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Database: PDB
Entry: 5IE1
LinkDB: 5IE1
Original site: 5IE1 
HEADER    HYDROLASE                               24-FEB-16   5IE1              
TITLE     CRYSTAL STRUCTURE OF BACE1 IN COMPLEX WITH 3-(2-AMINO-6-(O-TOLYL)     
TITLE    2 QUINOLIN-3-YL)-N-(3,3-DIMETHYLBUTYL)PROPANAMIDE                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-SECRETASE 1;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 43-453;                                       
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: ENTEROBACTERIA PHAGE L1;                          
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 268588                                      
KEYWDS    ASPARTIC PROTEASE, ALZHEIMER'S DISEASE, APP, AMYLOID PRECURSOR        
KEYWDS   2 PROTEIN, HYDROLASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.JORDAN,D.A.WHITTINGTON,M.D.BARTBERGER,E.A.SICKMIER,K.CHEN,        
AUTHOR   2 Y.CHENG,T.JUDD                                                       
REVDAT   3   11-MAY-16 5IE1    1       JRNL                                     
REVDAT   2   20-APR-16 5IE1    1       JRNL                                     
REVDAT   1   30-MAR-16 5IE1    0                                                
JRNL        AUTH   J.B.JORDAN,D.A.WHITTINGTON,M.D.BARTBERGER,E.A.SICKMIER,      
JRNL        AUTH 2 K.CHEN,Y.CHENG,T.JUDD                                        
JRNL        TITL   FRAGMENT-LINKING APPROACH USING (19)F NMR SPECTROSCOPY TO    
JRNL        TITL 2 OBTAIN HIGHLY POTENT AND SELECTIVE INHIBITORS OF             
JRNL        TITL 3 BETA-SECRETASE.                                              
JRNL        REF    J.MED.CHEM.                   V.  59  3732 2016              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   26978477                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.5B01917                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 23543                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.214                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.120                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1205                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.5899 -  4.7731    1.00     2728   174  0.2060 0.2250        
REMARK   3     2  4.7731 -  3.7911    1.00     2587   143  0.1761 0.2223        
REMARK   3     3  3.7911 -  3.3126    1.00     2552   133  0.2033 0.2541        
REMARK   3     4  3.3126 -  3.0100    1.00     2546   114  0.2174 0.2488        
REMARK   3     5  3.0100 -  2.7945    1.00     2538   117  0.2351 0.2640        
REMARK   3     6  2.7945 -  2.6298    1.00     2513   115  0.2465 0.3036        
REMARK   3     7  2.6298 -  2.4982    1.00     2476   150  0.2478 0.3302        
REMARK   3     8  2.4982 -  2.3895    0.98     2421   131  0.2521 0.2855        
REMARK   3     9  2.3895 -  2.2975    0.80     1977   128  0.2571 0.3198        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.01                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004           2963                                  
REMARK   3   ANGLE     :  0.821           4020                                  
REMARK   3   CHIRALITY :  0.050            433                                  
REMARK   3   PLANARITY :  0.004            511                                  
REMARK   3   DIHEDRAL  : 15.808           1730                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5IE1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218598.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23699                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.298                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 11.20                              
REMARK 200  R MERGE                    (I) : 0.06200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.38                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26100                            
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: PHASER                                                
REMARK 200 STARTING MODEL: IN-HOUSE MODEL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% POLYETHYLENE GLYCOL 5000 MME, 200    
REMARK 280  MM AMMONIUM IODIDE, 170 MM SODIUM CITRATE (PH 6.6), VAPOR           
REMARK 280  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       56.44933            
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      112.89867            
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       84.67400            
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      141.12333            
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       28.22467            
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       56.44933            
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      112.89867            
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      141.12333            
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       84.67400            
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       28.22467            
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 675  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 706  LIES ON A SPECIAL POSITION.                          
