HEADER    ANTIBIOTIC/ION CHANNEL                  24-JAN-03   1OB6              
TITLE     CEPHAIBOL B                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CEPHAIBOL B;                                               
COMPND   3 CHAIN: A, B                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ACREMONIUM TUBAKII                              
KEYWDS    CEPHAIBOL, PEPTAIBOL, ANTIBIOTIC, ION CHANNEL                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BUNKOCZI,M.SCHIELL,L.VERTESY,G.M.SHELDRICK                          
REVDAT   1   11-DEC-03 1OB6    0                                                
JRNL        AUTH   G.BUNKOCZI,M.SCHIELL,L.VERTESY,G.M.SHELDRICK                 
JRNL        TITL   CRYSTAL STRUCTURES OF CEPHAIBOLS                             
JRNL        REF    J.PEPT.SCI.                   V.   9   745 2003              
JRNL        REFN   ASTM JPSIEI  UK ISSN 1075-2617                               
REMARK   2                                                                      
REMARK   2 RESOLUTION. 0.89 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : SHELXL-97                                            
REMARK   3   AUTHORS     : G.M.SHELDRICK                                        
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 0.89                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.4                           
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.0                            
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.0                           
REMARK   3   CROSS-VALIDATION METHOD           : RFREE                          
REMARK   3   FREE R VALUE TEST SET SELECTION   : THIN SHELLS                    
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (NO CUTOFF).                         
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.0746                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : 0.0744                 
REMARK   3   FREE R VALUE                  (NO CUTOFF) : 0.0793                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : 5                      
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : 778                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 16045                  
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL FOR DATA WITH F>4SIG(F).                     
REMARK   3   R VALUE   (WORKING + TEST SET, F>4SIG(F)) : 0.0709                 
REMARK   3   R VALUE          (WORKING SET, F>4SIG(F)) : 0.0706                 
REMARK   3   FREE R VALUE                  (F>4SIG(F)) : 0.0756                 
REMARK   3   FREE R VALUE TEST SET SIZE (%, F>4SIG(F)) : 5                      
REMARK   3   FREE R VALUE TEST SET COUNT   (F>4SIG(F)) : 738                    
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (F>4SIG(F)) : 14248                  
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 96                                      
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 219                                     
REMARK   3   SOLVENT ATOMS            : 26                                      
REMARK   3                                                                      
REMARK   3  MODEL REFINEMENT.                                                   
REMARK   3   OCCUPANCY SUM OF NON-HYDROGEN ATOMS      : 267.5                   
REMARK   3   OCCUPANCY SUM OF HYDROGEN ATOMS          : 252                     
REMARK   3   NUMBER OF DISCRETELY DISORDERED RESIDUES : 10                      
REMARK   3   NUMBER OF LEAST-SQUARES PARAMETERS       : 3121                    
REMARK   3   NUMBER OF RESTRAINTS                     : 4640                    
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM RESTRAINT TARGET VALUES.                        
REMARK   3   BOND LENGTHS                         (A) : 0.021                   
REMARK   3   ANGLE DISTANCES                      (A) : 0.040                   
REMARK   3   SIMILAR DISTANCES (NO TARGET VALUES) (A) : 0.012                   
REMARK   3   DISTANCES FROM RESTRAINT PLANES      (A) : 0.505                   
REMARK   3   ZERO CHIRAL VOLUMES               (A**3) : 0.131                   
REMARK   3   NON-ZERO CHIRAL VOLUMES           (A**3) : 0.093                   
REMARK   3   ANTI-BUMPING DISTANCE RESTRAINTS     (A) : 0.050                   
REMARK   3   RIGID-BOND ADP COMPONENTS         (A**2) : 0.006                   
REMARK   3   SIMILAR ADP COMPONENTS            (A**2) : 0.040                   
REMARK   3   APPROXIMATELY ISOTROPIC ADPS      (A**2) : NULL                    
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED: MOEWS & KRETSINGER                                    
REMARK   3                                                                      
REMARK   3  STEREOCHEMISTRY TARGET VALUES : ENGH AND HUBER                      
REMARK   3   SPECIAL CASE: RESTRAINTS FOR AIB, DIV, HYP AND PHL FROM            
REMARK   3   ANTIAMOEBIN (PDB 1JOH)                                             
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1OB6 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY EBI  ON 29-JAN-2003.                
REMARK 100 THE EBI ID CODE IS EBI-12026.                                        
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAY-2002                        
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER M06XCE                      
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD SMART6000                      
REMARK 200  DETECTOR MANUFACTURER          : BRUKER                             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SAINT                              
REMARK 200  DATA SCALING SOFTWARE          : SADABS                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16045                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 0.89                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.4                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY                : 4.44                               
REMARK 200  R MERGE                    (I) : 0.0437                             
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.29                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 0.89                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.16                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.0786                             
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 10.37                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: DIRECT METHODS               
REMARK 200 SOFTWARE USED: SHELXD                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): 20                                         
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAAC/HAC PH=4.6,                   
REMARK 280  32% ETOH                                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-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   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        4.56300            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 295                                                                      
REMARK 295 NON-CRYSTALLOGRAPHIC SYMMETRY                                        
REMARK 295 THE TRANSFORMATIONS PRESENTED ON THE MTRIX RECORDS BELOW             
REMARK 295 DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG ATOMS              
REMARK 295 IN THIS ENTRY.  APPLYING THE APPROPRIATE MTRIX                       
REMARK 295 TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD               
REMARK 295 APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND.              
REMARK 295 CHAIN IDENTIFIERS GIVEN AS "?" REFER TO CHAINS FOR WHICH             
REMARK 295 ATOMS ARE NOT FOUND IN THIS ENTRY.                                   
