HEADER    HYDROLASE INHIBITOR, TOXIN              14-FEB-96   1EVB              
TITLE     NMR STRUCTURE OF CYANOBACTERIAL TOXIN, PHOSPHATASE-1/-2A INHIBITOR    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MICROCYSTIN-LR;                                            
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MICROCYSTIS;                                    
SOURCE   3 ORGANISM_TAXID: 1125                                                 
KEYWDS    TOXIN, HYDROLASE INHIBITOR                                            
EXPDTA    SOLUTION NMR                                                          
AUTHOR    J.R.BAGU,B.D.SYKES                                                    
REVDAT   6   15-NOV-23 1EVB    1       LINK   ATOM                              
REVDAT   5   23-AUG-23 1EVB    1       REMARK                                   
REVDAT   4   05-JUL-23 1EVB    1       REMARK LINK                              
REVDAT   3   13-JUL-11 1EVB    1       VERSN                                    
REVDAT   2   24-FEB-09 1EVB    1       VERSN                                    
REVDAT   1   08-NOV-96 1EVB    0                                                
JRNL        AUTH   J.R.BAGU,F.D.SONNICHSEN,D.WILLIAMS,R.J.ANDERSEN,B.D.SYKES,   
JRNL        AUTH 2 C.F.HOLMES                                                   
JRNL        TITL   COMPARISON OF THE SOLUTION STRUCTURES OF MICROCYSTIN-LR AND  
JRNL        TITL 2 MOTUPORIN.                                                   
JRNL        REF    NAT.STRUCT.BIOL.              V.   2   114 1995              
JRNL        REFN                   ISSN 1072-8368                               
JRNL        PMID   7749913                                                      
JRNL        DOI    10.1038/NSB0295-114                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.GOLDBERG,H.HUANG,Y.KWON,P.GREENGARD,A.C.NAIRN,J.KURIYAN    
REMARK   1  TITL   THREE-DIMENSIONAL STRUCTURE OF THE CATALYTIC SUBUNIT OF      
REMARK   1  TITL 2 PROTEIN SERINE/THREONINE PHOSPHATASE-1                       
REMARK   1  REF    NATURE                        V. 376   745 1995              
REMARK   1  REFN                   ISSN 0028-0836                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. NOT APPLICABLE.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : DGII                                                 
REMARK   3   AUTHORS     : HAVEL                                                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1EVB 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_1000173180.                                   
REMARK 210                                                                      
REMARK 210 EXPERIMENTAL DETAILS                                                 
REMARK 210  EXPERIMENT TYPE                : NMR                                
REMARK 210  TEMPERATURE           (KELVIN) : 278                                
REMARK 210  PH                             : 7                                  
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE MICROCYSTIN LR IS OLIGOPEPTIDE, A MEMBER OF TOXIN CLASS.         
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: MICROCYSTIN LR                                               
REMARK 400   CHAIN: A                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   N    DAL A     1     O    DAM A     7              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A   4   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 1ZN A    5     FGA A    6                  142.67                    
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   4         0.11    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    1ZN A   5        -17.99                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1EVA   RELATED DB: PDB                                   
DBREF  1EVB A    1     7  NOR    NOR00109 NOR00109         1      7             
SEQRES   1 A    7  DAL LEU ACB ARG 1ZN FGA DAM                                  
HET    DAL  A   1      10                                                       
HET    ACB  A   3      15                                                       
HET    1ZN  A   5      50                                                       
HET    FGA  A   6      14                                                       
