       
ARG     HD2      H        9777         0.89         4.69       3.12       0.23       
ARG     HD3      H        8645         0.89         4.29       3.11       0.25       
ARG     HE       H        3346         2.99        11.88       7.38       0.62       
ARG     HH11     H        345          5.88         9.82       6.90       0.45       
ARG     HH12     H        254          6.01        10.73       6.83       0.41       
ARG     HH21     H        313          5.90        11.35       6.81       0.48       
ARG     HH22     H        244          5.97        10.18       6.76       0.40       
ARG     C        C        9120       167.44       184.51     176.44       2.04       
ARG     CA       C        12941       43.27        67.98      56.78       2.31       
ARG     CB       C        11750       20.95        42.50      30.67       1.84       
ARG     CG       C        7355        18.22        37.83      27.23       1.19       
ARG     CD       C        7489        35.05        49.06      43.17       0.86       
ARG     CZ       C        179        156.20       177.70     160.09       3.29       
ARG     N        N        13983      103.60       137.60     120.81       3.72       
ARG     NE       N        1602        75.15        99.81      84.68       1.63       
ARG     NH1      N        53          67.60        87.07      73.64       4.11       
ARG     NH2      N        49          70.10        85.28      73.43       3.49       

ASP     H        H        18668        4.06        12.61       8.31       0.58       
ASP     HA       H        14306        2.33         6.33       4.60       0.32       
ASP     HB2      H        13209       -0.39         4.58       2.72       0.27       
ASP     HB3      H        12552        0.02         4.58       2.67       0.28       
ASP     C        C        11284      166.80       182.70     176.44       1.76       
ASP     CA       C        15593       44.81        62.49      54.68       2.04       
ASP     CB       C        14484       27.48        51.09      40.86       1.64       
ASP     CG       C        260        170.72       183.94     179.27       1.83       
ASP     N        N        17050      101.90       143.52     120.68       3.91       

ASN     H        H        13233        2.61        12.40       8.35       0.63       
ASN     HA       H        10395        1.75         6.43       4.67       0.37       
ASN     HB2      H        9633         0.23         4.47       2.81       0.31       
ASN     HB3      H        9191        -0.07         4.47       2.76       0.33       
ASN     HD21     H        6984         3.55         9.60       7.35       0.48       
ASN     HD22     H        6928         3.08        10.80       7.14       0.49       
ASN     C        C        7649       167.04       181.90     175.31       1.81       
ASN     CA       C        10781       41.31        61.80      53.55       1.90       
ASN     CB       C        9991        28.64        55.09      38.68       1.68       
ASN     CG       C        757        166.40       181.20     176.77       1.38       
ASN     N        N        11604      101.71       137.49     118.96       4.03       
ASN     ND2      N        5490        99.40       133.86     112.79       2.27       

CYS     H        H        7396         4.73        12.12       8.40       0.67       
CYS     HA       H        6504         1.64         6.43       4.67       0.56       
CYS     HB2      H        6210        -0.54         4.65       2.95       0.45       
CYS     HB3      H        6042        -0.83         4.69       2.90       0.47       
CYS     HG       H        53           0.25         7.39       1.90       1.46       
CYS     C        C        2959       166.73       182.73     174.87       2.06       
CYS     CA       C        4222        42.45        67.64      58.17       3.37       
CYS     CB       C        3841        17.99        62.07      32.91       6.29       
CYS     N        N        4936       100.48       135.89     120.16       4.62       

GLU     H        H        24703        4.24        12.17       8.34       0.60       
GLU     HA       H        19108        1.77         6.29       4.25       0.41       
GLU     HB2      H        17271        0.34         3.44       2.03       0.21       
GLU     HB3      H        15873        0.34         3.44       2.00       0.22       
GLU     HG2      H        15931        0.57         3.77       2.28       0.21       
GLU     HG3      H        14443        0.56         3.83       2.26       0.21       
GLU     HE2      H        1            2.73         2.73       2.73       0.00       
GLU     C        C        15424      166.80       183.52     176.93       1.97       
GLU     CA       C        21063       44.35        64.60      57.35       2.09       
GLU     CB       C        19433       18.71        42.33      30.00       1.73       
GLU     CG       C        12874       25.50        50.28      36.10       1.22       
GLU     CD       C        284        173.41       189.46     182.58       1.97       
GLU     N        N        22952      104.54       138.60     120.69       3.51       

