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Database: PDB
Entry: 2F3F
LinkDB: 2F3F
Original site: 2F3F 
HEADER    HYDROLASE                               21-NOV-05   2F3F              
TITLE     CRYSTAL STRUCTURE OF THE BACE COMPLEX WITH BDF488, A MACROCYCLIC      
TITLE    2 INHIBITOR                                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-SECRETASE 1;                                          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: CATALYTIC DOMAIN;                                          
COMPND   5 SYNONYM: BETA-SITE APP CLEAVING ENZYME 1, BETA-SITE AMYLOID PRECURSOR
COMPND   6 PROTEIN CLEAVING ENZYME 1, ASPARTYL PROTEASE 2, ASP 2, ASP2,         
COMPND   7 MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2, MEMAPSIN-2;                 
COMPND   8 EC: 3.4.23.46;                                                       
COMPND   9 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: BACE1, BACE;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET24                                     
KEYWDS    BETA-SECRETASE, MEMAPSIN2, ALZHEIMER'S DISEASE, ASPARTIC PROTEASE,    
KEYWDS   2 MACROCYCLIC PEPTIDOMIMETIC INHIBITOR, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.-M.RONDEAU                                                          
REVDAT   3   18-OCT-17 2F3F    1       REMARK                                   
REVDAT   2   24-FEB-09 2F3F    1       VERSN                                    
REVDAT   1   05-SEP-06 2F3F    0                                                
JRNL        AUTH   S.HANESSIAN,G.YANG,J.-M.RONDEAU,U.NEUMANN,C.BETSCHART,       
JRNL        AUTH 2 M.TINTELNOT-BLOMLEY                                          
JRNL        TITL   STRUCTURE-BASED DESIGN AND SYNTHESIS OF MACROHETEROCYCLIC    
JRNL        TITL 2 PEPTIDOMIMETIC INHIBITORS OF THE ASPARTIC PROTEASE BETA-SITE 
JRNL        TITL 3 AMYLOID PRECURSOR PROTEIN CLEAVING ENZYME (BACE).            
JRNL        REF    J.MED.CHEM.                   V.  49  4544 2006              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   16854060                                                     
JRNL        DOI    10.1021/JM060154A                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 63.29                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 16369373.000                   
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 72197                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3670                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : 0.1920               
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : 0.1900               
REMARK   3   FREE R VALUE                    (NO CUTOFF) : 0.220                
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : 5.100                
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : 3670                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 72197                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10821                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2410                       
REMARK   3   BIN FREE R VALUE                    : 0.2750                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 576                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.011                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8885                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 102                                     
REMARK   3   SOLVENT ATOMS            : 508                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 50.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.00000                                             
REMARK   3    B22 (A**2) : 7.59000                                              
REMARK   3    B33 (A**2) : 0.41000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.24000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.25                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.30                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.000                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 22.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.630                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 3.170 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 4.610 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 4.840 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 6.410 ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 52.70                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN.TOP                                    
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  PARAMETER FILE  3  : WATER.TOP                                      
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN_REP.PARAM                              
REMARK   3  TOPOLOGY FILE  2   : NVP-BDF488.PRM                                 
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.PARAM                                
REMARK   3  TOPOLOGY FILE  4   : CIS_PEPTIDE.PARAM                              
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2F3F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 07-DEC-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000035404.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-DEC-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97840                            
