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Database: PDB
Entry: 2ZEJ
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Original site: 2ZEJ 
HEADER    TRANSFERASE                             13-DEC-07   2ZEJ              
TITLE     STRUCTURE OF THE ROC DOMAIN FROM THE PARKINSON'S DISEASE-ASSOCIATED   
TITLE    2 LEUCINE-RICH REPEAT KINASE 2 REVEALS A DIMERIC GTPASE                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LEUCINE-RICH REPEAT KINASE 2;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ROC-GTPASE DOMAIN, UNP RESIDUES 1333-1516;                 
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;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21GOLDDE3;                               
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSKB3                                     
KEYWDS    PARKINSON'S DISEASE, LRRK2, ROC, GTPASE, ROCO, KINASE, ATP-BINDING,   
KEYWDS   2 DISEASE MUTATION, GTP-BINDING, GTPASE ACTIVATION, LEUCINE-RICH       
KEYWDS   3 REPEAT, MEMBRANE, NUCLEOTIDE-BINDING, PARKINSON DISEASE,             
KEYWDS   4 SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.DENG                                                                
REVDAT   5   13-JUL-11 2ZEJ    1       VERSN                                    
REVDAT   4   24-FEB-09 2ZEJ    1       VERSN                                    
REVDAT   3   22-APR-08 2ZEJ    1       JRNL                                     
REVDAT   2   12-FEB-08 2ZEJ    1       JRNL                                     
REVDAT   1   22-JAN-08 2ZEJ    0                                                
JRNL        AUTH   J.DENG,P.A.LEWIS,E.GREGGIO,E.SLUCH,A.BEILINA,M.R.COOKSON     
JRNL        TITL   STRUCTURE OF THE ROC DOMAIN FROM THE PARKINSON'S             
JRNL        TITL 2 DISEASE-ASSOCIATED LEUCINE-RICH REPEAT KINASE 2 REVEALS A    
JRNL        TITL 3 DIMERIC GTPASE                                               
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 105  1499 2008              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   18230735                                                     
JRNL        DOI    10.1073/PNAS.0709098105                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.80                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 22346                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1192                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1191                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 67.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2220                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 46                           
REMARK   3   BIN FREE R VALUE                    : 0.3200                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2538                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 58                                      
REMARK   3   SOLVENT ATOMS            : 112                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 29.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.31000                                              
REMARK   3    B22 (A**2) : -0.59000                                             
REMARK   3    B33 (A**2) : 0.76000                                              
REMARK   3    B12 (A**2) : -0.16000                                             
REMARK   3    B13 (A**2) : -0.43000                                             
REMARK   3    B23 (A**2) : -0.38000                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.198         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.182         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.140         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.660         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2601 ; 0.017 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3530 ; 2.145 ; 1.980       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   317 ;15.908 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   105 ;34.987 ;24.571       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   455 ;20.045 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;20.346 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   408 ; 0.270 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1876 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1097 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1725 ; 0.305 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   165 ; 0.139 ; 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):    33 ; 0.202 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.222 ; 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):  1634 ; 1.206 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2556 ; 1.736 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1127 ; 3.497 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   972 ; 4.627 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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  1335        A  1507                          
REMARK   3    ORIGIN FOR THE GROUP (A):  29.4030  37.2140  44.7930              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1422 T22:  -0.0961                                     
REMARK   3      T33:   0.0565 T12:   0.0392                                     
REMARK   3      T13:  -0.0209 T23:  -0.0677                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2397 L22:   1.6663                                     
REMARK   3      L33:   0.8813 L12:   0.9937                                     
