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Database: PDB
Entry: 5KOQ
LinkDB: 5KOQ
Original site: 5KOQ 
HEADER    HYDROLASE/HYDROLASE INHIBITOR           01-JUL-16   5KOQ              
TITLE     DISCOVERY OF TAK-272: A NOVEL, POTENT AND ORALLY ACTIVE RENIN IN-     
TITLE    2 HIBITOR                                                              
CAVEAT     5KOQ    NAG B 401 HAS WRONG CHIRALITY AT ATOM C1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RENIN;                                                     
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 70-406;                                       
COMPND   5 SYNONYM: ANGIOTENSINOGENASE;                                         
COMPND   6 EC: 3.4.23.15;                                                       
COMPND   7 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: REN;                                                           
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HEK 293                                 
KEYWDS    PROTEIN-INHIBITOR COMPLEX, HYDROLASE-HYDROLASE INHIBITOR COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.P.SNELL,C.A.BEHNKE,K.OKADA,O.HIDEYUKI,B.-C.SANG,W.LANE              
REVDAT   4   29-JUL-20 5KOQ    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   16-NOV-16 5KOQ    1       JRNL                                     
REVDAT   2   09-NOV-16 5KOQ    1       JRNL                                     
REVDAT   1   02-NOV-16 5KOQ    0                                                
JRNL        AUTH   Y.IMAEDA,M.TAWADA,S.SUZUKI,M.TOMIMOTO,M.KONDO,N.TARUI,       
JRNL        AUTH 2 T.SANADA,R.KANAGAWA,G.SNELL,C.A.BEHNKE,K.KUBO,T.KUROITA      
JRNL        TITL   STRUCTURE-BASED DESIGN OF A NEW SERIES OF                    
JRNL        TITL 2 N-(PIPERIDIN-3-YL)PYRIMIDINE-5-CARBOXAMIDES AS RENIN         
JRNL        TITL 3 INHIBITORS.                                                  
JRNL        REF    BIOORG.MED.CHEM.              V.  24  5771 2016              
JRNL        REFN                   ESSN 1464-3391                               
JRNL        PMID   27687967                                                     
JRNL        DOI    10.1016/J.BMC.2016.09.030                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   Y.IMAEDA,H.TOKUHARA,Y.FUKASE,R.KANAGAWA,Y.KAJIMOTO,          
REMARK   1  AUTH 2 K.KUSUMOTO,M.KONDO,G.SNELL,C.A.BEHNKE,T.KUROITA              
REMARK   1  TITL   DISCOVERY OF TAK-272: A NOVEL, POTENT, AND ORALLY ACTIVE     
REMARK   1  TITL 2 RENIN INHIBITOR.                                             
REMARK   1  REF    ACS MED.CHEM.LETT.            V.   7   933 2016              
REMARK   1  REFN                   ISSN 1948-5875                               
REMARK   1  PMID   27774132                                                     
REMARK   1  DOI    10.1021/ACSMEDCHEMLETT.6B00251                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0135                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 23173                          
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) : 0.206                           
REMARK   3   R VALUE            (WORKING SET) : 0.204                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1244                            
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1710                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.50                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2800                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 88                           
REMARK   3   BIN FREE R VALUE                    : 0.3500                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5062                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 95                                      