REMARK 295                                                                      
REMARK 295               APPLIED TO          TRANSFORMED TO                     
REMARK 295   TRANSFORM CHAIN  RESIDUES       CHAIN  RESIDUES     RMSD           
REMARK 295     SSS                                                              
REMARK 295    M  1       A    1 ..  17         B    1 ..  17     0.388          
REMARK 295                                                                      
REMARK 295    WHERE SSS -> COLUMNS 8-10 OF MTRIX RECORDS                        
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF   2 CHAIN(S). SEE REMARK 350 FOR                   
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 300                                                                      
REMARK 300 QUATERNARY STRUCTURE FOR THIS ENTRY: MONOMERIC                       
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 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 350 BIOMOLECULE:  2                                                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES ARE GIVEN CHAIN IDENTIFIERS TO                 
REMARK 525 INDICATE THE PROTEIN CHAIN TO WHICH THEY ARE MOST CLOSELY            
REMARK 525 ASSOCIATED WITH:                                                     
REMARK 525   PROTEIN CHAIN  SOLVENT CHAIN                                       
REMARK 525     A              Z                                                 
REMARK 525     B              Y                                                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1OB4   RELATED DB: PDB                                   
REMARK 900  CEPHAIBOL A                                                         
REMARK 900 RELATED ID: 1OB7   RELATED DB: PDB                                   
REMARK 900  CEPHAIBOL C                                                         
DBREF  1OB6 A    1    17  PDB    1OB6     1OB6             1     17             
DBREF  1OB6 B    1    17  PDB    1OB6     1OB6             1     17             
SEQRES   1 A   17  ACE PHE AIB AIB AIB DIV GLY LEU DIV AIB HYP GLN DIV          
SEQRES   2 A   17  HYP AIB PRO PHL                                              
SEQRES   1 B   17  ACE PHE AIB AIB AIB DIV GLY LEU DIV AIB HYP GLN DIV          
SEQRES   2 B   17  HYP AIB PRO PHL                                              
MODRES 1OB6 AIB A    3  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 AIB A    4  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 AIB A    5  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 DIV A    6  VAL  D-ISOVALINE                                        
MODRES 1OB6 DIV A    9  VAL  D-ISOVALINE                                        
MODRES 1OB6 AIB A   10  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 HYP A   11  PRO  4-HYDROXYPROLINE                                   
MODRES 1OB6 DIV A   13  VAL  D-ISOVALINE                                        
MODRES 1OB6 HYP A   14  PRO  4-HYDROXYPROLINE                                   
MODRES 1OB6 AIB A   15  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 PHL A   17  PHE  L-PHENYLALANINOL                                   
MODRES 1OB6 AIB B    3  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 AIB B    4  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 AIB B    5  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 DIV B    6  VAL  D-ISOVALINE                                        
MODRES 1OB6 DIV B    9  VAL  D-ISOVALINE                                        
MODRES 1OB6 AIB B   10  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 HYP B   11  PRO  4-HYDROXYPROLINE                                   
MODRES 1OB6 DIV B   13  VAL  D-ISOVALINE                                        
MODRES 1OB6 HYP B   14  PRO  4-HYDROXYPROLINE                                   
MODRES 1OB6 AIB B   15  ALA  ALPHA-AMINOISOBUTYRIC ACID                         
MODRES 1OB6 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    DIV  A   9       7                                                       
HET    AIB  A  10       6                                                       
HET    HYP  A  11      12                                                       
HET    DIV  A  13      14                                                       
HET    HYP  A  14      16                                                       
HET    AIB  A  15      12                                                       
HET    PHL  A  17      22                                                       
HET    ACE  B   1       6                                                       
HET    AIB  B   3      12                                                       
HET    AIB  B   4       7                                                       
HET    AIB  B   5       6                                                       
HET    DIV  B   6       7                                                       
HET    DIV  B   9       7                                                       
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      12                                                       
HET    EOH  A  29       3                                                       
HET    ACT  B  29       4                                                       
HET    EOH  B  30       3                                                       
HETNAM     ACE ACETYL GROUP                                                     
HETNAM     AIB ALPHA-AMINOISOBUTYRIC ACID                                       
HETNAM     DIV D-ISOVALINE                                                      
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM     PHL L-PHENYLALANINOL                                                 
HETNAM     EOH ETHANOL                                                          
HETNAM     ACT ACETATE ION                                                      
FORMUL   3  ACE    2(C2 H3 O1)                                                  
FORMUL   5  AIB    10(C4 H9 N1 O2)                                              
FORMUL   6  DIV    6(C5 H11 N1 O2)                                              
FORMUL   7  HYP    4(C5 H9 N1 O3)                                               
FORMUL   8  PHL    2(C9 H13 N1 O1)                                              
FORMUL   9  EOH    2(C2 H6 O1)                                                  
FORMUL  10  ACT    C2 H3 O2 1-                                                  
FORMUL  11  HOH   *26(H2 O1)                                                    
LINK         C   ACE A   1                 N   PHE A   2     1555   1555        
LINK         C   PHE A   2                 N   AIB A   3     1555   1555        
LINK         C   AIB A   3                 N   AIB A   4     1555   1555        
LINK         C   AIB A   4                 N   AIB A   5     1555   1555        
LINK         C   AIB A   5                 N   DIV A   6     1555   1555        
LINK         C   DIV A   6                 N   GLY A   7     1555   1555        
LINK         C   LEU A   8                 N   DIV A   9     1555   1555        
LINK         C   DIV A   9                 N   AIB A  10     1555   1555        
LINK         C   AIB A  10                 N   HYP A  11     1555   1555        
LINK         C   HYP A  11                 N   GLN A  12     1555   1555        
LINK         C   GLN A  12                 N  ADIV A  13     1555   1555        
LINK         C   GLN A  12                 N  BDIV A  13     1555   1555        
LINK         C  ADIV A  13                 N  BHYP A  14     1555   1555        
LINK         C  BDIV A  13                 N  AHYP A  14     1555   1555        
LINK         C  ADIV A  13                 N  AHYP A  14     1555   1555        
LINK         C  BDIV A  13                 N  BHYP A  14     1555   1555        
LINK         C  BHYP A  14                 N  BAIB A  15     1555   1555        
LINK         C  AHYP A  14                 N  AAIB A  15     1555   1555        
LINK         C  BAIB A  15                 N  APRO A  16     1555   1555        
LINK         C  AAIB A  15                 N  APRO A  16     1555   1555        