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 72219                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 3.900                              
REMARK 200  R MERGE                    (I) : 0.09700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.40700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNX 2002                                              
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M AMMONIUM SULFATE, PH 5.5, VAPOR     
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 292K                           
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       51.60100            
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                                                 
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS A MONOMER                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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 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     GLY A    33P                                                     
REMARK 465     PRO A    34P                                                     
REMARK 465     ASP A    35P                                                     
REMARK 465     GLU A    36P                                                     
REMARK 465     GLU A    37P                                                     
REMARK 465     PRO A    38P                                                     
REMARK 465     GLU A    39P                                                     
REMARK 465     GLU A    40P                                                     
REMARK 465     PRO A    41P                                                     
REMARK 465     GLY A    42P                                                     
REMARK 465     ARG A    43P                                                     
REMARK 465     ARG A    44P                                                     
REMARK 465     GLY A    45P                                                     
REMARK 465     GLY A   158                                                      
REMARK 465     PHE A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     LEU A   161                                                      
REMARK 465     ASN A   162                                                      
REMARK 465     GLN A   163                                                      
REMARK 465     SER A   164                                                      
REMARK 465     GLU A   165                                                      
REMARK 465     VAL A   166                                                      
REMARK 465     LEU A   167                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     SER A   169                                                      
REMARK 465     VAL A   170                                                      
REMARK 465     ILE A   386                                                      
REMARK 465     GLY B    33P                                                     
REMARK 465     PRO B    34P                                                     
REMARK 465     ASP B    35P                                                     
REMARK 465     GLU B    36P                                                     
REMARK 465     GLU B    37P                                                     
REMARK 465     PRO B    38P                                                     
REMARK 465     GLU B    39P                                                     
REMARK 465     GLU B    40P                                                     
REMARK 465     PRO B    41P                                                     
REMARK 465     GLY B    42P                                                     
REMARK 465     ARG B    43P                                                     
REMARK 465     ARG B    44P                                                     
REMARK 465     GLY B    45P                                                     
REMARK 465     GLY B   158                                                      
REMARK 465     PHE B   159                                                      
REMARK 465     PRO B   160                                                      
REMARK 465     LEU B   161                                                      
REMARK 465     ASN B   162                                                      
REMARK 465     GLN B   163                                                      
REMARK 465     SER B   164                                                      
REMARK 465     GLU B   165                                                      
REMARK 465     VAL B   166                                                      
REMARK 465     LEU B   167                                                      
REMARK 465     ALA B   168                                                      
REMARK 465     ILE B   386                                                      
REMARK 465     GLY C    33P                                                     
REMARK 465     PRO C    34P                                                     
REMARK 465     ASP C    35P                                                     
