Complet list of 1q01 con fileClick here to see the 3D structure Complete list of 1q01.con file
COMMENT BEGIN
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COMMENT END
CONTACTS BETWEEN
CHAIN(S) "A"
AND
CHAIN(S) "A"

HYDROPHOBIC 2.00 3.80   157
C A 0001  GLY C   2.439 C A 0002  ASP CA 
C A 0001  GLY C   3.076 C A 0002  ASP C  
C A 0001  GLY C   2.950 C A 0002  ASP CB 
C A 0001  GLY C   3.259 C A 0002  ASP CG 
C A 0002  ASP C   2.434 C A 0003  ASN CA 
C A 0002  ASP C   3.126 C A 0003  ASN C  
C A 0002  ASP C   3.695 C A 0003  ASN CB 
C A 0003  ASN C   2.434 C A 0004  LYS CA 
C A 0003  ASN C   3.392 C A 0004  LYS C  
C A 0003  ASN C   3.566 C A 0004  LYS CB 
C A 0003  ASN C   3.401 C A 0005  PRO CD 
C A 0004  LYS CA  2.904 C A 0005  PRO CD 
C A 0004  LYS C   2.467 C A 0005  PRO CA 
C A 0004  LYS C   3.144 C A 0005  PRO C  
C A 0004  LYS C   3.648 C A 0005  PRO CB 
C A 0004  LYS C   3.642 C A 0005  PRO CG 
C A 0004  LYS C   2.506 C A 0005  PRO CD 
C A 0005  PRO CA  2.918 C A 0006  PRO CD 
C A 0005  PRO C   2.466 C A 0006  PRO CA 
C A 0005  PRO C   3.133 C A 0006  PRO C  
C A 0005  PRO C   3.651 C A 0006  PRO CB 
C A 0005  PRO C   3.643 C A 0006  PRO CG 
C A 0005  PRO C   2.511 C A 0006  PRO CD 
C A 0006  PRO C   2.434 C A 0007  LYS CA 
C A 0006  PRO C   3.000 C A 0007  LYS C  
C A 0006  PRO C   3.714 C A 0007  LYS CB 
C A 0007  LYS C   2.440 C A 0008  LYS CA 
C A 0007  LYS C   2.942 C A 0008  LYS C  
C A 0007  LYS C   3.732 C A 0008  LYS CB 
C A 0007  LYS CE  3.157 C A 0016  GLY CA 
C A 0008  LYS CA  3.778 C A 0009  GLY CA 
C A 0008  LYS C   2.416 C A 0009  GLY CA 
C A 0008  LYS C   2.991 C A 0009  GLY C  
C A 0008  LYS C   3.776 C A 0010  PRO CD 
C A 0009  GLY CA  2.927 C A 0010  PRO CD 
C A 0009  GLY C   2.466 C A 0010  PRO CA 
C A 0009  GLY C   3.134 C A 0010  PRO C  
C A 0009  GLY C   3.651 C A 0010  PRO CB 
C A 0009  GLY C   3.643 C A 0010  PRO CG 
C A 0009  GLY C   2.510 C A 0010  PRO CD 
C A 0010  PRO CA  2.904 C A 0011  PRO CD 
C A 0010  PRO C   2.464 C A 0011  PRO CA 
C A 0010  PRO C   3.136 C A 0011  PRO C  
C A 0010  PRO C   3.647 C A 0011  PRO CB 
C A 0010  PRO C   3.641 C A 0011  PRO CG 
C A 0010  PRO C   2.506 C A 0011  PRO CD 
C A 0010  PRO CB  3.222 C A 0011  PRO CD 
C A 0011  PRO C   2.435 C A 0012  ASN CA 
C A 0011  PRO C   3.008 C A 0012  ASN C  
C A 0011  PRO C   2.997 C A 0012  ASN CB 
C A 0012  ASN CA  3.791 C A 0013  GLY CA 
C A 0012  ASN C   2.417 C A 0013  GLY CA 
C A 0012  ASN C   3.664 C A 0013  GLY C  
C A 0013  GLY CA  3.798 C A 0014  CYS CA 
C A 0013  GLY C   2.435 C A 0014  CYS CA 
C A 0013  GLY C   2.985 C A 0014  CYS C  
C A 0013  GLY C   3.720 C A 0014  CYS CB 
C A 0014  CYS C   2.438 C A 0015  PHE CA 
C A 0014  CYS C   2.936 C A 0015  PHE C  
C A 0014  CYS C   3.716 C A 0015  PHE CB 
C A 0015  PHE CA  3.795 C A 0016  GLY CA 
C A 0015  PHE C   2.420 C A 0016  GLY CA 
C A 0015  PHE C   2.973 C A 0016  GLY C  
C A 0015  PHE CD2 3.769 C A 0027  GLY C  
C A 0015  PHE CE2 3.753 C A 0027  GLY C  
C A 0015  PHE CB  3.569 C A 0028  LEU CD2
C A 0015  PHE CG  3.583 C A 0028  LEU CA 
C A 0015  PHE CD1 3.391 C A 0028  LEU CA 
C A 0015  PHE CD1 3.500 C A 0028  LEU C  
C A 0015  PHE CE1 3.528 C A 0028  LEU C  
C A 0015  PHE CE1 3.436 C A 0029  GLY C  
C A 0016  GLY CA  3.795 C A 0017  HIS CA 
C A 0016  GLY C   2.434 C A 0017  HIS CA 
C A 0016  GLY C   3.040 C A 0017  HIS C  
C A 0016  GLY C   3.705 C A 0017  HIS CB 
C A 0017  HIS CA  3.797 C A 0018  LYS CA 
