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Database: PDB
Entry: 2IL2
LinkDB: 2IL2
Original site: 2IL2 
HEADER    HYDROLASE                               02-OCT-06   2IL2              
TITLE     CRYSTAL STRUCTURE OF HUMAN RENIN COMPLEXED WITH INHIBITOR             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RENIN;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ANGIOTENSINOGENASE;                                         
COMPND   5 EC: 3.4.23.15;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 EXPRESSION_SYSTEM_CELL: OVARY                                        
KEYWDS    RENIN, INHIBITORS, DRUG DESIGN, HYDROLASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.MOCHALKIN                                                           
REVDAT   6   30-AUG-23 2IL2    1       REMARK                                   
REVDAT   5   18-OCT-17 2IL2    1       REMARK                                   
REVDAT   4   13-JUL-11 2IL2    1       VERSN                                    
REVDAT   3   24-FEB-09 2IL2    1       VERSN                                    
REVDAT   2   02-JAN-07 2IL2    1       JRNL                                     
REVDAT   1   05-DEC-06 2IL2    0                                                
JRNL        AUTH   R.W.SARVER,J.PEEVERS,W.L.CODY,F.L.CISKE,J.DYER,S.D.EMERSON,  
JRNL        AUTH 2 J.C.HAGADORN,D.D.HOLSWORTH,M.JALAIE,M.KAUFMAN,M.MASTRONARDI, 
JRNL        AUTH 3 P.MCCONNELL,N.A.POWELL,J.QUIN,C.A.VAN HUIS,E.ZHANG,          
JRNL        AUTH 4 I.MOCHALKIN                                                  
JRNL        TITL   BINDING THERMODYNAMICS OF SUBSTITUTED DIAMINOPYRIMIDINE      
JRNL        TITL 2 RENIN INHIBITORS.                                            
JRNL        REF    ANAL.BIOCHEM.                 V. 360    30 2007              
JRNL        REFN                   ISSN 0003-2697                               
JRNL        PMID   17113558                                                     
JRNL        DOI    10.1016/J.AB.2006.10.017                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.24 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) : 2.24                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 45166                          
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) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.206                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2281                            
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) : 2.24                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3055                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.02                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3230                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 166                          
REMARK   3   BIN FREE R VALUE                    : 0.3820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5212                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 101                                     
REMARK   3   SOLVENT ATOMS            : 242                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.244         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.297        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5446 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3600 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7403 ; 1.411 ; 1.977       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8764 ; 0.884 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   674 ; 7.584 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   224 ;34.472 ;24.196       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   866 ;16.160 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;20.333 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   814 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6082 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1142 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   833 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3644 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2598 ; 0.180 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2902 