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Database: PDB
Entry: 4FSL
LinkDB: 4FSL
Original site: 4FSL 
HEADER    HYDROLASE/INHIBITOR                     27-JUN-12   4FSL              
TITLE     CRYSTAL STRUCTURE OF BETA-SITE APP-CLEAVING ENZYME 1 (BACE-DB-MUT)    
TITLE    2 COMPLEX WITH N-(N-(4- ACETAMIDO-3-CHLORO-5-METHYLBENZYL)             
TITLE    3 CARBAMIMIDOYL)-3-(4- METHOXYPHENYL)-5-METHYL-4-ISOTHIAZOLECARBOXAMIDE
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BETA-SECRETASE 1;                                          
COMPND   3 CHAIN: A, B, D, E;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 43-453;                                       
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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    ALZHEIMER'S DISEASE, BETA-SECRETASE, MEMAPSIN 2, BASE, ASPARTIC       
KEYWDS   2 PROTEASE, HYDROLASE-INHIBITOR COMPLEX                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.K.MUCKELBAUER                                                       
REVDAT   5   17-JUL-19 4FSL    1       REMARK                                   
REVDAT   4   13-JUN-18 4FSL    1       REMARK                                   
REVDAT   3   15-NOV-17 4FSL    1       REMARK                                   
REVDAT   2   10-JUL-13 4FSL    1       JRNL                                     
REVDAT   1   10-OCT-12 4FSL    0                                                
JRNL        AUTH   S.W.GERRITZ,W.ZHAI,S.SHI,S.ZHU,J.H.TOYN,J.E.MEREDITH,        
JRNL        AUTH 2 L.G.IBEN,C.R.BURTON,C.F.ALBRIGHT,A.C.GOOD,A.J.TEBBEN,        
JRNL        AUTH 3 J.K.MUCKELBAUER,D.M.CAMAC,W.METZLER,L.S.COOK,R.PADMANABHA,   
JRNL        AUTH 4 K.A.LENTZ,M.J.SOFIA,M.A.POSS,J.E.MACOR,L.A.THOMPSON          
JRNL        TITL   ACYL GUANIDINE INHIBITORS OF BETA-SECRETASE (BACE-1):        
JRNL        TITL 2 OPTIMIZATION OF A MICROMOLAR HIT TO A NANOMOLAR LEAD VIA     
JRNL        TITL 3 ITERATIVE SOLID- AND SOLUTION-PHASE LIBRARY SYNTHESIS        
JRNL        REF    J.MED.CHEM.                   V.  55  9208 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   23030502                                                     
JRNL        DOI    10.1021/JM300931Y                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 66542                          
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) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.224                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3377                            
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) : 2.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4284                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.77                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 246                          
REMARK   3   BIN FREE R VALUE                    : 0.3590                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 12156                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 144                                     
REMARK   3   SOLVENT ATOMS            : 819                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.52000                                             
REMARK   3    B22 (A**2) : -1.86000                                             
REMARK   3    B33 (A**2) : 4.51000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.52000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.639         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.325         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.218         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.853         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.936                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.902                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 12619 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 17174 ; 1.154 ; 1.958       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1544 ; 5.612 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   576 ;36.086 ;23.958       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1976 ;14.724 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    68 ;14.327 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1848 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9784 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  5905 ; 0.179 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  8558 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1070 ; 0.125 ; 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):   101 ; 0.222 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.099 ; 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):  7715 ; 0.318 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12419 ; 0.589 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  5572 ; 0.623 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  4755 ; 1.073 ; 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 4FSL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-12.                  
REMARK 100 THE DEPOSITION ID IS D_1000073303.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 29-APR-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54000                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MICROMAX CONFOCAL                  
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 92                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66645                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.8                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.08700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.7000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 35% PEG8K, 0.2 M AMMONIUM SULFATE, PH    
REMARK 280  6.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
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       65.58850            
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, 4                                              
