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Database: PDB
Entry: 6DLP
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Original site: 6DLP 
HEADER    CYTOSOLIC PROTEIN                       02-JUN-18   6DLP              
TITLE     CRYSTAL STRUCTURE OF LRRK2 WD40 DOMAIN DIMER                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUCINE-RICH REPEAT SERINE/THREONINE-PROTEIN KINASE 2;     
COMPND   3 CHAIN: B, A;                                                         
COMPND   4 FRAGMENT: WD40 DOMAIN RESIDUES 2142-2527;                            
COMPND   5 SYNONYM: DARDARIN;                                                   
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: LRRK2, PARK8;                                                  
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108                                        
KEYWDS    PARKINSON'S DISEASE, LRRK2, WD40, CYTOSOLIC PROTEIN                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.ZHANG,H.RU,L.WANG,H.WU                                              
REVDAT   4   13-MAR-24 6DLP    1       REMARK                                   
REVDAT   3   13-FEB-19 6DLP    1       JRNL                                     
REVDAT   2   23-JAN-19 6DLP    1       JRNL                                     
REVDAT   1   09-JAN-19 6DLP    0                                                
JRNL        AUTH   P.ZHANG,Y.FAN,H.RU,L.WANG,V.G.MAGUPALLI,S.S.TAYLOR,          
JRNL        AUTH 2 D.R.ALESSI,H.WU                                              
JRNL        TITL   CRYSTAL STRUCTURE OF THE WD40 DOMAIN DIMER OF LRRK2.         
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 116  1579 2019              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   30635421                                                     
JRNL        DOI    10.1073/PNAS.1817889116                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.13_2998)                                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 4.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 76.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.580                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 7975                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.870                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 388                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 76.2694 -  5.7687    0.99     2675   138  0.2454 0.3298        
REMARK   3     2  5.7687 -  4.5789    0.97     2525   133  0.2057 0.2120        
REMARK   3     3  4.5789 -  4.0002    0.94     2387   117  0.2304 0.2401        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.580           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.002           4891                                  
REMARK   3   ANGLE     :  0.537           6604                                  
REMARK   3   CHIRALITY :  0.045            806                                  
REMARK   3   PLANARITY :  0.003            803                                  
REMARK   3   DIHEDRAL  :  6.802           2923                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):   3.3759  -0.0916  11.0459              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2884 T22:   0.3195                                     
REMARK   3      T33:   0.2429 T12:  -0.1030                                     
REMARK   3      T13:   0.0755 T23:  -0.2020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9536 L22:   0.8447                                     
REMARK   3      L33:   0.4124 L12:   0.6854                                     
REMARK   3      L13:   0.4740 L23:   0.3790                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1535 S12:   0.5476 S13:  -0.0251                       
REMARK   3      S21:  -0.2244 S22:   0.1939 S23:  -0.2332                       
REMARK   3      S31:  -0.0927 S32:   0.2158 S33:  -0.1229                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6DLP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-JUN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000234881.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-JUL-16                          
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               : 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) : 0.89260                            
