HEADER    TOXIN, HYDROLASE INHIBITOR              30-DEC-95   1LCM              
TITLE     NMR MINIMIZED AVERAGE STRUCTURE OF MICROCYSTIN-LR                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MICROCYSTIN LR;                                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MICROCYSTIN-LR                                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MICROCYSTIS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 1126;                                                
SOURCE   4 STRAIN: FROM A NATURAL BLOOM IN LAKE AKERSVATN, NORWAY               
KEYWDS    TOXIN, HYDROLASE INHIBITOR                                            
EXPDTA    SOLUTION NMR                                                          
AUTHOR    G.TROGEN,J.ZDUNEK                                                     
REVDAT   5   15-NOV-23 1LCM    1       REMARK LINK   ATOM                       
REVDAT   4   06-FEB-13 1LCM    1       LINK                                     
REVDAT   3   13-JUL-11 1LCM    1       VERSN                                    
REVDAT   2   24-FEB-09 1LCM    1       VERSN                                    
REVDAT   1   07-DEC-96 1LCM    0                                                
JRNL        AUTH   G.B.TROGEN,A.ANNILA,J.ERIKSSON,M.KONTTELI,J.MERILUOTO,       
JRNL        AUTH 2 I.SETHSON,J.ZDUNEK,U.EDLUND                                  
JRNL        TITL   CONFORMATIONAL STUDIES OF MICROCYSTIN-LR USING NMR           
JRNL        TITL 2 SPECTROSCOPY AND MOLECULAR DYNAMICS CALCULATIONS.            
JRNL        REF    BIOCHEMISTRY                  V.  35  3197 1996              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   8605154                                                      
JRNL        DOI    10.1021/BI952368S                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   J.R.BAGU,F.D.SONNICHSEN,D.WILLIAMS,R.J.ANDERSEN,B.D.SYKES,   
REMARK   1  AUTH 2 C.F.HOLMES                                                   
REMARK   1  TITL   COMPARISON OF THE SOLUTION STRUCTURES OF MICROCYSTIN-LR AND  
REMARK   1  TITL 2 MOTUPORIN                                                    
REMARK   1  REF    NAT.STRUCT.BIOL.              V.   2   114 1995              
REMARK   1  REFN                   ISSN 1072-8368                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   J.GOLDBERG,H.B.HUANG,Y.G.KWON,P.GREENGARD,A.C.NAIRN,         
REMARK   1  AUTH 2 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     : X-PLOR 3.0                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1LCM 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_1000174659.                                   
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  : MINIMIZED AVERAGE                  
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              2.19            
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                  140.35                    
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        -26.31                                           
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 DAL A 1                   
DBREF  1LCM 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  1.31  
LINK         N   DAL A   1                 C   DAM A   7     1555   1555  1.30  
LINK         C   LEU A   2                 N   ACB A   3     1555   1555  1.30  
LINK         CG  ACB A   3                 N   ARG A   4     1555   1555  1.30  
LINK         C   ARG A   4                 N   1ZN A   5     1555   1555  1.30  
LINK         C   1ZN A   5                 N   FGA A   6     1555   1555  1.30  
LINK         CD  FGA A   6                 N   DAM A   7     1555   1555  1.31  
SITE     1 AC1  3 LEU A   2  FGA A   6  DAM A   7                               
