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Database: PDB
Entry: 3SQO
LinkDB: 3SQO
Original site: 3SQO 
HEADER    HYDROLASE/IMMUNE SYSTEM                 05-JUL-11   3SQO              
TITLE     PCSK9 J16 FAB COMPLEX                                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROPROTEIN CONVERTASE SUBTILISIN/KEXIN TYPE 9;             
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: NEURAL APOPTOSIS-REGULATED CONVERTASE 1, NARC-1, PROPROTEIN 
COMPND   5 CONVERTASE 9, PC9, SUBTILISIN/KEXIN-LIKE PROTEASE PC9;               
COMPND   6 EC: 3.4.21.-;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: J16 HEAVY CHAIN;                                           
COMPND  10 CHAIN: H;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: J16 LIGHT CHAIN;                                           
COMPND  14 CHAIN: L;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: PCSK9 PRODOMAIN;                                           
COMPND  18 CHAIN: P;                                                            
COMPND  19 SYNONYM: NEURAL APOPTOSIS-REGULATED CONVERTASE 1, NARC-1, PROPROTEIN 
COMPND  20 CONVERTASE 9, PC9, SUBTILISIN/KEXIN-LIKE PROTEASE PC9;               
COMPND  21 EC: 3.4.21.-;                                                        
COMPND  22 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: PCSK9, NARC1, PSEC0052;                                        
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  15 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  16 MOL_ID: 3;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  18 ORGANISM_COMMON: HUMAN;                                              
SOURCE  19 ORGANISM_TAXID: 9606;                                                
SOURCE  20 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  22 EXPRESSION_SYSTEM_CELL_LINE: HEK293;                                 
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  25 ORGANISM_COMMON: HUMAN;                                              
SOURCE  26 ORGANISM_TAXID: 9606;                                                
SOURCE  27 GENE: PCSK9, NARC1, PSEC0052;                                        
SOURCE  28 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  30 EXPRESSION_SYSTEM_CELL_LINE: HEK293                                  
KEYWDS    CHOLESTEROL REGULATION, LDLR, HYDROLASE-IMMUNE SYSTEM COMPLEX         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.STROP                                                               
REVDAT   1   16-MAY-12 3SQO    0                                                
JRNL        AUTH   H.LIANG,J.CHAPARRO-RIGGERS,P.STROP,T.GENG,J.E.SUTTON,D.TSAI, 
JRNL        AUTH 2 L.BAI,Y.ABDICHE,J.DILLEY,J.YU,S.WU,S.M.CHIN,N.A.LEE,A.ROSSI, 
JRNL        AUTH 3 J.C.LIN,A.RAJPAL,J.PONS,D.L.SHELTON                          
JRNL        TITL   PROPROTEIN CONVERTASE SUBSTILISIN/KEXIN TYPE 9 ANTAGONISM    
JRNL        TITL 2 REDUCES LOW-DENSITY LIPOPROTEIN CHOLESTEROL IN               
JRNL        TITL 3 STATIN-TREATED HYPERCHOLESTEROLEMIC NONHUMAN PRIMATES.       
JRNL        REF    J.PHARMACOL.EXP.THER.         V. 340   228 2012              
JRNL        REFN                   ISSN 0022-3565                               
JRNL        PMID   22019884                                                     
JRNL        DOI    10.1124/JPET.111.187419                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 33325                          
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) : 0.226                           
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.283                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1721                            
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) : 1975                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 83.09                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3090                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 98                           
REMARK   3   BIN FREE R VALUE                    : 0.3750                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 7624                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 32                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.26000                                             
REMARK   3    B22 (A**2) : 0.15000                                              
