Complet list of 1h20 con fileClick here to see the 3D structure Complete list of 1h20.con file
COMMENT BEGIN
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COMMENT END
CONTACTS BETWEEN
CHAIN(S) "A"
AND
CHAIN(S) "A"

HYDROPHOBIC 2.00 3.80   171
C A 0001  GLU C   2.522 C A 0002  GLN CA 
C A 0001  GLU C   3.236 C A 0002  GLN C  
C A 0001  GLU C   3.169 C A 0002  GLN CB 
C A 0001  GLU C   3.542 C A 0002  GLN CD 
C A 0001  GLU CD  3.483 C A 0003  HIS CD2
C A 0002  GLN C   2.537 C A 0003  HIS CA 
C A 0002  GLN C   3.214 C A 0003  HIS C  
C A 0002  GLN C   3.376 C A 0003  HIS CB 
C A 0002  GLN C   3.412 C A 0003  HIS CG 
C A 0002  GLN C   3.729 C A 0003  HIS CD2
C A 0002  GLN C   3.780 C A 0003  HIS CE1
C A 0003  HIS C   2.474 C A 0004  ALA CA 
C A 0003  HIS C   3.168 C A 0004  ALA C  
C A 0003  HIS C   3.650 C A 0004  ALA CB 
C A 0004  ALA C   2.500 C A 0005  ASP CA 
C A 0004  ALA C   3.295 C A 0005  ASP C  
C A 0004  ALA C   3.637 C A 0005  ASP CB 
C A 0004  ALA CA  3.754 C A 0022  TRP CZ2
C A 0004  ALA C   3.373 C A 0022  TRP CZ2
C A 0005  ASP CA  2.880 C A 0006  PRO CD 
C A 0005  ASP C   2.472 C A 0006  PRO CA 
C A 0005  ASP C   3.400 C A 0006  PRO C  
C A 0005  ASP C   3.580 C A 0006  PRO CB 
C A 0005  ASP C   3.679 C A 0006  PRO CG 
C A 0005  ASP C   2.486 C A 0006  PRO CD 
C A 0005  ASP CG  3.702 C A 0006  PRO CD 
C A 0005  ASP CB  3.785 C A 0023  PHE CB 
C A 0006  PRO C   2.487 C A 0007  ILE CA 
C A 0006  PRO C   3.361 C A 0007  ILE C  
C A 0006  PRO C   3.551 C A 0007  ILE CB 
C A 0007  ILE C   2.444 C A 0008  CYS CA 
C A 0007  ILE C   2.991 C A 0008  CYS C  
C A 0007  ILE C   3.759 C A 0008  CYS CB 
C A 0007  ILE CG2 3.316 C A 0021  ALA CB 
C A 0007  ILE CG2 3.571 C A 0024  CYS C  
C A 0007  ILE CG2 3.562 C A 0024  CYS CB 
C A 0007  ILE CG2 3.433 E A 0034  CYS CB 
C A 0008  CYS CA  3.751 C A 0009  ASN CA 
C A 0008  CYS C   2.547 C A 0009  ASN CA 
C A 0008  CYS C   3.453 C A 0009  ASN C  
C A 0008  CYS C   3.104 C A 0009  ASN CB 
C A 0008  CYS C   3.700 C A 0009  ASN CG 
C A 0008  CYS CA  3.790 C A 0024  CYS CB 
C A 0009  ASN C   2.473 C A 0010  LYS CA 
C A 0009  ASN C   3.020 C A 0010  LYS C  
C A 0009  ASN C   3.751 C A 0010  LYS CB 
C A 0009  ASN C   3.788 C A 0011  PRO CD 
C A 0009  ASN CA  3.511 C A 0033  THR CB 
C A 0009  ASN C   3.386 C A 0033  THR CB 
C A 0009  ASN C   3.580 C A 0033  THR CG2
C A 0010  LYS CA  2.919 C A 0011  PRO CD 
C A 0010  LYS C   2.435 C A 0011  PRO CA 
C A 0010  LYS C   3.147 C A 0011  PRO C  
C A 0010  LYS C   3.636 C A 0011  PRO CB 