C A 0017  HIS C   2.433 C A 0018  LYS CA 
C A 0017  HIS C   3.263 C A 0018  LYS C  
C A 0017  HIS C   3.642 C A 0018  LYS CB 
C A 0017  HIS CB  3.724 C A 0019  ILE CG1
C A 0017  HIS C   3.752 C A 0028  LEU CB 
C A 0017  HIS C   3.525 C A 0029  GLY CA 
C A 0017  HIS CE1 3.595 C A 0031  ASN CB 
C A 0017  HIS CE1 3.174 C A 0031  ASN CG 
C A 0018  LYS C   2.434 C A 0019  ILE CA 
C A 0018  LYS C   3.170 C A 0019  ILE C  
C A 0018  LYS C   3.708 C A 0019  ILE CB 
C A 0018  LYS CA  3.629 C A 0029  GLY CA 
C A 0018  LYS CB  3.473 C A 0029  GLY CA 
C A 0018  LYS CD  3.781 C A 0033  VAL CG1
C A 0018  LYS CE  3.132 C A 0033  VAL CG1
C A 0019  ILE C   2.434 C A 0020  ASP CA 
C A 0019  ILE C   3.176 C A 0020  ASP C  
C A 0019  ILE C   3.680 C A 0020  ASP CB 
C A 0020  ASP C   2.434 C A 0021  ARG CA 
C A 0020  ASP C   3.235 C A 0021  ARG C  
C A 0020  ASP C   3.656 C A 0021  ARG CB 
C A 0021  ARG C   2.439 C A 0022  ILE CA 
C A 0021  ARG C   2.962 C A 0022  ILE C  
C A 0021  ARG C   3.098 C A 0022  ILE CB 
C A 0021  ARG C   3.167 C A 0022  ILE CG1
C A 0022  ILE CA  3.794 C A 0023  GLY CA 
C A 0022  ILE C   2.417 C A 0023  GLY CA 
C A 0022  ILE C   3.668 C A 0023  GLY C  
C A 0023  GLY CA  3.796 C A 0024  SER CA 
C A 0023  GLY C   2.434 C A 0024  SER CA 
C A 0023  GLY C   2.998 C A 0024  SER C  
C A 0023  GLY C   3.714 C A 0024  SER CB 
C A 0024  SER C   2.434 C A 0025  HIS CA 
C A 0024  SER C   3.035 C A 0025  HIS C  
C A 0024  SER C   3.711 C A 0025  HIS CB 
C A 0025  HIS C   2.434 C A 0026  SER CA 
C A 0025  HIS C   3.108 C A 0026  SER C  
C A 0025  HIS C   3.700 C A 0026  SER CB 
C A 0026  SER CA  3.791 C A 0027  GLY CA 
C A 0026  SER C   2.417 C A 0027  GLY CA 
C A 0026  SER C   3.708 C A 0027  GLY C  
C A 0027  GLY CA  3.796 C A 0028  LEU CA 
C A 0027  GLY C   2.434 C A 0028  LEU CA 
C A 0027  GLY C   3.003 C A 0028  LEU C  
C A 0027  GLY C   3.717 C A 0028  LEU CB 
C A 0028  LEU CA  3.792 C A 0029  GLY CA 
C A 0028  LEU C   2.418 C A 0029  GLY CA 
C A 0028  LEU C   3.549 C A 0029  GLY C  
C A 0029  GLY CA  3.798 C A 0030  CYS CA 
C A 0029  GLY C   2.435 C A 0030  CYS CA 
C A 0029  GLY C   3.142 C A 0030  CYS C  
C A 0029  GLY C   3.692 C A 0030  CYS CB 
C A 0030  CYS C   2.434 C A 0031  ASN CA 
C A 0030  CYS C   3.314 C A 0031  ASN C  
C A 0030  CYS C   3.616 C A 0031  ASN CB 
C A 0031  ASN C   2.434 C A 0032  LYS CA 
C A 0031  ASN C   3.282 C A 0032  LYS C  
C A 0031  ASN C   3.635 C A 0032  LYS CB 
C A 0032  LYS CA  3.800 C A 0033  VAL CA 
C A 0032  LYS C   2.431 C A 0033  VAL CA 
C A 0032  LYS C   3.408 C A 0033  VAL C  
C A 0032  LYS C   3.573 C A 0033  VAL CB 
C A 0032  LYS C   3.734 C A 0033  VAL CG1
C A 0032  LYS CE  3.618 C A 0037  LYS CG 
C A 0033  VAL C   2.432 C A 0034  ASP CA 
C A 0033  VAL C   3.224 C A 0034  ASP C  
C A 0033  VAL C   3.657 C A 0034  ASP CB 
C A 0034  ASP C   2.434 C A 0035  ASP CA 
C A 0034  ASP C   3.666 C A 0035  ASP C  
C A 0034  ASP C   3.213 C A 0035  ASP CB 
C A 0035  ASP C   2.437 C A 0036  ASN CA 
C A 0035  ASP C   2.935 C A 0036  ASN C  
C A 0035  ASP C   3.713 C A 0036  ASN CB 
C A 0036  ASN C   2.434 C A 0037  LYS CA 
C A 0036  ASN C   3.688 C A 0037  LYS C  
C A 0036  ASN C   3.152 C A 0037  LYS CB 
C A 0036  ASN C   3.780 C A 0037  LYS CG 
C A 0036  ASN C   3.552 C A 0037  LYS CD 
C A 0037  LYS CA  3.791 C A 0038  GLY CA 
C A 0037  LYS C   2.417 C A 0038  GLY CA 
C A 0037  LYS C   3.597 C A 0038  GLY C  

