HEADER    PEPTIDE ANTIBIOTIC                      11-OCT-97   1JOH              
TITLE     THE STRUCTURE OF ANTIAMOEBIN I, A MEMBRANE-ACTIVE PEPTIDE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ANTIAMOEBIN I;                                             
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 BIOLOGICAL_UNIT: MONOMERS OR DIMERS AGGREGATE IN THE                 
COMPND   5 MEMBRANE TO FACILITATE ION TRANSPORT                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: EMERCELLIOPSIS SP.                              
KEYWDS    ANTIAMOEBIN, PEPTAIBOL, PEPTIDE ANTIBIOTIC                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.F.SNOOK,B.A.WALLACE                                                 
REVDAT   1   20-JAN-99 1JOH    0                                                
JRNL        AUTH   C.F.SNOOK,G.A.WOOLLEY,G.OLIVA,V.PATTABHI,S.F.WOOD,           
JRNL        AUTH 2 T.L.BLUNDELL,B.A.WALLACE                                     
JRNL        TITL   THE STRUCTURE AND FUNCTION OF ANTIAMOEBIN I, A               
JRNL        TITL 2 PROLINE-RICH MEMBRANE-ACTIVE POLYPEPTIDE                     
JRNL        REF    STRUCTURE (LONDON)            V.   6   783 1998              
JRNL        REFN   ASTM STRUE6  UK ISSN 0969-2126                 2005          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   C.F.SNOOK,B.A.WALLACE                                        
REMARK   1  TITL   THE MOLECULAR REPLACEMENT SOLUTION OF A SMALL                
REMARK   1  TITL 2 POLYPEPTIDE THAT REQUIRED HIGH RESOLUTION DATA TO            
REMARK   1  TITL 3 SOLVE                                                        
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                  0353          
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   C.F.SNOOK                                                    
REMARK   1  REF    THE STRUCTURE AND FUNCTION                 1997              
REMARK   1  REF  2 OF ANTIAMOEBIN I, A                                          
REMARK   1  REF  3 MEMBRANE-ACTIVE PEPTIDE                                      
REMARK   1  PUBL   LONDON : UNIVERSITY OF LONDON (THESIS)                       
REMARK   1  REFN   ASTM         UK ISBN                           2188          
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   G.OLIVA                                                      
REMARK   1  REF    MOLECULAR REDUNDANCY AND                   1988              
REMARK   1  REF  2 PROTEIN CRYSTALLOGRAPHY :                                    
REMARK   1  REF  3 X-RAY STRUCTURE ANALYSIS OF                                  
REMARK   1  REF  4 ANTIAMOEBIN I, BOVINE                                        
REMARK   1  REF  5 PANCREATIC POLYPEPTIDE AND                                   
REMARK   1  REF  6 HUMAN SERUM AMYLOID P                                        
REMARK   1  REF  7 COMPONENT                                                    
REMARK   1  PUBL   LONDON : UNIVERSITY OF LONDON (THESIS)                       
REMARK   1  REFN   ASTM         UK ISBN                           2189          
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.4  ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-93                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.4                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.0                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0                              
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   CROSS-VALIDATION METHOD           : NULL                           
REMARK   3   FREE R VALUE TEST SET SELECTION   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1558                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 4359                   
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.1355                 
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 3567                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS      : 238                                           
REMARK   3   NUCLEIC ACID ATOMS : 0                                             
REMARK   3   HETEROGEN ATOMS    : 160                                           
REMARK   3   SOLVENT ATOMS      : 30                                            
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 268.00                  
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : NULL                    
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : NULL                    
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 1074                    
REMARK   3   NUMBER OF RESTRAINTS                     : 982                     
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.036                   
REMARK   3   ANGLE DISTANCES                      (A) : 3.152                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.000                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.000                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.000                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.000                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.016                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.005                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.022                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : 0.065                   
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: NULL                                                  
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: HETATM DATA FROM CCSD                                
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: REFINEMENT STARTED USING 10.0 TO          
REMARK   3  2.5A AND DATA CUT-OFF AT 2 SIGMA IN X-PLOR.  HIGH                   
REMARK   3  RESOLUTION LIMIT INCREASED TO 2.0A, LOW RESOLUTION                  
REMARK   3  DECREASED TO 25.0A AND DATA CUT-OFF DECREASED TO 0.0 SIGMA          
REMARK   3  AT 2.0A RESOLUTION.  RESOLUTION INCREASED FROM 2.0A TO              
REMARK   3  1.4A WITH ALL DATA USING SHELXL-93.  REFINEMENT CEASED              
REMARK   3  AFTER RESIDUES 1 TO 5 IN B-CHAIN IDENTIFIED AS DISORDERED           
REMARK   3  IN DENSITY.                                                         
REMARK   4                                                                      
REMARK   4 1JOH COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996                        
REMARK   6                                                                      
REMARK   6 BIOMOLECULE ANTIAMOEBIN I IS ACTIVE AS A MONOMER THAT                
REMARK   6 INSERTS INTO THE LIPID BILAYER AND AGGREGATES IN A                   
REMARK   6 MANNER THAT ALLOWS CHARGE DISSIPATION.                               
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 1986                               
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : SEALED TUBE                        
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : 290 4-CIRCLE                       
REMARK 200    DIFFRACTOMETER                                                    
REMARK 200  DETECTOR MANUFACTURER          : HILGER-WATTS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6715                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.2                                
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.                                
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0                                  
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 1                                  
REMARK 200  R MERGE                    (I) : 1.2                                
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR                    
REMARK 200    REPLACEMENT                                                       
REMARK 200 SOFTWARE USED: AMORE (CCP4 VERSION)                                  
REMARK 200 STARTING MODEL: RESIDUES 6 - 16 OF LEU1-ZERVAMICIN WITH ALL          
REMARK 200    NON-EQUIVALENT SIDE-CHAINS TRIMMED TO ALA.                        
