GenomeNet

Database: PDB
Entry: 3NXB
LinkDB: 3NXB
Original site: 3NXB 
HEADER    TRANSCRIPTION                           13-JUL-10   3NXB              
TITLE     CRYSTAL STRUCTURE OF THE BROMODOMAIN OF HUMAN CECR2                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CAT EYE SYNDROME CRITICAL REGION PROTEIN 2;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: BROMODOMAIN (UNP RESIDUES 424-538);                        
COMPND   5 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: CECR2, KIAA1740;                                               
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    STRUCTURAL GENOMICS CONSORTIUM, SGC, CECR2, CAT EYE SYNDROME          
KEYWDS   2 CHROMOSOME REGION CANDIDATE 2, BROMODOMAIN, STRUCTURAL GENOMICS,     
KEYWDS   3 TRANSCRIPTION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.FILIPPAKOPOULOS,S.PICAUD,T.KEATES,J.MUNIZ,F.VON DELFT,              
AUTHOR   2 C.H.ARROWSMITH,A.EDWARDS,J.WEIGELT,C.BOUNTRA,S.KNAPP,STRUCTURAL      
AUTHOR   3 GENOMICS CONSORTIUM (SGC)                                            
REVDAT   3   31-JAN-18 3NXB    1       AUTHOR                                   
REVDAT   2   11-APR-12 3NXB    1       JRNL   VERSN                             
REVDAT   1   18-AUG-10 3NXB    0                                                
JRNL        AUTH   P.FILIPPAKOPOULOS,S.PICAUD,M.MANGOS,T.KEATES,J.P.LAMBERT,    
JRNL        AUTH 2 D.BARSYTE-LOVEJOY,I.FELLETAR,R.VOLKMER,S.MULLER,T.PAWSON,    
JRNL        AUTH 3 A.C.GINGRAS,C.H.ARROWSMITH,S.KNAPP                           
JRNL        TITL   HISTONE RECOGNITION AND LARGE-SCALE STRUCTURAL ANALYSIS OF   
JRNL        TITL 2 THE HUMAN BROMODOMAIN FAMILY.                                
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 149   214 2012              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   22464331                                                     
JRNL        DOI    10.1016/J.CELL.2012.02.013                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.83 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.83                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 22343                          
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) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1147                            
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) : 1.83                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1520                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.69                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4480                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 66                           
REMARK   3   BIN FREE R VALUE                    : 0.5390                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1639                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 12                                      
REMARK   3   SOLVENT ATOMS            : 209                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 30.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 29.56                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.20000                                             
REMARK   3    B22 (A**2) : 0.06000                                              
REMARK   3    B33 (A**2) : 0.28000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.26000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.119         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.086         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.461         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.954                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1720 ; 0.016 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1235 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2298 ; 1.423 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  3002 ; 0.905 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   201 ; 5.349 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    83 ;33.689 ;24.217       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   329 ;15.497 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;16.070 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   235 ; 0.086 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1855 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   352 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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   437        A   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  24.6121   5.2381  16.7843              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0756 T22:   0.0556                                     
REMARK   3      T33:   0.0504 T12:   0.0233                                     
REMARK   3      T13:  -0.0021 T23:   0.0244                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8978 L22:   0.5976                                     
REMARK   3      L33:   0.6448 L12:  -0.1118                                     
REMARK   3      L13:   0.0408 L23:   0.1508                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0079 S12:  -0.0275 S13:   0.0266                       
REMARK   3      S21:  -0.0182 S22:   0.0658 S23:   0.0664                       
REMARK   3      S31:   0.0950 S32:   0.0512 S33:  -0.0580                       
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   438        B   537                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.5872  21.0119   1.0261              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0667 T22:   0.0539                                     
REMARK   3      T33:   0.1098 T12:  -0.0131                                     
REMARK   3      T13:  -0.0037 T23:   0.0386                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4637 L22:   0.7943                                     
REMARK   3      L33:   0.4785 L12:   0.4080                                     
REMARK   3      L13:   0.0278 L23:   0.5730                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0206 S12:  -0.0197 S13:  -0.2992                       
REMARK   3      S21:  -0.0827 S22:  -0.0351 S23:  -0.0544                       
REMARK   3      S31:  -0.0953 S32:  -0.0133 S33:   0.0145                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES: WITH TLS ADDED                                  
REMARK   4                                                                      
REMARK   4 3NXB COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-JUL-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000060395.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E SUPERBRIGHT            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.16                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22346                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.830                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.500                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : 0.05800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.83                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.92                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.54100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.1.4                                          
REMARK 200 STARTING MODEL: ENSEMBLE OF PDB ENTRIES 2OSS, 2OUO, 2GRC, 2OO1,      
REMARK 200  3DAI, 3D7C, 3DWY                                                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MES, 12% PEG 20,000, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 277K, PH 6.5                   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       63.58000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.75500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       63.58000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.75500            