REMARK   3   SOLVENT ATOMS            : 87                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.868         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.330         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.255         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.441        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.945                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.909                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5284 ; 0.008 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7182 ; 1.272 ; 1.965       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   664 ; 6.843 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   212 ;35.837 ;24.245       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   794 ;15.466 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    17 ;12.963 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   810 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3958 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2668 ; 0.948 ; 4.564       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3328 ; 1.663 ; 6.845       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2616 ; 1.007 ; 4.637       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 10                                   
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     5        A    78                          
REMARK   3    RESIDUE RANGE :   A    79        A    91                          
REMARK   3    RESIDUE RANGE :   A    92        A   154                          
REMARK   3    RESIDUE RANGE :   A   155        A   248                          
REMARK   3    RESIDUE RANGE :   A   249        A   265                          
REMARK   3    RESIDUE RANGE :   A   266        A   280                          
REMARK   3    RESIDUE RANGE :   A   281        A   298                          
REMARK   3    RESIDUE RANGE :   A   299        A   302                          
REMARK   3    RESIDUE RANGE :   A   303        A   312                          
REMARK   3    RESIDUE RANGE :   A   313        A   340                          
REMARK   3    ORIGIN FOR THE GROUP (A): -40.4103   3.6437  11.1455              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0827 T22:   0.1115                                     
REMARK   3      T33:   0.0416 T12:  -0.0288                                     
REMARK   3      T13:   0.0174 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5579 L22:   2.1718                                     
REMARK   3      L33:   1.0379 L12:  -1.7515                                     
REMARK   3      L13:   0.5688 L23:  -0.4553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2323 S12:   0.3019 S13:   0.0516                       
REMARK   3      S21:  -0.1464 S22:  -0.2071 S23:  -0.2396                       
REMARK   3      S31:  -0.0300 S32:   0.3065 S33:  -0.0253                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 10                                   
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     4        B    78                          
REMARK   3    RESIDUE RANGE :   B    79        B    91                          
REMARK   3    RESIDUE RANGE :   B    92        B   154                          
REMARK   3    RESIDUE RANGE :   B   155        B   248                          
REMARK   3    RESIDUE RANGE :   B   249        B   265                          
REMARK   3    RESIDUE RANGE :   B   266        B   280                          
REMARK   3    RESIDUE RANGE :   B   281        B   298                          
REMARK   3    RESIDUE RANGE :   B   299        B   302                          
REMARK   3    RESIDUE RANGE :   B   303        B   312                          
REMARK   3    RESIDUE RANGE :   B   313        B   340                          
REMARK   3    ORIGIN FOR THE GROUP (A): -17.1994 -12.4726  34.0571              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0361 T22:   0.1440                                     
REMARK   3      T33:   0.1382 T12:   0.0267                                     
REMARK   3      T13:  -0.0353 T23:  -0.0815                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9321 L22:   2.9053                                     
REMARK   3      L33:   3.0385 L12:   1.4714                                     