C A 0010  LYS C   3.547 C A 0011  PRO CG 
C A 0010  LYS C   2.461 C A 0011  PRO CD 
C A 0010  LYS C   3.797 C A 0033  THR CA 
C A 0011  PRO CA  3.796 C A 0012  CYS CA 
C A 0011  PRO C   2.527 C A 0012  CYS CA 
C A 0011  PRO C   3.773 C A 0012  CYS C  
C A 0011  PRO C   3.145 C A 0012  CYS CB 
C A 0012  CYS C   2.445 C A 0013  LYS CA 
C A 0012  CYS C   3.594 C A 0013  LYS C  
C A 0012  CYS C   3.413 C A 0013  LYS CB 
C A 0012  CYS CB  3.585 C A 0017  ASP CB 
C A 0012  CYS CB  3.304 C A 0017  ASP CG 
C A 0013  LYS C   2.492 C A 0014  THR CA 
C A 0013  LYS C   3.331 C A 0014  THR C  
C A 0013  LYS C   3.678 C A 0014  THR CB 
C A 0013  LYS C   3.639 E A 0027  CYS CB 
C A 0014  THR C   2.434 C A 0015  HIS CA 
C A 0014  THR C   3.244 C A 0015  HIS C  
C A 0014  THR C   3.597 C A 0015  HIS CB 
C A 0014  THR C   3.460 E A 0027  CYS CB 
C A 0015  HIS C   2.522 C A 0016  ASP CA 
C A 0015  HIS C   3.158 C A 0016  ASP C  
C A 0015  HIS C   3.714 C A 0016  ASP CB 
C A 0015  HIS CD2 3.488 C A 0016  ASP CG 
C A 0015  HIS CB  3.536 E A 0026  ALA CA 
C A 0016  ASP C   2.461 C A 0017  ASP CA 
C A 0016  ASP C   3.045 C A 0017  ASP C  
C A 0016  ASP C   3.709 C A 0017  ASP CB 
C A 0017  ASP C   2.502 C A 0018  CYS CA 
C A 0017  ASP C   3.301 C A 0018  CYS C  
C A 0017  ASP C   3.652 C A 0018  CYS CB 
C A 0018  CYS C   2.520 C A 0019  SER CA 
C A 0018  CYS C   3.189 C A 0019  SER C  
C A 0018  CYS C   3.739 C A 0019  SER CB 
C A 0019  SER C   2.470 C A 0020  GLY CA 
C A 0019  SER C   3.267 C A 0020  GLY C  
C A 0020  GLY C   2.474 C A 0021  ALA CA 
C A 0020  GLY C   3.126 C A 0021  ALA C  
C A 0020  GLY C   3.724 C A 0021  ALA CB 
C A 0021  ALA CA  3.799 C A 0022  TRP CA 
C A 0021  ALA C   2.474 C A 0022  TRP CA 
C A 0021  ALA C   3.633 C A 0022  TRP C  
C A 0021  ALA C   3.379 C A 0022  TRP CB 
C A 0021  ALA C   3.671 C A 0025  GLN CG 
C A 0021  ALA CB  3.780 C A 0025  GLN CA 
C A 0021  ALA CB  3.775 C A 0025  GLN CG 
C A 0022  TRP C   2.488 C A 0023  PHE CA 
C A 0022  TRP C   3.442 C A 0023  PHE C  
C A 0022  TRP C   3.568 C A 0023  PHE CB 
C A 0023  PHE C   2.483 C A 0024  CYS CA 
C A 0023  PHE C   3.295 C A 0024  CYS C  
C A 0023  PHE C   3.697 C A 0024  CYS CB 
C A 0023  PHE CE2 3.711 C A 0036  PRO CB 
C A 0024  CYS CA  3.794 C A 0025  GLN CA 
C A 0024  CYS C   2.509 C A 0025  GLN CA 
C A 0024  CYS C   3.333 C A 0025  GLN C  
C A 0024  CYS C   3.679 C A 0025  GLN CB 
C A 0024  CYS CB  3.462 E A 0034  CYS C  
C A 0024  CYS CA  3.308 E A 0035  GLY C  
C A 0024  CYS CB  3.533 E A 0035  GLY C  