REMARK 200                                                                      
REMARK 200 REMARK: USED NORMALISED STRUCTURE FACTORS                            
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 28.                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ANTIAMOEBIN I WAS DISSOLVED IN           
REMARK 280 METHANOL AT 170 MG/ML AND GENTLY HEATED TO 303 K. THE                
REMARK 280 CLOSED VESSEL WAS THEN ALLOWED TO COOL TO ROOM                       
REMARK 280 TEMPERATURE (293 K). LEFT AT RT UNTIL CRYSTALS APPEARED.             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    PHL A    17     C    MOH       1     1556     1.76            
REMARK 500   O    MOH      19     O    MOH      21     1556     1.99            
REMARK 500   C    PHL A    17     C    MOH       1     1556     2.10            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
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   O    MOH      21  -  C    ARG       5              1.84            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 650                                                                      
REMARK 650 HELIX                                                                
REMARK 650 DETERMINATION METHOD: INSPECTION OF RAMACHANDRAN PLOT FROM           
REMARK 650 PROCHECK, LATER USE OF PROMOTIF GAVE RESIDUES 2-9 ALPHA              
REMARK 650 HELIX, RESIDUES 10-12 3/10-HELIX, AND RESIDUES 13-17 TWO             
REMARK 650 OVERLAPPING TYPE I BETA-TURNS.                                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 REFERENCE: PANDEY, R.C., H.MENG, J.C.COOK JR,                        
REMARK 999 K.L.RINEHART JR., J.AM.CHEM.SOC., V.99, (1977), 5203-5205.           
DBREF  1JOH A    1    17  PDB    1JOH     1JOH             1     17             
DBREF  1JOH B    1    17  PDB    1JOH     1JOH             1     17             
SEQRES   1 A   17  ACE PHE AIB AIB AIB DIV GLY LEU AIB AIB HYP GLN DIV          
SEQRES   2 A   17  HYP AIB PRO PHL                                              
SEQRES   1 B   17  ACE PHE AIB AIB AIB DIV GLY LEU AIB AIB HYP GLN DIV          
SEQRES   2 B   17  HYP AIB PRO PHL                                              
MODRES 1JOH DIV A    6  VAL  D-ISOVALINE                                        
MODRES 1JOH DIV A   13  VAL  D-ISOVALINE                                        
MODRES 1JOH HYP A   14  PRO  GAMMA-HYDROXPROLINE                                
MODRES 1JOH PHL A   17  PHE  L-PHENYLALANINOL                                   
MODRES 1JOH DIV B    6  VAL  D-ISOVALINE                                        
MODRES 1JOH HYP B   11  PRO  GAMMA-HYDROXPROLINE                                
MODRES 1JOH DIV B   13  VAL  D-ISOVALINE                                        
MODRES 1JOH HYP B   14  PRO  GAMMA-HYDROXPROLINE                                
MODRES 1JOH PHL B   17  PHE  L-PHENYLALANINOL                                   
HET    ACE  A   1       3                                                       
HET    AIB  A   3       6                                                       
HET    AIB  A   4       6                                                       
HET    AIB  A   5       6                                                       
HET    DIV  A   6       7                                                       
HET    AIB  A   9       6                                                       
HET    AIB  A  10       6                                                       
HET    HYP  A  11       8                                                       
HET    DIV  A  13       7                                                       
HET    HYP  A  14       8                                                       
HET    AIB  A  15       6                                                       
HET    PHL  A  17      11                                                       
HET    ACE  B   1       3                                                       
HET    AIB  B   3       6                                                       
HET    AIB  B   4       6                                                       
HET    AIB  B   5       6                                                       
HET    DIV  B   6       7                                                       
HET    AIB  B   9       6                                                       
HET    AIB  B  10       6                                                       
HET    HYP  B  11       8                                                       
HET    DIV  B  13       7                                                       
HET    HYP  B  14       8                                                       
HET    AIB  B  15       6                                                       
HET    PHL  B  17      11                                                       
HET    MOH      1       2                                                       
HET    MOH      2       2                                                       
HET    MOH      3       2                                                       
HET    MOH      4       2                                                       
HET    MOH      5       2                                                       
HET    MOH      6       2                                                       
HET    MOH      7       2                                                       
HET    MOH      8       1                                                       
HET    MOH      9       1                                                       
HET    MOH     10       1                                                       
HET    MOH     11       1                                                       
HET    MOH     12       1                                                       
HET    MOH     13       1                                                       
HET    MOH     14       1                                                       
HET    MOH     15       1                                                       
HET    MOH     16       1                                                       
HET    MOH     17       1                                                       
HET    MOH     18       1                                                       
HET    MOH     19       1                                                       
HET    MOH     20       1                                                       
HET    MOH     21       1                                                       
HET    MOH     22       1                                                       
HET    MOH     23       1                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     AIB ALPHA-AMINOISOBUTYRIC ACID                                       
HETNAM     DIV D-ISOVALINE                                                      