CHARGE_ATTR 2.00 12.00    23
C A 0002  ASP OD1 6.278 C A 0025  HIS ND1
C A 0002  ASP OD1 7.169 C A 0025  HIS NE2
C A 0002  ASP OD2 4.737 C A 0025  HIS ND1
C A 0002  ASP OD2 5.527 C A 0025  HIS NE2
C A 0020  ASP OD1 4.426 C A 0004  LYS NZ 
C A 0020  ASP OD2 3.880 C A 0004  LYS NZ 
C A 0020  ASP OD2 10.92 C A 0007  LYS NZ 
C A 0020  ASP OD1 7.226 C A 0021  ARG NH1
C A 0020  ASP OD1 8.052 C A 0021  ARG NH2
C A 0020  ASP OD2 7.018 C A 0021  ARG NH1
C A 0020  ASP OD2 7.948 C A 0021  ARG NH2
C A 0034  ASP OD1 10.68 C A 0018  LYS NZ 
C A 0034  ASP OD2 10.71 C A 0018  LYS NZ 
C A 0034  ASP OD1 8.687 C A 0032  LYS NZ 
C A 0034  ASP OD2 10.60 C A 0032  LYS NZ 
C A 0034  ASP OD1 7.973 C A 0037  LYS NZ 
C A 0034  ASP OD2 9.209 C A 0037  LYS NZ 
C A 0035  ASP OD1 8.512 C A 0018  LYS NZ 
C A 0035  ASP OD2 8.090 C A 0018  LYS NZ 
C A 0035  ASP OD1 11.78 C A 0032  LYS NZ 
C A 0035  ASP OD2 11.63 C A 0032  LYS NZ 
C A 0035  ASP OD1 9.077 C A 0037  LYS NZ 
C A 0035  ASP OD2 8.952 C A 0037  LYS NZ 

