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Database: PDB
Entry: 4IRH
LinkDB: 4IRH
Original site: 4IRH 
HEADER    DNA BINDING PROTEIN                     14-JAN-13   4IRH              
TITLE     AUTO-INHIBITED ERG ETS DOMAIN                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSCRIPTIONAL REGULATOR ERG;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: ETS DOMAIN;                                                
COMPND   5 SYNONYM: TRANSFORMING PROTEIN ERG;                                   
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: ERG;                                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    WINGED HELIX-TURN-HELIX, ETS DOMAIN, DNA BINDING PROTEIN              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.C.REGAN,P.S.HORANYI,E.E.PRYOR,J.L.SARVER,D.S.CAFISO,J.H.BUSHWELLER  
REVDAT   3   28-AUG-13 4IRH    1       JRNL                                     
REVDAT   2   14-AUG-13 4IRH    1       JRNL                                     
REVDAT   1   31-JUL-13 4IRH    0                                                
JRNL        AUTH   M.C.REGAN,P.S.HORANYI,E.E.PRYOR,J.L.SARVER,D.S.CAFISO,       
JRNL        AUTH 2 J.H.BUSHWELLER                                               
JRNL        TITL   STRUCTURAL AND DYNAMIC STUDIES OF THE TRANSCRIPTION FACTOR   
JRNL        TITL 2 ERG REVEAL DNA BINDING IS ALLOSTERICALLY AUTOINHIBITED.      
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 110 13374 2013              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   23898196                                                     
JRNL        DOI    10.1073/PNAS.1301726110                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : 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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.28                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 6071                           
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) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : 0.215                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.700                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 301                             
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) : 306                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 66.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 16                           
REMARK   3   BIN FREE R VALUE                    : 0.2310                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 820                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 26                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.88                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.02000                                             
REMARK   3    B12 (A**2) : 0.01000                                              
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): 0.220         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.113         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.323         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   839 ; 0.022 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):   581 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1133 ; 1.752 ; 1.938       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1401 ; 1.015 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   101 ; 6.260 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    42 ;30.874 ;23.571       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   140 ;15.177 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;15.825 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   114 ; 0.119 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   943 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   184 ; 0.001 ; 0.020       
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):   506 ; 1.173 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   206 ; 0.307 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   804 ; 2.180 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   333 ; 3.357 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   329 ; 5.176 ; 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  : 1                                          
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   283        A   384                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.8998  12.9495  81.2174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0963 T22:   0.0130                                     
REMARK   3      T33:   0.0298 T12:  -0.0184                                     
REMARK   3      T13:  -0.0001 T23:  -0.0058                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6730 L22:   1.3409                                     
REMARK   3      L33:   1.3934 L12:  -0.0995                                     
REMARK   3      L13:   0.2121 L23:   0.4451                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0345 S12:   0.0817 S13:   0.0774                       
REMARK   3      S21:  -0.0491 S22:  -0.0041 S23:  -0.0172                       
REMARK   3      S31:  -0.2074 S32:   0.0775 S33:   0.0385                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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                                                           
REMARK   4                                                                      
REMARK   4 4IRH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 28-JAN-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB077116.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-AUG-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9787                             
REMARK 200  MONOCHROMATOR                  : SI 111                             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 6372                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
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) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: SAD                          
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M SODIUM CITRATE, PH 4.5, VAPOR       
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 290K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65 2 2                         
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   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+1/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+5/6                                            
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      116.72200            
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       58.36100            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       87.54150            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       29.18050            