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: D                                     
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: 4                                                       
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: E                                     
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     LEU A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     ARG A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     THR A    34                                                      
REMARK 465     ASP A    35                                                      
REMARK 465     GLU A    36                                                      
REMARK 465     GLU A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     GLU A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     PRO A    41                                                      
REMARK 465     GLY A    42                                                      
REMARK 465     LYS A    43                                                      
REMARK 465     LYS A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     ILE A   434                                                      
REMARK 465     PRO A   435                                                      
REMARK 465     GLN A   436                                                      
REMARK 465     THR A   437                                                      
REMARK 465     ASP A   438                                                      
REMARK 465     GLU A   439                                                      
REMARK 465     SER A   440                                                      
REMARK 465     THR A   441                                                      
REMARK 465     LEU B    30                                                      
REMARK 465     PRO B    31                                                      
REMARK 465     ARG B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     THR B    34                                                      
REMARK 465     ASP B    35                                                      
REMARK 465     GLU B    36                                                      
REMARK 465     GLU B    37                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     GLU B    39                                                      
REMARK 465     GLU B    40                                                      
REMARK 465     PRO B    41                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     LYS B    43                                                      
REMARK 465     LYS B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     ILE B   434                                                      
REMARK 465     PRO B   435                                                      
REMARK 465     GLN B   436                                                      
REMARK 465     THR B   437                                                      
REMARK 465     ASP B   438                                                      
REMARK 465     GLU B   439                                                      
REMARK 465     SER B   440                                                      
REMARK 465     THR B   441                                                      
REMARK 465     LEU D    30                                                      
REMARK 465     PRO D    31                                                      
REMARK 465     ARG D    32                                                      
REMARK 465     GLU D    33                                                      
REMARK 465     THR D    34                                                      
REMARK 465     ASP D    35                                                      
REMARK 465     GLU D    36                                                      
REMARK 465     GLU D    37                                                      
REMARK 465     PRO D    38                                                      
REMARK 465     GLU D    39                                                      
REMARK 465     GLU D    40                                                      
REMARK 465     PRO D    41                                                      
REMARK 465     GLY D    42                                                      
REMARK 465     LYS D    43                                                      
REMARK 465     LYS D    44                                                      
REMARK 465     GLY D    45                                                      
REMARK 465     SER D    46                                                      
REMARK 465     ILE D   434                                                      
REMARK 465     PRO D   435                                                      
REMARK 465     GLN D   436                                                      
REMARK 465     THR D   437                                                      
REMARK 465     ASP D   438                                                      
REMARK 465     GLU D   439                                                      
REMARK 465     SER D   440                                                      
REMARK 465     THR D   441                                                      
REMARK 465     LEU E    30                                                      
REMARK 465     PRO E    31                                                      
REMARK 465     ARG E    32                                                      
REMARK 465     GLU E    33                                                      
REMARK 465     THR E    34                                                      
REMARK 465     ASP E    35                                                      
REMARK 465     GLU E    36                                                      
REMARK 465     GLU E    37                                                      