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   242 ; 0.129 ; 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):    24 ; 0.274 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    52 ; 0.295 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    16 ; 0.177 ; 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):  4266 ; 0.846 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1392 ; 0.119 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5396 ; 1.003 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2561 ; 1.585 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2007 ; 2.325 ; 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  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -2        A   335                          
REMARK   3    ORIGIN FOR THE GROUP (A): -29.6190   3.5720 -11.8910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1035 T22:  -0.1322                                     
REMARK   3      T33:  -0.2244 T12:   0.0330                                     
REMARK   3      T13:   0.0344 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0904 L22:   1.3826                                     
REMARK   3      L33:   0.8378 L12:   1.0732                                     
REMARK   3      L13:   0.4399 L23:   0.2925                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1464 S12:  -0.2421 S13:   0.0532                       
REMARK   3      S21:   0.0852 S22:  -0.1672 S23:   0.0467                       
REMARK   3      S31:  -0.0889 S32:  -0.1629 S33:   0.0207                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -2        B   335                          
REMARK   3    ORIGIN FOR THE GROUP (A): -52.8230 -12.8220 -35.1220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1890 T22:  -0.0762                                     
REMARK   3      T33:  -0.1894 T12:  -0.0446                                     
REMARK   3      T13:   0.0114 T23:   0.0719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2909 L22:   2.2840                                     
REMARK   3      L33:   1.8717 L12:  -0.6795                                     
REMARK   3      L13:  -0.0766 L23:   0.6876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0710 S12:  -0.0238 S13:  -0.1185                       
REMARK   3      S21:   0.1526 S22:  -0.0093 S23:   0.1720                       
REMARK   3      S31:   0.2626 S32:  -0.3023 S33:  -0.0618                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   401        A   401                          
REMARK   3    ORIGIN FOR THE GROUP (A): -24.8090  -2.2850 -10.2660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0119 T22:  -0.0208                                     
REMARK   3      T33:  -0.0188 T12:  -0.0282                                     
REMARK   3      T13:   0.0337 T23:   0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  18.1908 L22:   6.2848                                     
REMARK   3      L33:  25.6952 L12:  -9.2382                                     
REMARK   3      L13:   5.5401 L23:   0.7370                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0549 S12:  -0.5931 S13:  -1.2898                       
REMARK   3      S21:  -0.0097 S22:   0.2503 S23:   0.9134                       
REMARK   3      S31:   1.0692 S32:  -0.3536 S33:  -0.3053                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   402        B   402                          
REMARK   3    RESIDUE RANGE :   A   501        A   501                          
REMARK   3    ORIGIN FOR THE GROUP (A): -47.3100 -18.8210 -29.6350              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0218 T22:   0.0075                                     
REMARK   3      T33:   0.0027 T12:   0.0255                                     
REMARK   3      T13:   0.0084 T23:   0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.1241 L22:   2.5538                                     
REMARK   3      L33:   2.8292 L12:   2.5072                                     
REMARK   3      L13:   4.6714 L23:  -0.2486                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4582 S12:  -0.9633 S13:  -0.4694                       
