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Database: PDB
Entry: 4A64
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HEADER    CELL CYCLE                              31-OCT-11   4A64              
TITLE     CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN CUL4B AT 2.57A    
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CULLIN-4B;                                                 
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: N-TERMINAL DOMAIN, RESIDUES 188-539;                       
COMPND   5 SYNONYM: CUL4B, CUL-4B;                                              
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;                                
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC-ZB                                   
KEYWDS    CELL CYCLE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.VOLLMAR,V.AYINAMPUDI,C.COOPER,K.GUO,T.KROJER,J.R.C.MUNIZ,F.VON      
AUTHOR   2 DELFT,J.WEIGELT,C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,A.BULLOCK         
REVDAT   2   24-JAN-18 4A64    1       JRNL                                     
REVDAT   1   29-FEB-12 4A64    0                                                
JRNL        AUTH   M.VOLLMAR,V.AYINAMPUDI,C.COOPER,K.GUO,T.KROJER,J.R.C.MUNIZ,  
JRNL        AUTH 2 F.VON DELFT,J.WEIGELT,C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,    
JRNL        AUTH 3 A.BULLOCK                                                    
JRNL        TITL   CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF HUMAN CUL4B AT 
JRNL        TITL 2 2.57A RESOLUTION                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.57 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
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) : 2.57                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 55064                          
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) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2940                            
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) : 2.57                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3890                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.90                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3470                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 208                          
REMARK   3   BIN FREE R VALUE                    : 0.4040                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 11036                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 253                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 67.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.11                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.70000                                              
REMARK   3    B22 (A**2) : -0.56000                                             
REMARK   3    B33 (A**2) : -2.45000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.54000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.529         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.274         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.206         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.020        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.963                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.942                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 11315 ; 0.014 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  7742 ; 0.007 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 15255 ; 1.600 ; 1.961       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 18892 ; 1.414 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1362 ; 5.142 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   602 ;37.765 ;24.950       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  2181 ;16.428 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    79 ;20.331 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1725 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 12443 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  2256 ; 0.006 ; 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  : 8                                          
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     1        A   363                          
REMARK   3    ORIGIN FOR THE GROUP (A):  20.4437  -9.1511  38.1586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2101 T22:   0.0649                                     
REMARK   3      T33:   0.1913 T12:  -0.0216                                     
REMARK   3      T13:  -0.0248 T23:  -0.0851                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7542 L22:   1.1211                                     
REMARK   3      L33:   3.8841 L12:  -0.8884                                     
REMARK   3      L13:   2.6954 L23:  -1.5528                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2823 S12:   0.0924 S13:   0.2423                       
REMARK   3      S21:   0.0572 S22:   0.0180 S23:  -0.0556                       
REMARK   3      S31:  -0.3342 S32:  -0.0199 S33:   0.2643                       
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 :   A   364        A   533                          
REMARK   3    ORIGIN FOR THE GROUP (A):  48.0027 -44.8202  62.6735              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0950 T22:   0.1865                                     
REMARK   3      T33:   0.2715 T12:   0.0005                                     
