Complet list of 1wo6 con fileClick here to see the 3D structure Complete list of 1wo6.con file
COMMENT BEGIN
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COMMENT END
CONTACTS BETWEEN
CHAIN(S) "A"
AND
CHAIN(S) "A"

HYDROPHOBIC 2.00 3.80    94
C A 0001  ALA C   2.433 C A 0002  VAL CA 
C A 0001  ALA C   3.234 C A 0002  VAL C  
C A 0001  ALA C   3.682 C A 0002  VAL CB 
C A 0001  ALA CA  3.286 C A 0016  VAL CG2
C A 0001  ALA C   3.143 C A 0016  VAL CG2
C A 0002  VAL C   2.435 C A 0003  TYR CA 
C A 0002  VAL C   2.980 C A 0003  TYR C  
C A 0002  VAL C   3.717 C A 0003  TYR CB 
C A 0002  VAL C   3.790 C A 0005  CYS CB 
C A 0002  VAL CA  3.613 C A 0016  VAL CG2
C A 0002  VAL CB  3.598 C A 0016  VAL CG2
C A 0003  TYR C   2.434 C A 0004  TYR CA 
C A 0003  TYR C   3.321 C A 0004  TYR C  
C A 0003  TYR C   3.613 C A 0004  TYR CB 
C A 0004  TYR C   2.436 C A 0005  CYS CA 
C A 0004  TYR C   3.270 C A 0005  CYS C  
C A 0004  TYR C   3.639 C A 0005  CYS CB 
C A 0005  CYS C   2.435 C A 0006  ILE CA 
C A 0005  CYS C   3.321 C A 0006  ILE C  
C A 0005  CYS C   3.640 C A 0006  ILE CB 
C A 0005  CYS CB  3.391 C A 0019  HIS CE1
C A 0006  ILE C   2.434 C A 0007  LEU CA 
C A 0006  ILE C   3.500 C A 0007  LEU C  
C A 0006  ILE C   3.470 C A 0007  LEU CB 
C A 0007  LEU CA  2.919 C A 0008  PRO CD 
C A 0007  LEU C   2.467 C A 0008  PRO CA 
C A 0007  LEU C   3.165 C A 0008  PRO C  
C A 0007  LEU C   3.642 C A 0008  PRO CB 
C A 0007  LEU C   3.653 C A 0008  PRO CG 
C A 0007  LEU C   2.510 C A 0008  PRO CD 
C A 0007  LEU CB  3.781 C A 0008  PRO CD 
C A 0007  LEU CD2 3.741 C A 0008  PRO CD 
C A 0007  LEU CB  3.634 C A 0010  CYS CB 
C A 0008  PRO C   2.435 C A 0009  LYS CA 
C A 0008  PRO C   3.463 C A 0009  LYS C  
C A 0008  PRO C   3.505 C A 0009  LYS CB 
C A 0008  PRO C   3.793 C A 0009  LYS CG 
C A 0009  LYS C   2.434 C A 0010  CYS CA 
C A 0009  LYS C   3.293 C A 0010  CYS C  
C A 0009  LYS C   3.627 C A 0010  CYS CB 
C A 0010  CYS C   2.433 C A 0011  ALA CA 
C A 0010  CYS C   3.335 C A 0011  ALA C  
C A 0010  CYS C   3.593 C A 0011  ALA CB 
C A 0011  ALA C   2.434 C A 0012  ALA CA 
C A 0011  ALA C   3.128 C A 0012  ALA C  
C A 0011  ALA C   3.686 C A 0012  ALA CB 
C A 0011  ALA CB  3.764 C A 0014  ALA CA 
C A 0012  ALA C   2.433 C A 0013  ALA CA 
C A 0012  ALA C   3.391 C A 0013  ALA C  
C A 0012  ALA C   3.555 C A 0013  ALA CB 
C A 0013  ALA C   2.435 C A 0014  ALA CA 
C A 0013  ALA C   2.997 C A 0014  ALA C  
C A 0013  ALA C   3.013 C A 0014  ALA CB 
C A 0014  ALA C   2.433 C A 0015  ASN CA 
C A 0014  ALA C   3.173 C A 0015  ASN C  
C A 0014  ALA C   3.678 C A 0015  ASN CB 
C A 0015  ASN CA  3.787 C A 0016  VAL CA 
C A 0015  ASN C   2.431 C A 0016  VAL CA 
C A 0015  ASN C   3.347 C A 0016  VAL C  
C A 0015  ASN C   3.601 C A 0016  VAL CB 
C A 0015  ASN CG  3.784 C A 0018  ALA CB 
C A 0016  VAL C   2.438 C A 0017  ALA CA 
C A 0016  VAL C   2.934 C A 0017  ALA C  
C A 0016  VAL C   3.704 C A 0017  ALA CB 
C A 0016  VAL CG2 3.300 C A 0019  HIS CD2
C A 0017  ALA C   2.432 C A 0018  ALA CA 
C A 0017  ALA C   3.337 C A 0018  ALA C  
C A 0017  ALA C   3.592 C A 0018  ALA CB 
C A 0018  ALA C   2.433 C A 0019  HIS CA 
C A 0018  ALA C   3.180 C A 0019  HIS C  
C A 0018  ALA C   3.686 C A 0019  HIS CB 
C A 0019  HIS C   2.439 C A 0020  THR CA 
C A 0019  HIS C   2.917 C A 0020  THR C  
C A 0019  HIS C   3.709 C A 0020  THR CB 
C A 0019  HIS CD2 3.525 C A 0020  THR CA 
C A 0019  HIS CA  3.507 C A 0022  HIS CE1
C A 0019  HIS C   3.498 C A 0022  HIS CD2
C A 0019  HIS CE1 2.919 C A 0023  CYS CB 
C A 0020  THR C   2.438 C A 0021  THR CA 
C A 0020  THR C   2.934 C A 0021  THR C  
C A 0020  THR C   3.711 C A 0021  THR CB 
C A 0021  THR C   2.438 C A 0022  HIS CA 
C A 0021  THR C   3.365 C A 0022  HIS C  
C A 0021  THR C   3.599 C A 0022  HIS CB 
C A 0022  HIS CA  3.782 C A 0023  CYS CA 
C A 0022  HIS C   2.424 C A 0023  CYS CA 
C A 0022  HIS C   3.216 C A 0023  CYS C  
C A 0022  HIS C   3.628 C A 0023  CYS CB 
C A 0023  CYS C   2.434 C A 0024  PHE CA 
C A 0023  CYS C   3.327 C A 0024  PHE C  
C A 0023  CYS C   3.609 C A 0024  PHE CB 
C A 0024  PHE C   2.434 C A 0025  LYS CA 
C A 0024  PHE C   2.998 C A 0025  LYS C  
C A 0024  PHE C   3.003 C A 0025  LYS CB 