REMARK   3      S21:  -0.2344 S22:  -0.2054 S23:   0.3581                       
REMARK   3      S31:   0.7524 S32:  -0.6346 S33:  -0.2528                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2IL2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-OCT-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000039704.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JAN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45325                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.240                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.07300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.24                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.62700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.62700                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.280                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 2IKO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.18                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10-20 % PEG 3350, 50 MM SODIUM CITRATE   
REMARK 280  PH 4.5, 0.6 M NACL., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE     
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 3                           
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290       5555   Z,X,Y                                                   
REMARK 290       6555   Z+1/2,-X+1/2,-Y                                         
REMARK 290       7555   -Z+1/2,-X,Y+1/2                                         
REMARK 290       8555   -Z,X+1/2,-Y+1/2                                         
REMARK 290       9555   Y,Z,X                                                   
REMARK 290      10555   -Y,Z+1/2,-X+1/2                                         
REMARK 290      11555   Y+1/2,-Z+1/2,-X                                         
REMARK 290      12555   -Y+1/2,-Z,X+1/2                                         
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       70.76650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       70.76650            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       70.76650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       70.76650            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       70.76650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       70.76650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY2   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   6  0.000000  0.000000  1.000000       70.76650            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       70.76650            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       70.76650            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       70.76650            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       70.76650            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       70.76650            
REMARK 290   SMTRY1   9  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   9  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY3   9  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  10  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2  10  0.000000  0.000000  1.000000       70.76650            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       70.76650            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       70.76650            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       70.76650            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       70.76650            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       70.76650            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEXAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 24710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 71340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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   BIOMT1   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000        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    -4                                                      