HET    DAM  A   7      11                                                       
HETNAM     DAL D-ALANINE                                                        
HETNAM     ACB 3-METHYL-BETA-D-ASPARTIC ACID                                    
HETNAM     1ZN (2S,3S,4E,6E,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-           
HETNAM   2 1ZN  10-PHENYLDECA-4,6-DIENOIC ACID                                  
HETNAM     FGA GAMMA-D-GLUTAMIC ACID                                            
HETNAM     DAM N-METHYL-ALPHA-BETA-DEHYDROALANINE                               
HETSYN     ACB (3S)-3-METHYL-D-ASPARTIC ACID; D-METHYL ASPARTIC ACID            
HETSYN     FGA D-GLUTAMIC ACID                                                  
FORMUL   1  DAL    C3 H7 N O2                                                   
FORMUL   1  ACB    C5 H9 N O4                                                   
FORMUL   1  1ZN    C20 H29 N O3                                                 
FORMUL   1  FGA    C5 H9 N O4                                                   
FORMUL   1  DAM    C4 H7 N O2                                                   
LINK         C   DAL A   1                 N   LEU A   2     1555   1555  1.32  
LINK         N   DAL A   1                 C   DAM A   7     1555   1555  1.32  
LINK         C   LEU A   2                 N   ACB A   3     1555   1555  1.32  
LINK         CG  ACB A   3                 N   ARG A   4     1555   1555  1.32  
LINK         C   ARG A   4                 N   1ZN A   5     1555   1555  1.32  
LINK         C   1ZN A   5                 N   FGA A   6     1555   1555  1.32  
LINK         CD  FGA A   6                 N   DAM A   7     1555   1555  1.32  
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                         
HETATM    1  N   DAL A   1       7.902   0.279  10.158  1.00  0.00           N  
HETATM    2  CA  DAL A   1       8.669   0.056   8.936  1.00  0.00           C  
HETATM    3  CB  DAL A   1       8.403   1.190   8.044  1.00  0.00           C  
HETATM    4  C   DAL A   1       8.477  -1.252   8.207  1.00  0.00           C  
HETATM    5  O   DAL A   1       9.081  -1.473   7.195  1.00  0.00           O  
HETATM    6  H1  DAL A   1       6.983  -0.100   9.888  1.00  0.00           H  
HETATM    7  HA  DAL A   1       9.692   0.092   9.309  1.00  0.00           H  
HETATM    8  HB1 DAL A   1       7.376   1.136   7.682  1.00  0.00           H  
HETATM    9  HB2 DAL A   1       8.547   2.123   8.588  1.00  0.00           H  
HETATM   10  HB3 DAL A   1       9.088   1.155   7.197  1.00  0.00           H  
ATOM     11  N   LEU A   2       7.636  -2.143   8.700  1.00  0.00           N  
ATOM     12  CA  LEU A   2       7.339  -3.447   8.112  1.00  0.00           C  
ATOM     13  C   LEU A   2       6.113  -3.320   7.239  1.00  0.00           C  
ATOM     14  O   LEU A   2       6.086  -3.792   6.122  1.00  0.00           O  
ATOM     15  CB  LEU A   2       7.145  -4.476   9.213  1.00  0.00           C  
ATOM     16  CG  LEU A   2       8.050  -4.448  10.383  1.00  0.00           C  
ATOM     17  CD1 LEU A   2       7.613  -5.133  11.554  1.00  0.00           C  
ATOM     18  CD2 LEU A   2       9.292  -4.947  10.051  1.00  0.00           C  
ATOM     19  H   LEU A   2       7.149  -1.898   9.574  1.00  0.00           H  
ATOM     20  HA  LEU A   2       8.170  -3.706   7.456  1.00  0.00           H  
ATOM     21  HB2 LEU A   2       6.132  -4.329   9.587  1.00  0.00           H  
ATOM     22  HB3 LEU A   2       7.262  -5.450   8.739  1.00  0.00           H  
ATOM     23  HG  LEU A   2       8.100  -3.386  10.625  1.00  0.00           H  
ATOM     24 HD11 LEU A   2       6.631  -4.763  11.847  1.00  0.00           H  
ATOM     25 HD12 LEU A   2       7.552  -6.202  11.349  1.00  0.00           H  
ATOM     26 HD13 LEU A   2       8.323  -4.959  12.363  1.00  0.00           H  
ATOM     27 HD21 LEU A   2       9.659  -4.444   9.156  1.00  0.00           H  
ATOM     28 HD22 LEU A   2       9.985  -4.775  10.874  1.00  0.00           H  
ATOM     29 HD23 LEU A   2       9.214  -6.017   9.859  1.00  0.00           H  
HETATM   30  C   ACB A   3       2.638  -3.270   7.687  1.00  0.00           C  
HETATM   31  O   ACB A   3       2.629  -3.590   8.878  1.00  0.00           O  
HETATM   32  OXT ACB A   3       1.684  -3.577   6.970  1.00  0.00           O  
