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Database: PDB
Entry: 2V5Q
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Original site: 2V5Q 
HEADER    TRANSFERASE                             08-JUL-07   2V5Q              
TITLE     CRYSTAL STRUCTURE OF WILD-TYPE PLK-1 KINASE DOMAIN IN                 
TITLE    2 COMPLEX WITH A SELECTIVE DARPIN                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 33-345;                            
COMPND   5 SYNONYM: PLK-1, SERINE/THREONINE-PROTEIN KINASE 13, STPK13,          
COMPND   6  POLO-LIKE KINASE 1, HUMAN POLO-LIKE KINASE 1;                       
COMPND   7 EC: 2.7.11.21;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 OTHER_DETAILS: CONSTRUCT 4;                                          
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: DESIGN ANKYRIN REPEAT PROTEIN;                             
COMPND  12 CHAIN: C, D;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: VARIANT 3H10                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: UNIDENTIFIED;                                   
SOURCE   9 ORGANISM_TAXID: 32644;                                               
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 OTHER_DETAILS: DESIGNED PROTEIN                                      
KEYWDS    DESIGN ANKYRIN REPEAT PROTEIN, TRANSFERASE COMPLEX, PHOSPHORYLATION,  
KEYWDS   2 NUCLEOTIDE-BINDING, SERINE/THREONINE-PROTEIN KINASE, KINASE,         
KEYWDS   3 NUCLEUS, TRANSFERASE, ATP-BINDING, SERINE/THREONINE PROTEIN KINASE   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.M.BANDEIRAS,R.C.HILLIG,P.M.MATIAS,U.EBERSPAECHER,J.FANGHAENEL,      
AUTHOR   2 M.THOMAZ,S.MIRANDA,K.CRUSIUS,V.PUETTER,P.AMSTUTZ,                    
AUTHOR   3 M.GULOTTI-GEORGIEVA,H.K.BINZ,C.HOLZ,A.A.P.SCHMITZ,C.LANG,P.DONNER,   
AUTHOR   4 U.EGNER,M.A.CARRONDO,B.MUELLER-TIEMANN                               
REVDAT   3   13-JUL-11 2V5Q    1       VERSN                                    
REVDAT   2   24-FEB-09 2V5Q    1       VERSN                                    
REVDAT   1   01-APR-08 2V5Q    0                                                
JRNL        AUTH   T.M.BANDEIRAS,R.C.HILLIG,P.M.MATIAS,U.EBERSPAECHER,          
JRNL        AUTH 2 J.FANGHAENEL,M.THOMAZ,S.MIRANDA,K.CRUSIUS,V.PUETTER,         
JRNL        AUTH 3 P.AMSTUTZ,M.GULOTTI-GEORGIEVA,H.K.BINZ,C.HOLZ,A.A.P.SCHMITZ, 
JRNL        AUTH 4 C.LANG,P.DONNER,U.EGNER,M.A.CARRONDO,B.MUELLER-TIEMANN       
JRNL        TITL   STRUCTURE PF WILD-TYPE PLK-1 KINASE DOMAIN IN COMPLEX WITH   
JRNL        TITL 2 A SELECTIVE DARPIN                                           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  64   339 2008              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   18391401                                                     
JRNL        DOI    10.1107/S0907444907068217                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0037                                      
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) : 61.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 49051                          
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) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.182                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2601                            
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) : 3580                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 172                          
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6523                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 406                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 45.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.28                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.07000                                              
REMARK   3    B22 (A**2) : -1.87000                                             
REMARK   3    B33 (A**2) : 0.80000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.245         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.198         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.145         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.227        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.950                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6697 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9072 ; 1.265 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   833 ; 5.952 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   298 ;35.477 ;23.490       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1188 ;15.116 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    49 ;18.875 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1036 ; 0.087 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5019 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  3169 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4572 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   453 ; 0.144 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    40 ; 0.207 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    14 ; 0.162 ; 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):  4262 ; 1.615 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6691 ; 2.800 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2691 ; 5.214 ; 9.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2377 ; 7.068 ;12.000       
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  : 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    45        A   131                          
REMARK   3    ORIGIN FOR THE GROUP (A): -14.7900  29.1250  33.1390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1241 T22:   0.0725                                     
