Complet list of 1bh4 con fileClick here to see the 3D structure Complete list of 1bh4.con file
COMMENT BEGIN
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COMMENT END
CONTACTS BETWEEN
CHAIN(S) "A"
AND
CHAIN(S) "A"

HYDROPHOBIC 2.00 3.80   121
C A 0001  CYS C   2.432 C A 0002  GLY CA 
C A 0001  CYS C   3.632 C A 0002  GLY C  
C A 0001  CYS CB  3.682 C A 0017  CYS CB 
C A 0001  CYS CA  2.445 C A 0030  PRO C  
C A 0001  CYS C   3.162 C A 0030  PRO C  
C A 0001  CYS CB  3.659 C A 0030  PRO C  
C A 0002  GLY C   2.464 C A 0003  GLU CA 
C A 0002  GLY C   3.758 C A 0003  GLU C  
C A 0002  GLY C   2.996 C A 0003  GLU CB 
C A 0003  GLU C   2.448 C A 0004  SER CA 
C A 0003  GLU C   3.009 C A 0004  SER C  
C A 0003  GLU C   3.715 C A 0004  SER CB 
C A 0004  SER CA  3.780 C A 0005  CYS CA 
C A 0004  SER C   2.455 C A 0005  CYS CA 
C A 0004  SER C   3.559 C A 0005  CYS C  
C A 0004  SER C   3.371 C A 0005  CYS CB 
C A 0004  SER CA  3.530 C A 0022  LYS C  
C A 0004  SER CA  3.792 C A 0023  VAL CA 
C A 0005  CYS C   2.446 C A 0006  VAL CA 
C A 0005  CYS C   3.067 C A 0006  VAL C  
C A 0005  CYS C   3.716 C A 0006  VAL CB 
C A 0006  VAL C   2.440 C A 0007  TRP CA 
C A 0006  VAL C   3.097 C A 0007  TRP C  
C A 0006  VAL C   3.689 C A 0007  TRP CB 
C A 0006  VAL CG2 3.474 C A 0022  LYS CB 
C A 0007  TRP C   2.448 C A 0008  ILE CA 
C A 0007  TRP C   3.592 C A 0008  ILE C  
C A 0007  TRP C   3.414 C A 0008  ILE CB 
C A 0007  TRP C   3.715 C A 0008  ILE CG1
C A 0007  TRP C   3.719 C A 0008  ILE CG2
C A 0008  ILE CA  2.905 C A 0009  PRO CD 
C A 0008  ILE C   2.470 C A 0009  PRO CA 
C A 0008  ILE C   3.169 C A 0009  PRO C  
C A 0008  ILE C   3.651 C A 0009  PRO CB 
C A 0008  ILE C   3.685 C A 0009  PRO CG 
C A 0008  ILE C   2.498 C A 0009  PRO CD 
C A 0008  ILE CB  3.522 C A 0009  PRO CD 
C A 0009  PRO C   2.450 C A 0010  CYS CA 
C A 0009  PRO C   3.242 C A 0010  CYS C  
C A 0009  PRO C   3.668 C A 0010  CYS CB 
C A 0010  CYS C   2.456 C A 0011  ILE CA 
C A 0010  CYS C   3.492 C A 0011  ILE C  
C A 0010  CYS C   3.495 C A 0011  ILE CB 
C A 0010  CYS CB  3.790 C A 0013  ALA CB 
C A 0011  ILE C   2.446 C A 0012  SER CA 
C A 0011  ILE C   3.018 C A 0012  SER C  
C A 0011  ILE C   3.694 C A 0012  SER CB 
C A 0011  ILE C   3.792 C A 0014  ALA CB 
C A 0012  SER C   2.445 C A 0013  ALA CA 
C A 0012  SER C   3.219 C A 0013  ALA C  
C A 0012  SER C   3.661 C A 0013  ALA CB 
C A 0013  ALA C   2.446 C A 0014  ALA CA 
C A 0013  ALA C   3.255 C A 0014  ALA C  
C A 0013  ALA C   3.640 C A 0014  ALA CB 
C A 0013  ALA CA  3.719 C A 0017  CYS CB 
C A 0013  ALA C   3.774 C A 0017  CYS C  
C A 0014  ALA C   2.446 C A 0015  LEU CA 
C A 0014  ALA C   3.107 C A 0015  LEU C  
