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Database: PDB
Entry: 4XRS
LinkDB: 4XRS
Original site: 4XRS 
HEADER    TRANSCRIPTION                           21-JAN-15   4XRS              
TITLE     HETERODIMERIC COMPLEX OF TRANSCRIPTION FACTORS MEIS1 AND DLX3 ON      
TITLE    2 SPECIFIC DNA                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DNA (5'-D(P*CP*AP*AP*TP*TP*AP*TP*CP*CP*TP*GP*TP*CP*AP*A)-  
COMPND   3 3');                                                                 
COMPND   4 CHAIN: M;                                                            
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: DNA (5'-                                                   
COMPND   8 D(P*AP*CP*AP*AP*TP*TP*AP*TP*CP*CP*TP*GP*TP*CP*AP*AP*C)-3');          
COMPND   9 CHAIN: D;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: DNA (5'-                                                   
COMPND  13 D(P*GP*TP*TP*GP*AP*CP*AP*GP*GP*AP*TP*AP*AP*TP*TP*GP*TP*T)-3');       
COMPND  14 CHAIN: E;                                                            
COMPND  15 ENGINEERED: YES;                                                     
COMPND  16 MOL_ID: 4;                                                           
COMPND  17 MOLECULE: DNA (5'-                                                   
COMPND  18 D(P*TP*TP*GP*AP*CP*AP*GP*GP*AP*TP*AP*AP*TP*TP*GP*T)-3');             
COMPND  19 CHAIN: L;                                                            
COMPND  20 ENGINEERED: YES;                                                     
COMPND  21 MOL_ID: 5;                                                           
COMPND  22 MOLECULE: HOMEOBOX PROTEIN MEIS1;                                    
COMPND  23 CHAIN: A, B;                                                         
COMPND  24 FRAGMENT: UNP RESIDUES 283-340;                                      
COMPND  25 ENGINEERED: YES;                                                     
COMPND  26 MOL_ID: 6;                                                           
COMPND  27 MOLECULE: HOMEOBOX PROTEIN DLX-3;                                    
COMPND  28 CHAIN: G, I;                                                         
COMPND  29 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   4 ORGANISM_TAXID: 32630;                                               
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 SYNTHETIC: YES;                                                      
SOURCE   7 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE   8 ORGANISM_TAXID: 32630;                                               
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 SYNTHETIC: YES;                                                      
SOURCE  11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  12 ORGANISM_TAXID: 32630;                                               
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 SYNTHETIC: YES;                                                      
SOURCE  15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  16 ORGANISM_TAXID: 32630;                                               
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  19 ORGANISM_COMMON: HUMAN;                                              
SOURCE  20 ORGANISM_TAXID: 9606;                                                
SOURCE  21 GENE: MEIS1;                                                         
SOURCE  22 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  24 EXPRESSION_SYSTEM_VARIANT: ROSETTA;                                  
SOURCE  25 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  26 EXPRESSION_SYSTEM_PLASMID: PETG20A;                                  
SOURCE  27 MOL_ID: 6;                                                           
SOURCE  28 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  29 ORGANISM_COMMON: HUMAN;                                              
SOURCE  30 ORGANISM_TAXID: 9606;                                                
SOURCE  31 GENE: DLX3;                                                          
SOURCE  32 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  33 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  34 EXPRESSION_SYSTEM_VARIANT: ROSETTA;                                  
SOURCE  35 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  36 EXPRESSION_SYSTEM_PLASMID: PETG20A                                   
KEYWDS    TRANSCRIPTION, HETERODIMER, DNA                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.JORMA,Y.YIN,K.R.NITTA,K.DAVE,M.ENGE,T.KIVIOJA,A.POPOV,E.MORGUNOVA,  
AUTHOR   2 J.TAIPALE                                                            
REVDAT   4   03-APR-19 4XRS    1       SOURCE                                   
REVDAT   3   02-DEC-15 4XRS    1       JRNL                                     
REVDAT   2   18-NOV-15 4XRS    1       JRNL                                     
REVDAT   1   04-NOV-15 4XRS    0                                                
JRNL        AUTH   A.JOLMA,Y.YIN,K.R.NITTA,K.DAVE,A.POPOV,M.TAIPALE,M.ENGE,     
JRNL        AUTH 2 T.KIVIOJA,E.MORGUNOVA,J.TAIPALE                              
JRNL        TITL   DNA-DEPENDENT FORMATION OF TRANSCRIPTION FACTOR PAIRS ALTERS 
JRNL        TITL 2 THEIR BINDING SPECIFICITY.                                   
