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Database: PDB
Entry: 4HW3
LinkDB: 4HW3
Original site: 4HW3 
HEADER    APOPTOSIS/INHIBITOR                     07-NOV-12   4HW3              
TITLE     DISCOVERY OF POTENT MCL-1 INHIBITORS USING FRAGMENT-BASED METHODS AND 
TITLE    2 STRUCTURE-BASED DESIGN                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INDUCED MYELOID LEUKEMIA CELL DIFFERENTIATION PROTEIN MCL- 
COMPND   3 1;                                                                   
COMPND   4 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   5 SYNONYM: BCL-2-LIKE PROTEIN 3, BCL2-L-3, BCL-2-RELATED PROTEIN       
COMPND   6 EAT/MCL1, MCL1/EAT;                                                  
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MCL1, BCL2L3;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODONPLUS (DE3)-RIL;                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDEST-HISMBP                              
KEYWDS    REGULATION OF APOPTOSIS, MAINTENANCE OF VIABILITY, APOPTOSIS,         
KEYWDS   2 APOPTOSIS-INHIBITOR COMPLEX                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    B.ZHAO                                                                
REVDAT   2   06-MAR-13 4HW3    1       JRNL                                     
REVDAT   1   09-JAN-13 4HW3    0                                                
JRNL        AUTH   A.FRIBERG,D.VIGIL,B.ZHAO,R.N.DANIELS,J.P.BURKE,              
JRNL        AUTH 2 P.M.GARCIA-BARRANTES,D.CAMPER,B.A.CHAUDER,T.LEE,             
JRNL        AUTH 3 E.T.OLEJNICZAK,S.W.FESIK                                     
JRNL        TITL   DISCOVERY OF POTENT MYELOID CELL LEUKEMIA 1 (MCL-1)          
JRNL        TITL 2 INHIBITORS USING FRAGMENT-BASED METHODS AND STRUCTURE-BASED  
JRNL        TITL 3 DESIGN.                                                      
JRNL        REF    J.MED.CHEM.                   V.  56    15 2013              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23244564                                                     
JRNL        DOI    10.1021/JM301448P                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8_1069)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.460                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 88346                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.260                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2001                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9826 -  5.7717    0.99     6505   151  0.1779 0.2156        
REMARK   3     2  5.7717 -  4.5864    1.00     6319   148  0.1989 0.2356        
REMARK   3     3  4.5864 -  4.0082    1.00     6304   146  0.1882 0.2237        
REMARK   3     4  4.0082 -  3.6424    0.99     6223   141  0.1975 0.2369        
REMARK   3     5  3.6424 -  3.3817    0.99     6239   148  0.2271 0.2724        
REMARK   3     6  3.3817 -  3.1826    0.99     6232   140  0.2404 0.3160        
REMARK   3     7  3.1826 -  3.0234    0.99     6190   141  0.2427 0.3010        
REMARK   3     8  3.0234 -  2.8919    0.98     6115   143  0.2461 0.3070        
REMARK   3     9  2.8919 -  2.7806    0.98     6113   147  0.2446 0.3096        
REMARK   3    10  2.7806 -  2.6847    0.98     6057   143  0.2467 0.3174        
REMARK   3    11  2.6847 -  2.6008    0.97     6088   137  0.2488 0.2773        
REMARK   3    12  2.6008 -  2.5265    0.97     5983   145  0.2597 0.3373        
REMARK   3    13  2.5265 -  2.4600    0.96     5978   130  0.2685 0.3500        
REMARK   3    14  2.4600 -  2.4000    0.96     5999   141  0.2715 0.3131        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010          14919                                  
REMARK   3   ANGLE     :  1.411          20092                                  
REMARK   3   CHIRALITY :  0.080           2193                                  
REMARK   3   PLANARITY :  0.008           2551                                  
REMARK   3   DIHEDRAL  : 19.612           5550                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4HW3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-NOV-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB075992.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-JUN-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 21-ID-G                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97856                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05300                            
REMARK 200  R SYM                      (I) : 0.04500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 23.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29900                            
REMARK 200  R SYM FOR SHELL            (I) : 0.36400                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.550                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG3350, 0.2M MGCL2, PH 6.5, VAPOR   
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 298K                           
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       29.38000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12                   
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
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                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F                                     
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                                                                      
REMARK 350 BIOMOLECULE: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G                                     
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                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H                                     
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                                                                      