HETATM   33  CA  ACB A   3       3.808  -2.461   7.080  1.00  0.00           C  
HETATM   34  N   ACB A   3       5.084  -2.679   7.762  1.00  0.00           N  
HETATM   35  CB  ACB A   3       3.477  -1.052   6.649  1.00  0.00           C  
HETATM   36  CG  ACB A   3       2.762  -0.196   7.667  1.00  0.00           C  
HETATM   37  C4  ACB A   3       4.692  -0.322   6.099  1.00  0.00           C  
HETATM   38  OD2 ACB A   3       3.126  -0.166   8.827  1.00  0.00           O  
HETATM   39  HA  ACB A   3       4.151  -3.012   6.204  1.00  0.00           H  
HETATM   40  H   ACB A   3       5.186  -2.307   8.717  1.00  0.00           H  
HETATM   41  HB3 ACB A   3       2.676  -1.129   5.913  1.00  0.00           H  
HETATM   42  H41 ACB A   3       5.078  -0.859   5.233  1.00  0.00           H  
HETATM   43  H42 ACB A   3       4.406   0.687   5.803  1.00  0.00           H  
HETATM   44  H43 ACB A   3       5.463  -0.270   6.868  1.00  0.00           H  
ATOM     45  N   ARG A   4       1.734   0.505   7.225  1.00  0.00           N  
ATOM     46  CA  ARG A   4       0.887   1.339   8.072  1.00  0.00           C  
ATOM     47  C   ARG A   4      -0.394   0.636   8.454  1.00  0.00           C  
ATOM     48  O   ARG A   4      -1.215   1.224   8.997  1.00  0.00           O  
ATOM     49  CB  ARG A   4       0.409   2.640   7.423  1.00  0.00           C  
ATOM     50  CG  ARG A   4       1.574   3.390   6.951  1.00  0.00           C  
ATOM     51  CD  ARG A   4       1.419   4.263   5.808  1.00  0.00           C  
ATOM     52  NE  ARG A   4       1.108   5.614   6.121  1.00  0.00           N  
ATOM     53  CZ  ARG A   4       1.257   6.582   5.220  1.00  0.00           C  
ATOM     54  NH1 ARG A   4       1.289   6.393   3.899  1.00  0.00           N  
ATOM     55  NH2 ARG A   4       1.376   7.818   5.654  1.00  0.00           N  
ATOM     56  H   ARG A   4       1.517   0.461   6.219  1.00  0.00           H  
ATOM     57  HA  ARG A   4       1.465   1.491   8.983  1.00  0.00           H  
ATOM     58  HB2 ARG A   4      -0.280   2.412   6.589  1.00  0.00           H  
ATOM     59  HB3 ARG A   4      -0.105   3.273   8.166  1.00  0.00           H  
ATOM     60  HG2 ARG A   4       2.139   3.804   7.791  1.00  0.00           H  
ATOM     61  HG3 ARG A   4       2.161   2.650   6.410  1.00  0.00           H  
ATOM     62  HD2 ARG A   4       2.465   4.310   5.492  1.00  0.00           H  
ATOM     63  HD3 ARG A   4       0.762   3.817   5.048  1.00  0.00           H  
ATOM     64  HE  ARG A   4       1.232   5.887   7.093  1.00  0.00           H  
ATOM     65 HH11 ARG A   4       1.194   5.423   3.582  1.00  0.00           H  
ATOM     66 HH12 ARG A   4       1.422   7.220   3.308  1.00  0.00           H  
ATOM     67 HH21 ARG A   4       1.358   7.955   6.670  1.00  0.00           H  
ATOM     68 HH22 ARG A   4       1.507   8.542   4.941  1.00  0.00           H  
HETATM   69  C1  1ZN A   5      -8.227   0.328   3.671  1.00  0.00           C  
HETATM   70  O1  1ZN A   5      -8.185  -0.418   4.832  1.00  0.00           O  
HETATM   71  C2  1ZN A   5      -7.620  -1.650   4.748  1.00  0.00           C  
HETATM   72  C3  1ZN A   5      -8.235  -2.562   3.696  1.00  0.00           C  
HETATM   73  C4  1ZN A   5      -9.721  -2.642   3.543  1.00  0.00           C  
HETATM   74  C5  1ZN A   5     -10.268  -2.589   2.249  1.00  0.00           C  
HETATM   75  C6  1ZN A   5     -11.629  -2.780   2.044  1.00  0.00           C  
HETATM   76  C7  1ZN A   5     -12.463  -3.034   3.126  1.00  0.00           C  
HETATM   77  C8  1ZN A   5     -11.938  -3.096   4.415  1.00  0.00           C  
HETATM   78  C9  1ZN A   5     -10.572  -2.909   4.623  1.00  0.00           C  
HETATM   79  C10 1ZN A   5      -6.180  -1.516   4.474  1.00  0.00           C  
HETATM   80  C11 1ZN A   5      -5.678  -0.886   3.213  1.00  0.00           C  
HETATM   81  C12 1ZN A   5      -5.413  -1.030   5.680  1.00  0.00           C  
HETATM   82  C13 1ZN A   5      -4.314  -1.662   6.073  1.00  0.00           C  
HETATM   83  C14 1ZN A   5      -4.003  -2.887   5.274  1.00  0.00           C  
HETATM   84  C15 1ZN A   5      -3.604  -1.220   7.099  1.00  0.00           C  
HETATM   85  C16 1ZN A   5      -2.443  -1.801   7.387  1.00  0.00           C  
HETATM   86  CA  1ZN A   5      -1.686  -1.492   8.575  1.00  0.00           C  