LINK         C  BAIB A  15                 N  BPRO A  16     1555   1555        
LINK         C  AAIB A  15                 N  BPRO A  16     1555   1555        
LINK         C  BPRO A  16                 N  BPHL A  17     1555   1555        
LINK         C  APRO A  16                 N  APHL A  17     1555   1555        
LINK         C  AACE B   1                 N  APHE B   2     1555   1555        
LINK         C  BACE B   1                 N  BPHE B   2     1555   1555        
LINK         CH3BACE B   1                 N  APHE B   2     1555   1555        
LINK         C  BACE B   1                 N  APHE B   2     1555   1555        
LINK         C  APHE B   2                 N  AAIB B   3     1555   1555        
LINK         C  APHE B   2                 N  BAIB B   3     1555   1555        
LINK         C  BPHE B   2                 N  BAIB B   3     1555   1555        
LINK         C  BAIB B   3                 N  BAIB B   4     1555   1555        
LINK         C  AAIB B   3                 N  BAIB B   4     1555   1555        
LINK         C  BAIB B   3                 N  AAIB B   4     1555   1555        
LINK         C  AAIB B   3                 N  AAIB B   4     1555   1555        
LINK         C   AIB B   4                 N   AIB B   5     1555   1555        
LINK         C   AIB B   5                 N   DIV B   6     1555   1555        
LINK         C   DIV B   6                 N   GLY B   7     1555   1555        
LINK         C   LEU B   8                 N   DIV B   9     1555   1555        
LINK         C   DIV B   9                 N   AIB B  10     1555   1555        
LINK         C   AIB B  10                 N   HYP B  11     1555   1555        
LINK         C   HYP B  11                 N   GLN B  12     1555   1555        
LINK         C   GLN B  12                 N   DIV B  13     1555   1555        
LINK         C   DIV B  13                 N   HYP B  14     1555   1555        
LINK         C   HYP B  14                 N   AIB B  15     1555   1555        
LINK         C   AIB B  15                 N   PRO B  16     1555   1555        
LINK         C   PRO B  16                 N   PHL B  17     1555   1555        
CRYST1   32.146    9.126   37.982  90.00 111.36  90.00 P 1 21 1      4          
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      0.031108  0.000000  0.012166        0.00000                         
SCALE2      0.000000  0.109577  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.028270        0.00000                         
MTRIX1   1  0.994460  0.016940  0.103710       19.39953    1                    
MTRIX2   1 -0.016340  0.999840 -0.006660        5.28985    1                    
MTRIX3   1 -0.103810  0.004930  0.994580      -19.99939    1                    
HETATM    1  C   ACE A   1      12.098   7.057  11.245  1.00  4.77           C  
HETATM    2  O   ACE A   1      11.031   6.503  11.546  1.00  4.92           O  
HETATM    3  CH3 ACE A   1      13.049   6.496  10.256  1.00  5.71           C  
ATOM      4  N   PHE A   2      12.471   8.202  11.818  1.00  4.38           N  
ATOM      5  CA  PHE A   2      11.663   8.758  12.872  1.00  4.16           C  
ATOM      6  C   PHE A   2      10.304   9.229  12.375  1.00  3.38           C  
ATOM      7  O   PHE A   2       9.323   9.132  13.081  1.00  3.22           O  
ATOM      8  CB  PHE A   2      12.433   9.892  13.568  1.00  4.53           C  
ATOM      9  CG  PHE A   2      11.708  10.380  14.808  1.00  4.05           C  
ATOM     10  CD1 PHE A   2      10.898  11.476  14.792  1.00  4.30           C  
ATOM     11  CD2 PHE A   2      11.830   9.644  15.989  1.00  5.08           C  
ATOM     12  CE1 PHE A   2      10.197  11.876  15.905  1.00  4.90           C  
ATOM     13  CE2 PHE A   2      11.145  10.053  17.117  1.00  5.31           C  
ATOM     14  CZ  PHE A   2      10.325  11.152  17.083  1.00  4.76           C  
HETATM   15  N   AIB A   3      10.270   9.785  11.147  1.00  3.97           N  
HETATM   16  CA  AIB A   3       9.013  10.310  10.585  1.00  4.07           C  
HETATM   17  C   AIB A   3       7.970   9.171  10.601  1.00  3.37           C  
HETATM   18  O1  AIB A   3       6.852   9.335  11.071  1.00  3.50           O  
HETATM   19  CB1 AIB A   3       9.257  10.747   9.150  1.00  5.61           C  
HETATM   20  CB2 AIB A   3       8.543  11.500  11.396  1.00  4.85           C  
HETATM   21  N   AIB A   4       8.368   8.015  10.063  1.00  3.74           N  
HETATM   22  CA  AIB A   4       7.491   6.847   9.959  1.00  3.80           C  
HETATM   23  C   AIB A   4       7.015   6.463  11.377  1.00  3.20           C  
HETATM   24  O1  AIB A   4       5.829   6.188  11.609  1.00  3.43           O  
HETATM   25  CB1 AIB A   4       8.317   5.684   9.419  1.00  4.72           C  
HETATM   26  CB2 AIB A   4       6.282   7.112   9.052  1.00  4.79           C  
HETATM   27  N   AIB A   5       7.965   6.410  12.324  1.00  2.85           N  
HETATM   28  CA  AIB A   5       7.691   6.039  13.715  1.00  2.99           C  
HETATM   29  C   AIB A   5       6.560   6.932  14.273  1.00  2.60           C  
HETATM   30  O1  AIB A   5       5.539   6.445  14.786  1.00  3.12           O  
HETATM   31  CB1 AIB A   5       8.975   6.256  14.523  1.00  2.95           C  
HETATM   32  CB2 AIB A   5       7.282   4.573  13.816  1.00  3.40           C  
HETATM   33  N   DIV A   6       6.770   8.245  14.196  1.00  2.74           N  
HETATM   34  CA  DIV A   6       5.801   9.218  14.709  1.00  2.91           C  
HETATM   35  CB1 DIV A   6       5.735   9.172  16.252  1.00  3.12           C  
HETATM   36  CG1 DIV A   6       6.973   9.741  16.929  1.00  4.11           C  
HETATM   37  CB2 DIV A   6       6.227  10.612  14.242  1.00  3.24           C  
HETATM   38  C   DIV A   6       4.420   8.928  14.089  1.00  2.90           C  
HETATM   39  O   DIV A   6       3.373   8.913  14.742  1.00  3.36           O  
ATOM     40  N   GLY A   7       4.419   8.782  12.761  1.00  3.12           N  
ATOM     41  CA  GLY A   7       3.167   8.691  12.044  1.00  3.38           C  
ATOM     42  C   GLY A   7       2.375   7.442  12.345  1.00  3.19           C  
ATOM     43  O   GLY A   7       1.133   7.476  12.369  1.00  4.21           O  
ATOM     44  N   LEU A   8       3.046   6.330  12.533  1.00  3.08           N  
ATOM     45  CA  LEU A   8       2.372   5.075  12.821  1.00  2.92           C  
ATOM     46  C   LEU A   8       1.909   4.979  14.267  1.00  3.14           C  
ATOM     47  O   LEU A   8       0.857   4.413  14.535  1.00  3.82           O  
ATOM     48  CB  LEU A   8       3.266   3.896  12.441  1.00  3.09           C  
ATOM     49  CG  LEU A   8       3.452   3.763  10.926  1.00  3.40           C  
ATOM     50  CD1 LEU A   8       4.665   2.884  10.623  1.00  4.82           C  
ATOM     51  CD2 LEU A   8       2.223   3.174  10.270  1.00  4.22           C  
HETATM   52  N   DIV A   9       2.702   5.515  15.200  1.00  2.80           N  
HETATM   53  CA  DIV A   9       2.337   5.510  16.630  1.00  2.68           C  
HETATM   54  CB1 DIV A   9       2.134   4.097  17.180  1.00  3.63           C  
HETATM   55  CG1 DIV A   9       3.274   3.143  16.851  1.00  4.38           C  
HETATM   56  CB2 DIV A   9       3.486   6.222  17.378  1.00  3.14           C  
HETATM   57  C   DIV A   9       1.083   6.375  16.849  1.00  2.84           C  
HETATM   58  O   DIV A   9       0.235   6.046  17.678  1.00  3.19           O  
HETATM   59  N   AIB A  10       1.045   7.524  16.168  1.00  2.98           N  
HETATM   60  CA  AIB A  10       0.191   8.652  16.591  1.00  3.47           C  
HETATM   61  C   AIB A  10      -1.264   8.225  16.771  1.00  3.38           C  
HETATM   62  O1  AIB A  10      -1.916   8.615  17.750  1.00  3.80           O  
HETATM   63  CB1 AIB A  10       0.278   9.768  15.551  1.00  4.07           C  
HETATM   64  CB2 AIB A  10       0.739   9.162  17.932  1.00  3.95           C  
HETATM   65  N   HYP A  11      -1.866   7.473  15.827  1.00  3.78           N  
HETATM   66  CA  HYP A  11      -3.308   7.205  15.953  1.00  4.29           C  
HETATM   67  C   HYP A  11      -3.696   6.359  17.132  1.00  4.02           C  
HETATM   68  O   HYP A  11      -4.893   6.227  17.430  1.00  5.11           O  