REMARK   3      L13:  -0.4448 L23:  -0.6123                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0056 S12:   0.1624 S13:  -0.3420                       
REMARK   3      S21:  -0.1001 S22:   0.0340 S23:  -0.2871                       
REMARK   3      S31:   0.2492 S32:   0.1791 S33:  -0.0396                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
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: U VALUES : WITH TLS ADDED                 
REMARK   4                                                                      
REMARK   4 5KOQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000222510.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-FEB-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.3                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4R                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 24640                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72100                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 23% PEG600, 100 MM CITRIC ACID, PH       
REMARK 280  7.6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
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       69.28100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       69.28100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       69.28100            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       69.28100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       69.28100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       69.28100            
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       69.28100            
REMARK 290   SMTRY2   6 -1.000000  0.000000  0.000000       69.28100            
REMARK 290   SMTRY3   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  0.000000 -1.000000       69.28100            
REMARK 290   SMTRY2   7 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  1.000000  0.000000       69.28100            
REMARK 290   SMTRY1   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY2   8  1.000000  0.000000  0.000000       69.28100            
REMARK 290   SMTRY3   8  0.000000 -1.000000  0.000000       69.28100            
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       69.28100            
REMARK 290   SMTRY3  10 -1.000000  0.000000  0.000000       69.28100            
REMARK 290   SMTRY1  11  0.000000  1.000000  0.000000       69.28100            
REMARK 290   SMTRY2  11  0.000000  0.000000 -1.000000       69.28100            
REMARK 290   SMTRY3  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY1  12  0.000000 -1.000000  0.000000       69.28100            
REMARK 290   SMTRY2  12  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY3  12  1.000000  0.000000  0.000000       69.28100            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 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 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 16580 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 70840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 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      -69.28100            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000      -69.28100            
REMARK 350   BIOMT3   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      -69.28100            
REMARK 350   BIOMT2   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3   3  1.000000  0.000000  0.000000       69.28100            
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     GLY A     4                                                      
REMARK 465     SER A   212                                                      
REMARK 465     TYR B    83                                                      
REMARK 465     SER B    84                                                      
REMARK 465     THR B    85                                                      
REMARK 465     GLY B    86                                                      
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     ASN A   5    CG   OD1  ND2                                       
