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Ramachandran Map 

Godfrey Beddard, School of Chemistry, University of Leeds, LS2 3JT UK. 

The Ramachandram map is a plot of the phi vs psi torsion angles in a protein and is formed by adding a point at (f,  y) for each amino acid residue.The angles range from +-180o. 

A torsion angle is defined between two planes, for example as the angle between the two pages of an open book, and in a protein these angles are defined as shown in the figure.   The backbone O=C-N(H)Ca and the CaC(=O)NH  atoms are each in a plane (shown shaded) and the angle y is that between the planes containing the Ca and N atoms and that containing the C(=O) and N(H) atoms, and f bewtween (O=)CN and CaC(=O) as shown. 

 

Image 

Although Ca has only single bonds which are therefore free to rotate, not all psi and phi torsion angles are observed because van der Waals interactions between non-bonded atoms in the backbone, and with atoms in the amino acid residues, R, make large ranges of angles too high in energy to be observed in most proteins. For example, if the oxygen atoms are ingored, and the bond  (N-Ca) (angle f ) is rotated the two carbon atoms eventually reach a cis conformation rather than the trans shown above. They are now relatively close to one another and because of the mutual repulsion of their electrons this conformation may not be allowed and is sterically forbidden. 

The main secondary structures of proteins are the a-helix and b-sheet.  Alpha helices are found in the region bouded approximately by (f) phi = -60 +/- 10 ,  (y) psi = -45 +/- 10 ,  and b-sheets in the region phi = -45 to -150,  psi = 100 to 180.  

Ramachandran maps (also called plots) are described in most textbook dealing with protiens, see Branden & Tooze, 'Introduction to Protein Science', publ Garland Publishing 1991, or Finkelstein and Ptitsyn, 'Protein Physics', publ Academic Press, 2002. See Davis et al. Proteins vol, 50 p 437, 2003 for a more sophisticated method of calculating forbidden regions. Calculating torsion angles and general properties of vectors are described in Beddard, 'Applying Maths in the Chemical and Biosciences, an example based approach', publ OUP, 2009. 

To use this programmme 

(1) Download some data from the RCSB Protein data bank http://www.rcsb.org/pdb/home/home.do
(2) The input is all of pdb file just as downloaded
(3) Put the data in the same folder as this document and finally add the .pdb name to the list as shown below. Some examples are shown 

The output is
(1) Torsion angles. This option can be disabled at the printf statements which are placed just before plotting.
(2) Ramachandran graphs produced are 

       (a) all residues, (b) glycines only , (c) prolines only and (d) pre-prolines only 

      Superimposed on the maps are grey lines to indicate the (approximate) sterically allowed areas. 

 

> restart:  with(LinearAlgebra):  with(plots):  with(StringTools):
 

> #####################################################################
# some pdb data set names
dataname:= `1FBB.pdb`:            # bacteriorhodopsin, largely alpha helix
#dataname:= `1jb0.pdb`:            # photosystem 1, huge data set
#dataname:= `1THB.pdb`:            # haem largely alpha helix
#dataname:= `107L.pdb`:            # myoglobin, largely alpha-helix
#dataname:= `1RUZ.pdb`:            # hemoggutinin 2028 residues
#dataname:= `I27.pdb`:             # I27, small protein
#dataname:= `1qjp.pdb`:            # beta-barrel, E-coli outer membrane protein, 170 residues
#dataname:= `1crn.pdb`:            # crambin
#dataname:= `1alc.pdb`:            # alpha lactalbumin, 212 residues
#dataname:= `1e1q.pdb`:            # Bovine ATPase; huge data set, 3225 residues
 

