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Database: PDB
Entry: 2V62
LinkDB: 2V62
Original site: 2V62 
HEADER    TRANSFERASE                             13-JUL-07   2V62              
TITLE     STRUCTURE OF VACCINIA-RELATED KINASE 2                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE VRK2;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 14-335;                            
COMPND   5 SYNONYM: VACCINIA RELATED PROTEIN KINASE 2;                          
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 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    TRANSFERASE, ATP-BINDING, MEMBRANE, NUCLEOTIDE-BINDING, TRANSMEMBRANE 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BUNKOCZI,J.ESWARAN,C.COOPER,O.FEDOROV,T.KEATES,P.RELLOS,E.SALAH,    
AUTHOR   2 P.SAVITSKY,E.UGOCHUKWU,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,         
AUTHOR   3 M.SUNDSTROM,J.WEIGELT,S.KNAPP                                        
REVDAT   6   13-DEC-23 2V62    1       REMARK LINK                              
REVDAT   5   30-NOV-11 2V62    1       REMARK                                   
REVDAT   4   13-JUL-11 2V62    1       VERSN                                    
REVDAT   3   04-AUG-09 2V62    1       JRNL   REMARK                            
REVDAT   2   24-FEB-09 2V62    1       VERSN                                    
REVDAT   1   21-AUG-07 2V62    0                                                
JRNL        AUTH   E.D.SCHEEFF,J.ESWARAN,G.BUNKOCZI,S.KNAPP,G.MANNING           
JRNL        TITL   STRUCTURE OF THE PSEUDOKINASE VRK3 REVEALS A DEGRADED        
JRNL        TITL 2 CATALYTIC SITE, A HIGHLY CONSERVED KINASE FOLD, AND A        
JRNL        TITL 3 PUTATIVE REGULATORY BINDING SITE.                            
JRNL        REF    STRUCTURE                     V.  17   128 2009              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   19141289                                                     
JRNL        DOI    10.1016/J.STR.2008.10.018                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0034                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 64302                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3413                            
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) : 1.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.75                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4358                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3120                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 217                          
REMARK   3   BIN FREE R VALUE                    : 0.3540                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4756                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 21                                      
REMARK   3   SOLVENT ATOMS            : 334                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.73                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.28000                                              
REMARK   3    B22 (A**2) : -0.83000                                             
REMARK   3    B33 (A**2) : 0.55000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.121         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.117         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.104         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.559         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.955                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4958 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  3322 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6727 ; 1.483 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  8122 ; 1.012 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   617 ; 5.602 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   215 ;33.469 ;24.512       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   801 ;13.311 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    20 ;16.691 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   741 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5519 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   975 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1029 ; 0.198 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  3320 ; 0.191 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2372 ; 0.183 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  2510 ; 0.086 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   235 ; 0.169 ; 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 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):   100 ; 0.295 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    13 ; 0.158 ; 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):  3193 ; 3.326 ; 3.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4955 ; 4.590 ; 5.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2047 ; 7.114 ; 8.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1772 ; 8.803 ;11.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 3                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     15       A      62      5                      
REMARK   3           1     B     15       B      62      5                      
REMARK   3           2     A     98       A     122      3                      
REMARK   3           2     B     98       B     122      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    145 ;  0.04 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    245 ;  0.04 ;  0.50           
REMARK   3   LOOSE POSITIONAL   1    A    (A):    419 ;  0.03 ;  5.00           
REMARK   3   TIGHT THERMAL      1    A (A**2):    145 ;  0.19 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    245 ;  0.17 ;  2.00           
REMARK   3   LOOSE THERMAL      1    A (A**2):    419 ;  0.18 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     68       A      97      5                      
REMARK   3           1     B     68       B      97      5                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    178 ;  0.12 ;  0.50           
REMARK   3   LOOSE POSITIONAL   2    A    (A):    238 ;  0.30 ;  5.00           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    178 ;  1.07 ;  2.00           