REMARK 465     PRO E    38                                                      
REMARK 465     GLU E    39                                                      
REMARK 465     GLU E    40                                                      
REMARK 465     PRO E    41                                                      
REMARK 465     GLY E    42                                                      
REMARK 465     LYS E    43                                                      
REMARK 465     LYS E    44                                                      
REMARK 465     GLY E    45                                                      
REMARK 465     SER E    46                                                      
REMARK 465     ILE E   434                                                      
REMARK 465     PRO E   435                                                      
REMARK 465     GLN E   436                                                      
REMARK 465     THR E   437                                                      
REMARK 465     ASP E   438                                                      
REMARK 465     GLU E   439                                                      
REMARK 465     SER E   440                                                      
REMARK 465     THR E   441                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A 304    CG   CD   CE   NZ                                   
REMARK 470     VAL A 360    CG1  CG2                                            
REMARK 470     VAL B 360    CG1  CG2                                            
REMARK 470     THR B 362    OG1  CG2                                            
REMARK 470     VAL E 360    CG1  CG2                                            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH E   798     O    HOH E   805              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASP B  80   CG    ASP B  80   OD2     0.166                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP B  80   CB  -  CG  -  OD1 ANGL. DEV. =  11.1 DEGREES          
REMARK 500    ASP B  80   CB  -  CG  -  OD2 ANGL. DEV. =  -6.9 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    TRP A 245      -75.95   -137.37                                   
REMARK 500    THR A 362       29.03     47.22                                   
REMARK 500    SER A 363     -167.54    -71.92                                   
REMARK 500    HIS B 137       40.53    -98.67                                   
REMARK 500    TRP B 245      -82.15   -135.76                                   
REMARK 500    THR B 362       19.16     51.16                                   
REMARK 500    SER B 363     -177.17    -60.77                                   
REMARK 500    ALA B 371       32.48    -93.55                                   
REMARK 500    ASP B 411     -169.59   -115.10                                   
REMARK 500    HIS D 137       49.82    -94.83                                   
REMARK 500    TRP D 245      -79.27   -136.41                                   
REMARK 500    THR D 302      -18.91    -46.30                                   
REMARK 500    ALA D 320      119.48    -36.26                                   
REMARK 500    ASN D 341       14.08     57.83                                   
REMARK 500    THR D 362       13.28     57.52                                   
REMARK 500    SER D 363     -174.67    -66.52                                   
REMARK 500    ALA D 371       30.13    -99.98                                   
REMARK 500    ARG E 112       55.18     34.88                                   
REMARK 500    HIS E 137       51.88   -104.62                                   
REMARK 500    TRP E 245      -82.37   -134.63                                   
REMARK 500    THR E 362       29.49     47.12                                   
REMARK 500    SER E 363     -172.72    -69.50                                   
REMARK 500    ALA E 371       36.94    -95.17                                   
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 0VB A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0VB B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0VB D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD D 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0VB E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE IOD E 504                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FSE   RELATED DB: PDB                                   
DBREF  4FSL A   30   440  UNP    P56817   BACE1_HUMAN     43    453             
DBREF  4FSL B   30   440  UNP    P56817   BACE1_HUMAN     43    453             
DBREF  4FSL D   30   440  UNP    P56817   BACE1_HUMAN     43    453             
DBREF  4FSL E   30   440  UNP    P56817   BACE1_HUMAN     43    453             
SEQADV 4FSL LYS A   43  UNP  P56817    ARG    56 CONFLICT                       
SEQADV 4FSL LYS A   44  UNP  P56817    ARG    57 CONFLICT                       
SEQADV 4FSL THR A  441  UNP  P56817              EXPRESSION TAG                 
SEQADV 4FSL LYS B   43  UNP  P56817    ARG    56 CONFLICT                       
SEQADV 4FSL LYS B   44  UNP  P56817    ARG    57 CONFLICT                       
SEQADV 4FSL THR B  441  UNP  P56817              EXPRESSION TAG                 
SEQADV 4FSL LYS D   43  UNP  P56817    ARG    56 CONFLICT                       
SEQADV 4FSL LYS D   44  UNP  P56817    ARG    57 CONFLICT                       
SEQADV 4FSL THR D  441  UNP  P56817              EXPRESSION TAG                 
SEQADV 4FSL LYS E   43  UNP  P56817    ARG    56 CONFLICT                       
SEQADV 4FSL LYS E   44  UNP  P56817    ARG    57 CONFLICT                       
SEQADV 4FSL THR E  441  UNP  P56817              EXPRESSION TAG                 
SEQRES   1 A  412  LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO GLY          
SEQRES   2 A  412  LYS LYS GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG          