> #####################################################################

ramachandran:= proc(dataname)

local TorsionAngle,angle_psi,angle_phi,aline,n_atoms,n,st,MAT,j,k,i,len,m,val_phi,jend,resd,val_psi,res_name,ss,res_A,phi_A,psi_A,ss_A,p1,p2,p3,p4,L1:
global indx,Solid_Lines,lines:
                   # proc TorsionAngle ################################################
# calculate torsion angle given atom coordinates
TorsionAngle:= proc(atom1,atom2,atom3,atom4)
local m,n,A,B,C,cos_angle,angle:
A:=atom2-atom1;  B:=atom3-atom2: C:=atom4-atom3:
m:= A &x B:
n:= B &x C:
cos_angle:=(m . n )/(sqrt(n.n)*sqrt(m.m));
angle:= sign(A.n) * evalf( arccos(cos_angle)*180.0/Pi );
end proc:
                   # proc angle_psi ################################################
# search for atoms N-CA-C-N coordinates starting at position m in pdb list
angle_psi:= proc( m )
global indx:
local n,j,i,N1,C,CA,N2,psi,n_atom,c_atom:
n_atom:="N":
c_atom:="C":
j:= 0:
while MAT[m+j,3] <> n_atom do  j:=j+1; end do;
n:= m + j;
N1:= < MAT[n,7]  | MAT[n,8]  | MAT[n,9]  >;      
CA:= < MAT[n+1,7]| MAT[n+1,8]| MAT[n+1,9]>;     
C:=  < MAT[n+2,7]| MAT[n+2,8]| MAT[n+2,9]>;   
i:=1:
while MAT[n+i,3] <> n_atom do i:= i + 1; end do:
if MAT[n+i,3] = n_atom then
N2:= < MAT[n+i,7]| MAT[n+i,8]| MAT[n+i,9]>;     end if;
indx:= n + i:
TorsionAngle(N1,CA,C,N2);# angle psi
end proc:
 

>                     # proc angle_phi ################################################
# search for atoms C-N-CA-C starting at position m in pdb list
angle_phi:= proc( m )
global indx:
local n,j,i,C1,N,CA,C2,phi,n_atom,c_atom:
n_atom:="N":
c_atom:="C":
j:= 0:
while MAT[m+j,3] <> c_atom do  j:= j + 1; end do;
n:= m + j;
C1:= < MAT[n,7]   | MAT[n,8]  |   MAT[n,9]> ;
i:= 1:
while MAT[n+i,3] <> n_atom do i:= i + 1; end do:
N:=  < MAT[n+i,7]  | MAT[n+i,8]  | MAT[n+i,9]  >;     
CA:= < MAT[n+i+1,7]| MAT[n+i+1,8]| MAT[n+i+1,9]>;   
C2:= < MAT[n+i+2,7]| MAT[n+i+2,8]| MAT[n+i+2,9]>;  
indx:= n + i + 2:
TorsionAngle(C1,N,CA,C2); # angle phi
end proc:

                  # proc Solid_lines ################################################
         ############  solid lines for conventionally folded structures ############

Solid_Lines:= proc()                                         # approximate angles
local xa,ya,sa:
lines:=[ ]:
xa:=[-176, -57, -40, -40, -108, -108, -40, -40, -175, -175, -159, -95, -95, -176, -176]:
ya:=[180, 180, 163, 98, 98, 36, -30, -66, -66, -40, -58, -58, -21, 60, 180]:
sa:=seq([xa[i],ya[i]],i=1..nops(xa)):
lines:=[op(lines),plot([sa],color=grey)];

xa:=[62, 62, 41, 41, 62];
ya:=[125, 13, 36, 102, 125];
sa:=seq([xa[i],ya[i]],i=1..nops(xa)):
lines:=[op(lines),plot([sa],color=grey)];

xa:=[-177, -63, -63, -177, -177]:
ya:=[-168, -168, -179, -179, -168]:
sa:=seq([xa[i],ya[i]],i=1..nops(xa)):
lines:=[ op(lines), plot([sa],color=grey) ];

end proc:
                  ################################################
 

> # read all of pdb look for ATOM
aline:= readline(dataname):                                   # work out size of data
n_atoms:=0:  n:= 1: st:=0:
while aline <> 0 do
 aline:=readline(dataname):
 if aline[1..4] = "ATOM" then
   n_atoms:= n_atoms + 1;
   if st = 0 then st:= n + 1: end if
 end if;
 n:= n + 1;
end do:
printf("%s %a %s %a %s %a \n","Atom coords start at line",st ," and there are ",n_atoms, "atoms. pdb ends at line", n-1);
MAT:= Matrix(n_atoms,12):

