GenomeNet

Database: PDB
Entry: 3C5L
LinkDB: 3C5L
Original site: 3C5L 
HEADER    TRANSFERASE                             31-JAN-08   3C5L              
TITLE     POLO-LIKE KINASE 1 POLO BOX DOMAIN IN COMPLEX WITH PPHSPT             
TITLE    2 PEPTIDE                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PLK1;                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: POLO BOX 1, POLO BOX 2, UNP RESIDUES 373-593;              
COMPND   5 SYNONYM: POLO-LIKE KINASE 1, PLK-1, SERINE/THREONINE-                
COMPND   6 PROTEIN KINASE 13, STPK13;                                           
COMPND   7 EC: 2.7.11.21;                                                       
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PEPTIDE;                                                   
COMPND  11 CHAIN: B;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PLK1, PLK;                                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA 2;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES                                                       
KEYWDS    PLK1, POLO-LIKE KINASE 1, POLO BOX DOMAIN, PHOSPHOPEPTIDE,            
KEYWDS   2 ATP-BINDING, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN,            
KEYWDS   3 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.C.LIM,M.B.YAFFE                                                     
REVDAT   2   25-AUG-09 3C5L    1       JRNL                                     
REVDAT   1   17-FEB-09 3C5L    0                                                
JRNL        AUTH   S.M.YUN,T.MOULAEI,D.LIM,J.K.BANG,J.E.PARK,                   
JRNL        AUTH 2 S.R.SHENOY,F.LIU,Y.H.KANG,C.LIAO,N.K.SOUNG,S.LEE,            
JRNL        AUTH 3 D.Y.YOON,Y.LIM,D.H.LEE,A.OTAKA,E.APPELLA,                    
JRNL        AUTH 4 J.B.MCMAHON,M.C.NICKLAUS,T.R.BURKE,M.B.YAFFE,                
JRNL        AUTH 5 A.WLODAWER,K.S.LEE                                           
JRNL        TITL   STRUCTURAL AND FUNCTIONAL ANALYSES OF MINIMAL                
JRNL        TITL 2 PHOSPHOPEPTIDES TARGETING THE POLO-BOX DOMAIN OF             
JRNL        TITL 3 POLO-LIKE KINASE 1.                                          
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  16   876 2009              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   19597481                                                     
JRNL        DOI    10.1038/NSMB.1628                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.33 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.33                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.61                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 612513.780                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 91.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 10186                          
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 SET) : 0.246                           
REMARK   3   FREE R VALUE                     : 0.293                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 529                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.013                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.33                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.48                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 59.70                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1032                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3500                       
REMARK   3   BIN FREE R VALUE                    : 0.4480                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.50                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 49                           
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.064                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1810                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 35                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.45000                                              
REMARK   3    B22 (A**2) : 10.38000                                             
REMARK   3    B33 (A**2) : -12.83000                                            
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.35                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.45                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.20                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.94                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.850 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.760 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.670 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 3.710 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.37                                                 
REMARK   3   BSOL        : 40.26                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3C5L COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-FEB-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB046369.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-AUG-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10764                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.330                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 5.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY                : 6.200                              
REMARK 200  R MERGE                    (I) : 0.05100                            
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 27.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.33                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.41                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.26800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.26800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: EPMR                                                  
REMARK 200 STARTING MODEL: PDB ENTRY 1UMW, CHAIN A                              
