Complet list of 1x5v con fileClick here to see the 3D structure Complete list of 1x5v.con file
COMMENT BEGIN
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COMMENT END
CONTACTS BETWEEN
CHAIN(S) "A"
AND
CHAIN(S) "A"

HYDROPHOBIC 2.00 3.80   164
C A 0001  ALA CA  3.754 C A 0002  CYS CA 
C A 0001  ALA C   2.431 C A 0002  CYS CA 
C A 0001  ALA C   3.118 C A 0002  CYS C  
C A 0001  ALA C   3.694 C A 0002  CYS CB 
C A 0002  CYS CA  3.752 C A 0003  GLY CA 
C A 0002  CYS C   2.430 C A 0003  GLY CA 
C A 0002  CYS C   2.948 C A 0003  GLY C  
C A 0002  CYS CB  3.556 C A 0018  CYS C  
C A 0002  CYS CB  3.591 C A 0019  CYS CA 
C A 0003  GLY CA  3.783 C A 0004  ILE CA 
C A 0003  GLY C   2.436 C A 0004  ILE CA 
C A 0003  GLY C   3.404 C A 0004  ILE C  
C A 0003  GLY C   3.567 C A 0004  ILE CB 
C A 0003  GLY C   3.735 C A 0004  ILE CG2
C A 0003  GLY CA  3.469 C A 0018  CYS CA 
C A 0003  GLY C   3.759 C A 0018  CYS CA 
C A 0004  ILE CA  3.766 C A 0005  LEU CA 
C A 0004  ILE C   2.484 C A 0005  LEU CA 
C A 0004  ILE C   3.072 C A 0005  LEU C  
C A 0004  ILE C   3.749 C A 0005  LEU CB 
C A 0004  ILE CG1 3.453 C A 0007  ASP CB 
C A 0004  ILE CA  3.406 E A 0022  LEU CD1
C A 0004  ILE C   3.769 E A 0022  LEU CD1
C A 0005  LEU CA  3.785 C A 0006  HIS CA 
C A 0005  LEU C   2.434 C A 0006  HIS CA 
C A 0005  LEU C   3.625 C A 0006  HIS C  
C A 0005  LEU C   3.269 C A 0006  HIS CB 
C A 0005  LEU CG  3.564 C A 0006  HIS CD2
C A 0005  LEU CD2 3.703 C A 0006  HIS CD2
C A 0005  LEU CB  3.468 E A 0031  VAL CB 
C A 0006  HIS CA  3.755 C A 0007  ASP CA 
C A 0006  HIS C   2.429 C A 0007  ASP CA 
C A 0006  HIS C   3.337 C A 0007  ASP C  
C A 0006  HIS C   3.568 C A 0007  ASP CB 
C A 0007  ASP CA  3.772 E A 0008  ASN CA 
C A 0007  ASP C   2.457 E A 0008  ASN CA 
C A 0007  ASP C   2.957 E A 0008  ASN C  
C A 0007  ASP C   3.741 E A 0008  ASN CB 
E A 0008  ASN CA  3.762 E A 0009  CYS CA 
E A 0008  ASN C   2.431 E A 0009  CYS CA 
E A 0008  ASN C   3.669 E A 0009  CYS C  
E A 0008  ASN C   3.131 E A 0009  CYS CB 
E A 0009  CYS CA  3.770 C A 0010  VAL CA 
E A 0009  CYS C   2.449 C A 0010  VAL CA 
E A 0009  CYS C   3.470 C A 0010  VAL C  
E A 0009  CYS C   3.521 C A 0010  VAL CB 
E A 0009  CYS C   3.633 C A 0010  VAL CG1
E A 0009  CYS CB  3.737 E A 0024  CYS CB 
C A 0010  VAL CA  3.767 C A 0011  TYR CA 
C A 0010  VAL C   2.442 C A 0011  TYR CA 
C A 0010  VAL C   3.107 C A 0011  TYR C  