REMARK   3   LOOSE THERMAL      2    A (A**2):    238 ;  1.06 ; 10.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    123       A     330      3                      
REMARK   3           1     B    123       B     330      3                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   3    A    (A):   1220 ;  0.03 ;  0.05           
REMARK   3   LOOSE POSITIONAL   3    A    (A):   1465 ;  0.05 ;  5.00           
REMARK   3   TIGHT THERMAL      3    A (A**2):   1220 ;  0.27 ;  0.50           
REMARK   3   LOOSE THERMAL      3    A (A**2):   1465 ;  0.24 ; 10.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    67                          
REMARK   3    RESIDUE RANGE :   A    98        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4035  -1.7714  28.8268              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2811 T22:   0.1399                                     
REMARK   3      T33:   0.0509 T12:   0.0470                                     
REMARK   3      T13:  -0.0388 T23:  -0.0512                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.7570 L22:   5.7041                                     
REMARK   3      L33:   1.6924 L12:  -2.6505                                     
REMARK   3      L13:   0.9759 L23:  -0.5670                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3218 S12:   0.4531 S13:  -0.3997                       
REMARK   3      S21:  -0.9798 S22:  -0.1401 S23:  -0.1118                       
REMARK   3      S31:   0.5739 S32:   0.4571 S33:  -0.1816                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    68        A    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):   8.7818  11.6726  35.4781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0869 T22:  -0.1637                                     
REMARK   3      T33:  -0.0627 T12:  -0.0594                                     
REMARK   3      T13:  -0.0206 T23:   0.0209                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7695 L22:   1.5859                                     
REMARK   3      L33:   4.3243 L12:  -2.2205                                     
REMARK   3      L13:   1.0702 L23:  -0.6609                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0336 S12:  -0.0893 S13:  -0.5311                       
REMARK   3      S21:   0.0180 S22:   0.1398 S23:   0.2568                       
REMARK   3      S31:   0.3398 S32:  -0.3091 S33:  -0.1062                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   123        A   330                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9835  27.7157  30.1806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1358 T22:  -0.1262                                     
REMARK   3      T33:  -0.1213 T12:   0.0047                                     
REMARK   3      T13:   0.0018 T23:   0.0350                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0556 L22:   1.3213                                     
REMARK   3      L33:   1.4893 L12:  -0.0793                                     
REMARK   3      L13:   0.1324 L23:  -0.4239                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0460 S12:   0.1833 S13:   0.1590                       
REMARK   3      S21:  -0.1844 S22:  -0.0333 S23:  -0.0163                       
REMARK   3      S31:   0.0776 S32:   0.0210 S33:  -0.0128                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B    67                          
REMARK   3    RESIDUE RANGE :   B    98        B   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.9299  80.0317  56.4216              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3050 T22:   0.1216                                     
REMARK   3      T33:   0.0578 T12:   0.0442                                     
REMARK   3      T13:   0.0231 T23:   0.0460                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8714 L22:   5.6988                                     
REMARK   3      L33:   0.9482 L12:  -2.2242                                     
REMARK   3      L13:  -0.9552 L23:   0.4026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3259 S12:   0.4610 S13:   0.3237                       
REMARK   3      S21:  -1.0514 S22:  -0.2104 S23:   0.1798                       
REMARK   3      S31:  -0.5570 S32:  -0.3261 S33:  -0.1154                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    68        B    97                          
REMARK   3    ORIGIN FOR THE GROUP (A):  27.7547  66.7924  63.5871              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0675 T22:  -0.1425                                     
REMARK   3      T33:  -0.0108 T12:  -0.0690                                     
REMARK   3      T13:   0.0254 T23:   0.0046                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4470 L22:   0.5866                                     
REMARK   3      L33:   3.1432 L12:  -1.5562                                     
REMARK   3      L13:  -0.7946 L23:   0.9933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1360 S12:  -0.0688 S13:   0.5786                       
REMARK   3      S21:  -0.1198 S22:   0.0371 S23:  -0.1839                       
REMARK   3      S31:  -0.2966 S32:   0.3520 S33:  -0.1731                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   123        B   330                          
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8436  50.8887  58.3550              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1289 T22:  -0.1367                                     
REMARK   3      T33:  -0.1004 T12:  -0.0019                                     
REMARK   3      T13:   0.0096 T23:  -0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1754 L22:   1.4095                                     
REMARK   3      L33:   1.6716 L12:  -0.1653                                     
REMARK   3      L13:  -0.0948 L23:   0.4885                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0351 S12:   0.1720 S13:  -0.1430                       
REMARK   3      S21:  -0.1881 S22:  -0.0208 S23:  -0.0390                       
REMARK   3      S31:  -0.1022 S32:   0.0361 S33:  -0.0143                       
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 2V62 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-07.                  