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.28                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.38                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350, PH 6, VAPOR DIFFUSION,          
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
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       17.72100            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       52.90850            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       33.24750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       52.90850            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.72100            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       33.24750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: 1                                                            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 820 ANGSTROM**2                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASP A   503                                                      
REMARK 465     GLU A   504                                                      
REMARK 465     LEU A   505                                                      
REMARK 465     ALA A   506                                                      
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    GLU A 391       41.63    -89.60                                   
REMARK 500    ARG A 396       65.98   -111.22                                   
REMARK 500    PRO A 403      -34.48    -36.79                                   
REMARK 500    CYS A 405       28.79    -79.17                                   
REMARK 500    TYR A 421      -59.50   -121.30                                   
REMARK 500    ASN A 430       -2.91     78.69                                   
REMARK 500    ASN A 446        2.27    -65.03                                   
REMARK 500    ASP A 457        4.10    -53.76                                   
REMARK 500    THR A 459       94.52    -65.75                                   
REMARK 500    ASN A 496       33.68    -90.99                                   
REMARK 500    GLN A 536      -70.59    -42.01                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  3C5L A  373   593  UNP    P53350   PLK1_HUMAN     373    593             
DBREF  3C5L B    1     5  PDB    3C5L     3C5L             1      5             
SEQRES   1 A  221  HIS LEU SER ASP MET LEU GLN GLN LEU HIS SER VAL ASN          
SEQRES   2 A  221  ALA SER LYS PRO SER GLU ARG GLY LEU VAL ARG GLN GLU          
SEQRES   3 A  221  GLU ALA GLU ASP PRO ALA CYS ILE PRO ILE PHE TRP VAL          
SEQRES   4 A  221  SER LYS TRP VAL ASP TYR SER ASP LYS TYR GLY LEU GLY          
SEQRES   5 A  221  TYR GLN LEU CYS ASP ASN SER VAL GLY VAL LEU PHE ASN          
SEQRES   6 A  221  ASP SER THR ARG LEU ILE LEU TYR ASN ASP GLY ASP SER          
SEQRES   7 A  221  LEU GLN TYR ILE GLU ARG ASP GLY THR GLU SER TYR LEU          
SEQRES   8 A  221  THR VAL SER SER HIS PRO ASN SER LEU MET LYS LYS ILE          
SEQRES   9 A  221  THR LEU LEU LYS TYR PHE ARG ASN TYR MET SER GLU HIS          
SEQRES  10 A  221  LEU LEU LYS ALA GLY ALA ASN ILE THR PRO ARG GLU GLY          
SEQRES  11 A  221  ASP GLU LEU ALA ARG LEU PRO TYR LEU ARG THR TRP PHE          
SEQRES  12 A  221  ARG THR ARG SER ALA ILE ILE LEU HIS LEU SER ASN GLY          
SEQRES  13 A  221  SER VAL GLN ILE ASN PHE PHE GLN ASP HIS THR LYS LEU          
SEQRES  14 A  221  ILE LEU CYS PRO LEU MET ALA ALA VAL THR TYR ILE ASP          
SEQRES  15 A  221  GLU LYS ARG ASP PHE ARG THR TYR ARG LEU SER LEU LEU          
SEQRES  16 A  221  GLU GLU TYR GLY CYS CYS LYS GLU LEU ALA SER ARG LEU          
SEQRES  17 A  221  ARG TYR ALA ARG THR MET VAL ASP LYS LEU LEU SER SER          
SEQRES   1 B    5  PRO PRO HIS SER TPO                                          
MODRES 3C5L TPO B    5  THR  PHOSPHOTHREONINE                                   
HET    TPO  B   5      12                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   2  TPO    C4 H10 N O6 P                                                
FORMUL   3  HOH   *35(H2 O)                                                     
HELIX    1   1 HIS A  373  SER A  387  1                                  15    
HELIX    2   2 ARG A  396  GLU A  401  5                                   6    
HELIX    3   3 ASP A  402  ILE A  406  5                                   5    
HELIX    4   4 SER A  466  HIS A  468  5                                   3    
HELIX    5   5 PRO A  469  SER A  471  5                                   3    
HELIX    6   6 LEU A  472  LEU A  490  1                                  19    
HELIX    7   7 LEU A  564  GLU A  568  1                                   5    
HELIX    8   8 CYS A  573  SER A  592  1                                  20    
SHEET    1   A 6 VAL A 411  ASP A 416  0                                        
SHEET    2   A 6 GLY A 422  LEU A 427 -1  O  GLN A 426   N  SER A 412           
SHEET    3   A 6 VAL A 432  PHE A 436 -1  O  LEU A 435   N  LEU A 423           
SHEET    4   A 6 ARG A 441  LEU A 444 -1  O  LEU A 444   N  VAL A 432           
SHEET    5   A 6 SER A 450  ILE A 454 -1  O  ILE A 454   N  ARG A 441           
SHEET    6   A 6 GLU A 460  THR A 464 -1  O  LEU A 463   N  LEU A 451           
SHEET    1   B 6 LEU A 511  THR A 517  0                                        
SHEET    2   B 6 ALA A 520  LEU A 525 -1  O  ILE A 522   N  PHE A 515           
SHEET    3   B 6 VAL A 530  PHE A 534 -1  O  GLN A 531   N  LEU A 523           
SHEET    4   B 6 LYS A 540  CYS A 544 -1  O  LEU A 543   N  VAL A 530           
SHEET    5   B 6 ALA A 549  ILE A 553 -1  O  ILE A 553   N  LYS A 540           
SHEET    6   B 6 PHE A 559  ARG A 563 -1  O  ARG A 560   N  TYR A 552           
LINK         C   SER B   4                 N   TPO B   5     1555   1555  1.33  
CRYST1   35.442   66.495  105.817  90.00  90.00  90.00 P 21 21 21    4          
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      0.028215  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015039  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009450        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system