C A 0024  CYS CA  3.800 C A 0036  PRO CA 
C A 0025  GLN C   2.463 E A 0026  ALA CA 
C A 0025  GLN C   3.550 E A 0026  ALA C  
C A 0025  GLN C   3.488 E A 0026  ALA CB 
C A 0025  GLN CB  3.663 C A 0037  TYR CB 
C A 0025  GLN CB  3.756 C A 0037  TYR CG 
E A 0026  ALA C   2.431 E A 0027  CYS CA 
E A 0026  ALA C   3.154 E A 0027  CYS C  
E A 0026  ALA C   3.639 E A 0027  CYS CB 
E A 0026  ALA CB  3.577 C A 0037  TYR CA 
E A 0026  ALA CB  3.704 C A 0037  TYR CD1
E A 0027  CYS C   2.477 C A 0028  TRP CA 
E A 0027  CYS C   3.218 C A 0028  TRP C  
E A 0027  CYS C   3.743 C A 0028  TRP CB 
C A 0028  TRP CA  3.796 C A 0029  ASN CA 
C A 0028  TRP C   2.486 C A 0029  ASN CA 
C A 0028  TRP C   3.159 C A 0029  ASN C  
C A 0028  TRP C   3.738 C A 0029  ASN CB 
C A 0028  TRP CD1 3.518 E A 0035  GLY CA 
C A 0028  TRP CE2 3.759 C A 0036  PRO CD 
C A 0028  TRP CZ2 3.626 C A 0036  PRO CG 
C A 0028  TRP CZ2 3.691 C A 0036  PRO CD 
C A 0029  ASN C   2.471 C A 0030  SER CA 
C A 0029  ASN C   3.169 C A 0030  SER C  
C A 0029  ASN C   3.721 C A 0030  SER CB 
C A 0030  SER C   2.444 C A 0031  ALA CA 
C A 0030  SER C   3.192 C A 0031  ALA C  
C A 0030  SER C   3.678 C A 0031  ALA CB 
C A 0031  ALA C   2.495 C A 0032  ARG CA 
C A 0031  ALA C   3.040 C A 0032  ARG C  
C A 0031  ALA C   3.155 C A 0032  ARG CB 
C A 0031  ALA C   3.776 C A 0032  ARG CG 
C A 0032  ARG C   2.473 C A 0033  THR CA 
C A 0032  ARG C   3.649 C A 0033  THR C  
C A 0032  ARG C   3.368 C A 0033  THR CB 
C A 0032  ARG C   3.388 C A 0033  THR CG2
C A 0033  THR C   2.494 E A 0034  CYS CA 
C A 0033  THR C   3.121 E A 0034  CYS C  
C A 0033  THR C   3.742 E A 0034  CYS CB 
E A 0034  CYS CA  3.791 E A 0035  GLY CA 
E A 0034  CYS C   2.520 E A 0035  GLY CA 
E A 0034  CYS C   3.400 E A 0035  GLY C  
E A 0035  GLY CA  2.992 C A 0036  PRO CD 
E A 0035  GLY C   2.440 C A 0036  PRO CA 
E A 0035  GLY C   3.003 C A 0036  PRO C  
E A 0035  GLY C   3.652 C A 0036  PRO CB 
E A 0035  GLY C   3.672 C A 0036  PRO CG 
E A 0035  GLY C   2.506 C A 0036  PRO CD 
C A 0036  PRO C   2.468 C A 0037  TYR CA 
C A 0036  PRO C   3.270 C A 0037  TYR C  
C A 0036  PRO C   3.672 C A 0037  TYR CB 
C A 0037  TYR C   2.512 C A 0038  VAL CA 
C A 0037  TYR C   3.132 C A 0038  VAL C  
C A 0037  TYR C   3.192 C A 0038  VAL CB 
C A 0037  TYR C   3.471 C A 0038  VAL CG2
C A 0038  VAL C   2.500 C A 0039  GLY CA 
C A 0038  VAL C   3.110 C A 0039  GLY C  

CHARGE_ATTR 2.00 12.00    26
C A 0001  GLU OE1 4.376 C A 0003  HIS ND1
C A 0001  GLU OE1 2.851 C A 0003  HIS NE2