REMARK 465     THR A    -3                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     THR B    -3                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B   18   CA   CB   CG   CD   OE1  OE2                        
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    ASN A  70      -66.47   -131.16                                   
REMARK 500    SER A 207       56.72   -102.43                                   
REMARK 500    SER A 208      126.99   -170.00                                   
REMARK 500    CYS A 216     -166.97   -161.62                                   
REMARK 500    ARG A 246     -166.70   -114.41                                   
REMARK 500    ALA A 294       46.74    -89.46                                   
REMARK 500    ASP B  12       12.37     56.52                                   
REMARK 500    ASN B  70      -56.97   -129.42                                   
REMARK 500    ARG B 134       44.88     37.53                                   
REMARK 500    GLN B 165       50.03   -100.23                                   
REMARK 500    SER B 207       79.58   -102.67                                   
REMARK 500    SER B 208      117.56    158.31                                   
REMARK 500    ARG B 246      -92.24    -60.70                                   
REMARK 500    LEU B 247      -61.99   -120.98                                   
REMARK 500    ALA B 294       40.61    -90.14                                   
REMARK 500    ALA B 334     -128.84     96.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY B   96     ILE B   97                  149.72                    
REMARK 500 LEU B  333     ALA B  334                  136.92                    
REMARK 500 ALA B  334     ARG B  335                  -35.09                    
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 LIX A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LIX B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CIT A 501                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2IKU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2IKO   RELATED DB: PDB                                   
DBREF  2IL2 A   -4   335  UNP    P00797   RENI_HUMAN      67    406             
DBREF  2IL2 B   -4   335  UNP    P00797   RENI_HUMAN      67    406             
SEQRES   1 A  340  LEU THR LEU GLY ASN THR THR SER SER VAL ILE LEU THR          
SEQRES   2 A  340  ASN TYR MET ASP THR GLN TYR TYR GLY GLU ILE GLY ILE          
SEQRES   3 A  340  GLY THR PRO PRO GLN THR PHE LYS VAL VAL PHE ASP THR          
SEQRES   4 A  340  GLY SER SER ASN VAL TRP VAL PRO SER SER LYS CYS SER          
SEQRES   5 A  340  ARG LEU TYR THR ALA CYS VAL TYR HIS LYS LEU PHE ASP          
SEQRES   6 A  340  ALA SER ASP SER SER SER TYR LYS HIS ASN GLY THR GLU          
SEQRES   7 A  340  LEU THR LEU ARG TYR SER THR GLY THR VAL SER GLY PHE          
SEQRES   8 A  340  LEU SER GLN ASP ILE ILE THR VAL GLY GLY ILE THR VAL          
SEQRES   9 A  340  THR GLN MET PHE GLY GLU VAL THR GLU MET PRO ALA LEU          
SEQRES  10 A  340  PRO PHE MET LEU ALA GLU PHE ASP GLY VAL VAL GLY MET          
SEQRES  11 A  340  GLY PHE ILE GLU GLN ALA ILE GLY ARG VAL THR PRO ILE          
SEQRES  12 A  340  PHE ASP ASN ILE ILE SER GLN GLY VAL LEU LYS GLU ASP          
SEQRES  13 A  340  VAL PHE SER PHE TYR TYR ASN ARG ASP SER GLU ASN SER          
SEQRES  14 A  340  GLN SER LEU GLY GLY GLN ILE VAL LEU GLY GLY SER ASP          
SEQRES  15 A  340  PRO GLN HIS TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU          
SEQRES  16 A  340  ILE LYS THR GLY VAL TRP GLN ILE GLN MET LYS GLY VAL          
SEQRES  17 A  340  SER VAL GLY SER SER THR LEU LEU CYS GLU ASP GLY CYS          
SEQRES  18 A  340  LEU ALA LEU VAL ASP THR GLY ALA SER TYR ILE SER GLY          
SEQRES  19 A  340  SER THR SER SER ILE GLU LYS LEU MET GLU ALA LEU GLY          
SEQRES  20 A  340  ALA LYS LYS ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN          
SEQRES  21 A  340  GLU GLY PRO THR LEU PRO ASP ILE SER PHE HIS LEU GLY          
SEQRES  22 A  340  GLY LYS GLU TYR THR LEU THR SER ALA ASP TYR VAL PHE          
SEQRES  23 A  340  GLN GLU SER TYR SER SER LYS LYS LEU CYS THR LEU ALA          
SEQRES  24 A  340  ILE HIS ALA MET ASP ILE PRO PRO PRO THR GLY PRO THR          
