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Database: PDB
Entry: 3KYR
LinkDB: 3KYR
Original site: 3KYR 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           07-DEC-09   3KYR              
TITLE     BACE-1 IN COMPLEX WITH A NORSTATINE TYPE INHIBITOR                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-SECRETASE 1;                                          
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: UNP RESIDUES 42-446;                                       
COMPND   5 SYNONYM: BETA-SITE AMYLOID PRECURSOR PROTEIN CLEAVING ENZYME 1, BETA-
COMPND   6 SITE APP 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                                                      
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_PLASMID: PET11A                                    
KEYWDS    BACE, BETA-SECRETASE, MEMAPSIN-2, ASPARTYL PROTEASE, INHIBITOR,       
KEYWDS   2 NORSTATINE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.D.LINDBERG,N.BORKAKOTI,D.DERBYSHIRE,S.NYSTROM                       
REVDAT   2   06-SEP-23 3KYR    1       REMARK                                   
REVDAT   1   29-DEC-10 3KYR    0                                                
JRNL        AUTH   F.WANGSELL,P.NORDEMAN,J.SAVMARKER,R.EMANUELSSON,K.JANSSON,   
JRNL        AUTH 2 J.LINDBERG,A.ROSENQVIST,B.SAMUELSSON,M.LARHED                
JRNL        TITL   INVESTIGATION OF A-PHENYLNORSTATINE AND A-BENZYLNORSTATINE   
JRNL        TITL 2 AS TRANSITION STATE ISOSTERE MOTIFS IN THE SEARCH FOR NEW    
JRNL        TITL 3 BACE-1 INHIBIOTRS                                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 99.01                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 45951                          
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) : 0.210                           
REMARK   3   R VALUE            (WORKING SET) : 0.207                           
REMARK   3   FREE R VALUE                     : 0.269                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2320                            
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3227                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 180                          
REMARK   3   BIN FREE R VALUE                    : 0.4030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8570                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 156                                     
REMARK   3   SOLVENT ATOMS            : 76                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.66                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 24.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.11000                                              
REMARK   3    B33 (A**2) : -0.14000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.03000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.561         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.320         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.209         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.650         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.860                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8952 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12163 ; 1.659 ; 1.964       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1076 ; 7.294 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   401 ;34.073 ;23.666       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1404 ;18.383 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    51 ;19.848 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1322 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6859 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3625 ; 0.225 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  5981 ; 0.322 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   320 ; 0.154 ; 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):    71 ; 0.264 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     7 ; 0.150 ; 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):  5519 ; 0.957 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8704 ; 1.621 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4033 ; 2.059 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3459 ; 3.298 ; 4.500       
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 : 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 3KYR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-MAY-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000056615.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JUN-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.07225                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 1                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.2.25                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 46304                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 99.015                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.9                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : 0.11400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38600                            
REMARK 200  R SYM FOR SHELL            (I) : 0.38600                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 1.3.3                                          