REMARK 350 BIOMOLECULE: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I                                     
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                                                                      
REMARK 350 BIOMOLECULE: 10                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
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                                                                      
REMARK 350 BIOMOLECULE: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: K                                     
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                                                                      
REMARK 350 BIOMOLECULE: 12                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L                                     
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     VAL A   321                                                      
REMARK 465     GLU A   322                                                      
REMARK 465     ASP A   323                                                      
REMARK 465     GLU B   322                                                      
REMARK 465     ASP B   323                                                      
REMARK 465     VAL C   321                                                      
REMARK 465     GLU C   322                                                      
REMARK 465     ASP C   323                                                      
REMARK 465     GLU E   322                                                      
REMARK 465     ASP E   323                                                      
REMARK 465     GLU F   322                                                      
REMARK 465     ASP F   323                                                      
REMARK 465     GLU G   322                                                      
REMARK 465     ASP G   323                                                      
REMARK 465     VAL H   321                                                      
REMARK 465     GLU H   322                                                      
REMARK 465     ASP H   323                                                      
REMARK 465     MET I   199                                                      
REMARK 465     GLY I   200                                                      
REMARK 465     ARG I   201                                                      
REMARK 465     VAL I   321                                                      
REMARK 465     GLU I   322                                                      
REMARK 465     ASP I   323                                                      
REMARK 465     GLY J   171                                                      
REMARK 465     GLU J   322                                                      
REMARK 465     ASP J   323                                                      
REMARK 465     GLU K   322                                                      
REMARK 465     ASP K   323                                                      
REMARK 465     ALA L   193                                                      
REMARK 465     LYS L   194                                                      
REMARK 465     ASP L   195                                                      
REMARK 465     THR L   196                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 197    CG   CD   CE   NZ                                   
REMARK 470     PRO A 198    CG   CD                                             
REMARK 470     ARG A 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR D 196    OG1  CG2                                            
REMARK 470     LYS D 197    CG   CD   CE   NZ                                   
REMARK 470     ARG D 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 322    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 323    CG   OD1  OD2                                       
REMARK 470     LYS E 194    CG   CD   CE   NZ                                   
REMARK 470     THR G 196    OG1  CG2                                            
REMARK 470     LYS G 197    CG   CD   CE   NZ                                   
REMARK 470     LYS H 194    CG   CD   CE   NZ                                   
REMARK 470     THR H 196    OG1  CG2                                            
REMARK 470     LYS H 197    CG   CD   CE   NZ                                   
REMARK 470     PRO H 198    CG   CD                                             
REMARK 470     MET H 199    CG   SD   CE                                        
REMARK 470     ARG H 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS I 194    CG   CD   CE   NZ                                   
REMARK 470     ASP I 195    CG   OD1  OD2                                       
REMARK 470     THR I 196    OG1  CG2                                            
REMARK 470     LYS I 197    CG   CD   CE   NZ                                   
REMARK 470     PRO I 198    CG   CD                                             
REMARK 470     LYS J 194    CG   CD   CE   NZ                                   
REMARK 470     THR J 196    OG1  CG2                                            
REMARK 470     LYS J 197    CG   CD   CE   NZ                                   
REMARK 470     ARG J 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS K 197    CG   CD   CE   NZ                                   
REMARK 470     LYS L 197    CG   CD   CE   NZ                                   
REMARK 470     ARG L 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER L 202    OG                                                  
REMARK 470     LEU L 278    CG   CD1  CD2                                       
REMARK 470     LYS L 279    CG   CD   CE   NZ                                   
REMARK 470     ASN L 282    CG   OD1  ND2                                       