SEQRES  25 A  340  TRP ALA LEU GLY ALA THR PHE ILE ARG LYS PHE TYR THR          
SEQRES  26 A  340  GLU PHE ASP ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU          
SEQRES  27 A  340  ALA ARG                                                      
SEQRES   1 B  340  LEU THR LEU GLY ASN THR THR SER SER VAL ILE LEU THR          
SEQRES   2 B  340  ASN TYR MET ASP THR GLN TYR TYR GLY GLU ILE GLY ILE          
SEQRES   3 B  340  GLY THR PRO PRO GLN THR PHE LYS VAL VAL PHE ASP THR          
SEQRES   4 B  340  GLY SER SER ASN VAL TRP VAL PRO SER SER LYS CYS SER          
SEQRES   5 B  340  ARG LEU TYR THR ALA CYS VAL TYR HIS LYS LEU PHE ASP          
SEQRES   6 B  340  ALA SER ASP SER SER SER TYR LYS HIS ASN GLY THR GLU          
SEQRES   7 B  340  LEU THR LEU ARG TYR SER THR GLY THR VAL SER GLY PHE          
SEQRES   8 B  340  LEU SER GLN ASP ILE ILE THR VAL GLY GLY ILE THR VAL          
SEQRES   9 B  340  THR GLN MET PHE GLY GLU VAL THR GLU MET PRO ALA LEU          
SEQRES  10 B  340  PRO PHE MET LEU ALA GLU PHE ASP GLY VAL VAL GLY MET          
SEQRES  11 B  340  GLY PHE ILE GLU GLN ALA ILE GLY ARG VAL THR PRO ILE          
SEQRES  12 B  340  PHE ASP ASN ILE ILE SER GLN GLY VAL LEU LYS GLU ASP          
SEQRES  13 B  340  VAL PHE SER PHE TYR TYR ASN ARG ASP SER GLU ASN SER          
SEQRES  14 B  340  GLN SER LEU GLY GLY GLN ILE VAL LEU GLY GLY SER ASP          
SEQRES  15 B  340  PRO GLN HIS TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU          
SEQRES  16 B  340  ILE LYS THR GLY VAL TRP GLN ILE GLN MET LYS GLY VAL          
SEQRES  17 B  340  SER VAL GLY SER SER THR LEU LEU CYS GLU ASP GLY CYS          
SEQRES  18 B  340  LEU ALA LEU VAL ASP THR GLY ALA SER TYR ILE SER GLY          
SEQRES  19 B  340  SER THR SER SER ILE GLU LYS LEU MET GLU ALA LEU GLY          
SEQRES  20 B  340  ALA LYS LYS ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN          
SEQRES  21 B  340  GLU GLY PRO THR LEU PRO ASP ILE SER PHE HIS LEU GLY          
SEQRES  22 B  340  GLY LYS GLU TYR THR LEU THR SER ALA ASP TYR VAL PHE          
SEQRES  23 B  340  GLN GLU SER TYR SER SER LYS LYS LEU CYS THR LEU ALA          
SEQRES  24 B  340  ILE HIS ALA MET ASP ILE PRO PRO PRO THR GLY PRO THR          
SEQRES  25 B  340  TRP ALA LEU GLY ALA THR PHE ILE ARG LYS PHE TYR THR          
SEQRES  26 B  340  GLU PHE ASP ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU          
SEQRES  27 B  340  ALA ARG                                                      
HET    LIX  A 401      44                                                       
HET    CIT  A 501      13                                                       
HET    LIX  B 402      44                                                       
HETNAM     LIX N-[2-({2-AMINO-6-ETHYL-5-[4-(3-METHOXYPROPYL)-2,2-               
HETNAM   2 LIX  DIMETHYL-3-OXO-3,4-DIHYDRO-2H-1,4-BENZOXAZIN-6-                 
HETNAM   3 LIX  YL]PYRIMIDIN-4-YL}AMINO)ETHYL]NAPHTHALENE-2-                    
HETNAM   4 LIX  SULFONAMIDE                                                     
HETNAM     CIT CITRIC ACID                                                      
FORMUL   3  LIX    2(C32 H38 N6 O5 S)                                           
FORMUL   4  CIT    C6 H8 O7                                                     
FORMUL   6  HOH   *242(H2 O)                                                    
HELIX    1   1 TYR A   50  TYR A   55  1                                   6    
HELIX    2   2 ASP A   60  SER A   64  5                                   5    
HELIX    3   3 PRO A  110  MET A  115  1                                   6    
HELIX    4   4 PHE A  127  VAL A  135  5                                   9    
HELIX    5   5 PRO A  137  SER A  144  1                                   8    
HELIX    6   6 ASP A  177  GLN A  179  5                                   3    
HELIX    7   7 SER A  230  GLY A  242  1                                  13    
HELIX    8   8 GLU A  256  LEU A  260  5                                   5    
HELIX    9   9 THR A  275  VAL A  280  1                                   6    
HELIX   10  10 GLY A  311  ARG A  316  1                                   6    
HELIX   11  11 TYR B   50  TYR B   55  1                                   6    