REMARK   3      T13:   0.0017 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2826 L22:  10.1832                                     
REMARK   3      L33:   2.0627 L12:  -2.1401                                     
REMARK   3      L13:   1.0316 L23:  -2.4481                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0806 S12:  -0.0791 S13:  -0.0317                       
REMARK   3      S21:   0.2555 S22:  -0.3039 S23:  -1.0272                       
REMARK   3      S31:   0.2412 S32:   0.3121 S33:   0.2233                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   364                          
REMARK   3    ORIGIN FOR THE GROUP (A):  28.6030 -60.0375  35.5289              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1329 T22:   0.0514                                     
REMARK   3      T33:   0.1989 T12:  -0.0803                                     
REMARK   3      T13:   0.0116 T23:  -0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7132 L22:   1.5670                                     
REMARK   3      L33:   7.1641 L12:  -0.3462                                     
REMARK   3      L13:  -0.7179 L23:   2.1753                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1231 S12:   0.1038 S13:  -0.0399                       
REMARK   3      S21:   0.0694 S22:  -0.0194 S23:   0.0284                       
REMARK   3      S31:   0.3193 S32:  -0.1320 S33:   0.1425                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   365        B   533                          
REMARK   3    ORIGIN FOR THE GROUP (A):  21.7316 -24.2430  71.5712              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0453 T22:   0.2115                                     
REMARK   3      T33:   0.1198 T12:   0.0338                                     
REMARK   3      T13:  -0.0176 T23:  -0.0719                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0968 L22:   8.7382                                     
REMARK   3      L33:   2.8108 L12:   0.4669                                     
REMARK   3      L13:   0.1599 L23:   3.3397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1106 S12:  -0.2816 S13:   0.1402                       
REMARK   3      S21:   0.2766 S22:  -0.2293 S23:   0.6149                       
REMARK   3      S31:  -0.0508 S32:  -0.2976 S33:   0.3399                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   196        C   321                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.7574 -50.0396  28.9653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0833 T22:   0.3206                                     
REMARK   3      T33:   0.2719 T12:  -0.0806                                     
REMARK   3      T13:  -0.0205 T23:   0.0435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6670 L22:   5.8461                                     
REMARK   3      L33:   7.6685 L12:  -0.7921                                     
REMARK   3      L13:   1.5308 L23:  -1.7085                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1955 S12:  -0.0573 S13:  -0.0482                       
REMARK   3      S21:   0.4547 S22:  -0.3896 S23:  -0.6176                       
REMARK   3      S31:   0.1505 S32:   0.8032 S33:   0.1941                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C   322        C   534                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3528 -22.0239   5.6970              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0888 T22:   0.1296                                     
REMARK   3      T33:   0.0214 T12:  -0.0570                                     
REMARK   3      T13:   0.0035 T23:  -0.0278                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3907 L22:   2.7419                                     
REMARK   3      L33:   1.2088 L12:  -2.8819                                     
REMARK   3      L13:   1.7641 L23:  -1.1396                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0514 S12:   0.1265 S13:   0.1662                       
REMARK   3      S21:  -0.2197 S22:  -0.0671 S23:  -0.0938                       
REMARK   3      S31:  -0.0724 S32:   0.0601 S33:   0.1185                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   196        D   313                          
REMARK   3    ORIGIN FOR THE GROUP (A):   2.1304 -18.5240  44.1421              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2263 T22:   0.3734                                     
REMARK   3      T33:   0.1688 T12:  -0.0527                                     
REMARK   3      T13:   0.1088 T23:  -0.0845                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8092 L22:   4.3334                                     
REMARK   3      L33:   5.4817 L12:   1.0618                                     
REMARK   3      L13:   1.4644 L23:   1.5798                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1477 S12:  -0.6612 S13:   0.0547                       
REMARK   3      S21:   0.7139 S22:  -0.2144 S23:   0.2023                       
REMARK   3      S31:  -0.3234 S32:  -0.4570 S33:   0.0667                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   314        D   532                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9661 -46.0156   8.6078              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2506 T22:   0.1346                                     
REMARK   3      T33:   0.0833 T12:  -0.0477                                     
REMARK   3      T13:  -0.0165 T23:  -0.0316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0360 L22:   3.3481                                     