REMARK 470     GLN L 283    CG   CD   OE1  NE2                                  
REMARK 470     GLU L 284    CG   CD   OE1  OE2                                  
REMARK 470     SER L 285    OG                                                  
REMARK 470     ASP L 323    CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B 172   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    GLY L 200   N   -  CA  -  C   ANGL. DEV. =  22.1 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 172     -128.17     47.76                                   
REMARK 500    ALA A 193     -179.90    179.92                                   
REMARK 500    ARG A 201     -124.55   -109.61                                   
REMARK 500    ILE A 281       20.81    -75.69                                   
REMARK 500    ASP B 172     -126.93     46.19                                   
REMARK 500    MET B 199     -106.84    -90.68                                   
REMARK 500    ARG B 201      -35.07    -38.24                                   
REMARK 500    ILE B 281        6.64    -65.76                                   
REMARK 500    ASP C 172     -128.70     46.24                                   
REMARK 500    MET C 199      172.32     73.38                                   
REMARK 500    ARG C 201      -59.90     71.25                                   
REMARK 500    ASP D 172     -128.53     48.47                                   
REMARK 500    ALA D 193      158.57    -31.37                                   
REMARK 500    THR D 280      -72.75    -74.71                                   
REMARK 500    ILE D 281       22.36    -59.90                                   
REMARK 500    ASP E 172     -131.41     47.69                                   
REMARK 500    ALA E 193       89.34   -154.53                                   
REMARK 500    LYS E 194      153.87     94.39                                   
REMARK 500    THR E 280      -71.82    -77.78                                   
REMARK 500    ILE E 281        0.68    -56.58                                   
REMARK 500    HIS E 320     -125.01     53.07                                   
REMARK 500    ASP F 172     -131.31     47.85                                   
REMARK 500    LYS F 194      138.08     17.72                                   
REMARK 500    SER F 255       31.38    -92.84                                   
REMARK 500    ILE F 281        3.37    -54.55                                   
REMARK 500    ASP G 172     -127.74     52.70                                   
REMARK 500    LYS G 194      149.20     68.98                                   
REMARK 500    THR G 280      -71.57    -75.86                                   
REMARK 500    ILE G 281        3.73    -58.52                                   
REMARK 500    ASP H 172     -131.53     47.02                                   
REMARK 500    LYS H 194      140.77     82.06                                   
REMARK 500    MET H 199      177.69     77.11                                   
REMARK 500    THR H 280      -71.11    -78.34                                   
REMARK 500    ILE H 281        5.26    -57.97                                   
REMARK 500    ASP I 172     -123.06     54.49                                   
REMARK 500    LYS I 194      128.14     51.82                                   
REMARK 500    THR I 196     -130.98     54.17                                   
REMARK 500    LYS I 197       59.00   -155.15                                   
REMARK 500    ILE I 281        3.12    -55.62                                   
REMARK 500    LYS J 194      144.51     85.83                                   
REMARK 500    THR J 196      -55.70     69.12                                   
REMARK 500    SER J 202       74.11   -101.81                                   
REMARK 500    ASN J 282       49.97     76.27                                   
REMARK 500    ASP K 172     -129.11     49.15                                   
REMARK 500    THR K 196     -130.60     53.80                                   
REMARK 500    LYS K 197      -52.29   -129.66                                   
REMARK 500    PRO K 198      178.20    -59.56                                   
REMARK 500    MET K 199     -169.55   -172.51                                   
REMARK 500    ASP K 256      128.56     91.11                                   
REMARK 500    ASP L 172     -127.15     50.40                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      57 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A  197     PRO A  198                 -148.08                    
REMARK 500 PRO A  198     MET A  199                 -139.43                    
REMARK 500 ASP E  195     THR E  196                 -141.22                    
REMARK 500 ALA F  193     LYS F  194                  121.43                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    SER C 255        22.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN D 282        24.0      L          L   OUTSIDE RANGE           
REMARK 500    THR E 196        23.5      L          L   OUTSIDE RANGE           
REMARK 500    LYS F 194        23.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN L 282        23.1      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G B 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G C 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G D 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G E 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G F 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G G 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G H 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G I 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G J 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G K 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 19G L 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4HW2   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4HW4   RELATED DB: PDB                                   