REMARK   3      L13:  -0.6975 L23:  -0.2484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0109 S12:  -0.2056 S13:  -0.2176                       
REMARK   3      S21:   0.0711 S22:  -0.0122 S23:  -0.0512                       
REMARK   3      S31:   0.1104 S32:  -0.0294 S33:   0.0231                       
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 :   B  1336        B  1510                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.6750  49.9640  33.2210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1452 T22:  -0.1007                                     
REMARK   3      T33:   0.0367 T12:   0.0347                                     
REMARK   3      T13:  -0.0028 T23:  -0.0865                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3402 L22:   1.9717                                     
REMARK   3      L33:   0.8358 L12:   0.8869                                     
REMARK   3      L13:  -0.7825 L23:  -0.5634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0136 S12:  -0.0048 S13:   0.0275                       
REMARK   3      S21:  -0.1842 S22:  -0.0553 S23:  -0.1414                       
REMARK   3      S31:  -0.0609 S32:   0.0771 S33:   0.0416                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2ZEJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-DEC-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB027871.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-JUN-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97948                            
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-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23675                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.12600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.03                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 62.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.39800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: HKL3000                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 4000, 100MM MGCL2, 0.1M TRIS,    
REMARK 280  5MM GTP, PH 8.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
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: 7850 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14510 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.5 KCAL/MOL                        
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     ASN A  1333                                                      
REMARK 465     ARG A  1334                                                      
REMARK 465     THR A  1357                                                      
REMARK 465     LYS A  1358                                                      
REMARK 465     LYS A  1359                                                      
REMARK 465     SER A  1360                                                      
REMARK 465     ASP A  1361                                                      
REMARK 465     LEU A  1362                                                      
REMARK 465     GLY A  1363                                                      
REMARK 465     MSE A  1364                                                      
REMARK 465     GLN A  1365                                                      
REMARK 465     SER A  1366                                                      
REMARK 465     ALA A  1367                                                      
REMARK 465     GLN A  1379                                                      
REMARK 465     ILE A  1380                                                      
REMARK 465     ARG A  1381                                                      
REMARK 465     ASP A  1382                                                      
REMARK 465     LYS A  1383                                                      
REMARK 465     ARG A  1384                                                      
REMARK 465     LYS A  1385                                                      
REMARK 465     ARG A  1386                                                      
REMARK 465     ASP A  1387                                                      
REMARK 465     LYS A  1512                                                      
REMARK 465     ILE A  1513                                                      
REMARK 465     ARG A  1514                                                      
REMARK 465     ASP A  1515                                                      
REMARK 465     GLN A  1516                                                      
REMARK 465     ASN B  1333                                                      
REMARK 465     ARG B  1334                                                      
REMARK 465     LYS B  1358                                                      
REMARK 465     LYS B  1359                                                      
REMARK 465     SER B  1360                                                      
REMARK 465     ASP B  1361                                                      
REMARK 465     LEU B  1362                                                      
REMARK 465     GLY B  1363                                                      
REMARK 465     MSE B  1364                                                      
REMARK 465     GLN B  1379                                                      
REMARK 465     ILE B  1380                                                      
REMARK 465     ARG B  1381                                                      