                  ################################################

# now read data into matrix MAT
# reading is done explicitly because there are not always gaps between different entries
# in the line of data i.e. CD1AILE can occur rather than CD1 ILE
j:= 1:
res_A:= 0:
for k from 1 to n - 1 do
 aline:= readline(dataname):
 if k >= st and aline[1..4] = "ATOM" then
  m:=sscanf(aline, "%27c %8f %8f %8f %4f %6f %s");
  MAT[j,1]:= m[1][1..4];                                      # atom             # 1
  MAT[j,2]:= convert(DeleteSpace(m[1][5..11]),decimal,10);    # atom number      # 2
  MAT[j,3]:= DeleteSpace(m[1][12..16]);                       # atom label       # 3
  MAT[j,4]:= DeleteSpace(m[1][17..20]);                       # residue name     # 4
  MAT[j,5]:= DeleteSpace(m[1][21..23]);                       # chain A , B etc. # 5
  # check if some residues are labelled 49A for example
  if m[1][27]<> " " then res_A:= res_A + 1: end if:  
  MAT[j,6]:= convert(DeleteSpace(m[1][24..26]),decimal,10);   # residue number   # 6
  for i from 2 to 7 do         
    MAT[j,i+5]:= m[i];                                        # MAT 7,8, 9 are coordinates
  end do:
  j:= j + 1;
 end if;
end do:
j:= j - 1:                                                     # number of atoms
close(dataname):
len:=0:
if MAT[n_atoms, 5] <> "A" then
 for i from 2 to n_atoms do
   if MAT[i,6] < MAT[i-1,6]  then
     len:= len + MAT[i-1,6];
   end if;
 end do;
 len:= len + MAT[n_atoms,6]                                   # add last chain
else
 len:= MAT[n_atoms,6]:                                        # number of residues
end if:
len:= len + res_A :  
# check last residue in case it is not complete
L1:=0:
for i from n_atoms by -1 to n_atoms-4 do
   if MAT[ i,6] <> MAT[i-1,6] then L1:=L1+1 end if;
end do;
if L1 <> 0 then
 len:= len - 1;
 n_atoms:= n_atoms - L1;
 printf("%s \n","Last residue incomplete");
end if;                      
printf("%s %a %s \n","There are ",len," residues");

                  ################################################
 

> # make array to hold results then calc angle phi
val_phi:= Vector(1..len):
for i from 1 to len do val_phi[i]:= 200 end do:   # 200 so it is not plotted if empty
jend:= n_atoms:
while MAT[jend,4] = MAT[jend-1,4] do jend:= jend - 1 end do:
j:= 1:  indx:= 1: resd:= 1:                       # calculate phi
while indx <= jend  do                            # indx is incremented in angle_phi
 val_phi[j]:= angle_phi(indx):
 resd:= MAT[indx,2]:
 j:= j + 1:
end do:

# make array to hold results then calc angle psi and print angles.
#
# Comment out printf statements to prevent printing angles.
#
val_psi:=Vector(1..len):
res_name:=Vector(1..len):
for i from 1 to len do val_psi[i]:=200 end do:
printf(" %s \n" ,"        atom    residue       phi       psi    ");
j:= 1:  indx:= 2: resd:=1:                        # calculate psi, ignore ist residue
while indx <  jend do
 val_psi[j]:= angle_psi(indx):
 res_name[j]:= MAT[indx-1,4]:                     # need names for some plots
 resd:= MAT[indx,2];
 printf("%5a %s %5a %4s %2s %4a %9.4g %9.4g \n",j,":",MAT[indx-1,2],MAT[indx-1,4],MAT[indx-1,5],
                                                      MAT[indx-1,6],val_phi[j],val_psi[j]):
j:= j + 1:
end do:
                  ################################################
            ###########       plot all residues         #################
 

> ss:=seq([val_phi[i],val_psi[i]],i=1..len):   
p1:=plot([ss],style=point,color=black,axes=boxed,scaling=constrained,labels=["phi","psi"],
   symbolsize=10,style=point,symbol=circle,view=[-180..180,-180..180],
   tickmarks=[spacing(30),spacing(30)],axis=[gridlines=[majorlines=1,color=grey]],
   axesfont=[times,12],font=[times,12], resolution=600,numpoints=1000,
   title="All Residues  "|| dataname ):
Solid_Lines():
print(display(p1,lines));