REMARK 200 STARTING MODEL: PDB ENTRY 3DM6                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.06                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 16% PEG8000, 0.1M CITRATE, 0.3M          
REMARK 280  LITHIUM SULPHATE, 0.1M SODIUM CHLORIDE, PH 5.0, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 299K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       51.38700            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    29P                                                     
REMARK 465     LEU A    30P                                                     
REMARK 465     PRO A    31P                                                     
REMARK 465     ARG A    32P                                                     
REMARK 465     GLU A    33P                                                     
REMARK 465     THR A    34P                                                     
REMARK 465     ASP A    35P                                                     
REMARK 465     GLU A    36P                                                     
REMARK 465     GLU A    37P                                                     
REMARK 465     PRO A    38P                                                     
REMARK 465     GLU A    39P                                                     
REMARK 465     GLU A    40P                                                     
REMARK 465     PRO A    41P                                                     
REMARK 465     GLY A    42P                                                     
REMARK 465     ARG A    43P                                                     
REMARK 465     ARG A    44P                                                     
REMARK 465     GLY A    45P                                                     
REMARK 465     GLY A   158                                                      
REMARK 465     PHE A   159                                                      
REMARK 465     PRO A   160                                                      
REMARK 465     LEU A   161                                                      
REMARK 465     ASN A   162                                                      
REMARK 465     GLN A   163                                                      
REMARK 465     SER A   164                                                      
REMARK 465     GLU A   165                                                      
REMARK 465     VAL A   166                                                      
REMARK 465     LEU A   167                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     LYS A   256                                                      
REMARK 465     PHE A   257                                                      
REMARK 465     PRO A   258                                                      
REMARK 465     ASP A   259                                                      
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     ASN A   385                                                      
REMARK 465     ARG B    29P                                                     
REMARK 465     LEU B    30P                                                     
REMARK 465     PRO B    31P                                                     
REMARK 465     ARG B    32P                                                     
REMARK 465     GLU B    33P                                                     
REMARK 465     THR B    34P                                                     
REMARK 465     ASP B    35P                                                     
REMARK 465     GLU B    36P                                                     
REMARK 465     GLU B    37P                                                     
REMARK 465     PRO B    38P                                                     
REMARK 465     GLU B    39P                                                     
REMARK 465     GLU B    40P                                                     
REMARK 465     PRO B    41P                                                     
REMARK 465     GLY B    42P                                                     
REMARK 465     ARG B    43P                                                     
REMARK 465     ARG B    44P                                                     
REMARK 465     GLY B    45P                                                     
REMARK 465     GLY B   158                                                      
REMARK 465     PHE B   159                                                      
REMARK 465     PRO B   160                                                      
REMARK 465     LEU B   161                                                      
REMARK 465     ASN B   162                                                      
REMARK 465     GLN B   163                                                      
REMARK 465     SER B   164                                                      
REMARK 465     GLU B   165                                                      
REMARK 465     VAL B   166                                                      
REMARK 465     LEU B   167                                                      
REMARK 465     ALA B   168                                                      