REMARK   3    B33 (A**2) : -0.23000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.65000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.387         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.310         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 32.279        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.925                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.873                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7801 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  5261 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 10605 ; 1.062 ; 1.952       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 12773 ; 0.932 ; 3.005       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   995 ; 6.070 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   317 ;32.606 ;23.281       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1248 ;17.252 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    55 ;14.167 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1202 ; 0.058 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8717 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1564 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1559 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  5325 ; 0.189 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  3686 ; 0.172 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  4429 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   185 ; 0.131 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.016 ; 0.200       
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 ; 0.265 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    59 ; 0.195 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     5 ; 0.163 ; 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):  6377 ; 0.556 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2037 ; 0.074 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8047 ; 0.539 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3241 ; 0.939 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2558 ; 1.331 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 7                                          
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   153        A   449                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.8370 -20.6930 -13.1480              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1587 T22:  -0.4373                                     
REMARK   3      T33:  -0.2207 T12:   0.0357                                     
REMARK   3      T13:  -0.0849 T23:   0.0040                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2951 L22:   2.5116                                     
REMARK   3      L33:   2.8159 L12:   0.6907                                     
REMARK   3      L13:   0.7993 L23:   0.0681                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1261 S12:   0.2751 S13:   0.1157                       
REMARK   3      S21:  -0.1680 S22:   0.0849 S23:   0.0900                       
REMARK   3      S31:  -0.2561 S32:   0.0341 S33:   0.0412                       
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 :   A   453        A   659                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.2130 -31.6730  12.0050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0577 T22:  -0.1639                                     
REMARK   3      T33:  -0.1209 T12:   0.0770                                     
REMARK   3      T13:   0.0288 T23:   0.0445                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8482 L22:   5.9855                                     
REMARK   3      L33:   5.5415 L12:  -1.1627                                     
REMARK   3      L13:  -0.6233 L23:  -0.3236                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1474 S12:  -0.5405 S13:  -0.3143                       
REMARK   3      S21:   0.8210 S22:   0.1163 S23:   0.5030                       
REMARK   3      S31:   0.0305 S32:  -0.4332 S33:   0.0311                       
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 :   P    61        P   152                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.7960 -26.0430   5.2670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1335 T22:  -0.5249                                     
REMARK   3      T33:  -0.1751 T12:  -0.0173                                     
REMARK   3      T13:  -0.0998 T23:   0.0496                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9805 L22:   3.3998                                     
REMARK   3      L33:   4.4977 L12:   0.8498                                     
REMARK   3      L13:   2.9643 L23:   1.4566                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0170 S12:  -0.1861 S13:   0.0113                       
REMARK   3      S21:   0.2546 S22:   0.0004 S23:  -0.4128                       
REMARK   3      S31:  -0.0379 S32:   0.1028 S33:   0.0166                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L     4        L   105                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.5570 -20.6450 -48.6430              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0202 T22:  -0.2390                                     
REMARK   3      T33:  -0.2773 T12:   0.0470                                     
REMARK   3      T13:  -0.0133 T23:   0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6967 L22:   4.6140                                     
REMARK   3      L33:   8.2790 L12:   1.1251                                     
REMARK   3      L13:   3.1457 L23:   0.7441                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0153 S12:   0.3699 S13:  -0.0137                       
REMARK   3      S21:  -0.2475 S22:  -0.0795 S23:  -0.0398                       
REMARK   3      S31:   0.3515 S32:   0.3109 S33:   0.0641                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   L   106        L   214                          