HETATM   69  CB AHYP A  11      -3.650   6.461  14.641  0.86  6.05           C  
HETATM   70  CG AHYP A  11      -2.553   6.899  13.663  0.86  6.00           C  
HETATM   71  CD AHYP A  11      -1.336   6.927  14.547  0.86  4.26           C  
HETATM   72  OD AHYP A  11      -2.850   8.240  13.215  0.86  8.62           O  
HETATM   73  CB BHYP A  11      -3.851   6.745  14.625  0.14  6.65           C  
HETATM   74  CG BHYP A  11      -2.591   6.247  13.977  0.14  4.77           C  
HETATM   75  CD BHYP A  11      -1.521   7.261  14.396  0.14  4.55           C  
HETATM   76  OD BHYP A  11      -2.733   6.351  12.565  0.14  8.97           O  
ATOM     77  N   GLN A  12      -2.725   5.733  17.800  1.00  3.55           N  
ATOM     78  CA  GLN A  12      -2.999   4.921  18.952  1.00  3.81           C  
ATOM     79  C   GLN A  12      -2.876   5.678  20.281  1.00  4.34           C  
ATOM     80  O   GLN A  12      -3.156   5.085  21.331  1.00  5.22           O  
ATOM     81  CB  GLN A  12      -2.124   3.671  18.966  1.00  4.38           C  
ATOM     82  CG  GLN A  12      -2.441   2.731  17.801  1.00  4.98           C  
ATOM     83  CD  GLN A  12      -3.834   2.171  17.828  1.00  4.42           C  
ATOM     84  OE1 GLN A  12      -4.389   1.819  16.703  1.00  6.61           O  
ATOM     85  NE2 GLN A  12      -4.409   2.027  18.919  1.00  4.54           N  
HETATM   86  N  ADIV A  13      -2.618   6.981  20.283  0.56  4.17           N  
HETATM   87  CA ADIV A  13      -2.542   7.731  21.550  0.56  4.83           C  
HETATM   88  CB1ADIV A  13      -1.344   7.244  22.372  0.56  6.64           C  
HETATM   89  CG1ADIV A  13      -0.017   7.383  21.615  0.56  9.57           C  
HETATM   90  CB2ADIV A  13      -2.343   9.236  21.180  0.56  5.44           C  
HETATM   91  C  ADIV A  13      -3.789   7.615  22.396  0.56  4.08           C  
HETATM   92  O  ADIV A  13      -3.698   7.539  23.629  0.56  4.82           O  
HETATM   93  N  BDIV A  13      -2.394   6.915  20.196  0.44  4.34           N  
HETATM   94  CA BDIV A  13      -2.292   7.756  21.385  0.44  4.33           C  
HETATM   95  CB1BDIV A  13      -1.188   7.216  22.301  0.44  4.16           C  
HETATM   96  CG1BDIV A  13       0.193   7.186  21.632  0.44  5.06           C  
HETATM   97  CB2BDIV A  13      -1.985   9.222  20.973  0.44  4.49           C  
HETATM   98  C  BDIV A  13      -3.604   7.769  22.166  0.44  5.02           C  
HETATM   99  O  BDIV A  13      -3.593   7.874  23.416  0.44  4.58           O  
HETATM  100  N  AHYP A  14      -5.004   7.420  21.811  0.56  4.15           N  
HETATM  101  CA AHYP A  14      -6.175   7.223  22.647  0.56  4.10           C  
HETATM  102  C  AHYP A  14      -6.263   5.944  23.403  0.56  4.14           C  
HETATM  103  O  AHYP A  14      -7.182   5.832  24.273  0.56  4.90           O  
HETATM  104  CB AHYP A  14      -7.385   7.300  21.702  0.56  4.90           C  
HETATM  105  CG AHYP A  14      -6.880   8.289  20.649  0.56  4.75           C  
HETATM  106  CD AHYP A  14      -5.447   7.851  20.466  0.56  4.37           C  
HETATM  107  OD AHYP A  14      -6.977   9.557  21.292  0.56  5.84           O  
HETATM  108  N  BHYP A  14      -4.794   7.759  21.539  0.44  3.71           N  
HETATM  109  CA BHYP A  14      -6.021   7.791  22.337  0.44  3.85           C  
HETATM  110  C  BHYP A  14      -6.264   6.558  23.147  0.44  3.72           C  
HETATM  111  O  BHYP A  14      -7.205   6.539  23.990  0.44  3.82           O  
HETATM  112  CB BHYP A  14      -7.138   7.912  21.287  0.44  4.01           C  
HETATM  113  CG BHYP A  14      -6.461   8.622  20.121  0.44  4.35           C  
HETATM  114  CD BHYP A  14      -5.123   8.004  20.116  0.44  3.62           C  
HETATM  115  OD BHYP A  14      -6.406   9.998  20.508  0.44  4.46           O  
HETATM  116  N  AAIB A  15      -5.433   4.961  23.129  0.56  4.94           N  
HETATM  117  CA AAIB A  15      -5.755   3.569  23.553  0.56  5.70           C  
HETATM  118  C  AAIB A  15      -6.031   3.450  25.057  0.56  4.48           C  
HETATM  119  O1 AAIB A  15      -6.963   2.685  25.413  0.56  6.15           O  
HETATM  120  CB1AAIB A  15      -4.553   2.660  23.274  0.56  7.17           C  
HETATM  121  CB2AAIB A  15      -7.014   3.076  22.774  0.56  7.35           C  
HETATM  122  N  BAIB A  15      -5.589   5.449  22.897  0.44  3.97           N  
HETATM  123  CA BAIB A  15      -6.004   4.116  23.316  0.44  4.17           C  
HETATM  124  C  BAIB A  15      -6.332   3.963  24.814  0.44  3.15           C  
HETATM  125  O1 BAIB A  15      -7.295   3.226  25.090  0.44  3.78           O  
HETATM  126  CB1BAIB A  15      -4.854   3.118  23.103  0.44  5.45           C  
HETATM  127  CB2BAIB A  15      -7.271   3.781  22.462  0.44  5.31           C  
ATOM    128  N  APRO A  16      -5.417   4.232  25.946  0.56  5.60           N  
ATOM    129  CA APRO A  16      -5.933   4.132  27.325  0.56  5.22           C  
ATOM    130  C  APRO A  16      -7.030   5.103  27.702  0.56  4.25           C  
ATOM    131  O  APRO A  16      -7.423   4.956  28.880  0.56  5.31           O  
ATOM    132  CB APRO A  16      -4.640   4.392  28.117  0.56  5.38           C  
ATOM    133  CG APRO A  16      -3.987   5.500  27.317  0.56  5.85           C  
ATOM    134  CD APRO A  16      -4.248   5.123  25.872  0.56  5.79           C  
ATOM    135  N  BPRO A  16      -5.502   4.342  25.811  0.44  5.07           N  
ATOM    136  CA BPRO A  16      -5.649   3.912  27.232  0.44  5.04           C  
ATOM    137  C  BPRO A  16      -6.677   4.674  28.045  0.44  4.21           C  
ATOM    138  O  BPRO A  16      -6.807   4.541  29.255  0.44  5.81           O  
ATOM    139  CB BPRO A  16      -4.266   4.219  27.857  0.44  5.21           C  
ATOM    140  CG BPRO A  16      -3.909   5.488  27.111  0.44  5.39           C  
ATOM    141  CD BPRO A  16      -4.309   5.221  25.662  0.44  5.53           C  
HETATM  142  N  APHL A  17      -7.483   5.990  26.868  0.56  4.48           N  
HETATM  143  CA APHL A  17      -8.469   6.996  27.272  0.56  5.96           C  
HETATM  144  C  APHL A  17      -9.891   6.632  26.796  0.56  8.27           C  
HETATM  145  O  APHL A  17     -10.329   5.416  27.342  0.56  7.12           O  
HETATM  146  CB APHL A  17      -8.010   8.342  26.741  0.56  6.16           C  
HETATM  147  CG APHL A  17      -6.629   8.808  27.139  0.56  5.12           C  
HETATM  148  CD1APHL A  17      -6.396   9.196  28.426  0.56  5.96           C  
HETATM  149  CD2APHL A  17      -5.599   8.936  26.228  0.56  5.91           C  
HETATM  150  CE1APHL A  17      -5.181   9.666  28.859  0.56  6.70           C  
HETATM  151  CE2APHL A  17      -4.314   9.271  26.672  0.56  5.93           C  
HETATM  152  CZ APHL A  17      -4.125   9.638  27.976  0.56  4.44           C  
HETATM  153  N  BPHL A  17      -7.326   5.547  27.327  0.44  4.31           N  
HETATM  154  CA BPHL A  17      -8.243   6.511  27.920  0.44  4.44           C  
HETATM  155  C  BPHL A  17      -9.683   6.006  27.819  0.44  5.39           C  
HETATM  156  O  BPHL A  17      -9.907   4.754  28.419  0.44  6.32           O  
HETATM  157  CB BPHL A  17      -8.055   7.905  27.324  0.44  4.70           C  
HETATM  158  CG BPHL A  17      -6.673   8.486  27.474  0.44  3.24           C  
HETATM  159  CD1BPHL A  17      -6.217   9.056  28.638  0.44  3.44           C  
HETATM  160  CD2BPHL A  17      -5.758   8.405  26.451  0.44  4.14           C  
HETATM  161  CE1BPHL A  17      -4.941   9.554  28.767  0.44  4.17           C  
HETATM  162  CE2BPHL A  17      -4.517   9.007  26.506  0.44  5.00           C  
HETATM  163  CZ BPHL A  17      -4.077   9.555  27.680  0.44  5.18           C  
TER     164      PHL A  17                                                      
HETATM  165  C  AACE B   1     -10.106   2.254  28.362  0.50  4.94           C  
HETATM  166  O  AACE B   1     -11.115   1.560  28.464  0.50  6.28           O  
HETATM  167  CH3AACE B   1      -9.196   2.472  27.215  0.50  9.57           C  
HETATM  168  C  BACE B   1     -10.506   2.156  30.337  0.50 12.12           C  
HETATM  169  O  BACE B   1     -11.545   1.460  30.341  0.50 12.89           O  
HETATM  170  CH3BACE B   1      -9.430   1.926  29.296  0.50 23.74           C  
