GenomeNet

Database: PDB
Entry: 2OF0
LinkDB: 2OF0
Original site: 2OF0 
HEADER    HYDROLASE                               02-JAN-07   2OF0              
TITLE     X-RAY CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 5   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-SECRETASE 1;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: PROTEASE DOMAIN;                                           
COMPND   5 SYNONYM: BETA-SITE APP CLEAVING ENZYME 1, BETA-SITE AMYLOID PRECURSOR
COMPND   6 PROTEIN CLEAVING ENZYME 1, MEMBRANE-ASSOCIATED ASPARTIC PROTEASE 2,  
COMPND   7 MEMAPSIN-2, ASPARTYL PROTEASE 2, ASP 2, ASP2;                        
COMPND   8 EC: 3.4.23.46;                                                       
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 MUTATION: 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 BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET                                       
KEYWDS    ALTERNATIVE SPLICING, ALZHEIMER'S DISEASE, ASPARTIC PROTEASE,         
KEYWDS   2 ASPARTYL PROTEASE, BASE, BETA-SECRETASE, GLYCOPROTEIN, HYDROLASE,    
KEYWDS   3 MEMAPSIN 2, TRANSMEMBRANE, ZYMOGEN                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.PATEL                                                               
REVDAT   6   30-AUG-23 2OF0    1       REMARK                                   
REVDAT   5   20-OCT-21 2OF0    1       REMARK SEQADV                            
REVDAT   4   18-OCT-17 2OF0    1       REMARK                                   
REVDAT   3   24-FEB-09 2OF0    1       VERSN                                    
REVDAT   2   01-MAY-07 2OF0    1       JRNL                                     
REVDAT   1   13-MAR-07 2OF0    0                                                
JRNL        AUTH   C.W.MURRAY,O.CALLAGHAN,G.CHESSARI,A.CLEASBY,M.CONGREVE,      
JRNL        AUTH 2 M.FREDERICKSON,M.J.HARTSHORN,R.MCMENAMIN,S.PATEL,N.WALLIS    
JRNL        TITL   APPLICATION OF FRAGMENT SCREENING BY X-RAY CRYSTALLOGRAPHY   
JRNL        TITL 2 TO BETA-SECRETASE.                                           
JRNL        REF    J.MED.CHEM.                   V.  50  1116 2007              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   17315856                                                     
JRNL        DOI    10.1021/JM0611962                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019C                                     
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.19                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 23631                          
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) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.280                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1278                            
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) : 2.25                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.31                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1420                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 82.15                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 90                           
REMARK   3   BIN FREE R VALUE                    : 0.3320                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2966                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 179                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.41                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.37000                                             
REMARK   3    B22 (A**2) : -0.37000                                             
REMARK   3    B33 (A**2) : 0.56000                                              
REMARK   3    B12 (A**2) : -0.19000                                             
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): 0.272         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.236         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.174         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.964         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.934                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.890                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3052 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  2027 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4150 ; 1.407 ; 1.953       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  4915 ; 0.890 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   375 ; 6.986 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   137 ;36.126 ;24.015       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   488 ;14.774 ;15.092       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;12.739 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   453 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3404 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   637 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   634 ; 0.193 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  2118 ; 0.204 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1496 ; 0.185 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  1566 ; 0.089 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    46 ; 0.147 ; 0.200       