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM     PHL L-PHENYLALANINOL                                                 
HETNAM     MOH METHANOL                                                         
HETSYN     HYP HYDROXYPROLINE                                                   
FORMUL   1  ACE    C2 H3 O1                                                     
FORMUL   1  AIB    6(C4 H9 N1 O2)                                               
FORMUL   1  DIV    2(C5 H11 N1 O2)                                              
FORMUL   1  HYP    2(C5 H9 N1 O3)                                               
FORMUL   1  PHL    C9 H13 N1 O1                                                 
FORMUL   2  ACE    C2 H3 O1                                                     
FORMUL   2  AIB    6(C4 H9 N1 O2)                                               
FORMUL   2  DIV    2(C5 H11 N1 O2)                                              
FORMUL   2  HYP    2(C5 H9 N1 O3)                                               
FORMUL   2  PHL    C9 H13 N1 O1                                                 
FORMUL   3  MOH    23(C1 H4 O1)                                                 
HELIX    1   1 PHE A    2  AIB A    9  1 SEE REMARK 650                    8    
HELIX    2   2 AIB A   10  GLN A   12  1 SEE REMARK 650                    3    
TURN     1   1 HYP A  14  PHL A  17     1 SEE REMARK 650                        
TURN     2   2 HYP B  14  PHL B  17     1 SEE REMARK 650                        
LINK         C   ACE A   1                 N   PHE A   2                        
LINK         N   AIB A   3                 C   PHE A   2                        
LINK         C   AIB A   3                 N   AIB A   4                        
LINK         C   AIB A   4                 N   AIB A   5                        
LINK         C   AIB A   5                 N   DIV A   6                        
LINK         C   DIV A   6                 N   GLY A   7                        
LINK         N   AIB A   9                 C   LEU A   8                        
LINK         C   AIB A   9                 N   AIB A  10                        
LINK         C   AIB A  10                 N   HYP A  11                        
LINK         C   HYP A  11                 N   GLN A  12                        
LINK         N   DIV A  13                 C   GLN A  12                        
LINK         C   DIV A  13                 N   HYP A  14                        
LINK         C   HYP A  14                 N   AIB A  15                        
LINK         C   AIB A  15                 N   PRO A  16                        
LINK         N   PHL A  17                 C   PRO A  16                        
LINK         C   ACE B   1                 N   PHE B   2                        
LINK         N   AIB B   3                 C   PHE B   2                        
LINK         C   AIB B   3                 N   AIB B   4                        
LINK         C   AIB B   4                 N   AIB B   5                        
LINK         C   AIB B   5                 N   DIV B   6                        
LINK         C   DIV B   6                 N   GLY B   7                        
LINK         N   AIB B   9                 C   LEU B   8                        
LINK         C   AIB B   9                 N   AIB B  10                        
LINK         C   AIB B  10                 N   HYP B  11                        
LINK         C   HYP B  11                 N   GLN B  12                        
LINK         N   DIV B  13                 C   GLN B  12                        
LINK         C   DIV B  13                 N   HYP B  14                        
LINK         C   HYP B  14                 N   AIB B  15                        
LINK         C   AIB B  15                 N   PRO B  16                        
LINK         N   PHL B  17                 C   PRO B  16                        
CRYST1   26.530   28.820    9.060  88.90  96.64 123.85 P 1           2          
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      0.037693  0.025281  0.005782        0.00000                         
SCALE2      0.000000  0.041780  0.002293        0.00000                         
SCALE3      0.000000  0.000000  0.111288        0.00000                         
MTRIX1   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX2   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000 -1.000000      115.46000    1                    
HETATM    1  C   ACE A   1       2.849  -3.303   6.755  1.00  8.83           C  
HETATM    2  O   ACE A   1       3.769  -3.853   5.982  1.00 22.92           O  
HETATM    3  CH3 ACE A   1       2.419  -2.235   6.503  1.00  4.21           C  
ATOM      4  N   PHE A   2       2.432  -4.074   7.771  1.00  7.96           N  
ATOM      5  CA  PHE A   2       1.337  -3.613   8.648  1.00  7.17           C  
ATOM      6  C   PHE A   2       1.691  -2.333   9.360  1.00  6.64           C  
ATOM      7  O   PHE A   2       0.928  -1.330   9.208  1.00  7.33           O  
ATOM      8  CB  PHE A   2       1.038  -4.740   9.652  1.00  8.33           C  
ATOM      9  CG  PHE A   2      -0.151  -4.431  10.566  1.00  8.62           C  
ATOM     10  CD1 PHE A   2      -1.429  -4.737  10.137  1.00 11.83           C  
ATOM     11  CD2 PHE A   2       0.061  -3.900  11.832  1.00 10.07           C  
ATOM     12  CE1 PHE A   2      -2.529  -4.522  10.975  1.00 11.43           C  
ATOM     13  CE2 PHE A   2      -1.042  -3.639  12.638  1.00 12.54           C  
ATOM     14  CZ  PHE A   2      -2.308  -3.970  12.211  1.00 10.36           C  
HETATM   15  N   AIB A   3       2.770  -2.270  10.120  1.00  6.21           N  
HETATM   16  CA  AIB A   3       3.157  -1.040  10.817  1.00  7.61           C  
HETATM   17  C   AIB A   3       3.293   0.115   9.820  1.00  8.28           C  
HETATM   18  O1  AIB A   3       2.831   1.246  10.068  1.00  8.19           O  
HETATM   19  CB1 AIB A   3       4.545  -1.217  11.467  1.00 10.28           C  
HETATM   20  CB2 AIB A   3       2.126  -0.739  11.915  1.00  7.96           C  
HETATM   21  N   AIB A   4       3.974  -0.164   8.707  1.00  7.79           N  
HETATM   22  CA  AIB A   4       4.232   0.853   7.686  1.00  7.70           C  
HETATM   23  C   AIB A   4       2.966   1.513   7.180  1.00  7.96           C  
HETATM   24  O1  AIB A   4       2.890   2.740   6.965  1.00  8.35           O  
HETATM   25  CB1 AIB A   4       4.884   0.147   6.447  1.00 10.30           C  
HETATM   26  CB2 AIB A   4       5.230   1.883   8.222  1.00  8.15           C  
HETATM   27  N   AIB A   5       1.934   0.729   6.981  1.00  6.27           N  
HETATM   28  CA  AIB A   5       0.663   1.236   6.468  1.00  6.89           C  
HETATM   29  C   AIB A   5       0.185   2.406   7.316  1.00  7.88           C  
HETATM   30  O1  AIB A   5      -0.100   3.493   6.823  1.00  8.54           O  
HETATM   31  CB1 AIB A   5      -0.373   0.109   6.503  1.00  8.47           C  