JRNL        REF    NATURE                        V. 527   384 2015              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   26550823                                                     
JRNL        DOI    10.1038/NATURE15518                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX PHENIX.REFINE: 1.9_1692                       
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : TWIN_LSQ_F                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.31                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.270                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 6829                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.343                           
REMARK   3   R VALUE            (WORKING SET) : 0.331                           
REMARK   3   FREE R VALUE                     : 0.359                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.330                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 651                             
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.7704 -  5.5578    0.82     2845   139  0.3022 0.3086        
REMARK   3     2  5.5578 -  4.4127    0.84     2890   157  0.3674 0.4049        
REMARK   3     3  4.4127 -  3.8552    0.85     2941   153  0.3819 0.4272        
REMARK   3     4  3.8552 -  3.5029    0.84     2894   163  0.3823 0.4685        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 45.010           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 109.7                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 136.3                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: 0.0800                                                   
REMARK   3   OPERATOR: K,H,-L                                                   
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           3471                                  
REMARK   3   ANGLE     :  1.179           4961                                  
REMARK   3   CHIRALITY :  0.183            550                                  
REMARK   3   PLANARITY :  0.007            398                                  
REMARK   3   DIHEDRAL  : 27.214           1390                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XRS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 03-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206212.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7 - 8                              
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9724                             
REMARK 200  MONOCHROMATOR                  : MIRROR                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11191                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
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     (%) : 90.5                               
REMARK 200  DATA REDUNDANCY                : 4.100                              
REMARK 200  R MERGE                    (I) : 0.06080                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.0800                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.96                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.06080                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.630                              
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: 3K2A, 2DJN                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.98                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TRIS, MAGNESIUM CHLORIDE,      
REMARK 280  BUTHANOL, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       34.81800            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       58.44400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       34.92250            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       58.44400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       34.81800            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       34.92250            
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: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14060 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: M, L, A, G                            
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: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4260 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 14450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, B, I                            
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      DG L     1                                                      
REMARK 465     PHE A   279                                                      
REMARK 465     ASP A   336                                                      
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     LYS I 131    CG   CD   CE   NZ                                   
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    ALA A   309     N    GLY A   313              2.01            