REMARK 100 THE DEPOSITION ID IS D_1290033183.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X10SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9999                             
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 67759                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.800                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.9                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.3000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2JII                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SUCCINIC ACID PH=7.0 15%           
REMARK 280  PEG3350, PH 7                                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       35.32750            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       78.76600            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       35.32750            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       78.76600            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET A    -9                                                      
REMARK 465     HIS A    -8                                                      
REMARK 465     HIS A    -7                                                      
REMARK 465     HIS A    -6                                                      
REMARK 465     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     SER A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     VAL A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     TYR A     9                                                      
REMARK 465     PHE A    10                                                      
REMARK 465     GLN A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     MET A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     GLY A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     GLY A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     PHE A    40                                                      
REMARK 465     GLY A    41                                                      
REMARK 465     ASN A    67                                                      
REMARK 465     SER A   331                                                      
REMARK 465     ILE A   332                                                      
REMARK 465     ASN A   333                                                      
REMARK 465     VAL A   334                                                      
REMARK 465     HIS A   335                                                      
REMARK 465     MET B    -9                                                      
REMARK 465     HIS B    -8                                                      
REMARK 465     HIS B    -7                                                      
REMARK 465     HIS B    -6                                                      
REMARK 465     HIS B    -5                                                      
REMARK 465     HIS B    -4                                                      
REMARK 465     HIS B    -3                                                      
REMARK 465     SER B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     VAL B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     TYR B     9                                                      
REMARK 465     PHE B    10                                                      
REMARK 465     GLN B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     MET B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     GLY B    36                                                      
REMARK 465     SER B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     GLY B    39                                                      
REMARK 465     PHE B    40                                                      
REMARK 465     ASN B    67                                                      
REMARK 465     SER B   331                                                      
REMARK 465     ILE B   332                                                      
REMARK 465     ASN B   333                                                      
REMARK 465     VAL B   334                                                      
REMARK 465     HIS B   335                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  17    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  22    CG   OD1  OD2                                       