HETATM   32  CB2 AIB A   5       0.836   1.718   5.011  1.00  9.23           C  
HETATM   33  N   DIV A   6       0.167   2.148   8.634  1.00  7.12           N  
HETATM   34  CA  DIV A   6      -0.253   3.141   9.610  1.00  7.05           C  
HETATM   35  CB1 DIV A   6      -1.713   3.539   9.354  1.00  9.23           C  
HETATM   36  CG1 DIV A   6      -2.397   4.188  10.534  1.00 25.33           C  
HETATM   37  CB2 DIV A   6      -0.100   2.475  11.023  1.00  8.89           C  
HETATM   38  C   DIV A   6       0.593   4.375   9.564  1.00  5.89           C  
HETATM   39  O   DIV A   6       0.167   5.539   9.554  1.00  8.17           O  
ATOM     40  N   GLY A   7       1.912   4.182   9.598  1.00  6.19           N  
ATOM     41  CA  GLY A   7       2.886   5.254   9.704  1.00  7.19           C  
ATOM     42  C   GLY A   7       2.914   6.174   8.512  1.00  5.35           C  
ATOM     43  O   GLY A   7       3.063   7.385   8.629  1.00  7.75           O  
ATOM     44  N   LEU A   8       2.780   5.597   7.330  1.00  5.64           N  
ATOM     45  CA  LEU A   8       2.854   6.397   6.095  1.00  6.70           C  
ATOM     46  C   LEU A   8       1.574   7.165   5.870  1.00  6.54           C  
ATOM     47  O   LEU A   8       1.656   8.343   5.433  1.00  7.30           O  
ATOM     48  CB  LEU A   8       3.220   5.497   4.921  1.00  7.21           C  
ATOM     49  CG  LEU A   8       4.556   4.764   5.027  1.00  7.63           C  
ATOM     50  CD1 LEU A   8       4.764   3.818   3.841  1.00 11.77           C  
ATOM     51  CD2 LEU A   8       5.731   5.755   5.065  1.00 16.31           C  
HETATM   52  N   AIB A   9       0.409   6.608   6.146  1.00  4.35           N  
HETATM   53  CA  AIB A   9      -0.870   7.294   6.066  1.00  5.85           C  
HETATM   54  C   AIB A   9      -1.001   8.403   7.100  1.00  5.94           C  
HETATM   55  O1  AIB A   9      -1.715   9.391   6.881  1.00  6.16           O  
HETATM   56  CB1 AIB A   9      -2.001   6.270   6.447  1.00  6.76           C  
HETATM   57  CB2 AIB A   9      -1.177   7.821   4.660  1.00  8.38           C  
HETATM   58  N   AIB A  10      -0.413   8.141   8.272  1.00  5.08           N  
HETATM   59  CA  AIB A  10      -0.770   8.895   9.491  1.00  4.94           C  
HETATM   60  C   AIB A  10      -0.834  10.381   9.327  1.00  6.40           C  
HETATM   61  O1  AIB A  10      -1.777  11.044   9.800  1.00  5.57           O  
HETATM   62  CB1 AIB A  10       0.221   8.564  10.615  1.00  7.11           C  
HETATM   63  CB2 AIB A  10      -2.196   8.362   9.895  1.00  7.37           C  
HETATM   64  N   HYP A  11       0.143  11.039   8.731  1.00  4.40           N  
HETATM   65  CA  HYP A  11       0.131  12.494   8.662  1.00  6.09           C  
HETATM   66  C   HYP A  11      -1.009  13.013   7.815  1.00  5.05           C  
HETATM   67  O   HYP A  11      -1.261  14.254   7.917  1.00  8.19           O  
HETATM   68  CB  HYP A  11       1.480  12.860   8.029  1.00  7.19           C  
HETATM   69  CG  HYP A  11       2.340  11.650   8.211  1.00  5.68           C  
HETATM   70  CD  HYP A  11       1.376  10.469   8.125  1.00  5.74           C  
HETATM   71  OD  HYP A  11       2.921  11.622   9.531  1.00  5.58           O  
ATOM     72  N   GLN A  12      -1.654  12.215   7.006  1.00  3.92           N  
ATOM     73  CA  GLN A  12      -2.721  12.693   6.138  1.00  5.80           C  
ATOM     74  C   GLN A  12      -4.078  12.603   6.823  1.00  7.39           C  
ATOM     75  O   GLN A  12      -5.049  13.233   6.380  1.00  7.66           O  
ATOM     76  CB  GLN A  12      -2.789  11.904   4.829  1.00  5.53           C  
ATOM     77  CG  GLN A  12      -1.453  11.787   4.130  1.00  5.88           C  
ATOM     78  CD  GLN A  12      -0.667  13.054   4.056  1.00  7.55           C  
ATOM     79  OE1 GLN A  12       0.621  13.046   4.204  1.00 10.44           O  
ATOM     80  NE2 GLN A  12      -1.256  14.166   3.823  1.00  6.08           N  
HETATM   81  N   DIV A  13      -4.148  11.862   7.933  1.00  6.43           N  
HETATM   82  CA  DIV A  13      -5.419  11.605   8.616  1.00  7.28           C  
HETATM   83  CB1 DIV A  13      -6.309  10.714   7.757  1.00  8.98           C  
HETATM   84  CG1 DIV A  13      -5.691   9.373   7.401  1.00 13.62           C  
HETATM   85  CB2 DIV A  13      -5.067  10.879   9.967  1.00  9.55           C  
HETATM   86  C   DIV A  13      -6.229  12.824   8.969  1.00  7.72           C  
HETATM   87  O   DIV A  13      -7.475  12.754   8.957  1.00  8.18           O  
HETATM   88  N   HYP A  14      -5.644  13.938   9.337  1.00  6.35           N  
HETATM   89  CA  HYP A  14      -6.432  15.123   9.713  1.00  8.98           C  
HETATM   90  C   HYP A  14      -7.180  15.789   8.577  1.00  9.98           C  
HETATM   91  O   HYP A  14      -8.037  16.659   8.873  1.00  8.86           O  
HETATM   92  CB  HYP A  14      -5.426  16.095  10.312  1.00  9.83           C  
HETATM   93  CG  HYP A  14      -4.302  15.171  10.797  1.00 10.14           C  
HETATM   94  CD  HYP A  14      -4.205  14.149   9.686  1.00  9.14           C  
HETATM   95  OD  HYP A  14      -4.696  14.594  12.046  1.00  9.64           O  
HETATM   96  N   AIB A  15      -6.799  15.551   7.333  1.00  8.32           N  
HETATM   97  CA  AIB A  15      -7.356  16.335   6.212  1.00  9.38           C  
HETATM   98  C   AIB A  15      -8.852  16.516   6.238  1.00  7.17           C  
HETATM   99  O1  AIB A  15      -9.338  17.629   5.905  1.00  9.81           O  
HETATM  100  CB1 AIB A  15      -7.001  15.658   4.893  1.00 11.12           C  
HETATM  101  CB2 AIB A  15      -6.657  17.731   6.270  1.00 11.85           C  
ATOM    102  N   PRO A  16      -9.671  15.519   6.457  1.00  6.27           N  
ATOM    103  CA  PRO A  16     -11.127  15.750   6.362  1.00  7.12           C  
ATOM    104  C   PRO A  16     -11.667  16.516   7.581  1.00  7.10           C  
ATOM    105  O   PRO A  16     -12.813  16.988   7.491  1.00  8.18           O  
ATOM    106  CB  PRO A  16     -11.715  14.349   6.376  1.00 12.38           C  
ATOM    107  CG  PRO A  16     -10.630  13.399   6.597  1.00 15.47           C  
ATOM    108  CD  PRO A  16      -9.354  14.097   6.706  1.00  8.76           C  
HETATM  109  C   PHL A  17     -11.017  18.626  10.000  1.00  9.22           C  
HETATM  110  O   PHL A  17     -11.698  19.267  11.032  1.00 10.13           O  
HETATM  111  CA  PHL A  17     -11.446  17.174   9.928  1.00  7.79           C  
HETATM  112  N   PHL A  17     -10.941  16.569   8.676  1.00  8.43           N  
HETATM  113  CB  PHL A  17     -10.894  16.353  11.096  1.00  9.14           C  
HETATM  114  CG  PHL A  17     -11.366  14.934  11.120  1.00 10.68           C  
HETATM  115  CD1 PHL A  17     -12.662  14.608  11.496  1.00 14.34           C  
HETATM  116  CD2 PHL A  17     -10.525  13.900  10.713  1.00 13.72           C  
HETATM  117  CE1 PHL A  17     -13.121  13.312  11.481  1.00 15.62           C  