DBREF  4HW3 A  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 B  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 C  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 D  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 E  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 F  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 G  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 H  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 I  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 J  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 K  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
DBREF  4HW3 L  172   323  UNP    Q07820   MCL1_HUMAN     172    323             
SEQADV 4HW3 GLY A  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY B  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY C  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY D  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY E  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY F  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY G  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY H  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY I  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY J  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY K  171  UNP  Q07820              EXPRESSION TAG                 
SEQADV 4HW3 GLY L  171  UNP  Q07820              EXPRESSION TAG                 
SEQRES   1 A  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 A  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 A  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 A  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 A  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 A  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 A  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 A  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 A  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 A  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 A  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 A  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 B  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 B  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 B  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 B  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 B  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 B  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 B  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 B  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 B  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 B  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 B  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 B  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 C  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 C  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 C  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 C  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 C  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 C  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 C  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 C  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 C  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 C  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 C  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 C  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 D  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 D  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 D  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 D  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 D  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 D  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 D  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 D  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 D  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 D  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 D  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 D  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 E  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 E  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 E  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 E  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 E  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 E  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 E  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 E  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 E  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 E  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 E  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 E  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 F  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 F  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 F  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 F  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 F  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 F  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 F  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 F  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 F  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 F  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 F  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 F  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 G  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 G  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 G  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 G  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 