HEADER    NEUROTOXIN                              12-DEC-92   1TCH              
TITLE     STRUCTURE-ACTIVITY RELATIONSHIPS OF MU-CONOTOXIN GIIIA: STRUCTURE     
TITLE    2 DETERMINATION OF ACTIVE AND INACTIVE SODIUM CHANNEL BLOCKER PEPTIDES 
TITLE    3 BY NMR AND SIMULATED ANNEALING CALCULATIONS                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MU-CONOTOXIN GIIIA;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1                                                             
KEYWDS    NEUROTOXIN                                                            
EXPDTA    SOLUTION NMR                                                          
AUTHOR    J.-M.LANCELIN,D.KOHDA,F.INAGAKI                                       
REVDAT   4   29-NOV-17 1TCH    1       REMARK HELIX                             
REVDAT   3   24-FEB-09 1TCH    1       VERSN                                    
REVDAT   2   01-APR-03 1TCH    1       JRNL                                     
REVDAT   1   31-JAN-94 1TCH    0                                                
JRNL        AUTH   K.WAKAMATSU,D.KOHDA,H.HATANAKA,J.M.LANCELIN,Y.ISHIDA,M.OYA,  
JRNL        AUTH 2 H.NAKAMURA,F.INAGAKI,K.SATO                                  
JRNL        TITL   STRUCTURE-ACTIVITY RELATIONSHIPS OF MU-CONOTOXIN GIIIA:      
JRNL        TITL 2 STRUCTURE DETERMINATION OF ACTIVE AND INACTIVE SODIUM        
JRNL        TITL 3 CHANNEL BLOCKER PEPTIDES BY NMR AND SIMULATED ANNEALING      
JRNL        TITL 4 CALCULATIONS.                                                
JRNL        REF    BIOCHEMISTRY                  V.  31 12577 1992              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   1335283                                                      
JRNL        DOI    10.1021/BI00165A006                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.-M.LANCELIN,D.KOHDA,S.-I.TATE,Y.YANAGAWA,T.ABE,M.SATAKE,   
REMARK   1  AUTH 2 F.INAGAKI                                                    
REMARK   1  TITL   TERTIARY STRUCTURE OF CONOTOXIN GIIIA IN AQUEOUS SOLUTION    
REMARK   1  REF    BIOCHEMISTRY                  V.  30  6908 1991              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   K.SATO,Y.ISHIDA,K.WAKAMATSU,R.KATO,H.HONDA,Y.OHIZUMI,        
REMARK   1  AUTH 2 H.NAKAMURA,M.OHYA,J.-M.LANCELIN,D.KOHDA,F.INAGAKI            
REMARK   1  TITL   ACTIVE SITE OF MU-CONOTOXIN GIIIA, A PEPTIDE BLOCKER OF      
REMARK   1  TITL 2 MUSCLE SODIUM CHANNELS                                       
REMARK   1  REF    J.BIOL.CHEM.                  V. 266 16989 1991              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 2.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1TCH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000176614.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : NULL                               
REMARK 210  PH                             : NULL                               
REMARK 210  IONIC STRENGTH                 : NULL                               
REMARK 210  PRESSURE                       : NULL                               
REMARK 210  SAMPLE CONTENTS                : NULL                               
REMARK 210                                                                      
REMARK 210  NMR EXPERIMENTS CONDUCTED      : NULL                               
REMARK 210  SPECTROMETER FIELD STRENGTH    : NULL                               
REMARK 210  SPECTROMETER MODEL             : NULL                               
REMARK 210  SPECTROMETER MANUFACTURER      : NULL                               
REMARK 210                                                                      
REMARK 210  STRUCTURE DETERMINATION.                                            
REMARK 210   SOFTWARE USED                 : NULL                               
REMARK 210   METHOD USED                   : NULL                               
REMARK 210                                                                      
REMARK 210 CONFORMERS, NUMBER CALCULATED   : NULL                               
REMARK 210 CONFORMERS, NUMBER SUBMITTED    : 1                                  
REMARK 210 CONFORMERS, SELECTION CRITERIA  : NULL                               
REMARK 210                                                                      
REMARK 210 BEST REPRESENTATIVE CONFORMER IN THIS ENSEMBLE : NULL                
REMARK 210                                                                      
REMARK 210 REMARK: NULL                                                         
REMARK 215                                                                      
REMARK 215 NMR STUDY                                                            
REMARK 215 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM SOLUTION           
REMARK 215 NMR DATA.  PROTEIN DATA BANK CONVENTIONS REQUIRE THAT                
REMARK 215 CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES ON              
REMARK 215 THESE RECORDS ARE MEANINGLESS.                                       
