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Database: PDB
Entry: 2VN9
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Original site: 2VN9 
HEADER    TRANSFERASE                             31-JAN-08   2VN9              
TITLE     CRYSTAL STRUCTURE OF HUMAN CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE
TITLE    2 II DELTA ISOFORM 1, CAMKD                                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CALCIUM/CALMODULIN-DEPENDENT PROTEIN KINASE TYPE II DELTA  
COMPND   3 CHAIN;                                                               
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 FRAGMENT: KINASE DOMAIN, RESIDUES 11-309;                            
COMPND   6 SYNONYM: CAM-KINASE II DELTA CHAIN, CAM KINASE II SUBUNIT DELTA,     
COMPND   7 CAMK-II SUBUNIT DELTA, CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II
COMPND   8 DELTA ISOFORM 1;                                                     
COMPND   9 EC: 2.7.11.17;                                                       
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;                                
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, SERINE-THREONINE KINASE, CELLULAR    
KEYWDS   2 DIFFERENTIATION, VASCULAR SMOOTH MUSCLE, KINASE, TRANSFERASE, ATP-   
KEYWDS   3 BINDING, PHOSPHOPROTEIN, CALMODULIN-BINDING, NUCLEOTIDE-BINDING      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.K.ROOS,P.RELLOS,E.SALAH,A.C.W.PIKE,O.FEDOROV,E.S.PILKA,F.VON DELFT, 
AUTHOR   2 C.H.ARROWSMITH,J.WEIGELT,A.EDWARDS,C.BOUNTRA,S.KNAPP                 
REVDAT   5   13-DEC-17 2VN9    1       SOURCE JRNL                              
REVDAT   4   10-AUG-11 2VN9    1       JRNL   REMARK HETSYN FORMUL              
REVDAT   3   13-JUL-11 2VN9    1       VERSN                                    
REVDAT   2   24-FEB-09 2VN9    1       VERSN                                    
REVDAT   1   26-FEB-08 2VN9    0                                                
JRNL        AUTH   P.RELLOS,A.C.W.PIKE,F.H.NIESEN,E.SALAH,W.H.LEE,F.VON DELFT,  
JRNL        AUTH 2 S.KNAPP                                                      
JRNL        TITL   STRUCTURE OF THE CAMKIIDELTA/CALMODULIN COMPLEX REVEALS THE  
JRNL        TITL 2 MOLECULAR MECHANISM OF CAMKII KINASE ACTIVATION.             
JRNL        REF    PLOS BIOL.                    V.   8   426 2010              
JRNL        REFN                   ISSN 1544-9173                               
JRNL        PMID   20668654                                                     
JRNL        DOI    10.1371/JOURNAL.PBIO.1000426                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.4.0066                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.03                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 37042                          
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) : 0.213                           
REMARK   3   R VALUE            (WORKING SET) : 0.211                           
REMARK   3   FREE R VALUE                     : 0.248                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1960                            
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2704                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2980                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 140                          
REMARK   3   BIN FREE R VALUE                    : 0.3810                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4721                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 97                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 58.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.15000                                              
REMARK   3    B22 (A**2) : 1.15000                                              
REMARK   3    B33 (A**2) : -1.72000                                             
REMARK   3    B12 (A**2) : 0.57000                                              
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): 0.262         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.212         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.193         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.783        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4928 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3332 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6686 ; 1.425 ; 1.976       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8071 ; 0.976 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   600 ; 5.808 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   216 ;33.025 ;23.796       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   820 ;14.525 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;21.522 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   725 ; 0.080 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5440 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   980 ; 0.002 ; 0.020       
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):  3000 ; 1.684 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1210 ; 0.870 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4823 ; 2.481 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1928 ; 4.495 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1857 ; 5.576 ;11.000       
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 : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     -1       A     309      1                      
REMARK   3           1     B     -1       B     309      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   3959 ;  0.04 ;  0.05           
REMARK   3   TIGHT POSITIONAL   1    B    (A):   3959 ;  0.04 ;  0.05           