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12211                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.450                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 112.660                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 6.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.45                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.78                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AUTOSOL                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.57                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS-HCL AT PH 8.5, 1 M LICL,      
REMARK 280  16% POLYETHYLENE GLYCOL (PEG) 6000, AND 10% ADDITIVE OF 30%         
REMARK 280  GALACTOSE. THE CRYSTAL WAS SOAKED IN 1 MM TRANS-PLATINUM (II)       
REMARK 280  DIAMMINE DICHLORIDE FOR 1.5 HOURS, VAPOR DIFFUSION, SITTING DROP,   
REMARK 280  TEMPERATURE 289K                                                    
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       39.64650            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       56.33200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       51.79500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       56.33200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       39.64650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       51.79500            
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 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: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2750 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 26900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -108.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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 B  2139                                                      
REMARK 465     GLY B  2140                                                      
REMARK 465     HIS B  2160                                                      
REMARK 465     ASN B  2161                                                      
REMARK 465     SER B  2162                                                      
REMARK 465     ARG B  2163                                                      
REMARK 465     ASN B  2164                                                      
REMARK 465     SER B  2252                                                      
REMARK 465     PHE B  2253                                                      
REMARK 465     SER B  2254                                                      
REMARK 465     LYS B  2255                                                      
REMARK 465     GLN B  2256                                                      
REMARK 465     SER B  2257                                                      
REMARK 465     LYS B  2258                                                      
REMARK 465     GLN B  2259                                                      
REMARK 465     GLU B  2305                                                      
REMARK 465     SER B  2306                                                      
REMARK 465     THR B  2307                                                      
REMARK 465     ASN B  2308                                                      
REMARK 465     SER B  2309                                                      
REMARK 465     THR B  2310                                                      
REMARK 465     GLU B  2311                                                      
REMARK 465     ARG B  2312                                                      
REMARK 465     ASN B  2313                                                      
REMARK 465     VAL B  2396                                                      
REMARK 465     MET B  2397                                                      
REMARK 465     VAL B  2398                                                      
REMARK 465     LYS B  2399                                                      
REMARK 465     GLU B  2400                                                      
REMARK 465     ASN B  2401                                                      
REMARK 465     LYS B  2402                                                      
REMARK 465     GLU B  2403                                                      
REMARK 465     SER B  2404                                                      
REMARK 465     LYS B  2405                                                      
REMARK 465     HIS B  2406                                                      
REMARK 465     LYS B  2407                                                      
REMARK 465     LYS B  2421                                                      
REMARK 465     ASN B  2422                                                      
REMARK 465     THR B  2423                                                      