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       7.766   4.772   3.973  1.00  0.00           N  
HETATM    2  CA  DAL A   1       8.998   4.482   3.189  1.00  0.00           C  
HETATM    3  CB  DAL A   1       8.728   4.715   1.698  1.00  0.00           C  
HETATM    4  C   DAL A   1       9.423   3.028   3.421  1.00  0.00           C  
HETATM    5  O   DAL A   1      10.566   2.670   3.221  1.00  0.00           O  
HETATM    6  H1  DAL A   1       6.929   4.980   3.507  1.00  0.00           H  
HETATM    7  HA  DAL A   1       9.790   5.140   3.515  1.00  0.00           H  
HETATM    8  HB1 DAL A   1       9.666   4.749   1.162  1.00  0.00           H  
HETATM    9  HB2 DAL A   1       8.207   5.653   1.567  1.00  0.00           H  
HETATM   10  HB3 DAL A   1       8.122   3.910   1.310  1.00  0.00           H  
ATOM     11  N   LEU A   2       8.507   2.178   3.812  1.00  0.00           N  
ATOM     12  CA  LEU A   2       8.867   0.742   4.017  1.00  0.00           C  
ATOM     13  C   LEU A   2       8.122  -0.099   2.994  1.00  0.00           C  
ATOM     14  O   LEU A   2       8.691  -0.919   2.300  1.00  0.00           O  
ATOM     15  CB  LEU A   2       8.451   0.284   5.417  1.00  0.00           C  
ATOM     16  CG  LEU A   2       8.777   1.382   6.417  1.00  0.00           C  
ATOM     17  CD1 LEU A   2       7.960   1.169   7.710  1.00  0.00           C  
ATOM     18  CD2 LEU A   2      10.272   1.335   6.747  1.00  0.00           C  
ATOM     19  H   LEU A   2       7.580   2.477   3.944  1.00  0.00           H  
ATOM     20  HA  LEU A   2       9.932   0.618   3.898  1.00  0.00           H  
ATOM     21  HB2 LEU A   2       7.389   0.086   5.429  1.00  0.00           H  
ATOM     22  HB3 LEU A   2       8.989  -0.615   5.679  1.00  0.00           H  
ATOM     23  HG  LEU A   2       8.536   2.337   5.966  1.00  0.00           H  
ATOM     24 HD11 LEU A   2       7.025   0.680   7.475  1.00  0.00           H  
ATOM     25 HD12 LEU A   2       8.522   0.550   8.398  1.00  0.00           H  
ATOM     26 HD13 LEU A   2       7.756   2.123   8.175  1.00  0.00           H  
ATOM     27 HD21 LEU A   2      10.809   0.895   5.920  1.00  0.00           H  
ATOM     28 HD22 LEU A   2      10.634   2.338   6.919  1.00  0.00           H  
ATOM     29 HD23 LEU A   2      10.427   0.739   7.634  1.00  0.00           H  
HETATM   30  C   ACB A   3       4.956  -1.568   2.938  1.00  0.00           C  
HETATM   31  O   ACB A   3       4.618  -1.069   3.999  1.00  0.00           O  
HETATM   32  OXT ACB A   3       4.556  -2.647   2.535  1.00  0.00           O  
HETATM   33  CA  ACB A   3       6.001  -0.828   2.098  1.00  0.00           C  
HETATM   34  N   ACB A   3       6.830   0.032   2.978  1.00  0.00           N  
HETATM   35  CB  ACB A   3       5.312   0.049   1.056  1.00  0.00           C  
HETATM   36  CG  ACB A   3       4.093   0.745   1.661  1.00  0.00           C  
HETATM   37  C4  ACB A   3       6.292   1.094   0.548  1.00  0.00           C  
HETATM   38  OD2 ACB A   3       4.221   1.729   2.362  1.00  0.00           O  
HETATM   39  HA  ACB A   3       6.633  -1.546   1.597  1.00  0.00           H  
HETATM   40  H   ACB A   3       6.399   0.650   3.605  1.00  0.00           H  
HETATM   41  HB3 ACB A   3       5.003  -0.559   0.238  1.00  0.00           H  
HETATM   42  H41 ACB A   3       6.369   1.013  -0.527  1.00  0.00           H  
HETATM   43  H42 ACB A   3       7.259   0.923   0.994  1.00  0.00           H  
HETATM   44  H43 ACB A   3       5.936   2.076   0.813  1.00  0.00           H  
ATOM     45  N   ARG A   4       2.932   0.422   1.164  1.00  0.00           N  
ATOM     46  CA  ARG A   4       1.736   1.264   1.449  1.00  0.00           C  
ATOM     47  C   ARG A   4       0.869   0.581   2.509  1.00  0.00           C  
ATOM     48  O   ARG A   4      -0.250   0.985   2.757  1.00  0.00           O  