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6630  -9.0980 -78.6240              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1927 T22:   0.0115                                     
REMARK   3      T33:  -0.1782 T12:   0.2156                                     
REMARK   3      T13:   0.0083 T23:  -0.0283                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7147 L22:   6.6438                                     
REMARK   3      L33:   8.2002 L12:  -1.1702                                     
REMARK   3      L13:   2.3891 L23:  -3.1581                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1281 S12:   0.2234 S13:   0.3364                       
REMARK   3      S21:  -0.5348 S22:  -0.2853 S23:  -0.3786                       
REMARK   3      S31:  -0.3573 S32:  -0.5924 S33:   0.1572                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H     4        H   110                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.1970   0.7270 -46.0660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2310 T22:  -0.1808                                     
REMARK   3      T33:   0.0197 T12:  -0.1304                                     
REMARK   3      T13:  -0.1504 T23:   0.0623                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1729 L22:   6.0379                                     
REMARK   3      L33:   7.2765 L12:   1.1876                                     
REMARK   3      L13:   1.3011 L23:  -3.7084                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3405 S12:   0.0416 S13:   0.4442                       
REMARK   3      S21:   0.1597 S22:   0.0133 S23:  -0.5247                       
REMARK   3      S31:  -1.1534 S32:   0.5318 S33:   0.3272                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   H   111        H   212                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.9730   1.9550 -66.3910              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4011 T22:   0.0148                                     
REMARK   3      T33:  -0.0806 T12:   0.3154                                     
REMARK   3      T13:  -0.1406 T23:  -0.0649                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.2187 L22:   8.1739                                     
REMARK   3      L33:   6.3897 L12:   5.1981                                     
REMARK   3      L13:   4.3506 L23:   0.1609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4303 S12:  -0.4611 S13:   0.5589                       
REMARK   3      S21:  -0.0921 S22:  -0.3394 S23:   0.5178                       
REMARK   3      S31:  -0.8667 S32:  -1.1647 S33:   0.7697                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 3SQO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066532.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 5.0.2                              
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                  : DOUBLE-CRYSTAL, SI(111)            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35342                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.7                               
REMARK 200  DATA REDUNDANCY                : 2.900                              
REMARK 200  R MERGE                    (I) : 0.11900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.47200                            
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: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 7% PEG 10000, 100 MM HEPES PH 7.2,       
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.49050            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, P                            
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 CHAINS A AND P ARE EXPRESSED AS A SINGLE CHAIN. THERE IS AN AUTO-    
REMARK 400 PROTEOLYSIS THAT CUTS THE CHAIN INTO TWO, BUT THE SECOND CHAIN       
REMARK 400 STAYS VERY TIGHTLY ASSOCIATED. IT HAS BEEN THE NOMENCLATURE OF THE   
REMARK 400 PREVIOUSLY PUBLISHED PCSK9 STRUCTURES TO HAVE CHAIN P AS THE PRO-    
REMARK 400 DOMAIN AND CHAIN A AS THE CATALYTIC DOMAIN                           
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     ASP A   169                                                      
REMARK 465     GLU A   170                                                      
REMARK 465     TYR A   171                                                      
REMARK 465     GLN A   172                                                      
REMARK 465     PRO A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     ASP A   175                                                      
REMARK 465     ASP A   212                                                      
REMARK 465     GLY A   213                                                      
REMARK 465     THR A   214                                                      
REMARK 465     ARG A   215                                                      
REMARK 465     PHE A   216                                                      
REMARK 465     HIS A   217                                                      