REMARK 470     LYS A  33    CG   CD   CE   NZ                                   
REMARK 470     LYS A  34    CG   CD   CE   NZ                                   
REMARK 470     LEU A  42    CG   CD1  CD2                                       
REMARK 470     LYS A  51    CG   CD   CE   NZ                                   
REMARK 470     GLU A  53    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  54    CD   CE   NZ                                        
REMARK 470     ASP A  55    CG   OD1  OD2                                       
REMARK 470     ARG A  57    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A  64    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU A  66    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  83    CG   CD   CE   NZ                                   
REMARK 470     LYS A  87    CG   CD   CE   NZ                                   
REMARK 470     LYS A  88    CG   CD   CE   NZ                                   
REMARK 470     LYS A  93    CE   NZ                                             
REMARK 470     GLU A 110    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 111    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS A 112    CG   CD   CE   NZ                                   
REMARK 470     ARG A 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 130    CD   CE   NZ                                        
REMARK 470     GLN A 134    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 139    CE   NZ                                             
REMARK 470     LYS A 177    CD   CE   NZ                                        
REMARK 470     ASP A 180    CG   OD1  OD2                                       
REMARK 470     GLN A 203    CD   OE1  NE2                                       
REMARK 470     LYS A 208    CE   NZ                                             
REMARK 470     GLU A 251    CD   OE1  OE2                                       
REMARK 470     LYS A 255    CD   CE   NZ                                        
REMARK 470     GLN A 307    CD   OE1  NE2                                       
REMARK 470     ILE A 318    CG1  CG2  CD1                                       
REMARK 470     THR A 327    OG1  CG2                                            
REMARK 470     LYS A 328    CE   NZ                                             
REMARK 470     GLN A 330    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  33    CG   CD   CE   NZ                                   
REMARK 470     LYS B  34    CG   CD   CE   NZ                                   
REMARK 470     LEU B  42    CG   CD1  CD2                                       
REMARK 470     LYS B  51    CD   CE   NZ                                        
REMARK 470     LYS B  54    CD   CE   NZ                                        
REMARK 470     ARG B  57    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR B  64    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B  66    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  83    CG   CD   CE   NZ                                   
REMARK 470     LYS B  87    CG   CD   CE   NZ                                   
REMARK 470     LYS B  88    CG   CD   CE   NZ                                   
REMARK 470     GLU B 110    CD   OE1  OE2                                       
REMARK 470     PHE B 111    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS B 112    CG   CD   CE   NZ                                   
REMARK 470     ARG B 114    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 130    CD   CE   NZ                                        
REMARK 470     GLN B 134    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 139    CE   NZ                                             
REMARK 470     LYS B 177    CG   CD   CE   NZ                                   
REMARK 470     ASP B 180    CG   OD1  OD2                                       
REMARK 470     LYS B 208    CE   NZ                                             
REMARK 470     GLU B 251    CD   OE1  OE2                                       
REMARK 470     LYS B 255    CD   CE   NZ                                        
REMARK 470     GLN B 307    CD   OE1  NE2                                       
REMARK 470     THR B 327    OG1  CG2                                            
REMARK 470     LYS B 328    CD   CE   NZ                                        