REMARK   3   TIGHT THERMAL      1    A (A**2):   3959 ;  0.16 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):   3959 ;  0.16 ;  0.50           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
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    -1        A    39                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.4802  37.9307  55.7746              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4185 T22:   0.1348                                     
REMARK   3      T33:   0.0596 T12:  -0.0372                                     
REMARK   3      T13:   0.0242 T23:  -0.0222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7580 L22:   8.4180                                     
REMARK   3      L33:  11.6520 L12:   0.4387                                     
REMARK   3      L13:   0.7231 L23:   1.9160                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3062 S12:  -0.3087 S13:   0.5231                       
REMARK   3      S21:  -0.0987 S22:   0.1327 S23:   0.2238                       
REMARK   3      S31:  -0.7694 S32:  -0.4147 S33:   0.1735                       
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    40        A    83                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.2753  30.2185  53.5075              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.4955 T22:   0.1371                                     
REMARK   3      T33:  -0.1308 T12:  -0.0343                                     
REMARK   3      T13:   0.0055 T23:   0.0496                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7529 L22:   1.8197                                     
REMARK   3      L33:   1.3251 L12:  -3.0149                                     
REMARK   3      L13:  -0.3544 L23:   0.9449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1694 S12:  -0.3660 S13:   0.4505                       
REMARK   3      S21:   0.0963 S22:   0.0796 S23:   0.0180                       
REMARK   3      S31:  -0.0176 S32:  -0.1205 S33:   0.0898                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    84        A   309                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0084  15.6757  36.1947              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2976 T22:   0.1063                                     
REMARK   3      T33:  -0.1776 T12:  -0.1446                                     
REMARK   3      T13:   0.0777 T23:   0.0230                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3598 L22:   1.9079                                     
REMARK   3      L33:   2.0951 L12:   0.5050                                     
REMARK   3      L13:  -0.2368 L23:   1.2558                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2771 S12:   0.6060 S13:  -0.3184                       
REMARK   3      S21:  -0.4213 S22:   0.2423 S23:  -0.1134                       
REMARK   3      S31:   0.1423 S32:  -0.0756 S33:   0.0348                       
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 :   B    -1        B    39                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.5939  57.9775  -6.0806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1722 T22:  -0.0916                                     
REMARK   3      T33:   0.0591 T12:  -0.2799                                     
REMARK   3      T13:  -0.1864 T23:   0.0621                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.4621 L22:   7.4556                                     
REMARK   3      L33:  10.1546 L12:   0.7162                                     
REMARK   3      L13:   1.0051 L23:  -0.3826                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2801 S12:  -0.0299 S13:   0.4969                       
REMARK   3      S21:  -0.4617 S22:   0.2955 S23:   0.2677                       
REMARK   3      S31:  -0.3389 S32:  -0.6191 S33:  -0.0155                       
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 :   B    40        B    83                          
REMARK   3    ORIGIN FOR THE GROUP (A):   3.7954  65.3807  -1.3540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2174 T22:  -0.1521                                     
REMARK   3      T33:  -0.1419 T12:  -0.3370                                     
REMARK   3      T13:  -0.1012 T23:   0.0336                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2188 L22:   8.9965                                     
REMARK   3      L33:   3.5945 L12:   0.3249                                     
REMARK   3      L13:   0.7225 L23:  -2.1354                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3533 S12:   0.0536 S13:   0.2378                       
REMARK   3      S21:  -0.9819 S22:   0.1194 S23:   0.2851                       
REMARK   3      S31:  -0.1204 S32:   0.0687 S33:   0.2339                       
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 :   B    84        B   309                          
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0597  54.9420  19.5083              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1601 T22:   0.0152                                     
REMARK   3      T33:  -0.2501 T12:  -0.1217                                     
REMARK   3      T13:   0.0039 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5556 L22:   4.0334                                     
REMARK   3      L33:   5.6129 L12:   0.1549                                     
REMARK   3      L13:   1.6079 L23:  -2.5982                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2961 S12:  -0.5224 S13:   0.1137                       
REMARK   3      S21:   0.1363 S22:   0.1430 S23:   0.0182                       
REMARK   3      S31:  -0.4519 S32:  -0.3415 S33:   0.1531                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2VN9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-JAN-08.                  
