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Database: PDB
Entry: 4DPI
LinkDB: 4DPI
Original site: 4DPI 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           13-FEB-12   4DPI              
TITLE     BACE-1 IN COMPLEX WITH HEA-MACROCYCLIC INHIBITOR, MV078512            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-SECRETASE 1;                                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 57-446;                                       
COMPND   5 SYNONYM: ASPARTYL PROTEASE 2, ASP2, ASP 2, BETA-SITE AMYLOID         
COMPND   6 PRECURSOR PROTEIN CLEAVING ENZYME 1, BETA-SITE APP CLEAVING ENZYME 1,
COMPND   7 MEMAPSIN-2, 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;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21                                     
KEYWDS    BACE1, ASP2, BACE, MACROCYCLE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LINDBERG,N.BORKAKOTI,D.DERBYSHIRE                                   
REVDAT   2   02-JAN-13 4DPI    1       JRNL                                     
REVDAT   1   11-JUL-12 4DPI    0                                                
JRNL        AUTH   V.SANDGREN,T.AGBACK,P.O.JOHANSSON,J.LINDBERG,I.KVARNSTROM,   
JRNL        AUTH 2 B.SAMUELSSON,O.BELDA,A.DAHLGREN                              
JRNL        TITL   HIGHLY POTENT MACROCYCLIC BACE-1 INHIBITORS INCORPORATING A  
JRNL        TITL 2 HYDROXYETHYLAMINE CORE: DESIGN, SYNTHESIS AND X-RAY CRYSTAL  
JRNL        TITL 3 STRUCTURES OF ENZYME INHIBITOR COMPLEXES.                    
JRNL        REF    BIOORG.MED.CHEM.              V.  20  4377 2012              
JRNL        REFN                   ISSN 0968-0896                               
JRNL        PMID   22698785                                                     
JRNL        DOI    10.1016/J.BMC.2012.05.039                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 31372                          
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) : 0.174                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1580                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2108                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 95.49                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2370                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 94                           
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2943                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 41                                      
REMARK   3   SOLVENT ATOMS            : 185                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
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): 0.151         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.142         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.745         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3279 ; 0.025 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4505 ; 1.969 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   424 ; 6.874 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   150 ;33.727 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   524 ;15.112 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    19 ;18.359 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   496 ; 0.168 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2560 ; 0.011 ; 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):  1942 ; 1.334 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3186 ; 2.263 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1337 ; 3.469 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1294 ; 5.439 ; 4.500       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   385                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2463   1.5409  14.9754              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0125 T22:   0.0244                                     
REMARK   3      T33:   0.0342 T12:   0.0021                                     
REMARK   3      T13:  -0.0069 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0662 L22:   0.3460                                     
REMARK   3      L33:   0.6589 L12:   0.1379                                     
REMARK   3      L13:  -0.0666 L23:  -0.0029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0073 S12:  -0.0106 S13:  -0.0108                       
REMARK   3      S21:  -0.0089 S22:   0.0063 S23:  -0.0049                       
REMARK   3      S31:   0.0045 S32:   0.0487 S33:  -0.0136                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 4DPI COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-FEB-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070621.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-JUN-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.976                              
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31429                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 61.843                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.00                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.24100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.24100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.18                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 18% PEG 1000, 0.1 NA-ACETATE PH4.5, 5%   
REMARK 280  GLYCEROL, VAPOR DIFFUSION, TEMPERATURE 291K                         
