Complet list of 1y29 con fileClick here to see the 3D structure Complete list of 1y29.con file
COMMENT BEGIN
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COMMENT END
CONTACTS BETWEEN
CHAIN(S) "A"
AND
CHAIN(S) "A"

HYDROPHOBIC 2.00 3.80   107
C A 0001  LYS C   2.440 C A 0002  CYS CA 
C A 0001  LYS C   3.090 C A 0002  CYS C  
C A 0001  LYS C   3.651 C A 0002  CYS CB 
C A 0002  CYS C   2.442 C A 0003  LEU CA 
C A 0002  CYS C   3.093 C A 0003  LEU C  
C A 0002  CYS C   3.656 C A 0003  LEU CB 
C A 0003  LEU CA  2.877 C A 0004  PRO CD 
C A 0003  LEU C   2.438 C A 0004  PRO CA 
C A 0003  LEU C   3.089 C A 0004  PRO C  
C A 0003  LEU C   3.624 C A 0004  PRO CB 
C A 0003  LEU C   3.622 C A 0004  PRO CG 
C A 0003  LEU C   2.493 C A 0004  PRO CD 
C A 0003  LEU CB  3.719 C A 0004  PRO CD 
C A 0003  LEU CG  3.216 C A 0016  ILE CG1
C A 0003  LEU CD1 3.092 C A 0016  ILE CG1
C A 0003  LEU CD1 3.554 C A 0016  ILE CG2
C A 0003  LEU CD2 3.411 C A 0016  ILE CG1
C A 0004  PRO CA  2.878 C A 0005  PRO CD 
C A 0004  PRO C   2.433 C A 0005  PRO CA 
C A 0004  PRO C   3.077 C A 0005  PRO C  
C A 0004  PRO C   3.621 C A 0005  PRO CB 
C A 0004  PRO C   3.625 C A 0005  PRO CG 
C A 0004  PRO C   2.494 C A 0005  PRO CD 
C A 0004  PRO CB  3.339 C A 0005  PRO CD 
C A 0004  PRO CG  3.516 C A 0007  LYS CG 
C A 0004  PRO CD  3.497 C A 0007  LYS CG 
C A 0004  PRO CD  3.671 C A 0007  LYS CE 
C A 0005  PRO C   2.437 C A 0006  GLY CA 
C A 0005  PRO C   3.398 C A 0006  GLY C  
C A 0006  GLY C   2.440 C A 0007  LYS CA 
C A 0006  GLY C   3.215 C A 0007  LYS C  
C A 0006  GLY C   3.620 C A 0007  LYS CB 
C A 0007  LYS CA  2.880 C A 0008  PRO CD 
C A 0007  LYS C   2.435 C A 0008  PRO CA 
C A 0007  LYS C   3.111 C A 0008  PRO C  
C A 0007  LYS C   3.618 C A 0008  PRO CB 
C A 0007  LYS C   3.635 C A 0008  PRO CG 
C A 0007  LYS C   2.493 C A 0008  PRO CD 
C A 0008  PRO C   2.435 C A 0009  CYS CA 
C A 0008  PRO C   3.217 C A 0009  CYS C  
C A 0008  PRO C   3.616 C A 0009  CYS CB 
C A 0008  PRO CA  3.783 C A 0025  ASN C  
C A 0009  CYS C   2.431 C A 0010  TYR CA 
C A 0009  CYS C   3.330 C A 0010  TYR C  
C A 0009  CYS C   3.544 C A 0010  TYR CB 
C A 0010  TYR C   2.442 C A 0011  GLY CA 
C A 0010  TYR C   2.960 C A 0011  GLY C  
C A 0011  GLY C   2.435 C A 0012  ALA CA 
C A 0011  GLY C   3.507 C A 0012  ALA C  
C A 0011  GLY C   3.410 C A 0012  ALA CB 
C A 0012  ALA C   2.439 C A 0013  THR CA 
C A 0012  ALA C   3.387 C A 0013  THR C  
C A 0012  ALA C   3.523 C A 0013  THR CB 
C A 0013  THR C   2.436 C A 0014  GLN CA 
C A 0013  THR C   3.713 C A 0014  GLN C  
C A 0013  THR C   3.005 C A 0014  GLN CB 
C A 0013  THR C   3.478 C A 0014  GLN CG 
C A 0014  GLN C   2.437 C A 0015  LYS CA 
C A 0014  GLN C   3.272 C A 0015  LYS C  
C A 0014  GLN C   3.592 C A 0015  LYS CB 
C A 0014  GLN CD  3.756 C A 0016  ILE CG2
C A 0015  LYS C   2.436 C A 0016  ILE CA 
C A 0015  LYS C   3.468 C A 0016  ILE C  
C A 0015  LYS C   3.450 C A 0016  ILE CB 
C A 0016  ILE CA  2.867 C A 0017  PRO CD 
C A 0016  ILE C   2.433 C A 0017  PRO CA 
C A 0016  ILE C   3.132 C A 0017  PRO C  
C A 0016  ILE C   3.610 C A 0017  PRO CB 
C A 0016  ILE C   3.634 C A 0017  PRO CG 
C A 0016  ILE C   2.491 C A 0017  PRO CD 
C A 0016  ILE CD1 3.745 C A 0017  PRO CD 
C A 0017  PRO C   2.430 C A 0018  CYS CA 
C A 0017  PRO C   3.158 C A 0018  CYS C  
C A 0017  PRO C   3.621 C A 0018  CYS CB 
C A 0018  CYS C   2.435 C A 0019  CYS CA 
C A 0018  CYS C   2.967 C A 0019  CYS C  
C A 0018  CYS C   3.656 C A 0019  CYS CB 
C A 0018  CYS CB  3.764 C A 0027  CYS CB 
C A 0019  CYS C   2.436 C A 0020  GLY CA 
C A 0019  CYS C   3.442 C A 0020  GLY C  
C A 0020  GLY C   2.439 C A 0021  VAL CA 
C A 0020  GLY C   3.560 C A 0021  VAL C  
C A 0020  GLY C   3.366 C A 0021  VAL CB 
C A 0020  GLY C   3.162 C A 0021  VAL CG2
C A 0020  GLY CA  3.364 C A 0028  THR C  
C A 0021  VAL C   2.431 C A 0022  CYS CA 
C A 0021  VAL C   3.172 C A 0022  CYS C  
C A 0021  VAL C   3.625 C A 0022  CYS CB 
C A 0022  CYS C   2.433 C A 0023  SER CA 
C A 0022  CYS C   3.481 C A 0023  SER C  
C A 0022  CYS C   3.418 C A 0023  SER CB 
C A 0023  SER C   2.447 C A 0024  HIS CA 
C A 0023  SER C   2.953 C A 0024  HIS C  
C A 0023  SER C   2.955 C A 0024  HIS CB 
C A 0024  HIS C   2.456 C A 0025  ASN CA 
C A 0024  HIS C   3.061 C A 0025  ASN C  
C A 0024  HIS C   2.891 C A 0025  ASN CB 
C A 0025  ASN C   2.451 C A 0026  LYS CA 
C A 0025  ASN C   3.655 C A 0026  LYS C  
C A 0025  ASN C   3.224 C A 0026  LYS CB 
C A 0025  ASN C   3.056 C A 0026  LYS CG 
C A 0026  LYS C   2.433 C A 0027  CYS CA 
C A 0026  LYS C   3.601 C A 0027  CYS C  
C A 0026  LYS C   3.274 C A 0027  CYS CB 
C A 0027  CYS C   2.433 C A 0028  THR CA 
C A 0027  CYS C   3.259 C A 0028  THR C  
C A 0027  CYS C   3.591 C A 0028  THR CB 