REMARK   3      T33:   0.1671 T12:   0.0763                                     
REMARK   3      T13:  -0.0216 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6756 L22:   3.0215                                     
REMARK   3      L33:   5.9214 L12:  -2.2970                                     
REMARK   3      L13:  -3.5416 L23:  -1.1850                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0418 S12:  -0.3611 S13:  -0.1878                       
REMARK   3      S21:   0.4811 S22:   0.2548 S23:   0.9448                       
REMARK   3      S31:  -0.4088 S32:  -0.5455 S33:  -0.2130                       
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   132        A   323                          
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0670  32.4140  28.8270              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2267 T22:  -0.1560                                     
REMARK   3      T33:  -0.2206 T12:   0.0852                                     
REMARK   3      T13:   0.0149 T23:  -0.0615                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5273 L22:   3.1399                                     
REMARK   3      L33:   2.1696 L12:   0.0644                                     
REMARK   3      L13:   0.2201 L23:   0.1300                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0387 S12:  -0.1407 S13:   0.1577                       
REMARK   3      S21:  -0.0875 S22:   0.0795 S23:  -0.2592                       
REMARK   3      S31:  -0.2076 S32:   0.0773 S33:  -0.0407                       
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 :   B    45        B   131                          
REMARK   3    ORIGIN FOR THE GROUP (A):  30.6530  -1.5770  10.7100              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1103 T22:   0.1953                                     
REMARK   3      T33:   0.1191 T12:   0.1118                                     
REMARK   3      T13:   0.0308 T23:   0.0200                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8270 L22:   9.4992                                     
REMARK   3      L33:   1.4472 L12:  -5.3070                                     
REMARK   3      L13:  -2.4114 L23:   1.1887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1891 S12:  -0.3782 S13:  -0.7550                       
REMARK   3      S21:  -0.0832 S22:   0.1317 S23:  -0.5104                       
REMARK   3      S31:   0.3984 S32:   0.5704 S33:   0.0574                       
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   132        B   323                          
REMARK   3    ORIGIN FOR THE GROUP (A):  11.4680  12.1320   2.1410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1183 T22:  -0.2196                                     
REMARK   3      T33:  -0.1976 T12:   0.0385                                     
REMARK   3      T13:   0.1146 T23:  -0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4006 L22:   2.7190                                     
REMARK   3      L33:   2.6390 L12:   0.6165                                     
REMARK   3      L13:  -0.3271 L23:  -0.5671                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1086 S12:   0.1410 S13:  -0.1117                       
REMARK   3      S21:  -0.4210 S22:   0.1813 S23:  -0.1760                       
REMARK   3      S31:  -0.1658 S32:   0.0279 S33:  -0.0726                       
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 :   C    13        C   141                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.9580 -13.7140  17.7940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1803 T22:  -0.2275                                     
REMARK   3      T33:  -0.0968 T12:   0.0160                                     
REMARK   3      T13:  -0.0160 T23:   0.0711                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7395 L22:   3.1828                                     
REMARK   3      L33:   4.1490 L12:   0.7043                                     
REMARK   3      L13:  -0.2374 L23:   0.8409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0557 S12:   0.0616 S13:  -0.3610                       
REMARK   3      S21:   0.0332 S22:  -0.1063 S23:   0.0727                       
REMARK   3      S31:   0.1993 S32:  -0.2828 S33:   0.0506                       
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 :   D    14        D   141                          
REMARK   3    ORIGIN FOR THE GROUP (A):   6.4910   7.3110  50.3620              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1269 T22:  -0.0324                                     
REMARK   3      T33:  -0.1541 T12:   0.0837                                     
REMARK   3      T13:  -0.1111 T23:   0.0678                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4394 L22:   7.0708                                     
REMARK   3      L33:   3.8178 L12:   0.2042                                     
REMARK   3      L13:   0.2423 L23:   1.4234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1239 S12:  -0.4054 S13:  -0.1728                       
REMARK   3      S21:   1.2007 S22:   0.1309 S23:  -0.4975                       
REMARK   3      S31:   0.4983 S32:   0.0303 S33:  -0.2547                       
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   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS.                                                   
REMARK   4                                                                      
REMARK   4 2V5Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  09-JUL-07.                 