ATOM     49  CB  ARG A   4       0.917   1.451   0.160  1.00  0.00           C  
ATOM     50  CG  ARG A   4       0.526   0.081  -0.402  1.00  0.00           C  
ATOM     51  CD  ARG A   4       1.611  -0.401  -1.377  1.00  0.00           C  
ATOM     52  NE  ARG A   4       0.995  -0.705  -2.700  1.00  0.00           N  
ATOM     53  CZ  ARG A   4       1.751  -0.860  -3.756  1.00  0.00           C  
ATOM     54  NH1 ARG A   4       3.049  -0.755  -3.656  1.00  0.00           N  
ATOM     55  NH2 ARG A   4       1.207  -1.123  -4.913  1.00  0.00           N  
ATOM     56  H   ARG A   4       2.852  -0.367   0.590  1.00  0.00           H  
ATOM     57  HA  ARG A   4       2.058   2.227   1.820  1.00  0.00           H  
ATOM     58  HB2 ARG A   4       0.022   2.017   0.377  1.00  0.00           H  
ATOM     59  HB3 ARG A   4       1.508   1.981  -0.573  1.00  0.00           H  
ATOM     60  HG2 ARG A   4       0.423  -0.625   0.411  1.00  0.00           H  
ATOM     61  HG3 ARG A   4      -0.418   0.163  -0.925  1.00  0.00           H  
ATOM     62  HD2 ARG A   4       2.359   0.371  -1.500  1.00  0.00           H  
ATOM     63  HD3 ARG A   4       2.082  -1.293  -0.984  1.00  0.00           H  
ATOM     64  HE  ARG A   4       0.022  -0.788  -2.779  1.00  0.00           H  
ATOM     65 HH11 ARG A   4       3.469  -0.556  -2.771  1.00  0.00           H  
ATOM     66 HH12 ARG A   4       3.623  -0.874  -4.466  1.00  0.00           H  
ATOM     67 HH21 ARG A   4       0.214  -1.207  -4.992  1.00  0.00           H  
ATOM     68 HH22 ARG A   4       1.784  -1.242  -5.721  1.00  0.00           H  
HETATM   69  C1  1ZN A   5      -4.708  -4.926  -0.869  1.00  0.00           C  
HETATM   70  O1  1ZN A   5      -4.322  -6.215  -0.404  1.00  0.00           O  
HETATM   71  C2  1ZN A   5      -3.492  -6.252   0.754  1.00  0.00           C  
HETATM   72  C3  1ZN A   5      -3.392  -7.684   1.274  1.00  0.00           C  
HETATM   73  C4  1ZN A   5      -4.634  -8.454   0.897  1.00  0.00           C  
HETATM   74  C5  1ZN A   5      -5.695  -8.565   1.806  1.00  0.00           C  
HETATM   75  C6  1ZN A   5      -6.846  -9.283   1.456  1.00  0.00           C  
HETATM   76  C7  1ZN A   5      -6.936  -9.891   0.196  1.00  0.00           C  
HETATM   77  C8  1ZN A   5      -5.875  -9.781  -0.712  1.00  0.00           C  
HETATM   78  C9  1ZN A   5      -4.724  -9.062  -0.362  1.00  0.00           C  
HETATM   79  C10 1ZN A   5      -2.096  -5.750   0.407  1.00  0.00           C  
HETATM   80  C11 1ZN A   5      -1.969  -5.612  -1.111  1.00  0.00           C  
HETATM   81  C12 1ZN A   5      -1.898  -4.401   1.030  1.00  0.00           C  
HETATM   82  C13 1ZN A   5      -1.186  -4.275   2.162  1.00  0.00           C  
HETATM   83  C14 1ZN A   5      -0.262  -5.370   2.572  1.00  0.00           C  
HETATM   84  C15 1ZN A   5      -1.015  -3.038   2.717  1.00  0.00           C  
HETATM   85  C16 1ZN A   5       0.173  -2.710   3.233  1.00  0.00           C  
HETATM   86  CA  1ZN A   5       0.431  -1.361   3.863  1.00  0.00           C  
HETATM   87  N   1ZN A   5       1.298  -0.548   2.997  1.00  0.00           N  
HETATM   88  C18 1ZN A   5       1.110  -1.550   5.200  1.00  0.00           C  
HETATM   89  C19 1ZN A   5       0.338  -2.575   6.005  1.00  0.00           C  
HETATM   90  C   1ZN A   5       1.160  -0.220   5.940  1.00  0.00           C  
HETATM   91  O   1ZN A   5       0.142   0.370   6.244  1.00  0.00           O  
HETATM   92  H2  1ZN A   5       2.134  -0.927   2.690  1.00  0.00           H  
HETATM   93  H1  1ZN A   5      -4.152  -4.683  -1.762  1.00  0.00           H  
HETATM   94  H29 1ZN A   5      -5.765  -4.925  -1.093  1.00  0.00           H  
HETATM   95  H3  1ZN A   5      -4.502  -4.189  -0.107  1.00  0.00           H  