C A 0010  VAL C   3.701 C A 0011  TYR CB 
C A 0010  VAL CG2 3.758 H A 0012  VAL CG2
C A 0010  VAL C   3.554 E A 0024  CYS CB 
C A 0011  TYR CA  3.770 H A 0012  VAL CA 
C A 0011  TYR C   2.446 H A 0012  VAL CA 
C A 0011  TYR C   3.527 H A 0012  VAL C  
C A 0011  TYR C   3.474 H A 0012  VAL CB 
C A 0011  TYR C   3.573 H A 0012  VAL CG1
C A 0011  TYR C   3.478 H A 0013  PRO CD 
C A 0011  TYR CE1 3.718 H A 0013  PRO CG 
C A 0011  TYR CZ  3.759 H A 0013  PRO CG 
C A 0011  TYR CB  3.800 C A 0026  TYR CD2
C A 0011  TYR CB  3.577 C A 0026  TYR CE2
C A 0011  TYR CB  3.757 C A 0026  TYR CZ 
H A 0012  VAL CA  2.848 H A 0013  PRO CD 
H A 0012  VAL C   2.477 H A 0013  PRO CA 
H A 0012  VAL C   3.103 H A 0013  PRO C  
H A 0012  VAL C   3.673 H A 0013  PRO CB 
H A 0012  VAL C   3.602 H A 0013  PRO CG 
H A 0012  VAL C   2.509 H A 0013  PRO CD 
H A 0013  PRO CA  3.775 H A 0014  ALA CA 
H A 0013  PRO C   2.463 H A 0014  ALA CA 
H A 0013  PRO C   2.965 H A 0014  ALA C  
H A 0013  PRO C   3.723 H A 0014  ALA CB 
H A 0014  ALA CA  3.753 H A 0015  GLN CA 
H A 0014  ALA C   2.429 H A 0015  GLN CA 
H A 0014  ALA C   3.531 H A 0015  GLN C  
H A 0014  ALA C   3.358 H A 0015  GLN CB 
H A 0015  GLN CA  3.769 H A 0016  ASN CA 
H A 0015  GLN C   2.462 H A 0016  ASN CA 
H A 0015  GLN C   2.971 H A 0016  ASN C  
H A 0015  GLN C   3.743 H A 0016  ASN CB 
H A 0016  ASN CA  2.844 C A 0017  PRO CD 
H A 0016  ASN C   2.474 C A 0017  PRO CA 
H A 0016  ASN C   3.282 C A 0017  PRO C  
H A 0016  ASN C   3.590 C A 0017  PRO CB 
H A 0016  ASN C   3.661 C A 0017  PRO CG 
H A 0016  ASN C   2.513 C A 0017  PRO CD 
H A 0016  ASN CG  3.780 C A 0018  CYS CB 
C A 0017  PRO CA  3.750 C A 0018  CYS CA 
C A 0017  PRO C   2.434 C A 0018  CYS CA 
C A 0017  PRO C   3.217 C A 0018  CYS C  
C A 0017  PRO C   3.647 C A 0018  CYS CB 
C A 0018  CYS CA  3.737 C A 0019  CYS CA 
C A 0018  CYS C   2.431 C A 0019  CYS CA 
C A 0018  CYS C   3.035 C A 0019  CYS C  
C A 0018  CYS C   3.692 C A 0019  CYS CB 
C A 0019  CYS CA  3.779 C A 0020  ARG CA 
C A 0019  CYS C   2.452 C A 0020  ARG CA 
C A 0019  CYS C   2.955 C A 0020  ARG C  
C A 0019  CYS C   3.737 C A 0020  ARG CB 
C A 0020  ARG CA  3.738 C A 0021  GLY CA 
C A 0020  ARG C   2.427 C A 0021  GLY CA 
C A 0020  ARG C   3.558 C A 0021  GLY C  
C A 0021  GLY CA  3.788 E A 0022  LEU CA 
C A 0021  GLY C   2.445 E A 0022  LEU CA 
