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Database: PDB
Entry: 2AC3
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Original site: 2AC3 
HEADER    TRANSFERASE                             18-JUL-05   2AC3              
TITLE     STRUCTURE OF HUMAN MNK2 KINASE DOMAIN                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MAP KINASE-INTERACTING SERINE/THREONINE KINASE 2;          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 70-385;                                           
COMPND   5 SYNONYM: MAP KINASE SIGNAL-INTEGRATING KINASE 2, MNK2;               
COMPND   6 EC: 2.7.1.37;                                                        
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 BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX-4T1                                  
KEYWDS    DFD MOTIF, TRANSFERASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.JAUCH,M.C.WAHL,C.NETTER,S.JAKEL,K.SCHREITER,B.AICHER,H.JACKLE       
REVDAT   4   13-JUL-11 2AC3    1       VERSN                                    
REVDAT   3   03-NOV-10 2AC3    1       JRNL                                     
REVDAT   2   24-FEB-09 2AC3    1       VERSN                                    
REVDAT   1   04-OCT-05 2AC3    0                                                
JRNL        AUTH   R.JAUCH,S.JAKEL,C.NETTER,K.SCHREITER,B.AICHER,H.JACKLE,      
JRNL        AUTH 2 M.C.WAHL                                                     
JRNL        TITL   CRYSTAL STRUCTURES OF THE MNK2 KINASE DOMAIN REVEAL AN       
JRNL        TITL 2 INHIBITORY CONFORMATION AND A ZINC BINDING SITE.             
JRNL        REF    STRUCTURE                     V.  13  1559 2005              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   16216586                                                     
JRNL        DOI    10.1016/J.STR.2005.07.013                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 15.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 24664                          
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) : 0.217                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.254                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1295                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1851                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.59                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3050                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 93                           
REMARK   3   BIN FREE R VALUE                    : 0.3520                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2215                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 161                                     
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) : 75.77                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.83000                                             
REMARK   3    B22 (A**2) : -1.83000                                             
REMARK   3    B33 (A**2) : 2.75000                                              
REMARK   3    B12 (A**2) : -0.92000                                             
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): 0.184         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.171         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 11.283        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.950                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2266 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3060 ; 1.207 ; 1.947       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   274 ; 5.773 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   116 ;37.648 ;24.138       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   390 ;16.510 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    15 ;15.152 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   326 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1747 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   974 ; 0.212 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1555 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   139 ; 0.175 ; 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):    85 ; 0.184 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.199 ; 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):  1419 ; 4.357 ; 4.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2212 ; 5.630 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   958 ; 4.677 ; 4.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   848 ; 6.400 ; 6.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
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    70        A   128                          
REMARK   3    RESIDUE RANGE :   A   154        A   184                          
REMARK   3    ORIGIN FOR THE GROUP (A):  41.3010  34.0820  10.9990              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0256 T22:  -0.0207                                     
REMARK   3      T33:  -0.1915 T12:  -0.0536                                     
REMARK   3      T13:  -0.0042 T23:   0.0517                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5710 L22:   2.5582                                     
REMARK   3      L33:   2.2195 L12:   1.9455                                     
REMARK   3      L13:   2.8960 L23:   1.6460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3010 S12:  -0.7611 S13:  -0.3660                       
REMARK   3      S21:   0.3393 S22:  -0.2828 S23:   0.3725                       
REMARK   3      S31:   0.3537 S32:  -0.5270 S33:  -0.0182                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   129        A   153                          
REMARK   3    RESIDUE RANGE :   A   204        A   258                          
REMARK   3    RESIDUE RANGE :   A   263        A   322                          
REMARK   3    ORIGIN FOR THE GROUP (A):  51.0060  58.2180   7.7040              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1519 T22:  -0.1828                                     
REMARK   3      T33:  -0.1826 T12:  -0.0681                                     
REMARK   3      T13:  -0.0762 T23:   0.0036                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0262 L22:   2.0337                                     
REMARK   3      L33:   2.5167 L12:  -2.0000                                     
REMARK   3      L13:   2.2786 L23:  -1.5077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2456 S12:  -0.1082 S13:   0.8938                       
REMARK   3      S21:  -0.0821 S22:   0.0027 S23:  -0.2995                       
REMARK   3      S31:  -0.2045 S32:  -0.1068 S33:   0.2429                       
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: NULL                                      
REMARK   4                                                                      
REMARK   4 2AC3 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-05.                  
