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

HYDROPHOBIC 2.00 3.80   142
C A 0001  CYS C   2.426 C A 0002  ALA CA 
C A 0001  CYS C   3.233 C A 0002  ALA C  
C A 0001  CYS C   3.641 C A 0002  ALA CB 
C A 0001  CYS CB  3.641 H A 0013  THR CB 
C A 0001  CYS CB  3.370 H A 0013  THR CG2
C A 0001  CYS CB  3.700 E A 0025  CYS C  
C A 0001  CYS CA  3.791 C A 0030  PRO CA 
C A 0001  CYS CA  2.419 C A 0030  PRO C  
C A 0001  CYS C   3.219 C A 0030  PRO C  
C A 0001  CYS CB  3.619 C A 0030  PRO C  
C A 0002  ALA CA  3.794 C A 0003  GLU CA 
C A 0002  ALA C   2.426 C A 0003  GLU CA 
C A 0002  ALA C   3.654 C A 0003  GLU C  
C A 0002  ALA C   3.235 C A 0003  GLU CB 
C A 0002  ALA C   3.330 C A 0003  GLU CG 
C A 0003  GLU CA  3.778 C A 0004  SER CA 
C A 0003  GLU C   2.419 C A 0004  SER CA 
C A 0003  GLU C   3.332 C A 0004  SER C  
C A 0003  GLU C   3.551 C A 0004  SER CB 
C A 0003  GLU CB  3.740 H A 0013  THR CG2
C A 0003  GLU CG  3.581 H A 0013  THR CG2
C A 0003  GLU CD  3.699 H A 0013  THR CG2
C A 0004  SER CA  3.784 C A 0005  CYS CA 
C A 0004  SER C   2.410 C A 0005  CYS CA 
C A 0004  SER C   3.245 C A 0005  CYS C  
C A 0004  SER C   3.620 C A 0005  CYS CB 
C A 0004  SER CB  3.695 C A 0006  VAL CG2
C A 0005  CYS C   2.477 C A 0006  VAL CA 
C A 0005  CYS C   2.938 C A 0006  VAL C  
C A 0005  CYS C   3.744 C A 0006  VAL CB 
C A 0005  CYS CA  3.784 C A 0008  ILE C  
C A 0005  CYS CB  3.715 E A 0020  CYS CB 
C A 0006  VAL C   2.428 C A 0007  TYR CA 
C A 0006  VAL C   3.515 C A 0007  TYR C  
C A 0006  VAL C   3.472 C A 0007  TYR CB 
C A 0006  VAL C   3.411 C A 0007  TYR CD1
C A 0006  VAL CG1 3.523 C A 0007  TYR CD1
C A 0006  VAL CG1 3.771 C A 0007  TYR CE1
C A 0006  VAL CG2 3.541 C A 0023  ARG CB 
C A 0007  TYR C   2.444 C A 0008  ILE CA 
C A 0007  TYR C   3.700 C A 0008  ILE C  
C A 0007  TYR C   3.233 C A 0008  ILE CB 
C A 0007  TYR C   3.572 C A 0008  ILE CG1
C A 0007  TYR C   3.389 C A 0008  ILE CG2
C A 0008  ILE CA  2.892 C A 0009  PRO CD 
C A 0008  ILE C   2.467 C A 0009  PRO CA 
C A 0008  ILE C   3.072 C A 0009  PRO C  
C A 0008  ILE C   3.662 C A 0009  PRO CB 
C A 0008  ILE C   3.608 C A 0009  PRO CG 
C A 0008  ILE C   2.497 C A 0009  PRO CD 
C A 0008  ILE CB  3.573 C A 0009  PRO CD 
C A 0009  PRO C   2.453 C A 0010  CYS CA 
C A 0009  PRO C   2.957 C A 0010  CYS C  
C A 0009  PRO C   3.709 C A 0010  CYS CB 
C A 0010  CYS CA  3.792 H A 0011  THR CA 
C A 0010  CYS C   2.418 H A 0011  THR CA 
C A 0010  CYS C   3.444 H A 0011  THR C  
C A 0010  CYS C   3.513 H A 0011  THR CB 
C A 0010  CYS C   3.707 H A 0014  ALA CB 
H A 0011  THR C   2.428 H A 0012  VAL CA 
H A 0011  THR C   2.994 H A 0012  VAL C  
H A 0011  THR C   3.747 H A 0012  VAL CB 
H A 0012  VAL CA  3.764 H A 0013  THR CA 
H A 0012  VAL C   2.415 H A 0013  THR CA 
H A 0012  VAL C   3.041 H A 0013  THR C  
H A 0012  VAL C   3.710 H A 0013  THR CB 
H A 0013  THR C   2.422 H A 0014  ALA CA 
H A 0013  THR C   2.993 H A 0014  ALA C  
H A 0013  THR C   3.707 H A 0014  ALA CB 
H A 0013  THR C   3.650 C A 0018  CYS CB 