REMARK 470     GLN B 330    CG   CD   OE1  NE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    CYS A 194   CB    CYS A 194   SG     -0.097                       
REMARK 500    CYS A 294   CB    CYS A 294   SG     -0.141                       
REMARK 500    GLN B  65   CB    GLN B  65   CG      8.353                       
REMARK 500    CYS B 294   CB    CYS B 294   SG     -0.132                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLN B  65   CA  -  CB  -  CG  ANGL. DEV. = -83.0 DEGREES          
REMARK 500    GLN B  65   CB  -  CG  -  CD  ANGL. DEV. =  27.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  55       52.66    -94.89                                   
REMARK 500    TYR A  64      177.98    -59.54                                   
REMARK 500    ALA A  81       53.67    -92.39                                   
REMARK 500    LYS A 112     -100.89   -127.41                                   
REMARK 500    GLU A 161        8.70     83.59                                   
REMARK 500    ASP A 166       45.78   -151.06                                   
REMARK 500    TYR A 176      -61.81   -100.69                                   
REMARK 500    ASP A 186       82.15     61.40                                   
REMARK 500    HIS A 210       31.66     71.36                                   
REMARK 500    SER A 283       85.48   -153.63                                   
REMARK 500    ASP B  55       52.34    -93.68                                   
REMARK 500    LYS B 112     -102.57   -127.24                                   
REMARK 500    GLU B 161        6.94     83.73                                   
REMARK 500    ASP B 166       42.25   -151.81                                   
REMARK 500    TYR B 176      -62.42    -98.36                                   
REMARK 500    ASP B 186       82.78     58.38                                   
REMARK 500    SER B 283       82.52   -153.65                                   
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 A1331  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG A 207   O                                                      
REMARK 620 2 HOH A1084   O    91.1                                              
REMARK 620 3 HOH A1085   O    92.2  86.4                                        
REMARK 620 4 ARG B 207   O   175.7  89.4  83.5                                  
REMARK 620 5 HOH B1094   O    95.1 167.2  82.2  83.6                            
REMARK 620 6 HOH B1096   O    90.9  98.9 173.8  93.3  92.2                      
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 1331                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN A 1332                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1331                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1333                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1334                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE FIRST 23 RESIDUES BELONG TO AN UNCLEAVED HIS-TAG                 
DBREF  2V62 A   14   335  UNP    Q86Y07   VRK2_HUMAN      14    335             
DBREF  2V62 B   14   335  UNP    Q86Y07   VRK2_HUMAN      14    335             
SEQADV 2V62 MET A   -9  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS A   -8  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS A   -7  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS A   -6  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS A   -5  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS A   -4  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS A   -3  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 SER A   -2  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 SER A   -1  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 GLY A    0  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 VAL A    1  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 ASP A    2  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 LEU A    3  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 GLY A    4  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 THR A    5  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 GLU A    6  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 ASN A    7  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 LEU A    8  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 