ATOM    171  N  APHE B   2      -9.698   3.041  29.389  0.50  4.61           N  
ATOM    172  CA APHE B   2     -10.399   3.013  30.674  0.50  4.33           C  
ATOM    173  C  APHE B   2     -11.796   3.609  30.514  0.50  3.48           C  
ATOM    174  O  APHE B   2     -12.617   3.229  31.346  0.50  4.15           O  
ATOM    175  CB APHE B   2      -9.555   3.714  31.716  0.50  5.57           C  
ATOM    176  CG APHE B   2      -8.225   2.995  31.939  0.50  4.87           C  
ATOM    177  CD1APHE B   2      -7.035   3.586  31.672  0.50  4.11           C  
ATOM    178  CD2APHE B   2      -8.193   1.706  32.427  0.50  5.45           C  
ATOM    179  CE1APHE B   2      -5.771   2.978  31.810  0.50  5.28           C  
ATOM    180  CE2APHE B   2      -6.980   1.087  32.603  0.50  5.11           C  
ATOM    181  CZ APHE B   2      -5.784   1.653  32.362  0.50  4.46           C  
ATOM    182  N  BPHE B   2     -10.302   3.254  30.994  0.50 10.19           N  
ATOM    183  CA BPHE B   2     -11.406   3.602  31.895  0.50  6.50           C  
ATOM    184  C  BPHE B   2     -12.634   3.999  31.075  0.50  4.73           C  
ATOM    185  O  BPHE B   2     -13.700   4.040  31.661  0.50  5.36           O  
ATOM    186  CB BPHE B   2     -10.846   4.715  32.775  0.50  7.12           C  
ATOM    187  CG BPHE B   2     -10.432   5.974  32.121  0.50  5.74           C  
ATOM    188  CD1BPHE B   2     -11.387   6.905  31.694  0.50  6.80           C  
ATOM    189  CD2BPHE B   2      -9.115   6.245  31.866  0.50  5.56           C  
ATOM    190  CE1BPHE B   2     -10.998   8.030  31.083  0.50  6.92           C  
ATOM    191  CE2BPHE B   2      -8.626   7.416  31.322  0.50  6.65           C  
ATOM    192  CZ BPHE B   2      -9.679   8.229  30.883  0.50  6.52           C  
HETATM  193  N  AAIB B   3     -12.090   4.382  29.458  0.50  3.68           N  
HETATM  194  CA AAIB B   3     -13.454   4.904  29.293  0.50  4.69           C  
HETATM  195  C  AAIB B   3     -14.479   3.752  29.340  0.50  4.52           C  
HETATM  196  O1 AAIB B   3     -15.553   3.948  29.936  0.50  4.03           O  
HETATM  197  CB1AAIB B   3     -13.589   5.545  27.911  0.50  4.88           C  
HETATM  198  CB2AAIB B   3     -13.766   5.990  30.358  0.50  4.25           C  
HETATM  199  N  BAIB B   3     -12.436   4.430  29.814  0.50  4.77           N  
HETATM  200  CA BAIB B   3     -13.584   4.841  29.000  0.50  4.63           C  
HETATM  201  C  BAIB B   3     -14.628   3.716  29.046  0.50  4.06           C  
HETATM  202  O1 BAIB B   3     -15.789   3.857  29.415  0.50  3.44           O  
HETATM  203  CB1BAIB B   3     -13.156   5.000  27.535  0.50  7.05           C  
HETATM  204  CB2BAIB B   3     -14.247   6.100  29.528  0.50  6.44           C  
HETATM  205  CA  AIB B   4     -15.077   1.427  28.571  1.00  4.64           C  
HETATM  206  C   AIB B   4     -15.636   1.085  29.948  1.00  3.90           C  
HETATM  207  O1  AIB B   4     -16.813   0.750  30.099  1.00  4.14           O  
HETATM  208  CB1 AIB B   4     -14.270   0.202  28.090  1.00  5.46           C  
HETATM  209  CB2 AIB B   4     -16.225   1.688  27.578  1.00  6.00           C  
HETATM  210  N  AAIB B   4     -14.210   2.595  28.721  0.50  4.39           N  
HETATM  211  N  BAIB B   4     -14.165   2.555  28.593  0.50  4.91           N  
HETATM  212  N   AIB B   5     -14.774   1.095  30.974  1.00  3.71           N  
HETATM  213  CA  AIB B   5     -15.156   0.725  32.334  1.00  3.66           C  
HETATM  214  C   AIB B   5     -16.364   1.566  32.761  1.00  3.24           C  
HETATM  215  O1  AIB B   5     -17.396   1.053  33.187  1.00  3.66           O  
HETATM  216  CB1 AIB B   5     -13.965   1.018  33.272  1.00  4.48           C  
HETATM  217  CB2 AIB B   5     -15.503  -0.760  32.400  1.00  4.74           C  
HETATM  218  N   DIV B   6     -16.188   2.886  32.666  1.00  3.47           N  
HETATM  219  CA  DIV B   6     -17.209   3.847  33.099  1.00  3.45           C  
HETATM  220  CB1 DIV B   6     -17.436   3.776  34.600  1.00  4.09           C  
HETATM  221  CG1 DIV B   6     -16.219   4.115  35.452  1.00  6.29           C  
HETATM  222  CB2 DIV B   6     -16.741   5.248  32.684  1.00  4.14           C  
HETATM  223  C   DIV B   6     -18.501   3.563  32.333  1.00  3.08           C  
HETATM  224  O   DIV B   6     -19.608   3.526  32.874  1.00  3.46           O  
ATOM    225  N   GLY B   7     -18.371   3.411  31.001  1.00  3.32           N  
ATOM    226  CA  GLY B   7     -19.555   3.305  30.177  1.00  3.44           C  
ATOM    227  C   GLY B   7     -20.337   2.018  30.371  1.00  3.26           C  
ATOM    228  O   GLY B   7     -21.578   2.029  30.248  1.00  3.97           O  
ATOM    229  N   LEU B   8     -19.644   0.928  30.641  1.00  3.07           N  
ATOM    230  CA  LEU B   8     -20.315  -0.350  30.860  1.00  3.12           C  
ATOM    231  C   LEU B   8     -20.933  -0.441  32.249  1.00  3.24           C  
ATOM    232  O   LEU B   8     -21.992  -1.036  32.412  1.00  4.20           O  
ATOM    233  CB  LEU B   8     -19.340  -1.503  30.590  1.00  3.33           C  
ATOM    234  CG  LEU B   8     -18.986  -1.673  29.103  1.00  3.45           C  
ATOM    235  CD1 LEU B   8     -17.778  -2.570  28.942  1.00  4.11           C  
ATOM    236  CD2 LEU B   8     -20.193  -2.229  28.335  1.00  4.33           C  
HETATM  237  N   DIV B   9     -20.252   0.117  33.258  1.00  2.98           N  
HETATM  238  CA  DIV B   9     -20.769   0.103  34.635  1.00  3.21           C  
HETATM  239  CB1 DIV B   9     -21.036  -1.321  35.143  1.00  3.86           C  
HETATM  240  CG1 DIV B   9     -19.886  -2.287  34.864  1.00  4.85           C  
HETATM  241  CB2 DIV B   9     -19.720   0.786  35.529  1.00  3.82           C  
HETATM  242  C   DIV B   9     -22.030   0.971  34.745  1.00  3.04           C  
HETATM  243  O   DIV B   9     -22.936   0.690  35.527  1.00  3.25           O  
HETATM  244  N   AIB B  10     -22.013   2.119  34.025  1.00  3.31           N  
HETATM  245  CA  AIB B  10     -22.868   3.260  34.380  1.00  3.28           C  
HETATM  246  C   AIB B  10     -24.336   2.865  34.513  1.00  2.94           C  
HETATM  247  O1  AIB B  10     -25.015   3.310  35.440  1.00  3.27           O  
HETATM  248  CB1 AIB B  10     -22.722   4.351  33.301  1.00  4.26           C  
HETATM  249  CB2 AIB B  10     -22.366   3.811  35.728  1.00  3.91           C  
HETATM  250  N   HYP B  11     -24.913   2.091  33.574  1.00  3.47           N  
HETATM  251  CA  HYP B  11     -26.361   1.843  33.649  1.00  3.93           C  
HETATM  252  C   HYP B  11     -26.804   1.029  34.847  1.00  3.63           C  
HETATM  253  O   HYP B  11     -28.006   0.956  35.113  1.00  5.10           O  
HETATM  254  CB  HYP B  11     -26.666   1.100  32.344  1.00  5.42           C  
HETATM  255  CG  HYP B  11     -25.506   1.457  31.414  1.00  5.35           C  
HETATM  256  CD  HYP B  11     -24.342   1.494  32.339  1.00  4.10           C  
HETATM  257  OD  HYP B  11     -25.727   2.778  30.874  1.00  5.81           O  
ATOM    258  N   GLN B  12     -25.846   0.425  35.551  1.00  3.22           N  
ATOM    259  CA  GLN B  12     -26.127  -0.353  36.751  1.00  3.09           C  
ATOM    260  C   GLN B  12     -25.999   0.453  38.037  1.00  3.01           C  
ATOM    261  O   GLN B  12     -26.286  -0.098  39.111  1.00  3.61           O  
ATOM    262  CB  GLN B  12     -25.260  -1.611  36.801  1.00  3.82           C  
ATOM    263  CG  GLN B  12     -25.508  -2.529  35.622  1.00  4.39           C  
ATOM    264  CD  GLN B  12     -26.902  -3.101  35.568  1.00  4.46           C  
ATOM    265  OE1 GLN B  12     -27.339  -3.484  34.389  1.00  7.34           O  
ATOM    266  NE2 GLN B  12     -27.568  -3.196  36.619  1.00  4.25           N  
HETATM  267  N   DIV B  13     -25.597   1.725  37.970  1.00  3.22           N  
HETATM  268  CA  DIV B  13     -25.491   2.581  39.155  1.00  3.26           C  
HETATM  269  CB1 DIV B  13     -24.356   2.091  40.054  1.00  3.60           C  
HETATM  270  CG1 DIV B  13     -22.972   2.106  39.379  1.00  4.62           C  
HETATM  271  CB2 DIV B  13     -25.269   4.041  38.722  1.00  3.83           C  
HETATM  272  C   DIV B  13     -26.804   2.532  39.960  1.00  3.28           C  
