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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 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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