C A 0001  GLU OE2 4.820 C A 0003  HIS ND1
C A 0001  GLU OE2 2.726 C A 0003  HIS NE2
C A 0005  ASP OD1 8.842 C A 0003  HIS ND1
C A 0005  ASP OD1 10.55 C A 0003  HIS NE2
C A 0005  ASP OD2 8.713 C A 0003  HIS ND1
C A 0005  ASP OD2 10.58 C A 0003  HIS NE2
C A 0005  ASP OD2 11.52 C A 0010  LYS NZ 
C A 0005  ASP OD1 10.38 C A 0015  HIS ND1
C A 0005  ASP OD2 11.13 C A 0015  HIS ND1
C A 0016  ASP OD2 11.83 C A 0010  LYS NZ 
C A 0016  ASP OD2 10.27 C A 0013  LYS NZ 
C A 0016  ASP OD1 4.455 C A 0015  HIS ND1
C A 0016  ASP OD1 2.706 C A 0015  HIS NE2
C A 0016  ASP OD2 4.599 C A 0015  HIS ND1
C A 0016  ASP OD2 3.186 C A 0015  HIS NE2
C A 0017  ASP OD1 2.970 C A 0010  LYS NZ 
C A 0017  ASP OD2 3.047 C A 0010  LYS NZ 
C A 0017  ASP OD1 10.02 C A 0013  LYS NZ 
C A 0017  ASP OD2 10.49 C A 0013  LYS NZ 
C A 0017  ASP OD1 9.426 C A 0015  HIS ND1
C A 0017  ASP OD1 10.24 C A 0015  HIS NE2
C A 0017  ASP OD2 10.40 C A 0015  HIS ND1
C A 0017  ASP OD2 10.80 C A 0015  HIS NE2
C A 0017  ASP OD1 11.91 C A 0032  ARG NH1

CHARGE_REPU 2.00 12.00    13
C A 0001  GLU OE1 11.76 C A 0005  ASP OD1
C A 0005  ASP OD1 11.25 C A 0017  ASP OD1
C A 0005  ASP OD2 10.18 C A 0017  ASP OD1
C A 0010  LYS NZ  11.54 C A 0013  LYS NZ 
C A 0010  LYS NZ  11.26 C A 0032  ARG NH1
C A 0013  LYS NZ  11.07 C A 0015  HIS ND1
C A 0013  LYS NZ  11.59 C A 0015  HIS NE2
C A 0013  LYS NZ  8.893 C A 0032  ARG NH1
C A 0013  LYS NZ  9.347 C A 0032  ARG NH2
C A 0016  ASP OD1 9.904 C A 0017  ASP OD1
C A 0016  ASP OD1 9.929 C A 0017  ASP OD2
C A 0016  ASP OD2 9.111 C A 0017  ASP OD1
C A 0016  ASP OD2 9.086 C A 0017  ASP OD2

HB_MM       2.00 3.20    60
C A 0002  GLN N   2.251 C A 0001  GLU O  
C A 0003  HIS N   2.767 C A 0001  GLU O  
C A 0003  HIS N   2.250 C A 0002  GLN O  
C A 0004  ALA N   2.887 C A 0002  GLN O  
C A 0004  ALA N   2.226 C A 0003  HIS O  
C A 0005  ASP N   2.869 C A 0003  HIS O  
C A 0005  ASP N   2.247 C A 0004  ALA O  
C A 0006  PRO N   2.256 C A 0005  ASP O  
C A 0007  ILE N   2.249 C A 0006  PRO O  
C A 0008  CYS N   2.250 C A 0007  ILE O  
C A 0009  ASN N   2.977 C A 0007  ILE O  
C A 0009  ASN N   2.283 C A 0008  CYS O  
C A 0009  ASN N   2.987 E A 0034  CYS O  
C A 0010  LYS N   2.791 C A 0007  ILE O  
C A 0010  LYS N   2.246 C A 0009  ASN O  
C A 0011  PRO N   2.252 C A 0010  LYS O  
C A 0012  CYS N   2.288 C A 0011  PRO O  
C A 0012  CYS N   2.807 C A 0032  ARG O  
C A 0013  LYS N   2.243 C A 0012  CYS O  
C A 0014  THR N   2.271 C A 0013  LYS O  
C A 0015  HIS N   2.229 C A 0014  THR O  
C A 0016  ASP N   2.249 C A 0015  HIS O  