REMARK 465     ARG B  2477                                                      
REMARK 465     LYS B  2478                                                      
REMARK 465     ASN B  2479                                                      
REMARK 465     THR B  2480                                                      
REMARK 465     GLU B  2481                                                      
REMARK 465     GLY B  2482                                                      
REMARK 465     THR B  2483                                                      
REMARK 465     GLN B  2484                                                      
REMARK 465     LYS B  2485                                                      
REMARK 465     GLN B  2486                                                      
REMARK 465     LYS B  2487                                                      
REMARK 465     ASN B  2499                                                      
REMARK 465     LEU B  2500                                                      
REMARK 465     PRO B  2501                                                      
REMARK 465     HIS B  2502                                                      
REMARK 465     GLU B  2503                                                      
REMARK 465     VAL B  2504                                                      
REMARK 465     GLN B  2505                                                      
REMARK 465     ASN B  2506                                                      
REMARK 465     LEU B  2507                                                      
REMARK 465     GLU B  2508                                                      
REMARK 465     LYS B  2509                                                      
REMARK 465     HIS B  2510                                                      
REMARK 465     ILE B  2511                                                      
REMARK 465     GLU B  2512                                                      
REMARK 465     VAL B  2513                                                      
REMARK 465     ARG B  2514                                                      
REMARK 465     LYS B  2515                                                      
REMARK 465     GLU B  2516                                                      
REMARK 465     LEU B  2517                                                      
REMARK 465     ALA B  2518                                                      
REMARK 465     GLU B  2519                                                      
REMARK 465     LYS B  2520                                                      
REMARK 465     MET B  2521                                                      
REMARK 465     ARG B  2522                                                      
REMARK 465     ARG B  2523                                                      
REMARK 465     THR B  2524                                                      
REMARK 465     SER B  2525                                                      
REMARK 465     VAL B  2526                                                      
REMARK 465     GLU B  2527                                                      
REMARK 465     GLY A  2139                                                      
REMARK 465     GLY A  2140                                                      
REMARK 465     HIS A  2159                                                      
REMARK 465     HIS A  2160                                                      
REMARK 465     ASN A  2161                                                      
REMARK 465     SER A  2162                                                      
REMARK 465     ARG A  2163                                                      
REMARK 465     SER A  2254                                                      
REMARK 465     LYS A  2255                                                      
REMARK 465     GLN A  2256                                                      
REMARK 465     SER A  2257                                                      
REMARK 465     LYS A  2258                                                      
REMARK 465     SER A  2306                                                      
REMARK 465     THR A  2307                                                      
REMARK 465     ASN A  2308                                                      
REMARK 465     SER A  2309                                                      
REMARK 465     THR A  2310                                                      
REMARK 465     GLU A  2311                                                      