REMARK 465     ARG A   218                                                      
REMARK 465     ALA A   451                                                      
REMARK 465     GLY A   452                                                      
REMARK 465     THR A   573                                                      
REMARK 465     HIS A   574                                                      
REMARK 465     LYS A   575                                                      
REMARK 465     PRO A   576                                                      
REMARK 465     PRO A   577                                                      
REMARK 465     VAL A   578                                                      
REMARK 465     LEU A   579                                                      
REMARK 465     ARG A   580                                                      
REMARK 465     PRO A   581                                                      
REMARK 465     ARG A   582                                                      
REMARK 465     GLY A   583                                                      
REMARK 465     GLN A   584                                                      
REMARK 465     ASP A   660                                                      
REMARK 465     VAL A   661                                                      
REMARK 465     SER A   662                                                      
REMARK 465     THR A   663                                                      
REMARK 465     THR A   664                                                      
REMARK 465     GLY A   665                                                      
REMARK 465     SER A   666                                                      
REMARK 465     THR A   667                                                      
REMARK 465     SER A   668                                                      
REMARK 465     GLU A   669                                                      
REMARK 465     ARG A   682                                                      
REMARK 465     HIS A   683                                                      
REMARK 465     LEU A   684                                                      
REMARK 465     ALA A   685                                                      
REMARK 465     GLN A   686                                                      
REMARK 465     ALA A   687                                                      
REMARK 465     SER A   688                                                      
REMARK 465     GLN A   689                                                      
REMARK 465     GLU A   690                                                      
REMARK 465     LEU A   691                                                      
REMARK 465     GLN A   692                                                      
REMARK 465     SER H   119                                                      
REMARK 465     ARG H   133                                                      
REMARK 465     SER H   134                                                      
REMARK 465     THR H   135                                                      
REMARK 465     SER H   136                                                      
REMARK 465     GLU H   137                                                      
REMARK 465     SER H   138                                                      
REMARK 465     LYS H   218                                                      
REMARK 465     ASP L     1                                                      
REMARK 465     GLN P    31                                                      
REMARK 465     GLU P    32                                                      
REMARK 465     ASP P    33                                                      
REMARK 465     GLU P    34                                                      
REMARK 465     ASP P    35                                                      
REMARK 465     GLY P    36                                                      
REMARK 465     ASP P    37                                                      
REMARK 465     TYR P    38                                                      
REMARK 465     GLU P    39                                                      
REMARK 465     GLU P    40                                                      
REMARK 465     LEU P    41                                                      
REMARK 465     VAL P    42                                                      
REMARK 465     LEU P    43                                                      
REMARK 465     ALA P    44                                                      
REMARK 465     LEU P    45                                                      
REMARK 465     ARG P    46                                                      
REMARK 465     SER P    47                                                      
REMARK 465     GLU P    48                                                      
REMARK 465     GLU P    49                                                      
REMARK 465     ASP P    50                                                      