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LYS A   9   CB  -  CG  -  CD  ANGL. DEV. =  17.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  12     -178.70    -67.85                                   
REMARK 500    GLN A  14       -1.35    -54.58                                   
REMARK 500    CYS A  21      -56.99   -152.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A   1         0.26    SIDE CHAIN                              
REMARK 500    ARG A  19         0.27    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NH2 A 23                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1TCK   RELATED DB: PDB                                   
DBREF  1TCH A    1    22  UNP    P01523   CXM1_CONGE       1     22             
SEQADV 1TCH HYP A    6  UNP  P01523    PRO     6 CONFLICT                       
SEQADV 1TCH HYP A    7  UNP  P01523    PRO     7 CONFLICT                       
SEQADV 1TCH ALA A   13  UNP  P01523    ARG    13 CONFLICT                       
SEQADV 1TCH HYP A   17  UNP  P01523    PRO    17 CONFLICT                       
SEQRES   1 A   23  ARG ASP CYS CYS THR HYP HYP LYS LYS CYS LYS ASP ALA          
SEQRES   2 A   23  GLN CYS LYS HYP GLN ARG CYS CYS ALA NH2                      
MODRES 1TCH HYP A    6  PRO  4-HYDROXYPROLINE                                   
MODRES 1TCH HYP A    7  PRO  4-HYDROXYPROLINE                                   
MODRES 1TCH HYP A   17  PRO  4-HYDROXYPROLINE                                   
HET    HYP  A   6      15                                                       
HET    HYP  A   7      15                                                       
HET    HYP  A  17      15                                                       
HET    NH2  A  23       3                                                       
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM     NH2 AMINO GROUP                                                      
HETSYN     HYP HYDROXYPROLINE                                                   
FORMUL   1  HYP    3(C5 H9 N O3)                                                
FORMUL   1  NH2    H2 N                                                         
SSBOND   1 CYS A    3    CYS A   15                          1555   1555  2.02  
SSBOND   2 CYS A    4    CYS A   20                          1555   1555  2.02  
SSBOND   3 CYS A   10    CYS A   21                          1555   1555  2.02  
LINK         C   ALA A  22                 N   NH2 A  23     1555   1555  1.31  
LINK         C   THR A   5                 N   HYP A   6     1555   1555  1.32  
LINK         C   HYP A   6                 N   HYP A   7     1555   1555  1.33  
LINK         C   HYP A   7                 N   LYS A   8     1555   1555  1.30  
LINK         C   LYS A  16                 N   HYP A  17     1555   1555  1.32  
LINK         C   HYP A  17                 N   GLN A  18     1555   1555  1.30  
CISPEP   1 HYP A    6    HYP A    7          0        -1.65                     
SITE     1 AC1  1 ALA A  22                                                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   ARG A   1       0.890   1.260   0.511  1.00  2.56           N  
ATOM      2  CA  ARG A   1       0.337   0.862  -0.810  1.00  1.88           C  
ATOM      3  C   ARG A   1       1.475   0.554  -1.781  1.00  1.45           C  
ATOM      4  O   ARG A   1       2.569   1.062  -1.635  1.00  1.78           O  
ATOM      5  CB  ARG A   1      -0.508   2.005  -1.386  1.00  2.15           C  
ATOM      6  CG  ARG A   1      -1.643   2.330  -0.411  1.00  2.73           C  
ATOM      7  CD  ARG A   1      -1.309   3.622   0.340  1.00  3.28           C  
ATOM      8  NE  ARG A   1      -2.356   3.867   1.370  1.00  4.13           N  
ATOM      9  CZ  ARG A   1      -3.005   4.999   1.368  1.00  4.89           C  
ATOM     10  NH1 ARG A   1      -3.639   5.359   0.285  1.00  5.21           N  
ATOM     11  NH2 ARG A   1      -3.001   5.732   2.448  1.00  5.85           N  
ATOM     12  H1  ARG A   1       0.136   1.684   1.089  1.00  2.81           H  
ATOM     13  H2  ARG A   1       1.268   0.421   0.996  1.00  2.81           H  
ATOM     14  H3  ARG A   1       1.652   1.953   0.372  1.00  2.98           H  
ATOM     15  HA  ARG A   1      -0.262  -0.035  -0.680  1.00  2.08           H  
ATOM     16  HB2 ARG A   1       0.111   2.879  -1.527  1.00  2.55           H  
ATOM     17  HB3 ARG A   1      -0.922   1.707  -2.339  1.00  2.34           H  
ATOM     18  HG2 ARG A   1      -2.565   2.458  -0.958  1.00  3.27           H  
ATOM     19  HG3 ARG A   1      -1.758   1.521   0.295  1.00  3.31           H  
ATOM     20  HD2 ARG A   1      -0.347   3.528   0.821  1.00  3.67           H  
ATOM     21  HD3 ARG A   1      -1.285   4.453  -0.350  1.00  3.50           H  
ATOM     22  HE  ARG A   1      -2.555   3.184   2.046  1.00  4.49           H  
ATOM     23 HH11 ARG A   1      -3.622   4.772  -0.524  1.00  4.87           H  
ATOM     24 HH12 ARG A   1      -4.143   6.223   0.266  1.00  6.10           H  