REMARK 465     LYS B   256                                                      
REMARK 465     PHE B   257                                                      
REMARK 465     PRO B   258                                                      
REMARK 465     VAL B   309                                                      
REMARK 465     GLU B   310                                                      
REMARK 465     ASP B   311                                                      
REMARK 465     VAL B   312                                                      
REMARK 465     ALA B   313                                                      
REMARK 465     THR B   314                                                      
REMARK 465     SER B   315                                                      
REMARK 465     GLN B   316                                                      
REMARK 465     GLY B   383                                                      
REMARK 465     TYR B   384                                                      
REMARK 465     ASN B   385                                                      
REMARK 465     ARG C    29P                                                     
REMARK 465     LEU C    30P                                                     
REMARK 465     PRO C    31P                                                     
REMARK 465     ARG C    32P                                                     
REMARK 465     GLU C    33P                                                     
REMARK 465     THR C    34P                                                     
REMARK 465     ASP C    35P                                                     
REMARK 465     GLU C    36P                                                     
REMARK 465     GLU C    37P                                                     
REMARK 465     PRO C    38P                                                     
REMARK 465     GLU C    39P                                                     
REMARK 465     GLU C    40P                                                     
REMARK 465     PRO C    41P                                                     
REMARK 465     GLY C    42P                                                     
REMARK 465     ARG C    43P                                                     
REMARK 465     ARG C    44P                                                     
REMARK 465     GLY C    45P                                                     
REMARK 465     GLY C   158                                                      
REMARK 465     PHE C   159                                                      
REMARK 465     PRO C   160                                                      
REMARK 465     LEU C   161                                                      
REMARK 465     ASN C   162                                                      
REMARK 465     GLN C   163                                                      
REMARK 465     SER C   164                                                      
REMARK 465     GLU C   165                                                      
REMARK 465     VAL C   166                                                      
REMARK 465     LEU C   167                                                      
REMARK 465     ALA C   168                                                      
REMARK 465     SER C   252                                                      
REMARK 465     SER C   253                                                      
REMARK 465     THR C   254                                                      
REMARK 465     GLU C   255                                                      
REMARK 465     LYS C   256                                                      
REMARK 465     PHE C   257                                                      
REMARK 465     PRO C   258                                                      
REMARK 465     ASP C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     GLU C   310                                                      
REMARK 465     ASP C   311                                                      
REMARK 465     VAL C   312                                                      
REMARK 465     ALA C   313                                                      
REMARK 465     THR C   314                                                      
REMARK 465     SER C   315                                                      
REMARK 465     GLN C   316                                                      
REMARK 465     ASP C   317                                                      
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 B 149   CA  -  CB  -  CG  ANGL. DEV. =  16.6 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    SER A  36       12.31   -150.95                                   
REMARK 500    HIS A  89       46.92   -106.12                                   
REMARK 500    ASN A 114       -0.95     82.13                                   
REMARK 500    ALA A 122     -151.10    -85.32                                   
REMARK 500    TRP A 197      -84.45   -136.70                                   
REMARK 500    LYS A 214       -6.39     74.67                                   
REMARK 500    TYR A 222       94.19    -43.40                                   