REMARK 465     GLY P    51                                                      
REMARK 465     LEU P    52                                                      
REMARK 465     ALA P    53                                                      
REMARK 465     GLU P    54                                                      
REMARK 465     ALA P    55                                                      
REMARK 465     PRO P    56                                                      
REMARK 465     GLU P    57                                                      
REMARK 465     HIS P    58                                                      
REMARK 465     GLY P    59                                                      
REMARK 465     THR P    60                                                      
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    ASP A 186     -139.35   -159.38                                   
REMARK 500    ASN A 207       87.77   -159.03                                   
REMARK 500    VAL A 280     -141.00   -114.20                                   
REMARK 500    ASN A 317       43.45   -106.14                                   
REMARK 500    PRO A 446     -175.00    -68.92                                   
REMARK 500    SER A 447     -101.72    -57.71                                   
REMARK 500    GLN A 531     -119.60    -63.49                                   
REMARK 500    ALA A 532     -168.89    176.44                                   
REMARK 500    ASN A 533       91.16     34.68                                   
REMARK 500    ALA A 542     -127.58   -102.72                                   
REMARK 500    ALA A 544      -81.29    -54.98                                   
REMARK 500    SER A 564      117.66   -163.47                                   
REMARK 500    PRO A 616      174.68    -48.42                                   
REMARK 500    ALA A 617      -74.74    -48.46                                   
REMARK 500    THR A 641     -166.59    -71.59                                   
REMARK 500    SER A 642      -62.43   -140.20                                   
REMARK 500    ASP A 651     -121.88     53.94                                   
REMARK 500    CYS H  22      113.83   -162.43                                   
REMARK 500    GLN H  43      -64.81   -164.20                                   
REMARK 500    ALA H 100       79.53    -10.75                                   
REMARK 500    SER H 100A      80.56     52.90                                   
REMARK 500    SER H 131       38.46   -145.91                                   
REMARK 500    ASP H 148       83.43     46.39                                   
REMARK 500    THR H 164      -46.85   -139.77                                   
REMARK 500    THR H 195       50.52   -144.87                                   
REMARK 500    ASN H 208       68.49     65.44                                   
REMARK 500    GLU H 216      -84.68   -113.70                                   
REMARK 500    CYS L  23      115.84   -164.30                                   
REMARK 500    SER L  30     -131.10     49.80                                   
REMARK 500    ALA L  51      -22.96     83.03                                   
REMARK 500    ASN L 138       62.75     64.03                                   
REMARK 500    LYS L 169      -65.40   -101.20                                   
REMARK 500    LYS L 188       20.63    -77.85                                   
REMARK 500    LYS L 190      -63.23    -97.59                                   
REMARK 500    GLU P  84      -66.39    -17.55                                   
REMARK 500    HIS P 139       -9.95     87.00                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3SQO A  153   692  UNP    Q8NBP7   PCSK9_HUMAN    153    692             
DBREF  3SQO P   31   152  UNP    Q8NBP7   PCSK9_HUMAN     31    152             
DBREF  3SQO H    1   218  PDB    3SQO     3SQO             1    218             
DBREF  3SQO L    1   214  PDB    3SQO     3SQO             1    214             
SEQADV 3SQO ILE A  474  UNP  Q8NBP7    VAL   474 CONFLICT                       
SEQADV 3SQO GLU A  670  UNP  Q8NBP7    GLY   670 CONFLICT                       
SEQRES   1 A  540  SER ILE PRO TRP ASN LEU GLU ARG ILE THR PRO PRO ARG          
SEQRES   2 A  540  TYR ARG ALA ASP GLU TYR GLN PRO PRO ASP GLY GLY SER          
SEQRES   3 A  540  LEU VAL GLU VAL TYR LEU LEU ASP THR SER ILE GLN SER          
SEQRES   4 A  540  ASP HIS ARG GLU ILE GLU GLY ARG VAL MET VAL THR ASP          
SEQRES   5 A  540  PHE GLU ASN VAL PRO GLU GLU ASP GLY THR ARG PHE HIS          
SEQRES   6 A  540  ARG GLN ALA SER LYS CYS ASP SER HIS GLY THR HIS LEU          
SEQRES   7 A  540  ALA GLY VAL VAL SER GLY ARG ASP ALA GLY VAL ALA LYS          
SEQRES   8 A  540  GLY ALA SER MET ARG SER LEU ARG VAL LEU ASN CYS GLN          
SEQRES   9 A  540  GLY LYS GLY THR VAL SER GLY THR LEU ILE GLY LEU GLU          
SEQRES  10 A  540  PHE ILE ARG LYS SER GLN LEU VAL GLN PRO VAL GLY PRO          
SEQRES  11 A  540  LEU VAL VAL LEU LEU PRO LEU ALA GLY GLY TYR SER ARG          
SEQRES  12 A  540  VAL LEU ASN ALA ALA CYS GLN ARG LEU ALA ARG ALA GLY          