                  ################################################
 

> res_A:=Vector(1..len):                        # plot GLY
phi_A:=Vector(1..len):
psi_A:=Vector(1..len):
j:=1:
for i from 1 to len do
 if res_name[i]="GLY" then
   phi_A[j]:=val_phi[i];  psi_A[j]:=val_psi[i]:  j:=j+1:
 end if:
end do:
ss_A:=seq([phi_A[i],psi_A[i]],i=1..j-1):
p2:=plot([ss_A],color=black,   axes=boxed,  scaling=constrained,
  labels=["phi","psi"], symbolsize=10,style=point,symbol=circle,
  view=[-180..180,-180..180],tickmarks=[spacing(30),spacing(30)],
  axis=[gridlines=[majorlines=1,color=grey]],axesfont=[times,12],font=[times,12],
  resolution=600,numpoints=1000,title="Glycines  "||dataname):
print(display(p2,lines));

                  ################################################
 

> j:=1:
for i from 1 to len do                        # plot PRO
 if res_name[i]="PRO" then
   phi_A[j]:=val_phi[i];  psi_A[j]:=val_psi[i]:  j:=j+1:
 end if:
end do:
ss_A:=seq([phi_A[i],psi_A[i]],i=1..j-1):
p3:=plot([ss_A],color=black,   axes=boxed,  scaling=constrained,
  labels=["phi","psi"], symbolsize=10,style=point,symbol=circle,
  view=[-180..180,-180..180],tickmarks=[spacing(30),spacing(30)],
  axis=[gridlines=[majorlines=1,color=grey]],axesfont=[times,12],font=[times,12],
  resolution=600,numpoints=1000,title="prolines   "||dataname):
print(display(p3,lines));

                  ################################################
 

> j:=1:
for i from 2 to len do                       # plot pre PRO
 if res_name[i]="PRO" then
   phi_A[j]:=val_phi[i-1];  psi_A[j]:=val_psi[i-1]:  j:=j+1:
 end if:
end do:
ss_A:=seq([phi_A[i],psi_A[i]],i=1..j-1):
p4:=plot([ss_A],color=black,   axes=boxed,  scaling=constrained,
  labels=["phi","psi"], symbolsize=10,style=point,symbol=circle,
  view=[-180..180,-180..180],tickmarks=[spacing(30),spacing(30)],
  axis=[gridlines=[majorlines=1,color=grey]],axesfont=[times,12],font=[times,12],
  resolution=600,numpoints=1000,title="pre-prolines  " ||dataname):
print(display(p4,lines));

end proc:                  # ramachandran

#####################################################################
 

> # now do the calculation

ramachandran(dataname);
 

 

 

Atom coords start at line 278  and there are  1733 atoms. pdb ends at line 2054
 

 

There are  227  residues
 

 

        atom    residue       phi       psi     
   1 :    12  THR  A    5     174.1     50.44
   2 :    16  GLY  A    6     114.6     4.028
   3 :    27  ARG  A    7    -130.3    -46.57
   4 :    34  PRO  A    8    -61.35    -40.99
   5 :    43  GLU  A    9    -94.45     13.08
   6 :    57  TRP  A   10    -49.38    -28.84
   7 :    65  ILE  A   11    -63.48    -81.76
   8 :    79  TRP  A   12    -36.04    -46.57
   9 :    87  LEU  A   13    -52.09    -58.92
  10 :    92  ALA  A   14    -51.99    -46.44
  11 :   100  LEU  A   15    -58.83    -39.51
  12 :   104  GLY  A   16    -68.28    -37.09
  13 :   111  THR  A   17    -66.48     -48.5
  14 :   116  ALA  A   18    -53.57    -40.59
  15 :   124  LEU  A   19     -72.6     -48.1
  16 :   132  MET  A   20    -57.16    -50.85
  17 :   136  GLY  A   21     -68.8    -34.46
  18 :   144  LEU  A   22    -63.03     -49.8
  19 :   148  GLY  A   23    -54.42    -33.11
  20 :   155  THR  A   24    -67.03    -57.44
  21 :   163  LEU  A   25    -54.08     -32.3
  22 :   175  TYR  A   26    -64.06    -60.57
  23 :   186  PHE  A   27     -51.8    -57.56
  24 :   194  LEU  A   28    -40.19     -46.9
  25 :   201  VAL  A   29    -92.51      48.9
  26 :   210  LYS  A   30    -158.7    -9.583
  27 :   214  GLY  A   31    -110.4    -1.595
  28 :   222  MET  A   32       -45    -56.81
  29 :   226  GLY  A   33    -58.75    -83.99
  30 :   233  VAL  A   34      27.1     107.3
  31 :   239  SER  A   35    -101.2    -48.03
 