SEQRES   3 A  412  GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL          
SEQRES   4 A  412  GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR          
SEQRES   5 A  412  GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO          
SEQRES   6 A  412  PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR          
SEQRES   7 A  412  TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR          
SEQRES   8 A  412  GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL          
SEQRES   9 A  412  SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN          
SEQRES  10 A  412  ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN          
SEQRES  11 A  412  GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA          
SEQRES  12 A  412  GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE          
SEQRES  13 A  412  ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE          
SEQRES  14 A  412  SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN          
SEQRES  15 A  412  SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE          
SEQRES  16 A  412  GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP          
SEQRES  17 A  412  TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE          
SEQRES  18 A  412  ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET          
SEQRES  19 A  412  ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP          
SEQRES  20 A  412  SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE          
SEQRES  21 A  412  GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER THR          
SEQRES  22 A  412  GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU          
SEQRES  23 A  412  VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE          
SEQRES  24 A  412  PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN          
SEQRES  25 A  412  GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU          
SEQRES  26 A  412  ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS          
SEQRES  27 A  412  TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR VAL          
SEQRES  28 A  412  MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE          
SEQRES  29 A  412  ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA          
SEQRES  30 A  412  CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU          
SEQRES  31 A  412  GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR          
SEQRES  32 A  412  ASN ILE PRO GLN THR ASP GLU SER THR                          
SEQRES   1 B  412  LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO GLY          
SEQRES   2 B  412  LYS LYS GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG          
SEQRES   3 B  412  GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL          
SEQRES   4 B  412  GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR          
SEQRES   5 B  412  GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO          
SEQRES   6 B  412  PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR          
SEQRES   7 B  412  TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR          
SEQRES   8 B  412  GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL          
SEQRES   9 B  412  SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN          
SEQRES  10 B  412  ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN          
SEQRES  11 B  412  GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA          
SEQRES  12 B  412  GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE          
SEQRES  13 B  412  ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE          
SEQRES  14 B  412  SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN          
SEQRES  15 B  412  SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE          
SEQRES  16 B  412  GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP          
SEQRES  17 B  412  TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE          
SEQRES  18 B  412  ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET          
SEQRES  19 B  412  ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP          
SEQRES  20 B  412  SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE          
SEQRES  21 B  412  GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER THR          
SEQRES  22 B  412  GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU          
SEQRES  23 B  412  VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE          
SEQRES  24 B  412  PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN          
SEQRES  25 B  412  GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU          
SEQRES  26 B  412  ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS          
SEQRES  27 B  412  TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR VAL          
SEQRES  28 B  412  MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE          
SEQRES  29 B  412  ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA          
SEQRES  30 B  412  CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU          
SEQRES  31 B  412  GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR          
SEQRES  32 B  412  ASN ILE PRO GLN THR ASP GLU SER THR                          
SEQRES   1 D  412  LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO GLY          
SEQRES   2 D  412  LYS LYS GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG          
SEQRES   3 D  412  GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL          
SEQRES   4 D  412  GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR          
SEQRES   5 D  412  GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO          
SEQRES   6 D  412  PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR          
SEQRES   7 D  412  TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR          
SEQRES   8 D  412  GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL          
SEQRES   9 D  412  SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN          