REMARK 100 THE RCSB ID CODE IS RCSB033729.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-JUN-04                          
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               : MPG/DESY, HAMBURG                  
REMARK 200  BEAMLINE                       : BW6                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.05                               
REMARK 200  MONOCHROMATOR                  : BW6                                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31011                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
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) : 2.10                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.52                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SALT, PH 7, VAPOR DIFFUSION,             
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+1/3                                           
REMARK 290       6555   -X,-X+Y,-Z+2/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       48.23400            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.11700            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.11700            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       48.23400            
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: MONOMERIC                         
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 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A   232                                                      
REMARK 465     ILE A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     LEU A   235                                                      
REMARK 465     ASN A   236                                                      
REMARK 465     GLY A   237                                                      
REMARK 465     ASP A   238                                                      
REMARK 465     CYS A   239                                                      
REMARK 465     SER A   240                                                      
REMARK 465     PRO A   241                                                      
REMARK 465     ILE A   242                                                      
REMARK 465     SER A   243                                                      
REMARK 465     THR A   244                                                      
REMARK 465     PRO A   245                                                      
REMARK 465     GLU A   246                                                      
REMARK 465     LEU A   247                                                      
REMARK 465     LEU A   248                                                      
REMARK 465     THR A   249                                                      
REMARK 465     PRO A   250                                                      
REMARK 465     ASP A   306                                                      
REMARK 465     ARG A   307                                                      
REMARK 465     GLY A   308                                                      
REMARK 465     GLU A   309                                                      
REMARK 465     GLY A   370                                                      
REMARK 465     CYS A   371                                                      
REMARK 465     ALA A   372                                                      
REMARK 465     PRO A   373                                                      
REMARK 465     GLU A   374                                                      
REMARK 465     ASN A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     LEU A   377                                                      
REMARK 465     PRO A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     PRO A   380                                                      
REMARK 465     MET A   381                                                      
REMARK 465     VAL A   382                                                      
REMARK 465     LEU A   383                                                      
REMARK 465     GLN A   384                                                      
REMARK 465     ARG A   385                                                      
REMARK 475                                                                      
REMARK 475 ZERO OCCUPANCY RESIDUES                                              
REMARK 475 THE FOLLOWING RESIDUES WERE MODELED WITH ZERO OCCUPANCY.             
REMARK 475 THE LOCATION AND PROPERTIES OF THESE RESIDUES MAY NOT                
REMARK 475 BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;                      
REMARK 475 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE)          
REMARK 475   M RES C SSEQI                                                      
REMARK 475     ASP A  226                                                       
REMARK 475     PHE A  227                                                       
REMARK 475     ASP A  228                                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    PHE A    79     O    VAL A    82              2.02            
REMARK 500   O    HOH A   646     O    HOH A   648              2.05            
REMARK 500   O    HOH A   639     O    HOH A   641              2.08            
REMARK 500   O    HOH A   647     O    HOH A   648              2.12            
REMARK 500   OE2  GLU A   129     O    HOH A   657              2.18            
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  73      107.41    -43.45                                   
REMARK 500    TYR A  83      131.74     84.46                                   
REMARK 500    GLU A  87       80.07    -63.16                                   
REMARK 500    LEU A  90        6.78    -65.10                                   
REMARK 500    ILE A 122       94.70     39.38                                   
REMARK 500    GLU A 152      -73.05    -10.39                                   
REMARK 500    ARG A 175      -46.12     75.52                                   
REMARK 500    ARG A 204       -9.80     83.27                                   
REMARK 500    SER A 301       46.71   -148.09                                   