REMARK 100 THE DEPOSITION ID IS D_1290035204.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-OCT-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98248                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39106                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRY 2V7O                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.6 M NAKPO4 HEPES PH 7.5                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      208.96667            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      104.48333            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      104.48333            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      208.96667            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A  -1    OG                                                  
REMARK 470     LYS A  22    CE   NZ                                             
REMARK 470     PHE A  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A  49    CE   NZ                                             
REMARK 470     LYS A  69    CE   NZ                                             
REMARK 470     GLN A 165    CD   OE1  NE2                                       
REMARK 470     GLN A 168    CD   OE1  NE2                                       
REMARK 470     ARG A 187    CZ   NH1  NH2                                       
REMARK 470     LYS A 188    NZ                                                  
REMARK 470     ARG A 221    CZ   NH1  NH2                                       
REMARK 470     GLN A 224    CD   OE1  NE2                                       
REMARK 470     LYS A 259    NZ                                                  
REMARK 470     LYS A 292    CE   NZ                                             
REMARK 470     LYS A 299    CE   NZ                                             
REMARK 470     LEU A 309    CG   CD1  CD2                                       
REMARK 470     SER B  -1    OG                                                  
REMARK 470     LEU B  16    CG   CD1  CD2                                       
REMARK 470     LYS B  22    CE   NZ                                             
REMARK 470     PHE B  25    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B  48    CD   CE   NZ                                        
REMARK 470     LYS B  49    CG   CD   CE   NZ                                   
REMARK 470     LYS B  69    CE   NZ                                             
REMARK 470     GLN B 165    CG   CD   OE1  NE2                                  
REMARK 470     GLN B 168    CD   OE1  NE2                                       
REMARK 470     LYS B 188    CE   NZ                                             
REMARK 470     GLN B 224    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 259    CD   CE   NZ                                        
REMARK 470     LYS B 268    CE   NZ                                             
REMARK 470     LYS B 292    CD   CE   NZ                                        
REMARK 470     LYS B 293    CD   CE   NZ                                        
REMARK 470     LYS B 299    CE   NZ                                             
REMARK 470     LYS B 301    CG   CD   CE   NZ                                   
REMARK 470     LEU B 309    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 298   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ARG A 298   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    PHE A  17     -136.38   -116.79                                   
REMARK 500    PHE A  25       31.13   -171.85                                   
REMARK 500    ASP A 136       46.64   -149.72                                   
REMARK 500    ASP A 157       92.42     55.20                                   
REMARK 500    LYS A 301     -143.04     67.00                                   
REMARK 500    PHE B  17     -135.64   -118.09                                   
REMARK 500    PHE B  25       29.91   -171.19                                   
REMARK 500    ASP B 136       47.14   -147.49                                   