SEQRES  10 D  412  ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN          
SEQRES  11 D  412  GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA          
SEQRES  12 D  412  GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE          
SEQRES  13 D  412  ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE          
SEQRES  14 D  412  SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN          
SEQRES  15 D  412  SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE          
SEQRES  16 D  412  GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP          
SEQRES  17 D  412  TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE          
SEQRES  18 D  412  ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET          
SEQRES  19 D  412  ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP          
SEQRES  20 D  412  SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE          
SEQRES  21 D  412  GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER THR          
SEQRES  22 D  412  GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU          
SEQRES  23 D  412  VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE          
SEQRES  24 D  412  PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN          
SEQRES  25 D  412  GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU          
SEQRES  26 D  412  ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS          
SEQRES  27 D  412  TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR VAL          
SEQRES  28 D  412  MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE          
SEQRES  29 D  412  ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA          
SEQRES  30 D  412  CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU          
SEQRES  31 D  412  GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR          
SEQRES  32 D  412  ASN ILE PRO GLN THR ASP GLU SER THR                          
SEQRES   1 E  412  LEU PRO ARG GLU THR ASP GLU GLU PRO GLU GLU PRO GLY          
SEQRES   2 E  412  LYS LYS GLY SER PHE VAL GLU MET VAL ASP ASN LEU ARG          
SEQRES   3 E  412  GLY LYS SER GLY GLN GLY TYR TYR VAL GLU MET THR VAL          
SEQRES   4 E  412  GLY SER PRO PRO GLN THR LEU ASN ILE LEU VAL ASP THR          
SEQRES   5 E  412  GLY SER SER ASN PHE ALA VAL GLY ALA ALA PRO HIS PRO          
SEQRES   6 E  412  PHE LEU HIS ARG TYR TYR GLN ARG GLN LEU SER SER THR          
SEQRES   7 E  412  TYR ARG ASP LEU ARG LYS GLY VAL TYR VAL PRO TYR THR          
SEQRES   8 E  412  GLN GLY LYS TRP GLU GLY GLU LEU GLY THR ASP LEU VAL          
SEQRES   9 E  412  SER ILE PRO HIS GLY PRO ASN VAL THR VAL ARG ALA ASN          
SEQRES  10 E  412  ILE ALA ALA ILE THR GLU SER ASP LYS PHE PHE ILE ASN          
SEQRES  11 E  412  GLY SER ASN TRP GLU GLY ILE LEU GLY LEU ALA TYR ALA          
SEQRES  12 E  412  GLU ILE ALA ARG PRO ASP ASP SER LEU GLU PRO PHE PHE          
SEQRES  13 E  412  ASP SER LEU VAL LYS GLN THR HIS VAL PRO ASN LEU PHE          
SEQRES  14 E  412  SER LEU GLN LEU CYS GLY ALA GLY PHE PRO LEU ASN GLN          
SEQRES  15 E  412  SER GLU VAL LEU ALA SER VAL GLY GLY SER MET ILE ILE          
SEQRES  16 E  412  GLY GLY ILE ASP HIS SER LEU TYR THR GLY SER LEU TRP          
SEQRES  17 E  412  TYR THR PRO ILE ARG ARG GLU TRP TYR TYR GLU VAL ILE          
SEQRES  18 E  412  ILE VAL ARG VAL GLU ILE ASN GLY GLN ASP LEU LYS MET          
SEQRES  19 E  412  ASP CYS LYS GLU TYR ASN TYR ASP LYS SER ILE VAL ASP          
SEQRES  20 E  412  SER GLY THR THR ASN LEU ARG LEU PRO LYS LYS VAL PHE          
SEQRES  21 E  412  GLU ALA ALA VAL LYS SER ILE LYS ALA ALA SER SER THR          
SEQRES  22 E  412  GLU LYS PHE PRO ASP GLY PHE TRP LEU GLY GLU GLN LEU          
SEQRES  23 E  412  VAL CYS TRP GLN ALA GLY THR THR PRO TRP ASN ILE PHE          
SEQRES  24 E  412  PRO VAL ILE SER LEU TYR LEU MET GLY GLU VAL THR ASN          
SEQRES  25 E  412  GLN SER PHE ARG ILE THR ILE LEU PRO GLN GLN TYR LEU          
SEQRES  26 E  412  ARG PRO VAL GLU ASP VAL ALA THR SER GLN ASP ASP CYS          
SEQRES  27 E  412  TYR LYS PHE ALA ILE SER GLN SER SER THR GLY THR VAL          
SEQRES  28 E  412  MET GLY ALA VAL ILE MET GLU GLY PHE TYR VAL VAL PHE          
SEQRES  29 E  412  ASP ARG ALA ARG LYS ARG ILE GLY PHE ALA VAL SER ALA          
SEQRES  30 E  412  CYS HIS VAL HIS ASP GLU PHE ARG THR ALA ALA VAL GLU          
SEQRES  31 E  412  GLY PRO PHE VAL THR LEU ASP MET GLU ASP CYS GLY TYR          
SEQRES  32 E  412  ASN ILE PRO GLN THR ASP GLU SER THR                          
HET    0VB  A 501      33                                                       
HET    IOD  A 502       1                                                       
HET    IOD  A 503       1                                                       
HET    IOD  A 504       1                                                       
HET    0VB  B 501      33                                                       
HET    IOD  B 502       1                                                       
HET    IOD  B 503       1                                                       
HET    IOD  B 504       1                                                       
HET    0VB  D 501      33                                                       
HET    IOD  D 502       1                                                       
HET    IOD  D 503       1                                                       
HET    IOD  D 504       1                                                       
HET    0VB  E 501      33                                                       
HET    IOD  E 502       1                                                       
HET    IOD  E 503       1                                                       
HET    IOD  E 504       1                                                       
HETNAM     0VB N-{N-[4-(ACETYLAMINO)-3-CHLORO-5-                                
HETNAM   2 0VB  METHYLBENZYL]CARBAMIMIDOYL}-3-(4-METHOXYPHENYL)-5-              