CHARGE_REPU 2.00 12.00     6
C A 0019  HIS ND1 5.841 C A 0022  HIS ND1
C A 0019  HIS ND1 3.826 C A 0022  HIS NE2
C A 0019  HIS NE2 7.476 C A 0022  HIS ND1
C A 0019  HIS NE2 5.682 C A 0022  HIS NE2
C A 0019  HIS ND1 11.29 C A 0025  LYS NZ 
C A 0019  HIS NE2 9.305 C A 0025  LYS NZ 

HB_MM       2.00 3.20    34
C A 0002  VAL N   2.250 C A 0001  ALA O  
C A 0003  TYR N   2.250 C A 0002  VAL O  
C A 0004  TYR N   3.108 C A 0002  VAL O  
C A 0004  TYR N   2.251 C A 0003  TYR O  
C A 0005  CYS N   2.820 C A 0002  VAL O  
C A 0005  CYS N   2.250 C A 0004  TYR O  
C A 0006  ILE N   2.249 C A 0005  CYS O  
C A 0007  LEU N   2.249 C A 0006  ILE O  
C A 0008  PRO N   2.252 C A 0007  LEU O  
C A 0009  LYS N   2.250 C A 0008  PRO O  
C A 0010  CYS N   2.249 C A 0009  LYS O  
C A 0011  ALA N   2.250 C A 0010  CYS O  
C A 0012  ALA N   2.250 C A 0011  ALA O  
C A 0013  ALA N   2.250 C A 0012  ALA O  
C A 0014  ALA N   2.250 C A 0013  ALA O  
C A 0015  ASN N   3.097 C A 0013  ALA O  
C A 0015  ASN N   2.250 C A 0014  ALA O  
C A 0016  VAL N   2.249 C A 0015  ASN O  
C A 0017  ALA N   2.251 C A 0016  VAL O  
C A 0018  ALA N   2.824 C A 0016  VAL O  
C A 0018  ALA N   2.251 C A 0017  ALA O  
C A 0019  HIS N   2.709 C A 0016  VAL O  
C A 0019  HIS N   2.250 C A 0018  ALA O  
C A 0020  THR N   2.740 C A 0016  VAL O  
C A 0020  THR N   2.243 C A 0019  HIS O  
C A 0021  THR N   2.696 C A 0019  HIS O  
C A 0021  THR N   2.249 C A 0020  THR O  
C A 0022  HIS N   2.826 C A 0019  HIS O  
C A 0022  HIS N   3.052 C A 0020  THR O  
C A 0022  HIS N   2.251 C A 0021  THR O  
C A 0023  CYS N   3.094 C A 0019  HIS O  
C A 0023  CYS N   2.246 C A 0022  HIS O  
C A 0024  PHE N   2.250 C A 0023  CYS O  
C A 0025  LYS N   2.250 C A 0024  PHE O  

HB_MS       2.00 3.20     2
C A 0001  ALA O   2.654 C A 0019  HIS NE2
C A 0019  HIS O   2.741 C A 0022  HIS NE2

AROMATIC    0.00 8.00     1
C A 0019  HIS 5.458 C A 0022  HIS