GLN     H        H        13124        5.18        12.04       8.22       0.59       
GLN     HA       H        10247        1.60         6.23       4.26       0.43       
GLN     HB2      H        9226        -0.12         4.00       2.05       0.25       
GLN     HB3      H        8581        -0.52         4.04       2.02       0.27       
GLN     HG2      H        8636         0.04         3.66       2.32       0.27       
GLN     HG3      H        7721        -1.08         3.66       2.30       0.29       
GLN     HE21     H        6286         3.69        11.11       7.24       0.46       
GLN     HE22     H        6245         3.59         9.79       7.02       0.45       
GLN     C        C        7947       168.09       182.22     176.36       1.96       
GLN     CA       C        11097       47.87        66.60      56.60       2.14       
GLN     CB       C        10209       20.27        42.20      29.17       1.83       
GLN     CG       C        6855        21.64        41.95      33.78       1.12       
GLN     CD       C        719        171.70       183.54     179.67       1.37       
GLN     N        N        11966      104.10       139.55     119.86       3.63       
GLN     NE2      N        5318        92.49       124.30     111.87       1.80       

GLY     H        H        23513        3.01        12.22       8.33       0.66       
GLY     HA2      H        18020        0.86         6.43       3.97       0.38       
GLY     HA3      H        16897        1.04         6.39       3.90       0.38       
GLY     C        C        13671      163.27       183.16     173.93       1.87       
GLY     CA       C        19293       35.78        58.67      45.35       1.29       
GLY     N        N        20739       94.07       162.19     109.68       3.86       

HIS     H        H        7032         5.24        12.39       8.24       0.69       
HIS     HA       H        5497         1.93         8.90       4.61       0.44       
HIS     HB2      H        5057         0.18         8.70       3.11       0.36       
HIS     HB3      H        4876         0.39         8.70       3.05       0.39       
HIS     HD1      H        262          3.79        17.20       8.79       2.71       
HIS     HD2      H        3534         3.46         9.01       7.03       0.45       
HIS     HE1      H        2925         3.21        10.26       7.98       0.51       
HIS     HE2      H        124          6.58        16.53       9.79       2.62       
HIS     C        C        4239       166.90       182.80     175.28       1.98       
HIS     CA       C        5987        46.01        66.98      56.49       2.33       
HIS     CB       C        5546        18.75        43.30      30.21       2.09       
HIS     CG       C        77         122.67       137.19     131.49       3.33       
HIS     CD2      C        1932       112.07       159.95     120.48       3.46       
HIS     CE1      C        1498       104.67       144.54     137.55       2.41       
HIS     N        N        6345       105.00       136.48     119.62       4.04       
HIS     ND1      N        127        164.64       229.14     195.73      18.04       
HIS     NE2      N        146        161.70       226.29     182.19      14.39       

ILE     H        H        16824        3.43        11.69       8.28       0.69       
ILE     HA       H        12991        1.32         6.36       4.18       0.56       
ILE     HB       H        12117       -1.28         3.87       1.79       0.29       
ILE     HG12     H        10874       -2.38         2.69       1.27       0.40       
ILE     HG13     H        10302       -2.04         2.99       1.21       0.41       
ILE     HG2      H        11468       -1.14         1.87       0.78       0.27       
ILE     HD1      H        11512       -1.08         2.82       0.68       0.29       
ILE     C        C        10401      167.00       183.40     175.88       1.95       
ILE     CA       C        14169       51.15        71.70      61.63       2.69       
ILE     CB       C        13058       20.94        51.88      38.62       2.04       
ILE     CG1      C        8570        12.90        39.05      27.74       1.75       
ILE     CG2      C        9199         3.45        29.80      17.54       1.41       
ILE     CD1      C        9257         2.70        29.60      13.47       1.68       
ILE     N        N        15335       99.00       138.12     121.50       4.33       

LEU     H        H        27402        3.01        13.22       8.22       0.65       
LEU     HA       H        21123        1.93         6.24       4.31       0.47       
LEU     HB2      H        19175       -1.21         3.18       1.62       0.34       
LEU     HB3      H        18054       -1.29         3.18       1.53       0.36       
LEU     HG       H        16926       -1.06         3.90       1.51       0.33       
LEU     HD1      H        18806       -1.73         2.36       0.76       0.28       
LEU     HD2      H        18027       -1.65         2.78       0.74       0.28       
LEU     C        C        16702      167.49       189.78     177.02       2.00       
LEU     CA       C        22974       46.36        65.83      55.66       2.14       
LEU     CB       C        21272       26.40        53.70      42.29       1.87       
LEU     CG       C        13274       15.57        39.56      26.80       1.15       
LEU     CD1      C        14699       10.95        31.83      24.68       1.61       
LEU     CD2      C        13894       11.71        30.40      24.10       1.69       
LEU     N        N        24920       40.20       144.55     121.85       3.96       