REMARK 465     GLU C    36P                                                     
REMARK 465     GLU C    37P                                                     
REMARK 465     PRO C    38P                                                     
REMARK 465     GLU C    39P                                                     
REMARK 465     GLU C    40P                                                     
REMARK 465     PRO C    41P                                                     
REMARK 465     GLY C    42P                                                     
REMARK 465     ARG C    43P                                                     
REMARK 465     ARG C    44P                                                     
REMARK 465     GLY C    45P                                                     
REMARK 465     GLY C   158                                                      
REMARK 465     PHE C   159                                                      
REMARK 465     PRO C   160                                                      
REMARK 465     LEU C   161                                                      
REMARK 465     ASN C   162                                                      
REMARK 465     GLN C   163                                                      
REMARK 465     SER C   164                                                      
REMARK 465     GLU C   165                                                      
REMARK 465     VAL C   166                                                      
REMARK 465     LEU C   167                                                      
REMARK 465     ALA C   168                                                      
REMARK 465     ILE C   386                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   667     O    HOH B   703              2.19            
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    PHE A 108      -63.40    -98.65                                   
REMARK 500    TRP A 197      -82.10   -137.78                                   
REMARK 500    GLU A 265      -65.65    -98.53                                   
REMARK 500    ALA A 313     -158.90   -129.74                                   
REMARK 500    CYS A 359       58.66   -102.07                                   
REMARK 500    LYS B   9     -145.68    -77.32                                   
REMARK 500    HIS B  89       40.69   -103.76                                   
REMARK 500    PHE B 108      -61.43    -99.40                                   
REMARK 500    TRP B 197      -82.85   -139.79                                   
REMARK 500    GLU B 265      -65.85    -99.48                                   
REMARK 500    GLN B 303       -8.88    -58.18                                   
REMARK 500    ALA B 313     -158.99   -129.31                                   
REMARK 500    CYS B 359       49.98   -108.03                                   
REMARK 500    ASP B 363     -126.90   -105.99                                   
REMARK 500    HIS C  89       40.02   -103.91                                   
REMARK 500    PHE C 108      -62.32    -99.09                                   
REMARK 500    VAL C 170      -72.41   -152.73                                   
REMARK 500    TRP C 197      -82.40   -138.64                                   
REMARK 500    ARG C 205      140.19   -172.85                                   
REMARK 500    GLU C 265      -66.79    -98.90                                   
REMARK 500    ALA C 313     -159.54   -129.63                                   
REMARK 500    CYS C 359       60.75   -101.67                                   
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 AXF A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXF B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE AXF C 603                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2F3E   RELATED DB: PDB                                   
REMARK 900 BACE1 IN COMPLEX WITH RELATED MACROCYCLIC PEPTIDOMIMETIC INHIBITOR   
DBREF  2F3F A   35P  386  UNP    P56817   BACE1_HUMAN     48    447             
DBREF  2F3F B   35P  386  UNP    P56817   BACE1_HUMAN     48    447             
DBREF  2F3F C   35P  386  UNP    P56817   BACE1_HUMAN     48    447             
SEQADV 2F3F GLY A   33P UNP  P56817              CLONING ARTIFACT               
SEQADV 2F3F PRO A   34P UNP  P56817              CLONING ARTIFACT               
SEQADV 2F3F GLY B   33P UNP  P56817              CLONING ARTIFACT               
SEQADV 2F3F PRO B   34P UNP  P56817              CLONING ARTIFACT               
SEQADV 2F3F GLY C   33P UNP  P56817              CLONING ARTIFACT               
SEQADV 2F3F PRO C   34P UNP  P56817              CLONING ARTIFACT               
SEQRES   1 A  402  GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY          
SEQRES   2 A  402  SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER          
SEQRES   3 A  402  GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO          
SEQRES   4 A  402  PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER          
SEQRES   5 A  402  ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS          
SEQRES   6 A  402  ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP          