HETATM  273  O   DIV B  13     -26.787   2.563  41.203  1.00  3.88           O  
HETATM  274  N   HYP B  14     -28.001   2.436  39.322  1.00  3.37           N  
HETATM  275  CA  HYP B  14     -29.211   2.422  40.102  1.00  4.34           C  
HETATM  276  C   HYP B  14     -29.416   1.178  40.942  1.00  4.32           C  
HETATM  277  O   HYP B  14     -30.381   1.201  41.748  1.00  5.04           O  
HETATM  278  CB  HYP B  14     -30.314   2.559  39.042  1.00  5.54           C  
HETATM  279  CG  HYP B  14     -29.656   3.351  37.932  1.00  5.47           C  
HETATM  280  CD  HYP B  14     -28.312   2.725  37.895  1.00  4.02           C  
HETATM  281  OD  HYP B  14     -29.543   4.711  38.323  1.00  8.19           O  
HETATM  282  N   AIB B  15     -28.675   0.110  40.760  1.00  3.95           N  
HETATM  283  CA  AIB B  15     -29.037  -1.218  41.255  1.00  4.81           C  
HETATM  284  C   AIB B  15     -29.465  -1.205  42.737  1.00  4.04           C  
HETATM  285  O1  AIB B  15     -30.494  -1.793  43.092  1.00  4.50           O  
HETATM  286  CB1 AIB B  15     -27.833  -2.155  41.114  1.00  6.15           C  
HETATM  287  CB2 AIB B  15     -30.215  -1.708  40.405  1.00  6.78           C  
ATOM    288  N   PRO B  16     -28.689  -0.619  43.684  1.00  3.63           N  
ATOM    289  CA  PRO B  16     -29.107  -0.726  45.087  1.00  4.06           C  
ATOM    290  C   PRO B  16     -30.230   0.219  45.483  1.00  3.59           C  
ATOM    291  O   PRO B  16     -30.755   0.097  46.604  1.00  4.28           O  
ATOM    292  CB  PRO B  16     -27.826  -0.328  45.866  1.00  4.67           C  
ATOM    293  CG  PRO B  16     -27.189   0.702  44.967  1.00  4.91           C  
ATOM    294  CD  PRO B  16     -27.392   0.087  43.571  1.00  4.78           C  
HETATM  295  N   PHL B  17     -30.523   1.183  44.637  1.00  4.06           N  
HETATM  296  CA  PHL B  17     -31.442   2.287  44.934  1.00  4.53           C  
HETATM  297  C   PHL B  17     -32.826   1.922  44.485  1.00  6.73           C  
HETATM  298  CB  PHL B  17     -30.948   3.559  44.231  1.00  4.01           C  
HETATM  299  CG  PHL B  17     -29.588   4.026  44.649  1.00  3.80           C  
HETATM  300  CD1 PHL B  17     -28.497   3.911  43.812  1.00  4.65           C  
HETATM  301  CD2 PHL B  17     -29.391   4.588  45.907  1.00  4.59           C  
HETATM  302  CE1 PHL B  17     -27.233   4.361  44.179  1.00  5.12           C  
HETATM  303  CE2 PHL B  17     -28.125   5.048  46.272  1.00  5.52           C  
HETATM  304  CZ  PHL B  17     -27.046   4.934  45.415  1.00  5.87           C  
HETATM  305  O  APHL B  17     -33.720   2.906  44.951  0.55  4.76           O  
HETATM  306  O  BPHL B  17     -33.431   0.764  44.805  0.45  4.63           O  
TER     307      PHL B  17                                                      
HETATM  308  C1  EOH A  29      -1.090   8.638  11.074  1.00 33.73           C  
HETATM  309  C2  EOH A  29      -2.410   8.608  10.450  1.00 14.39           C  
HETATM  310  O   EOH A  29      -0.216   9.736  11.405  1.00  9.68           O  
HETATM  311  C   ACT B  29     -29.646  -1.260  49.461  1.00 12.93           C  
HETATM  312  O   ACT B  29     -30.304  -1.892  48.408  1.00  7.01           O  
HETATM  313  OXT ACT B  29     -29.632  -0.048  49.761  1.00 29.45           O  
HETATM  314  CH3 ACT B  29     -28.591  -2.131  49.931  1.00 19.43           C  
HETATM  315  C1  EOH B  30     -31.534  -4.838  49.941  1.00 13.45           C  
HETATM  316  C2  EOH B  30     -31.639  -4.321  48.552  1.00  6.16           C  
HETATM  317  O   EOH B  30     -32.373  -3.821  50.573  1.00 35.09           O  
HETATM  318  O   HOH Y   1     -23.115   4.129  29.349  1.00 10.67           O  
HETATM  319  O  AHOH Y   2     -23.258  -0.257  29.074  0.50  3.01           O  
HETATM  320  O   HOH Y   3     -23.401  -2.550  30.610  1.00  5.84           O  
HETATM  321  O   HOH Y   4     -29.694  -5.226  34.114  1.00 18.00           O  
HETATM  322  O  AHOH Y   5     -11.844  -0.548  25.890  0.50 56.93           O  
HETATM  323  O  AHOH Y   6     -11.948   1.703  26.336  0.50 20.76           O  
HETATM  324  O   HOH Y   7     -25.786   5.539  31.797  1.00  7.86           O  
HETATM  325  O   HOH Y   8     -26.816   2.130  28.489  1.00  5.82           O  
HETATM  326  O   HOH Y   9     -32.884   2.284  41.092  1.00 11.39           O  
HETATM  327  O  AHOH Y  10     -34.030   4.200  42.624  0.50  4.05           O  
HETATM  328  O  AHOH Y  11     -33.977   3.926  47.332  0.50  3.62           O  
HETATM  329  O   HOH Y  12     -35.146  -1.157  43.540  1.00  7.12           O  
HETATM  330  O   HOH Z   1      -5.733   2.305  31.968  0.50 20.99           O  
HETATM  331  O   HOH Z   2      -0.746   2.969  12.849  1.00  7.64           O  
HETATM  332  O   HOH Z   3      -7.625   3.418  31.508  0.50 11.90           O  
HETATM  333  O  AHOH Z   4      -8.989   7.494  31.292  0.50 22.45           O  
HETATM  334  O  BHOH Z   5      -0.779   5.908  10.626  0.50 18.72           O  
HETATM  335  O   HOH Z   6     -10.900  -0.302  24.142  0.50 15.35           O  
HETATM  336  O   HOH Z   7      -7.229   4.142  18.750  0.50 10.13           O  
HETATM  337  O  AHOH Z   8      -6.907   5.101  18.960  0.50  4.01           O  
HETATM  338  O   HOH Z   9      -2.953  10.850  14.138  1.00  9.78           O  
HETATM  339  O   HOH Z  10      -9.609   5.968  23.975  0.50 37.60           O  
HETATM  340  O  AHOH Z  11      -9.792   7.093  23.665  0.50 30.63           O  
HETATM  341  O  AHOH Z  12      -6.851  11.466  19.413  0.50  3.92           O  
HETATM  342  O  BHOH Z  13      -9.510   2.859  26.446  0.50 17.21           O  
HETATM  343  O  AHOH Z  14      -8.420   0.902  23.781  0.50  7.13           O  
CONECT    4    1                                                                
CONECT    6   15                                                                
CONECT   15   16    6                                                           
CONECT   16   15   17   19   20                                                 
CONECT   17   16   18   21                                                      
CONECT   18   17                                                                
CONECT   19   16                                                                
CONECT   20   16                                                                
CONECT   21   22   17                                                           
CONECT   22   21   23   25   26                                                 
CONECT   23   22   24   27                                                      
CONECT   24   23                                                                
CONECT   25   22                                                                
CONECT   26   22                                                                
CONECT   27   28   23                                                           
CONECT   28   27   29   31   32                                                 
CONECT   29   28   30   33                                                      
CONECT   30   29                                                                
CONECT   31   28                                                                
CONECT   32   28                                                                
CONECT   33   34   29                                                           
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                                                                
CONECT   46   52                                                                
CONECT   52   53   46                                                           
CONECT   53   52   54   56   57                                                 
CONECT   54   53   55                                                           
CONECT   55   54                                                                
CONECT   56   53                                                                
CONECT   57   53   58   59                                                      
CONECT   58   57                                                                
CONECT   59   57   60                                                           