REMARK 500    ASP A 223      -74.88    106.36                                   
REMARK 500    LYS A 238      -60.49    -23.25                                   
REMARK 500    THR A 254       -6.28    -55.09                                   
REMARK 500    ALA A 272      125.87    -27.16                                   
REMARK 500    THR A 329     -146.99   -121.14                                   
REMARK 500    CYS A 359       44.24    -85.66                                   
REMARK 500    SER B  36       12.19   -141.18                                   
REMARK 500    ALA B  43      148.34   -175.34                                   
REMARK 500    HIS B  89       48.78    -93.66                                   
REMARK 500    PHE B 108      -62.83    -91.71                                   
REMARK 500    ASP B 131       -7.81    -53.42                                   
REMARK 500    LEU B 149      136.18   -172.38                                   
REMARK 500    TRP B 197      -89.41   -142.15                                   
REMARK 500    ARG B 205      143.30   -175.62                                   
REMARK 500    ASN B 209       50.96     37.84                                   
REMARK 500    TYR B 222      -99.11      1.58                                   
REMARK 500    LYS B 224      143.06    177.19                                   
REMARK 500    SER B 253        9.57    -69.23                                   
REMARK 500    ALA B 272      119.39    -30.39                                   
REMARK 500    ALA B 323       42.53   -102.22                                   
REMARK 500    THR B 329     -145.83   -103.23                                   
REMARK 500    CYS B 359       51.12   -113.69                                   
REMARK 500    SER C  36       12.21   -146.92                                   
REMARK 500    HIS C  89       53.21   -114.84                                   
REMARK 500    PHE C 108      -65.11   -101.08                                   
REMARK 500    ALA C 122     -169.32    -77.09                                   
REMARK 500    GLU C 125      -36.81    -39.62                                   
REMARK 500    LEU C 133       96.30    -68.93                                   
REMARK 500    TRP C 197      -92.51   -142.67                                   
REMARK 500    ASP C 223      -67.41     87.31                                   
REMARK 500    LYS C 224      142.16   -177.50                                   
REMARK 500    ALA C 272      132.48    -32.49                                   
REMARK 500    PRO C 276       33.66    -71.69                                   
REMARK 500    TRP C 277      -40.50    -28.97                                   
REMARK 500    ALA C 323       42.91   -102.01                                   
REMARK 500    THR C 329     -161.58   -122.32                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE ENZYME INHIBITOR                         
REMARK 630 MOLECULE NAME: 3-[[(2S)-2-[[[(2S)-2-[[(2S)-2-[[(2S)-2-AZANYL-3-(1H-  
REMARK 630 1,2,3,4-TETRAZOL-5-YLCARBONYLAMINO)PROPANOYL]AMINO]-3-METHYL-        
REMARK 630 BUTANOYL]AMINO]-4-METHYL-PENTANOYL]AMINO]METHYL]-2-HYDROXY-4-        
REMARK 630 PHENYL-BUTANOYL]AMINO]BENZOIC ACID                                   
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     038 A   500                                                      
REMARK 630     038 B   500                                                      
REMARK 630     038 C   500                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    35Y VAL LEU 22P GAB                                      
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 038 A 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 038 B 500                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 038 C 500                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3DM6   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3IXK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3IXJ   RELATED DB: PDB                                   
DBREF  3KYR A   29P  385  UNP    P56817   BACE1_HUMAN     42    446             
DBREF  3KYR B   29P  385  UNP    P56817   BACE1_HUMAN     42    446             
DBREF  3KYR C   29P  385  UNP    P56817   BACE1_HUMAN     42    446             
SEQRES   1 A  405  ARG LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO          
SEQRES   2 A  405  GLY ARG ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU          
SEQRES   3 A  405  ARG GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR          
SEQRES   4 A  405  VAL GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP          
SEQRES   5 A  405  THR GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS          
SEQRES   6 A  405  PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER          
SEQRES   7 A  405  THR TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR          
SEQRES   8 A  405  THR GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU          
SEQRES   9 A  405  VAL SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA          
SEQRES  10 A  405  ASN ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE          
SEQRES  11 A  405  ASN GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR          
SEQRES  12 A  405  ALA GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE          