C A 0021  GLY C   3.387 E A 0022  LEU C  
C A 0021  GLY C   3.548 E A 0022  LEU CB 
C A 0021  GLY C   3.670 E A 0022  LEU CG 
C A 0021  GLY C   3.664 E A 0022  LEU CD2
E A 0022  LEU CA  3.774 E A 0023  GLN CA 
E A 0022  LEU C   2.436 E A 0023  GLN CA 
E A 0022  LEU C   3.570 E A 0023  GLN C  
E A 0022  LEU C   3.348 E A 0023  GLN CB 
E A 0022  LEU CD2 3.489 E A 0031  VAL CA 
E A 0022  LEU CD2 3.751 E A 0031  VAL CB 
E A 0022  LEU CD2 3.601 E A 0031  VAL CG2
E A 0023  GLN CA  3.759 E A 0024  CYS CA 
E A 0023  GLN C   2.445 E A 0024  CYS CA 
E A 0023  GLN C   3.072 E A 0024  CYS C  
E A 0023  GLN C   3.722 E A 0024  CYS CB 
E A 0024  CYS CA  3.734 E A 0025  ARG CA 
E A 0024  CYS C   2.437 E A 0025  ARG CA 
E A 0024  CYS C   3.334 E A 0025  ARG C  
E A 0024  CYS C   3.559 E A 0025  ARG CB 
E A 0024  CYS CA  3.660 E A 0029  CYS CA 
E A 0025  ARG CA  3.784 C A 0026  TYR CA 
E A 0025  ARG C   2.454 C A 0026  TYR CA 
E A 0025  ARG C   2.964 C A 0026  TYR C  
E A 0025  ARG C   3.739 C A 0026  TYR CB 
E A 0025  ARG CB  3.502 E A 0030  LEU CG 
E A 0025  ARG CB  3.438 E A 0030  LEU CD1
C A 0026  TYR CA  3.736 E A 0027  GLY CA 
C A 0026  TYR C   2.422 E A 0027  GLY CA 
C A 0026  TYR C   3.593 E A 0027  GLY C  
E A 0027  GLY CA  3.793 E A 0028  LYS CA 
E A 0027  GLY C   2.437 E A 0028  LYS CA 
E A 0027  GLY C   3.646 E A 0028  LYS C  
E A 0027  GLY C   3.206 E A 0028  LYS CB 
E A 0028  LYS CA  3.747 E A 0029  CYS CA 
E A 0028  LYS C   2.431 E A 0029  CYS CA 
E A 0028  LYS C   3.117 E A 0029  CYS C  
E A 0028  LYS C   3.679 E A 0029  CYS CB 
E A 0028  LYS CE  3.466 E A 0030  LEU CD2
E A 0029  CYS CA  3.756 E A 0030  LEU CA 
E A 0029  CYS C   2.432 E A 0030  LEU CA 
E A 0029  CYS C   3.174 E A 0030  LEU C  
E A 0029  CYS C   3.681 E A 0030  LEU CB 
E A 0030  LEU CA  3.734 E A 0031  VAL CA 
E A 0030  LEU C   2.425 E A 0031  VAL CA 
E A 0030  LEU C   3.061 E A 0031  VAL C  
E A 0030  LEU C   3.719 E A 0031  VAL CB 
E A 0031  VAL CA  3.756 C A 0032  GLN CA 
E A 0031  VAL C   2.434 C A 0032  GLN CA 
E A 0031  VAL C   3.098 C A 0032  GLN C  
E A 0031  VAL C   3.700 C A 0032  GLN CB 
E A 0031  VAL CG2 3.658 C A 0033  VAL CG1
E A 0031  VAL CG2 3.646 C A 0033  VAL CG2
C A 0032  GLN CA  3.755 C A 0033  VAL CA 
C A 0032  GLN C   2.438 C A 0033  VAL CA 
C A 0032  GLN C   3.472 C A 0033  VAL C  
C A 0032  GLN C   3.504 C A 0033  VAL CB 
C A 0032  GLN C   3.576 C A 0033  VAL CG1