H A 0013  THR CB  3.353 C A 0018  CYS CB 
H A 0014  ALA CA  3.794 H A 0015  LEU CA 
H A 0014  ALA C   2.438 H A 0015  LEU CA 
H A 0014  ALA C   3.043 H A 0015  LEU C  
H A 0014  ALA C   3.728 H A 0015  LEU CB 
H A 0015  LEU CA  3.791 H A 0016  LEU CA 
H A 0015  LEU C   2.437 H A 0016  LEU CA 
H A 0015  LEU C   3.198 H A 0016  LEU C  
H A 0015  LEU C   3.675 H A 0016  LEU CB 
H A 0016  LEU CA  3.790 C A 0017  GLY CA 
H A 0016  LEU C   2.423 C A 0017  GLY CA 
H A 0016  LEU C   3.239 C A 0017  GLY C  
C A 0017  GLY CA  3.789 C A 0018  CYS CA 
C A 0017  GLY C   2.429 C A 0018  CYS CA 
C A 0017  GLY C   3.141 C A 0018  CYS C  
C A 0017  GLY C   3.684 C A 0018  CYS CB 
C A 0018  CYS CA  3.785 E A 0019  SER CA 
C A 0018  CYS C   2.421 E A 0019  SER CA 
C A 0018  CYS C   3.362 E A 0019  SER C  
C A 0018  CYS C   3.559 E A 0019  SER CB 
C A 0018  CYS CB  3.712 E A 0025  CYS CB 
C A 0018  CYS CA  3.760 C A 0027  ASN CB 
E A 0019  SER CA  3.800 E A 0020  CYS CA 
E A 0019  SER C   2.433 E A 0020  CYS CA 
E A 0019  SER C   3.098 E A 0020  CYS C  
E A 0019  SER C   3.697 E A 0020  CYS CB 
E A 0020  CYS CA  3.798 E A 0021  SER CA 
E A 0020  CYS C   2.428 E A 0021  SER CA 
E A 0020  CYS C   3.632 E A 0021  SER C  
E A 0020  CYS C   3.227 E A 0021  SER CB 
E A 0021  SER C   2.446 C A 0022  ASN CA 
E A 0021  SER C   2.989 C A 0022  ASN C  
E A 0021  SER C   3.050 C A 0022  ASN CB 
C A 0022  ASN C   2.465 C A 0023  ARG CA 
C A 0022  ASN C   3.139 C A 0023  ARG C  
C A 0022  ASN C   2.996 C A 0023  ARG CB 
C A 0022  ASN C   3.501 C A 0023  ARG CG 
C A 0022  ASN C   3.759 C A 0023  ARG CZ 
C A 0023  ARG C   2.418 E A 0024  VAL CA 
C A 0023  ARG C   3.593 E A 0024  VAL C  
C A 0023  ARG C   3.325 E A 0024  VAL CB 
E A 0024  VAL CA  3.793 E A 0025  CYS CA 
E A 0024  VAL C   2.416 E A 0025  CYS CA 
E A 0024  VAL C   3.138 E A 0025  CYS C  
E A 0024  VAL C   3.659 E A 0025  CYS CB 
E A 0024  VAL CG1 3.678 E A 0026  TYR CD1
E A 0024  VAL CG1 3.544 E A 0026  TYR CE1
E A 0024  VAL CG2 3.703 E A 0026  TYR CE1
E A 0025  CYS C   2.440 E A 0026  TYR CA 
E A 0025  CYS C   3.581 E A 0026  TYR C  
E A 0025  CYS C   3.388 E A 0026  TYR CB 
E A 0025  CYS C   3.371 E A 0026  TYR CD1
E A 0026  TYR CA  3.794 C A 0027  ASN CA 
E A 0026  TYR C   2.440 C A 0027  ASN CA 
E A 0026  TYR C   3.658 C A 0027  ASN C  
E A 0026  TYR C   3.161 C A 0027  ASN CB 
E A 0026  TYR CZ  3.642 C A 0030  PRO CB 
C A 0027  ASN CA  3.776 C A 0028  GLY CA 
C A 0027  ASN C   2.421 C A 0028  GLY CA 
C A 0027  ASN C   3.144 C A 0028  GLY C  
C A 0028  GLY CA  3.761 C A 0029  ILE CA 
C A 0028  GLY C   2.432 C A 0029  ILE CA 
C A 0028  GLY C   3.463 C A 0029  ILE C  
C A 0028  GLY C   3.501 C A 0029  ILE CB 
C A 0028  GLY C   3.600 C A 0029  ILE CG2
C A 0029  ILE CA  2.922 C A 0030  PRO CD 
C A 0029  ILE C   2.453 C A 0030  PRO CA 
C A 0029  ILE C   3.098 C A 0030  PRO C  
C A 0029  ILE C   3.654 C A 0030  PRO CB 
C A 0029  ILE C   3.586 C A 0030  PRO CG 
C A 0029  ILE C   2.500 C A 0030  PRO CD 
C A 0029  ILE CB  3.366 C A 0030  PRO CD 