REMARK   3      L33:   3.6495 L12:  -2.1123                                     
REMARK   3      L13:  -2.4345 L23:   1.8430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0294 S12:   0.1170 S13:  -0.2185                       
REMARK   3      S21:  -0.3271 S22:  -0.0590 S23:   0.1266                       
REMARK   3      S31:   0.4919 S32:   0.0007 S33:   0.0884                       
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 ADDED IN THE RIDING   
REMARK   3  POSITIONS. U VALUES WITH TLS ADDED                                  
REMARK   4                                                                      
REMARK   4 4A64 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-OCT-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290050158.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-AUG-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 58043                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.570                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 19.970                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.57                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.73000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRIES 1U6G, 1LDK, 1LDJ, 2HYE                   
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.92                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.79                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24% PEG4000, 100 MM LISO4, 100 MM TRIS   
REMARK 280  (PH 8.2)                                                            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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       78.54550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14710 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 59610 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -33.6 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, VAL 498 TO ARG                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU 502 TO ASP                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, VAL 498 TO ARG                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, LEU 502 TO ASP                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, VAL 498 TO ARG                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, LEU 502 TO ASP                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, VAL 498 TO ARG                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, LEU 502 TO ASP                        
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     ILE A   534                                                      
REMARK 465     ASN A   535                                                      
REMARK 465     LYS A   536                                                      
REMARK 465     ARG A   537                                                      
REMARK 465     PRO A   538                                                      
REMARK 465     ASN A   539                                                      
REMARK 465     GLU B   492                                                      
REMARK 465     LYS B   493                                                      
REMARK 465     ASP B   494                                                      
REMARK 465     ILE B   534                                                      
REMARK 465     ASN B   535                                                      
REMARK 465     LYS B   536                                                      
REMARK 465     ARG B   537                                                      
REMARK 465     PRO B   538                                                      
REMARK 465     ASN B   539                                                      
REMARK 465     SER C   186                                                      
REMARK 465     MET C   187                                                      
REMARK 465     PRO C   188                                                      
REMARK 465     LYS C   189                                                      
REMARK 465     LEU C   190                                                      
REMARK 465     PRO C   191                                                      
REMARK 465     GLU C   192                                                      
REMARK 465     ASN C   193                                                      
REMARK 465     TYR C   194                                                      
REMARK 465     THR C   195                                                      
REMARK 465     LYS C   233                                                      
REMARK 465     ILE C   234                                                      
REMARK 465     SER C   235                                                      
REMARK 465     ALA C   236                                                      
REMARK 465     ASP C   260                                                      
REMARK 465     SER C   261                                                      
REMARK 465     ASN C   535                                                      
REMARK 465     LYS C   536                                                      
REMARK 465     ARG C   537                                                      
REMARK 465     PRO C   538                                                      
REMARK 465     ASN C   539                                                      
REMARK 465     SER D   186                                                      