HELIX   12  12 ASP B   60  SER B   64  5                                   5    
HELIX   13  13 PRO B  110  MET B  115  1                                   6    
HELIX   14  14 PHE B  127  VAL B  135  5                                   9    
HELIX   15  15 PRO B  137  GLN B  145  1                                   9    
HELIX   16  16 ASP B  177  TYR B  181  5                                   5    
HELIX   17  17 SER B  230  GLY B  242  1                                  13    
HELIX   18  18 ASN B  255  LEU B  260  5                                   6    
HELIX   19  19 THR B  275  VAL B  280  1                                   6    
HELIX   20  20 GLY B  311  LYS B  317  1                                   7    
SHEET    1   A 9 LYS A  68  TYR A  78  0                                        
SHEET    2   A 9 GLY A  81  VAL A  94 -1  O  VAL A  83   N  LEU A  76           
SHEET    3   A 9 GLN A  14  ILE A  21 -1  N  GLY A  20   O  THR A  93           
SHEET    4   A 9 SER A   3  TYR A  10 -1  N  THR A   8   O  TYR A  16           
SHEET    5   A 9 GLY A 169  LEU A 173 -1  O  LEU A 173   N  SER A   3           
SHEET    6   A 9 VAL A 152  TYR A 157 -1  N  TYR A 156   O  GLN A 170           
SHEET    7   A 9 PHE A 318  ASP A 323 -1  O  PHE A 322   N  PHE A 153           
SHEET    8   A 9 ARG A 328  ALA A 334 -1  O  GLY A 330   N  GLU A 321           
SHEET    9   A 9 TYR A 181  ASN A 189 -1  N  ILE A 188   O  ILE A 329           
SHEET    1   B13 LYS A  68  TYR A  78  0                                        
SHEET    2   B13 GLY A  81  VAL A  94 -1  O  VAL A  83   N  LEU A  76           
SHEET    3   B13 ILE A  97  GLU A 108 -1  O  GLU A 105   N  PHE A  86           
SHEET    4   B13 VAL A  39  PRO A  42  1  N  VAL A  39   O  GLY A 104           
SHEET    5   B13 GLY A 121  GLY A 124 -1  O  VAL A 122   N  TRP A  40           
SHEET    6   B13 GLN A  26  ASP A  33  1  N  VAL A  31   O  VAL A 123           
SHEET    7   B13 GLN A  14  ILE A  21 -1  N  ILE A  21   O  GLN A  26           
SHEET    8   B13 SER A   3  TYR A  10 -1  N  THR A   8   O  TYR A  16           
SHEET    9   B13 GLY A 169  LEU A 173 -1  O  LEU A 173   N  SER A   3           
SHEET   10   B13 VAL A 152  TYR A 157 -1  N  TYR A 156   O  GLN A 170           
SHEET   11   B13 PHE A 318  ASP A 323 -1  O  PHE A 322   N  PHE A 153           
SHEET   12   B13 ARG A 328  ALA A 334 -1  O  GLY A 330   N  GLU A 321           
SHEET   13   B13 TYR A 181  ASN A 189 -1  N  ILE A 188   O  ILE A 329           
SHEET    1   C 5 GLN A 197  MET A 200  0                                        
SHEET    2   C 5 CYS A 216  VAL A 220 -1  O  CYS A 216   N  MET A 200           
SHEET    3   C 5 TRP A 308  LEU A 310  1  O  LEU A 310   N  LEU A 219           
SHEET    4   C 5 ILE A 227  GLY A 229 -1  N  SER A 228   O  ALA A 309           
SHEET    5   C 5 ILE A 295  ALA A 297  1  O  HIS A 296   N  ILE A 227           
SHEET    1   D 3 GLY A 202  VAL A 205  0                                        
SHEET    2   D 3 ILE A 263  LEU A 267 -1  O  HIS A 266   N  GLY A 202           
SHEET    3   D 3 LYS A 270  LEU A 274 -1  O  LEU A 274   N  ILE A 263           
SHEET    1   E 3 LYS A 244  LYS A 245  0                                        
SHEET    2   E 3 TYR A 250  LYS A 253 -1  O  VAL A 251   N  LYS A 244           
SHEET    3   E 3 LEU A 290  THR A 292 -1  O  CYS A 291   N  VAL A 252           
SHEET    1   F 9 LYS B  68  ARG B  77  0                                        
SHEET    2   F 9 THR B  82  VAL B  94 -1  O  VAL B  83   N  LEU B  76           
SHEET    3   F 9 GLN B  14  ILE B  21 -1  N  GLY B  20   O  THR B  93           
SHEET    4   F 9 SER B   3  TYR B  10 -1  N  THR B   8   O  TYR B  16           
SHEET    5   F 9 GLY B 169  LEU B 173 -1  O  LEU B 173   N  SER B   3           
SHEET    6   F 9 VAL B 152  TYR B 157 -1  N  TYR B 156   O  GLN B 170           
SHEET    7   F 9 PHE B 318  ASP B 323 -1  O  PHE B 322   N  PHE B 153           
SHEET    8   F 9 ARG B 328  LEU B 333 -1  O  GLY B 330   N  GLU B 321           
SHEET    9   F 9 GLU B 182  ASN B 189 -1  N  ILE B 188   O  ILE B 329           
SHEET    1   G13 LYS B  68  ARG B  77  0                                        