REMARK 465     ASP B  1382                                                      
REMARK 465     LYS B  1383                                                      
REMARK 465     ARG B  1384                                                      
REMARK 465     LYS B  1385                                                      
REMARK 465     ARG B  1386                                                      
REMARK 465     ASP B  1387                                                      
REMARK 465     ILE B  1513                                                      
REMARK 465     ARG B  1514                                                      
REMARK 465     ASP B  1515                                                      
REMARK 465     GLN B  1516                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     LYS A 1356   CE   NZ                                             
REMARK 480     ARG A 1398   CG                                                  
REMARK 480     GLN A 1411   CB   CG                                             
REMARK 480     ARG A 1412   CD   NE                                             
REMARK 480     LYS A 1463   CG   CD   CE   NZ                                   
REMARK 480     LYS A 1471   CD   CE   NZ                                        
REMARK 480     ARG A 1477   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     ARG A 1483   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     GLU A 1493   CG   CD   OE1  OE2                                  
REMARK 480     LYS A 1499   CE   NZ                                             
REMARK 480     PHE A 1511   CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 480     LYS B 1356   CE   NZ                                             
REMARK 480     GLN B 1365   CG   CD   OE1  NE2                                  
REMARK 480     SER B 1366   CB   OG                                             
REMARK 480     LYS B 1439   CE   NZ                                             
REMARK 480     LYS B 1463   NZ                                                  
REMARK 480     LYS B 1471   CD   CE   NZ                                        
REMARK 480     ARG B 1477   CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 480     TYR B 1485   CE1  OH                                             
REMARK 480     LYS B 1512   CG   CD   CE   NZ                                   
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 A1412       47.74   -103.68                                   
REMARK 500    ASN A1510       68.55   -108.90                                   
REMARK 500    ARG B1462      -37.90   -139.48                                   
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 GLN B 1461     ARG B 1462                 -127.62                    
REMARK 500 ARG B 1462     LYS B 1463                  135.33                    
REMARK 500 ARG B 1477     GLY B 1478                  -58.92                    
REMARK 500 GLY B 1478     PHE B 1479                  144.16                    
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    ASN A1475        23.6      L          L   OUTSIDE RANGE           
REMARK 500    LEU B1421        17.5      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A   2  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A1348   OG1                                                    
REMARK 620 2 GDP A   1   O3B  93.0                                              
REMARK 620 3 HOH A 201   O    84.7  90.1                                        
REMARK 620 4 HOH A 104   O    97.4  85.8 175.4                                  
REMARK 620 5 HOH A 200   O   172.6  92.5  90.5  87.9                            
REMARK 620 6 HOH A 202   O    91.0 176.0  90.3  93.7  83.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B   1  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B1348   OG1                                                    
REMARK 620 2 GDP B   2   O3B  92.3                                              
REMARK 620 3 HOH B1519   O   171.7  95.5                                        
REMARK 620 4 HOH B1517   O    85.5 170.6  86.4                                  
REMARK 620 5 HOH B1518   O    88.7  95.0  93.3  94.1                            
REMARK 620 6 HOH B1569   O    86.8  89.5  90.5  81.2 173.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 2                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 1                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP B 2                   
DBREF  2ZEJ A 1333  1516  UNP    Q17RV3   Q17RV3_HUMAN  1333   1516             
DBREF  2ZEJ B 1333  1516  UNP    Q17RV3   Q17RV3_HUMAN  1333   1516             
SEQRES   1 A  184  ASN ARG MSE LYS LEU MSE ILE VAL GLY ASN THR GLY SER          
SEQRES   2 A  184  GLY LYS THR THR LEU LEU GLN GLN LEU MSE LYS THR LYS          
SEQRES   3 A  184  LYS SER ASP LEU GLY MSE GLN SER ALA THR VAL GLY ILE          
SEQRES   4 A  184  ASP VAL LYS ASP TRP PRO ILE GLN ILE ARG ASP LYS ARG          
SEQRES   5 A  184  LYS ARG ASP LEU VAL LEU ASN VAL TRP ASP PHE ALA GLY          
SEQRES   6 A  184  ARG GLU GLU PHE TYR SER THR HIS PRO HIS PHE MSE THR          
SEQRES   7 A  184  GLN ARG ALA LEU TYR LEU ALA VAL TYR ASP LEU SER LYS          
SEQRES   8 A  184  GLY GLN ALA GLU VAL ASP ALA MSE LYS PRO TRP LEU PHE          
SEQRES   9 A  184  ASN ILE LYS ALA ARG ALA SER SER SER PRO VAL ILE LEU          
SEQRES  10 A  184  VAL GLY THR HIS LEU ASP VAL SER ASP GLU LYS GLN ARG          
SEQRES  11 A  184  LYS ALA CYS MSE SER LYS ILE THR LYS GLU LEU LEU ASN          
