Complet list of 1sx1 con fileClick here to see the 3D structure Complete list of 1sx1.con file
COMMENT BEGIN
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COMMENT END
CONTACTS BETWEEN
CHAIN(S) "A"
AND
CHAIN(S) "A"

HYDROPHOBIC 2.00 3.80    98
C A 0001  LYS C   2.434 C A 0002  VAL CA 
C A 0001  LYS C   3.519 C A 0002  VAL C  
C A 0001  LYS C   3.482 C A 0002  VAL CB 
C A 0002  VAL CA  3.779 C A 0003  GLY CA 
C A 0002  VAL C   2.409 C A 0003  GLY CA 
C A 0002  VAL C   3.154 C A 0003  GLY C  
C A 0002  VAL CG1 3.645 C A 0016  TYR CG 
C A 0002  VAL CG1 3.009 C A 0016  TYR CD2
C A 0002  VAL CG1 2.981 C A 0016  TYR CE2
C A 0002  VAL CG1 3.590 C A 0016  TYR CZ 
C A 0003  GLY C   2.458 C A 0004  ARG CA 
C A 0003  GLY C   2.905 C A 0004  ARG C  
C A 0003  GLY C   3.724 C A 0004  ARG CB 
C A 0004  ARG C   2.436 C A 0005  ASN CA 
C A 0004  ARG C   3.107 C A 0005  ASN C  
C A 0004  ARG C   3.704 C A 0005  ASN CB 
C A 0004  ARG CA  3.348 C A 0016  TYR CB 
C A 0004  ARG CB  3.780 C A 0016  TYR CB 
C A 0005  ASN C   2.439 C A 0006  ASP CA 
C A 0005  ASN C   3.410 C A 0006  ASP C  
C A 0005  ASN C   3.556 C A 0006  ASP CB 
C A 0006  ASP CA  2.912 C A 0007  PRO CD 
C A 0006  ASP C   2.466 C A 0007  PRO CA 
C A 0006  ASP C   2.964 C A 0007  PRO C  
C A 0006  ASP C   3.656 C A 0007  PRO CB 
C A 0006  ASP C   3.572 C A 0007  PRO CG 
C A 0006  ASP C   2.502 C A 0007  PRO CD 
C A 0006  ASP CB  3.583 C A 0007  PRO CD 
C A 0006  ASP CG  3.796 C A 0007  PRO CG 
C A 0006  ASP CG  3.157 C A 0007  PRO CD 
C A 0007  PRO C   2.452 C A 0008  CYS CA 
C A 0007  PRO C   2.886 C A 0008  CYS C  
C A 0007  PRO C   3.697 C A 0008  CYS CB 
C A 0007  PRO CA  3.791 C A 0015  LYS CA 
C A 0008  CYS CA  2.918 C A 0009  PRO CD 
C A 0008  CYS C   2.469 C A 0009  PRO CA 
C A 0008  CYS C   3.066 C A 0009  PRO C  
C A 0008  CYS C   3.667 C A 0009  PRO CB 
C A 0008  CYS C   3.616 C A 0009  PRO CG 
C A 0008  CYS C   2.507 C A 0009  PRO CD 
C A 0008  CYS CB  3.750 C A 0009  PRO CD 
C A 0008  CYS CB  3.774 C A 0019  CYS CB 
C A 0009  PRO C   2.434 C A 0010  CYS CA 
C A 0009  PRO C   2.980 C A 0010  CYS C  
C A 0009  PRO C   3.718 C A 0010  CYS CB 
C A 0009  PRO CD  3.707 C A 0016  TYR CD1
C A 0009  PRO CD  3.768 C A 0016  TYR CE1
C A 0010  CYS CA  3.792 C A 0011  GLY CA 
C A 0010  CYS C   2.417 C A 0011  GLY CA 
C A 0010  CYS C   3.227 C A 0011  GLY C  
C A 0010  CYS CB  3.701 C A 0020  HIS CE1
C A 0011  GLY CA  3.797 C A 0012  SER CA 
C A 0011  GLY C   2.434 C A 0012  SER CA 
C A 0011  GLY C   3.256 C A 0012  SER C  
C A 0011  GLY C   3.648 C A 0012  SER CB 
C A 0012  SER CA  3.791 C A 0013  GLY CA 
C A 0012  SER C   2.419 C A 0013  GLY CA 
C A 0012  SER C   3.595 C A 0013  GLY C  
C A 0013  GLY CA  3.796 C A 0014  LYS CA 
C A 0013  GLY C   2.435 C A 0014  LYS CA 
C A 0013  GLY C   3.262 C A 0014  LYS C  
C A 0013  GLY C   3.645 C A 0014  LYS CB 
C A 0014  LYS C   2.430 C A 0015  LYS CA 
C A 0014  LYS C   3.114 C A 0015  LYS C  
C A 0014  LYS C   3.698 C A 0015  LYS CB 
C A 0015  LYS C   2.441 C A 0016  TYR CA 
C A 0015  LYS C   2.931 C A 0016  TYR C  
C A 0015  LYS C   3.700 C A 0016  TYR CB 
C A 0015  LYS CG  3.331 C A 0017  LYS CG 
C A 0015  LYS CE  3.746 C A 0018  GLN CB 
C A 0016  TYR C   2.443 C A 0017  LYS CA 
C A 0016  TYR C   2.958 C A 0017  LYS C  
C A 0016  TYR C   3.719 C A 0017  LYS CB 
C A 0016  TYR CA  3.703 C A 0021  GLY CA 
C A 0016  TYR C   3.268 C A 0021  GLY CA 
C A 0016  TYR CB  3.632 C A 0021  GLY CA 
C A 0016  TYR CG  3.088 C A 0021  GLY CA 
C A 0016  TYR CD1 3.508 C A 0021  GLY CA 
C A 0016  TYR CD2 3.057 C A 0021  GLY CA 
C A 0016  TYR CE2 3.461 C A 0021  GLY CA 
C A 0017  LYS C   2.430 C A 0018  GLN CA 
C A 0017  LYS C   3.333 C A 0018  GLN C  
C A 0017  LYS C   3.604 C A 0018  GLN CB 
C A 0018  GLN CA  3.796 C A 0019  CYS CA 
C A 0018  GLN C   2.423 C A 0019  CYS CA 
C A 0018  GLN C   3.413 C A 0019  CYS C  
C A 0018  GLN C   3.520 C A 0019  CYS CB 
C A 0019  CYS C   2.440 C A 0020  HIS CA 
C A 0019  CYS C   3.025 C A 0020  HIS C  
C A 0019  CYS C   3.721 C A 0020  HIS CB 
C A 0020  HIS CA  3.799 C A 0021  GLY CA 
C A 0020  HIS C   2.421 C A 0021  GLY CA 
C A 0020  HIS C   2.921 C A 0021  GLY C  
C A 0021  GLY CA  3.800 C A 0022  ARG CA 
C A 0021  GLY C   2.434 C A 0022  ARG CA 
C A 0021  GLY C   3.679 C A 0022  ARG C  
C A 0021  GLY C   3.181 C A 0022  ARG CB 
C A 0021  GLY C   3.555 C A 0022  ARG CG 