HETATM   96  H4  1ZN A   5      -3.908  -5.622   1.520  1.00  0.00           H  
HETATM   97  H5  1ZN A   5      -2.527  -8.160   0.836  1.00  0.00           H  
HETATM   98  H6  1ZN A   5      -3.288  -7.668   2.348  1.00  0.00           H  
HETATM   99  H7  1ZN A   5      -5.625  -8.096   2.777  1.00  0.00           H  
HETATM  100  H8  1ZN A   5      -7.663  -9.369   2.156  1.00  0.00           H  
HETATM  101  H9  1ZN A   5      -7.823 -10.445  -0.073  1.00  0.00           H  
HETATM  102  H10 1ZN A   5      -5.944 -10.250  -1.682  1.00  0.00           H  
HETATM  103  H11 1ZN A   5      -3.907  -8.977  -1.063  1.00  0.00           H  
HETATM  104  H12 1ZN A   5      -1.353  -6.450   0.787  1.00  0.00           H  
HETATM  105  H13 1ZN A   5      -2.688  -6.257  -1.595  1.00  0.00           H  
HETATM  106  H14 1ZN A   5      -0.973  -5.885  -1.418  1.00  0.00           H  
HETATM  107  H15 1ZN A   5      -2.164  -4.585  -1.393  1.00  0.00           H  
HETATM  108  H16 1ZN A   5      -2.488  -3.559   0.670  1.00  0.00           H  
HETATM  109  H17 1ZN A   5       0.565  -5.412   1.881  1.00  0.00           H  
HETATM  110  H18 1ZN A   5      -0.793  -6.306   2.565  1.00  0.00           H  
HETATM  111  H19 1ZN A   5       0.107  -5.166   3.566  1.00  0.00           H  
HETATM  112  H20 1ZN A   5      -1.755  -2.248   2.545  1.00  0.00           H  
HETATM  113  H21 1ZN A   5       1.030  -3.371   3.044  1.00  0.00           H  
HETATM  114  HA  1ZN A   5      -0.503  -0.865   4.009  1.00  0.00           H  
HETATM  115  H25 1ZN A   5       2.109  -1.896   5.039  1.00  0.00           H  
HETATM  116  H26 1ZN A   5      -0.566  -2.832   5.474  1.00  0.00           H  
HETATM  117  H27 1ZN A   5       0.947  -3.456   6.131  1.00  0.00           H  
HETATM  118  H28 1ZN A   5       0.091  -2.159   6.967  1.00  0.00           H  
HETATM  119  N   FGA A   6       2.311   0.381   5.938  1.00  0.00           N  
HETATM  120  CA  FGA A   6       2.485   1.685   6.619  1.00  0.00           C  
HETATM  121  C   FGA A   6       2.420   1.488   8.134  1.00  0.00           C  
HETATM  122  O   FGA A   6       2.959   0.500   8.606  1.00  0.00           O  
HETATM  123  CB  FGA A   6       3.848   2.240   6.229  1.00  0.00           C  
HETATM  124  CG  FGA A   6       3.917   3.727   6.582  1.00  0.00           C  
HETATM  125  CD  FGA A   6       5.374   4.192   6.552  1.00  0.00           C  
HETATM  126  OE1 FGA A   6       6.290   3.403   6.671  1.00  0.00           O  
HETATM  127  H   FGA A   6       3.074  -0.029   5.477  1.00  0.00           H  
HETATM  128  HA  FGA A   6       1.713   2.370   6.304  1.00  0.00           H  
HETATM  129  HB2 FGA A   6       4.616   1.696   6.756  1.00  0.00           H  
HETATM  130  HB3 FGA A   6       3.990   2.115   5.166  1.00  0.00           H  
HETATM  131  HG2 FGA A   6       3.345   4.291   5.861  1.00  0.00           H  
HETATM  132  HG3 FGA A   6       3.508   3.890   7.569  1.00  0.00           H  
HETATM  133  N   DAM A   7       5.596   5.471   6.409  1.00  0.00           N  
HETATM  134  CM  DAM A   7       4.497   6.449   6.643  1.00  0.00           C  
HETATM  135  CA  DAM A   7       6.920   5.943   5.919  1.00  0.00           C  
HETATM  136  CB  DAM A   7       7.276   7.236   6.069  1.00  0.00           C  
HETATM  137  C   DAM A   7       7.858   4.979   5.257  1.00  0.00           C  
HETATM  138  O   DAM A   7       8.721   4.434   5.916  1.00  0.00           O  
HETATM  139  HM1 DAM A   7       3.640   6.174   6.046  1.00  0.00           H  
HETATM  140  HM2 DAM A   7       4.830   7.437   6.364  1.00  0.00           H  
HETATM  141  HM3 DAM A   7       4.225   6.439   7.687  1.00  0.00           H  
HETATM  142  HB1 DAM A   7       8.176   7.495   6.646  1.00  0.00           H  
HETATM  143  HB2 DAM A   7       6.666   8.031   5.615  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   93   94   95                                                 