REMARK 465     ARG A  2312                                                      
REMARK 465     ASN A  2313                                                      
REMARK 465     VAL A  2396                                                      
REMARK 465     MET A  2397                                                      
REMARK 465     VAL A  2398                                                      
REMARK 465     LYS A  2399                                                      
REMARK 465     GLU A  2400                                                      
REMARK 465     ASN A  2401                                                      
REMARK 465     LYS A  2402                                                      
REMARK 465     GLU A  2403                                                      
REMARK 465     SER A  2404                                                      
REMARK 465     LYS A  2405                                                      
REMARK 465     HIS A  2406                                                      
REMARK 465     LYS A  2407                                                      
REMARK 465     LEU A  2463                                                      
REMARK 465     GLY A  2464                                                      
REMARK 465     SER A  2465                                                      
REMARK 465     LEU A  2466                                                      
REMARK 465     LYS A  2467                                                      
REMARK 465     LYS A  2478                                                      
REMARK 465     ASN A  2479                                                      
REMARK 465     THR A  2480                                                      
REMARK 465     GLU A  2481                                                      
REMARK 465     GLY A  2482                                                      
REMARK 465     THR A  2483                                                      
REMARK 465     GLN A  2484                                                      
REMARK 465     LYS A  2485                                                      
REMARK 465     GLN A  2486                                                      
REMARK 465     LYS A  2487                                                      
REMARK 465     ASP A  2497                                                      
REMARK 465     ILE A  2498                                                      
REMARK 465     ASN A  2499                                                      
REMARK 465     LEU A  2500                                                      
REMARK 465     PRO A  2501                                                      
REMARK 465     HIS A  2502                                                      
REMARK 465     GLU A  2503                                                      
REMARK 465     VAL A  2504                                                      
REMARK 465     GLN A  2505                                                      
REMARK 465     ASN A  2506                                                      
REMARK 465     LEU A  2507                                                      
REMARK 465     GLU A  2508                                                      
REMARK 465     LYS A  2509                                                      
REMARK 465     HIS A  2510                                                      
REMARK 465     ILE A  2511                                                      
REMARK 465     GLU A  2512                                                      
REMARK 465     VAL A  2513                                                      
REMARK 465     ARG A  2514                                                      
REMARK 465     LYS A  2515                                                      
REMARK 465     GLU A  2516                                                      
REMARK 465     LEU A  2517                                                      
REMARK 465     ALA A  2518                                                      
REMARK 465     GLU A  2519                                                      
REMARK 465     LYS A  2520                                                      
REMARK 465     MET A  2521                                                      
REMARK 465     ARG A  2522                                                      
REMARK 465     ARG A  2523                                                      
REMARK 465     THR A  2524                                                      
REMARK 465     SER A  2525                                                      