HETNAM   3 0VB  METHYL-1,2-THIAZOLE-4-CARBOXAMIDE                               
HETNAM     IOD IODIDE ION                                                       
FORMUL   5  0VB    4(C23 H24 CL N5 O3 S)                                        
FORMUL   6  IOD    12(I 1-)                                                     
FORMUL  21  HOH   *819(H2 O)                                                    
HELIX    1   1 GLN A  101  SER A  105  5                                   5    
HELIX    2   2 TYR A  171  ALA A  175  5                                   5    
HELIX    3   3 PRO A  183  THR A  192  1                                  10    
HELIX    4   4 ASN A  210  SER A  217  1                                   8    
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  324  PHE A  328  5                                   5    
HELIX    9   9 LEU A  349  TYR A  353  1                                   5    
HELIX   10  10 GLY A  382  GLU A  387  1                                   6    
HELIX   11  11 ARG A  395  ARG A  397  5                                   3    
HELIX   12  12 ASP A  426  GLY A  431  5                                   6    
HELIX   13  13 GLN B  101  SER B  105  5                                   5    
HELIX   14  14 TYR B  171  ALA B  175  5                                   5    
HELIX   15  15 PRO B  183  THR B  192  1                                  10    
HELIX   16  16 ASN B  210  SER B  217  1                                   8    
HELIX   17  17 ASP B  228  SER B  230  5                                   3    
HELIX   18  18 ASP B  264  TYR B  270  5                                   7    
HELIX   19  19 LYS B  286  SER B  300  1                                  15    
HELIX   20  20 PRO B  306  LEU B  311  1                                   6    
HELIX   21  21 PRO B  324  PHE B  328  5                                   5    
HELIX   22  22 LEU B  349  TYR B  353  1                                   5    
HELIX   23  23 GLY B  382  GLU B  387  1                                   6    
HELIX   24  24 ASP B  426  GLY B  431  5                                   6    
HELIX   25  25 GLN D  101  SER D  105  5                                   5    
HELIX   26  26 TYR D  171  ALA D  175  5                                   5    
HELIX   27  27 PRO D  183  THR D  192  1                                  10    
HELIX   28  28 ASN D  210  SER D  217  1                                   8    
HELIX   29  29 ASP D  228  SER D  230  5                                   3    
HELIX   30  30 ASP D  264  TYR D  270  5                                   7    
HELIX   31  31 LYS D  286  SER D  300  1                                  15    
HELIX   32  32 PRO D  324  PHE D  328  5                                   5    
HELIX   33  33 LEU D  349  TYR D  353  1                                   5    
HELIX   34  34 GLY D  382  GLU D  387  1                                   6    
HELIX   35  35 ARG D  395  ARG D  397  5                                   3    
HELIX   36  36 ASP D  426  GLY D  431  5                                   6    
HELIX   37  37 GLN E  101  SER E  105  5                                   5    
HELIX   38  38 TYR E  171  ALA E  175  5                                   5    
HELIX   39  39 PRO E  183  THR E  192  1                                  10    
HELIX   40  40 ASN E  210  SER E  217  1                                   8    
HELIX   41  41 ASP E  264  TYR E  270  5                                   7    
HELIX   42  42 LYS E  286  SER E  300  1                                  15    
HELIX   43  43 PRO E  306  LEU E  311  1                                   6    
HELIX   44  44 PRO E  324  PHE E  328  5                                   5    
HELIX   45  45 LEU E  349  TYR E  353  1                                   5    
HELIX   46  46 GLY E  382  GLU E  387  1                                   6    
HELIX   47  47 ASP E  426  GLY E  431  5                                   6    
SHEET    1   A 8 LEU A  54  LYS A  57  0                                        
SHEET    2   A 8 GLY A  61  VAL A  68 -1  O  TYR A  63   N  ARG A  55           
SHEET    3   A 8 GLN A  73  ASP A  80 -1  O  ILE A  77   N  VAL A  64           
SHEET    4   A 8 GLY A 165  GLY A 168  1  O  LEU A 167   N  LEU A  78           
SHEET    5   A 8 PHE A  86  GLY A  89 -1  N  ALA A  87   O  ILE A 166           
SHEET    6   A 8 VAL A 143  ASP A 154  1  O  ILE A 150   N  VAL A  88           
SHEET    7   A 8 LYS A 123  SER A 134 -1  N  GLY A 129   O  ILE A 147           
SHEET    8   A 8 ARG A 109  PRO A 118 -1  N  VAL A 117   O  TRP A 124           
SHEET    1   B 4 LEU A  54  LYS A  57  0                                        
SHEET    2   B 4 GLY A  61  VAL A  68 -1  O  TYR A  63   N  ARG A  55           
SHEET    3   B 4 LYS A 123  SER A 134 -1  O  SER A 134   N  THR A  67           
SHEET    4   B 4 ARG A 109  PRO A 118 -1  N  VAL A 117   O  TRP A 124           
SHEET    1   C 5 GLY A 220  ILE A 224  0                                        
SHEET    2   C 5 PHE A 198  LEU A 202 -1  N  GLN A 201   O  SER A 221           
SHEET    3   C 5 PHE A 389  ASP A 394 -1  O  PHE A 393   N  PHE A 198           
SHEET    4   C 5 ARG A 399  SER A 405 -1  O  ALA A 403   N  TYR A 390           
SHEET    5   C 5 TYR A 232  PRO A 240 -1  N  THR A 239   O  ILE A 400           
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  ALA A 417   N  THR A 347           
SHEET    1   E 4 SER A 273  VAL A 275  0                                        
SHEET    2   E 4 THR A 379  MET A 381  1  O  MET A 381   N  ILE A 274           
SHEET    3   E 4 LEU A 282  PRO A 285 -1  N  ARG A 283   O  VAL A 380           
SHEET    4   E 4 ILE A 372  SER A 375  1  O  SER A 373   N  LEU A 282           
SHEET    1   F 3 VAL A 316  TRP A 318  0                                        
SHEET    2   F 3 ASP A 366  PHE A 370 -1  O  ASP A 366   N  TRP A 318           
SHEET    3   F 3 LEU A 354  VAL A 357 -1  N  ARG A 355   O  LYS A 369           