 

  32 :   247  ASP  A   36    -59.61     115.5
  33 :   254  PRO  A   37    -66.26    -33.96
  34 :   262  ASP  A   38    -49.99    -56.77
  35 :   267  ALA  A   39    -67.94    -35.84
  36 :   276  LYS  A   40    -44.64    -39.91
  37 :   285  LYS  A   41    -51.06    -63.07
  38 :   296  PHE  A   42    -40.25     -57.6
  39 :   308  TYR  A   43    -44.79    -71.43
  40 :   313  ALA  A   44    -37.14     -51.6
  41 :   321  ILE  A   45    -62.88    -63.47
  42 :   328  THR  A   46    -55.45      8.77
  43 :   335  THR  A   47    -120.5    -44.12
  44 :   343  LEU  A   48    -51.69    -47.85
  45 :   350  VAL  A   49    -42.03    -62.39
  46 :   357  PRO  A   50    -58.63    -49.53
  47 :   362  ALA  A   51    -47.31    -62.25
  48 :   370  ILE  A   52    -54.79    -48.51
  49 :   375  ALA  A   53    -48.64    -38.59
  50 :   386  PHE  A   54    -63.98    -45.97
  51 :   393  THR  A   55    -62.55    -37.42
  52 :   401  MET  A   56    -70.68    -49.74
  53 :   413  TYR  A   57    -62.06    -20.66
  54 :   421  LEU  A   58    -78.51    -49.22
  55 :   427  SER  A   59    -65.32    -27.14
  56 :   435  MET  A   60    -64.41    -46.53
  57 :   443  LEU  A   61    -65.24     -54.8
  58 :   451  LEU  A   62    -56.75    -26.72
  59 :   455  GLY  A   63     143.5    -73.16
  60 :   467  TYR  A   64    -22.11    -38.45
  61 :   471  GLY  A   65    -40.81    -77.29
  62 :   479  LEU  A   66    -58.61       173
  63 :   486  THR  A   67    -159.8     169.5
  64 :   494  MET  A   68    -114.5     95.13
  65 :   501  VAL  A   69    -89.72     126.7
  66 :   508  PRO  A   70    -87.01     108.7
  67 :   519  PHE  A   71    -146.4     123.1
  68 :   523  GLY  A   72     62.21     36.87
  69 :   527  GLY  A   73     129.8    -85.04
  70 :   536  GLU  A   74    -101.4    -179.3
  71 :   545  GLN  A   75    -89.38     117.2
  72 :   553  ASN  A   76    -105.2     145.3
  73 :   560  PRO  A   77    -75.71     141.7
  74 :   568  ILE  A   78    -147.1     93.62
  75 :   580  TYR  A   79    -64.02     84.17
  76 :   594  TRP  A   80    -61.78    -18.73
  77 :   599  ALA  A   81    -52.36    -34.77
  78 :   610  ARG  A   82     -56.9    -69.67
  79 :   622  TYR  A   83    -39.96     -39.4
  80 :   627  ALA  A   84    -53.75    -60.82
  81 :   635  ASP  A   85    -44.59    -74.77
  82 :   649  TRP  A   86    -42.29    -40.58
  83 :   657  LEU  A   87    -55.92    -33.45
  84 :   668  PHE  A   88    -96.17    -55.76
  85 :   675  THR  A   89    -49.87    -69.17
 

 