REMARK 470     ARG A 139    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 154    CG   CD   CE   NZ                                   
REMARK 470     GLN A 170    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 184    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 204    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 206    CG   CD   CE   NZ                                   
REMARK 470     LYS A 241    CG   CD   CE   NZ                                   
REMARK 470     GLU A 244    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 249    CG   CD   CE   NZ                                   
REMARK 470     LYS A 258    CG   CD   CE   NZ                                   
REMARK 470     GLU A 288    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  73    CG   CD   CE   NZ                                   
REMARK 470     LEU B  79    CG   CD1  CD2                                       
REMARK 470     ARG B  82    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 139    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B 170    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 241    CG   CD   CE   NZ                                   
REMARK 470     LYS B 249    CG   CD   CE   NZ                                   
REMARK 470     LYS B 250    CG   CD   CE   NZ                                   
REMARK 470     PHE B 253    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 275    CG   CD   CE   NZ                                   
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  75      -65.31   -135.21                                   
REMARK 500    ARG A 251     -169.53   -121.70                                   
REMARK 500    GLN A 287       73.96    -69.11                                   
REMARK 500    ALA A 299       34.61    -87.25                                   
REMARK 500    ASN B  75      -63.52   -135.20                                   
REMARK 500    ARG B 251      -89.87    -65.23                                   
REMARK 500    LEU B 252       -9.96   -145.23                                   
REMARK 500    PHE B 253      -51.12   -135.15                                   
REMARK 500    ALA B 299       32.94    -85.77                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5KOS   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5KOT   RELATED DB: PDB                                   
DBREF  5KOQ A    4   340  UNP    P00797   RENI_HUMAN      70    406             
DBREF  5KOQ B    4   340  UNP    P00797   RENI_HUMAN      70    406             
SEQRES   1 A  337  GLY ASN THR THR SER SER VAL ILE LEU THR ASN TYR MET          
SEQRES   2 A  337  ASP THR GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO          
SEQRES   3 A  337  PRO GLN THR PHE LYS VAL VAL PHE ASP THR GLY SER SER          
SEQRES   4 A  337  ASN VAL TRP VAL PRO SER SER LYS CYS SER ARG LEU TYR          
SEQRES   5 A  337  THR ALA CYS VAL TYR HIS LYS LEU PHE ASP ALA SER ASP          
SEQRES   6 A  337  SER SER SER TYR LYS HIS ASN GLY THR GLU LEU THR LEU          
SEQRES   7 A  337  ARG TYR SER THR GLY THR VAL SER GLY PHE LEU SER GLN          
SEQRES   8 A  337  ASP ILE ILE THR VAL GLY GLY ILE THR VAL THR GLN MET          
SEQRES   9 A  337  PHE GLY GLU VAL THR GLU MET PRO ALA LEU PRO PHE MET          
SEQRES  10 A  337  LEU ALA GLU PHE ASP GLY VAL VAL GLY MET GLY PHE ILE          
SEQRES  11 A  337  GLU GLN ALA ILE GLY ARG VAL THR PRO ILE PHE ASP ASN          
SEQRES  12 A  337  ILE ILE SER GLN GLY VAL LEU LYS GLU ASP VAL PHE SER          
SEQRES  13 A  337  PHE TYR TYR ASN ARG ASP SER GLU ASN SER GLN SER LEU          
SEQRES  14 A  337  GLY GLY GLN ILE VAL LEU GLY GLY SER ASP PRO GLN HIS          
SEQRES  15 A  337  TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU ILE LYS THR          
SEQRES  16 A  337  GLY VAL TRP GLN ILE GLN MET LYS GLY VAL SER VAL GLY          
SEQRES  17 A  337  SER SER THR LEU LEU CYS GLU ASP GLY CYS LEU ALA LEU          
SEQRES  18 A  337  VAL ASP THR GLY ALA SER TYR ILE SER GLY SER THR SER          
SEQRES  19 A  337  SER ILE GLU LYS LEU MET GLU ALA LEU GLY ALA LYS LYS          