ATOM     25 HH21 ARG A   1      -2.503   5.422   3.259  1.00  5.89           H  
ATOM     26 HH22 ARG A   1      -3.493   6.601   2.464  1.00  6.73           H  
ATOM     27  N   ASP A   2       1.193  -0.276  -2.754  1.00  1.13           N  
ATOM     28  CA  ASP A   2       2.246  -0.633  -3.748  1.00  0.77           C  
ATOM     29  C   ASP A   2       1.682  -0.652  -5.166  1.00  0.60           C  
ATOM     30  O   ASP A   2       0.519  -0.380  -5.384  1.00  0.79           O  
ATOM     31  CB  ASP A   2       2.768  -2.033  -3.410  1.00  1.12           C  
ATOM     32  CG  ASP A   2       4.297  -2.002  -3.334  1.00  1.73           C  
ATOM     33  OD1 ASP A   2       4.896  -2.199  -4.379  1.00  2.67           O  
ATOM     34  OD2 ASP A   2       4.778  -1.785  -2.234  1.00  2.28           O  
ATOM     35  H   ASP A   2       0.295  -0.661  -2.828  1.00  1.37           H  
ATOM     36  HA  ASP A   2       3.046   0.097  -3.702  1.00  0.68           H  
ATOM     37  HB2 ASP A   2       2.370  -2.353  -2.459  1.00  1.54           H  
ATOM     38  HB3 ASP A   2       2.465  -2.730  -4.178  1.00  1.05           H  
ATOM     39  N   CYS A   3       2.531  -0.978  -6.103  1.00  0.44           N  
ATOM     40  CA  CYS A   3       2.085  -1.026  -7.522  1.00  0.33           C  
ATOM     41  C   CYS A   3       1.479  -2.386  -7.872  1.00  0.32           C  
ATOM     42  O   CYS A   3       0.785  -2.515  -8.861  1.00  0.45           O  
ATOM     43  CB  CYS A   3       3.313  -0.808  -8.417  1.00  0.31           C  
ATOM     44  SG  CYS A   3       4.327   0.666  -8.120  1.00  0.32           S  
ATOM     45  H   CYS A   3       3.460  -1.185  -5.871  1.00  0.57           H  
ATOM     46  HA  CYS A   3       1.343  -0.254  -7.688  1.00  0.43           H  
ATOM     47  HB2 CYS A   3       3.956  -1.669  -8.313  1.00  0.39           H  
ATOM     48  HB3 CYS A   3       2.981  -0.776  -9.441  1.00  0.37           H  
ATOM     49  N   CYS A   4       1.757  -3.371  -7.054  1.00  0.28           N  
ATOM     50  CA  CYS A   4       1.209  -4.735  -7.321  1.00  0.28           C  
ATOM     51  C   CYS A   4       0.455  -5.291  -6.123  1.00  0.30           C  
ATOM     52  O   CYS A   4      -0.128  -6.352  -6.214  1.00  0.51           O  
ATOM     53  CB  CYS A   4       2.383  -5.669  -7.627  1.00  0.34           C  
ATOM     54  SG  CYS A   4       3.839  -4.935  -8.403  1.00  0.52           S  
ATOM     55  H   CYS A   4       2.325  -3.212  -6.274  1.00  0.37           H  
ATOM     56  HA  CYS A   4       0.521  -4.693  -8.163  1.00  0.33           H  
ATOM     57  HB2 CYS A   4       2.699  -6.127  -6.701  1.00  0.50           H  
ATOM     58  HB3 CYS A   4       2.026  -6.455  -8.276  1.00  0.50           H  
ATOM     59  N   THR A   5       0.482  -4.591  -5.020  1.00  0.34           N  
ATOM     60  CA  THR A   5      -0.250  -5.112  -3.838  1.00  0.36           C  
ATOM     61  C   THR A   5      -1.665  -4.507  -3.834  1.00  0.35           C  
ATOM     62  O   THR A   5      -1.826  -3.345  -4.143  1.00  0.41           O  
ATOM     63  CB  THR A   5       0.473  -4.666  -2.558  1.00  0.46           C  
ATOM     64  OG1 THR A   5       1.844  -4.600  -2.902  1.00  0.52           O  
ATOM     65  CG2 THR A   5       0.410  -5.730  -1.443  1.00  0.61           C  
ATOM     66  H   THR A   5       0.971  -3.742  -4.975  1.00  0.51           H  
ATOM     67  HA  THR A   5      -0.285  -6.185  -3.924  1.00  0.40           H  
ATOM     68  HB  THR A   5       0.110  -3.706  -2.227  1.00  0.46           H  
ATOM     69  HG1 THR A   5       2.314  -5.249  -2.375  1.00  0.97           H  
ATOM     70 HG21 THR A   5      -0.524  -5.638  -0.899  1.00  0.64           H  
ATOM     71 HG22 THR A   5       0.484  -6.722  -1.862  1.00  0.61           H  
ATOM     72 HG23 THR A   5       1.229  -5.579  -0.756  1.00  0.72           H  
HETATM   73  N   HYP A   6      -2.670  -5.285  -3.486  1.00  0.40           N  
HETATM   74  CA  HYP A   6      -4.059  -4.777  -3.458  1.00  0.52           C  
HETATM   75  C   HYP A   6      -4.230  -3.630  -2.435  1.00  0.65           C  
HETATM   76  O   HYP A   6      -3.935  -3.821  -1.273  1.00  0.72           O  
HETATM   77  CB  HYP A   6      -4.891  -5.980  -2.972  1.00  0.61           C  
HETATM   78  CG  HYP A   6      -3.891  -7.081  -2.561  1.00  0.56           C  
HETATM   79  CD  HYP A   6      -2.524  -6.700  -3.095  1.00  0.45           C  
HETATM   80  OD1 HYP A   6      -4.276  -8.246  -3.280  1.00  0.63           O  
HETATM   81  HA  HYP A   6      -4.344  -4.486  -4.450  1.00  0.53           H  
HETATM   82  HB2 HYP A   6      -5.497  -5.695  -2.125  1.00  0.72           H  
HETATM   83  HB3 HYP A   6      -5.528  -6.336  -3.769  1.00  0.68           H  
HETATM   84  HG  HYP A   6      -3.867  -7.247  -1.495  1.00  0.62           H  
HETATM   85 HD22 HYP A   6      -2.271  -7.304  -3.953  1.00  0.45           H  
HETATM   86 HD23 HYP A   6      -1.783  -6.800  -2.328  1.00  0.50           H  
HETATM   87  HD1 HYP A   6      -4.513  -8.922  -2.642  1.00  0.87           H  