SEQRES   7 A  402  LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS          
SEQRES   8 A  402  TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO          
SEQRES   9 A  402  HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA          
SEQRES  10 A  402  ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN          
SEQRES  11 A  402  TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA          
SEQRES  12 A  402  ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU          
SEQRES  13 A  402  VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN          
SEQRES  14 A  402  LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL          
SEQRES  15 A  402  LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE          
SEQRES  16 A  402  ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO          
SEQRES  17 A  402  ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG          
SEQRES  18 A  402  VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS          
SEQRES  19 A  402  GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR          
SEQRES  20 A  402  THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA          
SEQRES  21 A  402  VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE          
SEQRES  22 A  402  PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP          
SEQRES  23 A  402  GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE          
SEQRES  24 A  402  SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE          
SEQRES  25 A  402  ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL          
SEQRES  26 A  402  GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE          
SEQRES  27 A  402  ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA          
SEQRES  28 A  402  VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA          
SEQRES  29 A  402  ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL          
SEQRES  30 A  402  HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE          
SEQRES  31 A  402  VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE              
SEQRES   1 B  402  GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY          
SEQRES   2 B  402  SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER          
SEQRES   3 B  402  GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO          
SEQRES   4 B  402  PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER          
SEQRES   5 B  402  ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS          
SEQRES   6 B  402  ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP          
SEQRES   7 B  402  LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS          
SEQRES   8 B  402  TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO          
SEQRES   9 B  402  HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA          
SEQRES  10 B  402  ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN          
SEQRES  11 B  402  TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA          
SEQRES  12 B  402  ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU          
SEQRES  13 B  402  VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN          
SEQRES  14 B  402  LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL          
SEQRES  15 B  402  LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE          
SEQRES  16 B  402  ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO          
SEQRES  17 B  402  ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG          
SEQRES  18 B  402  VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS          
SEQRES  19 B  402  GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR          
SEQRES  20 B  402  THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA          
SEQRES  21 B  402  VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE          
SEQRES  22 B  402  PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP          
SEQRES  23 B  402  GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE          
SEQRES  24 B  402  SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE          
SEQRES  25 B  402  ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL          
SEQRES  26 B  402  GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE          
SEQRES  27 B  402  ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA          
SEQRES  28 B  402  VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA          
SEQRES  29 B  402  ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL          
SEQRES  30 B  402  HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE          
SEQRES  31 B  402  VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE              
SEQRES   1 C  402  GLY PRO ASP GLU GLU PRO GLU GLU PRO GLY ARG ARG GLY          
SEQRES   2 C  402  SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS SER          
SEQRES   3 C  402  GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER PRO          
SEQRES   4 C  402  PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER SER          
SEQRES   5 C  402  ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU HIS          
SEQRES   6 C  402  ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG ASP          
SEQRES   7 C  402  LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY LYS          