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     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     LYS A    -5                                                      
REMARK 465     LYS A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     PHE A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     LEU A   161                                                      
REMARK 465     ASN A   162                                                      
REMARK 465     GLN A   163                                                      
REMARK 465     SER A   164                                                      
REMARK 465     GLU A   165                                                      
REMARK 465     VAL A   166                                                      
REMARK 465     LEU A   167                                                      
REMARK 465     ALA A   272                                                      
REMARK 465     GLY A   273                                                      
REMARK 465     THR A   274                                                      
REMARK 465     THR A   275                                                      
REMARK 465     PRO A   276                                                      
REMARK 465     TRP A   277                                                      
REMARK 465     ASN A   278                                                      
REMARK 465     GLU A   310                                                      
REMARK 465     ASP A   311                                                      
REMARK 465     VAL A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     THR A   314                                                      
REMARK 465     SER A   315                                                      
REMARK 465     GLN A   316                                                      
REMARK 465     ASP A   317                                                      
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 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    SER A   328     O    HOH A   501              2.17            
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    LEU A 267   CA  -  CB  -  CG  ANGL. DEV. =  19.2 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    THR A  72       93.28    -67.72                                   
REMARK 500    GLN A  73       -7.65     71.50                                   
REMARK 500    HIS A  89       42.25    -98.11                                   
REMARK 500    TRP A 197      -79.13   -137.33                                   
REMARK 500    ARG A 205      143.08   -170.62                                   
REMARK 500    ASP A 223      -70.59     75.58                                   
REMARK 500    SER A 252       51.46   -110.64                                   
REMARK 500    ALA A 323       35.12    -99.58                                   
REMARK 500    ASP A 363     -167.75    -79.42                                   
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 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IOD A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6BS A 407                 
DBREF  5IE1 A  -18   392  UNP    P56817   BACE1_HUMAN     43    453             
SEQADV 5IE1 LYS A   -5  UNP  P56817    ARG    56 CONFLICT                       
SEQADV 5IE1 LYS A   -4  UNP  P56817    ARG    57 CONFLICT                       
SEQRES   1 A  411  LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO GLY          
SEQRES   2 A  411  LYS LYS GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG          
SEQRES   3 A  411  GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL          
SEQRES   4 A  411  GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR          
SEQRES   5 A  411  GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO          
SEQRES   6 A  411  PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR          
SEQRES   7 A  411  TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR          
SEQRES   8 A  411  GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL          
SEQRES   9 A  411  SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN          
SEQRES  10 A  411  ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN          
SEQRES  11 A  411  GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA          
SEQRES  12 A  411  GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE          
SEQRES  13 A  411  ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE          
SEQRES  14 A  411  SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN          
SEQRES  15 A  411  SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE          
SEQRES  16 A  411  GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP          
SEQRES  17 A  411  TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE          
SEQRES  18 A  411  ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET          
SEQRES  19 A  411  ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP          
SEQRES  20 A  411  SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE          
SEQRES  21 A  411  GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER THR          
SEQRES  22 A  411  GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU          
SEQRES  23 A  411  VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE          
SEQRES  24 A  411  PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN          
SEQRES  25 A  411  GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU          
SEQRES  26 A  411  ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS          
SEQRES  27 A  411  TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR VAL          
SEQRES  28 A  411  MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE          
SEQRES  29 A  411  ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA          
SEQRES  30 A  411  CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU          
SEQRES  31 A  411  GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR          
SEQRES  32 A  411  ASN ILE PRO GLN THR ASP GLU SER                              
HET    IOD  A 401       1                                                       