REMARK 465     MET D   187                                                      
REMARK 465     PRO D   188                                                      
REMARK 465     LYS D   189                                                      
REMARK 465     LEU D   190                                                      
REMARK 465     PRO D   191                                                      
REMARK 465     GLU D   192                                                      
REMARK 465     ASN D   193                                                      
REMARK 465     TYR D   194                                                      
REMARK 465     THR D   195                                                      
REMARK 465     SER D   231                                                      
REMARK 465     TYR D   232                                                      
REMARK 465     LYS D   233                                                      
REMARK 465     ILE D   234                                                      
REMARK 465     SER D   235                                                      
REMARK 465     ALA D   236                                                      
REMARK 465     SER D   261                                                      
REMARK 465     ASN D   490                                                      
REMARK 465     PRO D   491                                                      
REMARK 465     GLU D   492                                                      
REMARK 465     LYS D   493                                                      
REMARK 465     ASP D   494                                                      
REMARK 465     LYS D   495                                                      
REMARK 465     THR D   496                                                      
REMARK 465     MET D   497                                                      
REMARK 465     ARG D   498                                                      
REMARK 465     GLN D   499                                                      
REMARK 465     PHE D   533                                                      
REMARK 465     ILE D   534                                                      
REMARK 465     ASN D   535                                                      
REMARK 465     LYS D   536                                                      
REMARK 465     ARG D   537                                                      
REMARK 465     PRO D   538                                                      
REMARK 465     ASN D   539                                                      
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 A 189    CD   CE   NZ                                        
REMARK 470     LYS A 240    CE   NZ                                             
REMARK 470     SER A 261    OG                                                  
REMARK 470     GLN A 299    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 466    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 485    OG                                                  
REMARK 470     THR A 486    OG1  CG2                                            
REMARK 470     ILE A 487    CG1  CG2  CD1                                       
REMARK 470     ILE A 489    CG1  CG2  CD1                                       
REMARK 470     ASN A 490    CG   OD1  ND2                                       
REMARK 470     GLU A 492    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 493    CG   CD   CE   NZ                                   
REMARK 470     ASP A 494    CG   OD1  OD2                                       
REMARK 470     LYS A 495    CG   CD   CE   NZ                                   
REMARK 470     THR A 496    OG1  CG2                                            
REMARK 470     LYS A 521    CD   CE   NZ                                        
REMARK 470     GLU A 531    CD   OE1  OE2                                       
REMARK 470     LYS B 189    CD   CE   NZ                                        
REMARK 470     ASP B 260    CG   OD1  OD2                                       
REMARK 470     SER B 261    OG                                                  
REMARK 470     GLN B 299    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 323    CE   NZ                                             
REMARK 470     ARG B 466    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE B 489    CG1  CG2  CD1                                       
REMARK 470     ASN B 490    CG   OD1  ND2                                       
REMARK 470     LYS B 495    CG   CD   CE   NZ                                   
REMARK 470     LYS B 521    CD   CE   NZ                                        
REMARK 470     LYS B 527    CD   CE   NZ                                        
REMARK 470     LYS C 201    CD   CE   NZ                                        
REMARK 470     TYR C 232    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE C 254    CG1  CG2  CD1                                       
REMARK 470     GLU C 259    CG   CD   OE1  OE2                                  
REMARK 470     LEU C 262    CG   CD1  CD2                                       
REMARK 470     SER C 320    OG                                                  
REMARK 470     GLN C 322    CG   CD   OE1  NE2                                  
REMARK 470     LYS C 323    CG   CD   CE   NZ                                   
REMARK 470     ARG C 377    NE   CZ   NH1  NH2                                  