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       24.30000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.46000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       24.30000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.46000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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 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    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     ALA A   205                                                      
REMARK 465     GLY A   206                                                      
REMARK 465     PHE A   207                                                      
REMARK 465     PRO A   208                                                      
REMARK 465     LEU A   209                                                      
REMARK 465     ASN A   210                                                      
REMARK 465     GLN A   211                                                      
REMARK 465     SER A   212                                                      
REMARK 465     GLU A   213                                                      
REMARK 465     VAL A   214                                                      
REMARK 465     LEU A   215                                                      
REMARK 465     ALA A   216                                                      
REMARK 465     SER A   217                                                      
REMARK 465     VAL A   409                                                      
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  98   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    VAL A 404   CG1 -  CB  -  CG2 ANGL. DEV. =  10.5 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    PHE A 156      -65.40   -107.87                                   
REMARK 500    TRP A 245      -85.34   -145.17                                   
REMARK 500    ALA A 320      128.23    -37.23                                   
REMARK 500    ASN A 341       14.94     56.04                                   
REMARK 500    ALA A 371       34.74    -97.72                                   
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 0N1 A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4DPF   RELATED DB: PDB                                   
DBREF  4DPI A   44   433  UNP    P56817   BACE1_HUMAN     57    446             
SEQADV 4DPI MET A   43  UNP  P56817              INITIATING METHIONINE          
SEQRES   1 A  391  MET ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG          
SEQRES   2 A  391  GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL          
SEQRES   3 A  391  GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR          
SEQRES   4 A  391  GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO          
SEQRES   5 A  391  PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR          
SEQRES   6 A  391  TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR          
SEQRES   7 A  391  GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL          
SEQRES   8 A  391  SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN          
SEQRES   9 A  391  ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN          
SEQRES  10 A  391  GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA          
SEQRES  11 A  391  GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE          
SEQRES  12 A  391  ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE          
SEQRES  13 A  391  SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN          
SEQRES  14 A  391  SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE          
SEQRES  15 A  391  GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP          
SEQRES  16 A  391  TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE          
SEQRES  17 A  391  ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET          
SEQRES  18 A  391  ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP          
SEQRES  19 A  391  SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE          
SEQRES  20 A  391  GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER THR          
SEQRES  21 A  391  GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU          
SEQRES  22 A  391  VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE          
SEQRES  23 A  391  PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN          
SEQRES  24 A  391  GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU          
SEQRES  25 A  391  ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS          
SEQRES  26 A  391  TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR VAL          
SEQRES  27 A  391  MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE          
SEQRES  28 A  391  ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA          
SEQRES  29 A  391  CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU          
SEQRES  30 A  391  GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR          
SEQRES  31 A  391  ASN                                                          
HET    0N1  A 501      82                                                       
HETNAM     0N1 (4S,8E,11R)-4-[(1R)-1-HYDROXY-2-{[3-(PROPAN-2-YL)                
HETNAM   2 0N1  BENZYL]AMINO}ETHYL]-16-METHYL-11-PHENYL-6-OXA-3,12-             
HETNAM   3 0N1  DIAZABICYCLO[12.3.1]OCTADECA-1(18),8,14,16-TETRAENE-2,          
HETNAM   4 0N1  13-DIONE                                                        
