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Database: PDB
Entry: 4ZSP
LinkDB: 4ZSP
Original site: 4ZSP 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           13-MAY-15   4ZSP              
TITLE     BACE CRYSTAL STRUCTURE WITH BICYCLIC AMINOTHIAZINE INHIBITOR          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-SECRETASE 1;                                          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 14-454;                                       
COMPND   5 SYNONYM: ASPARTYL PROTEASE 2,ASP 2,BETA-SITE AMYLOID PRECURSOR       
COMPND   6 PROTEIN CLEAVING ENZYME 1,BETA-SITE APP CLEAVING ENZYME 1,MEMAPSIN-2,
COMPND   7 MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 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, KIAA1149;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ASPARTYL, PROTEASE, BETA-SECRETASE, HYDROLASE-HYDROLASE INHIBITOR     
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.E.TIMM                                                              
REVDAT   2   17-JUN-15 4ZSP    1       JRNL                                     
REVDAT   1   10-JUN-15 4ZSP    0                                                
JRNL        AUTH   L.L.WINNEROSKI,M.A.SCHIFFLER,J.A.ERICKSON,P.C.MAY,S.A.MONK,  
JRNL        AUTH 2 D.E.TIMM,J.E.AUDIA,J.P.BECK,L.N.BOGGS,A.R.BORDERS,R.D.BOYER, 
JRNL        AUTH 3 R.A.BRIER,K.J.HUDZIAK,V.J.KLIMKOWSKI,P.GARCIA LOSADA,        
JRNL        AUTH 4 B.M.MATHES,S.L.STOUT,B.M.WATSON,D.J.MERGOTT                  
JRNL        TITL   PREPARATION AND BIOLOGICAL EVALUATION OF CONFORMATIONALLY    
JRNL        TITL 2 CONSTRAINED BACE1 INHIBITORS.                                
JRNL        REF    BIOORG.MED.CHEM.              V.  23  3260 2015              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   26001341                                                     
JRNL        DOI    10.1016/J.BMC.2015.04.062                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.91 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0069                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.91                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 75.16                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 79061                          
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) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.300                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1039                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.91                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.96                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5737                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.14                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.3260                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6115                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 838                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.62                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -3.54000                                             
REMARK   3    B22 (A**2) : 5.53000                                              
REMARK   3    B33 (A**2) : -2.00000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.136         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.140         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.128         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.796         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.944                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6371 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8675 ; 1.462 ; 1.956       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   789 ; 6.556 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   292 ;35.679 ;23.973       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1007 ;13.674 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;17.608 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   945 ; 0.099 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4941 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  3126 ; 1.955 ; 2.940       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3907 ; 3.000 ; 4.398       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3245 ; 3.013 ; 3.218       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10630 ; 7.039 ;26.550       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4ZSP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-MAY-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000209822.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97929                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 92995                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 91.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 7.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG8000, SODIUM CACODYLATE, AMMONIUM     