  86 :   682  THR  A   90    -35.43    -45.75
  87 :   689  PRO  A   91    -64.79    -59.34
  88 :   697  LEU  A   92    -40.08    -42.52
  89 :   705  LEU  A   93    -60.92    -57.56
  90 :   713  LEU  A   94    -45.34    -47.44
  91 :   721  LEU  A   95     -56.8     -41.1
  92 :   729  ASP  A   96    -54.18     -44.9
  93 :   737  LEU  A   97    -67.44    -63.29
  94 :   742  ALA  A   98    -47.89    -58.84
  95 :   750  LEU  A   99    -47.86    -46.47
  96 :   758  LEU  A  100    -55.98    -70.17
  97 :   765  VAL  A  101    -75.04     45.77
  98 :   773  ASP  A  102     9.889     73.64
  99 :   778  ALA  A  103    -87.38       144
 100 :   786  ASP  A  104    -59.89     127.9
 101 :   795  GLN  A  105    -40.11    -33.31
 102 :   799  GLY  A  106    -49.35    -63.34
 103 :   806  THR  A  107    -62.04    -37.24
 104 :   814  ILE  A  108    -53.02    -62.09
 105 :   822  LEU  A  109    -46.52    -54.84
 106 :   827  ALA  A  110    -62.82    -29.31
 107 :   835  LEU  A  111    -73.73    -41.79
 108 :   842  VAL  A  112    -65.08    -53.25
 109 :   846  GLY  A  113    -56.95    -31.52
 110 :   851  ALA  A  114    -63.66    -52.76
 111 :   859  ASP  A  115    -61.67    -40.69
 112 :   863  GLY  A  116    -49.57    -60.82
 113 :   871  ILE  A  117    -57.49    -32.69
 114 :   879  MET  A  118    -61.51    -73.09
 115 :   887  ILE  A  119    -52.51    -51.23
 116 :   891  GLY  A  120    -47.25    -52.51
 117 :   898  THR  A  121    -68.58     -24.6
 118 :   902  GLY  A  122     -69.1    -28.74
 119 :   910  LEU  A  123    -71.12    -62.56
 120 :   917  VAL  A  124    -46.85     -35.7
 121 :   921  GLY  A  125    -58.29    -57.87
 122 :   926  ALA  A  126    -77.03     35.94
 123 :   934  LEU  A  127    -149.4     1.234
 124 :   941  THR  A  128    -77.53     144.8
 125 :   950  LYS  A  129    -88.43     -48.9
 126 :   957  VAL  A  130    -60.94     115.7
 127 :   969  TYR  A  131    -50.94    -43.77
 128 :   975  SER  A  132    -66.76    -38.11
 129 :   987  TYR  A  133     -62.7    -33.73
 130 :   998  ARG  A  134    -43.56    -46.67
 131 :  1009  PHE  A  135    -72.61    -26.07
 132 :  1016  VAL  A  136    -63.07    -37.39
 133 :  1030  TRP  A  137    -76.45    -43.31
 134 :  1044  TRP  A  138    -44.95    -44.51
 

 

