Complet list of 1vb8 con fileClick here to see the 3D structure Complete list of 1vb8.con file
COMMENT BEGIN
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COMMENT END
CONTACTS BETWEEN
CHAIN(S) "A"
AND
CHAIN(S) "A"

HYDROPHOBIC 2.00 3.80   130
C A 0001  CYS C   2.436 C A 0002  ALA CA 
C A 0001  CYS C   3.173 C A 0002  ALA C  
C A 0001  CYS C   3.673 C A 0002  ALA CB 
C A 0001  CYS CB  3.642 H A 0013  THR CG2
C A 0001  CYS CB  3.792 C A 0018  CYS CB 
C A 0001  CYS CA  3.797 C A 0030  PRO CA 
C A 0001  CYS CA  2.427 C A 0030  PRO C  
C A 0001  CYS C   3.098 C A 0030  PRO C  
C A 0001  CYS CB  3.688 C A 0030  PRO C  
C A 0002  ALA CA  3.799 C A 0003  GLU CA 
C A 0002  ALA C   2.431 C A 0003  GLU CA 
C A 0002  ALA C   3.650 C A 0003  GLU C  
C A 0002  ALA C   3.217 C A 0003  GLU CB 
C A 0003  GLU CA  3.786 C A 0004  SER CA 
C A 0003  GLU C   2.418 C A 0004  SER CA 
C A 0003  GLU C   3.386 C A 0004  SER C  
C A 0003  GLU C   3.526 C A 0004  SER CB 
C A 0003  GLU CD  3.515 C A 0010  CYS CA 
C A 0003  GLU CD  3.690 C A 0010  CYS CB 
C A 0004  SER CA  3.800 C A 0005  CYS CA 
C A 0004  SER C   2.429 C A 0005  CYS CA 
C A 0004  SER C   3.243 C A 0005  CYS C  
C A 0004  SER C   3.641 C A 0005  CYS CB 
C A 0004  SER CA  3.609 C A 0024  VAL CA 
C A 0005  CYS CA  3.798 C A 0006  VAL CA 
C A 0005  CYS C   2.434 C A 0006  VAL CA 
C A 0005  CYS C   3.014 C A 0006  VAL C  
C A 0005  CYS C   3.742 C A 0006  VAL CB 
C A 0005  CYS CB  3.585 C A 0009  PRO CA 
C A 0006  VAL CA  3.789 C A 0007  TRP CA 
C A 0006  VAL C   2.434 C A 0007  TRP CA 
C A 0006  VAL C   3.472 C A 0007  TRP C  
C A 0006  VAL C   3.481 C A 0007  TRP CB 
C A 0006  VAL C   3.521 C A 0007  TRP CG 
C A 0006  VAL C   3.776 C A 0007  TRP CD2
C A 0006  VAL CA  3.581 C A 0023  LYS CG 
C A 0007  TRP CA  3.794 C A 0008  ILE CA 
C A 0007  TRP C   2.435 C A 0008  ILE CA 
C A 0007  TRP C   3.272 C A 0008  ILE C  
C A 0007  TRP C   3.668 C A 0008  ILE CB 
C A 0007  TRP C   3.764 C A 0008  ILE CG1
C A 0008  ILE CA  2.913 C A 0009  PRO CD 
C A 0008  ILE C   2.469 C A 0009  PRO CA 
C A 0008  ILE C   3.136 C A 0009  PRO C  
C A 0008  ILE C   3.663 C A 0009  PRO CB 
C A 0008  ILE C   3.584 C A 0009  PRO CG 
C A 0008  ILE C   2.499 C A 0009  PRO CD 
C A 0008  ILE CB  3.751 C A 0009  PRO CD 
C A 0008  ILE CG2 3.513 C A 0009  PRO CD 
C A 0009  PRO C   2.431 C A 0010  CYS CA 
C A 0009  PRO C   3.021 C A 0010  CYS C  
C A 0009  PRO C   3.713 C A 0010  CYS CB 
C A 0010  CYS CA  3.790 C A 0011  THR CA 
C A 0010  CYS C   2.425 C A 0011  THR CA 
C A 0010  CYS C   3.557 C A 0011  THR C  
C A 0010  CYS C   3.405 C A 0011  THR CB 
C A 0010  CYS C   3.664 H A 0014  ALA CB 
C A 0011  THR C   2.432 C A 0012  VAL CA 
C A 0011  THR C   3.205 C A 0012  VAL C  
C A 0011  THR C   3.697 C A 0012  VAL CB 
C A 0012  VAL C   2.426 H A 0013  THR CA 
C A 0012  VAL C   3.249 H A 0013  THR C  