HETATM   88  N   HYP A   7      -4.699  -2.452  -2.849  1.00  0.72           N  
HETATM   89  CA  HYP A   7      -5.057  -2.103  -4.252  1.00  0.67           C  
HETATM   90  C   HYP A   7      -3.803  -1.946  -5.112  1.00  0.53           C  
HETATM   91  O   HYP A   7      -2.938  -1.152  -4.797  1.00  0.60           O  
HETATM   92  CB  HYP A   7      -5.746  -0.729  -4.148  1.00  0.81           C  
HETATM   93  CG  HYP A   7      -5.620  -0.262  -2.684  1.00  0.95           C  
HETATM   94  CD  HYP A   7      -4.937  -1.367  -1.875  1.00  0.89           C  
HETATM   95  OD1 HYP A   7      -6.950  -0.198  -2.192  1.00  1.13           O  
HETATM   96  HA  HYP A   7      -5.730  -2.838  -4.675  1.00  0.70           H  
HETATM   97  HB2 HYP A   7      -5.260  -0.022  -4.804  1.00  0.76           H  
HETATM   98  HB3 HYP A   7      -6.786  -0.817  -4.419  1.00  0.89           H  
HETATM   99  HG  HYP A   7      -5.113   0.688  -2.595  1.00  1.02           H  
HETATM  100 HD22 HYP A   7      -5.583  -1.714  -1.083  1.00  1.15           H  
HETATM  101 HD23 HYP A   7      -3.998  -1.019  -1.470  1.00  0.97           H  
HETATM  102  HD1 HYP A   7      -7.140  -1.026  -1.744  1.00  1.43           H  
ATOM    103  N   LYS A   8      -3.714  -2.692  -6.176  1.00  0.48           N  
ATOM    104  CA  LYS A   8      -2.506  -2.564  -7.035  1.00  0.41           C  
ATOM    105  C   LYS A   8      -2.475  -1.195  -7.713  1.00  0.44           C  
ATOM    106  O   LYS A   8      -3.459  -0.484  -7.725  1.00  0.85           O  
ATOM    107  CB  LYS A   8      -2.545  -3.660  -8.108  1.00  0.47           C  
ATOM    108  CG  LYS A   8      -2.771  -5.009  -7.424  1.00  0.70           C  
ATOM    109  CD  LYS A   8      -2.557  -6.138  -8.445  1.00  0.83           C  
ATOM    110  CE  LYS A   8      -2.497  -7.496  -7.731  1.00  1.77           C  
ATOM    111  NZ  LYS A   8      -3.836  -8.153  -7.741  1.00  2.39           N  
ATOM    112  H   LYS A   8      -4.426  -3.325  -6.406  1.00  0.58           H  
ATOM    113  HA  LYS A   8      -1.623  -2.666  -6.412  1.00  0.43           H  
ATOM    114  HB2 LYS A   8      -3.343  -3.465  -8.801  1.00  0.68           H  
ATOM    115  HB3 LYS A   8      -1.607  -3.673  -8.643  1.00  0.45           H  
ATOM    116  HG2 LYS A   8      -2.078  -5.111  -6.607  1.00  0.79           H  
ATOM    117  HG3 LYS A   8      -3.778  -5.057  -7.038  1.00  0.91           H  
ATOM    118  HD2 LYS A   8      -3.374  -6.141  -9.151  1.00  1.35           H  
ATOM    119  HD3 LYS A   8      -1.633  -5.974  -8.980  1.00  1.48           H  
ATOM    120  HE2 LYS A   8      -1.787  -8.134  -8.237  1.00  2.43           H  
ATOM    121  HE3 LYS A   8      -2.179  -7.365  -6.709  1.00  2.67           H  
ATOM    122  HZ1 LYS A   8      -4.579  -7.427  -7.697  1.00  2.60           H  
ATOM    123  HZ2 LYS A   8      -3.944  -8.707  -8.614  1.00  2.67           H  
ATOM    124  HZ3 LYS A   8      -3.918  -8.784  -6.918  1.00  3.09           H  
ATOM    125  N   LYS A   9      -1.341  -0.849  -8.263  1.00  0.47           N  
ATOM    126  CA  LYS A   9      -1.228   0.469  -8.942  1.00  0.60           C  
ATOM    127  C   LYS A   9      -0.313   0.370 -10.158  1.00  0.60           C  
ATOM    128  O   LYS A   9       0.868   0.119 -10.026  1.00  1.21           O  
ATOM    129  CB  LYS A   9      -0.617   1.471  -7.953  1.00  0.76           C  
ATOM    130  CG  LYS A   9      -1.519   2.702  -7.849  1.00  1.38           C  
ATOM    131  CD  LYS A   9      -1.413   3.901  -6.903  1.00  1.26           C  
ATOM    132  CE  LYS A   9      -2.782   4.573  -6.781  1.00  2.10           C  
ATOM    133  NZ  LYS A   9      -2.946   5.173  -5.426  1.00  2.73           N  
ATOM    134  H   LYS A   9      -0.573  -1.456  -8.236  1.00  0.73           H  
ATOM    135  HA  LYS A   9      -2.211   0.790  -9.263  1.00  0.66           H  
ATOM    136  HB2 LYS A   9      -0.522   1.009  -6.982  1.00  1.64           H  
ATOM    137  HB3 LYS A   9       0.361   1.771  -8.299  1.00  1.62           H  
ATOM    138  HG2 LYS A   9      -0.607   3.156  -8.208  1.00  2.18           H  
ATOM    139  HG3 LYS A   9      -1.732   2.224  -6.904  1.00  1.94           H  
ATOM    140  HD2 LYS A   9      -1.087   3.566  -5.929  1.00  1.92           H  
ATOM    141  HD3 LYS A   9      -0.696   4.608  -7.293  1.00  1.99           H  
ATOM    142  HE2 LYS A   9      -2.871   5.352  -7.526  1.00  2.94           H  
ATOM    143  HE3 LYS A   9      -3.560   3.842  -6.940  1.00  2.94           H  
ATOM    144  HZ1 LYS A   9      -2.010   5.381  -5.025  1.00  3.13           H  
ATOM    145  HZ2 LYS A   9      -3.448   4.503  -4.809  1.00  3.40           H  
ATOM    146  HZ3 LYS A   9      -3.496   6.054  -5.500  1.00  3.20           H  
ATOM    147  N   CYS A  10      -0.881   0.568 -11.316  1.00  0.45           N  
ATOM    148  CA  CYS A  10      -0.066   0.492 -12.560  1.00  0.41           C  
ATOM    149  C   CYS A  10      -0.414   1.632 -13.510  1.00  0.48           C  