C A 0014  ALA C   3.730 C A 0015  LEU CB 
C A 0015  LEU C   2.449 C A 0016  GLY CA 
C A 0015  LEU C   2.993 C A 0016  GLY C  
C A 0016  GLY C   2.440 C A 0017  CYS CA 
C A 0016  GLY C   3.092 C A 0017  CYS C  
C A 0016  GLY C   3.685 C A 0017  CYS CB 
C A 0017  CYS C   2.442 C A 0018  SER CA 
C A 0017  CYS C   3.676 C A 0018  SER C  
C A 0017  CYS C   3.243 C A 0018  SER CB 
C A 0017  CYS CB  3.735 C A 0025  TYR C  
C A 0018  SER C   2.433 C A 0019  CYS CA 
C A 0018  SER C   3.170 C A 0019  CYS C  
C A 0018  SER C   3.683 C A 0019  CYS CB 
C A 0019  CYS C   2.447 C A 0020  LYS CA 
C A 0019  CYS C   3.626 C A 0020  LYS C  
C A 0019  CYS C   3.274 C A 0020  LYS CB 
C A 0020  LYS C   2.462 C A 0021  ASN CA 
C A 0020  LYS C   2.954 C A 0021  ASN C  
C A 0020  LYS C   3.113 C A 0021  ASN CB 
C A 0020  LYS CD  3.771 C A 0021  ASN CB 
C A 0021  ASN C   2.479 C A 0022  LYS CA 
C A 0021  ASN C   3.011 C A 0022  LYS C  
C A 0021  ASN C   3.233 C A 0022  LYS CB 
C A 0021  ASN C   3.157 C A 0022  LYS CG 
C A 0022  LYS C   2.446 C A 0023  VAL CA 
C A 0022  LYS C   3.666 C A 0023  VAL C  
C A 0022  LYS C   3.175 C A 0023  VAL CB 
C A 0023  VAL C   2.448 C A 0024  CYS CA 
C A 0023  VAL C   3.320 C A 0024  CYS C  
C A 0023  VAL C   3.615 C A 0024  CYS CB 
C A 0023  VAL CG1 3.530 C A 0025  TYR CB 
C A 0023  VAL CG1 3.294 C A 0025  TYR CG 
C A 0023  VAL CG1 3.372 C A 0025  TYR CD2
C A 0023  VAL CG2 3.735 C A 0025  TYR CD2
C A 0023  VAL CG2 3.660 C A 0025  TYR CE1
C A 0023  VAL CG2 3.380 C A 0025  TYR CE2
C A 0023  VAL CG2 3.343 C A 0025  TYR CZ 
C A 0024  CYS C   2.453 C A 0025  TYR CA 
C A 0024  CYS C   3.362 C A 0025  TYR C  
C A 0024  CYS C   3.597 C A 0025  TYR CB 
C A 0024  CYS C   3.357 C A 0025  TYR CD1
C A 0025  TYR C   2.440 C A 0026  ARG CA 
C A 0025  TYR C   3.236 C A 0026  ARG C  
C A 0025  TYR C   3.631 C A 0026  ARG CB 
C A 0025  TYR CG  3.762 C A 0030  PRO CA 
C A 0025  TYR CD1 3.508 C A 0030  PRO CA 
C A 0025  TYR CE1 3.533 C A 0030  PRO CA 
C A 0026  ARG C   2.469 C A 0027  ASN CA 
C A 0026  ARG C   3.022 C A 0027  ASN C  
C A 0026  ARG C   3.053 C A 0027  ASN CB 
C A 0026  ARG CB  3.517 C A 0029  ILE CG2
C A 0027  ASN C   2.430 C A 0028  GLY CA 
C A 0027  ASN C   3.748 C A 0028  GLY C  
C A 0028  GLY C   2.448 C A 0029  ILE CA 
C A 0028  GLY C   3.472 C A 0029  ILE C  
C A 0028  GLY C   3.521 C A 0029  ILE CB 
C A 0029  ILE CA  2.927 C A 0030  PRO CD 
C A 0029  ILE C   2.449 C A 0030  PRO CA 
C A 0029  ILE C   3.044 C A 0030  PRO C  
C A 0029  ILE C   3.668 C A 0030  PRO CB 
C A 0029  ILE C   3.689 C A 0030  PRO CG 
C A 0029  ILE C   2.501 C A 0030  PRO CD 
C A 0029  ILE CG1 3.548 C A 0030  PRO CD 