SEQRES   8 C  402  TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE PRO          
SEQRES   9 C  402  HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA ALA          
SEQRES  10 C  402  ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER ASN          
SEQRES  11 C  402  TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE ALA          
SEQRES  12 C  402  ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER LEU          
SEQRES  13 C  402  VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU GLN          
SEQRES  14 C  402  LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU VAL          
SEQRES  15 C  402  LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY ILE          
SEQRES  16 C  402  ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR PRO          
SEQRES  17 C  402  ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL ARG          
SEQRES  18 C  402  VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS LYS          
SEQRES  19 C  402  GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY THR          
SEQRES  20 C  402  THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA ALA          
SEQRES  21 C  402  VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS PHE          
SEQRES  22 C  402  PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS TRP          
SEQRES  23 C  402  GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL ILE          
SEQRES  24 C  402  SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER PHE          
SEQRES  25 C  402  ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO VAL          
SEQRES  26 C  402  GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS PHE          
SEQRES  27 C  402  ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY ALA          
SEQRES  28 C  402  VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG ALA          
SEQRES  29 C  402  ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS VAL          
SEQRES  30 C  402  HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO PHE          
SEQRES  31 C  402  VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN ILE              
HET    AXF  A 601      34                                                       
HET    AXF  B 602      34                                                       
HET    AXF  C 603      34                                                       
HETNAM     AXF (2R,4S)-N-BUTYL-4-HYDROXY-2-METHYL- 4-((E)-(4AS,12R,             
HETNAM   2 AXF  15S,17AS)-15-METHYL -14,17-DIOXO-2,3,4,4A,6,9,11,12,            
HETNAM   3 AXF  13, 14,15,16,17,17A-TETRADECAHYDRO-1H-5 ,10-DITHIA-1,           
HETNAM   4 AXF  13,16-TRIAZA-BENZOCYCL OPENTADECEN-12-YL)-BUTYRAMIDE            
FORMUL   4  AXF    3(C24 H42 N4 O4 S2)                                          
FORMUL   7  HOH   *508(H2 O)                                                    
HELIX    1   2 GLN A   53  SER A   57  5                                   5    
HELIX    2   3 TYR A  123  ALA A  127  5                                   5    
HELIX    3   4 PRO A  135  THR A  144  1                                  10    
HELIX    4   5 ASP A  180  SER A  182  5                                   3    
HELIX    5   6 ASP A  216  TYR A  222  5                                   7    
HELIX    6   7 LYS A  238  SER A  252  1                                  15    
HELIX    7   8 PRO A  276  PHE A  280  5                                   5    
HELIX    8   9 LEU A  301  TYR A  305  1                                   5    
HELIX    9  10 GLY A  334  GLU A  339  1                                   6    
HELIX   10  11 ARG A  347  ARG A  349  5                                   3    
HELIX   11  12 ASP A  378  GLY A  383  5                                   6    
HELIX   12  14 GLN B   53  SER B   57  5                                   5    
HELIX   13  15 TYR B  123  ALA B  127  5                                   5    
HELIX   14  16 PRO B  135  THR B  144  1                                  10    
HELIX   15  17 ASP B  180  SER B  182  5                                   3    
HELIX   16  18 ASP B  216  TYR B  222  5                                   7    
HELIX   17  19 LYS B  238  SER B  252  1                                  15    
HELIX   18  20 PRO B  276  PHE B  280  5                                   5    
HELIX   19  21 LEU B  301  TYR B  305  1                                   5    
HELIX   20  22 GLY B  334  GLU B  339  1                                   6    
HELIX   21  23 ARG B  347  ARG B  349  5                                   3    
HELIX   22  24 ASP B  378  GLY B  383  5                                   6    
HELIX   23  26 GLN C   53  SER C   57  5                                   5    
HELIX   24  27 TYR C  123  ALA C  127  5                                   5    
HELIX   25  28 PRO C  135  THR C  144  1                                  10    
HELIX   26  29 ASP C  180  SER C  182  5                                   3    
HELIX   27  30 ASP C  216  TYR C  222  5                                   7    
HELIX   28  31 LYS C  238  SER C  252  1                                  15    
HELIX   29  32 PRO C  276  PHE C  280  5                                   5    
HELIX   30  33 LEU C  301  TYR C  305  1                                   5    