ATOM    150  O   CYS A  10      -0.285   1.505 -14.713  1.00  0.78           O  
ATOM    151  CB  CYS A  10      -0.360  -0.847 -13.243  1.00  0.45           C  
ATOM    152  SG  CYS A  10       0.320  -2.326 -12.458  1.00  0.42           S  
ATOM    153  H   CYS A  10      -1.839   0.762 -11.367  1.00  0.91           H  
ATOM    154  HA  CYS A  10       0.983   0.567 -12.301  1.00  0.37           H  
ATOM    155  HB2 CYS A  10      -1.430  -0.970 -13.307  1.00  0.52           H  
ATOM    156  HB3 CYS A  10       0.025  -0.803 -14.252  1.00  0.49           H  
ATOM    157  N   LYS A  11      -0.848   2.728 -12.945  1.00  0.44           N  
ATOM    158  CA  LYS A  11      -1.213   3.902 -13.783  1.00  0.46           C  
ATOM    159  C   LYS A  11      -0.112   4.959 -13.726  1.00  0.45           C  
ATOM    160  O   LYS A  11       0.179   5.612 -14.707  1.00  0.66           O  
ATOM    161  CB  LYS A  11      -2.508   4.505 -13.228  1.00  0.56           C  
ATOM    162  CG  LYS A  11      -3.699   3.679 -13.721  1.00  1.18           C  
ATOM    163  CD  LYS A  11      -4.778   3.659 -12.635  1.00  1.78           C  
ATOM    164  CE  LYS A  11      -6.106   3.221 -13.257  1.00  2.84           C  
ATOM    165  NZ  LYS A  11      -6.817   4.389 -13.848  1.00  3.33           N  
ATOM    166  H   LYS A  11      -0.932   2.777 -11.970  1.00  0.62           H  
ATOM    167  HA  LYS A  11      -1.344   3.580 -14.812  1.00  0.48           H  
ATOM    168  HB2 LYS A  11      -2.480   4.492 -12.148  1.00  0.99           H  
ATOM    169  HB3 LYS A  11      -2.608   5.525 -13.568  1.00  1.19           H  
ATOM    170  HG2 LYS A  11      -4.098   4.120 -14.622  1.00  1.77           H  
ATOM    171  HG3 LYS A  11      -3.378   2.670 -13.932  1.00  1.84           H  
ATOM    172  HD2 LYS A  11      -4.497   2.967 -11.856  1.00  2.66           H  
ATOM    173  HD3 LYS A  11      -4.884   4.646 -12.211  1.00  2.13           H  
ATOM    174  HE2 LYS A  11      -5.921   2.492 -14.032  1.00  3.33           H  
ATOM    175  HE3 LYS A  11      -6.732   2.775 -12.497  1.00  3.55           H  
ATOM    176  HZ1 LYS A  11      -7.437   4.065 -14.618  1.00  3.79           H  
ATOM    177  HZ2 LYS A  11      -7.390   4.853 -13.115  1.00  3.65           H  
ATOM    178  HZ3 LYS A  11      -6.122   5.065 -14.223  1.00  3.40           H  
ATOM    179  N   ASP A  12       0.478   5.102 -12.569  1.00  0.45           N  
ATOM    180  CA  ASP A  12       1.563   6.108 -12.418  1.00  0.45           C  
ATOM    181  C   ASP A  12       2.796   5.706 -13.220  1.00  0.42           C  
ATOM    182  O   ASP A  12       2.803   4.694 -13.893  1.00  0.72           O  
ATOM    183  CB  ASP A  12       1.944   6.188 -10.935  1.00  0.52           C  
ATOM    184  CG  ASP A  12       0.991   7.148 -10.220  1.00  1.04           C  
ATOM    185  OD1 ASP A  12       1.182   8.339 -10.407  1.00  1.85           O  
ATOM    186  OD2 ASP A  12       0.126   6.638  -9.528  1.00  1.64           O  
ATOM    187  H   ASP A  12       0.208   4.551 -11.806  1.00  0.59           H  
ATOM    188  HA  ASP A  12       1.211   7.068 -12.777  1.00  0.53           H  
ATOM    189  HB2 ASP A  12       1.869   5.210 -10.484  1.00  0.80           H  
ATOM    190  HB3 ASP A  12       2.957   6.551 -10.835  1.00  1.03           H  
ATOM    191  N   ALA A  13       3.814   6.513 -13.131  1.00  0.35           N  
ATOM    192  CA  ALA A  13       5.062   6.204 -13.879  1.00  0.35           C  
ATOM    193  C   ALA A  13       5.946   5.225 -13.122  1.00  0.29           C  
ATOM    194  O   ALA A  13       6.230   4.146 -13.593  1.00  0.38           O  
ATOM    195  CB  ALA A  13       5.863   7.497 -14.041  1.00  0.47           C  
ATOM    196  H   ALA A  13       3.753   7.320 -12.579  1.00  0.55           H  
ATOM    197  HA  ALA A  13       4.808   5.783 -14.845  1.00  0.39           H  
ATOM    198  HB1 ALA A  13       5.989   7.722 -15.089  1.00  0.61           H  
ATOM    199  HB2 ALA A  13       5.347   8.311 -13.558  1.00  0.50           H  
ATOM    200  HB3 ALA A  13       6.838   7.370 -13.582  1.00  0.48           H  
ATOM    201  N   GLN A  14       6.362   5.627 -11.958  1.00  0.33           N  
ATOM    202  CA  GLN A  14       7.233   4.742 -11.149  1.00  0.41           C  
ATOM    203  C   GLN A  14       6.616   3.358 -10.926  1.00  0.36           C  
ATOM    204  O   GLN A  14       7.226   2.513 -10.301  1.00  0.56           O  
ATOM    205  CB  GLN A  14       7.461   5.409  -9.788  1.00  0.58           C  
ATOM    206  CG  GLN A  14       7.863   6.870 -10.008  1.00  0.99           C  
ATOM    207  CD  GLN A  14       8.749   7.335  -8.850  1.00  1.21           C  
ATOM    208  OE1 GLN A  14       9.583   6.603  -8.357  1.00  1.92           O  
ATOM    209  NE2 GLN A  14       8.602   8.547  -8.390  1.00  2.24           N  
ATOM    210  H   GLN A  14       6.103   6.509 -11.618  1.00  0.42           H  
ATOM    211  HA  GLN A  14       8.171   4.628 -11.677  1.00  0.48           H  
ATOM    212  HB2 GLN A  14       6.553   5.365  -9.205  1.00  0.98           H  