TYR A    9  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 PHE A   10  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 GLN A   11  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 SER A   12  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 MET A   13  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 MET B   -9  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS B   -8  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS B   -7  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS B   -6  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS B   -5  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS B   -4  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 HIS B   -3  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 SER B   -2  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 SER B   -1  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 GLY B    0  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 VAL B    1  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 ASP B    2  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 LEU B    3  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 GLY B    4  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 THR B    5  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 GLU B    6  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 ASN B    7  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 LEU B    8  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 TYR B    9  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 PHE B   10  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 GLN B   11  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 SER B   12  UNP  Q86Y07              EXPRESSION TAG                 
SEQADV 2V62 MET B   13  UNP  Q86Y07              EXPRESSION TAG                 
SEQRES   1 A  345  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  345  GLY THR GLU ASN LEU TYR PHE GLN SER MET PRO PHE PRO          
SEQRES   3 A  345  GLU GLY LYS VAL LEU ASP ASP MET GLU GLY ASN GLN TRP          
SEQRES   4 A  345  VAL LEU GLY LYS LYS ILE GLY SER GLY GLY PHE GLY LEU          
SEQRES   5 A  345  ILE TYR LEU ALA PHE PRO THR ASN LYS PRO GLU LYS ASP          
SEQRES   6 A  345  ALA ARG HIS VAL VAL LYS VAL GLU TYR GLN GLU ASN GLY          
SEQRES   7 A  345  PRO LEU PHE SER GLU LEU LYS PHE TYR GLN ARG VAL ALA          
SEQRES   8 A  345  LYS LYS ASP CYS ILE LYS LYS TRP ILE GLU ARG LYS GLN          
SEQRES   9 A  345  LEU ASP TYR LEU GLY ILE PRO LEU PHE TYR GLY SER GLY          
SEQRES  10 A  345  LEU THR GLU PHE LYS GLY ARG SER TYR ARG PHE MET VAL          
SEQRES  11 A  345  MET GLU ARG LEU GLY ILE ASP LEU GLN LYS ILE SER GLY          
SEQRES  12 A  345  GLN ASN GLY THR PHE LYS LYS SER THR VAL LEU GLN LEU          
SEQRES  13 A  345  GLY ILE ARG MET LEU ASP VAL LEU GLU TYR ILE HIS GLU          
SEQRES  14 A  345  ASN GLU TYR VAL HIS GLY ASP ILE LYS ALA ALA ASN LEU          
SEQRES  15 A  345  LEU LEU GLY TYR LYS ASN PRO ASP GLN VAL TYR LEU ALA          
SEQRES  16 A  345  ASP TYR GLY LEU SER TYR ARG TYR CYS PRO ASN GLY ASN          
SEQRES  17 A  345  HIS LYS GLN TYR GLN GLU ASN PRO ARG LYS GLY HIS ASN          
SEQRES  18 A  345  GLY THR ILE GLU PHE THR SER LEU ASP ALA HIS LYS GLY          
SEQRES  19 A  345  VAL ALA LEU SER ARG ARG SER ASP VAL GLU ILE LEU GLY          
SEQRES  20 A  345  TYR CYS MET LEU ARG TRP LEU CYS GLY LYS LEU PRO TRP          
SEQRES  21 A  345  GLU GLN ASN LEU LYS ASP PRO VAL ALA VAL GLN THR ALA          
SEQRES  22 A  345  LYS THR ASN LEU LEU ASP GLU LEU PRO GLN SER VAL LEU          
SEQRES  23 A  345  LYS TRP ALA PRO SER GLY SER SER CYS CYS GLU ILE ALA          
SEQRES  24 A  345  GLN PHE LEU VAL CYS ALA HIS SER LEU ALA TYR ASP GLU          
SEQRES  25 A  345  LYS PRO ASN TYR GLN ALA LEU LYS LYS ILE LEU ASN PRO          
SEQRES  26 A  345  HIS GLY ILE PRO LEU GLY PRO LEU ASP PHE SER THR LYS          
SEQRES  27 A  345  GLY GLN SER ILE ASN VAL HIS                                  
SEQRES   1 B  345  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  345  GLY THR GLU ASN LEU TYR PHE GLN SER MET PRO PHE PRO          
SEQRES   3 B  345  GLU GLY LYS VAL LEU ASP ASP MET GLU GLY ASN GLN TRP          
SEQRES   4 B  345  VAL LEU GLY LYS LYS ILE GLY SER GLY GLY PHE GLY LEU          
SEQRES   5 B  345  ILE TYR LEU ALA PHE PRO THR ASN LYS PRO GLU LYS ASP          
SEQRES   6 B  345  ALA ARG HIS VAL VAL LYS VAL GLU TYR GLN GLU ASN GLY          