REMARK 465     VAL A  2526                                                      
REMARK 465     GLU A  2527                                                      
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 B2210       -9.56     72.98                                   
REMARK 500    ASP B2329       -1.82     75.70                                   
REMARK 500    SER B2345      -16.96     74.38                                   
REMARK 500    TYR B2346      151.11    177.33                                   
REMARK 500    ASP B2351       54.10    -92.18                                   
REMARK 500    THR B2361      -36.85   -131.28                                   
REMARK 500    SER B2454      119.33   -161.09                                   
REMARK 500    GLU A2210       -9.02     73.06                                   
REMARK 500    ASP A2351       53.79    -91.40                                   
REMARK 500    ASN A2422      -36.56   -132.26                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A2142         0.26    SIDE CHAIN                              
REMARK 500    ARG A2143         0.15    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PT B 2601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PT B 2602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PT B 2603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PT A 2601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PT A 2602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PT A 2603                 
DBREF  6DLP B 2142  2527  UNP    Q5S007   LRRK2_HUMAN   2142   2527             
DBREF  6DLP A 2142  2527  UNP    Q5S007   LRRK2_HUMAN   2142   2527             
SEQADV 6DLP GLY B 2139  UNP  Q5S007              EXPRESSION TAG                 
SEQADV 6DLP GLY B 2140  UNP  Q5S007              EXPRESSION TAG                 
SEQADV 6DLP SER B 2141  UNP  Q5S007              EXPRESSION TAG                 
SEQADV 6DLP GLY A 2139  UNP  Q5S007              EXPRESSION TAG                 
SEQADV 6DLP GLY A 2140  UNP  Q5S007              EXPRESSION TAG                 
SEQADV 6DLP SER A 2141  UNP  Q5S007              EXPRESSION TAG                 
SEQRES   1 B  389  GLY GLY SER ARG ARG ILE LEU LEU PRO LYS ASN VAL ILE          
SEQRES   2 B  389  VAL GLU CYS MET VAL ALA THR HIS HIS ASN SER ARG ASN          
SEQRES   3 B  389  ALA SER ILE TRP LEU GLY CYS GLY HIS THR ASP ARG GLY          
SEQRES   4 B  389  GLN LEU SER PHE LEU ASP LEU ASN THR GLU GLY TYR THR          
SEQRES   5 B  389  SER GLU GLU VAL ALA ASP SER ARG ILE LEU CYS LEU ALA          
SEQRES   6 B  389  LEU VAL HIS LEU PRO VAL GLU LYS GLU SER TRP ILE VAL          
SEQRES   7 B  389  SER GLY THR GLN SER GLY THR LEU LEU VAL ILE ASN THR          
SEQRES   8 B  389  GLU ASP GLY LYS LYS ARG HIS THR LEU GLU LYS MET THR          
SEQRES   9 B  389  ASP SER VAL THR CYS LEU TYR CYS ASN SER PHE SER LYS          
SEQRES  10 B  389  GLN SER LYS GLN LYS ASN PHE LEU LEU VAL GLY THR ALA          
SEQRES  11 B  389  ASP GLY LYS LEU ALA ILE PHE GLU ASP LYS THR VAL LYS          
SEQRES  12 B  389  LEU LYS GLY ALA ALA PRO LEU LYS ILE LEU ASN ILE GLY          
SEQRES  13 B  389  ASN VAL SER THR PRO LEU MET CYS LEU SER GLU SER THR          
SEQRES  14 B  389  ASN SER THR GLU ARG ASN VAL MET TRP GLY GLY CYS GLY          
SEQRES  15 B  389  THR LYS ILE PHE SER PHE SER ASN ASP PHE THR ILE GLN          
SEQRES  16 B  389  LYS LEU ILE GLU THR ARG THR SER GLN LEU PHE SER TYR          
SEQRES  17 B  389  ALA ALA PHE SER ASP SER ASN ILE ILE THR VAL VAL VAL          
SEQRES  18 B  389  ASP THR ALA LEU TYR ILE ALA LYS GLN ASN SER PRO VAL          
SEQRES  19 B  389  VAL GLU VAL TRP ASP LYS LYS THR GLU LYS LEU CYS GLY          
SEQRES  20 B  389  LEU ILE ASP CYS VAL HIS PHE LEU ARG GLU VAL MET VAL          
SEQRES  21 B  389  LYS GLU ASN LYS GLU SER LYS HIS LYS MET SER TYR SER          
SEQRES  22 B  389  GLY ARG VAL LYS THR LEU CYS LEU GLN LYS ASN THR ALA          
SEQRES  23 B  389  LEU TRP ILE GLY THR GLY GLY GLY HIS ILE LEU LEU LEU          
SEQRES  24 B  389  ASP LEU SER THR ARG ARG LEU ILE ARG VAL ILE TYR ASN          
SEQRES  25 B  389  PHE CYS ASN SER VAL ARG VAL MET MET THR ALA GLN LEU          
SEQRES  26 B  389  GLY SER LEU LYS ASN VAL MET LEU VAL LEU GLY TYR ASN          
SEQRES  27 B  389  ARG LYS ASN THR GLU GLY THR GLN LYS GLN LYS GLU ILE          
SEQRES  28 B  389  GLN SER CYS LEU THR VAL TRP ASP ILE ASN LEU PRO HIS          
SEQRES  29 B  389  GLU VAL GLN ASN LEU GLU LYS HIS ILE GLU VAL ARG LYS          
SEQRES  30 B  389  GLU LEU ALA GLU LYS MET ARG ARG THR SER VAL GLU              
SEQRES   1 A  389  GLY GLY SER ARG ARG ILE LEU LEU PRO LYS ASN VAL ILE          