HETATM  118  CE2 PHL A  17     -10.955  12.597  10.731  1.00 16.10           C  
HETATM  119  CZ  PHL A  17     -12.240  12.287  11.124  1.00 14.97           C  
TER     120      PHL A  17                                                      
HETATM  121  C   ACE B   1       2.587  26.291   3.660  1.00 24.85           C  
HETATM  122  O   ACE B   1       1.702  26.968   3.061  1.00 29.42           O  
HETATM  123  CH3 ACE B   1       2.872  25.053   3.359  1.00 10.13           C  
ATOM    124  N   PHE B   2       3.272  26.808   4.680  1.00 28.86           N  
ATOM    125  CA  PHE B   2       4.220  26.024   5.445  1.00 34.44           C  
ATOM    126  C   PHE B   2       3.657  25.348   6.683  1.00 33.73           C  
ATOM    127  O   PHE B   2       4.245  25.535   7.784  1.00 45.01           O  
ATOM    128  CB  PHE B   2       5.493  26.802   5.689  1.00 42.04           C  
ATOM    129  CG  PHE B   2       5.701  27.953   4.701  1.00 45.62           C  
ATOM    130  CD1 PHE B   2       6.284  27.726   3.468  1.00 48.24           C  
ATOM    131  CD2 PHE B   2       5.283  29.232   5.012  1.00 46.77           C  
ATOM    132  CE1 PHE B   2       6.484  28.774   2.583  1.00 50.12           C  
ATOM    133  CE2 PHE B   2       5.442  30.281   4.125  1.00 45.36           C  
ATOM    134  CZ  PHE B   2       6.060  30.053   2.903  1.00 48.80           C  
HETATM  135  N   AIB B   3       2.612  24.605   6.553  1.00 28.84           N  
HETATM  136  CA  AIB B   3       1.780  23.730   7.269  1.00 30.29           C  
HETATM  137  C   AIB B   3       1.469  22.494   6.359  1.00 27.68           C  
HETATM  138  O1  AIB B   3       1.822  21.383   6.683  1.00 31.21           O  
HETATM  139  CB1 AIB B   3       0.404  24.344   7.608  1.00 39.62           C  
HETATM  140  CB2 AIB B   3       2.423  23.175   8.543  1.00 39.95           C  
HETATM  141  N   AIB B   4       0.977  22.871   5.191  1.00 21.13           N  
HETATM  142  CA  AIB B   4       0.806  21.893   4.119  1.00 26.81           C  
HETATM  143  C   AIB B   4       2.182  21.241   3.860  1.00 26.03           C  
HETATM  144  O1  AIB B   4       2.277  20.061   3.609  1.00 23.45           O  
HETATM  145  CB1 AIB B   4       0.415  22.647   2.835  1.00 25.87           C  
HETATM  146  CB2 AIB B   4      -0.197  20.829   4.493  1.00 29.60           C  
HETATM  147  N   AIB B   5       3.215  22.120   3.879  1.00 17.16           N  
HETATM  148  CA  AIB B   5       4.511  21.589   3.452  1.00 15.10           C  
HETATM  149  C   AIB B   5       4.928  20.396   4.293  1.00  9.75           C  
HETATM  150  O1  AIB B   5       5.249  19.314   3.752  1.00 10.68           O  
HETATM  151  CB1 AIB B   5       5.568  22.677   3.485  1.00 14.02           C  
HETATM  152  CB2 AIB B   5       4.315  21.110   1.972  1.00 19.92           C  
HETATM  153  N   DIV B   6       4.963  20.569   5.604  1.00  7.57           N  
HETATM  154  CA  DIV B   6       5.401  19.558   6.529  1.00  8.21           C  
HETATM  155  CB1 DIV B   6       6.886  19.276   6.417  1.00 10.05           C  
HETATM  156  CG1 DIV B   6       7.792  20.473   6.710  1.00 14.33           C  
HETATM  157  CB2 DIV B   6       5.049  19.986   7.977  1.00 10.30           C  
HETATM  158  C   DIV B   6       4.644  18.251   6.251  1.00  8.19           C  
HETATM  159  O   DIV B   6       5.182  17.157   6.236  1.00  7.86           O  
ATOM    160  N   GLY B   7       3.316  18.385   6.075  1.00  6.46           N  
ATOM    161  CA  GLY B   7       2.443  17.239   5.931  1.00  7.68           C  
ATOM    162  C   GLY B   7       2.679  16.447   4.655  1.00  8.32           C  
ATOM    163  O   GLY B   7       2.580  15.227   4.648  1.00  8.71           O  
ATOM    164  N   LEU B   8       2.966  17.149   3.551  1.00  6.85           N  
ATOM    165  CA  LEU B   8       3.168  16.442   2.276  1.00  6.67           C  
ATOM    166  C   LEU B   8       4.502  15.737   2.188  1.00  6.52           C  
ATOM    167  O   LEU B   8       4.624  14.656   1.581  1.00  6.34           O  
ATOM    168  CB  LEU B   8       2.990  17.446   1.125  1.00  9.41           C  
ATOM    169  CG  LEU B   8       1.631  18.187   1.170  1.00  9.79           C  
ATOM    170  CD1 LEU B   8       1.465  19.094  -0.021  1.00 13.50           C  
ATOM    171  CD2 LEU B   8       0.484  17.207   1.304  1.00 14.37           C  
HETATM  172  N   AIB B   9       5.548  16.307   2.799  1.00  6.56           N  
HETATM  173  CA  AIB B   9       6.852  15.712   2.909  1.00  5.48           C  
HETATM  174  C   AIB B   9       6.835  14.494   3.813  1.00  6.95           C  
HETATM  175  O1  AIB B   9       7.565  13.522   3.611  1.00  6.68           O  
HETATM  176  CB1 AIB B   9       7.808  16.749   3.575  1.00  7.60           C  
HETATM  177  CB2 AIB B   9       7.430  15.347   1.532  1.00  7.93           C  
HETATM  178  N   AIB B  10       6.011  14.587   4.878  1.00  5.09           N  
HETATM  179  CA  AIB B  10       6.137  13.658   6.017  1.00  5.66           C  
HETATM  180  C   AIB B  10       6.248  12.207   5.647  1.00  5.17           C  
HETATM  181  O1  AIB B  10       7.122  11.494   6.236  1.00  5.95           O  
HETATM  182  CB1 AIB B  10       4.917  13.883   6.935  1.00  6.85           C  
HETATM  183  CB2 AIB B  10       7.428  14.077   6.810  1.00  6.63           C  
HETATM  184  N   HYP B  11       5.415  11.643   4.799  1.00  4.51           N  
HETATM  185  CA  HYP B  11       5.483  10.202   4.542  1.00  6.03           C  
HETATM  186  C   HYP B  11       6.795   9.767   3.916  1.00  8.18           C  
HETATM  187  O   HYP B  11       7.079   8.549   3.902  1.00  7.49           O  
HETATM  188  CB  HYP B  11       4.328   9.923   3.590  1.00  7.79           C  
HETATM  189  CG  HYP B  11       3.401  11.092   3.732  1.00  4.97           C  
HETATM  190  CD  HYP B  11       4.332  12.263   4.034  1.00  4.93           C  
HETATM  191  OD  HYP B  11       2.551  10.876   4.916  1.00  6.05           O  
ATOM    192  N   GLN B  12       7.567  10.679   3.352  1.00  6.63           N  
ATOM    193  CA  GLN B  12       8.850  10.274   2.747  1.00  5.77           C  
ATOM    194  C   GLN B  12       9.980  10.282   3.738  1.00  5.60           C  
ATOM    195  O   GLN B  12      11.080   9.745   3.411  1.00  7.87           O  
ATOM    196  CB  GLN B  12       9.170  11.244   1.593  1.00  6.51           C  
ATOM    197  CG  GLN B  12       8.013  11.438   0.611  1.00  6.31           C  
ATOM    198  CD  GLN B  12       7.370  10.189   0.127  1.00  7.07           C  
ATOM    199  OE1 GLN B  12       8.104   9.173  -0.156  1.00  9.28           O  
ATOM    200  NE2 GLN B  12       6.068  10.100   0.027  1.00  7.28           N  
HETATM  201  N   DIV B  13       9.830  10.804   4.941  1.00  5.65           N  
HETATM  202  CA  DIV B  13      10.873  10.914   5.934  1.00  5.28           C  
HETATM  203  CB1 DIV B  13      11.941  11.949   5.483  1.00  7.70           C  
HETATM  204  CG1 DIV B  13      11.297  13.303   5.149  1.00 11.10           C  