SEQRES  20 A  337  ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN GLU GLY PRO          
SEQRES  21 A  337  THR LEU PRO ASP ILE SER PHE HIS LEU GLY GLY LYS GLU          
SEQRES  22 A  337  TYR THR LEU THR SER ALA ASP TYR VAL PHE GLN GLU SER          
SEQRES  23 A  337  TYR SER SER LYS LYS LEU CYS THR LEU ALA ILE HIS ALA          
SEQRES  24 A  337  MET ASP ILE PRO PRO PRO THR GLY PRO THR TRP ALA LEU          
SEQRES  25 A  337  GLY ALA THR PHE ILE ARG LYS PHE TYR THR GLU PHE ASP          
SEQRES  26 A  337  ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU ALA ARG              
SEQRES   1 B  337  GLY ASN THR THR SER SER VAL ILE LEU THR ASN TYR MET          
SEQRES   2 B  337  ASP THR GLN TYR TYR GLY GLU ILE GLY ILE GLY THR PRO          
SEQRES   3 B  337  PRO GLN THR PHE LYS VAL VAL PHE ASP THR GLY SER SER          
SEQRES   4 B  337  ASN VAL TRP VAL PRO SER SER LYS CYS SER ARG LEU TYR          
SEQRES   5 B  337  THR ALA CYS VAL TYR HIS LYS LEU PHE ASP ALA SER ASP          
SEQRES   6 B  337  SER SER SER TYR LYS HIS ASN GLY THR GLU LEU THR LEU          
SEQRES   7 B  337  ARG TYR SER THR GLY THR VAL SER GLY PHE LEU SER GLN          
SEQRES   8 B  337  ASP ILE ILE THR VAL GLY GLY ILE THR VAL THR GLN MET          
SEQRES   9 B  337  PHE GLY GLU VAL THR GLU MET PRO ALA LEU PRO PHE MET          
SEQRES  10 B  337  LEU ALA GLU PHE ASP GLY VAL VAL GLY MET GLY PHE ILE          
SEQRES  11 B  337  GLU GLN ALA ILE GLY ARG VAL THR PRO ILE PHE ASP ASN          
SEQRES  12 B  337  ILE ILE SER GLN GLY VAL LEU LYS GLU ASP VAL PHE SER          
SEQRES  13 B  337  PHE TYR TYR ASN ARG ASP SER GLU ASN SER GLN SER LEU          
SEQRES  14 B  337  GLY GLY GLN ILE VAL LEU GLY GLY SER ASP PRO GLN HIS          
SEQRES  15 B  337  TYR GLU GLY ASN PHE HIS TYR ILE ASN LEU ILE LYS THR          
SEQRES  16 B  337  GLY VAL TRP GLN ILE GLN MET LYS GLY VAL SER VAL GLY          
SEQRES  17 B  337  SER SER THR LEU LEU CYS GLU ASP GLY CYS LEU ALA LEU          
SEQRES  18 B  337  VAL ASP THR GLY ALA SER TYR ILE SER GLY SER THR SER          
SEQRES  19 B  337  SER ILE GLU LYS LEU MET GLU ALA LEU GLY ALA LYS LYS          
SEQRES  20 B  337  ARG LEU PHE ASP TYR VAL VAL LYS CYS ASN GLU GLY PRO          
SEQRES  21 B  337  THR LEU PRO ASP ILE SER PHE HIS LEU GLY GLY LYS GLU          
SEQRES  22 B  337  TYR THR LEU THR SER ALA ASP TYR VAL PHE GLN GLU SER          
SEQRES  23 B  337  TYR SER SER LYS LYS LEU CYS THR LEU ALA ILE HIS ALA          
SEQRES  24 B  337  MET ASP ILE PRO PRO PRO THR GLY PRO THR TRP ALA LEU          
SEQRES  25 B  337  GLY ALA THR PHE ILE ARG LYS PHE TYR THR GLU PHE ASP          
SEQRES  26 B  337  ARG ARG ASN ASN ARG ILE GLY PHE ALA LEU ALA ARG              
HET    NAG  A 401      14                                                       
HET    6VR  A 402      30                                                       
HET    NAG  B 401      14                                                       
HET    6VR  B 402      30                                                       
HET    PEG  B 403       7                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     6VR 2-~{TERT}-BUTYL-4-(FURAN-2-YLMETHYLAMINO)-~{N}-(2-               
HETNAM   2 6VR  METHYLPROPYL)-~{N}-[(3~{S})-PIPERIDIN-3-YL]PYRIMIDINE-          
HETNAM   3 6VR  5-CARBOXAMIDE                                                   
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
FORMUL   3  NAG    2(C8 H15 N O6)                                               
FORMUL   4  6VR    2(C23 H35 N5 O2)                                             
FORMUL   7  PEG    C4 H10 O3                                                    
FORMUL   8  HOH   *87(H2 O)                                                     
HELIX    1 AA1 TYR A   55  HIS A   61  1                                   7    
HELIX    2 AA2 ASP A   65  SER A   69  5                                   5    
HELIX    3 AA3 PRO A  115  MET A  120  1                                   6    
HELIX    4 AA4 PHE A  132  VAL A  140  5                                   9    
HELIX    5 AA5 PRO A  142  GLY A  151  1                                  10    
HELIX    6 AA6 SER A  235  GLY A  247  1                                  13    