REMARK 280  SULFATE, PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       43.32350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       65.60250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.84450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       65.60250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.32350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.84450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 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     MET A   -48                                                      
REMARK 465     ALA A   -47                                                      
REMARK 465     GLY A   -46                                                      
REMARK 465     VAL A   -45                                                      
REMARK 465     LEU A   -44                                                      
REMARK 465     PRO A   -43                                                      
REMARK 465     ALA A   -42                                                      
REMARK 465     HIS A   -41                                                      
REMARK 465     GLY A   -40                                                      
REMARK 465     THR A   -39                                                      
REMARK 465     GLN A   -38                                                      
REMARK 465     HIS A   -37                                                      
REMARK 465     GLY A   -36                                                      
REMARK 465     ILE A   -35                                                      
REMARK 465     ARG A   -34                                                      
REMARK 465     LEU A   -33                                                      
REMARK 465     PRO A   -32                                                      
REMARK 465     LEU A   -31                                                      
REMARK 465     ARG A   -30                                                      
REMARK 465     SER A   -29                                                      
REMARK 465     GLY A   -28                                                      
REMARK 465     LEU A   -27                                                      
REMARK 465     GLY A   -26                                                      
REMARK 465     GLY A   -25                                                      
REMARK 465     ALA A   -24                                                      
REMARK 465     PRO A   -23                                                      
REMARK 465     LEU A   -22                                                      
REMARK 465     GLY A   -21                                                      
REMARK 465     LEU A   -20                                                      
REMARK 465     ARG A   -19                                                      
REMARK 465     LEU A   -18                                                      
REMARK 465     PRO A   -17                                                      
REMARK 465     ARG A   -16                                                      
REMARK 465     GLU A   -15                                                      
REMARK 465     THR A   -14                                                      
REMARK 465     ASP A   -13                                                      
REMARK 465     GLU A   -12                                                      
REMARK 465     GLU A   -11                                                      
REMARK 465     PRO A   -10                                                      
REMARK 465     GLU A    -9                                                      
REMARK 465     GLU A    -8                                                      
REMARK 465     PRO A    -7                                                      