FORMUL   2  0N1    C34 H41 N3 O4                                                
FORMUL   3  HOH   *185(H2 O)                                                    
HELIX    1   1 PHE A   47  VAL A   51  5                                   5    
HELIX    2   2 GLN A  101  SER A  105  5                                   5    
HELIX    3   3 TYR A  171  ALA A  175  5                                   5    
HELIX    4   4 PRO A  183  THR A  192  1                                  10    
HELIX    5   5 ASP A  228  SER A  230  5                                   3    
HELIX    6   6 ASP A  264  TYR A  270  5                                   7    
HELIX    7   7 LYS A  286  SER A  300  1                                  15    
HELIX    8   8 PRO A  306  LEU A  311  1                                   6    
HELIX    9   9 PRO A  324  PHE A  328  5                                   5    
HELIX   10  10 LEU A  349  TYR A  353  1                                   5    
HELIX   11  11 ASP A  359  SER A  363  5                                   5    
HELIX   12  12 GLY A  382  GLU A  387  1                                   6    
HELIX   13  13 ARG A  395  ARG A  397  5                                   3    
SHEET    1   A 9 ARG A 109  PRO A 118  0                                        
SHEET    2   A 9 LYS A 123  SER A 134 -1  O  LEU A 128   N  LYS A 113           
SHEET    3   A 9 GLY A  61  VAL A  68 -1  N  THR A  67   O  SER A 134           
SHEET    4   A 9 LEU A  54  LYS A  57 -1  N  ARG A  55   O  TYR A  63           
SHEET    5   A 9 GLY A 219  ILE A 224 -1  O  GLY A 220   N  LEU A  54           
SHEET    6   A 9 PHE A 198  CYS A 203 -1  N  GLN A 201   O  SER A 221           
SHEET    7   A 9 PHE A 389  ASP A 394 -1  O  PHE A 393   N  PHE A 198           
SHEET    8   A 9 ARG A 399  SER A 405 -1  O  GLY A 401   N  VAL A 392           
SHEET    9   A 9 TYR A 232  PRO A 240 -1  N  THR A 239   O  ILE A 400           
SHEET    1   B13 ARG A 109  PRO A 118  0                                        
SHEET    2   B13 LYS A 123  SER A 134 -1  O  LEU A 128   N  LYS A 113           
SHEET    3   B13 THR A 142  ASP A 154 -1  O  ALA A 149   N  GLU A 127           
SHEET    4   B13 PHE A  86  GLY A  89  1  N  VAL A  88   O  ILE A 150           
SHEET    5   B13 GLY A 165  GLY A 168 -1  O  ILE A 166   N  ALA A  87           
SHEET    6   B13 GLN A  73  ASP A  80  1  N  LEU A  78   O  LEU A 167           
SHEET    7   B13 GLY A  61  VAL A  68 -1  N  VAL A  64   O  ILE A  77           
SHEET    8   B13 LEU A  54  LYS A  57 -1  N  ARG A  55   O  TYR A  63           
SHEET    9   B13 GLY A 219  ILE A 224 -1  O  GLY A 220   N  LEU A  54           
SHEET   10   B13 PHE A 198  CYS A 203 -1  N  GLN A 201   O  SER A 221           
SHEET   11   B13 PHE A 389  ASP A 394 -1  O  PHE A 393   N  PHE A 198           
SHEET   12   B13 ARG A 399  SER A 405 -1  O  GLY A 401   N  VAL A 392           
SHEET   13   B13 TYR A 232  PRO A 240 -1  N  THR A 239   O  ILE A 400           
SHEET    1   C 5 GLU A 248  VAL A 249  0                                        
SHEET    2   C 5 SER A 273  VAL A 275 -1  O  SER A 273   N  VAL A 249           
SHEET    3   C 5 THR A 379  MET A 381  1  O  MET A 381   N  ILE A 274           
SHEET    4   C 5 LEU A 282  PRO A 285 -1  N  ARG A 283   O  VAL A 380           
SHEET    5   C 5 ILE A 372  SER A 375  1  O  SER A 373   N  LEU A 284           
SHEET    1   D 5 GLN A 259  ASP A 260  0                                        
SHEET    2   D 5 ILE A 251  ILE A 256 -1  N  ILE A 256   O  GLN A 259           
SHEET    3   D 5 ILE A 331  MET A 336 -1  O  TYR A 334   N  ARG A 253           
SHEET    4   D 5 GLN A 342  ILE A 348 -1  O  ILE A 348   N  ILE A 331           
SHEET    5   D 5 ALA A 417  VAL A 423 -1  O  GLU A 419   N  ARG A 345           
SHEET    1   E 3 VAL A 316  GLN A 319  0                                        
SHEET    2   E 3 ASP A 365  PHE A 370 -1  O  ASP A 366   N  TRP A 318           
SHEET    3   E 3 LEU A 354  PRO A 356 -1  N  ARG A 355   O  LYS A 369           
SSBOND   1 CYS A  203    CYS A  407                          1555   1555  2.18  
SSBOND   2 CYS A  265    CYS A  430                          1555   1555  2.10  
SSBOND   3 CYS A  317    CYS A  367                          1555   1555  2.10  
CISPEP   1 SER A   70    PRO A   71          0        -1.20                     
CISPEP   2 ARG A  176    PRO A  177          0         3.14                     
CISPEP   3 TYR A  270    ASP A  271          0         0.83                     
CISPEP   4 GLY A  420    PRO A  421          0        -0.16                     
SITE     1 AC1 23 GLY A  59  GLN A  60  GLY A  61  LEU A  78                    
SITE     2 AC1 23 ASP A  80  GLY A  82  SER A  83  VAL A 117                    
SITE     3 AC1 23 PRO A 118  TYR A 119  THR A 120  GLN A 121                    
SITE     4 AC1 23 ILE A 158  ARG A 176  TYR A 246  ASP A 276                    
SITE     5 AC1 23 SER A 277  GLY A 278  THR A 279  THR A 280                    
SITE     6 AC1 23 ARG A 283  ALA A 383  HOH A 624                               
CRYST1   48.600   76.920  104.000  90.00  90.00  90.00 P 21 21 21    4          
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      0.020576  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013001  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009615        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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