HETATM   87  N   1ZN A   5      -0.545  -0.652   8.207  1.00  0.00           N  
HETATM   88  C18 1ZN A   5      -1.286  -2.678   9.420  1.00  0.00           C  
HETATM   89  C19 1ZN A   5      -2.361  -3.729   9.581  1.00  0.00           C  
HETATM   90  C   1ZN A   5      -0.688  -2.282  10.737  1.00  0.00           C  
HETATM   91  O   1ZN A   5      -1.375  -1.968  11.674  1.00  0.00           O  
HETATM   92  H1  1ZN A   5      -7.314   0.930   3.616  1.00  0.00           H  
HETATM   93  H29 1ZN A   5      -8.313  -0.276   2.745  1.00  0.00           H  
HETATM   94  H3  1ZN A   5      -9.103   0.893   3.836  1.00  0.00           H  
HETATM   95  H4  1ZN A   5      -7.727  -2.078   5.742  1.00  0.00           H  
HETATM   96  H5  1ZN A   5      -7.853  -2.216   2.730  1.00  0.00           H  
HETATM   97  H6  1ZN A   5      -7.759  -3.534   3.842  1.00  0.00           H  
HETATM   98  H7  1ZN A   5      -9.638  -2.422   1.385  1.00  0.00           H  
HETATM   99  H8  1ZN A   5     -12.031  -2.750   1.041  1.00  0.00           H  
HETATM  100  H9  1ZN A   5     -13.519  -3.194   2.960  1.00  0.00           H  
HETATM  101  H10 1ZN A   5     -12.591  -3.306   5.249  1.00  0.00           H  
HETATM  102  H11 1ZN A   5     -10.177  -2.989   5.626  1.00  0.00           H  
HETATM  103  H12 1ZN A   5      -5.999  -2.559   4.220  1.00  0.00           H  
HETATM  104  H13 1ZN A   5      -4.770  -1.353   2.856  1.00  0.00           H  
HETATM  105  H14 1ZN A   5      -6.411  -1.040   2.426  1.00  0.00           H  
HETATM  106  H15 1ZN A   5      -5.536   0.183   3.375  1.00  0.00           H  
HETATM  107  H16 1ZN A   5      -5.765  -0.141   6.192  1.00  0.00           H  
HETATM  108  H17 1ZN A   5      -4.881  -3.543   5.436  1.00  0.00           H  
HETATM  109  H18 1ZN A   5      -3.927  -2.526   4.238  1.00  0.00           H  
HETATM  110  H19 1ZN A   5      -3.118  -3.447   5.463  1.00  0.00           H  
HETATM  111  H20 1ZN A   5      -3.961  -0.389   7.714  1.00  0.00           H  
HETATM  112  H21 1ZN A   5      -1.976  -2.577   6.788  1.00  0.00           H  
HETATM  113  HA  1ZN A   5      -2.224  -0.795   9.217  1.00  0.00           H  
HETATM  114  H   1ZN A   5       0.223  -1.116   7.701  1.00  0.00           H  
HETATM  115  H25 1ZN A   5      -0.423  -3.143   8.945  1.00  0.00           H  
HETATM  116  H26 1ZN A   5      -2.638  -4.120   8.602  1.00  0.00           H  
HETATM  117  H27 1ZN A   5      -1.985  -4.542  10.202  1.00  0.00           H  
HETATM  118  H28 1ZN A   5      -3.236  -3.285  10.055  1.00  0.00           H  
HETATM  119  N   FGA A   6       0.630  -2.300  10.810  1.00  0.00           N  
HETATM  120  CA  FGA A   6       1.396  -1.957  12.005  1.00  0.00           C  
HETATM  121  C   FGA A   6       1.081  -2.956  13.154  1.00  0.00           C  
HETATM  122  O   FGA A   6       1.220  -4.169  12.983  1.00  0.00           O  
HETATM  123  CB  FGA A   6       2.898  -1.804  11.830  1.00  0.00           C  
HETATM  124  CG  FGA A   6       3.146  -0.983  13.061  1.00  0.00           C  
HETATM  125  CD  FGA A   6       4.383  -0.161  12.741  1.00  0.00           C  
HETATM  126  OE1 FGA A   6       3.772   0.502  11.948  1.00  0.00           O  
HETATM  127  H   FGA A   6       1.154  -2.574   9.966  1.00  0.00           H  
HETATM  128  HA  FGA A   6       0.926  -1.011  12.276  1.00  0.00           H  
HETATM  129  HB2 FGA A   6       3.282  -2.816  11.961  1.00  0.00           H  
HETATM  130  HB3 FGA A   6       3.008  -1.435  10.810  1.00  0.00           H  
HETATM  131  HG2 FGA A   6       3.526  -1.657  13.828  1.00  0.00           H  
HETATM  132  HG3 FGA A   6       2.466  -0.216  13.431  1.00  0.00           H  
HETATM  133  N   DAM A   7       5.660   0.088  12.963  1.00  0.00           N  
HETATM  134  CM  DAM A   7       5.803  -0.944  13.971  1.00  0.00           C  
HETATM  135  CA  DAM A   7       6.832   0.901  12.649  1.00  0.00           C  
HETATM  136  CB  DAM A   7       7.130   1.741  13.420  1.00  0.00           C  
HETATM  137  C   DAM A   7       7.662   0.668  11.397  1.00  0.00           C  
HETATM  138  O   DAM A   7       8.531   1.185  12.043  1.00  0.00           O  
HETATM  139  HM1 DAM A   7       6.078  -0.488  14.922  1.00  0.00           H  
HETATM  140  HM2 DAM A   7       4.858  -1.476  14.083  1.00  0.00           H  