REMARK 465     GLY A    -6                                                      
REMARK 465     ARG A    -5                                                      
REMARK 465     ILE A   386                                                      
REMARK 465     PRO A   387                                                      
REMARK 465     GLN A   388                                                      
REMARK 465     THR A   389                                                      
REMARK 465     ASP A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     SER A   392                                                      
REMARK 465     THR A   393                                                      
REMARK 465     MET B   -48                                                      
REMARK 465     ALA B   -47                                                      
REMARK 465     GLY B   -46                                                      
REMARK 465     VAL B   -45                                                      
REMARK 465     LEU B   -44                                                      
REMARK 465     PRO B   -43                                                      
REMARK 465     ALA B   -42                                                      
REMARK 465     HIS B   -41                                                      
REMARK 465     GLY B   -40                                                      
REMARK 465     THR B   -39                                                      
REMARK 465     GLN B   -38                                                      
REMARK 465     HIS B   -37                                                      
REMARK 465     GLY B   -36                                                      
REMARK 465     ILE B   -35                                                      
REMARK 465     ARG B   -34                                                      
REMARK 465     LEU B   -33                                                      
REMARK 465     PRO B   -32                                                      
REMARK 465     LEU B   -31                                                      
REMARK 465     ARG B   -30                                                      
REMARK 465     SER B   -29                                                      
REMARK 465     GLY B   -28                                                      
REMARK 465     LEU B   -27                                                      
REMARK 465     GLY B   -26                                                      
REMARK 465     GLY B   -25                                                      
REMARK 465     ALA B   -24                                                      
REMARK 465     PRO B   -23                                                      
REMARK 465     LEU B   -22                                                      
REMARK 465     GLY B   -21                                                      
REMARK 465     LEU B   -20                                                      
REMARK 465     ARG B   -19                                                      
REMARK 465     LEU B   -18                                                      
REMARK 465     PRO B   -17                                                      
REMARK 465     ARG B   -16                                                      
REMARK 465     GLU B   -15                                                      
REMARK 465     THR B   -14                                                      
REMARK 465     ASP B   -13                                                      
REMARK 465     GLU B   -12                                                      
REMARK 465     GLU B   -11                                                      
REMARK 465     PRO B   -10                                                      
REMARK 465     GLU B    -9                                                      
REMARK 465     GLU B    -8                                                      
REMARK 465     PRO B    -7                                                      
REMARK 465     GLY B    -6                                                      
REMARK 465     ARG B    -5                                                      
REMARK 465     ARG B    -4                                                      
REMARK 465     ILE B   386                                                      
REMARK 465     PRO B   387                                                      