HELIX    7 AA7 ASN A  260  LEU A  265  5                                   6    
HELIX    8 AA8 THR A  280  VAL A  285  1                                   6    
HELIX    9 AA9 GLY A  316  LYS A  322  1                                   7    
HELIX   10 AB1 TYR B   55  TYR B   60  1                                   6    
HELIX   11 AB2 ASP B   65  SER B   69  5                                   5    
HELIX   12 AB3 PRO B  115  MET B  120  1                                   6    
HELIX   13 AB4 PHE B  132  VAL B  140  5                                   9    
HELIX   14 AB5 PRO B  142  GLY B  151  1                                  10    
HELIX   15 AB6 ASP B  182  GLN B  184  5                                   3    
HELIX   16 AB7 SER B  235  GLY B  247  1                                  13    
HELIX   17 AB8 GLU B  261  LEU B  265  5                                   5    
HELIX   18 AB9 THR B  280  VAL B  285  1                                   6    
HELIX   19 AC1 GLY B  316  LYS B  322  1                                   7    
SHEET    1 AA1 9 LYS A  73  TYR A  83  0                                        
SHEET    2 AA1 9 GLY A  86  VAL A  99 -1  O  GLN A  94   N  LYS A  73           
SHEET    3 AA1 9 GLN A  19  ILE A  26 -1  N  GLY A  25   O  THR A  98           
SHEET    4 AA1 9 SER A   8  TYR A  15 -1  N  TYR A  15   O  GLN A  19           
SHEET    5 AA1 9 GLY A 174  LEU A 178 -1  O  LEU A 178   N  SER A   8           
SHEET    6 AA1 9 VAL A 157  TYR A 162 -1  N  TYR A 161   O  GLN A 175           
SHEET    7 AA1 9 PHE A 323  ASP A 328 -1  O  PHE A 327   N  PHE A 158           
SHEET    8 AA1 9 ARG A 333  ALA A 339 -1  O  GLY A 335   N  GLU A 326           
SHEET    9 AA1 9 TYR A 186  ASN A 194 -1  N  ILE A 193   O  ILE A 334           
SHEET    1 AA213 LYS A  73  TYR A  83  0                                        
SHEET    2 AA213 GLY A  86  VAL A  99 -1  O  GLN A  94   N  LYS A  73           
SHEET    3 AA213 ILE A 102  GLU A 113 -1  O  VAL A 104   N  ILE A  97           
SHEET    4 AA213 VAL A  44  PRO A  47  1  N  VAL A  44   O  GLY A 109           
SHEET    5 AA213 GLY A 126  GLY A 129 -1  O  VAL A 127   N  TRP A  45           
SHEET    6 AA213 GLN A  31  ASP A  38  1  N  VAL A  36   O  VAL A 128           
SHEET    7 AA213 GLN A  19  ILE A  26 -1  N  GLY A  22   O  VAL A  35           
SHEET    8 AA213 SER A   8  TYR A  15 -1  N  TYR A  15   O  GLN A  19           
SHEET    9 AA213 GLY A 174  LEU A 178 -1  O  LEU A 178   N  SER A   8           
SHEET   10 AA213 VAL A 157  TYR A 162 -1  N  TYR A 161   O  GLN A 175           
SHEET   11 AA213 PHE A 323  ASP A 328 -1  O  PHE A 327   N  PHE A 158           
SHEET   12 AA213 ARG A 333  ALA A 339 -1  O  GLY A 335   N  GLU A 326           
SHEET   13 AA213 TYR A 186  ASN A 194 -1  N  ILE A 193   O  ILE A 334           
SHEET    1 AA3 4 THR A 214  LEU A 216  0                                        
SHEET    2 AA3 4 GLN A 202  VAL A 210 -1  N  VAL A 208   O  LEU A 216           
SHEET    3 AA3 4 ILE A 268  LEU A 272 -1  O  HIS A 271   N  GLY A 207           
SHEET    4 AA3 4 LYS A 275  LEU A 279 -1  O  LEU A 279   N  ILE A 268           
SHEET    1 AA4 6 THR A 214  LEU A 216  0                                        
SHEET    2 AA4 6 GLN A 202  VAL A 210 -1  N  VAL A 208   O  LEU A 216           
SHEET    3 AA4 6 CYS A 221  VAL A 225 -1  O  ALA A 223   N  ILE A 203           
SHEET    4 AA4 6 TRP A 313  LEU A 315  1  O  TRP A 313   N  LEU A 224           
SHEET    5 AA4 6 ILE A 232  GLY A 234 -1  N  SER A 233   O  ALA A 314           
SHEET    6 AA4 6 ILE A 300  ALA A 302  1  O  HIS A 301   N  ILE A 232           
SHEET    1 AA5 3 LYS A 249  LYS A 250  0                                        
SHEET    2 AA5 3 TYR A 255  LYS A 258 -1  O  VAL A 256   N  LYS A 249           
SHEET    3 AA5 3 LEU A 295  THR A 297 -1  O  CYS A 296   N  VAL A 257           
SHEET    1 AA6 9 LYS B  73  LEU B  81  0                                        
SHEET    2 AA6 9 VAL B  88  VAL B  99 -1  O  LEU B  92   N  GLY B  76           
SHEET    3 AA6 9 GLN B  19  ILE B  26 -1  N  GLY B  25   O  THR B  98           