CHARGE_ATTR 2.00 12.00     2
C A 0003  GLU OE1 5.665 C A 0022  LYS NZ 
C A 0003  GLU OE2 7.442 C A 0022  LYS NZ 

HB_MM       2.00 3.20    38
C A 0001  CYS N   2.892 C A 0029  ILE O  
C A 0001  CYS N   2.232 C A 0030  PRO O  
C A 0002  GLY N   2.237 C A 0001  CYS O  
C A 0003  GLU N   2.241 C A 0002  GLY O  
C A 0004  SER N   2.228 C A 0003  GLU O  
C A 0005  CYS N   2.244 C A 0004  SER O  
C A 0006  VAL N   2.228 C A 0005  CYS O  
C A 0007  TRP N   2.229 C A 0006  VAL O  
C A 0008  ILE N   2.234 C A 0007  TRP O  
C A 0009  PRO N   2.222 C A 0008  ILE O  
C A 0010  CYS N   2.232 C A 0009  PRO O  
C A 0011  ILE N   2.233 C A 0010  CYS O  
C A 0012  SER N   2.227 C A 0011  ILE O  
C A 0013  ALA N   2.234 C A 0012  SER O  
C A 0014  ALA N   3.066 C A 0011  ILE O  
C A 0014  ALA N   3.171 C A 0012  SER O  
C A 0014  ALA N   2.226 C A 0013  ALA O  
C A 0015  LEU N   2.233 C A 0014  ALA O  
C A 0016  GLY N   2.231 C A 0015  LEU O  
C A 0017  CYS N   2.232 C A 0016  GLY O  
C A 0018  SER N   2.221 C A 0017  CYS O  
C A 0018  SER N   3.043 C A 0025  TYR O  
C A 0019  CYS N   2.230 C A 0018  SER O  
C A 0020  LYS N   2.232 C A 0019  CYS O  
C A 0020  LYS N   2.958 C A 0023  VAL O  
C A 0021  ASN N   2.238 C A 0020  LYS O  
C A 0022  LYS N   2.239 C A 0021  ASN O  
C A 0023  VAL N   2.925 C A 0021  ASN O  
C A 0023  VAL N   2.224 C A 0022  LYS O  
C A 0024  CYS N   2.701 C A 0003  GLU O  
C A 0024  CYS N   2.225 C A 0023  VAL O  
C A 0025  TYR N   2.230 C A 0024  CYS O  
C A 0026  ARG N   2.229 C A 0025  TYR O  
C A 0027  ASN N   3.117 C A 0025  TYR O  
C A 0027  ASN N   2.237 C A 0026  ARG O  
C A 0028  GLY N   2.230 C A 0027  ASN O  
C A 0029  ILE N   2.229 C A 0028  GLY O  
C A 0030  PRO N   2.222 C A 0029  ILE O  

HB_MS       2.00 3.20     4
C A 0004  SER N   3.077 C A 0003  GLU OE1
C A 0016  GLY O   2.776 C A 0026  ARG NH1
C A 0017  CYS O   2.810 C A 0018  SER OG 
C A 0022  LYS O   2.807 C A 0004  SER OG 

HB_SS       2.00 3.20     1
C A 0003  GLU OE1 2.894 C A 0004  SER OG 

AROMATIC    0.00 8.00     1
C A 0022  LYS 7.827 C A 0025  TYR

SS_BOND     1.50 2.80     3
C A 0001  CYS SG  2.018 C A 0017  CYS SG 
C A 0005  CYS SG  2.019 C A 0019  CYS SG 
C A 0010  CYS SG  2.019 C A 0024  CYS SG