SHEET    2   G13 THR B  82  VAL B  94 -1  O  VAL B  83   N  LEU B  76           
SHEET    3   G13 ILE B  97  GLU B 108 -1  O  GLU B 105   N  PHE B  86           
SHEET    4   G13 VAL B  39  PRO B  42  1  N  VAL B  39   O  GLY B 104           
SHEET    5   G13 GLY B 121  GLY B 124 -1  O  VAL B 122   N  TRP B  40           
SHEET    6   G13 GLN B  26  ASP B  33  1  N  VAL B  31   O  VAL B 123           
SHEET    7   G13 GLN B  14  ILE B  21 -1  N  ILE B  21   O  GLN B  26           
SHEET    8   G13 SER B   3  TYR B  10 -1  N  THR B   8   O  TYR B  16           
SHEET    9   G13 GLY B 169  LEU B 173 -1  O  LEU B 173   N  SER B   3           
SHEET   10   G13 VAL B 152  TYR B 157 -1  N  TYR B 156   O  GLN B 170           
SHEET   11   G13 PHE B 318  ASP B 323 -1  O  PHE B 322   N  PHE B 153           
SHEET   12   G13 ARG B 328  LEU B 333 -1  O  GLY B 330   N  GLU B 321           
SHEET   13   G13 GLU B 182  ASN B 189 -1  N  ILE B 188   O  ILE B 329           
SHEET    1   H 5 GLN B 197  MET B 200  0                                        
SHEET    2   H 5 CYS B 216  VAL B 220 -1  O  CYS B 216   N  MET B 200           
SHEET    3   H 5 TRP B 308  LEU B 310  1  O  LEU B 310   N  LEU B 219           
SHEET    4   H 5 ILE B 227  GLY B 229 -1  N  SER B 228   O  ALA B 309           
SHEET    5   H 5 ILE B 295  ALA B 297  1  O  HIS B 296   N  ILE B 227           
SHEET    1   I 3 VAL B 203  VAL B 205  0                                        
SHEET    2   I 3 ILE B 263  LEU B 267 -1  O  SER B 264   N  SER B 204           
SHEET    3   I 3 LYS B 270  LEU B 274 -1  O  LEU B 274   N  ILE B 263           
SHEET    1   J 3 LYS B 244  LYS B 245  0                                        
SHEET    2   J 3 TYR B 250  LYS B 253 -1  O  VAL B 251   N  LYS B 244           
SHEET    3   J 3 LEU B 290  THR B 292 -1  O  CYS B 291   N  VAL B 252           
SSBOND   1 CYS A   46    CYS A   53                          1555   1555  2.02  
SSBOND   2 CYS A  212    CYS A  216                          1555   1555  2.04  
SSBOND   3 CYS A  254    CYS A  291                          1555   1555  2.03  
SSBOND   4 CYS B   46    CYS B   53                          1555   1555  2.03  
SSBOND   5 CYS B  212    CYS B  216                          1555   1555  2.04  
SSBOND   6 CYS B  254    CYS B  291                          1555   1555  2.05  
CISPEP   1 THR A   23    PRO A   24          0        -5.90                     
CISPEP   2 LEU A  112    PRO A  113          0         3.90                     
CISPEP   3 PRO A  302    PRO A  303          0         6.70                     
CISPEP   4 GLY A  305    PRO A  306          0        -4.83                     
CISPEP   5 THR B   23    PRO B   24          0         0.39                     
CISPEP   6 LEU B  112    PRO B  113          0        -0.30                     
CISPEP   7 PRO B  302    PRO B  303          0        10.42                     
CISPEP   8 GLY B  305    PRO B  306          0        -4.67                     
SITE     1 AC1 19 THR A  13  GLN A  14  TYR A  15  VAL A  31                    
SITE     2 AC1 19 ASP A  33  GLY A  35  TYR A  78  SER A  79                    
SITE     3 AC1 19 THR A  80  PRO A 113  LEU A 116  VAL A 122                    
SITE     4 AC1 19 ASP A 221  THR A 222  GLY A 223  SER A 225                    
SITE     5 AC1 19 PHE A 248  HOH A 504  HOH A 608                               
SITE     1 AC2 19 THR B  13  GLN B  14  TYR B  15  VAL B  31                    
SITE     2 AC2 19 ASP B  33  GLY B  35  TYR B  78  SER B  79                    
SITE     3 AC2 19 THR B  80  ASP B 221  THR B 222  GLY B 223                    
SITE     4 AC2 19 ALA B 224  SER B 225  TYR B 226  HIS B 296                    
SITE     5 AC2 19 ALA B 297  MET B 298  HOH B 475                               
SITE     1 AC3  1 LEU A 116                                                     
CRYST1  141.533  141.533  141.533  90.00  90.00  90.00 P 21 3       24          
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      0.007065  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007065  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007065        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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