REMARK 100 THE PDBE ID CODE IS EBI-33146.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.037                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 51702                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.30                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 96.20                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NONE                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.06                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.70                              
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     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.6                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.40                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.30                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 1.3                                            
REMARK 200 STARTING MODEL: PLK-1 - HOMOLOGY MODEL FROM PDB ENTRY 1OL5           
REMARK 200 DARPIN 3H10 - PDB ENTRY 1MJ0 TRUNCATED AFTER RESIDUE 141             
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL PH 8.0, 8% PEG            
REMARK 280  5000 MME, 0.01 M EDTA SODIUM SALT AT 303 K.                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
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       31.16450            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.41200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.61250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.41200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       31.16450            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.61250            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1960 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.7 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE:  2                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 TOTAL BURIED SURFACE AREA: 1920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23400 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.5 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    31                                                      
REMARK 465     SER A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     ALA A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     LYS A    38                                                      
REMARK 465     ARG A   324                                                      
REMARK 465     PHE A   325                                                      
REMARK 465     SER A   326                                                      
REMARK 465     ILE A   327                                                      
REMARK 465     ALA A   328                                                      
REMARK 465     PRO A   329                                                      
REMARK 465     SER A   330                                                      
REMARK 465     SER A   331                                                      
REMARK 465     LEU A   332                                                      
REMARK 465     ASP A   333                                                      
REMARK 465     PRO A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     ASN A   336                                                      
REMARK 465     ARG A   337                                                      
REMARK 465     LYS A   338                                                      
REMARK 465     PRO A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     THR A   341                                                      
REMARK 465     VAL A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     ASN A   344                                                      
REMARK 465     LYS A   345                                                      
REMARK 465     GLY B    31                                                      
REMARK 465     SER B    32                                                      
REMARK 465     ALA B    33                                                      
REMARK 465     ALA B    34                                                      
REMARK 465     PRO B    35                                                      
REMARK 465     PRO B    36                                                      
REMARK 465     ALA B    37                                                      
REMARK 465     LYS B    38                                                      
REMARK 465     ARG B   324                                                      