SEQRES  12 A  184  LYS ARG GLY PHE PRO ALA ILE ARG ASP TYR HIS PHE VAL          
SEQRES  13 A  184  ASN ALA THR GLU GLU SER ASP ALA LEU ALA LYS LEU ARG          
SEQRES  14 A  184  LYS THR ILE ILE ASN GLU SER LEU ASN PHE LYS ILE ARG          
SEQRES  15 A  184  ASP GLN                                                      
SEQRES   1 B  184  ASN ARG MSE LYS LEU MSE ILE VAL GLY ASN THR GLY SER          
SEQRES   2 B  184  GLY LYS THR THR LEU LEU GLN GLN LEU MSE LYS THR LYS          
SEQRES   3 B  184  LYS SER ASP LEU GLY MSE GLN SER ALA THR VAL GLY ILE          
SEQRES   4 B  184  ASP VAL LYS ASP TRP PRO ILE GLN ILE ARG ASP LYS ARG          
SEQRES   5 B  184  LYS ARG ASP LEU VAL LEU ASN VAL TRP ASP PHE ALA GLY          
SEQRES   6 B  184  ARG GLU GLU PHE TYR SER THR HIS PRO HIS PHE MSE THR          
SEQRES   7 B  184  GLN ARG ALA LEU TYR LEU ALA VAL TYR ASP LEU SER LYS          
SEQRES   8 B  184  GLY GLN ALA GLU VAL ASP ALA MSE LYS PRO TRP LEU PHE          
SEQRES   9 B  184  ASN ILE LYS ALA ARG ALA SER SER SER PRO VAL ILE LEU          
SEQRES  10 B  184  VAL GLY THR HIS LEU ASP VAL SER ASP GLU LYS GLN ARG          
SEQRES  11 B  184  LYS ALA CYS MSE SER LYS ILE THR LYS GLU LEU LEU ASN          
SEQRES  12 B  184  LYS ARG GLY PHE PRO ALA ILE ARG ASP TYR HIS PHE VAL          
SEQRES  13 B  184  ASN ALA THR GLU GLU SER ASP ALA LEU ALA LYS LEU ARG          
SEQRES  14 B  184  LYS THR ILE ILE ASN GLU SER LEU ASN PHE LYS ILE ARG          
SEQRES  15 B  184  ASP GLN                                                      
MODRES 2ZEJ MSE A 1335  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE A 1338  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE A 1355  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE A 1409  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE A 1431  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE A 1466  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE B 1335  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE B 1338  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE B 1355  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE B 1409  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE B 1431  MET  SELENOMETHIONINE                                   
MODRES 2ZEJ MSE B 1466  MET  SELENOMETHIONINE                                   
HET    MSE  A1335       8                                                       
HET    MSE  A1338       8                                                       
HET    MSE  A1355       8                                                       
HET    MSE  A1409       8                                                       
HET    MSE  A1431       8                                                       
HET    MSE  A1466       8                                                       
HET    MSE  B1335       8                                                       
HET    MSE  B1338       8                                                       
HET    MSE  B1355       8                                                       
HET    MSE  B1409       8                                                       
HET    MSE  B1431       8                                                       
HET    MSE  B1466       8                                                       
HET     MG  A   2       1                                                       
HET     MG  B   1       1                                                       
HET    GDP  A   1      28                                                       
HET    GDP  B   2      28                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   7  HOH   *112(H2 O)                                                    
HELIX    1   1 GLY A 1346  LYS A 1356  1                                  11    
HELIX    2   2 GLY A 1397  SER A 1403  1                                   7    
HELIX    3   3 HIS A 1405  ARG A 1412  1                                   8    
HELIX    4   4 GLY A 1424  ALA A 1430  1                                   7    
HELIX    5   5 ALA A 1430  ALA A 1442  1                                  13    
HELIX    6   6 HIS A 1453  SER A 1457  5                                   5    
HELIX    7   7 ASP A 1458  LEU A 1473  1                                  16    
HELIX    8   8 SER A 1494  ASN A 1510  1                                  17    
HELIX    9   9 GLY B 1346  LYS B 1356  1                                  11    
HELIX   10  10 GLY B 1397  THR B 1404  1                                   8    
HELIX   11  11 HIS B 1405  ARG B 1412  1                                   8    
HELIX   12  12 GLY B 1424  ALA B 1430  1                                   7    
HELIX   13  13 ALA B 1430  ALA B 1442  1                                  13    
HELIX   14  14 HIS B 1453  ASP B 1458  5                                   6    
HELIX   15  15 GLU B 1459  LEU B 1473  1                                  15    
HELIX   16  16 SER B 1494  LYS B 1512  1                                  19    
SHEET    1   A 6 ILE A1371  TRP A1376  0                                        
SHEET    2   A 6 LEU A1390  PHE A1395 -1  O  VAL A1392   N  LYS A1374           
SHEET    3   A 6 LYS A1336  VAL A1340  1  N  LEU A1337   O  TRP A1393           
SHEET    4   A 6 ALA B1413  ASP B1420  1  O  LEU B1414   N  MSE A1338           
SHEET    5   A 6 PRO B1446  THR B1452  1  O  VAL B1450   N  ALA B1417           
SHEET    6   A 6 ALA B1481  PHE B1487  1  O  ALA B1481   N  VAL B1447           
SHEET    1   B 6 ALA A1481  PHE A1487  0                                        