REMARK 500    ASP B 157       92.45     57.38                                   
REMARK 500    PHE B 233       68.62   -119.10                                   
REMARK 500    ARG B 284       62.05   -117.61                                   
REMARK 500    LYS B 301     -150.37     68.23                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVD B 1310                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GVD A 1314                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1310                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1311                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 1312                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1311                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1312                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EPE A 1313                
DBREF  2VN9 A   -1     0  PDB    2VN9     2VN9            -1      0             
DBREF  2VN9 A   11   309  UNP    Q13557   KCC2D_HUMAN     11    309             
DBREF  2VN9 B   -1     0  PDB    2VN9     2VN9            -1      0             
DBREF  2VN9 B   11   309  UNP    Q13557   KCC2D_HUMAN     11    309             
SEQRES   1 A  301  SER MET THR ASP GLU TYR GLN LEU PHE GLU GLU LEU GLY          
SEQRES   2 A  301  LYS GLY ALA PHE SER VAL VAL ARG ARG CYS MET LYS ILE          
SEQRES   3 A  301  PRO THR GLY GLN GLU TYR ALA ALA LYS ILE ILE ASN THR          
SEQRES   4 A  301  LYS LYS LEU SER ALA ARG ASP HIS GLN LYS LEU GLU ARG          
SEQRES   5 A  301  GLU ALA ARG ILE CYS ARG LEU LEU LYS HIS PRO ASN ILE          
SEQRES   6 A  301  VAL ARG LEU HIS ASP SER ILE SER GLU GLU GLY PHE HIS          
SEQRES   7 A  301  TYR LEU VAL PHE ASP LEU VAL THR GLY GLY GLU LEU PHE          
SEQRES   8 A  301  GLU ASP ILE VAL ALA ARG GLU TYR TYR SER GLU ALA ASP          
SEQRES   9 A  301  ALA SER HIS CYS ILE GLN GLN ILE LEU GLU SER VAL ASN          
SEQRES  10 A  301  HIS CYS HIS LEU ASN GLY ILE VAL HIS ARG ASP LEU LYS          
SEQRES  11 A  301  PRO GLU ASN LEU LEU LEU ALA SER LYS SER LYS GLY ALA          
SEQRES  12 A  301  ALA VAL LYS LEU ALA ASP PHE GLY LEU ALA ILE GLU VAL          
SEQRES  13 A  301  GLN GLY ASP GLN GLN ALA TRP PHE GLY PHE ALA GLY THR          
SEQRES  14 A  301  PRO GLY TYR LEU SER PRO GLU VAL LEU ARG LYS ASP PRO          
SEQRES  15 A  301  TYR GLY LYS PRO VAL ASP MET TRP ALA CYS GLY VAL ILE          
SEQRES  16 A  301  LEU TYR ILE LEU LEU VAL GLY TYR PRO PRO PHE TRP ASP          
SEQRES  17 A  301  GLU ASP GLN HIS ARG LEU TYR GLN GLN ILE LYS ALA GLY          
SEQRES  18 A  301  ALA TYR ASP PHE PRO SER PRO GLU TRP ASP THR VAL THR          
SEQRES  19 A  301  PRO GLU ALA LYS ASP LEU ILE ASN LYS MET LEU THR ILE          
SEQRES  20 A  301  ASN PRO ALA LYS ARG ILE THR ALA SER GLU ALA LEU LYS          
SEQRES  21 A  301  HIS PRO TRP ILE CYS GLN ARG SER THR VAL ALA SER MET          
SEQRES  22 A  301  MET HIS ARG GLN GLU THR VAL ASP CYS LEU LYS LYS PHE          
SEQRES  23 A  301  ASN ALA ARG ARG LYS LEU LYS GLY ALA ILE LEU THR THR          
SEQRES  24 A  301  MET LEU                                                      
SEQRES   1 B  301  SER MET THR ASP GLU TYR GLN LEU PHE GLU GLU LEU GLY          
SEQRES   2 B  301  LYS GLY ALA PHE SER VAL VAL ARG ARG CYS MET LYS ILE          
SEQRES   3 B  301  PRO THR GLY GLN GLU TYR ALA ALA LYS ILE ILE ASN THR          
SEQRES   4 B  301  LYS LYS LEU SER ALA ARG ASP HIS GLN LYS LEU GLU ARG          
SEQRES   5 B  301  GLU ALA ARG ILE CYS ARG LEU LEU LYS HIS PRO ASN ILE          
SEQRES   6 B  301  VAL ARG LEU HIS ASP SER ILE SER GLU GLU GLY PHE HIS          
SEQRES   7 B  301  TYR LEU VAL PHE ASP LEU VAL THR GLY GLY GLU LEU PHE          
SEQRES   8 B  301  GLU ASP ILE VAL ALA ARG GLU TYR TYR SER GLU ALA ASP          
SEQRES   9 B  301  ALA SER HIS CYS ILE GLN GLN ILE LEU GLU SER VAL ASN          
SEQRES  10 B  301  HIS CYS HIS LEU ASN GLY ILE VAL HIS ARG ASP LEU LYS          
SEQRES  11 B  301  PRO GLU ASN LEU LEU LEU ALA SER LYS SER LYS GLY ALA          
SEQRES  12 B  301  ALA VAL LYS LEU ALA ASP PHE GLY LEU ALA ILE GLU VAL          
SEQRES  13 B  301  GLN GLY ASP GLN GLN ALA TRP PHE GLY PHE ALA GLY THR          