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 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 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     SER A   423                                                      
REMARK 465     MET A   424                                                      
REMARK 465     ARG A   425                                                      
REMARK 465     GLU A   426                                                      
REMARK 465     GLU A   427                                                      
REMARK 465     LYS A   428                                                      
REMARK 465     LYS A   429                                                      
REMARK 465     THR A   430                                                      
REMARK 465     LYS A   431                                                      
REMARK 465     ASP A   432                                                      
REMARK 465     LEU A   433                                                      
REMARK 465     PHE A   434                                                      
REMARK 465     GLU A   435                                                      
REMARK 465     LEU A   436                                                      
REMARK 465     HIS A   538                                                      
REMARK 465     SER B   423                                                      
REMARK 465     MET B   424                                                      
REMARK 465     ARG B   425                                                      
REMARK 465     GLU B   426                                                      
REMARK 465     GLU B   427                                                      
REMARK 465     LYS B   428                                                      
REMARK 465     LYS B   429                                                      
REMARK 465     THR B   430                                                      
REMARK 465     LYS B   431                                                      
REMARK 465     ASP B   432                                                      
REMARK 465     LEU B   433                                                      
REMARK 465     PHE B   434                                                      
REMARK 465     GLU B   435                                                      
REMARK 465     LEU B   436                                                      
REMARK 465     ASP B   437                                                      
REMARK 465     HIS B   538                                                      
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     ASP A 437    CG   OD1  OD2                                       
REMARK 470     GLN A 473    CD   OE1  NE2                                       
REMARK 470     GLU A 516    CD   OE1  OE2                                       
REMARK 470     LYS A 537    CG   CD   CE   NZ                                   
REMARK 470     LYS B 454    CE   NZ                                             
REMARK 470     LYS B 537    CG   CD   CE   NZ                                   
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    MET B 503   CG  -  SD  -  CE  ANGL. DEV. = -13.3 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    ALA B 468       67.30   -158.28                                   
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 EDO A 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 3                   
DBREF  3NXB A  424   538  UNP    Q9BXF3   CECR2_HUMAN    424    538             
DBREF  3NXB B  424   538  UNP    Q9BXF3   CECR2_HUMAN    424    538             
SEQADV 3NXB SER A  423  UNP  Q9BXF3              EXPRESSION TAG                 
SEQADV 3NXB SER B  423  UNP  Q9BXF3              EXPRESSION TAG                 
SEQRES   1 A  116  SER MET ARG GLU GLU LYS LYS THR LYS ASP LEU PHE GLU          
SEQRES   2 A  116  LEU ASP ASP ASP PHE THR ALA MET TYR LYS VAL LEU ASP          
SEQRES   3 A  116  VAL VAL LYS ALA HIS LYS ASP SER TRP PRO PHE LEU GLU          
SEQRES   4 A  116  PRO VAL ASP GLU SER TYR ALA PRO ASN TYR TYR GLN ILE          
SEQRES   5 A  116  ILE LYS ALA PRO MET ASP ILE SER SER MET GLU LYS LYS          
SEQRES   6 A  116  LEU ASN GLY GLY LEU TYR CYS THR LYS GLU GLU PHE VAL          
SEQRES   7 A  116  ASN ASP MET LYS THR MET PHE ARG ASN CYS ARG LYS TYR          
SEQRES   8 A  116  ASN GLY GLU SER SER GLU TYR THR LYS MET SER ASP ASN          
SEQRES   9 A  116  LEU GLU ARG CYS PHE HIS ARG ALA MET MET LYS HIS              
SEQRES   1 B  116  SER MET ARG GLU GLU LYS LYS THR LYS ASP LEU PHE GLU          
SEQRES   2 B  116  LEU ASP ASP ASP PHE THR ALA MET TYR LYS VAL LEU ASP          
SEQRES   3 B  116  VAL VAL LYS ALA HIS LYS ASP SER TRP PRO PHE LEU GLU          
SEQRES   4 B  116  PRO VAL ASP GLU SER TYR ALA PRO ASN TYR TYR GLN ILE          
SEQRES   5 B  116  ILE LYS ALA PRO MET ASP ILE SER SER MET GLU LYS LYS          
SEQRES   6 B  116  LEU ASN GLY GLY LEU TYR CYS THR LYS GLU GLU PHE VAL          
SEQRES   7 B  116  ASN ASP MET LYS THR MET PHE ARG ASN CYS ARG LYS TYR          
SEQRES   8 B  116  ASN GLY GLU SER SER GLU TYR THR LYS MET SER ASP ASN          
SEQRES   9 B  116  LEU GLU ARG CYS PHE HIS ARG ALA MET MET LYS HIS              
HET    EDO  A   1       8                                                       
HET    EDO  B   2       4                                                       
HET    EDO  B   3       8                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    3(C2 H6 O2)                                                  
FORMUL   6  HOH   *209(H2 O)                                                    
HELIX    1   1 ASP A  438  HIS A  453  1                                  16    
HELIX    2   2 SER A  456  LEU A  460  5                                   5    
HELIX    3   3 ASN A  470  ILE A  475  1                                   6    
HELIX    4   4 ASP A  480  GLY A  490  1                                  11    
HELIX    5   5 THR A  495  GLY A  515  1                                  21    
HELIX    6   6 SER A  518  LYS A  537  1                                  20    
HELIX    7   7 ASP B  438  HIS B  453  1                                  16    
HELIX    8   8 LYS B  454  LEU B  460  5                                   7    
HELIX    9   9 ASP B  464  ALA B  468  5                                   5    
HELIX   10  10 ASN B  470  ILE B  475  1                                   6    
HELIX   11  11 ASP B  480  GLY B  490  1                                  11    
HELIX   12  12 THR B  495  GLY B  515  1                                  21    
HELIX   13  13 SER B  518  MET B  535  1                                  18    
SITE     1 AC1  6 HOH A 173  HOH A 188  PRO A 458  VAL A 463                    
SITE     2 AC1  6 TYR A 467  ASN A 514                                          
SITE     1 AC2  3 ASP B 439  MET B 443  THR B 495                               
SITE     1 AC3  8 HOH B  11  HOH B  72  HOH B 198  PRO B 458                    
SITE     2 AC3  8 VAL B 463  TYR B 513  ASN B 514  TYR B 520                    
CRYST1  127.160   45.510   45.590  90.00 105.67  90.00 C 1 2 1       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      0.007864  0.000000  0.002206        0.00000                         
SCALE2      0.000000  0.021973  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022781        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system