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      145.90250            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      116.72200            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       58.36100            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       29.18050            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       87.54150            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000      145.90250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1930 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 10420 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
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   BIOMT1   2  0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      145.90250            
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      HOH A 411  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 412  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 415  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 426  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   260                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     MSE A   262                                                      
REMARK 465     VAL A   263                                                      
REMARK 465     PRO A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     THR A   266                                                      
REMARK 465     GLU A   267                                                      
REMARK 465     ASP A   268                                                      
REMARK 465     GLN A   269                                                      
REMARK 465     ARG A   270                                                      
REMARK 465     PRO A   271                                                      
REMARK 465     GLN A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     ASP A   274                                                      
REMARK 465     PRO A   275                                                      
REMARK 465     TYR A   276                                                      
REMARK 465     GLN A   277                                                      
REMARK 465     ILE A   278                                                      
REMARK 465     LEU A   279                                                      
REMARK 465     GLY A   280                                                      
REMARK 465     PRO A   281                                                      
REMARK 465     THR A   282                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     PRO A   386                                                      
REMARK 465     PRO A   387                                                      
REMARK 465     GLU A   388                                                      
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     ARG A 285    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 340    CG   CD   CE   NZ                                   
REMARK 470     ASN A 342    CG   OD1  ND2                                       
REMARK 470     LYS A 363    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 319      111.54    -18.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4IRG   RELATED DB: PDB                                   
REMARK 900 UNINHIBITED ERG ETS DOMAIN                                           
REMARK 900 RELATED ID: 4IRI   RELATED DB: PDB                                   
DBREF  4IRH A  263   388  UNP    P11308   ERG_HUMAN      287    412             
SEQADV 4IRH GLY A  260  UNP  P11308              EXPRESSION TAG                 
SEQADV 4IRH ALA A  261  UNP  P11308              EXPRESSION TAG                 
SEQADV 4IRH MSE A  262  UNP  P11308              EXPRESSION TAG                 
SEQRES   1 A  129  GLY ALA MSE VAL PRO LYS THR GLU ASP GLN ARG PRO GLN          
SEQRES   2 A  129  LEU ASP PRO TYR GLN ILE LEU GLY PRO THR SER SER ARG          
SEQRES   3 A  129  LEU ALA ASN PRO GLY SER GLY GLN ILE GLN LEU TRP GLN          
SEQRES   4 A  129  PHE LEU LEU GLU LEU LEU SER ASP SER SER ASN SER SER          
SEQRES   5 A  129  CYS ILE THR TRP GLU GLY THR ASN GLY GLU PHE LYS MSE          
SEQRES   6 A  129  THR ASP PRO ASP GLU VAL ALA ARG ARG TRP GLY GLU ARG          
SEQRES   7 A  129  LYS SER LYS PRO ASN MSE ASN TYR ASP LYS LEU SER ARG          
SEQRES   8 A  129  ALA LEU ARG TYR TYR TYR ASP LYS ASN ILE MSE THR LYS          
SEQRES   9 A  129  VAL HIS GLY LYS ARG TYR ALA TYR LYS PHE ASP PHE HIS          
SEQRES  10 A  129  GLY ILE ALA GLN ALA LEU GLN PRO HIS PRO PRO GLU              
MODRES 4IRH MSE A  324  MET  SELENOMETHIONINE                                   
MODRES 4IRH MSE A  343  MET  SELENOMETHIONINE                                   
MODRES 4IRH MSE A  361  MET  SELENOMETHIONINE                                   
HET    MSE  A 324       8                                                       
HET    MSE  A 343       8                                                       
HET    MSE  A 361       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    3(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *26(H2 O)                                                     
HELIX    1   1 GLN A  295  ASP A  306  1                                  12    
HELIX    2   2 SER A  307  SER A  310  5                                   4    
HELIX    3   3 ASP A  326  SER A  339  1                                  14    
HELIX    4   4 ASN A  344  TYR A  354  1                                  11    
HELIX    5   5 TYR A  355  LYS A  358  5                                   4    
HELIX    6   6 ASP A  374  LEU A  382  1                                   9    
SHEET    1   A 4 THR A 314  TRP A 315  0                                        
SHEET    2   A 4 GLU A 321  LYS A 323 -1  O  LYS A 323   N  THR A 314           
SHEET    3   A 4 ALA A 370  PHE A 373 -1  O  TYR A 371   N  PHE A 322           
SHEET    4   A 4 MSE A 361  LYS A 363 -1  N  THR A 362   O  LYS A 372           
LINK         C   LYS A 323                 N   MSE A 324     1555   1555  1.33  
LINK         C   MSE A 324                 N   THR A 325     1555   1555  1.32  
LINK         C   ASN A 342                 N   MSE A 343     1555   1555  1.35  
LINK         C   MSE A 343                 N   ASN A 344     1555   1555  1.32  
LINK         C   ILE A 360                 N   MSE A 361     1555   1555  1.33  
LINK         C   MSE A 361                 N   THR A 362     1555   1555  1.32  
CRYST1   44.741   44.741  175.083  90.00  90.00 120.00 P 65 2 2     12          
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      0.022351  0.012904  0.000000        0.00000                         
SCALE2      0.000000  0.025809  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005712        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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