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):    16 ; 0.188 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    66 ; 0.251 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.113 ; 0.200       
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):  1871 ; 0.055 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   767 ; 0.021 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3025 ; 0.076 ; 6.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1181 ; 0.073 ; 6.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1125 ; 0.089 ; 7.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
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 : BABINET MODEL WITH 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 ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2OF0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-JAN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041052.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-OCT-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU300                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54180                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (SCALA)                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24904                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 38.200                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: C-SEARCH (IN-HOUSE MR PROGRAM                         
REMARK 200 STARTING MODEL: PDB ENTRY 1W50                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20-22.5% (W/V) PEG 5000                  
REMARK 280  MONOMETHYLETHER (MME), 200 MM SODIUM CITRATE (PH 6.6), 200 MM       
REMARK 280  AMMONIUM IODIDE, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.41233            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      112.82467            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       84.61850            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      141.03083            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       28.20617            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       56.41233            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000      112.82467            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      141.03083            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       84.61850            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       28.20617            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
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 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     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     LYS A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
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 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A    7   NE   CZ   NH1  NH2                                  
REMARK 480     ARG A   64   NE   CZ   NH1  NH2                                  
REMARK 480     GLN A  271   CG   CD   OE1  NE2                                  
REMARK 480     ASP A  381   CG   OD1  OD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  64   CD    ARG A  64   NE     -0.265                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  64   CG  -  CD  -  NE  ANGL. DEV. =  18.7 DEGREES          
REMARK 500    ARG A  64   CD  -  NE  -  CZ  ANGL. DEV. =   9.2 DEGREES          
REMARK 500    GLN A 271   CA  -  CB  -  CG  ANGL. DEV. =  14.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  89       44.62   -103.82                                   
REMARK 500    TRP A 197      -84.66   -142.88                                   
REMARK 500    ASN A 209       -2.10     71.45                                   
REMARK 500    ASP A 216      103.85    -48.99                                   
REMARK 500    ASN A 293       11.56     59.45                                   
REMARK 500    ALA A 358       -8.87    -56.83                                   
REMARK 500    ASP A 363     -142.04   -123.22                                   
REMARK 500    PHE A 365      -92.70    -88.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A   7         0.08    SIDE CHAIN                              
REMARK 500    ARG A  64         0.08    SIDE CHAIN                              
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 IOD A 386                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 387                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 388                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 389                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CMZ A 390                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OHK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH 1-AMINO-          
REMARK 900 ISOQUINOLINE                                                         
REMARK 900 RELATED ID: 2OHL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH 2-AMINOQUINOLINE  