REMARK 465     GLN B   388                                                      
REMARK 465     THR B   389                                                      
REMARK 465     ASP B   390                                                      
REMARK 465     GLU B   391                                                      
REMARK 465     SER B   392                                                      
REMARK 465     THR B   393                                                      
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 A   538     O    HOH A   611              2.14            
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    ASN A 114        3.07     81.34                                   
REMARK 500    TRP A 197      -82.32   -133.92                                   
REMARK 500    ALA A 272      125.45    -36.46                                   
REMARK 500    THR A 314       13.54     50.09                                   
REMARK 500    SER A 315     -161.47    -40.91                                   
REMARK 500    HIS B  89       50.74    -96.80                                   
REMARK 500    ASN B 114       -2.70     79.40                                   
REMARK 500    TRP B 197      -85.37   -134.52                                   
REMARK 500    ALA B 323       31.40    -99.14                                   
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 TRP B  197     TYR B  198                  147.44                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 917        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH B 921        DISTANCE =  6.49 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4RZ A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 4RZ B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4ZSM   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZSQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4ZSR   RELATED DB: PDB                                   
DBREF  4ZSP A  -47   393  UNP    P56817   BACE1_HUMAN     14    454             
DBREF  4ZSP B  -47   393  UNP    P56817   BACE1_HUMAN     14    454             
SEQADV 4ZSP MET A  -48  UNP  P56817              INITIATING METHIONINE          
SEQADV 4ZSP MET B  -48  UNP  P56817              INITIATING METHIONINE          
SEQRES   1 A  442  MET ALA GLY VAL LEU PRO ALA HIS GLY THR GLN HIS GLY          
SEQRES   2 A  442  ILE ARG LEU PRO LEU ARG SER GLY LEU GLY GLY ALA PRO          
SEQRES   3 A  442  LEU GLY LEU ARG LEU PRO ARG GLU THR ASP GLU GLU PRO          
SEQRES   4 A  442  GLU GLU PRO GLY ARG ARG GLY SER PHE VAL GLU MET VAL          
SEQRES   5 A  442  ASP ASN LEU ARG GLY LYS SER GLY GLN GLY TYR TYR VAL          
SEQRES   6 A  442  GLU MET THR VAL GLY SER PRO PRO GLN THR LEU ASN ILE          
SEQRES   7 A  442  LEU VAL ASP THR GLY SER SER ASN PHE ALA VAL GLY ALA          
SEQRES   8 A  442  ALA PRO HIS PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN          
SEQRES   9 A  442  LEU SER SER THR TYR ARG ASP LEU ARG LYS GLY VAL TYR          
SEQRES  10 A  442  VAL PRO TYR THR GLN GLY LYS TRP GLU GLY GLU LEU GLY          
SEQRES  11 A  442  THR ASP LEU VAL SER ILE PRO HIS GLY PRO ASN VAL THR          
SEQRES  12 A  442  VAL ARG ALA ASN ILE ALA ALA ILE THR GLU SER ASP LYS          
SEQRES  13 A  442  PHE PHE ILE ASN GLY SER ASN TRP GLU GLY ILE LEU GLY          
SEQRES  14 A  442  LEU ALA TYR ALA GLU ILE ALA ARG PRO ASP ASP SER LEU          
SEQRES  15 A  442  GLU PRO PHE PHE ASP SER LEU VAL LYS GLN THR HIS VAL          
SEQRES  16 A  442  PRO ASN LEU PHE SER LEU GLN LEU CYS GLY ALA GLY PHE          
SEQRES  17 A  442  PRO LEU ASN GLN SER GLU VAL LEU ALA SER VAL GLY GLY          
SEQRES  18 A  442  SER MET ILE ILE GLY GLY ILE ASP HIS SER LEU TYR THR          
SEQRES  19 A  442  GLY SER LEU TRP TYR THR PRO ILE ARG ARG GLU TRP TYR          
SEQRES  20 A  442  TYR GLU VAL ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN          
SEQRES  21 A  442  ASP LEU LYS MET ASP CYS LYS GLU TYR ASN TYR ASP LYS          
SEQRES  22 A  442  SER ILE VAL ASP SER GLY THR THR ASN LEU ARG LEU PRO          
SEQRES  23 A  442  LYS LYS VAL PHE GLU ALA ALA VAL LYS SER ILE LYS ALA          
SEQRES  24 A  442  ALA SER SER THR GLU LYS PHE PRO ASP GLY PHE TRP LEU          
SEQRES  25 A  442  GLY GLU GLN LEU VAL CYS TRP GLN ALA GLY THR THR PRO          
SEQRES  26 A  442  TRP ASN ILE PHE PRO VAL ILE SER LEU TYR LEU MET GLY          