G  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 G  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 G  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 G  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 G  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 G  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 G  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 G  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 H  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 H  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 H  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 H  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 H  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 H  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 H  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 H  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 H  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 H  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 H  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 H  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 I  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 I  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 I  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 I  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 I  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 I  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 I  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 I  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 I  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 I  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 I  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 I  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 J  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 J  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 J  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 J  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 J  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 J  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 J  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 J  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 J  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 J  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 J  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 J  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 K  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 K  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 K  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 K  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 K  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 K  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 K  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 K  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 K  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 K  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 K  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 K  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
SEQRES   1 L  153  GLY ASP GLU LEU TYR ARG GLN SER LEU GLU ILE ILE SER          
SEQRES   2 L  153  ARG TYR LEU ARG GLU GLN ALA THR GLY ALA LYS ASP THR          
SEQRES   3 L  153  LYS PRO MET GLY ARG SER GLY ALA THR SER ARG LYS ALA          
SEQRES   4 L  153  LEU GLU THR LEU ARG ARG VAL GLY ASP GLY VAL GLN ARG          
SEQRES   5 L  153  ASN HIS GLU THR ALA PHE GLN GLY MET LEU ARG LYS LEU          
SEQRES   6 L  153  ASP ILE LYS ASN GLU ASP ASP VAL LYS SER LEU SER ARG          
SEQRES   7 L  153  VAL MET ILE HIS VAL PHE SER ASP GLY VAL THR ASN TRP          
SEQRES   8 L  153  GLY ARG ILE VAL THR LEU ILE SER PHE GLY ALA PHE VAL          
SEQRES   9 L  153  ALA LYS HIS LEU LYS THR ILE ASN GLN GLU SER CYS ILE          
SEQRES  10 L  153  GLU PRO LEU ALA GLU SER ILE THR ASP VAL LEU VAL ARG          
SEQRES  11 L  153  THR LYS ARG ASP TRP LEU VAL LYS GLN ARG GLY TRP ASP          
SEQRES  12 L  153  GLY PHE VAL GLU PHE PHE HIS VAL GLU ASP                      
HET    19G  A 400      25                                                       
HET    19G  B 400      25                                                       
HET    19G  C 400      25                                                       
HET    19G  D 400      25                                                       
HET    19G  E 400      25                                                       
HET    19G  F 400      25                                                       
HET    19G  G 400      25                                                       
HET    19G  H 400      25                                                       
HET    19G  I 400      25                                                       
HET    19G  J 400      25                                                       
HET    19G  K 400      25                                                       
HET    19G  L 400      25                                                       
HETNAM     19G 3-[3-(4-CHLORO-3,5-DIMETHYLPHENOXY)PROPYL]-1-                    
HETNAM   2 19G  BENZOTHIOPHENE-2-CARBOXYLIC ACID                                
FORMUL  13  19G    12(C20 H19 CL O3 S)                                          
FORMUL  25  HOH   *251(H2 O)                                                    
HELIX    1   1 GLY A  171  THR A  191  1                                  21    
HELIX    2   2 SER A  202  HIS A  224  1                                  23    
HELIX    3   3 HIS A  224  ASP A  236  1                                  13    
HELIX    4   4 ASN A  239  LYS A  244  1                                   6    
HELIX    5   5 LEU A  246  SER A  255  1                                  10    
HELIX    6   6 ASN A  260  ILE A  281  1                                  22    