CHARGE_ATTR 2.00 12.00     3
C A 0006  ASP OD1 11.24 C A 0015  LYS NZ 
C A 0006  ASP OD2 11.59 C A 0015  LYS NZ 
C A 0006  ASP OD1 11.16 C A 0020  HIS ND1

CHARGE_REPU 2.00 12.00    14
C A 0001  LYS NZ  7.790 C A 0004  ARG NH1
C A 0001  LYS NZ  6.180 C A 0004  ARG NH2
C A 0004  ARG NH1 8.910 C A 0017  LYS NZ 
C A 0004  ARG NH2 9.708 C A 0017  LYS NZ 
C A 0004  ARG NH1 7.873 C A 0022  ARG NH1
C A 0004  ARG NH1 6.172 C A 0022  ARG NH2
C A 0004  ARG NH2 9.865 C A 0022  ARG NH1
C A 0004  ARG NH2 7.940 C A 0022  ARG NH2
C A 0014  LYS NZ  9.693 C A 0015  LYS NZ 
C A 0014  LYS NZ  6.674 C A 0020  HIS ND1
C A 0014  LYS NZ  7.665 C A 0020  HIS NE2
C A 0015  LYS NZ  6.335 C A 0017  LYS NZ 
C A 0017  LYS NZ  10.74 C A 0022  ARG NH1
C A 0017  LYS NZ  10.38 C A 0022  ARG NH2

HB_MM       2.00 3.20    38
C A 0002  VAL N   2.251 C A 0001  LYS O  
C A 0003  GLY N   2.248 C A 0002  VAL O  
C A 0004  ARG N   2.967 C A 0002  VAL O  
C A 0004  ARG N   2.255 C A 0003  GLY O  
C A 0005  ASN N   2.557 C A 0003  GLY O  
C A 0005  ASN N   2.246 C A 0004  ARG O  
C A 0006  ASP N   2.479 C A 0003  GLY O  
C A 0006  ASP N   2.993 C A 0004  ARG O  
C A 0006  ASP N   2.250 C A 0005  ASN O  
C A 0007  PRO N   2.252 C A 0006  ASP O  
C A 0008  CYS N   3.155 C A 0006  ASP O  
C A 0008  CYS N   2.256 C A 0007  PRO O  
C A 0008  CYS N   2.738 C A 0014  LYS O  
C A 0009  PRO N   2.253 C A 0008  CYS O  
C A 0010  CYS N   3.061 C A 0008  CYS O  
C A 0010  CYS N   2.249 C A 0009  PRO O  
C A 0011  GLY N   3.099 C A 0008  CYS O  
C A 0011  GLY N   3.090 C A 0009  PRO O  
C A 0011  GLY N   2.250 C A 0010  CYS O  
C A 0012  SER N   2.250 C A 0011  GLY O  
C A 0013  GLY N   2.250 C A 0012  SER O  
C A 0014  LYS N   2.251 C A 0013  GLY O  
C A 0015  LYS N   2.250 C A 0014  LYS O  
C A 0016  TYR N   2.249 C A 0015  LYS O  
C A 0017  LYS N   2.251 C A 0016  TYR O  
C A 0018  GLN N   2.814 C A 0015  LYS O  
C A 0018  GLN N   2.810 C A 0016  TYR O  
C A 0018  GLN N   2.246 C A 0017  LYS O  
C A 0019  CYS N   2.632 C A 0015  LYS O  
C A 0019  CYS N   2.827 C A 0016  TYR O  
C A 0019  CYS N   2.245 C A 0018  GLN O  
C A 0020  HIS N   2.248 C A 0019  CYS O  
C A 0021  GLY N   2.696 C A 0016  TYR O  
C A 0021  GLY N   2.248 C A 0020  HIS O  
C A 0022  ARG N   3.054 C A 0016  TYR O  
C A 0022  ARG N   3.165 C A 0019  CYS O  
C A 0022  ARG N   2.767 C A 0020  HIS O  
C A 0022  ARG N   2.251 C A 0021  GLY O  

HB_MS       2.00 3.20     2
C A 0007  PRO N   3.091 C A 0006  ASP OD1
C A 0013  GLY N   2.882 C A 0012  SER OG 

HB_SS       2.00 3.20     1
C A 0015  LYS NZ  3.156 C A 0018  GLN OE1