REMARK 465     PHE B   325                                                      
REMARK 465     SER B   326                                                      
REMARK 465     ILE B   327                                                      
REMARK 465     ALA B   328                                                      
REMARK 465     PRO B   329                                                      
REMARK 465     SER B   330                                                      
REMARK 465     SER B   331                                                      
REMARK 465     LEU B   332                                                      
REMARK 465     ASP B   333                                                      
REMARK 465     PRO B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     ASN B   336                                                      
REMARK 465     ARG B   337                                                      
REMARK 465     LYS B   338                                                      
REMARK 465     PRO B   339                                                      
REMARK 465     LEU B   340                                                      
REMARK 465     THR B   341                                                      
REMARK 465     VAL B   342                                                      
REMARK 465     LEU B   343                                                      
REMARK 465     ASN B   344                                                      
REMARK 465     LYS B   345                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ARG C     2                                                      
REMARK 465     GLY C     3                                                      
REMARK 465     SER C     4                                                      
REMARK 465     HIS C     5                                                      
REMARK 465     HIS C     6                                                      
REMARK 465     HIS C     7                                                      
REMARK 465     HIS C     8                                                      
REMARK 465     HIS C     9                                                      
REMARK 465     HIS C    10                                                      
REMARK 465     GLY C    11                                                      
REMARK 465     GLN C   142                                                      
REMARK 465     ASP C   143                                                      
REMARK 465     LYS C   144                                                      
REMARK 465     PHE C   145                                                      
REMARK 465     GLY C   146                                                      
REMARK 465     LYS C   147                                                      
REMARK 465     THR C   148                                                      
REMARK 465     ALA C   149                                                      
REMARK 465     PHE C   150                                                      
REMARK 465     ASP C   151                                                      
REMARK 465     ILE C   152                                                      
REMARK 465     SER C   153                                                      
REMARK 465     ILE C   154                                                      
REMARK 465     ASP C   155                                                      
REMARK 465     ASN C   156                                                      
REMARK 465     GLY C   157                                                      
REMARK 465     ASN C   158                                                      
REMARK 465     GLU C   159                                                      
REMARK 465     ASP C   160                                                      
REMARK 465     LEU C   161                                                      
REMARK 465     ALA C   162                                                      
REMARK 465     LYS C   163                                                      
REMARK 465     SER C   164                                                      
REMARK 465     CYS C   165                                                      
REMARK 465     ARG C   166                                                      
REMARK 465     ASN C   167                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ARG D     2                                                      
REMARK 465     GLY D     3                                                      
REMARK 465     SER D     4                                                      