HELIX   31  34 GLY C  334  GLU C  339  1                                   6    
HELIX   32  35 ARG C  347  ARG C  349  5                                   3    
HELIX   33  36 ASP C  378  GLY C  383  1                                   6    
SHEET    1   A 8 LEU A   6  LYS A   9  0                                        
SHEET    2   A 8 GLY A  13  VAL A  20 -1  O  TYR A  15   N  ARG A   7           
SHEET    3   A 8 GLN A  25  ASP A  32 -1  O  ILE A  29   N  VAL A  16           
SHEET    4   A 8 GLY A 117  GLY A 120  1  O  LEU A 119   N  LEU A  30           
SHEET    5   A 8 PHE A  38  GLY A  41 -1  N  ALA A  39   O  ILE A 118           
SHEET    6   A 8 VAL A  95  ASP A 106  1  O  ILE A 102   N  VAL A  40           
SHEET    7   A 8 LYS A  75  SER A  86 -1  N  GLU A  79   O  ALA A 101           
SHEET    8   A 8 ARG A  61  PRO A  70 -1  N  LYS A  65   O  LEU A  80           
SHEET    1   B 4 LEU A   6  LYS A   9  0                                        
SHEET    2   B 4 GLY A  13  VAL A  20 -1  O  TYR A  15   N  ARG A   7           
SHEET    3   B 4 LYS A  75  SER A  86 -1  O  SER A  86   N  THR A  19           
SHEET    4   B 4 ARG A  61  PRO A  70 -1  N  LYS A  65   O  LEU A  80           
SHEET    1   C 5 GLY A 172  ILE A 176  0                                        
SHEET    2   C 5 PHE A 150  LEU A 154 -1  N  GLN A 153   O  SER A 173           
SHEET    3   C 5 PHE A 341  ASP A 346 -1  O  PHE A 345   N  PHE A 150           
SHEET    4   C 5 ARG A 351  SER A 357 -1  O  ALA A 355   N  TYR A 342           
SHEET    5   C 5 TYR A 184  PRO A 192 -1  N  THR A 191   O  ILE A 352           
SHEET    1   D 5 GLN A 211  ASP A 212  0                                        
SHEET    2   D 5 ILE A 203  ILE A 208 -1  N  ILE A 208   O  GLN A 211           
SHEET    3   D 5 ILE A 283  MET A 288 -1  O  SER A 284   N  GLU A 207           
SHEET    4   D 5 GLN A 294  ILE A 300 -1  O  ILE A 300   N  ILE A 283           
SHEET    5   D 5 ALA A 369  VAL A 375 -1  O  GLU A 371   N  ARG A 297           
SHEET    1   E 4 SER A 225  VAL A 227  0                                        
SHEET    2   E 4 THR A 331  MET A 333  1  O  MET A 333   N  ILE A 226           
SHEET    3   E 4 LEU A 234  PRO A 237 -1  N  ARG A 235   O  VAL A 332           
SHEET    4   E 4 ILE A 324  SER A 327  1  O  SER A 327   N  LEU A 236           
SHEET    1   F 3 VAL A 268  TRP A 270  0                                        
SHEET    2   F 3 ASP A 318  PHE A 322 -1  O  TYR A 320   N  VAL A 268           
SHEET    3   F 3 LEU A 306  VAL A 309 -1  N  ARG A 307   O  LYS A 321           
SHEET    1   G 9 ARG B  61  PRO B  70  0                                        
SHEET    2   G 9 LYS B  75  SER B  86 -1  O  LEU B  80   N  LYS B  65           
SHEET    3   G 9 TYR B  15  VAL B  20 -1  N  THR B  19   O  SER B  86           
SHEET    4   G 9 LEU B   6  ARG B   7 -1  N  ARG B   7   O  TYR B  15           
SHEET    5   G 9 GLY B 171  ILE B 176 -1  O  GLY B 172   N  LEU B   6           
SHEET    6   G 9 PHE B 150  CYS B 155 -1  N  GLN B 153   O  SER B 173           
SHEET    7   G 9 PHE B 341  ASP B 346 -1  O  PHE B 345   N  PHE B 150           
SHEET    8   G 9 ARG B 351  SER B 357 -1  O  ALA B 355   N  TYR B 342           
SHEET    9   G 9 TYR B 184  PRO B 192 -1  N  THR B 191   O  ILE B 352           
SHEET    1   H13 ARG B  61  PRO B  70  0                                        
SHEET    2   H13 LYS B  75  SER B  86 -1  O  LEU B  80   N  LYS B  65           
SHEET    3   H13 VAL B  95  ASP B 106 -1  O  ALA B 101   N  GLU B  79           
SHEET    4   H13 PHE B  38  GLY B  41  1  N  VAL B  40   O  ILE B 102           
SHEET    5   H13 GLY B 117  GLY B 120 -1  O  ILE B 118   N  ALA B  39           
SHEET    6   H13 GLN B  25  ASP B  32  1  N  LEU B  30   O  LEU B 119           
SHEET    7   H13 TYR B  15  VAL B  20 -1  N  VAL B  16   O  ILE B  29           
SHEET    8   H13 LEU B   6  ARG B   7 -1  N  ARG B   7   O  TYR B  15           
SHEET    9   H13 GLY B 171  ILE B 176 -1  O  GLY B 172   N  LEU B   6           
SHEET   10   H13 PHE B 150  CYS B 155 -1  N  GLN B 153   O  SER B 173           
SHEET   11   H13 PHE B 341  ASP B 346 -1  O  PHE B 345   N  PHE B 150           
SHEET   12   H13 ARG B 351  SER B 357 -1  O  ALA B 355   N  TYR B 342           
SHEET   13   H13 TYR B 184  PRO B 192 -1  N  THR B 191   O  ILE B 352           
SHEET    1   I 5 GLN B 211  ASP B 212  0                                        
SHEET    2   I 5 ILE B 203  ILE B 208 -1  N  ILE B 208   O  GLN B 211           
SHEET    3   I 5 ILE B 283  MET B 288 -1  O  TYR B 286   N  ARG B 205           
SHEET    4   I 5 GLN B 294  ILE B 300 -1  O  ILE B 300   N  ILE B 283           
SHEET    5   I 5 ALA B 369  VAL B 375 -1  O  GLU B 371   N  ARG B 297           
SHEET    1   J 4 SER B 225  VAL B 227  0                                        
SHEET    2   J 4 THR B 331  MET B 333  1  O  MET B 333   N  ILE B 226           
SHEET    3   J 4 LEU B 234  PRO B 237 -1  N  ARG B 235   O  VAL B 332           
SHEET    4   J 4 ILE B 324  SER B 327  1  O  SER B 327   N  LEU B 236           
SHEET    1   K 3 VAL B 268  TRP B 270  0                                        
SHEET    2   K 3 ASP B 318  PHE B 322 -1  O  ASP B 318   N  TRP B 270           
SHEET    3   K 3 LEU B 306  VAL B 309 -1  N  ARG B 307   O  LYS B 321           
SHEET    1   L 8 LEU C   6  LYS C   9  0                                        