SEQRES   7 B  345  PRO LEU PHE SER GLU LEU LYS PHE TYR GLN ARG VAL ALA          
SEQRES   8 B  345  LYS LYS ASP CYS ILE LYS LYS TRP ILE GLU ARG LYS GLN          
SEQRES   9 B  345  LEU ASP TYR LEU GLY ILE PRO LEU PHE TYR GLY SER GLY          
SEQRES  10 B  345  LEU THR GLU PHE LYS GLY ARG SER TYR ARG PHE MET VAL          
SEQRES  11 B  345  MET GLU ARG LEU GLY ILE ASP LEU GLN LYS ILE SER GLY          
SEQRES  12 B  345  GLN ASN GLY THR PHE LYS LYS SER THR VAL LEU GLN LEU          
SEQRES  13 B  345  GLY ILE ARG MET LEU ASP VAL LEU GLU TYR ILE HIS GLU          
SEQRES  14 B  345  ASN GLU TYR VAL HIS GLY ASP ILE LYS ALA ALA ASN LEU          
SEQRES  15 B  345  LEU LEU GLY TYR LYS ASN PRO ASP GLN VAL TYR LEU ALA          
SEQRES  16 B  345  ASP TYR GLY LEU SER TYR ARG TYR CYS PRO ASN GLY ASN          
SEQRES  17 B  345  HIS LYS GLN TYR GLN GLU ASN PRO ARG LYS GLY HIS ASN          
SEQRES  18 B  345  GLY THR ILE GLU PHE THR SER LEU ASP ALA HIS LYS GLY          
SEQRES  19 B  345  VAL ALA LEU SER ARG ARG SER ASP VAL GLU ILE LEU GLY          
SEQRES  20 B  345  TYR CYS MET LEU ARG TRP LEU CYS GLY LYS LEU PRO TRP          
SEQRES  21 B  345  GLU GLN ASN LEU LYS ASP PRO VAL ALA VAL GLN THR ALA          
SEQRES  22 B  345  LYS THR ASN LEU LEU ASP GLU LEU PRO GLN SER VAL LEU          
SEQRES  23 B  345  LYS TRP ALA PRO SER GLY SER SER CYS CYS GLU ILE ALA          
SEQRES  24 B  345  GLN PHE LEU VAL CYS ALA HIS SER LEU ALA TYR ASP GLU          
SEQRES  25 B  345  LYS PRO ASN TYR GLN ALA LEU LYS LYS ILE LEU ASN PRO          
SEQRES  26 B  345  HIS GLY ILE PRO LEU GLY PRO LEU ASP PHE SER THR LYS          
SEQRES  27 B  345  GLY GLN SER ILE ASN VAL HIS                                  
HET     MG  A1331       1                                                       
HET    SIN  A1332       8                                                       
HET    EDO  A1333       4                                                       
HET    EDO  A1334       4                                                       
HET    EDO  B1331       4                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     SIN SUCCINIC ACID                                                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  SIN    C4 H6 O4                                                     
FORMUL   5  EDO    3(C2 H6 O2)                                                  
FORMUL   8  HOH   *334(H2 O)                                                    
HELIX    1   1 PRO A   52  ALA A   56  5                                   5    
HELIX    2   2 GLY A   68  ALA A   81  1                                  14    
HELIX    3   3 LYS A   82  GLN A   94  1                                  13    
HELIX    4   4 LEU A  128  SER A  132  1                                   5    
HELIX    5   5 GLN A  134  GLY A  136  5                                   3    
HELIX    6   6 LYS A  139  ASN A  160  1                                  22    
HELIX    7   7 LYS A  168  ALA A  170  5                                   3    
HELIX    8   8 CYS A  194  ASN A  198  5                                   5    
HELIX    9   9 ASN A  205  GLY A  209  5                                   5    
HELIX   10  10 SER A  218  GLY A  224  1                                   7    
HELIX   11  11 SER A  228  GLY A  246  1                                  19    
HELIX   12  12 TRP A  250  LEU A  254  5                                   5    
HELIX   13  13 ASP A  256  GLU A  270  1                                  15    
HELIX   14  14 PRO A  272  ALA A  279  1                                   8    
HELIX   15  15 CYS A  285  SER A  297  1                                  13    
HELIX   16  16 ASN A  305  ASN A  314  1                                  10    
HELIX   17  17 PRO B   52  ALA B   56  5                                   5    
HELIX   18  18 GLY B   68  ALA B   81  1                                  14    
HELIX   19  19 LYS B   82  LYS B   93  1                                  12    
HELIX   20  20 GLN B  134  GLY B  136  5                                   3    
HELIX   21  21 LYS B  139  ASN B  160  1                                  22    
HELIX   22  22 LYS B  168  ALA B  170  5                                   3    
HELIX   23  23 CYS B  194  ASN B  198  5                                   5    
HELIX   24  24 ASN B  205  GLY B  209  5                                   5    