SEQRES  27 A  442  GLU VAL THR ASN GLN SER PHE ARG ILE THR ILE LEU PRO          
SEQRES  28 A  442  GLN GLN TYR LEU ARG PRO VAL GLU ASP VAL ALA THR SER          
SEQRES  29 A  442  GLN ASP ASP CYS TYR LYS PHE ALA ILE SER GLN SER SER          
SEQRES  30 A  442  THR GLY THR VAL MET GLY ALA VAL ILE MET GLU GLY PHE          
SEQRES  31 A  442  TYR VAL VAL PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE          
SEQRES  32 A  442  ALA VAL SER ALA CYS HIS VAL HIS ASP GLU PHE ARG THR          
SEQRES  33 A  442  ALA ALA VAL GLU GLY PRO PHE VAL THR LEU ASP MET GLU          
SEQRES  34 A  442  ASP CYS GLY TYR ASN ILE PRO GLN THR ASP GLU SER THR          
SEQRES   1 B  442  MET ALA GLY VAL LEU PRO ALA HIS GLY THR GLN HIS GLY          
SEQRES   2 B  442  ILE ARG LEU PRO LEU ARG SER GLY LEU GLY GLY ALA PRO          
SEQRES   3 B  442  LEU GLY LEU ARG LEU PRO ARG GLU THR ASP GLU GLU PRO          
SEQRES   4 B  442  GLU GLU PRO GLY ARG ARG GLY SER PHE VAL GLU MET VAL          
SEQRES   5 B  442  ASP ASN LEU ARG GLY LYS SER GLY GLN GLY TYR TYR VAL          
SEQRES   6 B  442  GLU MET THR VAL GLY SER PRO PRO GLN THR LEU ASN ILE          
SEQRES   7 B  442  LEU VAL ASP THR GLY SER SER ASN PHE ALA VAL GLY ALA          
SEQRES   8 B  442  ALA PRO HIS PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN          
SEQRES   9 B  442  LEU SER SER THR TYR ARG ASP LEU ARG LYS GLY VAL TYR          
SEQRES  10 B  442  VAL PRO TYR THR GLN GLY LYS TRP GLU GLY GLU LEU GLY          
SEQRES  11 B  442  THR ASP LEU VAL SER ILE PRO HIS GLY PRO ASN VAL THR          
SEQRES  12 B  442  VAL ARG ALA ASN ILE ALA ALA ILE THR GLU SER ASP LYS          
SEQRES  13 B  442  PHE PHE ILE ASN GLY SER ASN TRP GLU GLY ILE LEU GLY          
SEQRES  14 B  442  LEU ALA TYR ALA GLU ILE ALA ARG PRO ASP ASP SER LEU          
SEQRES  15 B  442  GLU PRO PHE PHE ASP SER LEU VAL LYS GLN THR HIS VAL          
SEQRES  16 B  442  PRO ASN LEU PHE SER LEU GLN LEU CYS GLY ALA GLY PHE          
SEQRES  17 B  442  PRO LEU ASN GLN SER GLU VAL LEU ALA SER VAL GLY GLY          
SEQRES  18 B  442  SER MET ILE ILE GLY GLY ILE ASP HIS SER LEU TYR THR          
SEQRES  19 B  442  GLY SER LEU TRP TYR THR PRO ILE ARG ARG GLU TRP TYR          
SEQRES  20 B  442  TYR GLU VAL ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN          
SEQRES  21 B  442  ASP LEU LYS MET ASP CYS LYS GLU TYR ASN TYR ASP LYS          
SEQRES  22 B  442  SER ILE VAL ASP SER GLY THR THR ASN LEU ARG LEU PRO          
SEQRES  23 B  442  LYS LYS VAL PHE GLU ALA ALA VAL LYS SER ILE LYS ALA          
SEQRES  24 B  442  ALA SER SER THR GLU LYS PHE PRO ASP GLY PHE TRP LEU          
SEQRES  25 B  442  GLY GLU GLN LEU VAL CYS TRP GLN ALA GLY THR THR PRO          
SEQRES  26 B  442  TRP ASN ILE PHE PRO VAL ILE SER LEU TYR LEU MET GLY          
SEQRES  27 B  442  GLU VAL THR ASN GLN SER PHE ARG ILE THR ILE LEU PRO          
SEQRES  28 B  442  GLN GLN TYR LEU ARG PRO VAL GLU ASP VAL ALA THR SER          
SEQRES  29 B  442  GLN ASP ASP CYS TYR LYS PHE ALA ILE SER GLN SER SER          
SEQRES  30 B  442  THR GLY THR VAL MET GLY ALA VAL ILE MET GLU GLY PHE          
SEQRES  31 B  442  TYR VAL VAL PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE          
SEQRES  32 B  442  ALA VAL SER ALA CYS HIS VAL HIS ASP GLU PHE ARG THR          
SEQRES  33 B  442  ALA ALA VAL GLU GLY PRO PHE VAL THR LEU ASP MET GLU          
SEQRES  34 B  442  ASP CYS GLY TYR ASN ILE PRO GLN THR ASP GLU SER THR          
HET    4RZ  A 401      21                                                       
HET    GOL  A 402       6                                                       
HET    4RZ  B 401      21                                                       
HET    GOL  B 402       6                                                       
HETNAM     4RZ N-[(4AS,6S,8AR)-2-AMINO-4A,5,6,7,8,8A-HEXAHYDRO-4H-3,1-          
HETNAM   2 4RZ  BENZOTHIAZIN-6-YL]-3-CHLOROBENZAMIDE                            
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   3  4RZ    2(C15 H18 CL N3 O S)                                         
FORMUL   4  GOL    2(C3 H8 O3)                                                  
FORMUL   7  HOH   *838(H2 O)                                                    
HELIX    1 AA1 GLN A   53  SER A   57  5                                   5    
HELIX    2 AA2 TYR A  123  ALA A  127  5                                   5    
HELIX    3 AA3 PRO A  135  THR A  144  1                                  10    