C A 0012  VAL C   3.666 H A 0013  THR CB 
H A 0013  THR C   2.428 H A 0014  ALA CA 
H A 0013  THR C   3.010 H A 0014  ALA C  
H A 0013  THR C   3.700 H A 0014  ALA CB 
H A 0014  ALA C   2.436 H A 0015  LEU CA 
H A 0014  ALA C   3.179 H A 0015  LEU C  
H A 0014  ALA C   3.682 H A 0015  LEU CB 
H A 0015  LEU C   2.430 H A 0016  LEU CA 
H A 0015  LEU C   3.291 H A 0016  LEU C  
H A 0015  LEU C   3.621 H A 0016  LEU CB 
H A 0016  LEU CA  3.784 H A 0017  GLY CA 
H A 0016  LEU C   2.412 H A 0017  GLY CA 
H A 0016  LEU C   3.311 H A 0017  GLY C  
H A 0017  GLY CA  3.790 C A 0018  CYS CA 
H A 0017  GLY C   2.428 C A 0018  CYS CA 
H A 0017  GLY C   3.523 C A 0018  CYS C  
H A 0017  GLY C   3.410 C A 0018  CYS CB 
C A 0018  CYS CA  3.786 C A 0019  SER CA 
C A 0018  CYS C   2.420 C A 0019  SER CA 
C A 0018  CYS C   3.437 C A 0019  SER C  
C A 0018  CYS C   3.492 C A 0019  SER CB 
C A 0018  CYS CA  3.748 C A 0027  ASN CB 
C A 0019  SER CA  3.796 C A 0020  CYS CA 
C A 0019  SER C   2.432 C A 0020  CYS CA 
C A 0019  SER C   3.142 C A 0020  CYS C  
C A 0019  SER C   3.687 C A 0020  CYS CB 
C A 0020  CYS CA  3.797 C A 0021  SER CA 
C A 0020  CYS C   2.425 C A 0021  SER CA 
C A 0020  CYS C   3.098 C A 0021  SER C  
C A 0020  CYS C   3.677 C A 0021  SER CB 
C A 0021  SER C   2.438 C A 0022  ASN CA 
C A 0021  SER C   3.698 C A 0022  ASN C  
C A 0021  SER C   3.134 C A 0022  ASN CB 
C A 0022  ASN C   2.465 C A 0023  LYS CA 
C A 0022  ASN C   3.110 C A 0023  LYS C  
C A 0022  ASN C   3.012 C A 0023  LYS CB 
C A 0023  LYS C   2.435 C A 0024  VAL CA 
C A 0023  LYS C   3.639 C A 0024  VAL C  
C A 0023  LYS C   3.250 C A 0024  VAL CB 
C A 0023  LYS C   3.767 C A 0024  VAL CG1
C A 0024  VAL CA  3.797 C A 0025  CYS CA 
C A 0024  VAL C   2.423 C A 0025  CYS CA 
C A 0024  VAL C   3.150 C A 0025  CYS C  
C A 0024  VAL C   3.669 C A 0025  CYS CB 
C A 0025  CYS CA  3.787 C A 0026  TYR CA 
C A 0025  CYS C   2.423 C A 0026  TYR CA 
C A 0025  CYS C   3.636 C A 0026  TYR C  
C A 0025  CYS C   3.219 C A 0026  TYR CB 
C A 0026  TYR CA  3.787 C A 0027  ASN CA 
C A 0026  TYR C   2.424 C A 0027  ASN CA 
C A 0026  TYR C   3.550 C A 0027  ASN C  
C A 0026  TYR C   3.370 C A 0027  ASN CB 
C A 0026  TYR CZ  3.720 C A 0030  PRO CA 
C A 0026  TYR CZ  3.698 C A 0030  PRO CB 
C A 0027  ASN CA  3.780 C A 0028  GLY CA 
C A 0027  ASN C   2.414 C A 0028  GLY CA 
C A 0027  ASN C   3.171 C A 0028  GLY C  
C A 0028  GLY CA  3.784 C A 0029  ILE CA 
C A 0028  GLY C   2.429 C A 0029  ILE CA 
C A 0028  GLY C   3.400 C A 0029  ILE C  
C A 0028  GLY C   3.575 C A 0029  ILE CB 
C A 0029  ILE CA  2.912 C A 0030  PRO CD 
C A 0029  ILE C   2.462 C A 0030  PRO CA 
C A 0029  ILE C   3.178 C A 0030  PRO C  
C A 0029  ILE C   3.650 C A 0030  PRO CB 
C A 0029  ILE C   3.567 C A 0030  PRO CG 
C A 0029  ILE C   2.500 C A 0030  PRO CD 
C A 0029  ILE CB  3.388 C A 0030  PRO CD 