SEQRES  13 A  540  VAL VAL LEU VAL THR ALA ALA GLY ASN PHE ARG ASP ASP          
SEQRES  14 A  540  ALA CYS LEU TYR SER PRO ALA SER ALA PRO GLU VAL ILE          
SEQRES  15 A  540  THR VAL GLY ALA THR ASN ALA GLN ASP GLN PRO VAL THR          
SEQRES  16 A  540  LEU GLY THR LEU GLY THR ASN PHE GLY ARG CYS VAL ASP          
SEQRES  17 A  540  LEU PHE ALA PRO GLY GLU ASP ILE ILE GLY ALA SER SER          
SEQRES  18 A  540  ASP CYS SER THR CYS PHE VAL SER GLN SER GLY THR SER          
SEQRES  19 A  540  GLN ALA ALA ALA HIS VAL ALA GLY ILE ALA ALA MET MET          
SEQRES  20 A  540  LEU SER ALA GLU PRO GLU LEU THR LEU ALA GLU LEU ARG          
SEQRES  21 A  540  GLN ARG LEU ILE HIS PHE SER ALA LYS ASP VAL ILE ASN          
SEQRES  22 A  540  GLU ALA TRP PHE PRO GLU ASP GLN ARG VAL LEU THR PRO          
SEQRES  23 A  540  ASN LEU VAL ALA ALA LEU PRO PRO SER THR HIS GLY ALA          
SEQRES  24 A  540  GLY TRP GLN LEU PHE CYS ARG THR VAL TRP SER ALA HIS          
SEQRES  25 A  540  SER GLY PRO THR ARG MET ALA THR ALA ILE ALA ARG CYS          
SEQRES  26 A  540  ALA PRO ASP GLU GLU LEU LEU SER CYS SER SER PHE SER          
SEQRES  27 A  540  ARG SER GLY LYS ARG ARG GLY GLU ARG MET GLU ALA GLN          
SEQRES  28 A  540  GLY GLY LYS LEU VAL CYS ARG ALA HIS ASN ALA PHE GLY          
SEQRES  29 A  540  GLY GLU GLY VAL TYR ALA ILE ALA ARG CYS CYS LEU LEU          
SEQRES  30 A  540  PRO GLN ALA ASN CYS SER VAL HIS THR ALA PRO PRO ALA          
SEQRES  31 A  540  GLU ALA SER MET GLY THR ARG VAL HIS CYS HIS GLN GLN          
SEQRES  32 A  540  GLY HIS VAL LEU THR GLY CYS SER SER HIS TRP GLU VAL          
SEQRES  33 A  540  GLU ASP LEU GLY THR HIS LYS PRO PRO VAL LEU ARG PRO          
SEQRES  34 A  540  ARG GLY GLN PRO ASN GLN CYS VAL GLY HIS ARG GLU ALA          
SEQRES  35 A  540  SER ILE HIS ALA SER CYS CYS HIS ALA PRO GLY LEU GLU          
SEQRES  36 A  540  CYS LYS VAL LYS GLU HIS GLY ILE PRO ALA PRO GLN GLU          
SEQRES  37 A  540  GLN VAL THR VAL ALA CYS GLU GLU GLY TRP THR LEU THR          
SEQRES  38 A  540  GLY CYS SER ALA LEU PRO GLY THR SER HIS VAL LEU GLY          
SEQRES  39 A  540  ALA TYR ALA VAL ASP ASN THR CYS VAL VAL ARG SER ARG          
SEQRES  40 A  540  ASP VAL SER THR THR GLY SER THR SER GLU GLU ALA VAL          
SEQRES  41 A  540  THR ALA VAL ALA ILE CYS CYS ARG SER ARG HIS LEU ALA          
SEQRES  42 A  540  GLN ALA SER GLN GLU LEU GLN                                  
SEQRES   1 H  219  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL LYS LYS          
SEQRES   2 H  219  PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 H  219  TYR THR PHE THR SER TYR TYR MET HIS TRP VAL ARG GLN          
SEQRES   4 H  219  ALA PRO GLY GLN GLY LEU GLU TRP MET GLY GLU ILE SER          
SEQRES   5 H  219  PRO PHE GLY GLY ARG THR ASN TYR ASN GLU LYS PHE LYS          
SEQRES   6 H  219  SER ARG VAL THR MET THR ARG ASP THR SER THR SER THR          
SEQRES   7 H  219  VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR          
SEQRES   8 H  219  ALA VAL TYR TYR CYS ALA ARG GLU ARG PRO LEU TYR ALA          
SEQRES   9 H  219  SER ASP LEU TRP GLY GLN GLY THR THR VAL THR VAL SER          
SEQRES  10 H  219  SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA          
SEQRES  11 H  219  PRO SER SER ARG SER THR SER GLU SER THR ALA ALA LEU          
SEQRES  12 H  219  GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 H  219  VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS          
SEQRES  14 H  219  THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER          
SEQRES  15 H  219  LEU SER SER VAL VAL THR VAL PRO SER SER ASN PHE GLY          
SEQRES  16 H  219  THR GLN THR TYR THR CYS ASN VAL ASP HIS LYS PRO SER          
SEQRES  17 H  219  ASN THR LYS VAL ASP LYS THR VAL GLU ARG LYS                  
SEQRES   1 L  214  ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA          
SEQRES   2 L  214  SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ALA LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA SER          
SEQRES   5 L  214  TYR ARG TYR THR GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP PHE THR PHE THR ILE SER SER LEU          
SEQRES   7 L  214  GLN PRO GLU ASP ILE ALA THR TYR TYR CYS GLN GLN ARG          
SEQRES   8 L  214  TYR SER LEU TRP ARG THR PHE GLY GLN GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU SER                                      
SEQRES   1 P  122  GLN GLU ASP GLU ASP GLY ASP TYR GLU GLU LEU VAL LEU          
SEQRES   2 P  122  ALA LEU ARG SER GLU GLU ASP GLY LEU ALA GLU ALA PRO          
SEQRES   3 P  122  GLU HIS GLY THR THR ALA THR PHE HIS ARG CYS ALA LYS          
SEQRES   4 P  122  ASP PRO TRP ARG LEU PRO GLY THR TYR VAL VAL VAL LEU          
SEQRES   5 P  122  LYS GLU GLU THR HIS LEU SER GLN SER GLU ARG THR ALA          
SEQRES   6 P  122  ARG ARG LEU GLN ALA GLN ALA ALA ARG ARG GLY TYR LEU          
SEQRES   7 P  122  THR LYS ILE LEU HIS VAL PHE HIS GLY LEU LEU PRO GLY          
SEQRES   8 P  122  PHE LEU VAL LYS MET SER GLY ASP LEU LEU GLU LEU ALA          
SEQRES   9 P  122  LEU LYS LEU PRO HIS VAL ASP TYR ILE GLU GLU ASP SER          
SEQRES  10 P  122  SER VAL PHE ALA GLN                                          