LYS     H        H        24057        5.09        12.03       8.19       0.61       
LYS     HA       H        18613        1.30         6.17       4.26       0.44       
LYS     HB2      H        16677       -0.84         4.05       1.78       0.25       
LYS     HB3      H        15383       -0.97         3.95       1.75       0.27       
LYS     HG2      H        14910       -1.16         2.99       1.37       0.26       
LYS     HG3      H        13371       -1.11         2.99       1.35       0.28       
LYS     HD2      H        13075       -1.68         8.50       1.61       0.23       
LYS     HD3      H        11312       -1.02         3.61       1.60       0.23       
LYS     HE2      H        12948        1.25         4.36       2.92       0.19       
LYS     HE3      H        10988        1.24         4.55       2.91       0.19       
LYS     HZ       H        666          2.41         9.90       7.42       0.64       
LYS     C        C        13823      167.21       185.00     176.68       1.97       
LYS     CA       C        19226       46.60        63.38      56.96       2.20       
LYS     CB       C        17741       21.19        46.60      32.78       1.78       
LYS     CG       C        11299       18.20        36.22      24.93       1.15       
LYS     CD       C        10714       21.20        42.26      28.96       1.15       
LYS     CE       C        10328       30.48        52.20      41.91       0.81       
LYS     N        N        21285      101.10       140.30     121.09       3.80       
LYS     NZ       N        13          31.00        43.69      33.96       3.04       

MET     H        H        6595         4.87        12.46       8.26       0.60       
MET     HA       H        5287         1.13         6.35       4.41       0.48       
MET     HB2      H        4729        -1.05         3.87       2.03       0.34       
MET     HB3      H        4368        -0.99         3.20       2.00       0.34       
MET     HG2      H        4290        -0.36         4.40       2.43       0.36       
MET     HG3      H        4003        -0.30         4.24       2.40       0.38       
MET     HE       H        2834        -0.21        17.06       1.88       0.48       
MET     C        C        4125       167.40       183.16     176.21       2.09       
MET     CA       C        5843        45.50        66.56      56.13       2.25       
MET     CB       C        5286        20.98        46.46      32.99       2.24       
MET     CG       C        3264        20.46        38.58      32.04       1.26       
MET     CE       C        2301         0.00        40.77      17.17       1.94       
MET     N        N        6068        87.60       135.66     120.10       3.58       

PHE     H        H        11931        4.81        12.18       8.36       0.72       
PHE     HA       H        9125         1.78         6.57       4.62       0.56       
PHE     HB2      H        8460         0.17         4.46       3.00       0.37       
PHE     HB3      H        8182         0.42         4.31       2.95       0.38       
PHE     HD1      H        7062         4.72         8.08       7.06       0.30       
PHE     HD2      H        5638         4.72         8.15       7.07       0.30       
PHE     HE1      H        6215         4.10         8.80       7.09       0.31       
PHE     HE2      H        5048         4.10         8.80       7.08       0.32       
PHE     HZ       H        4426         4.53         9.50       7.00       0.42       
PHE     C        C        7108       166.85       183.77     175.48       1.99       
PHE     CA       C        9812        47.31        69.82      58.13       2.56       
PHE     CB       C        9086        25.52        48.53      39.93       2.10       
PHE     CG       C        104        128.30       152.84     138.34       2.35       
PHE     CD1      C        3509       118.50       138.70     131.55       1.20       
PHE     CD2      C        2200       118.50       138.70     131.61       1.14       
PHE     CE1      C        2998       114.75       135.60     130.68       1.43       
PHE     CE2      C        1899       118.00       139.70     130.77       1.19       
PHE     CZ       C        2225       116.46       138.60     129.24       1.54       
PHE     N        N        10732      102.20       139.02     120.49       4.15       

PRO     HA       H        10175        1.63         6.05       4.40       0.33       
PRO     HB2      H        9469        -0.28         4.02       2.07       0.35       
PRO     HB3      H        9012        -1.07         3.79       2.01       0.36       
PRO     HG2      H        8496        -0.39         4.42       1.93       0.31       
PRO     HG3      H        7721        -0.90         4.42       1.91       0.33       
PRO     HD2      H        8735         0.63         5.36       3.65       0.36       
PRO     HD3      H        8317        -0.26         5.36       3.62       0.38       
PRO     C        C        7467       168.43       182.30     176.73       1.53       
PRO     CA       C        10753       50.12        70.67      63.34       1.55       
PRO     CB       C        9916        24.69        43.70      31.85       1.19       
PRO     CG       C        6692        18.28        33.90      27.21       1.09       
PRO     CD       C        6741        40.05        58.30      50.36       0.98       
PRO     N        N        266        111.56       145.26     133.97       6.60       

SER     H        H        19972        3.76        13.13       8.28       0.59       
SER     HA       H        15812        1.66         6.44       4.48       0.41       
SER     HB2      H        14322        1.74         5.41       3.88       0.26       
SER     HB3      H        12983        1.51         5.01       3.85       0.28       
SER     HG       H        237          0.00         8.97       5.32       1.03       
SER     C        C        11819      164.47       184.88     174.69       1.75       
SER     CA       C        16738       45.13        68.40      58.76       2.10       
SER     CB       C        15232       52.61        73.90      63.80       1.49       
SER     N        N        17737      100.85       133.68     116.29       3.59       

