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Database: PDB
Entry: 3K2A
LinkDB: 3K2A
Original site: 3K2A 
HEADER    DNA BINDING PROTEIN                     29-SEP-09   3K2A              
TITLE     CRYSTAL STRUCTURE OF THE HOMEOBOX DOMAIN OF HUMAN HOMEOBOX PROTEIN    
TITLE    2 MEIS2                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HOMEOBOX PROTEIN MEIS2;                                    
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 281-345 (HOMEOBOX DOMAIN);                        
COMPND   5 SYNONYM: MEIS1-RELATED PROTEIN 1;                                    
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MEIS2, MRG1;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28-LIC                                 
KEYWDS    HOMEOBOX DOMAIN, HUMAN HOMEOBOX PROTEIN MEIS2, DNA-BINDING,           
KEYWDS   2 TRANSCRIPTION, HOMEOBOX, NUCLEUS, PHOSPHOPROTEIN, DNA BINDING        
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.LAM,M.SOLOVEYCHIK,K.P.BATTAILE,V.ROMANOV,K.LAM,I.BELETSKAYA,        
AUTHOR   2 E.GORDON,E.F.PAI,N.Y.CHIRGADZE                                       
REVDAT   2   01-NOV-17 3K2A    1       REMARK                                   
REVDAT   1   13-OCT-10 3K2A    0                                                
JRNL        AUTH   R.LAM,M.SOLOVEYCHIK,K.P.BATTAILE,V.ROMANOV,K.LAM,            
JRNL        AUTH 2 I.BELETSKAYA,E.GORDON,E.F.PAI,N.Y.CHIRGADZE                  
JRNL        TITL   CRYSTAL STRUCTURE OF THE HOMEOBOX DOMAIN OF HUMAN HOMEOBOX   
JRNL        TITL 2 PROTEIN MEIS2                                                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.95 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC REFMAC_5.5.0102                               
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) : 1.95                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 25.13                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 12250                          
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) : 0.216                           
REMARK   3   R VALUE            (WORKING SET) : 0.215                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 590                             
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) : 1.95                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.00                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 843                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.89                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 51                           
REMARK   3   BIN FREE R VALUE                    : 0.3170                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 931                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 48                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.97                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.41000                                              
REMARK   3    B22 (A**2) : 0.41000                                              
REMARK   3    B33 (A**2) : -0.81000                                             
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): 0.153         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.092         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.039         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.937                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   962 ; 0.013 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1303 ; 1.082 ; 1.924       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   109 ; 4.238 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    49 ;38.850 ;23.673       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   169 ;13.549 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;10.084 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   141 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   731 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):   565 ; 0.776 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   917 ; 1.473 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   397 ; 2.055 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   386 ; 3.337 ; 4.500       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   284        A   338                          
REMARK   3    ORIGIN FOR THE GROUP (A):  34.1210  39.9710  14.9980              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0879 T22:   0.0485                                     
REMARK   3      T33:   0.0567 T12:  -0.0564                                     
REMARK   3      T13:   0.0162 T23:  -0.0288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8310 L22:   3.0843                                     
REMARK   3      L33:   2.2103 L12:  -0.3800                                     
REMARK   3      L13:  -0.1380 L23:   1.0562                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0457 S12:  -0.0304 S13:   0.0023                       
REMARK   3      S21:  -0.2415 S22:   0.0309 S23:  -0.0110                       
REMARK   3      S31:  -0.2425 S32:   0.1187 S33:  -0.0765                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   283        B   338                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6800  52.7200  35.4760              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1172 T22:   0.0212                                     
REMARK   3      T33:   0.0563 T12:  -0.0198                                     
REMARK   3      T13:   0.0552 T23:  -0.0225                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2856 L22:   6.0776                                     
REMARK   3      L33:   1.1120 L12:  -0.5094                                     
REMARK   3      L13:  -0.0491 L23:   1.2554                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0770 S12:  -0.0078 S13:   0.0058                       
REMARK   3      S21:   0.3120 S22:   0.0490 S23:   0.2093                       