ATOM    213  HB3 GLN A  14       8.248   4.891  -9.259  1.00  1.21           H  
ATOM    214  HG2 GLN A  14       8.410   6.962 -10.935  1.00  1.76           H  
ATOM    215  HG3 GLN A  14       6.980   7.489 -10.053  1.00  1.91           H  
ATOM    216 HE21 GLN A  14       7.931   9.143  -8.784  1.00  2.81           H  
ATOM    217 HE22 GLN A  14       9.161   8.862  -7.649  1.00  2.83           H  
ATOM    218  N   CYS A  15       5.426   3.149 -11.437  1.00  0.24           N  
ATOM    219  CA  CYS A  15       4.764   1.821 -11.257  1.00  0.19           C  
ATOM    220  C   CYS A  15       4.596   1.093 -12.594  1.00  0.16           C  
ATOM    221  O   CYS A  15       4.243  -0.068 -12.623  1.00  0.24           O  
ATOM    222  CB  CYS A  15       3.371   2.048 -10.655  1.00  0.24           C  
ATOM    223  SG  CYS A  15       3.238   2.202  -8.854  1.00  0.26           S  
ATOM    224  H   CYS A  15       4.971   3.861 -11.932  1.00  0.34           H  
ATOM    225  HA  CYS A  15       5.367   1.204 -10.599  1.00  0.21           H  
ATOM    226  HB2 CYS A  15       2.961   2.948 -11.091  1.00  0.33           H  
ATOM    227  HB3 CYS A  15       2.740   1.226 -10.956  1.00  0.30           H  
ATOM    228  N   LYS A  16       4.847   1.782 -13.675  1.00  0.19           N  
ATOM    229  CA  LYS A  16       4.700   1.124 -15.001  1.00  0.20           C  
ATOM    230  C   LYS A  16       5.802   0.085 -15.262  1.00  0.20           C  
ATOM    231  O   LYS A  16       5.519  -0.997 -15.734  1.00  0.20           O  
ATOM    232  CB  LYS A  16       4.722   2.193 -16.104  1.00  0.27           C  
ATOM    233  CG  LYS A  16       3.392   2.160 -16.863  1.00  0.35           C  
ATOM    234  CD  LYS A  16       3.372   3.288 -17.897  1.00  0.66           C  
ATOM    235  CE  LYS A  16       2.177   4.205 -17.622  1.00  0.68           C  
ATOM    236  NZ  LYS A  16       2.066   5.249 -18.680  1.00  1.43           N  
ATOM    237  H   LYS A  16       5.126   2.719 -13.615  1.00  0.27           H  
ATOM    238  HA  LYS A  16       3.751   0.604 -15.007  1.00  0.21           H  
ATOM    239  HB2 LYS A  16       4.861   3.169 -15.663  1.00  0.26           H  
ATOM    240  HB3 LYS A  16       5.534   1.994 -16.787  1.00  0.33           H  
ATOM    241  HG2 LYS A  16       3.283   1.208 -17.362  1.00  0.57           H  
ATOM    242  HG3 LYS A  16       2.575   2.291 -16.168  1.00  0.51           H  
ATOM    243  HD2 LYS A  16       4.288   3.857 -17.831  1.00  0.85           H  
ATOM    244  HD3 LYS A  16       3.287   2.869 -18.889  1.00  0.91           H  
ATOM    245  HE2 LYS A  16       1.268   3.620 -17.607  1.00  1.03           H  
ATOM    246  HE3 LYS A  16       2.302   4.685 -16.663  1.00  0.75           H  
ATOM    247  HZ1 LYS A  16       2.817   5.956 -18.548  1.00  1.78           H  
ATOM    248  HZ2 LYS A  16       2.168   4.807 -19.616  1.00  1.68           H  
ATOM    249  HZ3 LYS A  16       1.138   5.713 -18.614  1.00  1.76           H  
HETATM  250  N   HYP A  17       7.045   0.427 -14.970  1.00  0.23           N  
HETATM  251  CA  HYP A  17       8.169  -0.506 -15.184  1.00  0.27           C  
HETATM  252  C   HYP A  17       8.154  -1.602 -14.111  1.00  0.25           C  
HETATM  253  O   HYP A  17       9.103  -1.791 -13.377  1.00  0.39           O  
HETATM  254  CB  HYP A  17       9.433   0.378 -15.053  1.00  0.33           C  
HETATM  255  CG  HYP A  17       8.965   1.757 -14.541  1.00  0.32           C  
HETATM  256  CD  HYP A  17       7.437   1.755 -14.454  1.00  0.27           C  
HETATM  257  OD1 HYP A  17       9.285   2.674 -15.576  1.00  0.35           O  
HETATM  258  HA  HYP A  17       8.096  -0.950 -16.170  1.00  0.28           H  
HETATM  259  HB2 HYP A  17      10.136  -0.054 -14.359  1.00  0.36           H  
HETATM  260  HB3 HYP A  17       9.905   0.487 -16.019  1.00  0.38           H  
HETATM  261  HG  HYP A  17       9.432   2.030 -13.606  1.00  0.34           H  
HETATM  262 HD22 HYP A  17       7.024   2.534 -15.067  1.00  0.28           H  
HETATM  263 HD23 HYP A  17       7.123   1.868 -13.428  1.00  0.28           H  
HETATM  264  HD1 HYP A  17      10.049   2.334 -16.047  1.00  1.07           H  
ATOM    265  N   GLN A  18       7.062  -2.312 -14.056  1.00  0.18           N  
ATOM    266  CA  GLN A  18       6.927  -3.397 -13.059  1.00  0.21           C  
ATOM    267  C   GLN A  18       6.231  -4.600 -13.684  1.00  0.21           C  
ATOM    268  O   GLN A  18       5.124  -4.491 -14.172  1.00  0.30           O  
ATOM    269  CB  GLN A  18       6.058  -2.873 -11.910  1.00  0.28           C  
ATOM    270  CG  GLN A  18       6.914  -2.684 -10.656  1.00  0.36           C  
ATOM    271  CD  GLN A  18       8.082  -1.747 -10.972  1.00  0.43           C  
ATOM    272  OE1 GLN A  18       7.899  -0.652 -11.464  1.00  1.17           O  
ATOM    273  NE2 GLN A  18       9.298  -2.141 -10.706  1.00  1.31           N  
ATOM    274  H   GLN A  18       6.337  -2.144 -14.685  1.00  0.21           H  