SHEET    4 AA6 9 SER B   8  TYR B  15 -1  N  TYR B  15   O  GLN B  19           
SHEET    5 AA6 9 GLY B 174  LEU B 178 -1  O  LEU B 178   N  SER B   8           
SHEET    6 AA6 9 VAL B 157  TYR B 162 -1  N  SER B 159   O  VAL B 177           
SHEET    7 AA6 9 PHE B 323  ASP B 328 -1  O  PHE B 327   N  PHE B 158           
SHEET    8 AA6 9 ARG B 333  ALA B 339 -1  O  GLY B 335   N  GLU B 326           
SHEET    9 AA6 9 TYR B 186  ASN B 194 -1  N  GLU B 187   O  LEU B 338           
SHEET    1 AA713 LYS B  73  LEU B  81  0                                        
SHEET    2 AA713 VAL B  88  VAL B  99 -1  O  LEU B  92   N  GLY B  76           
SHEET    3 AA713 ILE B 102  GLU B 113 -1  O  GLU B 110   N  PHE B  91           
SHEET    4 AA713 VAL B  44  PRO B  47  1  N  VAL B  44   O  GLY B 109           
SHEET    5 AA713 GLY B 126  GLY B 129 -1  O  VAL B 127   N  TRP B  45           
SHEET    6 AA713 GLN B  31  ASP B  38  1  N  ASP B  38   O  VAL B 128           
SHEET    7 AA713 GLN B  19  ILE B  26 -1  N  GLY B  22   O  VAL B  35           
SHEET    8 AA713 SER B   8  TYR B  15 -1  N  TYR B  15   O  GLN B  19           
SHEET    9 AA713 GLY B 174  LEU B 178 -1  O  LEU B 178   N  SER B   8           
SHEET   10 AA713 VAL B 157  TYR B 162 -1  N  SER B 159   O  VAL B 177           
SHEET   11 AA713 PHE B 323  ASP B 328 -1  O  PHE B 327   N  PHE B 158           
SHEET   12 AA713 ARG B 333  ALA B 339 -1  O  GLY B 335   N  GLU B 326           
SHEET   13 AA713 TYR B 186  ASN B 194 -1  N  GLU B 187   O  LEU B 338           
SHEET    1 AA8 5 GLN B 202  MET B 205  0                                        
SHEET    2 AA8 5 CYS B 221  VAL B 225 -1  O  ALA B 223   N  ILE B 203           
SHEET    3 AA8 5 TRP B 313  LEU B 315  1  O  LEU B 315   N  LEU B 224           
SHEET    4 AA8 5 ILE B 232  GLY B 234 -1  N  SER B 233   O  ALA B 314           
SHEET    5 AA8 5 ILE B 300  ALA B 302  1  O  HIS B 301   N  ILE B 232           
SHEET    1 AA9 4 SER B 213  LEU B 216  0                                        
SHEET    2 AA9 4 VAL B 208  VAL B 210 -1  N  VAL B 208   O  LEU B 216           
SHEET    3 AA9 4 ILE B 268  LEU B 272 -1  O  SER B 269   N  SER B 209           
SHEET    4 AA9 4 LYS B 275  LEU B 279 -1  O  LEU B 279   N  ILE B 268           
SHEET    1 AB1 3 LYS B 249  LYS B 250  0                                        
SHEET    2 AB1 3 TYR B 255  LYS B 258 -1  O  VAL B 256   N  LYS B 249           
SHEET    3 AB1 3 LEU B 295  THR B 297 -1  O  CYS B 296   N  VAL B 257           
SSBOND   1 CYS A   51    CYS A   58                          1555   1555  2.03  
SSBOND   2 CYS A  217    CYS A  221                          1555   1555  2.03  
SSBOND   3 CYS A  259    CYS A  296                          1555   1555  2.03  
SSBOND   4 CYS B   51    CYS B   58                          1555   1555  2.03  
SSBOND   5 CYS B  217    CYS B  221                          1555   1555  2.02  
SSBOND   6 CYS B  259    CYS B  296                          1555   1555  2.03  
LINK         ND2 ASN A  75                 C1  NAG A 401     1555   1555  1.44  
LINK         ND2 ASN B  75                 C1  NAG B 401     1555   1555  1.45  
CISPEP   1 THR A   28    PRO A   29          0        -4.53                     
CISPEP   2 LEU A  117    PRO A  118          0        10.30                     
CISPEP   3 PRO A  307    PRO A  308          0         2.43                     
CISPEP   4 GLY A  310    PRO A  311          0        -3.09                     
CISPEP   5 THR B   28    PRO B   29          0        -0.15                     
CISPEP   6 LEU B  117    PRO B  118          0         6.82                     
CISPEP   7 PRO B  307    PRO B  308          0         0.48                     
CISPEP   8 GLY B  310    PRO B  311          0         3.76                     
CRYST1  138.562  138.562  138.562  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      0.007217  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007217  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007217        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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