SHEET    2   L 8 GLY C  13  VAL C  20 -1  O  TYR C  15   N  ARG C   7           
SHEET    3   L 8 GLN C  25  ASP C  32 -1  O  ILE C  29   N  VAL C  16           
SHEET    4   L 8 GLY C 117  GLY C 120  1  O  LEU C 119   N  LEU C  30           
SHEET    5   L 8 PHE C  38  GLY C  41 -1  N  ALA C  39   O  ILE C 118           
SHEET    6   L 8 VAL C  95  ASP C 106  1  O  ILE C 102   N  VAL C  40           
SHEET    7   L 8 LYS C  75  SER C  86 -1  N  GLY C  81   O  ILE C  99           
SHEET    8   L 8 ARG C  61  PRO C  70 -1  N  LYS C  65   O  LEU C  80           
SHEET    1   M 4 LEU C   6  LYS C   9  0                                        
SHEET    2   M 4 GLY C  13  VAL C  20 -1  O  TYR C  15   N  ARG C   7           
SHEET    3   M 4 LYS C  75  SER C  86 -1  O  SER C  86   N  THR C  19           
SHEET    4   M 4 ARG C  61  PRO C  70 -1  N  LYS C  65   O  LEU C  80           
SHEET    1   N 5 GLY C 172  ILE C 176  0                                        
SHEET    2   N 5 PHE C 150  LEU C 154 -1  N  GLN C 153   O  SER C 173           
SHEET    3   N 5 PHE C 341  ASP C 346 -1  O  VAL C 343   N  LEU C 152           
SHEET    4   N 5 ARG C 351  SER C 357 -1  O  ALA C 355   N  TYR C 342           
SHEET    5   N 5 TYR C 184  PRO C 192 -1  N  THR C 191   O  ILE C 352           
SHEET    1   O 5 GLN C 211  ASP C 212  0                                        
SHEET    2   O 5 ILE C 203  ILE C 208 -1  N  ILE C 208   O  GLN C 211           
SHEET    3   O 5 ILE C 283  LEU C 287 -1  O  TYR C 286   N  ARG C 205           
SHEET    4   O 5 SER C 295  ILE C 300 -1  O  ILE C 300   N  ILE C 283           
SHEET    5   O 5 ALA C 369  PHE C 374 -1  O  GLU C 371   N  ARG C 297           
SHEET    1   P 4 SER C 225  VAL C 227  0                                        
SHEET    2   P 4 THR C 331  MET C 333  1  O  MET C 333   N  ILE C 226           
SHEET    3   P 4 LEU C 234  PRO C 237 -1  N  ARG C 235   O  VAL C 332           
SHEET    4   P 4 ILE C 324  SER C 327  1  O  SER C 327   N  LEU C 236           
SHEET    1   Q 3 VAL C 268  TRP C 270  0                                        
SHEET    2   Q 3 ASP C 318  PHE C 322 -1  O  ASP C 318   N  TRP C 270           
SHEET    3   Q 3 LEU C 306  VAL C 309 -1  N  ARG C 307   O  LYS C 321           
SSBOND   1 CYS A  155    CYS A  359                          1555   1555  2.04  
SSBOND   2 CYS A  217    CYS A  382                          1555   1555  2.04  
SSBOND   3 CYS A  269    CYS A  319                          1555   1555  2.04  
SSBOND   4 CYS B  155    CYS B  359                          1555   1555  2.04  
SSBOND   5 CYS B  217    CYS B  382                          1555   1555  2.04  
SSBOND   6 CYS B  269    CYS B  319                          1555   1555  2.04  
SSBOND   7 CYS C  155    CYS C  359                          1555   1555  2.04  
SSBOND   8 CYS C  217    CYS C  382                          1555   1555  2.05  
SSBOND   9 CYS C  269    CYS C  319                          1555   1555  2.04  
CISPEP   1 SER A   22    PRO A   23          0        -0.48                     
CISPEP   2 ARG A  128    PRO A  129          0         0.38                     
CISPEP   3 TYR A  222    ASP A  223          0         1.12                     
CISPEP   4 GLY A  372    PRO A  373          0        -0.93                     
CISPEP   5 SER B   22    PRO B   23          0        -0.69                     
CISPEP   6 ARG B  128    PRO B  129          0         0.52                     
CISPEP   7 TYR B  222    ASP B  223          0         1.17                     
CISPEP   8 GLY B  372    PRO B  373          0        -0.62                     
CISPEP   9 SER C   22    PRO C   23          0        -0.57                     
CISPEP  10 ARG C  128    PRO C  129          0        -0.58                     
CISPEP  11 TYR C  222    ASP C  223          0         0.71                     
CISPEP  12 GLY C  372    PRO C  373          0         0.75                     
SITE     1 AC1 13 GLY A  11  GLN A  12  GLY A  13  ASP A  32                    
SITE     2 AC1 13 GLY A  34  TYR A  71  THR A  72  GLN A  73                    
SITE     3 AC1 13 PHE A 108  ASP A 228  GLY A 230  THR A 232                    
SITE     4 AC1 13 HOH A 643                                                     
SITE     1 AC2 13 GLY B  11  GLN B  12  GLY B  13  ASP B  32                    
SITE     2 AC2 13 GLY B  34  TYR B  71  THR B  72  GLN B  73                    
SITE     3 AC2 13 PHE B 108  ASP B 228  GLY B 230  THR B 232                    
SITE     4 AC2 13 HOH B 689                                                     
SITE     1 AC3 15 GLY C  11  GLN C  12  GLY C  13  ASP C  32                    
SITE     2 AC3 15 GLY C  34  VAL C  69  PRO C  70  TYR C  71                    
SITE     3 AC3 15 THR C  72  GLN C  73  PHE C 108  ASP C 228                    
SITE     4 AC3 15 GLY C 230  THR C 232  HOH C 666                               
CRYST1   82.250  103.202  100.997  90.00 103.03  90.00 P 1 21 1      6          
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      0.012158  0.000000  0.002814        0.00000                         
SCALE2      0.000000  0.009690  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010163        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system