REMARK 465     HIS D     5                                                      
REMARK 465     HIS D     6                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HIS D     8                                                      
REMARK 465     HIS D     9                                                      
REMARK 465     HIS D    10                                                      
REMARK 465     GLY D    11                                                      
REMARK 465     SER D    12                                                      
REMARK 465     GLN D   142                                                      
REMARK 465     ASP D   143                                                      
REMARK 465     LYS D   144                                                      
REMARK 465     PHE D   145                                                      
REMARK 465     GLY D   146                                                      
REMARK 465     LYS D   147                                                      
REMARK 465     THR D   148                                                      
REMARK 465     ALA D   149                                                      
REMARK 465     PHE D   150                                                      
REMARK 465     ASP D   151                                                      
REMARK 465     ILE D   152                                                      
REMARK 465     SER D   153                                                      
REMARK 465     ILE D   154                                                      
REMARK 465     ASP D   155                                                      
REMARK 465     ASN D   156                                                      
REMARK 465     GLY D   157                                                      
REMARK 465     ASN D   158                                                      
REMARK 465     GLU D   159                                                      
REMARK 465     ASP D   160                                                      
REMARK 465     LEU D   161                                                      
REMARK 465     ALA D   162                                                      
REMARK 465     LYS D   163                                                      
REMARK 465     SER D   164                                                      
REMARK 465     CYS D   165                                                      
REMARK 465     ARG D   166                                                      
REMARK 465     ASN D   167                                                      
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     ARG A  95    NE   CZ   NH1  NH2                                  
REMARK 470     ARG A 207    NH2                                                 
REMARK 470     LYS A 248    CE   NZ                                             
REMARK 470     LYS A 264    CD   CE   NZ                                        
REMARK 470     LYS A 272    NZ                                                  
REMARK 470     ARG B  50    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  52    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP B  74    CG   OD1  OD2                                       
REMARK 470     LYS B  97    CE   NZ                                             
REMARK 470     LYS B 248    CD   CE   NZ                                        
REMARK 470     LYS D  16    NZ                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG D  31   CZ    ARG D  31   NH1     0.189                       
REMARK 500    ARG D  31   CZ    ARG D  31   NH2     0.079                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 144   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    ARG D  31   NE  -  CZ  -  NH2 ANGL. DEV. =  -9.4 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    ARG A  50       -4.64     79.04                                   
REMARK 500    LYS A  91     -143.60     60.39                                   
REMARK 500    PRO A  92      -87.64    -53.58                                   
REMARK 500    ASP A 122     -167.48   -113.22                                   
REMARK 500    ARG A 136     -137.13     59.96                                   
REMARK 500    LYS A 146     -122.64     59.72                                   
REMARK 500    ASP A 176       40.95   -154.36                                   
REMARK 500    ASP A 194       75.17     62.93                                   
REMARK 500    SER A 229     -152.37   -146.53                                   