REMARK 900 RELATED ID: 2OHM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH 2,3-              
REMARK 900 DIAMINOPYRIDINE                                                      
REMARK 900 RELATED ID: 2OHN   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 4        
REMARK 900 RELATED ID: 2OHP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 3        
REMARK 900 RELATED ID: 2OHQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 4        
REMARK 900 RELATED ID: 2OHR   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 6A       
REMARK 900 RELATED ID: 2OHS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 6B       
REMARK 900 RELATED ID: 2OHT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 7        
REMARK 900 RELATED ID: 2OHU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF BETA SECRETASE COMPLEXED WITH COMPOUND 8B       
DBREF  2OF0 A  -16   385  UNP    P56817   BACE1_HUMAN     45    446             
SEQADV 2OF0 LYS A   -5  UNP  P56817    ARG    56 ENGINEERED MUTATION            
SEQADV 2OF0 LYS A   -4  UNP  P56817    ARG    57 ENGINEERED MUTATION            
SEQRES   1 A  402  ARG GLU THR ASP GLU GLU PRO GLU GLU PRO GLY LYS LYS          
SEQRES   2 A  402  GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG GLY LYS          
SEQRES   3 A  402  SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL GLY SER          
SEQRES   4 A  402  PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR GLY SER          
SEQRES   5 A  402  SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO PHE LEU          
SEQRES   6 A  402  HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR TYR ARG          
SEQRES   7 A  402  ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR GLN GLY          
SEQRES   8 A  402  LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL SER ILE          
SEQRES   9 A  402  PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN ILE ALA          
SEQRES  10 A  402  ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN GLY SER          
SEQRES  11 A  402  ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA GLU ILE          
SEQRES  12 A  402  ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE ASP SER          
SEQRES  13 A  402  LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE SER LEU          
SEQRES  14 A  402  GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN SER GLU          
SEQRES  15 A  402  VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE GLY GLY          
SEQRES  16 A  402  ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP TYR THR          
SEQRES  17 A  402  PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE ILE VAL          
SEQRES  18 A  402  ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET ASP CYS          
SEQRES  19 A  402  LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP SER GLY          
SEQRES  20 A  402  THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE GLU ALA          
SEQRES  21 A  402  ALA VAL LYS SER ILE LYS ALA ALA SER SER THR GLU LYS          
SEQRES  22 A  402  PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU VAL CYS          
SEQRES  23 A  402  TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE PRO VAL          
SEQRES  24 A  402  ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN GLN SER          
SEQRES  25 A  402  PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU ARG PRO          
SEQRES  26 A  402  VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS TYR LYS          
SEQRES  27 A  402  PHE ALA ILE SER GLN SER SER THR GLY THR VAL MET GLY          
SEQRES  28 A  402  ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE ASP ARG          
SEQRES  29 A  402  ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA CYS HIS          
SEQRES  30 A  402  VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU GLY PRO          
SEQRES  31 A  402  PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR ASN              
HET    IOD  A 386       1                                                       
HET    IOD  A 387       1                                                       
HET    IOD  A 388       1                                                       
HET    DMS  A 389       4                                                       
HET    CMZ  A 390      19                                                       
HETNAM     IOD IODIDE ION                                                       
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     CMZ (2S)-1-(2,5-DIMETHYLPHENOXY)-3-MORPHOLIN-4-YLPROPAN-2-           
HETNAM   2 CMZ  OL                                                              
HETSYN     CMZ (S)-1-(2,5-DIMETHYLPHENOXY)-3-MORPHOLINOPROPAN-2-OL              
FORMUL   2  IOD    3(I 1-)                                                      
FORMUL   5  DMS    C2 H6 O S                                                    
FORMUL   6  CMZ    C15 H23 N O3                                                 
FORMUL   7  HOH   *179(H2 O)                                                    
HELIX    1   1 GLN A   53  SER A   57  5                                   5    