HETATM  205  CB2 DIV B  13      10.266  11.396   7.275  1.00  7.30           C  
HETATM  206  C   DIV B  13      11.616   9.613   6.189  1.00  7.25           C  
HETATM  207  O   DIV B  13      12.813   9.628   6.476  1.00  8.66           O  
HETATM  208  N   HYP B  14      10.928   8.457   6.201  1.00  6.47           N  
HETATM  209  CA  HYP B  14      11.632   7.219   6.508  1.00  8.28           C  
HETATM  210  C   HYP B  14      12.565   6.719   5.428  1.00 10.34           C  
HETATM  211  O   HYP B  14      13.320   5.761   5.758  1.00 11.64           O  
HETATM  212  CB  HYP B  14      10.535   6.172   6.760  1.00  9.09           C  
HETATM  213  CG  HYP B  14       9.316   7.013   7.131  1.00  7.61           C  
HETATM  214  CD  HYP B  14       9.447   8.234   6.201  1.00  5.53           C  
HETATM  215  OD  HYP B  14       9.419   7.423   8.500  1.00  9.83           O  
HETATM  216  N   AIB B  15      12.524   7.257   4.234  1.00 10.66           N  
HETATM  217  CA  AIB B  15      13.325   6.713   3.103  1.00 11.53           C  
HETATM  218  C   AIB B  15      14.764   6.441   3.459  1.00  9.90           C  
HETATM  219  O1  AIB B  15      15.283   5.340   3.096  1.00 12.59           O  
HETATM  220  CB1 AIB B  15      13.270   7.708   1.931  1.00 12.28           C  
HETATM  221  CB2 AIB B  15      12.634   5.383   2.694  1.00 14.81           C  
ATOM    222  N   PRO B  16      15.488   7.310   4.102  1.00 10.42           N  
ATOM    223  CA  PRO B  16      16.912   6.996   4.392  1.00  9.30           C  
ATOM    224  C   PRO B  16      17.140   6.032   5.514  1.00 11.65           C  
ATOM    225  O   PRO B  16      18.318   5.587   5.684  1.00 13.90           O  
ATOM    226  CB  PRO B  16      17.531   8.328   4.691  1.00 13.60           C  
ATOM    227  CG  PRO B  16      16.504   9.364   4.525  1.00 14.88           C  
ATOM    228  CD  PRO B  16      15.175   8.674   4.611  1.00 13.40           C  
HETATM  229  C   PHL B  17      15.775   3.475   7.194  1.00 21.21           C  
HETATM  230  O   PHL B  17      16.542   2.697   6.392  1.00 21.67           O  
HETATM  231  CA  PHL B  17      16.323   4.855   7.486  1.00 13.92           C  
HETATM  232  N   PHL B  17      16.133   5.718   6.298  1.00  9.75           N  
HETATM  233  CB  PHL B  17      15.610   5.514   8.681  1.00 16.99           C  
HETATM  234  CG  PHL B  17      16.010   6.930   8.916  1.00 10.79           C  
HETATM  235  CD1 PHL B  17      17.183   7.212   9.645  1.00 14.32           C  
HETATM  236  CD2 PHL B  17      15.295   8.012   8.463  1.00 11.28           C  
HETATM  237  CE1 PHL B  17      17.565   8.517   9.860  1.00 15.52           C  
HETATM  238  CE2 PHL B  17      15.670   9.312   8.636  1.00 13.03           C  
HETATM  239  CZ  PHL B  17      16.860   9.577   9.334  1.00 16.57           C  
TER     240      PHL B  17                                                      
HETATM  241  C   MOH     1      -9.104  19.596   2.871  1.00 32.55           C  
HETATM  242  O   MOH     1      -9.039  19.786   4.245  1.00 13.06           O  
HETATM  243  C   MOH     2      14.846   2.101   2.670  1.00 38.93           C  
HETATM  244  O   MOH     2      14.655   2.391   4.036  1.00 31.98           O  
HETATM  245  C   MOH     3     -15.131  17.431   4.958  1.00 16.57           C  
HETATM  246  O   MOH     3     -16.001  17.489   6.099  1.00 24.27           O  
HETATM  247  C   MOH     4     -16.077  15.353  10.500  1.00 18.86           C  
HETATM  248  O   MOH     4     -15.846  14.932   9.164  1.00 31.76           O  
HETATM  249  C   MOH     5       8.576   6.323   1.956  1.00 19.11           C  
HETATM  250  O   MOH     5       7.320   6.849   1.620  1.00 32.20           O  
HETATM  251  C   MOH     6      -7.258  10.203  12.697  1.00 15.38           C  
HETATM  252  O   MOH     6      -7.658  11.552  12.569  1.00 23.12           O  
HETATM  253  C   MOH     7      -2.431  16.770   5.992  1.00 34.52           C  
HETATM  254  O   MOH     7      -2.152  18.081   5.549  1.00 45.41           O  
HETATM  255  O   MOH     8      -3.148  -0.104  11.715  1.00 37.97           O  
HETATM  256  O   MOH     9       4.341  28.668   8.342  1.00 41.90           O  
HETATM  257  O   MOH    10      -2.572  19.932   3.594  1.00 59.74           O  
HETATM  258  O   MOH    11      11.917   2.498   5.871  1.00 47.73           O  
HETATM  259  O   MOH    12      -6.707  19.782   2.905  1.00 45.01           O  
HETATM  260  O   MOH    13      14.848   5.767   8.783  1.00 38.20           O  
HETATM  261  O   MOH    14       9.031   3.274   5.523  1.00 46.44           O  
HETATM  262  O   MOH    15      -6.975  23.471   4.885  1.00 56.37           O  
HETATM  263  O   MOH    16      -1.900  22.062   1.538  1.00 51.92           O  
HETATM  264  O   MOH    17      12.172   2.480   8.190  1.00 54.82           O  
HETATM  265  O   MOH    18      -2.782  20.731   8.046  1.00 53.23           O  
HETATM  266  O   MOH    19       8.255   4.166   9.062  1.00 48.65           O  
HETATM  267  O   MOH    20       9.578   0.127   8.470  1.00 57.75           O  
HETATM  268  O   MOH    21       8.367   4.496   1.820  1.00 71.46           O  
HETATM  269  O   MOH    22       9.293   0.709  10.916  1.00 59.91           O  
HETATM  270  O   MOH    23      12.757  -0.012   5.636  1.00 49.42           O  
CONECT    1    2    3    4                                                      
CONECT    2    1                                                                
CONECT    3    1                                                                
CONECT    4    1    5                                                           
CONECT    6    5    7   15                                                      
CONECT   15    6   16                                                           
CONECT   16   15   17   19   20                                                 
CONECT   17   16   18   21                                                      
CONECT   18   17                                                                
CONECT   19   16                                                                
CONECT   20   16                                                                
CONECT   21   17   22                                                           
CONECT   22   21   23   25   26                                                 
CONECT   23   22   24   27                                                      
CONECT   24   23                                                                
CONECT   25   22                                                                
CONECT   26   22                                                                
CONECT   27   23   28                                                           
CONECT   28   27   29   31   32                                                 
CONECT   29   28   30   33                                                      