HB_MM       2.00 3.20    41
C A 0001  CYS N   3.024 C A 0029  ILE O  
C A 0001  CYS N   2.245 C A 0030  PRO O  
C A 0002  ALA N   2.247 C A 0001  CYS O  
C A 0003  GLU N   2.805 C A 0001  CYS O  
C A 0003  GLU N   2.246 C A 0002  ALA O  
C A 0004  SER N   2.241 C A 0003  GLU O  
C A 0005  CYS N   2.244 C A 0004  SER O  
C A 0005  CYS N   2.771 C A 0023  LYS O  
C A 0006  VAL N   3.026 C A 0004  SER O  
C A 0006  VAL N   2.255 C A 0005  CYS O  
C A 0007  TRP N   2.250 C A 0006  VAL O  
C A 0008  ILE N   2.249 C A 0007  TRP O  
C A 0009  PRO N   2.251 C A 0008  ILE O  
C A 0010  CYS N   2.251 C A 0009  PRO O  
C A 0011  THR N   2.244 C A 0010  CYS O  
C A 0012  VAL N   2.247 C A 0011  THR O  
H A 0013  THR N   2.241 C A 0012  VAL O  
H A 0014  ALA N   2.247 H A 0013  THR O  
H A 0015  LEU N   2.248 H A 0014  ALA O  
H A 0016  LEU N   3.037 H A 0013  THR O  
H A 0016  LEU N   2.244 H A 0015  LEU O  
H A 0017  GLY N   2.247 H A 0016  LEU O  
C A 0018  CYS N   2.241 H A 0017  GLY O  
C A 0019  SER N   2.244 C A 0018  CYS O  
C A 0020  CYS N   2.251 C A 0019  SER O  
C A 0021  SER N   3.074 C A 0019  SER O  
C A 0021  SER N   2.244 C A 0020  CYS O  
C A 0021  SER N   3.043 C A 0024  VAL O  
C A 0022  ASN N   2.249 C A 0021  SER O  
C A 0023  LYS N   2.260 C A 0022  ASN O  
C A 0024  VAL N   3.024 C A 0022  ASN O  
C A 0024  VAL N   2.241 C A 0023  LYS O  
C A 0025  CYS N   2.748 C A 0003  GLU O  
C A 0025  CYS N   2.248 C A 0024  VAL O  
C A 0026  TYR N   2.981 C A 0019  SER O  
C A 0026  TYR N   2.246 C A 0025  CYS O  
C A 0027  ASN N   2.245 C A 0026  TYR O  
C A 0028  GLY N   2.248 C A 0027  ASN O  
C A 0029  ILE N   2.841 C A 0027  ASN O  
C A 0029  ILE N   2.246 C A 0028  GLY O  
C A 0030  PRO N   2.252 C A 0029  ILE O  

HB_MS       2.00 3.20     9
C A 0005  CYS O   2.810 C A 0023  LYS NZ 
C A 0006  VAL O   2.663 C A 0023  LYS NZ 
C A 0009  PRO O   3.092 C A 0011  THR OG1
C A 0011  THR N   2.640 C A 0003  GLU OE2
C A 0012  VAL N   2.731 C A 0003  GLU OE2
H A 0013  THR N   2.647 C A 0003  GLU OE1
H A 0017  GLY O   2.730 C A 0027  ASN ND2
C A 0023  LYS O   2.713 C A 0004  SER OG 
C A 0026  TYR O   2.969 C A 0021  SER OG 

HB_SS       2.00 3.20     1
C A 0003  GLU OE1 2.609 H A 0013  THR OG1

AROMATIC    0.00 8.00     1
C A 0023  LYS 6.525 C A 0007  TRP

SS_BOND     1.50 2.80     3
C A 0001  CYS SG  2.029 C A 0018  CYS SG 
C A 0005  CYS SG  2.029 C A 0020  CYS SG 
C A 0010  CYS SG  2.028 C A 0025  CYS SG