SEQRES  13 A  405  PHE ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU          
SEQRES  14 A  405  PHE SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN          
SEQRES  15 A  405  GLN SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE          
SEQRES  16 A  405  ILE GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU          
SEQRES  17 A  405  TRP TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL          
SEQRES  18 A  405  ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS          
SEQRES  19 A  405  MET ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL          
SEQRES  20 A  405  ASP SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL          
SEQRES  21 A  405  PHE GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER          
SEQRES  22 A  405  THR GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN          
SEQRES  23 A  405  LEU VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE          
SEQRES  24 A  405  PHE PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR          
SEQRES  25 A  405  ASN GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR          
SEQRES  26 A  405  LEU ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP          
SEQRES  27 A  405  CYS TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR          
SEQRES  28 A  405  VAL MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL          
SEQRES  29 A  405  PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER          
SEQRES  30 A  405  ALA CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL          
SEQRES  31 A  405  GLU GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY          
SEQRES  32 A  405  TYR ASN                                                      
SEQRES   1 B  405  ARG LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO          
SEQRES   2 B  405  GLY ARG ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU          
SEQRES   3 B  405  ARG GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR          
SEQRES   4 B  405  VAL GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP          
SEQRES   5 B  405  THR GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS          
SEQRES   6 B  405  PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER          
SEQRES   7 B  405  THR TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR          
SEQRES   8 B  405  THR GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU          
SEQRES   9 B  405  VAL SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA          
SEQRES  10 B  405  ASN ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE          
SEQRES  11 B  405  ASN GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR          
SEQRES  12 B  405  ALA GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE          
SEQRES  13 B  405  PHE ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU          
SEQRES  14 B  405  PHE SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN          
SEQRES  15 B  405  GLN SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE          
SEQRES  16 B  405  ILE GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU          
SEQRES  17 B  405  TRP TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL          
SEQRES  18 B  405  ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS          
SEQRES  19 B  405  MET ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL          
SEQRES  20 B  405  ASP SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL          
SEQRES  21 B  405  PHE GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER          
SEQRES  22 B  405  THR GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN          
SEQRES  23 B  405  LEU VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE          
SEQRES  24 B  405  PHE PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR          
SEQRES  25 B  405  ASN GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR          
SEQRES  26 B  405  LEU ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP          
SEQRES  27 B  405  CYS TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR          
SEQRES  28 B  405  VAL MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL          
SEQRES  29 B  405  PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER          
SEQRES  30 B  405  ALA CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL          
SEQRES  31 B  405  GLU GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY          
SEQRES  32 B  405  TYR ASN                                                      
SEQRES   1 C  405  ARG LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO          
SEQRES   2 C  405  GLY ARG ARG GLY SER PHE VAL GLU MET VAL ASP ASN LEU          
SEQRES   3 C  405  ARG GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR          
SEQRES   4 C  405  VAL GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP          
SEQRES   5 C  405  THR GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS          
SEQRES   6 C  405  PRO PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER          
SEQRES   7 C  405  THR TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR          
SEQRES   8 C  405  THR GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU          
SEQRES   9 C  405  VAL SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA          