SEQRES   2 A  389  VAL GLU CYS MET VAL ALA THR HIS HIS ASN SER ARG ASN          
SEQRES   3 A  389  ALA SER ILE TRP LEU GLY CYS GLY HIS THR ASP ARG GLY          
SEQRES   4 A  389  GLN LEU SER PHE LEU ASP LEU ASN THR GLU GLY TYR THR          
SEQRES   5 A  389  SER GLU GLU VAL ALA ASP SER ARG ILE LEU CYS LEU ALA          
SEQRES   6 A  389  LEU VAL HIS LEU PRO VAL GLU LYS GLU SER TRP ILE VAL          
SEQRES   7 A  389  SER GLY THR GLN SER GLY THR LEU LEU VAL ILE ASN THR          
SEQRES   8 A  389  GLU ASP GLY LYS LYS ARG HIS THR LEU GLU LYS MET THR          
SEQRES   9 A  389  ASP SER VAL THR CYS LEU TYR CYS ASN SER PHE SER LYS          
SEQRES  10 A  389  GLN SER LYS GLN LYS ASN PHE LEU LEU VAL GLY THR ALA          
SEQRES  11 A  389  ASP GLY LYS LEU ALA ILE PHE GLU ASP LYS THR VAL LYS          
SEQRES  12 A  389  LEU LYS GLY ALA ALA PRO LEU LYS ILE LEU ASN ILE GLY          
SEQRES  13 A  389  ASN VAL SER THR PRO LEU MET CYS LEU SER GLU SER THR          
SEQRES  14 A  389  ASN SER THR GLU ARG ASN VAL MET TRP GLY GLY CYS GLY          
SEQRES  15 A  389  THR LYS ILE PHE SER PHE SER ASN ASP PHE THR ILE GLN          
SEQRES  16 A  389  LYS LEU ILE GLU THR ARG THR SER GLN LEU PHE SER TYR          
SEQRES  17 A  389  ALA ALA PHE SER ASP SER ASN ILE ILE THR VAL VAL VAL          
SEQRES  18 A  389  ASP THR ALA LEU TYR ILE ALA LYS GLN ASN SER PRO VAL          
SEQRES  19 A  389  VAL GLU VAL TRP ASP LYS LYS THR GLU LYS LEU CYS GLY          
SEQRES  20 A  389  LEU ILE ASP CYS VAL HIS PHE LEU ARG GLU VAL MET VAL          
SEQRES  21 A  389  LYS GLU ASN LYS GLU SER LYS HIS LYS MET SER TYR SER          
SEQRES  22 A  389  GLY ARG VAL LYS THR LEU CYS LEU GLN LYS ASN THR ALA          
SEQRES  23 A  389  LEU TRP ILE GLY THR GLY GLY GLY HIS ILE LEU LEU LEU          
SEQRES  24 A  389  ASP LEU SER THR ARG ARG LEU ILE ARG VAL ILE TYR ASN          
SEQRES  25 A  389  PHE CYS ASN SER VAL ARG VAL MET MET THR ALA GLN LEU          
SEQRES  26 A  389  GLY SER LEU LYS ASN VAL MET LEU VAL LEU GLY TYR ASN          
SEQRES  27 A  389  ARG LYS ASN THR GLU GLY THR GLN LYS GLN LYS GLU ILE          
SEQRES  28 A  389  GLN SER CYS LEU THR VAL TRP ASP ILE ASN LEU PRO HIS          
SEQRES  29 A  389  GLU VAL GLN ASN LEU GLU LYS HIS ILE GLU VAL ARG LYS          
SEQRES  30 A  389  GLU LEU ALA GLU LYS MET ARG ARG THR SER VAL GLU              
HET     PT  B2601       1                                                       
HET     PT  B2602       1                                                       
HET     PT  B2603       1                                                       
HET     PT  A2601       1                                                       
HET     PT  A2602       1                                                       
HET     PT  A2603       1                                                       
HETNAM      PT PLATINUM (II) ION                                                
FORMUL   3   PT    6(PT 2+)                                                     
HELIX    1 AA1 LYS B 2278  LEU B 2282  5                                   5    
HELIX    2 AA2 ARG B 2339  PHE B 2344  5                                   6    
HELIX    3 AA3 CYS B 2389  ARG B 2394  1                                   6    
HELIX    4 AA4 LYS A 2278  LEU A 2282  5                                   5    
HELIX    5 AA5 TYR A 2346  ASP A 2351  1                                   6    
HELIX    6 AA6 CYS A 2389  ARG A 2394  1                                   6    
SHEET    1 AA1 4 ARG B2142  LEU B2145  0                                        
SHEET    2 AA1 4 SER B2491  ASP B2497 -1  O  LEU B2493   N  ILE B2144           
SHEET    3 AA1 4 ASN B2468  TYR B2475 -1  N  MET B2470   O  TRP B2496           
SHEET    4 AA1 4 SER B2454  GLN B2462 -1  N  MET B2459   O  LEU B2471           
SHEET    1 AA2 4 VAL B2152  THR B2158  0                                        
SHEET    2 AA2 4 SER B2166  CYS B2171 -1  O  TRP B2168   N  VAL B2156           
SHEET    3 AA2 4 GLY B2177  ASP B2183 -1  O  SER B2180   N  LEU B2169           
SHEET    4 AA2 4 TYR B2189  ALA B2195 -1  O  THR B2190   N  PHE B2181           
SHEET    1 AA3 4 ILE B2199  LEU B2207  0                                        
SHEET    2 AA3 4 GLU B2212  THR B2219 -1  O  VAL B2216   N  ALA B2203           
SHEET    3 AA3 4 LEU B2224  ASN B2228 -1  O  ILE B2227   N  ILE B2215           
SHEET    4 AA3 4 ARG B2235  THR B2237 -1  O  HIS B2236   N  VAL B2226           
SHEET    1 AA4 4 VAL B2245  ASN B2251  0                                        
SHEET    2 AA4 4 PHE B2262  THR B2267 -1  O  LEU B2264   N  TYR B2249           