CONECT   70   69   71                                                           
CONECT   71   70   72   79   96                                                 
CONECT   72   71   73   97   98                                                 
CONECT   73   72   74   78                                                      
CONECT   74   73   75   99                                                      
CONECT   75   74   76  100                                                      
CONECT   76   75   77  101                                                      
CONECT   77   76   78  102                                                      
CONECT   78   73   77  103                                                      
CONECT   79   71   80   81  104                                                 
CONECT   80   79  105  106  107                                                 
CONECT   81   79   82  108                                                      
CONECT   82   81   83   84                                                      
CONECT   83   82  109  110  111                                                 
CONECT   84   82   85  112                                                      
CONECT   85   84   86  113                                                      
CONECT   86   85   87   88  114                                                 
CONECT   87   47   86   92                                                      
CONECT   88   86   89   90  115                                                 
CONECT   89   88  116  117  118                                                 
CONECT   90   88   91  119                                                      
CONECT   91   90                                                                
CONECT   92   87                                                                
CONECT   93   69                                                                
CONECT   94   69                                                                
CONECT   95   69                                                                
CONECT   96   71                                                                
CONECT   97   72                                                                
CONECT   98   72                                                                
CONECT   99   74                                                                
CONECT  100   75                                                                
CONECT  101   76                                                                
CONECT  102   77                                                                
CONECT  103   78                                                                
CONECT  104   79                                                                
CONECT  105   80                                                                
CONECT  106   80                                                                
CONECT  107   80                                                                
CONECT  108   81                                                                
CONECT  109   83                                                                
CONECT  110   83                                                                
CONECT  111   83                                                                
CONECT  112   84                                                                
CONECT  113   85                                                                
CONECT  114   86                                                                
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      129    0    5    0    0    0    1    6   70    1  103    1          
END