SHEET    2   B 6 PRO A1446  THR A1452  1  N  VAL A1447   O  ARG A1483           
SHEET    3   B 6 ALA A1413  ASP A1420  1  N  ALA A1417   O  VAL A1450           
SHEET    4   B 6 LYS B1336  GLY B1341  1  O  MSE B1338   N  LEU A1414           
SHEET    5   B 6 LEU B1390  PHE B1395  1  O  TRP B1393   N  LEU B1337           
SHEET    6   B 6 ILE B1371  TRP B1376 -1  N  LYS B1374   O  VAL B1392           
LINK         OG1 THR A1348                MG    MG A   2     1555   1555  2.09  
LINK         OG1 THR B1348                MG    MG B   1     1555   1555  2.12  
LINK        MG    MG B   1                 O3B GDP B   2     1555   1555  2.09  
LINK        MG    MG A   2                 O3B GDP A   1     1555   1555  2.02  
LINK        MG    MG A   2                 O   HOH A 201     1555   1555  2.24  
LINK        MG    MG A   2                 O   HOH A 104     1555   1555  2.19  
LINK        MG    MG A   2                 O   HOH A 200     1555   1555  2.05  
LINK        MG    MG A   2                 O   HOH A 202     1555   1555  2.14  
LINK        MG    MG B   1                 O   HOH B1519     1555   1555  2.03  
LINK        MG    MG B   1                 O   HOH B1517     1555   1555  2.16  
LINK        MG    MG B   1                 O   HOH B1518     1555   1555  2.17  
LINK        MG    MG B   1                 O   HOH B1569     1555   1555  2.31  
LINK         C   MSE A1335                 N   LYS A1336     1555   1555  1.34  
LINK         C   LEU A1337                 N   MSE A1338     1555   1555  1.33  
LINK         C   MSE A1338                 N   ILE A1339     1555   1555  1.34  
LINK         C   LEU A1354                 N   MSE A1355     1555   1555  1.31  
LINK         C   MSE A1355                 N   LYS A1356     1555   1555  1.32  
LINK         C   PHE A1408                 N   MSE A1409     1555   1555  1.33  
LINK         C   MSE A1409                 N   THR A1410     1555   1555  1.33  
LINK         C   ALA A1430                 N   MSE A1431     1555   1555  1.33  
LINK         C   MSE A1431                 N   LYS A1432     1555   1555  1.34  
LINK         C   CYS A1465                 N   MSE A1466     1555   1555  1.33  
LINK         C   MSE A1466                 N   SER A1467     1555   1555  1.34  
LINK         C   MSE B1335                 N   LYS B1336     1555   1555  1.33  
LINK         C   LEU B1337                 N   MSE B1338     1555   1555  1.32  
LINK         C   MSE B1338                 N   ILE B1339     1555   1555  1.34  
LINK         C   LEU B1354                 N   MSE B1355     1555   1555  1.33  
LINK         C   MSE B1355                 N   LYS B1356     1555   1555  1.34  
LINK         C   PHE B1408                 N   MSE B1409     1555   1555  1.33  
LINK         C   MSE B1409                 N   THR B1410     1555   1555  1.32  
LINK         C   ALA B1430                 N   MSE B1431     1555   1555  1.32  
LINK         C   MSE B1431                 N   LYS B1432     1555   1555  1.33  
LINK         C   CYS B1465                 N   MSE B1466     1555   1555  1.33  
LINK         C   MSE B1466                 N   SER B1467     1555   1555  1.34  
CISPEP   1 ARG A 1477    GLY A 1478          0       -15.45                     
SITE     1 AC1  6 GDP A   1  HOH A 104  HOH A 200  HOH A 201                    
SITE     2 AC1  6 HOH A 202  THR A1348                                          
SITE     1 AC2  6 GDP B   2  THR B1348  HOH B1517  HOH B1518                    
SITE     2 AC2  6 HOH B1519  HOH B1569                                          
SITE     1 AC3 22  MG A   2  HOH A  10  HOH A  22  HOH A  49                    
SITE     2 AC3 22 HOH A 104  HOH A 114  HOH A 116  HOH A 200                    
SITE     3 AC3 22 HOH A 201  GLY A1344  SER A1345  GLY A1346                    
SITE     4 AC3 22 LYS A1347  THR A1348  THR A1349  PHE A1436                    
SITE     5 AC3 22 ASN A1437  HIS B1453  ASP B1455  ASN B1489                    
SITE     6 AC3 22 ALA B1490  THR B1491                                          
SITE     1 AC4 21 HIS A1453  ASP A1455  ASN A1489  ALA A1490                    
SITE     2 AC4 21 THR A1491   MG B   1  THR B1343  GLY B1344                    
SITE     3 AC4 21 SER B1345  GLY B1346  LYS B1347  THR B1348                    
SITE     4 AC4 21 THR B1349  PHE B1436  ASN B1437  HOH B1519                    
SITE     5 AC4 21 HOH B1522  HOH B1527  HOH B1538  HOH B1556                    
SITE     6 AC4 21 HOH B1569                                                     
CRYST1   44.438   44.404   53.681  81.51  69.00  78.71 P 1           2          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022503 -0.004493 -0.008288        0.00000                         
SCALE2      0.000000  0.022965 -0.001950        0.00000                         
SCALE3      0.000000  0.000000  0.020026        0.00000                         
HETATM    1  N   MSE A1335      40.849  41.003  24.904  1.00 38.86           N  
HETATM    2  CA  MSE A1335      39.557  41.091  25.644  1.00 39.43           C  
HETATM    3  C   MSE A1335      39.530  42.116  26.793  1.00 37.45           C  
HETATM    4  O   MSE A1335      38.606  42.922  26.814  1.00 36.14           O  
HETATM    5  CB  MSE A1335      39.095  39.709  26.133  1.00 41.32           C  
HETATM    6  CG  MSE A1335      37.758  39.625  26.797  1.00 48.96           C  
HETATM    7 SE   MSE A1335      36.341  39.046  25.517  1.00 76.92          SE  
HETATM    8  CE  MSE A1335      37.131  37.319  24.900  1.00 67.30           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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