CHARGE_ATTR 2.00 12.00     6
C A 0007  ASP OD1 6.214 C A 0006  HIS ND1
C A 0007  ASP OD1 7.575 C A 0006  HIS NE2
C A 0007  ASP OD2 7.791 C A 0006  HIS ND1
C A 0007  ASP OD2 9.131 C A 0006  HIS NE2
C A 0007  ASP OD1 11.71 E A 0028  LYS NZ 
C A 0007  ASP OD2 11.94 E A 0028  LYS NZ 

CHARGE_REPU 2.00 12.00     4
C A 0006  HIS ND1 8.317 E A 0028  LYS NZ 
C A 0006  HIS NE2 9.276 E A 0028  LYS NZ 
E A 0025  ARG NH1 11.30 E A 0028  LYS NZ 
E A 0025  ARG NH2 10.95 E A 0028  LYS NZ 

HB_MM       2.00 3.20    54
C A 0002  CYS N   2.225 C A 0001  ALA O  
C A 0003  GLY N   2.231 C A 0002  CYS O  
C A 0003  GLY N   2.673 C A 0017  PRO O  
C A 0004  ILE N   3.185 C A 0002  CYS O  
C A 0004  ILE N   2.260 C A 0003  GLY O  
C A 0005  LEU N   2.243 C A 0004  ILE O  
C A 0006  HIS N   2.622 C A 0004  ILE O  
C A 0006  HIS N   2.218 C A 0005  LEU O  
C A 0007  ASP N   2.752 C A 0004  ILE O  
C A 0007  ASP N   2.220 C A 0006  HIS O  
E A 0008  ASN N   2.236 C A 0007  ASP O  
E A 0009  CYS N   3.184 C A 0007  ASP O  
E A 0009  CYS N   2.220 E A 0008  ASN O  
E A 0009  CYS N   2.972 E A 0027  GLY O  
C A 0010  VAL N   2.227 E A 0009  CYS O  
C A 0011  TYR N   2.223 C A 0010  VAL O  
H A 0012  VAL N   2.590 C A 0010  VAL O  
H A 0012  VAL N   2.223 C A 0011  TYR O  
H A 0013  PRO N   2.224 H A 0012  VAL O  
H A 0014  ALA N   2.238 H A 0013  PRO O  
H A 0015  GLN N   2.880 H A 0013  PRO O  
H A 0015  GLN N   2.224 H A 0014  ALA O  
H A 0016  ASN N   2.882 H A 0013  PRO O  
H A 0016  ASN N   2.242 H A 0015  GLN O  
C A 0017  PRO N   3.010 H A 0015  GLN O  
C A 0017  PRO N   2.227 H A 0016  ASN O  
C A 0018  CYS N   2.219 C A 0017  PRO O  
C A 0019  CYS N   2.986 C A 0003  GLY O  
C A 0019  CYS N   2.228 C A 0018  CYS O  
C A 0020  ARG N   2.232 C A 0019  CYS O  
C A 0021  GLY N   2.782 C A 0019  CYS O  
C A 0021  GLY N   2.231 C A 0020  ARG O  
E A 0022  LEU N   2.705 C A 0019  CYS O  
E A 0022  LEU N   2.259 C A 0021  GLY O  
E A 0023  GLN N   2.223 E A 0022  LEU O  
E A 0023  GLN N   2.731 E A 0030  LEU O  
E A 0024  CYS N   2.226 E A 0023  GLN O  
E A 0025  ARG N   2.220 E A 0024  CYS O  
E A 0025  ARG N   2.644 E A 0028  LYS O  
C A 0026  TYR N   2.231 E A 0025  ARG O  
E A 0027  GLY N   2.691 E A 0009  CYS O  
E A 0027  GLY N   2.493 E A 0025  ARG O  
E A 0027  GLY N   2.229 C A 0026  TYR O  
E A 0028  LYS N   2.729 E A 0025  ARG O  
E A 0028  LYS N   2.250 E A 0027  GLY O  
E A 0029  CYS N   2.694 C A 0007  ASP O  
E A 0029  CYS N   2.222 E A 0028  LYS O  
E A 0030  LEU N   2.589 E A 0023  GLN O  
E A 0030  LEU N   2.220 E A 0029  CYS O  
E A 0031  VAL N   2.227 E A 0030  LEU O  
C A 0032  GLN N   3.067 E A 0030  LEU O  
C A 0032  GLN N   2.225 E A 0031  VAL O  
C A 0033  VAL N   2.500 E A 0031  VAL O  
C A 0033  VAL N   2.226 C A 0032  GLN O  

HB_MS       2.00 3.20     1
C A 0018  CYS N   2.813 H A 0016  ASN OD1

AROMATIC    0.00 8.00     1
E A 0025  ARG 5.536 C A 0026  TYR

SS_BOND     1.50 2.80     3
C A 0002  CYS SG  2.032 C A 0019  CYS SG 
E A 0009  CYS SG  2.030 E A 0024  CYS SG 
C A 0018  CYS SG  2.029 E A 0029  CYS SG