REMARK 500    ASP A 302       56.38   -143.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 558        DISTANCE =  5.42 ANGSTROMS                       
REMARK 525    HOH A 583        DISTANCE =  5.68 ANGSTROMS                       
REMARK 525    HOH A 605        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH A 615        DISTANCE =  5.35 ANGSTROMS                       
REMARK 525    HOH A 619        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH A 620        DISTANCE =  8.76 ANGSTROMS                       
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                              ZN A 531  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 311   SG                                                     
REMARK 620 2 CYS A 299   SG  119.2                                              
REMARK 620 3 CYS A 303   SG  118.9 110.9                                        
REMARK 620 4 CYS A 314   SG  108.3  93.6 100.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 531                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2AC5   RELATED DB: PDB                                   
REMARK 900 MNK2 KINASE DOMAIN MUTANT D228G                                      
DBREF  2AC3 A   72   385  UNP    Q9HBH9   MKNK2_HUMAN     25    338             
SEQADV 2AC3 GLY A   70  UNP  Q9HBH9              EXPRESSION TAG                 
SEQADV 2AC3 SER A   71  UNP  Q9HBH9              EXPRESSION TAG                 
SEQRES   1 A  316  GLY SER THR ASP SER PHE SER GLY ARG PHE GLU ASP VAL          
SEQRES   2 A  316  TYR GLN LEU GLN GLU ASP VAL LEU GLY GLU GLY ALA HIS          
SEQRES   3 A  316  ALA ARG VAL GLN THR CYS ILE ASN LEU ILE THR SER GLN          
SEQRES   4 A  316  GLU TYR ALA VAL LYS ILE ILE GLU LYS GLN PRO GLY HIS          
SEQRES   5 A  316  ILE ARG SER ARG VAL PHE ARG GLU VAL GLU MET LEU TYR          
SEQRES   6 A  316  GLN CYS GLN GLY HIS ARG ASN VAL LEU GLU LEU ILE GLU          
SEQRES   7 A  316  PHE PHE GLU GLU GLU ASP ARG PHE TYR LEU VAL PHE GLU          
SEQRES   8 A  316  LYS MET ARG GLY GLY SER ILE LEU SER HIS ILE HIS LYS          
SEQRES   9 A  316  ARG ARG HIS PHE ASN GLU LEU GLU ALA SER VAL VAL VAL          
SEQRES  10 A  316  GLN ASP VAL ALA SER ALA LEU ASP PHE LEU HIS ASN LYS          
SEQRES  11 A  316  GLY ILE ALA HIS ARG ASP LEU LYS PRO GLU ASN ILE LEU          
SEQRES  12 A  316  CYS GLU HIS PRO ASN GLN VAL SER PRO VAL LYS ILE CYS          
SEQRES  13 A  316  ASP PHE ASP LEU GLY SER GLY ILE LYS LEU ASN GLY ASP          
SEQRES  14 A  316  CYS SER PRO ILE SER THR PRO GLU LEU LEU THR PRO CYS          
SEQRES  15 A  316  GLY SER ALA GLU TYR MET ALA PRO GLU VAL VAL GLU ALA          
SEQRES  16 A  316  PHE SER GLU GLU ALA SER ILE TYR ASP LYS ARG CYS ASP          
SEQRES  17 A  316  LEU TRP SER LEU GLY VAL ILE LEU TYR ILE LEU LEU SER          
SEQRES  18 A  316  GLY TYR PRO PRO PHE VAL GLY ARG CYS GLY SER ASP CYS          
SEQRES  19 A  316  GLY TRP ASP ARG GLY GLU ALA CYS PRO ALA CYS GLN ASN          
SEQRES  20 A  316  MET LEU PHE GLU SER ILE GLN GLU GLY LYS TYR GLU PHE          
SEQRES  21 A  316  PRO ASP LYS ASP TRP ALA HIS ILE SER CYS ALA ALA LYS          
SEQRES  22 A  316  ASP LEU ILE SER LYS LEU LEU VAL ARG ASP ALA LYS GLN          
SEQRES  23 A  316  ARG LEU SER ALA ALA GLN VAL LEU GLN HIS PRO TRP VAL          
SEQRES  24 A  316  GLN GLY CYS ALA PRO GLU ASN THR LEU PRO THR PRO MET          
SEQRES  25 A  316  VAL LEU GLN ARG                                              
HET     ZN  A 531       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL   2   ZN    ZN 2+                                                        
FORMUL   3  HOH   *161(H2 O)                                                    
HELIX    1   1 ILE A  122  CYS A  136  1                                  15    
HELIX    2   2 SER A  166  ARG A  175  1                                  10    
HELIX    3   3 ASN A  178  LYS A  199  1                                  22    
HELIX    4   4 LYS A  207  GLU A  209  5                                   3    
HELIX    5   5 SER A  253  MET A  257  5                                   5    
HELIX    6   6 ALA A  258  PHE A  265  1                                   8    
HELIX    7   7 SER A  266  ASP A  273  1                                   8    
HELIX    8   8 ARG A  275  GLY A  291  1                                  17    
HELIX    9   9 CYS A  311  GLY A  325  1                                  15    
HELIX   10  10 PRO A  330  ALA A  335  1                                   6    
HELIX   11  11 SER A  338  LEU A  349  1                                  12    
HELIX   12  12 SER A  358  HIS A  365  1                                   8    
SHEET    1   A 5 GLN A  84  LEU A  85  0                                        
SHEET    2   A 5 ALA A  96  ILE A 102 -1  O  ILE A 102   N  GLN A  84           
SHEET    3   A 5 GLU A 109  GLU A 116 -1  O  ILE A 114   N  ARG A  97           
SHEET    4   A 5 ARG A 154  GLU A 160 -1  O  PHE A 159   N  ALA A 111           
SHEET    5   A 5 LEU A 145  GLU A 151 -1  N  GLU A 147   O  VAL A 158           
SHEET    1   B 2 ILE A 211  CYS A 213  0                                        
SHEET    2   B 2 VAL A 222  ILE A 224 -1  O  LYS A 223   N  LEU A 212           
LINK        ZN    ZN A 531                 SG  CYS A 311     1555   1555  2.29  
LINK        ZN    ZN A 531                 SG  CYS A 299     1555   1555  2.35  
LINK        ZN    ZN A 531                 SG  CYS A 303     1555   1555  2.49  
LINK        ZN    ZN A 531                 SG  CYS A 314     1555   1555  2.47  
CISPEP   1 PRO A  119    GLY A  120          0        -9.78                     
CISPEP   2 SER A  220    PRO A  221          0        -0.87                     
SITE     1 AC1  4 CYS A 299  CYS A 303  CYS A 311  CYS A 314                    
CRYST1  104.502  104.502   72.351  90.00  90.00 120.00 P 32 2 1      6          
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      0.009569  0.005525  0.000000        0.00000                         
SCALE2      0.000000  0.011050  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013822        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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