REMARK   3      S31:   0.0121 S32:  -0.0671 S33:   0.0281                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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. U VALUES: RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3K2A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-SEP-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000055455.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97910                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : SI(111) DOUBLE-CRYSTAL             
REMARK 200                                   MONOCHROMATOR                      
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12319                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.950                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY                : 28.50                              
REMARK 200  R MERGE                    (I) : 0.06300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.95                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.02                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 29.00                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.47300                            
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: SAD                          
REMARK 200 SOFTWARE USED: SHARP, DM 5.0                                         
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG4000, 8% ISOPROPANOL, 0.1M        
REMARK 280  SODIUM ACETATE, 10MM L-PROLINE, PH 7.5, VAPOR DIFFUSION, SITTING    
REMARK 280  DROP, TEMPERATURE 298.0K                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4 2 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   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   -X,Y,-Z                                                 
REMARK 290       6555   X,-Y,-Z                                                 
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290       9555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290      10555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290      11555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290      12555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290      13555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290      14555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290      15555   Y+1/2,X+1/2,-Z+1/2                                      
REMARK 290      16555   -Y+1/2,-X+1/2,-Z+1/2                                    
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  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  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        0.00000            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9  1.000000  0.000000  0.000000       56.79850            
REMARK 290   SMTRY2   9  0.000000  1.000000  0.000000       56.79850            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       25.12550            
REMARK 290   SMTRY1  10 -1.000000  0.000000  0.000000       56.79850            
REMARK 290   SMTRY2  10  0.000000 -1.000000  0.000000       56.79850            
REMARK 290   SMTRY3  10  0.000000  0.000000  1.000000       25.12550            
REMARK 290   SMTRY1  11  0.000000 -1.000000  0.000000       56.79850            
REMARK 290   SMTRY2  11  1.000000  0.000000  0.000000       56.79850            
REMARK 290   SMTRY3  11  0.000000  0.000000  1.000000       25.12550            
REMARK 290   SMTRY1  12  0.000000  1.000000  0.000000       56.79850            
REMARK 290   SMTRY2  12 -1.000000  0.000000  0.000000       56.79850            
REMARK 290   SMTRY3  12  0.000000  0.000000  1.000000       25.12550            
REMARK 290   SMTRY1  13 -1.000000  0.000000  0.000000       56.79850            
REMARK 290   SMTRY2  13  0.000000  1.000000  0.000000       56.79850            
REMARK 290   SMTRY3  13  0.000000  0.000000 -1.000000       25.12550            
REMARK 290   SMTRY1  14  1.000000  0.000000  0.000000       56.79850            
REMARK 290   SMTRY2  14  0.000000 -1.000000  0.000000       56.79850            
REMARK 290   SMTRY3  14  0.000000  0.000000 -1.000000       25.12550            
REMARK 290   SMTRY1  15  0.000000  1.000000  0.000000       56.79850            
REMARK 290   SMTRY2  15  1.000000  0.000000  0.000000       56.79850            
REMARK 290   SMTRY3  15  0.000000  0.000000 -1.000000       25.12550            
REMARK 290   SMTRY1  16  0.000000 -1.000000  0.000000       56.79850            
REMARK 290   SMTRY2  16 -1.000000  0.000000  0.000000       56.79850            
REMARK 290   SMTRY3  16  0.000000  0.000000 -1.000000       25.12550            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 33190 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 39020 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -260.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      113.59700            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      113.59700            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000      113.59700            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000      113.59700            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   5 -1.000000  0.000000  0.000000      113.59700            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000 -1.000000       50.25100            
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000 -1.000000  0.000000      113.59700            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000       50.25100            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000       50.25100            
REMARK 350   BIOMT1   8  0.000000 -1.000000  0.000000      113.59700            
REMARK 350   BIOMT2   8 -1.000000  0.000000  0.000000      113.59700            
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000       50.25100            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 CL    CL A 500  LIES ON A SPECIAL POSITION.                          
REMARK 375 CL    CL B 500  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A  37  LIES ON A SPECIAL POSITION.                          