SEQRES  10 C  405  ASN ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE          
SEQRES  11 C  405  ASN GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR          
SEQRES  12 C  405  ALA GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE          
SEQRES  13 C  405  PHE ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU          
SEQRES  14 C  405  PHE SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN          
SEQRES  15 C  405  GLN SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE          
SEQRES  16 C  405  ILE GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU          
SEQRES  17 C  405  TRP TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL          
SEQRES  18 C  405  ILE ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS          
SEQRES  19 C  405  MET ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL          
SEQRES  20 C  405  ASP SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL          
SEQRES  21 C  405  PHE GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER          
SEQRES  22 C  405  THR GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN          
SEQRES  23 C  405  LEU VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE          
SEQRES  24 C  405  PHE PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR          
SEQRES  25 C  405  ASN GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR          
SEQRES  26 C  405  LEU ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP          
SEQRES  27 C  405  CYS TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR          
SEQRES  28 C  405  VAL MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL          
SEQRES  29 C  405  PHE ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER          
SEQRES  30 C  405  ALA CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL          
SEQRES  31 C  405  GLU GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY          
SEQRES  32 C  405  TYR ASN                                                      
HET    038  A 500      52                                                       
HET    038  B 500      52                                                       
HET    038  C 500      52                                                       
HETNAM     038 3-[[(2S)-2-[[[(2S)-2-[[(2S)-2-[[(2S)-2-AZANYL-3-(1H-1,           
HETNAM   2 038  2,3,4-TETRAZOL-5-YLCARBONYLAMINO)PROPANOYL]AMINO]-3-            
HETNAM   3 038  METHYL-BUTANOYL]AMINO]-4-METHYL-                                
HETNAM   4 038  PENTANOYL]AMINO]METHYL]-2-HYDROXY-4-PHENYL-                     
HETNAM   5 038  BUTANOYL]AMINO]BENZOIC ACID                                     
FORMUL   4  038    3(C34 H46 N10 O8)                                            
FORMUL   7  HOH   *76(H2 O)                                                     
HELIX    1   1 SER A   46P VAL A    3  5                                   6    
HELIX    2   2 GLN A   53  SER A   57  5                                   5    
HELIX    3   3 TYR A  123  ALA A  127  5                                   5    
HELIX    4   4 PRO A  135  THR A  144  1                                  10    
HELIX    5   5 ASP A  180  TYR A  184  5                                   5    
HELIX    6   6 ASP A  216  TYR A  220  5                                   5    
HELIX    7   7 LYS A  238  SER A  253  1                                  16    
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 ASP A  378  GLY A  383  5                                   6    
HELIX   13  13 SER B   46P VAL B    3  5                                   6    
HELIX   14  14 GLN B   53  SER B   57  5                                   5    
HELIX   15  15 TYR B  123  ALA B  127  5                                   5    
HELIX   16  16 PRO B  135  THR B  144  1                                  10    
HELIX   17  17 ASP B  180  SER B  182  5                                   3    
HELIX   18  18 CYS B  217  TYR B  222  1                                   6    
HELIX   19  19 LYS B  238  SER B  253  1                                  16    
HELIX   20  20 PRO B  276  PHE B  280  5                                   5    
HELIX   21  21 LEU B  301  TYR B  305  1                                   5    
HELIX   22  22 GLY B  334  GLY B  340  1                                   7    
HELIX   23  23 ARG B  347  ARG B  349  5                                   3    
HELIX   24  24 PHE C   47P VAL C    3  5                                   5    
HELIX   25  25 GLN C   53  SER C   57  5                                   5    
HELIX   26  26 TYR C  123  ALA C  127  5                                   5    
HELIX   27  27 PRO C  135  THR C  144  1                                  10    
HELIX   28  28 ASP C  180  SER C  182  5                                   3    
HELIX   29  29 ASP C  216  TYR C  222  5                                   7    
HELIX   30  30 LYS C  238  ALA C  250  1                                  13    
HELIX   31  31 PRO C  276  PHE C  280  5                                   5    
HELIX   32  32 LEU C  301  TYR C  305  1                                   5    
HELIX   33  33 GLY C  334  GLU C  339  1                                   6    
HELIX   34  34 MET C  379  GLY C  383  5                                   5    
SHEET    1   A 9 ARG A  61  PRO A  70  0                                        