HELIX    7   7 GLN A  283  SER A  285  5                                   3    
HELIX    8   8 CYS A  286  GLN A  309  1                                  24    
HELIX    9   9 ARG A  310  PHE A  319  1                                  10    
HELIX   10  10 ASP B  172  THR B  191  1                                  20    
HELIX   11  11 SER B  202  HIS B  224  1                                  23    
HELIX   12  12 HIS B  224  ASP B  236  1                                  13    
HELIX   13  13 ASN B  239  SER B  245  1                                   7    
HELIX   14  14 LEU B  246  SER B  255  1                                  10    
HELIX   15  15 ASN B  260  ILE B  281  1                                  22    
HELIX   16  16 GLN B  283  SER B  285  5                                   3    
HELIX   17  17 CYS B  286  GLN B  309  1                                  24    
HELIX   18  18 ARG B  310  PHE B  319  1                                  10    
HELIX   19  19 ASP C  172  GLY C  192  1                                  21    
HELIX   20  20 SER C  202  HIS C  224  1                                  23    
HELIX   21  21 HIS C  224  ASP C  236  1                                  13    
HELIX   22  22 ASN C  239  LYS C  244  1                                   6    
HELIX   23  23 LEU C  246  ASP C  256  1                                  11    
HELIX   24  24 ASN C  260  ILE C  281  1                                  22    
HELIX   25  25 GLN C  283  SER C  285  5                                   3    
HELIX   26  26 CYS C  286  GLN C  309  1                                  24    
HELIX   27  27 ARG C  310  PHE C  319  1                                  10    
HELIX   28  28 ASP D  172  THR D  191  1                                  20    
HELIX   29  29 GLY D  203  HIS D  224  1                                  22    
HELIX   30  30 HIS D  224  ASP D  236  1                                  13    
HELIX   31  31 ASN D  239  LYS D  244  1                                   6    
HELIX   32  32 LEU D  246  SER D  255  1                                  10    
HELIX   33  33 ASN D  260  ILE D  281  1                                  22    
HELIX   34  34 GLN D  283  SER D  285  5                                   3    
HELIX   35  35 CYS D  286  GLN D  309  1                                  24    
HELIX   36  36 ARG D  310  PHE D  319  1                                  10    
HELIX   37  37 ASP E  172  THR E  191  1                                  20    
HELIX   38  38 SER E  202  HIS E  224  1                                  23    
HELIX   39  39 HIS E  224  ASP E  236  1                                  13    
HELIX   40  40 ASN E  239  LYS E  244  1                                   6    
HELIX   41  41 LEU E  246  SER E  255  1                                  10    
HELIX   42  42 ASN E  260  ILE E  281  1                                  22    
HELIX   43  43 GLN E  283  SER E  285  5                                   3    
HELIX   44  44 CYS E  286  GLN E  309  1                                  24    
HELIX   45  45 ARG E  310  PHE E  319  1                                  10    
HELIX   46  46 ASP F  172  THR F  191  1                                  20    
HELIX   47  47 SER F  202  HIS F  224  1                                  23    
HELIX   48  48 HIS F  224  ASP F  236  1                                  13    
HELIX   49  49 ASN F  239  LYS F  244  1                                   6    
HELIX   50  50 LEU F  246  SER F  255  1                                  10    
HELIX   51  51 ASN F  260  ILE F  281  1                                  22    
HELIX   52  52 GLN F  283  SER F  285  5                                   3    
HELIX   53  53 CYS F  286  GLN F  309  1                                  24    
HELIX   54  54 GLY F  311  PHE F  319  1                                   9    
HELIX   55  55 ASP G  172  GLY G  192  1                                  21    
HELIX   56  56 GLY G  203  HIS G  224  1                                  22    
HELIX   57  57 HIS G  224  ASP G  236  1                                  13    
HELIX   58  58 ASN G  239  SER G  245  1                                   7    
HELIX   59  59 LEU G  246  SER G  255  1                                  10    
HELIX   60  60 ASN G  260  ILE G  281  1                                  22    
HELIX   61  61 GLN G  283  SER G  285  5                                   3    
HELIX   62  62 CYS G  286  GLN G  309  1                                  24    
HELIX   63  63 ARG G  310  PHE G  319  1                                  10    
HELIX   64  64 ASP H  172  THR H  191  1                                  20    
HELIX   65  65 GLY H  203  HIS H  224  1                                  22    
HELIX   66  66 HIS H  224  ASP H  236  1                                  13    
HELIX   67  67 ASN H  239  SER H  245  1                                   7    
HELIX   68  68 SER H  245  SER H  255  1                                  11    
HELIX   69  69 ASN H  260  ASN H  282  1                                  23    
HELIX   70  70 GLN H  283  SER H  285  5                                   3    
HELIX   71  71 CYS H  286  LYS H  302  1                                  17    
HELIX   72  72 LYS H  302  GLN H  309  1                                   8    
HELIX   73  73 ARG H  310  PHE H  319  1                                  10    
HELIX   74  74 ASP I  172  THR I  191  1                                  20    
HELIX   75  75 GLY I  203  HIS I  224  1                                  22    
HELIX   76  76 HIS I  224  ASP I  236  1                                  13    
HELIX   77  77 ASN I  239  LYS I  244  1                                   6    
HELIX   78  78 LEU I  246  SER I  255  1                                  10    
HELIX   79  79 ASN I  260  ILE I  281  1                                  22    
HELIX   80  80 GLN I  283  SER I  285  5                                   3    