SEQRES  14 B  301  PRO GLY TYR LEU SER PRO GLU VAL LEU ARG LYS ASP PRO          
SEQRES  15 B  301  TYR GLY LYS PRO VAL ASP MET TRP ALA CYS GLY VAL ILE          
SEQRES  16 B  301  LEU TYR ILE LEU LEU VAL GLY TYR PRO PRO PHE TRP ASP          
SEQRES  17 B  301  GLU ASP GLN HIS ARG LEU TYR GLN GLN ILE LYS ALA GLY          
SEQRES  18 B  301  ALA TYR ASP PHE PRO SER PRO GLU TRP ASP THR VAL THR          
SEQRES  19 B  301  PRO GLU ALA LYS ASP LEU ILE ASN LYS MET LEU THR ILE          
SEQRES  20 B  301  ASN PRO ALA LYS ARG ILE THR ALA SER GLU ALA LEU LYS          
SEQRES  21 B  301  HIS PRO TRP ILE CYS GLN ARG SER THR VAL ALA SER MET          
SEQRES  22 B  301  MET HIS ARG GLN GLU THR VAL ASP CYS LEU LYS LYS PHE          
SEQRES  23 B  301  ASN ALA ARG ARG LYS LEU LYS GLY ALA ILE LEU THR THR          
SEQRES  24 B  301  MET LEU                                                      
HET    PO4  A1310       5                                                       
HET    PO4  A1311       5                                                       
HET     CL  A1312       1                                                       
HET    EPE  A1313      15                                                       
HET    GVD  A1314      29                                                       
HET    GVD  B1310      29                                                       
HET    PO4  B1311       5                                                       
HET    PO4  B1312       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     GVD [4-({4-[(5-CYCLOPROPYL-1H-PYRAZOL-3-YL)                          
HETNAM   2 GVD  AMINO]QUINAZOLIN-2-YL}IMINO)CYCLOHEXA-2,5-DIEN-1-               
HETNAM   3 GVD  YL]ACETONITRILE                                                 
HETSYN     EPE HEPES                                                            
FORMUL   3  PO4    4(O4 P 3-)                                                   
FORMUL   5   CL    CL 1-                                                        
FORMUL   6  EPE    C8 H18 N2 O4 S                                               
FORMUL   7  GVD    2(C22 H19 N7)                                                
FORMUL  11  HOH   *97(H2 O)                                                     
HELIX    1   1 SER A   -1  GLU A   13  1                                   5    
HELIX    2   2 SER A   51  LEU A   68  1                                  18    
HELIX    3   3 GLU A   97  ARG A  105  1                                   9    
HELIX    4   4 SER A  109  ASN A  130  1                                  22    
HELIX    5   5 LYS A  138  GLU A  140  5                                   3    
HELIX    6   6 THR A  177  LEU A  181  5                                   5    
HELIX    7   7 SER A  182  ARG A  187  1                                   6    
HELIX    8   8 LYS A  193  GLY A  210  1                                  18    
HELIX    9   9 ASP A  218  GLY A  229  1                                  12    
HELIX   10  10 PRO A  236  VAL A  241  5                                   6    
HELIX   11  11 THR A  242  LEU A  253  1                                  12    
HELIX   12  12 THR A  262  LEU A  267  1                                   6    
HELIX   13  13 HIS A  269  GLN A  274  1                                   6    
HELIX   14  14 GLN A  274  ALA A  279  1                                   6    
HELIX   15  15 ARG A  284  LEU A  300  1                                  17    
HELIX   16  16 SER B   -1  GLU B   13  1                                   5    
HELIX   17  17 SER B   51  LEU B   68  1                                  18    
HELIX   18  18 GLU B   97  ALA B  104  1                                   8    
HELIX   19  19 SER B  109  ASN B  130  1                                  22    
HELIX   20  20 LYS B  138  GLU B  140  5                                   3    
HELIX   21  21 THR B  177  LEU B  181  5                                   5    
HELIX   22  22 SER B  182  ARG B  187  1                                   6    
HELIX   23  23 LYS B  193  GLY B  210  1                                  18    
HELIX   24  24 ASP B  218  ALA B  228  1                                  11    