SHEET    2   A 9 LYS A  75  SER A  86 -1  O  LEU A  80   N  LYS A  65           
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  GLY A   8 -1  N  ARG A   7   O  TYR A  15           
SHEET    5   A 9 VAL A 170  ILE A 176 -1  O  GLY A 172   N  LEU A   6           
SHEET    6   A 9 PHE A 150  CYS A 155 -1  N  CYS A 155   O  GLY A 171           
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  VAL A 356 -1  O  ALA A 355   N  TYR A 342           
SHEET    9   A 9 TRP A 189  PRO A 192 -1  N  TRP A 189   O  PHE A 354           
SHEET    1   B13 ARG A  61  PRO A  70  0                                        
SHEET    2   B13 LYS A  75  SER A  86 -1  O  LEU A  80   N  LYS A  65           
SHEET    3   B13 THR A  94  ASP A 106 -1  O  ILE A  99   N  GLY A  81           
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  GLY A   8 -1  N  ARG A   7   O  TYR A  15           
SHEET    9   B13 VAL A 170  ILE A 176 -1  O  GLY A 172   N  LEU A   6           
SHEET   10   B13 PHE A 150  CYS A 155 -1  N  CYS A 155   O  GLY A 171           
SHEET   11   B13 PHE A 341  ASP A 346 -1  O  PHE A 345   N  PHE A 150           
SHEET   12   B13 ARG A 351  VAL A 356 -1  O  ALA A 355   N  TYR A 342           
SHEET   13   B13 TRP A 189  PRO A 192 -1  N  TRP A 189   O  PHE A 354           
SHEET    1   C 5 GLU A 200  VAL A 201  0                                        
SHEET    2   C 5 SER A 225  VAL A 227 -1  O  SER A 225   N  VAL A 201           
SHEET    3   C 5 VAL A 332  MET A 333  1  O  MET A 333   N  ILE A 226           
SHEET    4   C 5 LEU A 234  PRO A 237 -1  N  ARG A 235   O  VAL A 332           
SHEET    5   C 5 ILE A 324  SER A 327  1  O  SER A 327   N  LEU A 236           
SHEET    1   D 5 GLN A 211  ASP A 212  0                                        
SHEET    2   D 5 ILE A 203  ILE A 208 -1  N  ILE A 208   O  GLN A 211           
SHEET    3   D 5 ILE A 283  MET A 288 -1  O  SER A 284   N  GLU A 207           
SHEET    4   D 5 GLN A 294  ILE A 300 -1  O  ILE A 300   N  ILE A 283           
SHEET    5   D 5 ALA A 369  VAL A 375 -1  O  PHE A 374   N  SER A 295           
SHEET    1   E 3 VAL A 268  TRP A 270  0                                        
SHEET    2   E 3 ASP A 318  PHE A 322 -1  O  TYR A 320   N  VAL A 268           
SHEET    3   E 3 LEU A 306  VAL A 309 -1  N  VAL A 309   O  CYS A 319           
SHEET    1   F 9 ARG B  61  PRO B  70  0                                        
SHEET    2   F 9 LYS B  75  SER B  86 -1  O  TRP B  76   N  VAL B  69           
SHEET    3   F 9 TYR B  14  VAL B  20 -1  N  THR B  19   O  SER B  86           
SHEET    4   F 9 LEU B   6  GLY B   8 -1  N  ARG B   7   O  TYR B  15           
SHEET    5   F 9 VAL B 170  ILE B 176 -1  O  VAL B 170   N  GLY B   8           
SHEET    6   F 9 PHE B 150  LEU B 154 -1  N  GLN B 153   O  SER B 173           
SHEET    7   F 9 PHE B 341  ASP B 346 -1  O  VAL B 343   N  LEU B 152           
SHEET    8   F 9 ARG B 351  SER B 357 -1  O  ALA B 355   N  TYR B 342           
SHEET    9   F 9 TYR B 184  PRO B 192 -1  N  TRP B 189   O  PHE B 354           
SHEET    1   G13 ARG B  61  PRO B  70  0                                        
SHEET    2   G13 LYS B  75  SER B  86 -1  O  TRP B  76   N  VAL B  69           
SHEET    3   G13 VAL B  95  ASP B 106 -1  O  ILE B  99   N  GLY B  81           
SHEET    4   G13 PHE B  38  GLY B  41  1  N  VAL B  40   O  ILE B 102           
SHEET    5   G13 GLY B 117  GLY B 120 -1  O  ILE B 118   N  ALA B  39           
SHEET    6   G13 GLN B  25  ASP B  32  1  N  LEU B  30   O  GLY B 117           
SHEET    7   G13 TYR B  14  VAL B  20 -1  N  VAL B  16   O  ILE B  29           
SHEET    8   G13 LEU B   6  GLY B   8 -1  N  ARG B   7   O  TYR B  15           
SHEET    9   G13 VAL B 170  ILE B 176 -1  O  VAL B 170   N  GLY B   8           
SHEET   10   G13 PHE B 150  LEU B 154 -1  N  GLN B 153   O  SER B 173           
SHEET   11   G13 PHE B 341  ASP B 346 -1  O  VAL B 343   N  LEU B 152           
SHEET   12   G13 ARG B 351  SER B 357 -1  O  ALA B 355   N  TYR B 342           
SHEET   13   G13 TYR B 184  PRO B 192 -1  N  TRP B 189   O  PHE B 354           
SHEET    1   H 5 GLU B 200  VAL B 201  0                                        
SHEET    2   H 5 SER B 225  VAL B 227 -1  O  SER B 225   N  VAL B 201           
SHEET    3   H 5 VAL B 332  MET B 333  1  O  MET B 333   N  ILE B 226           
SHEET    4   H 5 LEU B 234  PRO B 237 -1  N  ARG B 235   O  VAL B 332           
SHEET    5   H 5 ILE B 324  SER B 327  1  O  SER B 327   N  LEU B 236           
SHEET    1   I 5 GLN B 211  ASP B 212  0                                        
SHEET    2   I 5 ILE B 203  ILE B 208 -1  N  ILE B 208   O  GLN B 211           
SHEET    3   I 5 ILE B 283  LEU B 287 -1  O  SER B 284   N  GLU B 207           
SHEET    4   I 5 SER B 295  ILE B 300 -1  O  ILE B 300   N  ILE B 283           
SHEET    5   I 5 ALA B 369  PHE B 374 -1  O  PHE B 374   N  SER B 295           
SHEET    1   J 3 VAL B 268  TRP B 270  0                                        
SHEET    2   J 3 ASP B 318  PHE B 322 -1  O  ASP B 318   N  TRP B 270           
SHEET    3   J 3 LEU B 306  ARG B 307 -1  N  ARG B 307   O  LYS B 321           
SHEET    1   K 9 ARG C  61  TYR C  71  0                                        
SHEET    2   K 9 GLY C  74  SER C  86 -1  O  GLY C  74   N  TYR C  71           