REMARK 500    THR A 320      -40.93   -135.56                                   
REMARK 500    PRO B  41      153.99    -49.10                                   
REMARK 500    ARG B  50       55.10     33.00                                   
REMARK 500    ARG B  57      130.41    -38.27                                   
REMARK 500    ASP B 122     -157.90   -116.41                                   
REMARK 500    ARG B 136     -134.50     60.59                                   
REMARK 500    LYS B 146     -130.29     50.59                                   
REMARK 500    ASP B 176       38.34   -149.14                                   
REMARK 500    ASP B 194       77.54     60.96                                   
REMARK 500    PHE B 195       32.21    -92.83                                   
REMARK 500    LYS B 209      -67.01   -136.92                                   
REMARK 500    SER B 229     -153.04   -156.28                                   
REMARK 500    THR B 320      -36.94   -130.87                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A   91     PRO A   92                 -124.78                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS A  91        18.8      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1Q4K   RELATED DB: PDB                                   
REMARK 900  THE POLO-BOX DOMAIN OF PLK1 IN COMPLEX                              
REMARK 900  WITH A PHOSPHO-PEPTIDE                                              
REMARK 900 RELATED ID: 1Q4O   RELATED DB: PDB                                   
REMARK 900  THE STRUCTURE OF THE POLO BOX DOMAIN OF                             
REMARK 900  HUMAN PLK1                                                          
REMARK 900 RELATED ID: 1UMW   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF A HUMAN PLK1 POLO-BOX DOMAIN                           
REMARK 900  /PHOSPHOPEPTIDE COMPLEX                                             
DBREF  2V5Q A   31    32  PDB    2V5Q     2V5Q            31     32             
DBREF  2V5Q A   33   345  UNP    P53350   PLK1_HUMAN      33    345             
DBREF  2V5Q B   31    32  PDB    2V5Q     2V5Q            31     32             
DBREF  2V5Q B   33   345  UNP    P53350   PLK1_HUMAN      33    345             
DBREF  2V5Q C    1   167  PDB    2V5Q     2V5Q             1    167             
DBREF  2V5Q D    1   167  PDB    2V5Q     2V5Q             1    167             
SEQRES   1 A  315  GLY SER ALA ALA PRO PRO ALA LYS GLU ILE PRO GLU VAL          
SEQRES   2 A  315  LEU VAL ASP PRO ARG SER ARG ARG ARG TYR VAL ARG GLY          
SEQRES   3 A  315  ARG PHE LEU GLY LYS GLY GLY PHE ALA LYS CYS PHE GLU          
SEQRES   4 A  315  ILE SER ASP ALA ASP THR LYS GLU VAL PHE ALA GLY LYS          
SEQRES   5 A  315  ILE VAL PRO LYS SER LEU LEU LEU LYS PRO HIS GLN ARG          
SEQRES   6 A  315  GLU LYS MET SER MET GLU ILE SER ILE HIS ARG SER LEU          
SEQRES   7 A  315  ALA HIS GLN HIS VAL VAL GLY PHE HIS GLY PHE PHE GLU          
SEQRES   8 A  315  ASP ASN ASP PHE VAL PHE VAL VAL LEU GLU LEU CYS ARG          
SEQRES   9 A  315  ARG ARG SER LEU LEU GLU LEU HIS LYS ARG ARG LYS ALA          
SEQRES  10 A  315  LEU THR GLU PRO GLU ALA ARG TYR TYR LEU ARG GLN ILE          
SEQRES  11 A  315  VAL LEU GLY CYS GLN TYR LEU HIS ARG ASN ARG VAL ILE          
SEQRES  12 A  315  HIS ARG ASP LEU LYS LEU GLY ASN LEU PHE LEU ASN GLU          
SEQRES  13 A  315  ASP LEU GLU VAL LYS ILE GLY ASP PHE GLY LEU ALA THR          
SEQRES  14 A  315  LYS VAL GLU TYR ASP GLY GLU ARG LYS LYS THR LEU CYS          
SEQRES  15 A  315  GLY THR PRO ASN TYR ILE ALA PRO GLU VAL LEU SER LYS          
SEQRES  16 A  315  LYS GLY HIS SER PHE GLU VAL ASP VAL TRP SER ILE GLY          
SEQRES  17 A  315  CYS ILE MET TYR THR LEU LEU VAL GLY LYS PRO PRO PHE          
SEQRES  18 A  315  GLU THR SER CYS LEU LYS GLU THR TYR LEU ARG ILE LYS          
SEQRES  19 A  315  LYS ASN GLU TYR SER ILE PRO LYS HIS ILE ASN PRO VAL          
SEQRES  20 A  315  ALA ALA SER LEU ILE GLN LYS MET LEU GLN THR ASP PRO          
SEQRES  21 A  315  THR ALA ARG PRO THR ILE ASN GLU LEU LEU ASN ASP GLU          
SEQRES  22 A  315  PHE PHE THR SER GLY TYR ILE PRO ALA ARG LEU PRO ILE          
SEQRES  23 A  315  THR CYS LEU THR ILE PRO PRO ARG PHE SER ILE ALA PRO          
SEQRES  24 A  315  SER SER LEU ASP PRO SER ASN ARG LYS PRO LEU THR VAL          
SEQRES  25 A  315  LEU ASN LYS                                                  
SEQRES   1 B  315  GLY SER ALA ALA PRO PRO ALA LYS GLU ILE PRO GLU VAL          
SEQRES   2 B  315  LEU VAL ASP PRO ARG SER ARG ARG ARG TYR VAL ARG GLY          