CONECT   60   59   61   63   64                                                 
CONECT   61   65   60   62                                                      
CONECT   62   61                                                                
CONECT   63   60                                                                
CONECT   64   60                                                                
CONECT   65   66   71   75   61                                                 
CONECT   66   65   67   69   73                                                 
CONECT   67   66   68   77                                                      
CONECT   68   67                                                                
CONECT   69   66   70                                                           
CONECT   70   69   71   72                                                      
CONECT   71   65   70                                                           
CONECT   72   70                                                                
CONECT   73   66   74                                                           
CONECT   74   73   75   76                                                      
CONECT   75   65   74                                                           
CONECT   76   74                                                                
CONECT   77   67                                                                
CONECT   79   86   93                                                           
CONECT   86   87   79                                                           
CONECT   87   86   88   90   91                                                 
CONECT   88   87   89                                                           
CONECT   89   88                                                                
CONECT   90   87                                                                
CONECT   91  108   87   92  100                                                 
CONECT   92   91                                                                
CONECT   93   94   79                                                           
CONECT   94   93   95   97   98                                                 
CONECT   95   94   96                                                           
CONECT   96   95                                                                
CONECT   97   94                                                                
CONECT   98   94   99  100  108                                                 
CONECT   99   98                                                                
CONECT  100  101  106   98   91                                                 
CONECT  101  100  102  104                                                      
CONECT  102  116  101  103                                                      
CONECT  103  102                                                                
CONECT  104  101  105                                                           
CONECT  105  104  106  107                                                      
CONECT  106  100  105                                                           
CONECT  107  105                                                                
CONECT  108  109  114   91   98                                                 
CONECT  109  108  110  112                                                      
CONECT  110  109  111  122                                                      
CONECT  111  110                                                                
CONECT  112  109  113                                                           
CONECT  113  112  114  115                                                      
CONECT  114  108  113                                                           
CONECT  115  113                                                                
CONECT  116  117  102                                                           
CONECT  117  116  118  120  121                                                 
CONECT  118  117  119  128  135                                                 
CONECT  119  118                                                                
CONECT  120  117                                                                
CONECT  121  117                                                                
CONECT  122  110  123                                                           
CONECT  123  122  124  126  127                                                 
CONECT  124  135  123  125  128                                                 
CONECT  125  124                                                                
CONECT  126  123                                                                
CONECT  127  123                                                                
CONECT  128  118  124                                                           
CONECT  130  142                                                                
CONECT  135  118  124                                                           
CONECT  137  153                                                                
CONECT  142  130  143                                                           
CONECT  143  142  144  146                                                      
CONECT  144  143  145                                                           
CONECT  145  144                                                                
CONECT  146  143  147                                                           
CONECT  147  146  148  149                                                      
CONECT  148  147  150                                                           
CONECT  149  147  151                                                           
CONECT  150  148  152                                                           
CONECT  151  149  152                                                           
CONECT  152  150  151                                                           
CONECT  153  137  154                                                           
CONECT  154  153  155  157                                                      
CONECT  155  154  156                                                           
CONECT  156  155                                                                
CONECT  157  154  158                                                           
CONECT  158  157  159  160                                                      
CONECT  159  158  161                                                           
CONECT  160  158  162                                                           
CONECT  161  159  163                                                           
CONECT  162  160  163                                                           
CONECT  163  161  162                                                           
CONECT  171  170  165  168                                                      
CONECT  173  193  199                                                           
CONECT  182  168                                                                
CONECT  184  199                                                                
CONECT  193  173  194                                                           
CONECT  194  193  195  197  198                                                 
CONECT  195  194  196  210  211                                                 
CONECT  196  195                                                                
CONECT  197  194                                                                
CONECT  198  194                                                                
CONECT  199  200  173  184                                                      
CONECT  200  199  201  203  204                                                 
CONECT  201  211  200  202  210                                                 
CONECT  202  201                                                                
CONECT  203  200                                                                