SHEET    3   K 9 TYR C  14  VAL C  20 -1  N  THR C  19   O  SER C  86           
SHEET    4   K 9 LEU C   6  GLY C   8 -1  N  ARG C   7   O  TYR C  15           
SHEET    5   K 9 VAL C 170  ILE C 176 -1  O  GLY C 172   N  LEU C   6           
SHEET    6   K 9 PHE C 150  CYS C 155 -1  N  GLN C 153   O  SER C 173           
SHEET    7   K 9 PHE C 341  ASP C 346 -1  O  VAL C 343   N  LEU C 152           
SHEET    8   K 9 ARG C 351  SER C 357 -1  O  GLY C 353   N  VAL C 344           
SHEET    9   K 9 TYR C 184  PRO C 192 -1  N  THR C 191   O  ILE C 352           
SHEET    1   L13 ARG C  61  TYR C  71  0                                        
SHEET    2   L13 GLY C  74  SER C  86 -1  O  GLY C  74   N  TYR C  71           
SHEET    3   L13 VAL C  95  ASP C 106 -1  O  ILE C  99   N  GLY C  81           
SHEET    4   L13 PHE C  38  GLY C  41  1  N  VAL C  40   O  ILE C 102           
SHEET    5   L13 GLY C 117  GLY C 120 -1  O  ILE C 118   N  ALA C  39           
SHEET    6   L13 GLN C  25  ASP C  32  1  N  LEU C  30   O  LEU C 119           
SHEET    7   L13 TYR C  14  VAL C  20 -1  N  VAL C  20   O  GLN C  25           
SHEET    8   L13 LEU C   6  GLY C   8 -1  N  ARG C   7   O  TYR C  15           
SHEET    9   L13 VAL C 170  ILE C 176 -1  O  GLY C 172   N  LEU C   6           
SHEET   10   L13 PHE C 150  CYS C 155 -1  N  GLN C 153   O  SER C 173           
SHEET   11   L13 PHE C 341  ASP C 346 -1  O  VAL C 343   N  LEU C 152           
SHEET   12   L13 ARG C 351  SER C 357 -1  O  GLY C 353   N  VAL C 344           
SHEET   13   L13 TYR C 184  PRO C 192 -1  N  THR C 191   O  ILE C 352           
SHEET    1   M 5 GLU C 200  VAL C 201  0                                        
SHEET    2   M 5 SER C 225  VAL C 227 -1  O  SER C 225   N  VAL C 201           
SHEET    3   M 5 VAL C 332  MET C 333  1  O  MET C 333   N  ILE C 226           
SHEET    4   M 5 LEU C 234  PRO C 237 -1  N  ARG C 235   O  VAL C 332           
SHEET    5   M 5 ILE C 324  SER C 327  1  O  SER C 325   N  LEU C 236           
SHEET    1   N 5 GLN C 211  ASP C 212  0                                        
SHEET    2   N 5 ILE C 203  ILE C 208 -1  N  ILE C 208   O  GLN C 211           
SHEET    3   N 5 ILE C 283  MET C 288 -1  O  SER C 284   N  GLU C 207           
SHEET    4   N 5 GLN C 294  ILE C 300 -1  O  ILE C 300   N  ILE C 283           
SHEET    5   N 5 ALA C 369  VAL C 375 -1  O  GLU C 371   N  ARG C 297           
SHEET    1   O 3 VAL C 268  CYS C 269  0                                        
SHEET    2   O 3 CYS C 319  PHE C 322 -1  O  TYR C 320   N  VAL C 268           
SHEET    3   O 3 LEU C 306  PRO C 308 -1  N  ARG C 307   O  LYS C 321           
SSBOND   1 CYS A  155    CYS A  359                          1555   1555  2.06  
SSBOND   2 CYS A  217    CYS A  382                          1555   1555  2.07  
SSBOND   3 CYS A  269    CYS A  319                          1555   1555  2.05  
SSBOND   4 CYS B  155    CYS B  359                          1555   1555  2.10  
SSBOND   5 CYS B  217    CYS B  382                          1555   1555  2.08  
SSBOND   6 CYS B  269    CYS B  319                          1555   1555  2.08  
SSBOND   7 CYS C  155    CYS C  359                          1555   1555  2.05  
SSBOND   8 CYS C  217    CYS C  382                          1555   1555  2.09  
SSBOND   9 CYS C  269    CYS C  319                          1555   1555  2.90  
CISPEP   1 SER A   22    PRO A   23          0        -7.24                     
CISPEP   2 ARG A  128    PRO A  129          0        -5.56                     
CISPEP   3 GLY A  372    PRO A  373          0        -3.21                     
CISPEP   4 SER B   22    PRO B   23          0        -1.70                     
CISPEP   5 ARG B  128    PRO B  129          0         8.30                     
CISPEP   6 GLY B  372    PRO B  373          0         1.69                     
CISPEP   7 SER C   22    PRO C   23          0        -8.11                     
CISPEP   8 ARG C  128    PRO C  129          0         1.46                     
CISPEP   9 GLY C  372    PRO C  373          0        -0.34                     
SITE     1 AC1 17 GLY A  34  SER A  35  TYR A  68  VAL A  69                    
SITE     2 AC1 17 PRO A  70  TYR A  71  THR A  72  LYS A  75                    
SITE     3 AC1 17 ILE A 126  ARG A 128  TYR A 198  LYS A 224                    
SITE     4 AC1 17 ILE A 226  ASP A 228  ARG A 235  THR A 329                    
SITE     5 AC1 17 HOH A 401                                                     
SITE     1 AC2 12 ASP A   4  GLY B  34  TYR B  68  VAL B  69                    
SITE     2 AC2 12 PRO B  70  TYR B  71  THR B  72  ARG B 128                    
SITE     3 AC2 12 TYR B 198  ASP B 228  ARG B 235  THR B 329                    
SITE     1 AC3 12 GLY C  34  TYR C  68  VAL C  69  PRO C  70                    
SITE     2 AC3 12 TYR C  71  THR C  72  ARG C 128  TYR C 198                    
SITE     3 AC3 12 LYS C 224  ASP C 228  THR C 231  ARG C 235                    
CRYST1   81.762  102.774  101.427  90.00 102.90  90.00 P 1 21 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012231  0.000000  0.002802        0.00000                         
SCALE2      0.000000  0.009730  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010115        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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