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   279                                                      
REMARK 465     SER A   280                                                      
REMARK 465     GLY A   281                                                      
REMARK 465     ILE A   282                                                      
REMARK 465     PHE A   283                                                      
REMARK 465     ILE A   339                                                      
REMARK 465     ASP A   340                                                      
REMARK 465     GLN A   341                                                      
REMARK 465     SER A   342                                                      
REMARK 465     ASN A   343                                                      
REMARK 465     ARG A   344                                                      
REMARK 465     ALA A   345                                                      
REMARK 465     GLY B   279                                                      
REMARK 465     SER B   280                                                      
REMARK 465     GLY B   281                                                      
REMARK 465     ILE B   282                                                      
REMARK 465     ILE B   339                                                      
REMARK 465     ASP B   340                                                      
REMARK 465     GLN B   341                                                      
REMARK 465     SER B   342                                                      
REMARK 465     ASN B   343                                                      
REMARK 465     ARG B   344                                                      
REMARK 465     ALA B   345                                                      
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    HIS A 301       73.61   -150.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT A 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 500                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACT B 510                 
DBREF  3K2A A  281   345  UNP    O14770   MEIS2_HUMAN    281    345             
DBREF  3K2A B  281   345  UNP    O14770   MEIS2_HUMAN    281    345             
SEQADV 3K2A GLY A  279  UNP  O14770              EXPRESSION TAG                 
SEQADV 3K2A SER A  280  UNP  O14770              EXPRESSION TAG                 
SEQADV 3K2A GLY B  279  UNP  O14770              EXPRESSION TAG                 
SEQADV 3K2A SER B  280  UNP  O14770              EXPRESSION TAG                 
SEQRES   1 A   67  GLY SER GLY ILE PHE PRO LYS VAL ALA THR ASN ILE MSE          
SEQRES   2 A   67  ARG ALA TRP LEU PHE GLN HIS LEU THR HIS PRO TYR PRO          
SEQRES   3 A   67  SER GLU GLU GLN LYS LYS GLN LEU ALA GLN ASP THR GLY          
SEQRES   4 A   67  LEU THR ILE LEU GLN VAL ASN ASN TRP PHE ILE ASN ALA          
SEQRES   5 A   67  ARG ARG ARG ILE VAL GLN PRO MSE ILE ASP GLN SER ASN          
SEQRES   6 A   67  ARG ALA                                                      
SEQRES   1 B   67  GLY SER GLY ILE PHE PRO LYS VAL ALA THR ASN ILE MSE          
SEQRES   2 B   67  ARG ALA TRP LEU PHE GLN HIS LEU THR HIS PRO TYR PRO          
SEQRES   3 B   67  SER GLU GLU GLN LYS LYS GLN LEU ALA GLN ASP THR GLY          
SEQRES   4 B   67  LEU THR ILE LEU GLN VAL ASN ASN TRP PHE ILE ASN ALA          
SEQRES   5 B   67  ARG ARG ARG ILE VAL GLN PRO MSE ILE ASP GLN SER ASN          
SEQRES   6 B   67  ARG ALA                                                      
MODRES 3K2A MSE A  291  MET  SELENOMETHIONINE                                   
MODRES 3K2A MSE A  338  MET  SELENOMETHIONINE                                   
MODRES 3K2A MSE B  291  MET  SELENOMETHIONINE                                   
MODRES 3K2A MSE B  338  MET  SELENOMETHIONINE                                   
HET    MSE  A 291       8                                                       
HET    MSE  A 338       8                                                       
HET    MSE  B 291       8                                                       
HET    MSE  B 338       8                                                       
HET     CL  A 500       1                                                       
HET    ACT  A 510       4                                                       
HET     CL  B 500       1                                                       
HET    ACT  B 510       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      CL CHLORIDE ION                                                     
HETNAM     ACT ACETATE ION                                                      
FORMUL   1  MSE    4(C5 H11 N O2 SE)                                            
FORMUL   3   CL    2(CL 1-)                                                     
FORMUL   4  ACT    2(C2 H3 O2 1-)                                               
FORMUL   7  HOH   *48(H2 O)                                                     
HELIX    1   1 PRO A  284  HIS A  298  1                                  15    
HELIX    2   2 SER A  305  GLY A  317  1                                  13    
HELIX    3   3 THR A  319  GLN A  336  1                                  18    
HELIX    4   4 PRO B  284  HIS B  298  1                                  15    
HELIX    5   5 SER B  305  GLY B  317  1                                  13    
HELIX    6   6 THR B  319  GLN B  336  1                                  18    
LINK         C   ILE A 290                 N   MSE A 291     1555   1555  1.33  
LINK         C   MSE A 291                 N   ARG A 292     1555   1555  1.34  
LINK         C   PRO A 337                 N   MSE A 338     1555   1555  1.34  
LINK         C   ILE B 290                 N   MSE B 291     1555   1555  1.33  
LINK         C   MSE B 291                 N   ARG B 292     1555   1555  1.34  
LINK         C   PRO B 337                 N   MSE B 338     1555   1555  1.34  
SITE     1 AC1  2 HOH A   4  ARG A 292                                          
SITE     1 AC2  3 GLN A 297  LEU A 299  ARG B 331                               
SITE     1 AC3  2 HOH B   1  ARG B 292                                          
SITE     1 AC4  3 ARG A 331  GLN B 297  LEU B 299                               
CRYST1  113.597  113.597   50.251  90.00  90.00  90.00 I 4 2 2      32          
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      0.008803  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008803  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.019900        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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