CONECT  204  200                                                                
CONECT  205  206  208  209  210  211                                            
CONECT  206  205  207  212                                                      
CONECT  207  206                                                                
CONECT  208  205                                                                
CONECT  209  205                                                                
CONECT  210  201  205  195                                                      
CONECT  211  195  201  205                                                      
CONECT  212  206  213                                                           
CONECT  213  212  214  216  217                                                 
CONECT  214  213  215  218                                                      
CONECT  215  214                                                                
CONECT  216  213                                                                
CONECT  217  213                                                                
CONECT  218  214  219                                                           
CONECT  219  218  220  222  223                                                 
CONECT  220  219  221                                                           
CONECT  221  220                                                                
CONECT  222  219                                                                
CONECT  223  225  219  224                                                      
CONECT  224  223                                                                
CONECT  225  223                                                                
CONECT  231  237                                                                
CONECT  237  231  238                                                           
CONECT  238  237  239  241  242                                                 
CONECT  239  238  240                                                           
CONECT  240  239                                                                
CONECT  241  238                                                                
CONECT  242  244  238  243                                                      
CONECT  243  242                                                                
CONECT  244  242  245                                                           
CONECT  245  244  246  248  249                                                 
CONECT  246  250  245  247                                                      
CONECT  247  246                                                                
CONECT  248  245                                                                
CONECT  249  245                                                                
CONECT  250  246  251  256                                                      
CONECT  251  250  252  254                                                      
CONECT  252  258  251  253                                                      
CONECT  253  252                                                                
CONECT  254  251  255                                                           
CONECT  255  254  256  257                                                      
CONECT  256  250  255                                                           
CONECT  257  255                                                                
CONECT  258  252                                                                
CONECT  260  267                                                                
CONECT  267  260  268                                                           
CONECT  268  267  269  271  272                                                 
CONECT  269  268  270                                                           
CONECT  270  269                                                                
CONECT  271  268                                                                
CONECT  272  274  268  273                                                      
CONECT  273  272                                                                
CONECT  274  272  275  280                                                      
CONECT  275  274  276  278                                                      
CONECT  276  282  275  277                                                      
CONECT  277  276                                                                
CONECT  278  275  279                                                           
CONECT  279  278  280  281                                                      
CONECT  280  274  279                                                           
CONECT  281  279                                                                
CONECT  282  276  283                                                           
CONECT  283  282  284  286  287                                                 
CONECT  284  288  283  285                                                      
CONECT  285  284                                                                
CONECT  286  283                                                                
CONECT  287  283                                                                
CONECT  288  284                                                                
CONECT  290  295                                                                
CONECT  295  290  296                                                           
CONECT  296  295  297  298                                                      
CONECT  297  296  306  305                                                      
CONECT  298  296  299                                                           
CONECT  299  298  300  301                                                      
CONECT  300  299  302                                                           
CONECT  301  299  303                                                           
CONECT  302  300  304                                                           
CONECT  303  301  304                                                           
CONECT  304  302  303                                                           
CONECT  305  297                                                                
CONECT  306  297                                                                
CONECT    1    2    3    4                                                      
CONECT    2    1                                                                
CONECT    3    1                                                                
CONECT  308  309  310                                                           
CONECT  309  308                                                                
CONECT  310  308                                                                
CONECT  165  166  167  171                                                      
CONECT  166  165                                                                
CONECT  167  165                                                                
CONECT  168  169  170  182  171                                                 
CONECT  169  168                                                                
CONECT  170  171  168                                                           
CONECT  311  312  313  314                                                      
CONECT  312  311                                                                
CONECT  313  311                                                                
CONECT  314  311                                                                
CONECT  315  316  317                                                           
CONECT  316  315                                                                
CONECT  317  315                                                                
MASTER      205    0   27    0    0    0    0    9  341    2  239    4          
END                                                                             