ATOM    275  HA  GLN A  18       7.910  -3.691 -12.707  1.00  0.24           H  
ATOM    276  HB2 GLN A  18       5.617  -1.929 -12.192  1.00  0.30           H  
ATOM    277  HB3 GLN A  18       5.272  -3.581 -11.706  1.00  0.33           H  
ATOM    278  HG2 GLN A  18       6.312  -2.249  -9.869  1.00  0.44           H  
ATOM    279  HG3 GLN A  18       7.297  -3.638 -10.328  1.00  0.38           H  
ATOM    280 HE21 GLN A  18       9.452  -3.023 -10.310  1.00  2.07           H  
ATOM    281 HE22 GLN A  18      10.057  -1.552 -10.902  1.00  1.37           H  
ATOM    282  N   ARG A  19       6.902  -5.714 -13.665  1.00  0.24           N  
ATOM    283  CA  ARG A  19       6.306  -6.949 -14.251  1.00  0.26           C  
ATOM    284  C   ARG A  19       4.819  -7.052 -13.916  1.00  0.24           C  
ATOM    285  O   ARG A  19       4.069  -7.712 -14.606  1.00  0.29           O  
ATOM    286  CB  ARG A  19       7.026  -8.176 -13.671  1.00  0.34           C  
ATOM    287  CG  ARG A  19       7.947  -7.745 -12.526  1.00  1.45           C  
ATOM    288  CD  ARG A  19       8.493  -8.993 -11.831  1.00  1.58           C  
ATOM    289  NE  ARG A  19       9.341  -9.750 -12.793  1.00  2.19           N  
ATOM    290  CZ  ARG A  19       9.618 -11.003 -12.555  1.00  2.84           C  
ATOM    291  NH1 ARG A  19      10.252 -11.311 -11.457  1.00  3.71           N  
ATOM    292  NH2 ARG A  19       9.253 -11.906 -13.423  1.00  3.16           N  
ATOM    293  H   ARG A  19       7.797  -5.733 -13.276  1.00  0.30           H  
ATOM    294  HA  ARG A  19       6.418  -6.912 -15.331  1.00  0.29           H  
ATOM    295  HB2 ARG A  19       6.295  -8.880 -13.300  1.00  1.29           H  
ATOM    296  HB3 ARG A  19       7.610  -8.651 -14.445  1.00  1.26           H  
ATOM    297  HG2 ARG A  19       8.768  -7.164 -12.917  1.00  2.18           H  
ATOM    298  HG3 ARG A  19       7.394  -7.149 -11.815  1.00  2.26           H  
ATOM    299  HD2 ARG A  19       9.088  -8.708 -10.976  1.00  2.36           H  
ATOM    300  HD3 ARG A  19       7.675  -9.620 -11.505  1.00  2.05           H  
ATOM    301  HE  ARG A  19       9.687  -9.312 -13.598  1.00  2.64           H  
ATOM    302 HH11 ARG A  19      10.517 -10.592 -10.814  1.00  3.99           H  
ATOM    303 HH12 ARG A  19      10.473 -12.265 -11.258  1.00  4.32           H  
ATOM    304 HH21 ARG A  19       8.768 -11.634 -14.254  1.00  3.15           H  
ATOM    305 HH22 ARG A  19       9.457 -12.871 -13.257  1.00  3.76           H  
ATOM    306  N   CYS A  20       4.424  -6.398 -12.859  1.00  0.30           N  
ATOM    307  CA  CYS A  20       2.991  -6.448 -12.466  1.00  0.37           C  
ATOM    308  C   CYS A  20       2.212  -5.326 -13.145  1.00  0.35           C  
ATOM    309  O   CYS A  20       1.193  -4.886 -12.652  1.00  0.53           O  
ATOM    310  CB  CYS A  20       2.900  -6.256 -10.949  1.00  0.57           C  
ATOM    311  SG  CYS A  20       3.245  -4.603 -10.302  1.00  1.13           S  
ATOM    312  H   CYS A  20       5.064  -5.878 -12.329  1.00  0.36           H  
ATOM    313  HA  CYS A  20       2.573  -7.404 -12.763  1.00  0.40           H  
ATOM    314  HB2 CYS A  20       1.903  -6.529 -10.633  1.00  0.76           H  
ATOM    315  HB3 CYS A  20       3.590  -6.942 -10.479  1.00  0.81           H  
ATOM    316  N   CYS A  21       2.711  -4.884 -14.267  1.00  0.25           N  
ATOM    317  CA  CYS A  21       2.016  -3.790 -14.995  1.00  0.33           C  
ATOM    318  C   CYS A  21       2.288  -3.876 -16.495  1.00  0.42           C  
ATOM    319  O   CYS A  21       1.374  -3.963 -17.291  1.00  0.62           O  
ATOM    320  CB  CYS A  21       2.549  -2.455 -14.468  1.00  0.38           C  
ATOM    321  SG  CYS A  21       2.312  -2.122 -12.708  1.00  0.40           S  
ATOM    322  H   CYS A  21       3.536  -5.269 -14.627  1.00  0.24           H  
ATOM    323  HA  CYS A  21       0.946  -3.872 -14.824  1.00  0.36           H  
ATOM    324  HB2 CYS A  21       3.609  -2.406 -14.672  1.00  0.41           H  
ATOM    325  HB3 CYS A  21       2.072  -1.659 -15.020  1.00  0.44           H  
ATOM    326  N   ALA A  22       3.543  -3.850 -16.851  1.00  0.50           N  
ATOM    327  CA  ALA A  22       3.892  -3.928 -18.294  1.00  0.61           C  
ATOM    328  C   ALA A  22       3.613  -5.324 -18.844  1.00  0.85           C  
ATOM    329  O   ALA A  22       3.742  -6.319 -18.159  1.00  1.50           O  
ATOM    330  CB  ALA A  22       5.388  -3.628 -18.445  1.00  0.68           C  
ATOM    331  H   ALA A  22       4.248  -3.780 -16.175  1.00  0.60           H  
ATOM    332  HA  ALA A  22       3.295  -3.207 -18.841  1.00  0.77           H  
ATOM    333  HB1 ALA A  22       5.946  -4.552 -18.460  1.00  1.17           H  
ATOM    334  HB2 ALA A  22       5.561  -3.093 -19.367  1.00  0.94           H  
ATOM    335  HB3 ALA A  22       5.723  -3.024 -17.615  1.00  0.72           H  
HETATM  336  N   NH2 A  23       3.226  -5.446 -20.085  1.00  1.71           N  
HETATM  337  HN1 NH2 A  23       3.119  -4.650 -20.645  1.00  2.38           H  