C A 0017  ASP N   2.246 C A 0016  ASP O  
C A 0018  CYS N   3.079 C A 0015  HIS O  
C A 0018  CYS N   2.235 C A 0017  ASP O  
C A 0019  SER N   3.173 C A 0016  ASP O  
C A 0019  SER N   2.981 C A 0017  ASP O  
C A 0019  SER N   2.229 C A 0018  CYS O  
C A 0020  GLY N   2.270 C A 0019  SER O  
C A 0021  ALA N   3.115 C A 0018  CYS O  
C A 0021  ALA N   2.254 C A 0020  GLY O  
C A 0022  TRP N   2.265 C A 0021  ALA O  
C A 0023  PHE N   2.245 C A 0022  TRP O  
C A 0024  CYS N   2.247 C A 0023  PHE O  
C A 0025  GLN N   2.881 C A 0023  PHE O  
C A 0025  GLN N   2.232 C A 0024  CYS O  
E A 0026  ALA N   3.143 C A 0024  CYS O  
E A 0026  ALA N   2.248 C A 0025  GLN O  
E A 0026  ALA N   3.114 E A 0035  GLY O  
E A 0027  CYS N   2.239 E A 0026  ALA O  
C A 0028  TRP N   2.235 E A 0027  CYS O  
C A 0028  TRP N   2.840 C A 0033  THR O  
C A 0029  ASN N   2.265 C A 0028  TRP O  
C A 0030  SER N   2.258 C A 0029  ASN O  
C A 0031  ALA N   2.249 C A 0030  SER O  
C A 0032  ARG N   2.877 C A 0028  TRP O  
C A 0032  ARG N   2.249 C A 0031  ALA O  
C A 0033  THR N   2.254 C A 0032  ARG O  
E A 0034  CYS N   2.835 C A 0010  LYS O  
E A 0034  CYS N   2.267 C A 0033  THR O  
E A 0035  GLY N   2.763 E A 0026  ALA O  
E A 0035  GLY N   2.983 C A 0033  THR O  
E A 0035  GLY N   2.251 E A 0034  CYS O  
C A 0036  PRO N   2.221 E A 0035  GLY O  
C A 0037  TYR N   2.976 C A 0023  PHE O  
C A 0037  TYR N   2.251 C A 0036  PRO O  
C A 0038  VAL N   2.848 C A 0036  PRO O  
C A 0038  VAL N   2.254 C A 0037  TYR O  
C A 0039  GLY N   2.740 C A 0037  TYR O  
C A 0039  GLY N   2.252 C A 0038  VAL O  

HB_MS       2.00 3.20    15
C A 0002  GLN N   2.824 C A 0001  GLU OE1
C A 0002  GLN O   2.980 C A 0003  HIS ND1
C A 0007  ILE N   2.919 C A 0005  ASP OD2
C A 0008  CYS N   3.081 C A 0005  ASP OD2
C A 0011  PRO O   2.938 C A 0010  LYS NZ 
C A 0019  SER O   3.082 C A 0025  GLN NE2
C A 0020  GLY N   2.936 C A 0019  SER OG 
C A 0021  ALA O   2.895 C A 0025  GLN NE2
C A 0023  PHE N   2.922 C A 0005  ASP OD1
C A 0024  CYS N   3.009 C A 0005  ASP OD1
C A 0025  GLN O   2.866 C A 0015  HIS ND1
E A 0027  CYS O   3.072 C A 0013  LYS NZ 
C A 0028  TRP O   2.980 C A 0013  LYS NZ 
C A 0031  ALA N   3.073 C A 0030  SER OG 
C A 0036  PRO O   2.871 C A 0028  TRP NE1

HB_SS       2.00 3.20     2
C A 0013  LYS NZ  3.198 C A 0029  ASN OD1
C A 0015  HIS ND1 2.704 C A 0025  GLN OE1

SS_BOND     1.50 2.80     3
C A 0008  CYS SG  2.040 C A 0024  CYS SG 
C A 0012  CYS SG  2.040 E A 0027  CYS SG 
C A 0018  CYS SG  2.040 E A 0034  CYS SG