HELIX    4 AA4 ASN A  162  SER A  169  1                                   8    
HELIX    5 AA5 ASP A  180  SER A  182  5                                   3    
HELIX    6 AA6 ASP A  216  TYR A  222  5                                   7    
HELIX    7 AA7 LYS A  238  SER A  252  1                                  15    
HELIX    8 AA8 PRO A  258  LEU A  263  1                                   6    
HELIX    9 AA9 PRO A  276  PHE A  280  5                                   5    
HELIX   10 AB1 LEU A  301  TYR A  305  1                                   5    
HELIX   11 AB2 GLY A  334  GLU A  339  1                                   6    
HELIX   12 AB3 ARG A  347  ARG A  349  5                                   3    
HELIX   13 AB4 ASP A  378  GLY A  383  5                                   6    
HELIX   14 AB5 GLN B   53  SER B   57  5                                   5    
HELIX   15 AB6 TYR B  123  ALA B  127  5                                   5    
HELIX   16 AB7 PRO B  135  THR B  144  1                                  10    
HELIX   17 AB8 ASN B  162  SER B  169  1                                   8    
HELIX   18 AB9 ASP B  180  SER B  182  5                                   3    
HELIX   19 AC1 ASP B  216  TYR B  222  5                                   7    
HELIX   20 AC2 LYS B  238  SER B  252  1                                  15    
HELIX   21 AC3 PRO B  258  LEU B  263  1                                   6    
HELIX   22 AC4 PRO B  276  PHE B  280  5                                   5    
HELIX   23 AC5 LEU B  301  TYR B  305  1                                   5    
HELIX   24 AC6 GLY B  334  GLU B  339  1                                   6    
HELIX   25 AC7 ASP B  378  GLY B  383  5                                   6    
SHEET    1 AA1 8 LEU A   6  LYS A   9  0                                        
SHEET    2 AA1 8 GLY A  13  VAL A  20 -1  O  TYR A  15   N  ARG A   7           
SHEET    3 AA1 8 GLN A  25  ASP A  32 -1  O  ILE A  29   N  VAL A  16           
SHEET    4 AA1 8 GLY A 117  GLY A 120  1  O  LEU A 119   N  LEU A  30           
SHEET    5 AA1 8 PHE A  38  GLY A  41 -1  N  ALA A  39   O  ILE A 118           
SHEET    6 AA1 8 VAL A  95  ASP A 106  1  O  ILE A 102   N  VAL A  40           
SHEET    7 AA1 8 LYS A  75  SER A  86 -1  N  GLY A  81   O  ILE A  99           
SHEET    8 AA1 8 ARG A  61  PRO A  70 -1  N  VAL A  69   O  TRP A  76           
SHEET    1 AA2 4 LEU A   6  LYS A   9  0                                        
SHEET    2 AA2 4 GLY A  13  VAL A  20 -1  O  TYR A  15   N  ARG A   7           
SHEET    3 AA2 4 LYS A  75  SER A  86 -1  O  SER A  86   N  THR A  19           
SHEET    4 AA2 4 ARG A  61  PRO A  70 -1  N  VAL A  69   O  TRP A  76           
SHEET    1 AA3 5 GLY A 172  ILE A 176  0                                        
SHEET    2 AA3 5 PHE A 150  LEU A 154 -1  N  GLN A 153   O  SER A 173           
SHEET    3 AA3 5 PHE A 341  ASP A 346 -1  O  VAL A 343   N  LEU A 152           
SHEET    4 AA3 5 ARG A 351  SER A 357 -1  O  ALA A 355   N  TYR A 342           
SHEET    5 AA3 5 TYR A 184  PRO A 192 -1  N  THR A 191   O  ILE A 352           
SHEET    1 AA4 5 GLU A 200  VAL A 201  0                                        
SHEET    2 AA4 5 SER A 225  VAL A 227 -1  O  SER A 225   N  VAL A 201           
SHEET    3 AA4 5 THR A 331  MET A 333  1  O  MET A 333   N  ILE A 226           
SHEET    4 AA4 5 LEU A 234  PRO A 237 -1  N  ARG A 235   O  VAL A 332           
SHEET    5 AA4 5 ILE A 324  SER A 327  1  O  SER A 325   N  LEU A 236           
SHEET    1 AA5 5 GLN A 211  ASP A 212  0                                        
SHEET    2 AA5 5 ILE A 203  ILE A 208 -1  N  ILE A 208   O  GLN A 211           
SHEET    3 AA5 5 ILE A 283  MET A 288 -1  O  TYR A 286   N  ARG A 205           
SHEET    4 AA5 5 GLN A 294  ILE A 300 -1  O  ILE A 300   N  ILE A 283           
SHEET    5 AA5 5 ALA A 369  VAL A 375 -1  O  GLU A 371   N  ARG A 297           
SHEET    1 AA6 3 VAL A 268  TRP A 270  0                                        
SHEET    2 AA6 3 ASP A 318  PHE A 322 -1  O  ASP A 318   N  TRP A 270           
SHEET    3 AA6 3 LEU A 306  VAL A 309 -1  N  ARG A 307   O  LYS A 321           
SHEET    1 AA7 8 LEU B   6  LYS B   9  0                                        
SHEET    2 AA7 8 GLY B  13  VAL B  20 -1  O  TYR B  15   N  ARG B   7           
SHEET    3 AA7 8 GLN B  25  ASP B  32 -1  O  LEU B  27   N  MET B  18           
SHEET    4 AA7 8 GLY B 117  GLY B 120  1  O  LEU B 119   N  LEU B  30           