FORMUL   5  HOH   *32(H2 O)                                                     
HELIX    1   1 PRO A  155  THR A  162  1                                   8    
HELIX    2   2 GLN A  219  GLY A  236  1                                  18    
HELIX    3   3 VAL A  261  GLN A  278  1                                  18    
HELIX    4   4 SER A  294  GLY A  308  1                                  15    
HELIX    5   5 ASP A  321  CYS A  323  5                                   3    
HELIX    6   6 GLY A  384  GLU A  403  1                                  20    
HELIX    7   7 THR A  407  PHE A  418  1                                  12    
HELIX    8   8 ASN A  425  PHE A  429  5                                   5    
HELIX    9   9 PRO A  430  ARG A  434  5                                   5    
HELIX   10  10 THR H   28  TYR H   32  5                                   5    
HELIX   11  11 PRO H   52A GLY H   55  5                                   4    
HELIX   12  12 ARG H   83  THR H   87  5                                   5    
HELIX   13  13 GLN L   79  ILE L   83  5                                   5    
HELIX   14  14 SER L  121  SER L  127  1                                   7    
HELIX   15  15 LYS L  183  LYS L  188  1                                   6    
HELIX   16  16 LYS P   69  PRO P   71  5                                   3    
HELIX   17  17 HIS P   87  ARG P  104  1                                  18    
HELIX   18  18 SER P  127  ASP P  129  5                                   3    
HELIX   19  19 LEU P  130  LEU P  135  1                                   6    
SHEET    1   A 7 VAL A 200  GLU A 206  0                                        
SHEET    2   A 7 SER A 246  ARG A 251  1  O  MET A 247   N  MET A 201           
SHEET    3   A 7 GLU A 181  ASP A 186  1  N  LEU A 184   O  ARG A 248           
SHEET    4   A 7 LEU A 283  LEU A 287  1  O  VAL A 284   N  TYR A 183           
SHEET    5   A 7 VAL A 310  ALA A 314  1  O  VAL A 312   N  LEU A 287           
SHEET    6   A 7 ILE A 334  THR A 339  1  O  ILE A 334   N  THR A 313           
SHEET    7   A 7 LEU A 361  PRO A 364  1  O  ALA A 363   N  THR A 339           
SHEET    1   B 3 LYS A 258  THR A 260  0                                        
SHEET    2   B 3 VAL P 140  ALA P 151 -1  O  VAL P 149   N  GLY A 259           
SHEET    3   B 3 THR P  63  HIS P  65  1  N  HIS P  65   O  ILE P 143           
SHEET    1   C 6 TYR A 325  SER A 326  0                                        
SHEET    2   C 6 LEU A 289  GLY A 292 -1  N  GLY A 291   O  SER A 326           
SHEET    3   C 6 VAL P 140  ALA P 151 -1  O  PHE P 150   N  ALA A 290           
SHEET    4   C 6 ARG P  73  LEU P  82 -1  N  VAL P  79   O  GLU P 144           
SHEET    5   C 6 GLY P 121  LYS P 125 -1  O  PHE P 122   N  VAL P  80           
SHEET    6   C 6 LYS P 110  PHE P 115 -1  N  LYS P 110   O  LYS P 125           
SHEET    1   D 2 ILE A 368  ALA A 371  0                                        
SHEET    2   D 2 PHE A 379  GLN A 382 -1  O  GLN A 382   N  ILE A 368           
SHEET    1   E 2 ALA A 420  LYS A 421  0                                        
SHEET    2   E 2 LEU A 440  VAL A 441 -1  O  VAL A 441   N  ALA A 420           
SHEET    1   F 3 CYS A 457  TRP A 461  0                                        
SHEET    2   F 3 TYR A 521  CYS A 527 -1  O  ALA A 524   N  VAL A 460           
SHEET    3   F 3 GLU A 482  PHE A 489 -1  N  GLU A 482   O  CYS A 527           
SHEET    1   G 3 ALA A 473  ALA A 475  0                                        
SHEET    2   G 3 LEU A 507  ASN A 513 -1  O  ALA A 511   N  ALA A 473           
SHEET    3   G 3 ARG A 495  ALA A 502 -1  N  ARG A 499   O  ARG A 510           
SHEET    1   H 3 ALA A 532  ALA A 539  0                                        
SHEET    2   H 3 SER A 595  HIS A 602 -1  O  ALA A 598   N  HIS A 537           
SHEET    3   H 3 HIS A 557  HIS A 565 -1  N  HIS A 565   O  SER A 595           
SHEET    1   I 2 THR A 548  HIS A 551  0                                        
SHEET    2   I 2 GLN A 587  GLY A 590 -1  O  CYS A 588   N  VAL A 550           
SHEET    1   J 3 GLU A 607  PRO A 616  0                                        
SHEET    2   J 3 ALA A 671  ARG A 680 -1  O  ALA A 676   N  LYS A 611           
SHEET    3   J 3 THR A 631  ALA A 637 -1  N  SER A 636   O  VAL A 675           
SHEET    1   K 3 GLN A 621  ALA A 625  0                                        
SHEET    2   K 3 THR A 653  SER A 658 -1  O  CYS A 654   N  VAL A 624           
SHEET    3   K 3 VAL A 644  VAL A 650 -1  N  TYR A 648   O  VAL A 655           
SHEET    1   L 2 GLN H   3  GLN H   6  0                                        
SHEET    2   L 2 CYS H  22  SER H  25 -1  O  LYS H  23   N  VAL H   5           
SHEET    1   M 6 GLU H  10  LYS H  12  0                                        
SHEET    2   M 6 THR H 107  VAL H 111  1  O  THR H 110   N  LYS H  12           
SHEET    3   M 6 ALA H  88  GLU H  95 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   M 6 TYR H  33  ALA H  40 -1  N  HIS H  35   O  ALA H  93           
SHEET    5   M 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  ARG H  38           
SHEET    6   M 6 THR H  57  TYR H  59 -1  O  ASN H  58   N  GLU H  50           