HET    IOD  A 402       1                                                       
HET    IOD  A 403       1                                                       
HET    IOD  A 404       1                                                       
HET    GOL  A 405       6                                                       
HET    GOL  A 406       6                                                       
HET    6BS  A 407      29                                                       
HETNAM     IOD IODIDE ION                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     6BS 3-[2-AMINO-6-(2-METHYLPHENYL)QUINOLIN-3-YL]-N-(3,3-              
HETNAM   2 6BS  DIMETHYLBUTYL)PROPANAMIDE                                       
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  IOD    4(I 1-)                                                      
FORMUL   6  GOL    2(C3 H8 O3)                                                  
FORMUL   8  6BS    C25 H31 N3 O                                                 
FORMUL   9  HOH   *215(H2 O)                                                    
HELIX    1 AA1 PHE A   -1  VAL A    3  5                                   5    
HELIX    2 AA2 GLN A   53  SER A   57  5                                   5    
HELIX    3 AA3 TYR A  123  ALA A  127  5                                   5    
HELIX    4 AA4 PRO A  135  THR A  144  1                                  10    
HELIX    5 AA5 ASP A  180  SER A  182  5                                   3    
HELIX    6 AA6 ASP A  216  ASN A  221  1                                   6    
HELIX    7 AA7 LYS A  238  SER A  252  1                                  15    
HELIX    8 AA8 ASP A  259  GLY A  264  5                                   6    
HELIX    9 AA9 LEU A  301  LEU A  306  1                                   6    
HELIX   10 AB1 GLY A  334  GLU A  339  1                                   6    
HELIX   11 AB2 MET A  379  GLY A  383  5                                   5    
SHEET    1 AA1 9 ARG A  61  PRO A  70  0                                        
SHEET    2 AA1 9 LYS A  75  SER A  86 -1  O  LEU A  80   N  LYS A  65           
SHEET    3 AA1 9 TYR A  14  VAL A  20 -1  N  THR A  19   O  SER A  86           
SHEET    4 AA1 9 LEU A   6  LYS A   9 -1  N  ARG A   7   O  TYR A  15           
SHEET    5 AA1 9 SER A 169  ILE A 176 -1  O  VAL A 170   N  GLY A   8           
SHEET    6 AA1 9 PHE A 150  CYS A 155 -1  N  CYS A 155   O  GLY A 171           
SHEET    7 AA1 9 PHE A 341  ASP A 346 -1  O  PHE A 345   N  PHE A 150           
SHEET    8 AA1 9 ARG A 351  SER A 357 -1  O  ALA A 355   N  TYR A 342           
SHEET    9 AA1 9 TYR A 184  PRO A 192 -1  N  THR A 191   O  ILE A 352           
SHEET    1 AA213 ARG A  61  PRO A  70  0                                        
SHEET    2 AA213 LYS A  75  SER A  86 -1  O  LEU A  80   N  LYS A  65           
SHEET    3 AA213 VAL A  95  ASP A 106 -1  O  ILE A  99   N  GLY A  81           
SHEET    4 AA213 PHE A  38  GLY A  41  1  N  VAL A  40   O  ILE A 102           
SHEET    5 AA213 GLY A 117  GLY A 120 -1  O  ILE A 118   N  ALA A  39           
SHEET    6 AA213 GLN A  25  ASP A  32  1  N  LEU A  30   O  LEU A 119           
SHEET    7 AA213 TYR A  14  VAL A  20 -1  N  TYR A  14   O  VAL A  31           
SHEET    8 AA213 LEU A   6  LYS A   9 -1  N  ARG A   7   O  TYR A  15           
SHEET    9 AA213 SER A 169  ILE A 176 -1  O  VAL A 170   N  GLY A   8           
SHEET   10 AA213 PHE A 150  CYS A 155 -1  N  CYS A 155   O  GLY A 171           
SHEET   11 AA213 PHE A 341  ASP A 346 -1  O  PHE A 345   N  PHE A 150           
SHEET   12 AA213 ARG A 351  SER A 357 -1  O  ALA A 355   N  TYR A 342           
SHEET   13 AA213 TYR A 184  PRO A 192 -1  N  THR A 191   O  ILE A 352           
SHEET    1 AA3 5 GLN A 211  ASP A 212  0                                        
SHEET    2 AA3 5 ILE A 203  ILE A 208 -1  N  ILE A 208   O  GLN A 211           
SHEET    3 AA3 5 ILE A 283  MET A 288 -1  O  TYR A 286   N  ARG A 205           
SHEET    4 AA3 5 GLN A 294  ILE A 300 -1  O  ILE A 298   N  LEU A 285           
SHEET    5 AA3 5 ALA A 369  VAL A 375 -1  O  GLU A 371   N  ARG A 297           
SHEET    1 AA4 4 SER A 225  VAL A 227  0                                        
SHEET    2 AA4 4 THR A 331  MET A 333  1  O  MET A 333   N  ILE A 226           
SHEET    3 AA4 4 LEU A 234  PRO A 237 -1  N  ARG A 235   O  VAL A 332           
SHEET    4 AA4 4 ILE A 324  SER A 327  1  O  SER A 325   N  LEU A 236           
SSBOND   1 CYS A  155    CYS A  359                          1555   1555  2.04  
SSBOND   2 CYS A  217    CYS A  382                          1555   1555  2.03  
SSBOND   3 CYS A  269    CYS A  319                          1555   1555  2.03  
CISPEP   1 SER A   22    PRO A   23          0        -1.63                     
CISPEP   2 ARG A  128    PRO A  129          0         3.08                     
CISPEP   3 GLY A  372    PRO A  373          0        -3.03                     
SITE     1 AC1  1 SER A 105                                                     
SITE     1 AC2  1 LYS A 107                                                     
SITE     1 AC3  1 ARG A  96                                                     
SITE     1 AC4  1 ARG A 349                                                     
SITE     1 AC5  8 LYS A   9  GLY A  11  GLY A  13  VAL A 170                    
SITE     2 AC5  8 SER A 229  THR A 231  THR A 232  ALA A 335                    
SITE     1 AC6  7 ARG A  50  TYR A  51  GLN A  53  SER A 187                    
SITE     2 AC6  7 HOH A 518  HOH A 544  HOH A 596                               
SITE     1 AC7 11 ASP A  32  GLY A  34  SER A  35  TYR A  71                    
SITE     2 AC7 11 LYS A  75  TRP A  76  PHE A 108  ILE A 118                    
SITE     3 AC7 11 ARG A 128  TYR A 198  ASP A 228                               
CRYST1  102.494  102.494  169.348  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      0.009757  0.005633  0.000000        0.00000                         
SCALE2      0.000000  0.011266  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005905        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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