HELIX   81  81 CYS I  286  GLN I  309  1                                  24    
HELIX   82  82 ARG I  310  PHE I  319  1                                  10    
HELIX   83  83 GLU J  173  THR J  191  1                                  19    
HELIX   84  84 SER J  202  HIS J  224  1                                  23    
HELIX   85  85 HIS J  224  ASP J  236  1                                  13    
HELIX   86  86 ASP J  242  LYS J  244  5                                   3    
HELIX   87  87 SER J  245  ASP J  256  1                                  12    
HELIX   88  88 ASN J  260  ASN J  282  1                                  23    
HELIX   89  89 GLN J  283  SER J  285  5                                   3    
HELIX   90  90 CYS J  286  GLN J  309  1                                  24    
HELIX   91  91 ARG J  310  PHE J  319  1                                  10    
HELIX   92  92 ASP K  172  THR K  191  1                                  20    
HELIX   93  93 GLY K  203  HIS K  224  1                                  22    
HELIX   94  94 HIS K  224  ASP K  236  1                                  13    
HELIX   95  95 ASN K  239  LYS K  244  1                                   6    
HELIX   96  96 LEU K  246  SER K  255  1                                  10    
HELIX   97  97 ASN K  260  ILE K  281  1                                  22    
HELIX   98  98 GLN K  283  SER K  285  5                                   3    
HELIX   99  99 CYS K  286  GLN K  309  1                                  24    
HELIX  100 100 ARG K  310  PHE K  319  1                                  10    
HELIX  101 101 ASP L  172  GLY L  192  1                                  21    
HELIX  102 102 SER L  202  HIS L  224  1                                  23    
HELIX  103 103 HIS L  224  ASP L  236  1                                  13    
HELIX  104 104 ASN L  239  SER L  245  1                                   7    
HELIX  105 105 LEU L  246  SER L  255  1                                  10    
HELIX  106 106 ASN L  260  THR L  280  1                                  21    
HELIX  107 107 CYS L  286  GLN L  309  1                                  24    
HELIX  108 108 ARG L  310  PHE L  319  1                                  10    
CISPEP   1 GLY A  192    ALA A  193          0         7.08                     
CISPEP   2 MET A  199    GLY A  200          0       -14.97                     
CISPEP   3 PRO D  198    MET D  199          0       -22.48                     
CISPEP   4 ARG D  201    SER D  202          0        -0.22                     
CISPEP   5 SER D  202    GLY D  203          0        10.03                     
CISPEP   6 THR E  196    LYS E  197          0        -9.45                     
CISPEP   7 GLY F  257    VAL F  258          0         3.78                     
CISPEP   8 MET G  199    GLY G  200          0       -13.05                     
CISPEP   9 ARG H  201    SER H  202          0         6.84                     
CISPEP  10 SER H  255    ASP H  256          0        -1.84                     
CISPEP  11 LYS J  197    PRO J  198          0       -15.85                     
CISPEP  12 LYS L  197    PRO L  198          0       -15.42                     
CISPEP  13 GLY L  257    VAL L  258          0         8.58                     
SITE     1 AC1  7 PHE A 228  LEU A 246  VAL A 253  ARG A 263                    
SITE     2 AC1  7 THR A 266  LEU A 267  PHE A 270                               
SITE     1 AC2 10 MET B 231  LEU B 246  MET B 250  VAL B 253                    
SITE     2 AC2 10 ARG B 263  THR B 266  LEU B 267  PHE B 270                    
SITE     3 AC2 10 ILE B 294  LYS D 308                                          
SITE     1 AC3  7 LYS A 308  PHE C 228  VAL C 253  ARG C 263                    
SITE     2 AC3  7 THR C 266  LEU C 267  PHE C 270                               
SITE     1 AC4  6 MET D 231  VAL D 253  ARG D 263  LEU D 267                    
SITE     2 AC4  6 PHE D 270  ILE D 294                                          
SITE     1 AC5  7 VAL A 258  MET E 231  LEU E 246  ARG E 263                    
SITE     2 AC5  7 THR E 266  LEU E 267  PHE E 270                               
SITE     1 AC6  9 VAL D 258  PHE F 228  LEU F 246  MET F 250                    
SITE     2 AC6  9 ARG F 263  THR F 266  LEU F 267  PHE F 270                    
SITE     3 AC6  9 ILE F 294                                                     
SITE     1 AC7  7 MET G 231  LEU G 246  VAL G 253  ARG G 263                    
SITE     2 AC7  7 THR G 266  LEU G 267  PHE G 270                               
SITE     1 AC8  8 PHE H 228  MET H 250  VAL H 253  ARG H 263                    
SITE     2 AC8  8 THR H 266  LEU H 267  PHE H 270  GLY H 271                    
SITE     1 AC9  8 LEU I 246  MET I 250  VAL I 253  PHE I 254                    
SITE     2 AC9  8 ARG I 263  LEU I 267  PHE I 270  HIS K 320                    
SITE     1 BC1 11 PHE J 228  MET J 231  LEU J 235  LEU J 246                    
SITE     2 BC1 11 MET J 250  VAL J 253  ARG J 263  THR J 266                    
SITE     3 BC1 11 LEU J 267  PHE J 270  GLY J 271                               
SITE     1 BC2  7 PHE K 228  VAL K 253  PHE K 254  ARG K 263                    
SITE     2 BC2  7 LEU K 267  PHE K 270  ILE K 294                               
SITE     1 BC3  8 LEU L 246  MET L 250  VAL L 253  ARG L 263                    
SITE     2 BC3  8 THR L 266  LEU L 267  PHE L 270  GLY L 271                    
CRYST1  139.446   58.760  140.675  90.00  90.71  90.00 P 1 21 1     24          
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      0.007171  0.000000  0.000088        0.00000                         
SCALE2      0.000000  0.017018  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007109        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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