CHARGE_REPU 2.00 12.00     2
C A 0024  HIS ND1 5.722 C A 0026  LYS NZ 
C A 0024  HIS NE2 7.461 C A 0026  LYS NZ 

HB_MM       2.00 3.20    34
C A 0002  CYS N   2.206 C A 0001  LYS O  
C A 0003  LEU N   2.208 C A 0002  CYS O  
C A 0004  PRO N   2.233 C A 0003  LEU O  
C A 0005  PRO N   2.231 C A 0004  PRO O  
C A 0006  GLY N   2.206 C A 0005  PRO O  
C A 0006  GLY N   2.764 C A 0027  CYS O  
C A 0007  LYS N   2.206 C A 0006  GLY O  
C A 0008  PRO N   2.231 C A 0007  LYS O  
C A 0009  CYS N   3.138 C A 0007  LYS O  
C A 0009  CYS N   2.208 C A 0008  PRO O  
C A 0010  TYR N   2.205 C A 0009  CYS O  
C A 0011  GLY N   2.210 C A 0010  TYR O  
C A 0012  ALA N   3.156 C A 0010  TYR O  
C A 0012  ALA N   2.206 C A 0011  GLY O  
C A 0013  THR N   2.207 C A 0012  ALA O  
C A 0014  GLN N   2.206 C A 0013  THR O  
C A 0015  LYS N   2.205 C A 0014  GLN O  
C A 0016  ILE N   2.207 C A 0015  LYS O  
C A 0017  PRO N   2.230 C A 0016  ILE O  
C A 0018  CYS N   2.203 C A 0017  PRO O  
C A 0019  CYS N   2.206 C A 0018  CYS O  
C A 0020  GLY N   3.113 C A 0018  CYS O  
C A 0020  GLY N   2.206 C A 0019  CYS O  
C A 0020  GLY N   3.036 C A 0028  THR O  
C A 0021  VAL N   2.204 C A 0020  GLY O  
C A 0022  CYS N   2.203 C A 0021  VAL O  
C A 0023  SER N   2.207 C A 0022  CYS O  
C A 0023  SER N   3.011 C A 0026  LYS O  
C A 0024  HIS N   2.208 C A 0023  SER O  
C A 0025  ASN N   2.213 C A 0024  HIS O  
C A 0026  LYS N   2.210 C A 0025  ASN O  
C A 0027  CYS N   2.823 C A 0007  LYS O  
C A 0027  CYS N   2.199 C A 0026  LYS O  
C A 0028  THR N   2.200 C A 0027  CYS O  

HB_MS       2.00 3.20     3
C A 0010  TYR N   3.033 C A 0014  GLN OE1
C A 0016  ILE O   3.079 C A 0014  GLN NE2
C A 0021  VAL N   3.054 C A 0028  THR OG1

SS_BOND     1.50 2.80     3
C A 0002  CYS SG  2.022 C A 0019  CYS SG 
C A 0009  CYS SG  2.022 C A 0022  CYS SG 
C A 0018  CYS SG  2.018 C A 0027  CYS SG