HELIX    2   2 TYR A  123  ALA A  127  5                                   5    
HELIX    3   3 PRO A  135  GLN A  143  1                                   9    
HELIX    4   4 ASP A  180  SER A  182  5                                   3    
HELIX    5   5 ASP A  216  ASN A  221  1                                   6    
HELIX    6   6 LYS A  238  SER A  252  1                                  15    
HELIX    7   7 PRO A  258  LEU A  263  1                                   6    
HELIX    8   8 PRO A  276  PHE A  280  5                                   5    
HELIX    9   9 LEU A  301  TYR A  305  1                                   5    
HELIX   10  10 GLY A  334  GLU A  339  1                                   6    
HELIX   11  11 ARG A  347  ARG A  349  5                                   3    
HELIX   12  12 MET A  379  GLY A  383  5                                   5    
SHEET    1   A 9 ARG A  61  TYR A  71  0                                        
SHEET    2   A 9 GLY A  74  SER A  86 -1  O  TRP A  76   N  VAL A  69           
SHEET    3   A 9 TYR A  14  VAL A  20 -1  N  THR A  19   O  SER A  86           
SHEET    4   A 9 LEU A   6  LYS A   9 -1  N  ARG A   7   O  TYR A  15           
SHEET    5   A 9 SER A 169  ILE A 176 -1  O  GLY A 172   N  LEU A   6           
SHEET    6   A 9 PHE A 150  LEU A 154 -1  N  GLN A 153   O  SER A 173           
SHEET    7   A 9 PHE A 341  ASP A 346 -1  O  PHE A 345   N  PHE A 150           
SHEET    8   A 9 ARG A 351  SER A 357 -1  O  GLY A 353   N  VAL A 344           
SHEET    9   A 9 TYR A 184  PRO A 192 -1  N  TRP A 189   O  PHE A 354           
SHEET    1   B13 ARG A  61  TYR A  71  0                                        
SHEET    2   B13 GLY A  74  SER A  86 -1  O  TRP A  76   N  VAL A  69           
SHEET    3   B13 VAL A  95  ASP A 106 -1  O  ASP A 106   N  LYS A  75           
SHEET    4   B13 PHE A  38  GLY A  41  1  N  VAL A  40   O  ILE A 102           
SHEET    5   B13 GLY A 117  GLY A 120 -1  O  ILE A 118   N  ALA A  39           
SHEET    6   B13 GLN A  25  ASP A  32  1  N  LEU A  30   O  LEU A 119           
SHEET    7   B13 TYR A  14  VAL A  20 -1  N  TYR A  14   O  VAL A  31           
SHEET    8   B13 LEU A   6  LYS A   9 -1  N  ARG A   7   O  TYR A  15           
SHEET    9   B13 SER A 169  ILE A 176 -1  O  GLY A 172   N  LEU A   6           
SHEET   10   B13 PHE A 150  LEU A 154 -1  N  GLN A 153   O  SER A 173           
SHEET   11   B13 PHE A 341  ASP A 346 -1  O  PHE A 345   N  PHE A 150           
SHEET   12   B13 ARG A 351  SER A 357 -1  O  GLY A 353   N  VAL A 344           
SHEET   13   B13 TYR A 184  PRO A 192 -1  N  TRP A 189   O  PHE A 354           
SHEET    1   C 5 GLN A 211  ASP A 212  0                                        
SHEET    2   C 5 ILE A 203  ILE A 208 -1  N  ILE A 208   O  GLN A 211           
SHEET    3   C 5 ILE A 283  MET A 288 -1  O  TYR A 286   N  ARG A 205           
SHEET    4   C 5 GLN A 294  ILE A 300 -1  O  ILE A 298   N  LEU A 285           
SHEET    5   C 5 ALA A 369  VAL A 375 -1  O  ALA A 369   N  THR A 299           
SHEET    1   D 4 SER A 225  VAL A 227  0                                        
SHEET    2   D 4 THR A 331  MET A 333  1  O  MET A 333   N  ILE A 226           
SHEET    3   D 4 LEU A 234  PRO A 237 -1  N  ARG A 235   O  VAL A 332           
SHEET    4   D 4 ILE A 324  SER A 327  1  O  SER A 325   N  LEU A 236           
SHEET    1   E 3 VAL A 268  TRP A 270  0                                        
SHEET    2   E 3 ASP A 318  PHE A 322 -1  O  ASP A 318   N  TRP A 270           
SHEET    3   E 3 LEU A 306  PRO A 308 -1  N  ARG A 307   O  LYS A 321           
SSBOND   1 CYS A  155    CYS A  359                          1555   1555  2.04  
SSBOND   2 CYS A  217    CYS A  382                          1555   1555  2.06  
SSBOND   3 CYS A  269    CYS A  319                          1555   1555  2.05  
CISPEP   1 SER A   22    PRO A   23          0        -8.15                     
CISPEP   2 ARG A  128    PRO A  129          0         0.83                     
CISPEP   3 TYR A  222    ASP A  223          0       -10.32                     
CISPEP   4 GLY A  372    PRO A  373          0        -2.79                     
SITE     1 AC1  1 SER A 105                                                     
SITE     1 AC2  2 LYS A 107  HOH A 476                                          
SITE     1 AC3  2 GLN A  55  HOH A 550                                          
SITE     1 AC4  5 THR A  82  ARG A  96  ASN A  98  GLN A 143                    
SITE     2 AC4  5 HOH A 420                                                     
SITE     1 AC5 10 LEU A  30  ASP A  32  GLY A  34  TYR A  71                    
SITE     2 AC5 10 GLN A  73  PHE A 108  TRP A 115  ILE A 226                    
SITE     3 AC5 10 ASP A 228  THR A 231                                          
CRYST1  102.412  102.412  169.237  90.00  90.00 120.00 P 61 2 2     12          
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      0.009764  0.005638  0.000000        0.00000                         
SCALE2      0.000000  0.011275  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005909        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system