SHEET    1   N 4 GLU H  10  LYS H  12  0                                        
SHEET    2   N 4 THR H 107  VAL H 111  1  O  THR H 110   N  LYS H  12           
SHEET    3   N 4 ALA H  88  GLU H  95 -1  N  ALA H  88   O  VAL H 109           
SHEET    4   N 4 LEU H 102  TRP H 103 -1  O  LEU H 102   N  ARG H  94           
SHEET    1   O 3 VAL H  18  VAL H  20  0                                        
SHEET    2   O 3 THR H  77  LEU H  82 -1  O  MET H  80   N  VAL H  20           
SHEET    3   O 3 THR H  68  ASP H  72 -1  N  THR H  70   O  TYR H  79           
SHEET    1   P 4 SER H 124  LEU H 128  0                                        
SHEET    2   P 4 ALA H 141  TYR H 149 -1  O  LEU H 145   N  PHE H 126           
SHEET    3   P 4 TYR H 180  THR H 187 -1  O  SER H 184   N  CYS H 144           
SHEET    4   P 4 VAL H 167  THR H 169 -1  N  HIS H 168   O  VAL H 185           
SHEET    1   Q 4 SER H 124  LEU H 128  0                                        
SHEET    2   Q 4 ALA H 141  TYR H 149 -1  O  LEU H 145   N  PHE H 126           
SHEET    3   Q 4 TYR H 180  THR H 187 -1  O  SER H 184   N  CYS H 144           
SHEET    4   Q 4 VAL H 173  LEU H 174 -1  N  VAL H 173   O  SER H 181           
SHEET    1   R 3 THR H 155  TRP H 158  0                                        
SHEET    2   R 3 TYR H 198  HIS H 204 -1  O  ASN H 201   N  SER H 157           
SHEET    3   R 3 THR H 209  VAL H 215 -1  O  VAL H 215   N  TYR H 198           
SHEET    1   S 4 MET L   4  SER L   7  0                                        
SHEET    2   S 4 VAL L  19  ALA L  25 -1  O  ARG L  24   N  THR L   5           
SHEET    3   S 4 ASP L  70  ILE L  75 -1  O  PHE L  73   N  ILE L  21           
SHEET    4   S 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1   T 6 SER L  10  SER L  14  0                                        
SHEET    2   T 6 THR L 102  LYS L 107  1  O  LYS L 107   N  ALA L  13           
SHEET    3   T 6 THR L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   T 6 LEU L  33  GLN L  38 -1  N  ALA L  34   O  GLN L  89           
SHEET    5   T 6 LYS L  45  TYR L  49 -1  O  LYS L  45   N  GLN L  37           
SHEET    6   T 6 TYR L  53  ARG L  54 -1  O  TYR L  53   N  TYR L  49           
SHEET    1   U 4 SER L  10  SER L  14  0                                        
SHEET    2   U 4 THR L 102  LYS L 107  1  O  LYS L 107   N  ALA L  13           
SHEET    3   U 4 THR L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4   U 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1   V 4 SER L 114  PHE L 118  0                                        
SHEET    2   V 4 THR L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3   V 4 TYR L 173  SER L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4   V 4 SER L 159  VAL L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1   W 4 ALA L 153  LEU L 154  0                                        
SHEET    2   W 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3   W 4 VAL L 191  THR L 197 -1  O  ALA L 193   N  LYS L 149           
SHEET    4   W 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SSBOND   1 CYS A  223    CYS A  255                          1555   1555  2.05  
SSBOND   2 CYS A  323    CYS A  358                          1555   1555  2.10  
SSBOND   3 CYS A  375    CYS A  378                          1555   1555  2.06  
SSBOND   4 CYS A  457    CYS A  527                          1555   1555  2.04  
SSBOND   5 CYS A  477    CYS A  526                          1555   1555  2.05  
SSBOND   6 CYS A  486    CYS A  509                          1555   1555  2.06  
SSBOND   7 CYS A  534    CYS A  601                          1555   1555  1.85  
SSBOND   8 CYS A  552    CYS A  600                          1555   1555  2.03  
SSBOND   9 CYS A  562    CYS A  588                          1555   1555  2.03  
SSBOND  10 CYS A  608    CYS A  679                          1555   1555  2.06  
SSBOND  11 CYS A  626    CYS A  678                          1555   1555  2.06  
SSBOND  12 CYS A  635    CYS A  654                          1555   1555  2.04  
SSBOND  13 CYS H   22    CYS H   92                          1555   1555  2.05  
SSBOND  14 CYS H  144    CYS H  200                          1555   1555  2.05  
SSBOND  15 CYS L   23    CYS L   88                          1555   1555  2.08  
SSBOND  16 CYS L  134    CYS L  194                          1555   1555  2.05  
CISPEP   1 SER A  326    PRO A  327          0         1.30                     
CISPEP   2 PHE H  150    PRO H  151          0         2.59                     
CISPEP   3 GLU H  152    PRO H  153          0        -1.13                     
CISPEP   4 SER L    7    PRO L    8          0        -4.04                     
CISPEP   5 TYR L  140    PRO L  141          0         2.65                     
CRYST1   81.921   70.981  109.156  90.00  95.90  90.00 P 1 21 1      2          
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      0.012207  0.000000  0.001261        0.00000                         
SCALE2      0.000000  0.014088  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009210        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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