THR     H        H        17903        5.32        11.73       8.24       0.62       
THR     HA       H        13855        0.87         6.36       4.46       0.48       
THR     HB       H        12592        0.92         8.35       4.17       0.33       
THR     HG1      H        407          0.32         8.21       5.01       1.54       
THR     HG2      H        12498       -1.19         4.07       1.14       0.23       
THR     C        C        10324      165.50       184.43     174.58       1.77       
THR     CA       C        14559       51.61        72.80      62.23       2.63       
THR     CB       C        13281       33.00        80.22      69.70       1.69       
THR     CG2      C        8976        11.70        36.73      21.56       1.11       
THR     N        N        15948       97.70       138.27     115.45       4.76       

TRP     H        H        3788         4.49        11.67       8.30       0.79       
TRP     HA       H        2886         2.28         6.52       4.68       0.52       
TRP     HB2      H        2686         0.42         4.54       3.19       0.36       
TRP     HB3      H        2573         0.77         4.44       3.13       0.36       
TRP     HD1      H        2397         4.90        10.75       7.15       0.35       
TRP     HE1      H        2566         5.80        12.92      10.10       0.54       
TRP     HE3      H        2146         4.89         8.79       7.32       0.40       
TRP     HZ2      H        2268         4.90         8.27       7.29       0.32       
TRP     HZ3      H        2069         3.88         8.90       6.87       0.40       
TRP     HH2      H        2099         4.53        10.90       6.99       0.39       
TRP     C        C        2051       168.17       181.89     176.15       2.02       
TRP     CA       C        2906        44.69        69.76      57.66       2.58       
TRP     CB       C        2680        21.10        43.02      29.98       2.02       
TRP     CG       C        103        105.30       116.53     110.65       1.88       
TRP     CD1      C        1212       108.45       132.35     126.47       1.94       
TRP     CD2      C        79         120.20       130.10     127.48       1.40       
TRP     CE2      C        70         118.50       177.71     138.63       6.80       
TRP     CE3      C        1029       111.86       137.60     120.51       1.72       
TRP     CZ2      C        1144        81.81       129.97     114.23       1.55       
TRP     CZ3      C        1032       113.32       138.39     121.42       1.58       
TRP     CH2      C        1067        91.62       131.54     123.81       1.84       
TRP     N        N        3202       106.44       138.11     121.63       4.17       
TRP     NE1      N        1833       107.64       139.20     129.36       2.05       

TYR     H        H        10047        4.16        11.98       8.32       0.74       
TYR     HA       H        7821         1.20         6.73       4.63       0.56       
TYR     HB2      H        7253         0.49         4.70       2.91       0.37       
TYR     HB3      H        7033        -0.19         4.70       2.85       0.39       
TYR     HD1      H        6473         4.98         8.53       6.94       0.30       
TYR     HD2      H        5255         4.20         8.50       6.94       0.30       
TYR     HE1      H        6204         2.78         7.86       6.71       0.23       
TYR     HE2      H        5089         3.13         8.50       6.71       0.24       
TYR     HH       H        116          5.99        13.75       9.30       1.42       
TYR     C        C        5494       167.86       182.92     175.41       1.99       
TYR     CA       C        7872        49.08        65.99      58.13       2.55       
TYR     CB       C        7207        28.82        57.73      39.30       2.15       
TYR     CG       C        95         117.70       174.59     129.76       5.25       
TYR     CD1      C        3165       116.44       138.65     132.76       1.25       
TYR     CD2      C        1930       113.00       136.70     132.71       1.45       
TYR     CE1      C        3137       110.70       134.01     117.93       1.23       
TYR     CE2      C        1922       113.10       134.01     117.92       1.33       
TYR     CZ       C        79         153.54       162.70     156.63       2.11       
TYR     N        N        8642       100.09       144.96     120.63       4.26       

VAL     H        H        21624        3.98        12.59       8.29       0.68       
VAL     HA       H        16806        0.97         6.30       4.19       0.58       
VAL     HB       H        15708       -0.54         3.32       1.99       0.32       
VAL     HG1      H        15354       -1.12         2.57       0.83       0.26       
VAL     HG2      H        14905       -2.32         2.78       0.80       0.28       
VAL     C        C        13095      165.65       183.69     175.66       1.90       
VAL     CA       C        18088       50.16        70.02      62.49       2.88       
VAL     CB       C        16694       20.55        45.33      32.72       1.80       
VAL     CG1      C        11828       13.53        32.27      21.50       1.38       
VAL     CG2      C        11267       13.58        30.46      21.29       1.57       
VAL     N        N        19732       97.95       143.29     121.13       4.59       
		   
 
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