REMARK 500   O    LEU I   156     N    ALA I   160              2.03            
REMARK 500   O3'   DA L    13     N    LYS G   131              2.05            
REMARK 500   O    ALA B   309     N    GLY B   313              2.15            
REMARK 500   O    LYS B   305     N    ALA B   309              2.15            
REMARK 500   O2    DT E    11     NH2  ARG I   133              2.17            
REMARK 500   NH2  ARG I   159     O    GLN I   170              2.17            
REMARK 500   OE2  GLU A   302     NZ   LYS A   305              2.19            
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     DA M  26   O4' -  C1' -  N9  ANGL. DEV. =   1.8 DEGREES          
REMARK 500     DT M  27   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DC M  29   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DA D  23   O4' -  C1' -  N9  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT D  24   O4' -  C1' -  N1  ANGL. DEV. =   2.7 DEGREES          
REMARK 500     DT D  25   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT D  27   O4' -  C1' -  N1  ANGL. DEV. =   2.1 DEGREES          
REMARK 500     DC D  29   O4' -  C1' -  N1  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DC D  33   O4' -  C1' -  N1  ANGL. DEV. =   4.1 DEGREES          
REMARK 500     DG E   1   O4' -  C1' -  N9  ANGL. DEV. =   2.4 DEGREES          
REMARK 500     DT E   3   O4' -  C1' -  N1  ANGL. DEV. =   2.3 DEGREES          
REMARK 500     DC E   6   O4' -  C1' -  N1  ANGL. DEV. =   2.6 DEGREES          
REMARK 500     DT L   3   O4' -  C1' -  N1  ANGL. DEV. =   2.9 DEGREES          
REMARK 500     DC L   6   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DT L  15   O4' -  C1' -  N1  ANGL. DEV. =   3.5 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    THR A 284      -59.38   -125.34                                   
REMARK 500    PRO A 298       67.77    -64.24                                   
REMARK 500    ALA A 309      -87.32    -70.29                                   
REMARK 500    LEU A 314      176.62     71.01                                   
REMARK 500    ALA A 326       -3.86   -147.62                                   
REMARK 500    VAL A 331      -46.80     60.20                                   
REMARK 500    LYS B 281     -156.34     59.73                                   
REMARK 500    THR B 312       -8.81   -140.53                                   
REMARK 500    ARG B 327       60.29    -68.25                                   
REMARK 500    ARG B 328      -77.83   -161.48                                   
REMARK 500    PRO G 132     -160.77    -72.05                                   
REMARK 500    THR G 134       96.66     56.30                                   
REMARK 500    SER G 137       19.00   -152.36                                   
REMARK 500    SER G 138     -103.18    -73.59                                   
REMARK 500    TYR G 139       89.80   -162.34                                   
REMARK 500    GLN G 140      -80.76     86.52                                   
REMARK 500    LEU G 141      -79.59    -75.59                                   
REMARK 500    ALA G 155     -155.88   -111.67                                   
REMARK 500    ALA G 160      -80.46    -59.22                                   
REMARK 500    ALA G 163      -33.32   -150.10                                   
REMARK 500    VAL G 173       -1.14   -141.50                                   
REMARK 500    PHE G 184     -107.85     48.93                                   
REMARK 500    THR I 134      143.03     70.24                                   
REMARK 500    GLN I 140      -56.63     76.46                                   
REMARK 500    LEU I 141      -77.39    -66.76                                   
REMARK 500    ARG I 147      -39.49     76.67                                   
REMARK 500    LYS I 150     -125.59    -79.84                                   
REMARK 500    LEU I 154     -151.13   -135.20                                   
REMARK 500    LEU I 166      -71.56     72.96                                   
REMARK 500    LEU I 168     -150.39   -137.63                                   
REMARK 500    VAL I 173      -55.20   -132.14                                   
REMARK 500    PHE I 177      -73.28    -49.74                                   
REMARK 500    PHE I 184      139.93   -175.88                                   
REMARK 500    LYS I 185     -110.40     52.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ARG B  328     ARG B  329                 -140.67                    
REMARK 500 ARG G  181     SER G  182                  148.82                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4XRS M   21    35  PDB    4XRS     4XRS            21     35             
DBREF  4XRS D   20    36  PDB    4XRS     4XRS            20     36             