HETATM  141  HM3 DAM A   7       6.580  -1.645  13.667  1.00  0.00           H  
HETATM  142  HB1 DAM A   7       7.997   2.373  13.229  1.00  0.00           H  
HETATM  143  HB2 DAM A   7       6.538   1.887  14.324  1.00  0.00           H  
TER     144      DAM A   7                                                      
CONECT    1    2  137                                                           
CONECT    2    1    3    4    7                                                 
CONECT    3    2    8    9   10                                                 
CONECT    4    2    5   11                                                      
CONECT    5    4                                                                
CONECT    7    2                                                                
CONECT    8    3                                                                
CONECT    9    3                                                                
CONECT   10    3                                                                
CONECT   11    4                                                                
CONECT   13   34                                                                
CONECT   30   31   32   33                                                      
CONECT   31   30                                                                
CONECT   32   30                                                                
CONECT   33   30   34   35   39                                                 
CONECT   34   13   33   40                                                      
CONECT   35   33   36   37   41                                                 
CONECT   36   35   38   45                                                      
CONECT   37   35   42   43   44                                                 
CONECT   38   36                                                                
CONECT   39   33                                                                
CONECT   40   34                                                                
CONECT   41   35                                                                
CONECT   42   37                                                                
CONECT   43   37                                                                
CONECT   44   37                                                                
CONECT   45   36                                                                
CONECT   47   87                                                                
CONECT   69   70   92   93   94                                                 
CONECT   70   69   71                                                           
CONECT   71   70   72   79   95                                                 
CONECT   72   71   73   96   97                                                 
CONECT   73   72   74   78                                                      
CONECT   74   73   75   98                                                      
CONECT   75   74   76   99                                                      
CONECT   76   75   77  100                                                      
CONECT   77   76   78  101                                                      
CONECT   78   73   77  102                                                      
CONECT   79   71   80   81  103                                                 
CONECT   80   79  104  105  106                                                 
CONECT   81   79   82  107                                                      
CONECT   82   81   83   84                                                      
CONECT   83   82  108  109  110                                                 
CONECT   84   82   85  111                                                      
CONECT   85   84   86  112                                                      
CONECT   86   85   87   88  113                                                 
CONECT   87   47   86  114                                                      
CONECT   88   86   89   90  115                                                 
CONECT   89   88  116  117  118                                                 
CONECT   90   88   91  119                                                      