HB_MM       2.00 3.20    51
C A 0001  CYS N   3.021 E A 0025  CYS O  
C A 0001  CYS N   2.242 C A 0030  PRO O  
C A 0002  ALA N   2.244 C A 0001  CYS O  
C A 0003  GLU N   3.020 C A 0001  CYS O  
C A 0003  GLU N   2.245 C A 0002  ALA O  
C A 0004  SER N   2.246 C A 0003  GLU O  
C A 0005  CYS N   2.234 C A 0004  SER O  
C A 0005  CYS N   2.929 C A 0023  ARG O  
C A 0006  VAL N   2.267 C A 0005  CYS O  
C A 0006  VAL N   3.075 C A 0023  ARG O  
C A 0007  TYR N   2.859 C A 0005  CYS O  
C A 0007  TYR N   2.245 C A 0006  VAL O  
C A 0008  ILE N   3.029 C A 0005  CYS O  
C A 0008  ILE N   2.247 C A 0007  TYR O  
C A 0009  PRO N   2.245 C A 0008  ILE O  
C A 0010  CYS N   2.258 C A 0009  PRO O  
H A 0011  THR N   2.246 C A 0010  CYS O  
H A 0012  VAL N   2.243 H A 0011  THR O  
H A 0013  THR N   2.250 H A 0012  VAL O  
H A 0014  ALA N   3.081 H A 0011  THR O  
H A 0014  ALA N   3.083 H A 0012  VAL O  
H A 0014  ALA N   2.245 H A 0013  THR O  
H A 0015  LEU N   3.061 H A 0012  VAL O  
H A 0015  LEU N   2.255 H A 0014  ALA O  
H A 0016  LEU N   2.959 H A 0013  THR O  
H A 0016  LEU N   2.251 H A 0015  LEU O  
C A 0017  GLY N   3.037 H A 0013  THR O  
C A 0017  GLY N   2.982 H A 0014  ALA O  
C A 0017  GLY N   2.251 H A 0016  LEU O  
C A 0018  CYS N   2.792 H A 0013  THR O  
C A 0018  CYS N   2.244 C A 0017  GLY O  
E A 0019  SER N   2.244 C A 0018  CYS O  
E A 0019  SER N   2.969 E A 0026  TYR O  
E A 0020  CYS N   2.252 E A 0019  SER O  
E A 0021  SER N   2.244 E A 0020  CYS O  
E A 0021  SER N   2.852 E A 0024  VAL O  
C A 0022  ASN N   2.246 E A 0021  SER O  
C A 0023  ARG N   3.194 E A 0021  SER O  
C A 0023  ARG N   2.256 C A 0022  ASN O  
E A 0024  VAL N   2.952 E A 0021  SER O  
E A 0024  VAL N   2.231 C A 0023  ARG O  
E A 0025  CYS N   2.936 C A 0003  GLU O  
E A 0025  CYS N   2.235 E A 0024  VAL O  
E A 0026  TYR N   2.897 E A 0019  SER O  
E A 0026  TYR N   2.252 E A 0025  CYS O  
C A 0027  ASN N   2.253 E A 0026  TYR O  
C A 0027  ASN N   3.061 C A 0029  ILE O  
C A 0028  GLY N   2.250 C A 0027  ASN O  
C A 0029  ILE N   2.792 C A 0027  ASN O  
C A 0029  ILE N   2.249 C A 0028  GLY O  
C A 0030  PRO N   2.255 C A 0029  ILE O  

HB_MS       2.00 3.20     6
H A 0011  THR N   2.689 C A 0003  GLU OE1
H A 0012  VAL N   3.161 C A 0003  GLU OE1
H A 0012  VAL N   2.716 C A 0003  GLU OE2
H A 0013  THR N   3.021 C A 0003  GLU OE1
H A 0016  LEU O   3.017 C A 0027  ASN ND2
E A 0020  CYS N   3.154 E A 0019  SER OG 

HB_SS       2.00 3.20     3
C A 0003  GLU OE1 2.674 H A 0013  THR OG1
C A 0023  ARG NH1 3.097 C A 0022  ASN OD1
C A 0023  ARG NH2 2.961 C A 0022  ASN OD1

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 E A 0020  CYS SG 
C A 0010  CYS SG  2.029 E A 0025  CYS SG