DBREF  4XRS E    1    18  PDB    4XRS     4XRS             1     18             
DBREF  4XRS L    1    17  PDB    4XRS     4XRS             1     17             
DBREF  4XRS A  279   336  UNP    O00470   MEIS1_HUMAN    279    336             
DBREF  4XRS B  279   336  UNP    O00470   MEIS1_HUMAN    279    336             
DBREF  4XRS G  131   186  UNP    O60479   DLX3_HUMAN     131    186             
DBREF  4XRS I  131   186  UNP    O60479   DLX3_HUMAN     131    186             
SEQRES   1 M   15   DC  DA  DA  DT  DT  DA  DT  DC  DC  DT  DG  DT  DC          
SEQRES   2 M   15   DA  DA                                                      
SEQRES   1 D   17   DA  DC  DA  DA  DT  DT  DA  DT  DC  DC  DT  DG  DT          
SEQRES   2 D   17   DC  DA  DA  DC                                              
SEQRES   1 E   18   DG  DT  DT  DG  DA  DC  DA  DG  DG  DA  DT  DA  DA          
SEQRES   2 E   18   DT  DT  DG  DT  DT                                          
SEQRES   1 L   17   DG  DT  DT  DG  DA  DC  DA  DG  DG  DA  DT  DA  DA          
SEQRES   2 L   17   DT  DT  DG  DT                                              
SEQRES   1 A   58  PHE PRO LYS VAL ALA THR ASN ILE MET ARG ALA TRP LEU          
SEQRES   2 A   58  PHE GLN HIS LEU THR HIS PRO TYR PRO SER GLU GLU GLN          
SEQRES   3 A   58  LYS LYS GLN LEU ALA GLN ASP THR GLY LEU THR ILE LEU          
SEQRES   4 A   58  GLN VAL ASN ASN TRP PHE ILE ASN ALA ARG ARG ARG ILE          
SEQRES   5 A   58  VAL GLN PRO MET ILE ASP                                      
SEQRES   1 B   58  PHE PRO LYS VAL ALA THR ASN ILE MET ARG ALA TRP LEU          
SEQRES   2 B   58  PHE GLN HIS LEU THR HIS PRO TYR PRO SER GLU GLU GLN          
SEQRES   3 B   58  LYS LYS GLN LEU ALA GLN ASP THR GLY LEU THR ILE LEU          
SEQRES   4 B   58  GLN VAL ASN ASN TRP PHE ILE ASN ALA ARG ARG ARG ILE          
SEQRES   5 B   58  VAL GLN PRO MET ILE ASP                                      
SEQRES   1 G   56  LYS PRO ARG THR ILE TYR SER SER TYR GLN LEU ALA ALA          
SEQRES   2 G   56  LEU GLN ARG ARG PHE GLN LYS ALA GLN TYR LEU ALA LEU          
SEQRES   3 G   56  PRO GLU ARG ALA GLU LEU ALA ALA GLN LEU GLY LEU THR          
SEQRES   4 G   56  GLN THR GLN VAL LYS ILE TRP PHE GLN ASN ARG ARG SER          
SEQRES   5 G   56  LYS PHE LYS LYS                                              
SEQRES   1 I   56  LYS PRO ARG THR ILE TYR SER SER TYR GLN LEU ALA ALA          
SEQRES   2 I   56  LEU GLN ARG ARG PHE GLN LYS ALA GLN TYR LEU ALA LEU          
SEQRES   3 I   56  PRO GLU ARG ALA GLU LEU ALA ALA GLN LEU GLY LEU THR          
SEQRES   4 I   56  GLN THR GLN VAL LYS ILE TRP PHE GLN ASN ARG ARG SER          
SEQRES   5 I   56  LYS PHE LYS LYS                                              
HELIX    1 AA1 THR A  284  TRP A  290  1                                   7    
HELIX    2 AA2 GLU A  303  GLN A  310  1                                   8    
HELIX    3 AA3 THR A  315  PHE A  323  1                                   9    
HELIX    4 AA4 LYS B  281  PHE B  292  1                                  12    
HELIX    5 AA5 GLN B  293  LEU B  295  5                                   3    
HELIX    6 AA6 SER B  301  GLN B  310  1                                  10    
HELIX    7 AA7 VAL B  319  ILE B  324  1                                   6    
HELIX    8 AA8 VAL B  331  ILE B  335  5                                   5    
HELIX    9 AA9 LEU G  144  ALA G  151  1                                   8    
HELIX   10 AB1 GLU G  158  ALA G  164  1                                   7    
HELIX   11 AB2 GLN G  170  ASN G  179  1                                  10    
HELIX   12 AB3 LEU I  141  ALA I  143  5                                   3    
HELIX   13 AB4 LEU I  144  GLN I  149  1                                   6    
HELIX   14 AB5 ALA I  155  ALA I  163  1                                   9    
HELIX   15 AB6 THR I  169  GLN I  172  5                                   4    
HELIX   16 AB7 VAL I  173  SER I  182  1                                  10    
CISPEP   1 LYS G  131    PRO G  132          0         0.45                     
CISPEP   2 TYR G  136    SER G  137          0       -25.55                     
CISPEP   3 TYR G  139    GLN G  140          0        -7.26                     
CISPEP   4 SER G  182    LYS G  183          0        28.82                     
CISPEP   5 LYS I  131    PRO I  132          0        -6.10                     
CISPEP   6 TYR I  136    SER I  137          0        -5.32                     
CISPEP   7 TYR I  139    GLN I  140          0       -12.04                     
CISPEP   8 PHE I  184    LYS I  185          0        -0.63                     
CRYST1   69.636   69.845  116.888  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014360  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014317  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008555        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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