CONECT   30   29                                                                
CONECT   31   28                                                                
CONECT   32   28                                                                
CONECT   33   29   34                                                           
CONECT   34   33   35   37   38                                                 
CONECT   35   34   36                                                           
CONECT   36   35                                                                
CONECT   37   34                                                                
CONECT   38   34   39   40                                                      
CONECT   39   38                                                                
CONECT   40   38   41                                                           
CONECT   46   45   47   52                                                      
CONECT   52   46   53                                                           
CONECT   53   52   54   56   57                                                 
CONECT   54   53   55   58                                                      
CONECT   55   54                                                                
CONECT   56   53                                                                
CONECT   57   53                                                                
CONECT   58   54   59                                                           
CONECT   59   58   60   62   63                                                 
CONECT   60   59   61   64                                                      
CONECT   61   60                                                                
CONECT   62   59                                                                
CONECT   63   59                                                                
CONECT   64   60   65   70                                                      
CONECT   65   64   66   68                                                      
CONECT   66   65   67   72                                                      
CONECT   67   66                                                                
CONECT   68   65   69                                                           
CONECT   69   68   70   71                                                      
CONECT   70   64   69                                                           
CONECT   71   69                                                                
CONECT   72   66   73                                                           
CONECT   74   73   75   81                                                      
CONECT   81   74   82                                                           
CONECT   82   81   83   85   86                                                 
CONECT   83   82   84                                                           
CONECT   84   83                                                                
CONECT   85   82                                                                
CONECT   86   82   87   88                                                      
CONECT   87   86                                                                
CONECT   88   86   89   94                                                      
CONECT   89   88   90   92                                                      
CONECT   90   89   91   96                                                      
CONECT   91   90                                                                
CONECT   92   89   93                                                           
CONECT   93   92   94   95                                                      
CONECT   94   88   93                                                           
CONECT   95   93                                                                
CONECT   96   90   97                                                           
CONECT   97   96   98  100  101                                                 
CONECT   98   97   99  102                                                      
CONECT   99   98                                                                
CONECT  100   97                                                                
CONECT  101   97                                                                
CONECT  102   98  103  108                                                      
CONECT  104  103  105  112                                                      
CONECT  109  110  111                                                           
CONECT  110  109                                                                
CONECT  111  109  112  113                                                      
CONECT  112  104  111                                                           
CONECT  113  111  114                                                           
CONECT  114  113  115  116                                                      
CONECT  115  114  117                                                           
CONECT  116  114  118                                                           
CONECT  117  115  119                                                           
CONECT  118  116  119                                                           
CONECT  119  117  118                                                           
CONECT  121  122  123  124                                                      
CONECT  122  121                                                                
CONECT  123  121                                                                
CONECT  124  121  125                                                           
CONECT  126  125  127  135                                                      
CONECT  135  126  136                                                           
CONECT  136  135  137  139  140                                                 
CONECT  137  136  138  141                                                      
CONECT  138  137                                                                
CONECT  139  136                                                                
CONECT  140  136                                                                
CONECT  141  137  142                                                           
CONECT  142  141  143  145  146                                                 
CONECT  143  142  144  147                                                      
CONECT  144  143                                                                
CONECT  145  142                                                                
CONECT  146  142                                                                
CONECT  147  143  148                                                           