 135 :  1049  ALA  A  139     -62.9    -66.44
 136 :  1057  ILE  A  140    -47.79    -37.05
 137 :  1063  SER  A  141    -67.17    -55.55
 138 :  1070  THR  A  142    -51.08    -50.05
 139 :  1075  ALA  A  143    -44.76    -40.61
 140 :  1080  ALA  A  144    -61.14    -47.85
 141 :  1088  MET  A  145    -63.34    -57.55
 142 :  1096  LEU  A  146     -45.4    -28.24
 143 :  1108  TYR  A  147    -68.17    -59.71
 144 :  1116  ILE  A  148    -47.41    -63.08
 145 :  1124  LEU  A  149    -50.42    -36.06
 146 :  1136  TYR  A  150    -62.94     -71.4
 147 :  1143  VAL  A  151    -62.82     19.15
 148 :  1151  LEU  A  152      -119    -52.15
 149 :  1162  PHE  A  153       -72    -11.48
 150 :  1173  PHE  A  154    -101.4    -70.18
 151 :  1177  GLY  A  155    -57.88    -79.43
 152 :  1188  PHE  A  156    -37.81    -17.72
 153 :  1195  THR  A  157    -78.24    -53.51
 154 :  1201  SER  A  158    -54.26    -70.78
 155 :  1210  LYS  A  159    -46.28     -42.7
 156 :  1215  ALA  A  160    -54.85    -61.92
 157 :  1224  GLU  A  161    -73.95     63.63
 158 :  1230  SER  A  162    -169.2     37.46
 159 :  1238  MET  A  163      -150      -120
 160 :  1249  ARG  A  164    -91.86     149.4
 161 :  1256  PRO  A  165    -60.93    -29.76
 162 :  1265  GLU  A  166    -51.75    -68.77
 163 :  1272  VAL  A  167    -45.76    -68.68
 164 :  1277  ALA  A  168    -33.02    -65.77
 165 :  1283  SER  A  169    -52.66    -57.26
 166 :  1290  THR  A  170    -52.87    -52.46
 167 :  1301  PHE  A  171    -45.19    -57.07
 168 :  1310  LYS  A  172    -49.65     -45.9
 169 :  1317  VAL  A  173    -46.98    -78.71
 170 :  1325  LEU  A  174    -47.12    -50.02
 171 :  1336  ARG  A  175    -48.51    -49.72
 172 :  1344  ASN  A  176    -67.87    -42.83
 173 :  1351  VAL  A  177    -59.42    -63.77
 174 :  1358  THR  A  178    -37.15    -50.48
 175 :  1365  VAL  A  179    -60.01    -54.12
 176 :  1372  VAL  A  180    -61.56    -62.24
 177 :  1380  LEU  A  181    -40.52    -76.19
 178 :  1394  TRP  A  182    -35.55    -64.04
 179 :  1400  SER  A  183    -41.05    -43.06
 180 :  1405  ALA  A  184    -41.75    -38.02
 181 :  1417  TYR  A  185    -53.21       -71
 182 :  1424  PRO  A  186    -31.32     -45.6
 183 :  1431  VAL  A  187    -70.71     -56.5
 184 :  1438  VAL  A  188    -47.84    -50.34
 185 :  1452  TRP  A  189    -53.61    -53.77
 186 :  1460  LEU  A  190    -52.98    -68.42
 187 :  1468  ILE  A  191    -49.21    -32.56
 188 :  1472  GLY  A  192    -69.52     174.5
 189 :  1478  SER  A  193    -66.64    -21.96
 190 :  1487  GLU  A  194    -71.61    -24.08
 191 :  1491  GLY  A  195    -117.2    -122.8
 192 :  1496  ALA  A  196    -79.19     113.9
 193 :  1500  GLY  A  197    -66.67     88.73
 194 :  1508  ILE  A  198    -96.47    -65.87
 195 :  1515  VAL  A  199    -83.64     162.4
 196 :  1522  PRO  A  200    -88.17     170.4
 

 

 

 

 

 

 

 

 197 :  1530  LEU  A  201    -64.74    -16.85
 198 :  1538  ASN  A  202     -57.2    -36.08
 199 :  1546  ILE  A  203    -85.62    -71.16
 200 :  1555  GLU  A  204     -18.1    -71.91
 201 :  1562  THR  A  205    -38.68    -62.84
 202 :  1570  LEU  A  206     -57.3    -31.42
 203 :  1578  LEU  A  207    -69.48    -67.91
 204 :  1589  PHE  A  208    -52.78    -23.46
 205 :  1597  MET  A  209    -64.02    -52.76
 206 :  1604  VAL  A  210    -66.24    -51.62
 207 :  1612  LEU  A  211    -53.56    -28.94
 208 :  1620  ASP  A  212     -69.9     -74.4
 209 :  1627  VAL  A  213    -49.64    -31.51
 210 :  1633  SER  A  214    -77.89    -40.17
 211 :  1638  ALA  A  215    -69.92    -42.89
 212 :  1647  LYS  A  216    -81.87    -59.03
 213 :  1654  VAL  A  217    -77.11    -24.73
 214 :  1658  GLY  A  218    -65.02    -68.98
 215 :  1669  PHE  A  219    -51.87    -11.55
 216 :  1673  GLY  A  220    -79.18    -62.05
 217 :  1681  LEU  A  221    -61.17    -52.88
 218 :  1689  ILE  A  222    -47.45    -66.49
 219 :  1697  LEU  A  223    -54.31    -89.21
 220 :  1705  LEU  A  224    -30.68    -28.77
 221 :  1716  ARG  A  225    -88.64     24.88
 222 :  1722  SER  A  226    -125.7     153.7
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