REMARK 470     GLU C 492    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 493    CG   CD   CE   NZ                                   
REMARK 470     ILE C 534    CG1  CG2  CD1                                       
REMARK 470     GLU D 197    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 203    CE   NZ                                             
REMARK 470     LYS D 240    CD   CE   NZ                                        
REMARK 470     GLU D 259    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 481    CG   CD   CE   NZ                                   
REMARK 470     ILE D 487    CG1  CG2  CD1                                       
REMARK 470     VAL D 488    CG1  CG2                                            
REMARK 470     ILE D 489    CG1  CG2  CD1                                       
REMARK 470     LEU D 501    CG   CD1  CD2                                       
REMARK 470     LYS D 521    CD   CE   NZ                                        
REMARK 470     PHE D 530    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU D 531    CD   OE1  OE2                                       
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    HOH C  2019     O    HOH C  2020              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    HIS A 255   CG    HIS A 255   CD2     0.057                       
REMARK 500    HIS B 397   CG    HIS B 397   CD2     0.056                       
REMARK 500    HIS C 397   CG    HIS C 397   CD2     0.063                       
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    MET A 387   CG  -  SD  -  CE  ANGL. DEV. = -12.1 DEGREES          
REMARK 500    LEU B 410   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG C 286   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500    LEU D 410   CB  -  CG  -  CD2 ANGL. DEV. = -10.8 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    PRO A 191      103.39    -57.03                                   
REMARK 500    ASP A 196        5.07     88.14                                   
REMARK 500    THR A 213     -158.96    -99.08                                   
REMARK 500    GLU A 259       24.32    -74.22                                   
REMARK 500    ASP A 263      132.67    -38.85                                   
REMARK 500    ILE A 318      -70.91   -111.92                                   
REMARK 500    TYR A 413       -9.12   -144.79                                   
REMARK 500    ASN A 490       74.56   -116.93                                   
REMARK 500    PRO B 191      104.46    -59.03                                   
REMARK 500    ASP B 196        4.81     86.71                                   
REMARK 500    GLU B 259       25.56    -75.51                                   
REMARK 500    ASP B 263      133.27    -39.99                                   
REMARK 500    ILE B 318      -70.50   -111.78                                   
REMARK 500    TYR B 413       -6.48   -145.10                                   
REMARK 500    ASN B 490       70.22   -117.41                                   
REMARK 500    ASP C 263      132.91    -39.47                                   
REMARK 500    TYR C 413      -10.04   -144.40                                   
REMARK 500    ASN C 490       67.26   -117.06                                   
REMARK 500    ASN C 490       68.09   -117.76                                   
REMARK 500    PHE C 533      -33.45   -140.26                                   
REMARK 500    GLU D 259       25.96    -77.36                                   
REMARK 500    ILE D 318      -72.21   -111.24                                   
REMARK 500    TYR D 413       -8.67   -142.29                                   
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 1534                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1535                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1536                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 1537                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1534                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C 1535                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO D 1533                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4A0C   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE CAND1-CUL4B-RBX1 COMPLEX                            
REMARK 900 RELATED ID: 4A0L   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF DDB1-DDB2-CUL4B-RBX1 BOUND TO A 12 BP ABASIC SITE       
REMARK 900 CONTAINING DNA-DUPLEX                                                
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 STARTING RESIDUES SER186 AND MET187 ARE DUE TO CLONING               
DBREF  4A64 A  188   539  UNP    Q13620   CUL4B_HUMAN    188    539             
DBREF  4A64 B  188   539  UNP    Q13620   CUL4B_HUMAN    188    539             
DBREF  4A64 C  188   539  UNP    Q13620   CUL4B_HUMAN    188    539             
DBREF  4A64 D  188   539  UNP    Q13620   CUL4B_HUMAN    188    539             
SEQADV 4A64 SER A  186  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A64 MET A  187  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A64 ARG A  498  UNP  Q13620    VAL   498 ENGINEERED MUTATION            
SEQADV 4A64 ASP A  502  UNP  Q13620    LEU   502 ENGINEERED MUTATION            
SEQADV 4A64 SER B  186  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A64 MET B  187  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A64 ARG B  498  UNP  Q13620    VAL   498 ENGINEERED MUTATION            
SEQADV 4A64 ASP B  502  UNP  Q13620    LEU   502 ENGINEERED MUTATION            