SEQRES   3 B  315  ARG PHE LEU GLY LYS GLY GLY PHE ALA LYS CYS PHE GLU          
SEQRES   4 B  315  ILE SER ASP ALA ASP THR LYS GLU VAL PHE ALA GLY LYS          
SEQRES   5 B  315  ILE VAL PRO LYS SER LEU LEU LEU LYS PRO HIS GLN ARG          
SEQRES   6 B  315  GLU LYS MET SER MET GLU ILE SER ILE HIS ARG SER LEU          
SEQRES   7 B  315  ALA HIS GLN HIS VAL VAL GLY PHE HIS GLY PHE PHE GLU          
SEQRES   8 B  315  ASP ASN ASP PHE VAL PHE VAL VAL LEU GLU LEU CYS ARG          
SEQRES   9 B  315  ARG ARG SER LEU LEU GLU LEU HIS LYS ARG ARG LYS ALA          
SEQRES  10 B  315  LEU THR GLU PRO GLU ALA ARG TYR TYR LEU ARG GLN ILE          
SEQRES  11 B  315  VAL LEU GLY CYS GLN TYR LEU HIS ARG ASN ARG VAL ILE          
SEQRES  12 B  315  HIS ARG ASP LEU LYS LEU GLY ASN LEU PHE LEU ASN GLU          
SEQRES  13 B  315  ASP LEU GLU VAL LYS ILE GLY ASP PHE GLY LEU ALA THR          
SEQRES  14 B  315  LYS VAL GLU TYR ASP GLY GLU ARG LYS LYS THR LEU CYS          
SEQRES  15 B  315  GLY THR PRO ASN TYR ILE ALA PRO GLU VAL LEU SER LYS          
SEQRES  16 B  315  LYS GLY HIS SER PHE GLU VAL ASP VAL TRP SER ILE GLY          
SEQRES  17 B  315  CYS ILE MET TYR THR LEU LEU VAL GLY LYS PRO PRO PHE          
SEQRES  18 B  315  GLU THR SER CYS LEU LYS GLU THR TYR LEU ARG ILE LYS          
SEQRES  19 B  315  LYS ASN GLU TYR SER ILE PRO LYS HIS ILE ASN PRO VAL          
SEQRES  20 B  315  ALA ALA SER LEU ILE GLN LYS MET LEU GLN THR ASP PRO          
SEQRES  21 B  315  THR ALA ARG PRO THR ILE ASN GLU LEU LEU ASN ASP GLU          
SEQRES  22 B  315  PHE PHE THR SER GLY TYR ILE PRO ALA ARG LEU PRO ILE          
SEQRES  23 B  315  THR CYS LEU THR ILE PRO PRO ARG PHE SER ILE ALA PRO          
SEQRES  24 B  315  SER SER LEU ASP PRO SER ASN ARG LYS PRO LEU THR VAL          
SEQRES  25 B  315  LEU ASN LYS                                                  
SEQRES   1 C  167  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 C  167  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 C  167  ASP ASP GLU VAL ARG ILE LEU ILE ALA ASN GLY ALA ASP          
SEQRES   4 C  167  VAL ASN ALA VAL ASP ASN THR GLY LEU THR PRO LEU HIS          
SEQRES   5 C  167  LEU ALA ALA VAL SER GLY HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 C  167  LEU LEU LYS HIS GLY ALA ASP VAL ASP ALA ALA ASP VAL          
SEQRES   7 C  167  TYR GLY PHE THR PRO LEU HIS LEU ALA ALA MET THR GLY          
SEQRES   8 C  167  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA          
SEQRES   9 C  167  ASP VAL ASN ALA PHE ASP MET THR GLY SER THR PRO LEU          
SEQRES  10 C  167  HIS LEU ALA ALA ASP GLU GLY HIS LEU GLU ILE VAL GLU          
SEQRES  11 C  167  VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLN ASP          
SEQRES  12 C  167  LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASP ASN          
SEQRES  13 C  167  GLY ASN GLU ASP LEU ALA LYS SER CYS ARG ASN                  
SEQRES   1 D  167  MET ARG GLY SER HIS HIS HIS HIS HIS HIS GLY SER ASP          
SEQRES   2 D  167  LEU GLY LYS LYS LEU LEU GLU ALA ALA ARG ALA GLY GLN          
SEQRES   3 D  167  ASP ASP GLU VAL ARG ILE LEU ILE ALA ASN GLY ALA ASP          
SEQRES   4 D  167  VAL ASN ALA VAL ASP ASN THR GLY LEU THR PRO LEU HIS          
SEQRES   5 D  167  LEU ALA ALA VAL SER GLY HIS LEU GLU ILE VAL GLU VAL          
SEQRES   6 D  167  LEU LEU LYS HIS GLY ALA ASP VAL ASP ALA ALA ASP VAL          
SEQRES   7 D  167  TYR GLY PHE THR PRO LEU HIS LEU ALA ALA MET THR GLY          
SEQRES   8 D  167  HIS LEU GLU ILE VAL GLU VAL LEU LEU LYS TYR GLY ALA          
SEQRES   9 D  167  ASP VAL ASN ALA PHE ASP MET THR GLY SER THR PRO LEU          
SEQRES  10 D  167  HIS LEU ALA ALA ASP GLU GLY HIS LEU GLU ILE VAL GLU          
SEQRES  11 D  167  VAL LEU LEU LYS TYR GLY ALA ASP VAL ASN ALA GLN ASP          
SEQRES  12 D  167  LYS PHE GLY LYS THR ALA PHE ASP ILE SER ILE ASP ASN          
SEQRES  13 D  167  GLY ASN GLU ASP LEU ALA LYS SER CYS ARG ASN                  
FORMUL   5  HOH   *406(H2 O)                                                    
HELIX    1   1 SER A   87  LEU A   89  5                                   3    
HELIX    2   2 LYS A   91  SER A  107  1                                  17    
HELIX    3   3 SER A  137  LYS A  146  1                                  10    
HELIX    4   4 THR A  149  ASN A  170  1                                  22    
HELIX    5   5 LYS A  178  GLY A  180  5                                   3    
HELIX    6   6 ALA A  219  SER A  224  1                                   6    
HELIX    7   7 PHE A  230  GLY A  247  1                                  18    
HELIX    8   8 CYS A  255  ASN A  266  1                                  12    