CHARGE_REPU 2.00 12.00    20
C A 0004  LYS NZ  9.619 C A 0007  LYS NZ 
C A 0004  LYS NZ  11.12 C A 0017  HIS ND1
C A 0004  LYS NZ  10.19 C A 0021  ARG NH1
C A 0004  LYS NZ  11.52 C A 0021  ARG NH2
C A 0004  LYS NZ  10.96 C A 0025  HIS ND1
C A 0007  LYS NZ  9.528 C A 0008  LYS NZ 
C A 0007  LYS NZ  4.484 C A 0017  HIS ND1
C A 0007  LYS NZ  4.609 C A 0017  HIS NE2
C A 0017  HIS ND1 10.07 C A 0018  LYS NZ 
C A 0017  HIS NE2 10.86 C A 0018  LYS NZ 
C A 0017  HIS ND1 11.43 C A 0032  LYS NZ 
C A 0017  HIS NE2 11.86 C A 0032  LYS NZ 
C A 0018  LYS NZ  8.715 C A 0021  ARG NH1
C A 0018  LYS NZ  10.55 C A 0021  ARG NH2
C A 0018  LYS NZ  11.32 C A 0032  LYS NZ 
C A 0032  LYS NZ  5.748 C A 0037  LYS NZ 
C A 0034  ASP OD1 7.568 C A 0035  ASP OD1
C A 0034  ASP OD1 9.089 C A 0035  ASP OD2
C A 0034  ASP OD2 6.538 C A 0035  ASP OD1
C A 0034  ASP OD2 8.413 C A 0035  ASP OD2

HB_MM       2.00 3.20    43
C A 0002  ASP N   2.252 C A 0001  GLY O  
C A 0003  ASN N   2.573 C A 0001  GLY O  
C A 0003  ASN N   2.249 C A 0002  ASP O  
C A 0004  LYS N   2.250 C A 0003  ASN O  
C A 0005  PRO N   2.252 C A 0004  LYS O  
C A 0006  PRO N   2.252 C A 0005  PRO O  
C A 0007  LYS N   2.250 C A 0006  PRO O  
C A 0008  LYS N   2.251 C A 0007  LYS O  
C A 0009  GLY N   2.251 C A 0008  LYS O  
C A 0010  PRO N   2.970 C A 0008  LYS O  
C A 0010  PRO N   2.250 C A 0009  GLY O  
C A 0011  PRO N   2.252 C A 0010  PRO O  
C A 0012  ASN N   2.620 C A 0010  PRO O  
C A 0012  ASN N   2.250 C A 0011  PRO O  
C A 0013  GLY N   2.249 C A 0012  ASN O  
C A 0014  CYS N   2.251 C A 0013  GLY O  
C A 0015  PHE N   2.251 C A 0014  CYS O  
C A 0016  GLY N   2.251 C A 0015  PHE O  
C A 0017  HIS N   2.250 C A 0016  GLY O  
C A 0018  LYS N   2.249 C A 0017  HIS O  
C A 0019  ILE N   3.124 C A 0017  HIS O  
C A 0019  ILE N   2.250 C A 0018  LYS O  
C A 0020  ASP N   2.250 C A 0019  ILE O  
C A 0021  ARG N   2.250 C A 0020  ASP O  
C A 0022  ILE N   2.251 C A 0021  ARG O  
C A 0023  GLY N   2.249 C A 0022  ILE O  
C A 0024  SER N   2.251 C A 0023  GLY O  
C A 0025  HIS N   2.251 C A 0024  SER O  
C A 0026  SER N   2.250 C A 0025  HIS O  
C A 0027  GLY N   2.251 C A 0026  SER O  
C A 0028  LEU N   2.249 C A 0027  GLY O  
C A 0029  GLY N   2.625 C A 0016  GLY O  
C A 0029  GLY N   2.250 C A 0028  LEU O  
C A 0030  CYS N   2.250 C A 0029  GLY O  
C A 0031  ASN N   2.250 C A 0030  CYS O  
C A 0032  LYS N   2.250 C A 0031  ASN O  
C A 0033  VAL N   2.250 C A 0032  LYS O  
C A 0034  ASP N   2.249 C A 0033  VAL O  
C A 0035  ASP N   2.996 C A 0033  VAL O  
C A 0035  ASP N   2.250 C A 0034  ASP O  
C A 0036  ASN N   2.251 C A 0035  ASP O  
C A 0037  LYS N   2.250 C A 0036  ASN O  
C A 0038  GLY N   2.250 C A 0037  LYS O  

HB_MS       2.00 3.20     2
C A 0019  ILE O   2.953 C A 0021  ARG NH1
C A 0037  LYS N   2.986 C A 0036  ASN OD1

AROMATIC    0.00 8.00     1
C A 0007  LYS 4.257 C A 0017  HIS

SS_BOND     1.50 2.80     1
C A 0014  CYS SG  2.029 C A 0030  CYS SG