SHEET    3 AA4 4 LYS B2271  GLU B2276 -1  O  LYS B2271   N  THR B2267           
SHEET    4 AA4 4 LYS B2289  ASN B2292 -1  O  LEU B2291   N  LEU B2272           
SHEET    1 AA5 4 LEU B2300  SER B2304  0                                        
SHEET    2 AA5 4 MET B2315  CYS B2319 -1  O  TRP B2316   N  SER B2304           
SHEET    3 AA5 4 LYS B2322  PHE B2326 -1  O  LYS B2322   N  CYS B2319           
SHEET    4 AA5 4 LEU B2335  GLU B2337 -1  O  ILE B2336   N  ILE B2323           
SHEET    1 AA6 4 ILE B2354  VAL B2359  0                                        
SHEET    2 AA6 4 LEU B2363  LYS B2367 -1  O  ALA B2366   N  ILE B2355           
SHEET    3 AA6 4 VAL B2372  TRP B2376 -1  O  TRP B2376   N  LEU B2363           
SHEET    4 AA6 4 LEU B2383  ASP B2388 -1  O  CYS B2384   N  VAL B2375           
SHEET    1 AA7 4 VAL B2414  CYS B2418  0                                        
SHEET    2 AA7 4 LEU B2425  THR B2429 -1  O  TRP B2426   N  CYS B2418           
SHEET    3 AA7 4 ILE B2434  LEU B2437 -1  O  LEU B2435   N  ILE B2427           
SHEET    4 AA7 4 LEU B2444  ILE B2448 -1  O  ILE B2448   N  ILE B2434           
SHEET    1 AA8 4 ARG A2142  LEU A2145  0                                        
SHEET    2 AA8 4 GLN A2490  TRP A2496 -1  O  LEU A2493   N  ILE A2144           
SHEET    3 AA8 4 VAL A2469  ASN A2476 -1  N  VAL A2472   O  THR A2494           
SHEET    4 AA8 4 VAL A2455  ALA A2461 -1  N  MET A2459   O  LEU A2471           
SHEET    1 AA9 4 VAL A2152  THR A2158  0                                        
SHEET    2 AA9 4 SER A2166  CYS A2171 -1  O  TRP A2168   N  VAL A2156           
SHEET    3 AA9 4 GLY A2177  ASP A2183 -1  O  SER A2180   N  LEU A2169           
SHEET    4 AA9 4 GLY A2188  ALA A2195 -1  O  THR A2190   N  PHE A2181           
SHEET    1 AB1 4 ILE A2199  LEU A2207  0                                        
SHEET    2 AB1 4 GLU A2212  THR A2219 -1  O  VAL A2216   N  ALA A2203           
SHEET    3 AB1 4 LEU A2224  ASN A2228 -1  O  ILE A2227   N  ILE A2215           
SHEET    4 AB1 4 ARG A2235  THR A2237 -1  O  HIS A2236   N  VAL A2226           
SHEET    1 AB2 4 VAL A2245  SER A2252  0                                        
SHEET    2 AB2 4 ASN A2261  THR A2267 -1  O  PHE A2262   N  ASN A2251           
SHEET    3 AB2 4 LYS A2271  GLU A2276 -1  O  LYS A2271   N  THR A2267           
SHEET    4 AB2 4 LYS A2289  ASN A2292 -1  O  LEU A2291   N  LEU A2272           
SHEET    1 AB3 4 LEU A2300  SER A2304  0                                        
SHEET    2 AB3 4 MET A2315  CYS A2319 -1  O  TRP A2316   N  SER A2304           
SHEET    3 AB3 4 LYS A2322  PHE A2326 -1  O  PHE A2326   N  MET A2315           
SHEET    4 AB3 4 ILE A2332  GLU A2337 -1  O  ILE A2336   N  ILE A2323           
SHEET    1 AB4 4 ILE A2354  VAL A2359  0                                        
SHEET    2 AB4 4 LEU A2363  LYS A2367 -1  O  ALA A2366   N  ILE A2355           
SHEET    3 AB4 4 VAL A2372  TRP A2376 -1  O  TRP A2376   N  LEU A2363           
SHEET    4 AB4 4 LEU A2383  ASP A2388 -1  O  CYS A2384   N  VAL A2375           
SHEET    1 AB5 4 VAL A2414  LEU A2419  0                                        
SHEET    2 AB5 4 ALA A2424  THR A2429 -1  O  TRP A2426   N  CYS A2418           
SHEET    3 AB5 4 ILE A2434  ASP A2438 -1  O  LEU A2435   N  ILE A2427           
SHEET    4 AB5 4 LEU A2444  ILE A2448 -1  O  ILE A2448   N  ILE A2434           
LINK         SG  CYS B2201                PT    PT B2601     1555   1555  2.56  
LINK         SG  CYS B2302                PT    PT B2602     1555   1555  2.12  
LINK         SG  CYS B2418                PT    PT B2603     1555   1555  2.53  
LINK         SG  CYS A2201                PT    PT A2603     1555   1555  2.59  
LINK         SG  CYS A2302                PT    PT A2602     1555   1555  2.13  
LINK         SG  CYS A2418                PT    PT A2601     1555   1555  2.77  
SITE     1 AC1  2 CYS B2154  CYS B2201                                          
SITE     1 AC2  2 CYS B2302  LEU B2303                                          
SITE     1 AC3  1 CYS B2418                                                     
SITE     1 AC4  1 CYS A2418                                                     
SITE     1 AC5  1 CYS A2302                                                     
SITE     1 AC6  2 CYS A2154  CYS A2201                                          
CRYST1   79.293  103.590  112.664  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      0.012611  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009653  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008876        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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