HELIX   25  25 SER B  218  GLY B  224  1                                   7    
HELIX   26  26 SER B  228  GLY B  246  1                                  19    
HELIX   27  27 TRP B  250  LEU B  254  5                                   5    
HELIX   28  28 ASP B  256  GLU B  270  1                                  15    
HELIX   29  29 PRO B  272  LYS B  277  1                                   6    
HELIX   30  30 CYS B  285  SER B  297  1                                  13    
HELIX   31  31 ASN B  305  ASN B  314  1                                  10    
SHEET    1  AA 6 VAL A  20  ASP A  22  0                                        
SHEET    2  AA 6 GLN A  28  LYS A  34 -1  O  TRP A  29   N  LEU A  21           
SHEET    3  AA 6 ILE A  43  PRO A  48 -1  O  LEU A  45   N  GLY A  32           
SHEET    4  AA 6 HIS A  58  TYR A  64 -1  O  HIS A  58   N  ALA A  46           
SHEET    5  AA 6 SER A 115  GLU A 122 -1  O  ARG A 117   N  GLU A  63           
SHEET    6  AA 6 PHE A 103  GLU A 110 -1  N  TYR A 104   O  VAL A 120           
SHEET    1  AB 3 LEU A 124  ASP A 127  0                                        
SHEET    2  AB 3 LEU A 172  GLY A 175 -1  O  LEU A 174   N  GLY A 125           
SHEET    3  AB 3 VAL A 182  LEU A 184 -1  O  TYR A 183   N  LEU A 173           
SHEET    1  AC 2 TYR A 162  VAL A 163  0                                        
SHEET    2  AC 2 TYR A 191  ARG A 192 -1  O  TYR A 191   N  VAL A 163           
SHEET    1  BA 6 VAL B  20  ASP B  22  0                                        
SHEET    2  BA 6 GLN B  28  ILE B  35 -1  O  TRP B  29   N  LEU B  21           
SHEET    3  BA 6 LEU B  42  PRO B  48 -1  O  ILE B  43   N  ILE B  35           
SHEET    4  BA 6 HIS B  58  VAL B  62 -1  O  HIS B  58   N  ALA B  46           
SHEET    5  BA 6 SER B 115  GLU B 122 -1  O  MET B 119   N  LYS B  61           
SHEET    6  BA 6 PHE B 103  GLU B 110 -1  N  TYR B 104   O  VAL B 120           
SHEET    1  BB 3 LEU B 124  ASP B 127  0                                        
SHEET    2  BB 3 LEU B 172  GLY B 175 -1  O  LEU B 174   N  GLY B 125           
SHEET    3  BB 3 VAL B 182  LEU B 184 -1  O  TYR B 183   N  LEU B 173           
SHEET    1  BC 2 TYR B 162  VAL B 163  0                                        
SHEET    2  BC 2 TYR B 191  ARG B 192 -1  O  TYR B 191   N  VAL B 163           
LINK         O   ARG A 207                MG    MG A1331     1555   1555  2.21  
LINK         O   HOH A1084                MG    MG A1331     1555   1555  2.31  
LINK         O   HOH A1085                MG    MG A1331     1555   1555  2.62  
LINK        MG    MG A1331                 O   ARG B 207     1555   4557  2.35  
LINK        MG    MG A1331                 O   HOH B1094     1555   4557  2.45  
LINK        MG    MG A1331                 O   HOH B1096     1555   4557  2.53  
CISPEP   1 LEU A  271    PRO A  272          0        -4.19                     
CISPEP   2 LEU B  271    PRO B  272          0        -4.10                     
SITE     1 AC1  6 ARG A 207  HOH A1084  HOH A1085  ARG B 207                    
SITE     2 AC1  6 HOH B1094  HOH B1096                                          
SITE     1 AC2 10 ARG A 117  HOH A1167  HOH A1168  HOH A1169                    
SITE     2 AC2 10 MET B  24  LEU B  74  GLN B  78  SER B 106                    
SITE     3 AC2 10 GLY B 107  ARG B 117                                          
SITE     1 AC3  4 SER A 297  CYS B 245  TRP B 278  PRO B 280                    
SITE     1 AC4  5 CYS A 245  TRP A 278  PRO A 280  SER B 297                    
SITE     2 AC4  5 HOH B1150                                                     
SITE     1 AC5  5 ARG A  79  ASN A 160  GLU A 161  GLU B  25                    
SITE     2 AC5  5 ARG B  92                                                     
CRYST1   70.655  157.532   56.288  90.00  90.00  90.00 P 21 21 2     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      0.014153  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006348  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017766        0.00000                         
MTRIX1   1 -0.999290  0.037720 -0.001270       35.71097    1                    
MTRIX2   1 -0.037720 -0.999270  0.006050       78.92622    1                    
MTRIX3   1 -0.001040  0.006100  0.999980       27.94197    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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