HETATM  338  HN2 NH2 A  23       3.042  -6.335 -20.455  1.00  1.96           H  
TER     339      NH2 A  23                                                      
CONECT   44  223                                                                
CONECT   54  311                                                                
CONECT   61   73                                                                
CONECT   73   61   74   79                                                      
CONECT   74   73   75   77   81                                                 
CONECT   75   74   76   88                                                      
CONECT   76   75                                                                
CONECT   77   74   78   82   83                                                 
CONECT   78   77   79   80   84                                                 
CONECT   79   73   78   85   86                                                 
CONECT   80   78   87                                                           
CONECT   81   74                                                                
CONECT   82   77                                                                
CONECT   83   77                                                                
CONECT   84   78                                                                
CONECT   85   79                                                                
CONECT   86   79                                                                
CONECT   87   80                                                                
CONECT   88   75   89   94                                                      
CONECT   89   88   90   92   96                                                 
CONECT   90   89   91  103                                                      
CONECT   91   90                                                                
CONECT   92   89   93   97   98                                                 
CONECT   93   92   94   95   99                                                 
CONECT   94   88   93  100  101                                                 
CONECT   95   93  102                                                           
CONECT   96   89                                                                
CONECT   97   92                                                                
CONECT   98   92                                                                
CONECT   99   93                                                                
CONECT  100   94                                                                
CONECT  101   94                                                                
CONECT  102   95                                                                
CONECT  103   90                                                                
CONECT  152  321                                                                
CONECT  223   44                                                                
CONECT  230  250                                                                
CONECT  250  230  251  256                                                      
CONECT  251  250  252  254  258                                                 
CONECT  252  251  253  265                                                      
CONECT  253  252                                                                
CONECT  254  251  255  259  260                                                 
CONECT  255  254  256  257  261                                                 
CONECT  256  250  255  262  263                                                 
CONECT  257  255  264                                                           
CONECT  258  251                                                                
CONECT  259  254                                                                
CONECT  260  254                                                                
CONECT  261  255                                                                
CONECT  262  256                                                                
CONECT  263  256                                                                
CONECT  264  257                                                                
CONECT  265  252                                                                
CONECT  311   54                                                                
CONECT  321  152                                                                
CONECT  328  336                                                                
CONECT  336  328  337  338                                                      
CONECT  337  336                                                                
CONECT  338  336                                                                
MASTER      141    0    4    0    0    0    1    6  170    1   59    2          
END