SHEET    5 AA7 8 PHE B  38  GLY B  41 -1  N  ALA B  39   O  ILE B 118           
SHEET    6 AA7 8 THR B  94  ASP B 106  1  O  ALA B 100   N  PHE B  38           
SHEET    7 AA7 8 LYS B  75  SER B  86 -1  N  GLU B  77   O  GLU B 104           
SHEET    8 AA7 8 ARG B  61  PRO B  70 -1  N  VAL B  69   O  TRP B  76           
SHEET    1 AA8 4 LEU B   6  LYS B   9  0                                        
SHEET    2 AA8 4 GLY B  13  VAL B  20 -1  O  TYR B  15   N  ARG B   7           
SHEET    3 AA8 4 LYS B  75  SER B  86 -1  O  SER B  86   N  THR B  19           
SHEET    4 AA8 4 ARG B  61  PRO B  70 -1  N  VAL B  69   O  TRP B  76           
SHEET    1 AA9 5 GLY B 172  ILE B 176  0                                        
SHEET    2 AA9 5 PHE B 150  LEU B 154 -1  N  GLN B 153   O  SER B 173           
SHEET    3 AA9 5 PHE B 341  ASP B 346 -1  O  PHE B 345   N  PHE B 150           
SHEET    4 AA9 5 ARG B 351  SER B 357 -1  O  ALA B 355   N  TYR B 342           
SHEET    5 AA9 5 TYR B 184  PRO B 192 -1  N  THR B 191   O  ILE B 352           
SHEET    1 AB1 5 GLN B 211  ASP B 212  0                                        
SHEET    2 AB1 5 ILE B 203  ILE B 208 -1  N  ILE B 208   O  GLN B 211           
SHEET    3 AB1 5 ILE B 283  MET B 288 -1  O  TYR B 286   N  ARG B 205           
SHEET    4 AB1 5 GLN B 294  ILE B 300 -1  O  ILE B 300   N  ILE B 283           
SHEET    5 AB1 5 ALA B 369  VAL B 375 -1  O  ALA B 369   N  THR B 299           
SHEET    1 AB2 4 SER B 225  VAL B 227  0                                        
SHEET    2 AB2 4 THR B 331  MET B 333  1  O  MET B 333   N  ILE B 226           
SHEET    3 AB2 4 LEU B 234  PRO B 237 -1  N  ARG B 235   O  VAL B 332           
SHEET    4 AB2 4 ILE B 324  SER B 327  1  O  SER B 325   N  LEU B 236           
SHEET    1 AB3 3 VAL B 268  TRP B 270  0                                        
SHEET    2 AB3 3 ASP B 318  PHE B 322 -1  O  ASP B 318   N  TRP B 270           
SHEET    3 AB3 3 LEU B 306  VAL B 309 -1  N  ARG B 307   O  LYS B 321           
SSBOND   1 CYS A  155    CYS A  359                          1555   1555  2.15  
SSBOND   2 CYS A  217    CYS A  382                          1555   1555  2.09  
SSBOND   3 CYS A  269    CYS A  319                          1555   1555  2.11  
SSBOND   4 CYS B  155    CYS B  359                          1555   1555  2.15  
SSBOND   5 CYS B  217    CYS B  382                          1555   1555  2.07  
SSBOND   6 CYS B  269    CYS B  319                          1555   1555  2.10  
CISPEP   1 SER A   22    PRO A   23          0        -4.65                     
CISPEP   2 ARG A  128    PRO A  129          0         4.76                     
CISPEP   3 TYR A  222    ASP A  223          0        -1.87                     
CISPEP   4 GLY A  372    PRO A  373          0         0.95                     
CISPEP   5 SER B   22    PRO B   23          0        -7.82                     
CISPEP   6 ARG B  128    PRO B  129          0         2.03                     
CISPEP   7 TYR B  222    ASP B  223          0        -0.30                     
CISPEP   8 GLY B  372    PRO B  373          0         0.16                     
SITE     1 AC1 13 SER A  10  GLY A  11  GLN A  12  GLY A  13                    
SITE     2 AC1 13 ASP A  32  GLY A  34  TYR A  71  TRP A 115                    
SITE     3 AC1 13 ASP A 228  SER A 229  GLY A 230  THR A 232                    
SITE     4 AC1 13 HOH A 618                                                     
SITE     1 AC2  8 ASP A 318  HOH A 513  HOH A 567  HOH A 729                    
SITE     2 AC2  8 SER B  58  THR B  59  ARG B  61  ARG B  96                    
SITE     1 AC3 13 SER B  10  GLY B  11  GLN B  12  GLY B  13                    
SITE     2 AC3 13 ASP B  32  GLY B  34  TYR B  71  TRP B 115                    
SITE     3 AC3 13 ASP B 228  SER B 229  GLY B 230  THR B 232                    
SITE     4 AC3 13 HOH B 544                                                     
SITE     1 AC4  8 SER A  58  THR A  59  ARG A  61  ARG A  96                    
SITE     2 AC4  8 ASP B 318  HOH B 528  HOH B 596  HOH B 635                    
CRYST1   86.647   91.689  131.205  90.00  90.00  90.00 P 21 21 21    8          
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      0.011541  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007622        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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