CONECT   91   90                                                                
CONECT   92   69                                                                
CONECT   93   69                                                                
CONECT   94   69                                                                
CONECT   95   71                                                                
CONECT   96   72                                                                
CONECT   97   72                                                                
CONECT   98   74                                                                
CONECT   99   75                                                                
CONECT  100   76                                                                
CONECT  101   77                                                                
CONECT  102   78                                                                
CONECT  103   79                                                                
CONECT  104   80                                                                
CONECT  105   80                                                                
CONECT  106   80                                                                
CONECT  107   81                                                                
CONECT  108   83                                                                
CONECT  109   83                                                                
CONECT  110   83                                                                
CONECT  111   84                                                                
CONECT  112   85                                                                
CONECT  113   86                                                                
CONECT  114   87                                                                
CONECT  115   88                                                                
CONECT  116   89                                                                
CONECT  117   89                                                                
CONECT  118   89                                                                
CONECT  119   90  120  127                                                      
CONECT  120  119  121  123  128                                                 
CONECT  121  120  122                                                           
CONECT  122  121                                                                
CONECT  123  120  124  129  130                                                 
CONECT  124  123  125  131  132                                                 
CONECT  125  124  126  133                                                      
CONECT  126  125                                                                
CONECT  127  119                                                                
CONECT  128  120                                                                
CONECT  129  123                                                                
CONECT  130  123                                                                
CONECT  131  124                                                                
CONECT  132  124                                                                
CONECT  133  125  134  135                                                      
CONECT  134  133  139  140  141                                                 
CONECT  135  133  136  137                                                      
CONECT  136  135  142  143                                                      
CONECT  137    1  135  138                                                      
CONECT  138  137                                                                
CONECT  139  134                                                                
CONECT  140  134                                                                
CONECT  141  134                                                                
CONECT  142  136                                                                
CONECT  143  136                                                                
MASTER      154    0    5    0    0    0    0    6   70    1  103    1          
END