HELIX   25  25 THR B  242  LEU B  253  1                                  12    
HELIX   26  26 THR B  262  LEU B  267  1                                   6    
HELIX   27  27 HIS B  269  GLN B  274  1                                   6    
HELIX   28  28 GLN B  274  ALA B  279  1                                   6    
HELIX   29  29 ARG B  284  LEU B  300  1                                  17    
SHEET    1  AA 5 TYR A  14  LYS A  22  0                                        
SHEET    2  AA 5 SER A  26  LYS A  33 -1  O  VAL A  28   N  LEU A  20           
SHEET    3  AA 5 GLU A  39  ASN A  46 -1  O  TYR A  40   N  CYS A  31           
SHEET    4  AA 5 PHE A  85  ASP A  91 -1  O  HIS A  86   N  ILE A  45           
SHEET    5  AA 5 LEU A  76  GLU A  82 -1  N  HIS A  77   O  VAL A  89           
SHEET    1  AB 2 ILE A 132  VAL A 133  0                                        
SHEET    2  AB 2 ILE A 162  GLU A 163 -1  O  ILE A 162   N  VAL A 133           
SHEET    1  AC 2 LEU A 142  LEU A 144  0                                        
SHEET    2  AC 2 VAL A 153  LEU A 155 -1  O  LYS A 154   N  LEU A 143           
SHEET    1  BA 5 TYR B  14  LYS B  22  0                                        
SHEET    2  BA 5 SER B  26  LYS B  33 -1  O  VAL B  28   N  LEU B  20           
SHEET    3  BA 5 GLU B  39  ASN B  46 -1  O  TYR B  40   N  CYS B  31           
SHEET    4  BA 5 PHE B  85  ASP B  91 -1  O  HIS B  86   N  ILE B  45           
SHEET    5  BA 5 LEU B  76  GLU B  82 -1  N  HIS B  77   O  VAL B  89           
SHEET    1  BB 2 ILE B 132  VAL B 133  0                                        
SHEET    2  BB 2 ILE B 162  GLU B 163 -1  O  ILE B 162   N  VAL B 133           
SHEET    1  BC 2 LEU B 142  LEU B 144  0                                        
SHEET    2  BC 2 VAL B 153  LEU B 155 -1  O  LYS B 154   N  LEU B 143           
CISPEP   1 ILE A   34    PRO A   35          0        -3.92                     
CISPEP   2 SER A  235    PRO A  236          0        -0.64                     
CISPEP   3 ILE B   34    PRO B   35          0        -5.67                     
CISPEP   4 SER B  235    PRO B  236          0         0.43                     
SITE     1 AC1  9 LEU B  20  LYS B  22  ALA B  41  LYS B  43                    
SITE     2 AC1  9 ASP B  91  LEU B  92  VAL B  93  ASP B 157                    
SITE     3 AC1  9 PO4 B1312                                                     
SITE     1 AC2 11 LEU A  20  LYS A  22  VAL A  28  ALA A  41                    
SITE     2 AC2 11 LYS A  43  PHE A  90  ASP A  91  LEU A  92                    
SITE     3 AC2 11 VAL A  93  ASP A 157  PO4 A1311                               
SITE     1 AC3  9 THR A  47  HIS A  55  SER A  81  GLU A  82                    
SITE     2 AC3  9 PHE A  85  HIS A  86  SER A 148  LYS A 149                    
SITE     3 AC3  9 HOH A2072                                                     
SITE     1 AC4  8 THR B  47  HIS B  55  SER B  81  GLU B  82                    
SITE     2 AC4  8 PHE B  85  HIS B  86  SER B 148  LYS B 149                    
SITE     1 AC5  2 LEU B  20  GVD B1310                                          
SITE     1 AC6  4 LEU A  20  GLY A  21  GVD A1314  HOH A2073                    
SITE     1 AC7  2 ARG A  75  HIS A  77                                          
SITE     1 AC8  8 TYR A 107  SER A 109  ALA A 111  ASP A 112                    
SITE     2 AC8  8 ARG A 275  SER A 276  MET A 281  HOH A2029                    
CRYST1   68.276   68.276  313.450  90.00  90.00 120.00 P 32 2 1     12          
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      0.014646  0.008456  0.000000        0.00000                         
SCALE2      0.000000  0.016912  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003190        0.00000                         
MTRIX1   1 -0.501000 -0.820000  0.275000       13.43522    1                    
MTRIX2   1 -0.865000  0.480000 -0.145000       58.73976    1                    
MTRIX3   1 -0.013000 -0.311000 -0.950000       58.85304    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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