SHEET    1   G 8 LEU B  54  LYS B  57  0                                        
SHEET    2   G 8 GLY B  61  VAL B  68 -1  O  TYR B  63   N  ARG B  55           
SHEET    3   G 8 GLN B  73  ASP B  80 -1  O  LEU B  75   N  MET B  66           
SHEET    4   G 8 GLY B 165  GLY B 168  1  O  GLY B 165   N  LEU B  78           
SHEET    5   G 8 PHE B  86  GLY B  89 -1  N  ALA B  87   O  ILE B 166           
SHEET    6   G 8 THR B 142  ASP B 154  1  O  ILE B 150   N  VAL B  88           
SHEET    7   G 8 LYS B 123  SER B 134 -1  N  LYS B 123   O  ASP B 154           
SHEET    8   G 8 ARG B 109  PRO B 118 -1  N  LYS B 113   O  LEU B 128           
SHEET    1   H 4 LEU B  54  LYS B  57  0                                        
SHEET    2   H 4 GLY B  61  VAL B  68 -1  O  TYR B  63   N  ARG B  55           
SHEET    3   H 4 LYS B 123  SER B 134 -1  O  SER B 134   N  THR B  67           
SHEET    4   H 4 ARG B 109  PRO B 118 -1  N  LYS B 113   O  LEU B 128           
SHEET    1   I 5 GLY B 220  ILE B 224  0                                        
SHEET    2   I 5 PHE B 198  LEU B 202 -1  N  GLN B 201   O  SER B 221           
SHEET    3   I 5 PHE B 389  ASP B 394 -1  O  PHE B 393   N  PHE B 198           
SHEET    4   I 5 ARG B 399  SER B 405 -1  O  ALA B 403   N  TYR B 390           
SHEET    5   I 5 TYR B 232  PRO B 240 -1  N  THR B 239   O  ILE B 400           
SHEET    1   J 5 GLN B 259  ASP B 260  0                                        
SHEET    2   J 5 ILE B 251  ILE B 256 -1  N  ILE B 256   O  GLN B 259           
SHEET    3   J 5 ILE B 331  MET B 336 -1  O  TYR B 334   N  ARG B 253           
SHEET    4   J 5 GLN B 342  ILE B 348 -1  O  ILE B 348   N  ILE B 331           
SHEET    5   J 5 ALA B 417  VAL B 423 -1  O  ALA B 417   N  THR B 347           
SHEET    1   K 4 SER B 273  VAL B 275  0                                        
SHEET    2   K 4 THR B 379  MET B 381  1  O  MET B 381   N  ILE B 274           
SHEET    3   K 4 LEU B 282  PRO B 285 -1  N  ARG B 283   O  VAL B 380           
SHEET    4   K 4 ILE B 372  SER B 375  1  O  SER B 375   N  LEU B 284           
SHEET    1   L 3 VAL B 316  TRP B 318  0                                        
SHEET    2   L 3 ASP B 366  PHE B 370 -1  O  ASP B 366   N  TRP B 318           
SHEET    3   L 3 LEU B 354  VAL B 357 -1  N  ARG B 355   O  LYS B 369           
SHEET    1   M 8 LEU D  54  LYS D  57  0                                        
SHEET    2   M 8 GLY D  61  VAL D  68 -1  O  TYR D  63   N  ARG D  55           
SHEET    3   M 8 GLN D  73  ASP D  80 -1  O  VAL D  79   N  TYR D  62           
SHEET    4   M 8 GLY D 165  GLY D 168  1  O  GLY D 165   N  LEU D  78           
SHEET    5   M 8 PHE D  86  GLY D  89 -1  N  ALA D  87   O  ILE D 166           
SHEET    6   M 8 VAL D 143  ASP D 154  1  O  ILE D 150   N  VAL D  88           
SHEET    7   M 8 GLY D 122  SER D 134 -1  N  GLY D 129   O  ILE D 147           
SHEET    8   M 8 ARG D 109  TYR D 119 -1  N  LYS D 113   O  LEU D 128           
SHEET    1   N 4 LEU D  54  LYS D  57  0                                        
SHEET    2   N 4 GLY D  61  VAL D  68 -1  O  TYR D  63   N  ARG D  55           
SHEET    3   N 4 GLY D 122  SER D 134 -1  O  SER D 134   N  THR D  67           
SHEET    4   N 4 ARG D 109  TYR D 119 -1  N  LYS D 113   O  LEU D 128           
SHEET    1   O 5 GLY D 220  ILE D 224  0                                        
SHEET    2   O 5 PHE D 198  LEU D 202 -1  N  GLN D 201   O  SER D 221           
SHEET    3   O 5 PHE D 389  ASP D 394 -1  O  VAL D 391   N  LEU D 200           
SHEET    4   O 5 ARG D 399  SER D 405 -1  O  GLY D 401   N  VAL D 392           
SHEET    5   O 5 TYR D 232  PRO D 240 -1  N  THR D 239   O  ILE D 400           
SHEET    1   P 5 GLU D 248  VAL D 249  0                                        
SHEET    2   P 5 SER D 273  VAL D 275 -1  O  SER D 273   N  VAL D 249           
SHEET    3   P 5 THR D 379  MET D 381  1  O  THR D 379   N  ILE D 274           
SHEET    4   P 5 LEU D 282  PRO D 285 -1  N  ARG D 283   O  VAL D 380           
SHEET    5   P 5 ILE D 372  SER D 375  1  O  SER D 375   N  LEU D 284           
SHEET    1   Q 5 GLN D 259  ASP D 260  0                                        
SHEET    2   Q 5 ILE D 251  ILE D 256 -1  N  ILE D 256   O  GLN D 259           
SHEET    3   Q 5 ILE D 331  MET D 336 -1  O  TYR D 334   N  VAL D 252           
SHEET    4   Q 5 GLN D 342  ILE D 348 -1  O  ILE D 348   N  ILE D 331           
SHEET    5   Q 5 ALA D 417  VAL D 423 -1  O  GLU D 419   N  ARG D 345           
SHEET    1   R 3 VAL D 316  TRP D 318  0                                        
SHEET    2   R 3 ASP D 366  PHE D 370 -1  O  ASP D 366   N  TRP D 318           
SHEET    3   R 3 LEU D 354  VAL D 357 -1  N  ARG D 355   O  LYS D 369           
SHEET    1   S 8 LEU E  54  LYS E  57  0                                        
SHEET    2   S 8 GLY E  61  VAL E  68 -1  O  TYR E  63   N  ARG E  55           
SHEET    3   S 8 GLN E  73  ASP E  80 -1  O  LEU E  75   N  MET E  66           
SHEET    4   S 8 GLY E 165  GLY E 168  1  O  LEU E 167   N  LEU E  78           
SHEET    5   S 8 PHE E  86  GLY E  89 -1  N  ALA E  87   O  ILE E 166           
SHEET    6   S 8 VAL E 143  ASP E 154  1  O  ILE E 150   N  VAL E  88           
SHEET    7   S 8 LYS E 123  SER E 134 -1  N  GLU E 125   O  GLU E 152           
SHEET    8   S 8 ARG E 109  PRO E 118 -1  N  VAL E 115   O  GLY E 126           
SHEET    1   T 4 LEU E  54  LYS E  57  0                                        
SHEET    2   T 4 GLY E  61  VAL E  68 -1  O  TYR E  63   N  ARG E  55           
SHEET    3   T 4 LYS E 123  SER E 134 -1  O  SER E 134   N  THR E  67           
SHEET    4   T 4 ARG E 109  PRO E 118 -1  N  VAL E 115   O  GLY E 126           
SHEET    1   U 5 GLY E 220  ILE E 224  0                                        
SHEET    2   U 5 PHE E 198  LEU E 202 -1  N  GLN E 201   O  SER E 221           
SHEET    3   U 5 PHE E 389  ASP E 394 -1  O  VAL E 391   N  LEU E 200           
SHEET    4   U 5 ARG E 399  SER E 405 -1  O  GLY E 401   N  VAL E 392           