CONECT  148  147  149  151  152                                                 
CONECT  149  148  150  153                                                      
CONECT  150  149                                                                
CONECT  151  148                                                                
CONECT  152  148                                                                
CONECT  153  149  154                                                           
CONECT  154  153  155  157  158                                                 
CONECT  155  154  156                                                           
CONECT  156  155                                                                
CONECT  157  154                                                                
CONECT  158  154  159  160                                                      
CONECT  159  158                                                                
CONECT  160  158  161                                                           
CONECT  166  165  167  172                                                      
CONECT  172  166  173                                                           
CONECT  173  172  174  176  177                                                 
CONECT  174  173  175  178                                                      
CONECT  175  174                                                                
CONECT  176  173                                                                
CONECT  177  173                                                                
CONECT  178  174  179                                                           
CONECT  179  178  180  182  183                                                 
CONECT  180  179  181  184                                                      
CONECT  181  180                                                                
CONECT  182  179                                                                
CONECT  183  179                                                                
CONECT  184  180  185  190                                                      
CONECT  185  184  186  188                                                      
CONECT  186  185  187  192                                                      
CONECT  187  186                                                                
CONECT  188  185  189                                                           
CONECT  189  188  190  191                                                      
CONECT  190  184  189                                                           
CONECT  191  189                                                                
CONECT  192  186  193                                                           
CONECT  194  193  195  201                                                      
CONECT  201  194  202                                                           
CONECT  202  201  203  205  206                                                 
CONECT  203  202  204                                                           
CONECT  204  203                                                                
CONECT  205  202                                                                
CONECT  206  202  207  208                                                      
CONECT  207  206                                                                
CONECT  208  206  209  214                                                      
CONECT  209  208  210  212                                                      
CONECT  210  209  211  216                                                      
CONECT  211  210                                                                
CONECT  212  209  213                                                           
CONECT  213  212  214  215                                                      
CONECT  214  208  213                                                           
CONECT  215  213                                                                
CONECT  216  210  217                                                           
CONECT  217  216  218  220  221                                                 
CONECT  218  217  219  222                                                      
CONECT  219  218                                                                
CONECT  220  217                                                                
CONECT  221  217                                                                
CONECT  222  218  223  228                                                      
CONECT  224  223  225  232                                                      
CONECT  229  230  231                                                           
CONECT  230  229                                                                
CONECT  231  229  232  233                                                      
CONECT  232  224  231                                                           
CONECT  233  231  234                                                           
CONECT  234  233  235  236                                                      
CONECT  235  234  237                                                           
CONECT  236  234  238                                                           
CONECT  237  235  239                                                           
CONECT  238  236  239                                                           
CONECT  239  237  238                                                           
CONECT  241  242                                                                
CONECT  242  241                                                                
CONECT  243  244                                                                
CONECT  244  243                                                                
CONECT  245  246                                                                
CONECT  246  245                                                                
CONECT  247  248                                                                
CONECT  248  247                                                                
CONECT  249  250                                                                
CONECT  250  249                                                                
CONECT  251  252                                                                
CONECT  252  251                                                                
CONECT  253  254                                                                
CONECT  254  253                                                                
MASTER      224    0   47    2    0    2    0    9  268    2  190    4          
END                                                                             