HELIX    9   9 ASN A  275  LEU A  286  1                                  12    
HELIX   10  10 ASP A  289  ARG A  293  5                                   5    
HELIX   11  11 THR A  295  ASN A  301  1                                   7    
HELIX   12  12 ASP A  302  SER A  307  1                                   6    
HELIX   13  13 PRO A  315  THR A  320  5                                   6    
HELIX   14  14 SER B   87  LEU B   89  5                                   3    
HELIX   15  15 LYS B   91  ARG B  106  1                                  16    
HELIX   16  16 SER B  137  LYS B  146  1                                  10    
HELIX   17  17 THR B  149  ASN B  170  1                                  22    
HELIX   18  18 LYS B  178  GLY B  180  5                                   3    
HELIX   19  19 ALA B  219  SER B  224  1                                   6    
HELIX   20  20 PHE B  230  GLY B  247  1                                  18    
HELIX   21  21 CYS B  255  ASN B  266  1                                  12    
HELIX   22  22 ASN B  275  LEU B  286  1                                  12    
HELIX   23  23 ASP B  289  ARG B  293  5                                   5    
HELIX   24  24 THR B  295  ASN B  301  1                                   7    
HELIX   25  25 ASP B  302  SER B  307  1                                   6    
HELIX   26  26 PRO B  315  THR B  320  5                                   6    
HELIX   27  27 SER C   12  GLY C   25  1                                  14    
HELIX   28  28 GLN C   26  ASN C   36  1                                  11    
HELIX   29  29 THR C   49  SER C   57  1                                   9    
HELIX   30  30 HIS C   59  HIS C   69  1                                  11    
HELIX   31  31 THR C   82  GLY C   91  1                                  10    
HELIX   32  32 HIS C   92  TYR C  102  1                                  11    
HELIX   33  33 THR C  115  GLU C  123  1                                   9    
HELIX   34  34 HIS C  125  TYR C  135  1                                  11    
HELIX   35  35 ASP D   13  GLY D   25  1                                  13    
HELIX   36  36 GLN D   26  ASN D   36  1                                  11    
HELIX   37  37 THR D   49  GLY D   58  1                                  10    
HELIX   38  38 HIS D   59  HIS D   69  1                                  11    
HELIX   39  39 THR D   82  GLY D   91  1                                  10    
HELIX   40  40 HIS D   92  TYR D  102  1                                  11    
HELIX   41  41 THR D  115  GLU D  123  1                                   9    
HELIX   42  42 HIS D  125  TYR D  135  1                                  11    
SHEET    1  AA 6 VAL A  43  VAL A  45  0                                        
SHEET    2  AA 6 ARG A  52  GLY A  62 -1  O  TYR A  53   N  LEU A  44           
SHEET    3  AA 6 ALA A  65  ASP A  72 -1  O  ALA A  65   N  GLY A  62           
SHEET    4  AA 6 VAL A  78  PRO A  85 -1  O  PHE A  79   N  ILE A  70           
SHEET    5  AA 6 PHE A 125  LEU A 130 -1  O  VAL A 126   N  VAL A  84           
SHEET    6  AA 6 PHE A 116  GLU A 121 -1  N  HIS A 117   O  VAL A 129           
SHEET    1  AB 2 VAL A 172  ILE A 173  0                                        
SHEET    2  AB 2 THR A 199  LYS A 200 -1  O  THR A 199   N  ILE A 173           
SHEET    1  AC 2 LEU A 182  LEU A 184  0                                        
SHEET    2  AC 2 VAL A 190  ILE A 192 -1  O  LYS A 191   N  PHE A 183           
SHEET    1  BA 6 VAL B  43  ASP B  46  0                                        
SHEET    2  BA 6 ARG B  51  GLY B  62 -1  O  ARG B  51   N  ASP B  46           
SHEET    3  BA 6 ALA B  65  ASP B  72 -1  O  ALA B  65   N  GLY B  62           
SHEET    4  BA 6 VAL B  78  PRO B  85 -1  O  PHE B  79   N  ILE B  70           
SHEET    5  BA 6 PHE B 125  LEU B 130 -1  O  VAL B 126   N  VAL B  84           
SHEET    6  BA 6 PHE B 116  GLU B 121 -1  N  HIS B 117   O  VAL B 129           
SHEET    1  BB 2 VAL B 172  ILE B 173  0                                        
SHEET    2  BB 2 THR B 199  LYS B 200 -1  O  THR B 199   N  ILE B 173           
SHEET    1  BC 2 LEU B 182  LEU B 184  0                                        
SHEET    2  BC 2 VAL B 190  ILE B 192 -1  O  LYS B 191   N  PHE B 183           
CRYST1   62.329  135.225  136.824  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016044  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007395  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007309        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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