SHEET    5   U 5 TYR E 232  PRO E 240 -1  N  THR E 239   O  ILE E 400           
SHEET    1   V 5 GLN E 259  ASP E 260  0                                        
SHEET    2   V 5 ILE E 251  ILE E 256 -1  N  ILE E 256   O  GLN E 259           
SHEET    3   V 5 ILE E 331  MET E 336 -1  O  TYR E 334   N  ARG E 253           
SHEET    4   V 5 GLN E 342  ILE E 348 -1  O  ILE E 348   N  ILE E 331           
SHEET    5   V 5 ALA E 417  VAL E 423 -1  O  GLU E 419   N  ARG E 345           
SHEET    1   W 4 SER E 273  VAL E 275  0                                        
SHEET    2   W 4 THR E 379  MET E 381  1  O  MET E 381   N  ILE E 274           
SHEET    3   W 4 LEU E 282  PRO E 285 -1  N  ARG E 283   O  VAL E 380           
SHEET    4   W 4 ILE E 372  SER E 375  1  O  SER E 375   N  LEU E 284           
SHEET    1   X 3 VAL E 316  TRP E 318  0                                        
SHEET    2   X 3 ASP E 366  PHE E 370 -1  O  ASP E 366   N  TRP E 318           
SHEET    3   X 3 LEU E 354  VAL E 357 -1  N  ARG E 355   O  LYS E 369           
SSBOND   1 CYS A  203    CYS A  407                          1555   1555  2.04  
SSBOND   2 CYS A  265    CYS A  430                          1555   1555  2.02  
SSBOND   3 CYS A  317    CYS A  367                          1555   1555  2.02  
SSBOND   4 CYS B  203    CYS B  407                          1555   1555  2.04  
SSBOND   5 CYS B  265    CYS B  430                          1555   1555  2.03  
SSBOND   6 CYS B  317    CYS B  367                          1555   1555  2.03  
SSBOND   7 CYS D  203    CYS D  407                          1555   1555  2.03  
SSBOND   8 CYS D  265    CYS D  430                          1555   1555  2.57  
SSBOND   9 CYS D  317    CYS D  367                          1555   1555  2.03  
SSBOND  10 CYS E  203    CYS E  407                          1555   1555  2.04  
SSBOND  11 CYS E  265    CYS E  430                          1555   1555  2.03  
SSBOND  12 CYS E  317    CYS E  367                          1555   1555  2.02  
CISPEP   1 SER A   70    PRO A   71          0        -4.50                     
CISPEP   2 ARG A  176    PRO A  177          0         3.20                     
CISPEP   3 TYR A  270    ASP A  271          0         4.60                     
CISPEP   4 GLY A  420    PRO A  421          0        -0.26                     
CISPEP   5 SER B   70    PRO B   71          0        -1.38                     
CISPEP   6 ARG B  176    PRO B  177          0         5.79                     
CISPEP   7 TYR B  270    ASP B  271          0        -5.60                     
CISPEP   8 GLY B  420    PRO B  421          0         3.51                     
CISPEP   9 SER D   70    PRO D   71          0        -4.69                     
CISPEP  10 ARG D  176    PRO D  177          0         2.00                     
CISPEP  11 TYR D  270    ASP D  271          0         1.76                     
CISPEP  12 GLY D  420    PRO D  421          0         1.39                     
CISPEP  13 SER E   70    PRO E   71          0        -0.33                     
CISPEP  14 ARG E  176    PRO E  177          0         0.41                     
CISPEP  15 TYR E  270    ASP E  271          0         3.90                     
CISPEP  16 GLY E  420    PRO E  421          0        -1.53                     
SITE     1 AC1 18 LEU A  78  ASP A  80  GLY A  82  TYR A 119                    
SITE     2 AC1 18 GLN A 121  GLY A 122  LYS A 155  PHE A 156                    
SITE     3 AC1 18 ILE A 158  TYR A 246  ILE A 274  ASP A 276                    
SITE     4 AC1 18 GLY A 278  THR A 279  ARG A 283  THR A 377                    
SITE     5 AC1 18 VAL A 380  IOD A 502                                          
SITE     1 AC2  4 THR A 279  ASN A 281  ARG A 283  0VB A 501                    
SITE     1 AC3  2 TYR A 116  PRO A 177                                          
SITE     1 AC4 18 ASP B  80  GLY B  82  SER B  83  TYR B 119                    
SITE     2 AC4 18 GLN B 121  GLY B 122  LYS B 155  PHE B 156                    
SITE     3 AC4 18 ILE B 158  TRP B 163  TYR B 246  ILE B 274                    
SITE     4 AC4 18 ASP B 276  THR B 279  ARG B 283  THR B 377                    
SITE     5 AC4 18 VAL B 380  HOH B 722                                          
SITE     1 AC5  2 ASN B 281  ARG B 283                                          
SITE     1 AC6  2 TYR B 116  PRO B 177                                          
SITE     1 AC7 17 LEU D  78  ASP D  80  TYR D 119  THR D 120                    
SITE     2 AC7 17 GLN D 121  LYS D 155  PHE D 156  ILE D 158                    
SITE     3 AC7 17 TRP D 163  TYR D 246  ILE D 274  ASP D 276                    
SITE     4 AC7 17 GLY D 278  THR D 279  ARG D 283  THR D 377                    
SITE     5 AC7 17 VAL D 380                                                     
SITE     1 AC8  2 ASN D 281  ARG D 283                                          
SITE     1 AC9  2 TYR D 116  PRO D 177                                          
SITE     1 BC1 17 LEU E  78  ASP E  80  GLY E  82  TYR E 119                    
SITE     2 BC1 17 GLN E 121  LYS E 155  PHE E 156  ILE E 158                    
SITE     3 BC1 17 TRP E 163  TYR E 246  ILE E 274  ASP E 276                    
SITE     4 BC1 17 GLY E 278  THR E 279  ARG E 283  THR E 377                    
SITE     5 BC1 17 VAL E 380                                                     
SITE     1 BC2  2 ASN E 281  ARG E 283                                          
SITE     1 BC3  2 TYR E 116  PRO E 177                                          
SITE     1 BC4  1 LYS E 123                                                     
CRYST1   86.540  131.177   90.315  90.00  97.61  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011555  0.000000  0.001544        0.00000                         
SCALE2      0.000000  0.007623  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011171        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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