SEQADV 4A64 SER C  186  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A64 MET C  187  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A64 ARG C  498  UNP  Q13620    VAL   498 ENGINEERED MUTATION            
SEQADV 4A64 ASP C  502  UNP  Q13620    LEU   502 ENGINEERED MUTATION            
SEQADV 4A64 SER D  186  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A64 MET D  187  UNP  Q13620              EXPRESSION TAG                 
SEQADV 4A64 ARG D  498  UNP  Q13620    VAL   498 ENGINEERED MUTATION            
SEQADV 4A64 ASP D  502  UNP  Q13620    LEU   502 ENGINEERED MUTATION            
SEQRES   1 A  354  SER MET PRO LYS LEU PRO GLU ASN TYR THR ASP GLU THR          
SEQRES   2 A  354  TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA ILE GLN ASN          
SEQRES   3 A  354  SER THR SER ILE LYS TYR ASN LEU GLU GLU LEU TYR GLN          
SEQRES   4 A  354  ALA VAL GLU ASN LEU CYS SER TYR LYS ILE SER ALA ASN          
SEQRES   5 A  354  LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU ASP HIS ILE          
SEQRES   6 A  354  LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP SER LEU ASP          
SEQRES   7 A  354  SER VAL LEU PHE LEU LYS LYS ILE ASP ARG CYS TRP GLN          
SEQRES   8 A  354  ASN HIS CYS ARG GLN MET ILE MET ILE ARG SER ILE PHE          
SEQRES   9 A  354  LEU PHE LEU ASP ARG THR TYR VAL LEU GLN ASN SER MET          
SEQRES  10 A  354  LEU PRO SER ILE TRP ASP MET GLY LEU GLU LEU PHE ARG          
SEQRES  11 A  354  ALA HIS ILE ILE SER ASP GLN LYS VAL GLN ASN LYS THR          
SEQRES  12 A  354  ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG GLU ARG ASN          
SEQRES  13 A  354  GLY GLU ALA ILE ASP ARG SER LEU LEU ARG SER LEU LEU          
SEQRES  14 A  354  SER MET LEU SER ASP LEU GLN ILE TYR GLN ASP SER PHE          
SEQRES  15 A  354  GLU GLN ARG PHE LEU GLU GLU THR ASN ARG LEU TYR ALA          
SEQRES  16 A  354  ALA GLU GLY GLN LYS LEU MET GLN GLU ARG GLU VAL PRO          
SEQRES  17 A  354  GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU GLU GLU GLU          
SEQRES  18 A  354  ALA ASP ARG LEU ILE THR TYR LEU ASP GLN THR THR GLN          
SEQRES  19 A  354  LYS SER LEU ILE ALA THR VAL GLU LYS GLN LEU LEU GLY          
SEQRES  20 A  354  GLU HIS LEU THR ALA ILE LEU GLN LYS GLY LEU ASN ASN          
SEQRES  21 A  354  LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU SER LEU LEU          
SEQRES  22 A  354  TYR GLN LEU PHE SER ARG VAL ARG GLY GLY VAL GLN VAL          
SEQRES  23 A  354  LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS ALA PHE GLY          
SEQRES  24 A  354  SER THR ILE VAL ILE ASN PRO GLU LYS ASP LYS THR MET          
SEQRES  25 A  354  ARG GLN GLU LEU ASP ASP PHE LYS ASP LYS VAL ASP HIS          
SEQRES  26 A  354  ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU LYS PHE ILE          
SEQRES  27 A  354  ASN ALA MET LYS GLU ALA PHE GLU THR PHE ILE ASN LYS          
SEQRES  28 A  354  ARG PRO ASN                                                  
SEQRES   1 B  354  SER MET PRO LYS LEU PRO GLU ASN TYR THR ASP GLU THR          
SEQRES   2 B  354  TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA ILE GLN ASN          
SEQRES   3 B  354  SER THR SER ILE LYS TYR ASN LEU GLU GLU LEU TYR GLN          
SEQRES   4 B  354  ALA VAL GLU ASN LEU CYS SER TYR LYS ILE SER ALA ASN          
SEQRES   5 B  354  LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU ASP HIS ILE          
SEQRES   6 B  354  LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP SER LEU ASP          
SEQRES   7 B  354  SER VAL LEU PHE LEU LYS LYS ILE ASP ARG CYS TRP GLN          
SEQRES   8 B  354  ASN HIS CYS ARG GLN MET ILE MET ILE ARG SER ILE PHE          
SEQRES   9 B  354  LEU PHE LEU ASP ARG THR TYR VAL LEU GLN ASN SER MET          
SEQRES  10 B  354  LEU PRO SER ILE TRP ASP MET GLY LEU GLU LEU PHE ARG          
SEQRES  11 B  354  ALA HIS ILE ILE SER ASP GLN LYS VAL GLN ASN LYS THR          
SEQRES  12 B  354  ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG GLU ARG ASN          
SEQRES  13 B  354  GLY GLU ALA ILE ASP ARG SER LEU LEU ARG SER LEU LEU          
SEQRES  14 B  354  SER MET LEU SER ASP LEU GLN ILE TYR GLN ASP SER PHE          
SEQRES  15 B  354  GLU GLN ARG PHE LEU GLU GLU THR ASN ARG LEU TYR ALA          
SEQRES  16 B  354  ALA GLU GLY GLN LYS LEU MET GLN GLU ARG GLU VAL PRO          
SEQRES  17 B  354  GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU GLU GLU GLU          
SEQRES  18 B  354  ALA ASP ARG LEU ILE THR TYR LEU ASP GLN THR THR GLN          
SEQRES  19 B  354  LYS SER LEU ILE ALA THR VAL GLU LYS GLN LEU LEU GLY          
SEQRES  20 B  354  GLU HIS LEU THR ALA ILE LEU GLN LYS GLY LEU ASN ASN          
SEQRES  21 B  354  LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU SER LEU LEU          
SEQRES  22 B  354  TYR GLN LEU PHE SER ARG VAL ARG GLY GLY VAL GLN VAL          
SEQRES  23 B  354  LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS ALA PHE GLY          
SEQRES  24 B  354  SER THR ILE VAL ILE ASN PRO GLU LYS ASP LYS THR MET          
SEQRES  25 B  354  ARG GLN GLU LEU ASP ASP PHE LYS ASP LYS VAL ASP HIS          
SEQRES  26 B  354  ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU LYS PHE ILE          
SEQRES  27 B  354  ASN ALA MET LYS GLU ALA PHE GLU THR PHE ILE ASN LYS          
SEQRES  28 B  354  ARG PRO ASN                                                  
SEQRES   1 C  354  SER MET PRO LYS LEU PRO GLU ASN TYR THR ASP GLU THR          
SEQRES   2 C  354  TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA ILE GLN ASN          
SEQRES   3 C  354  SER THR SER ILE LYS TYR ASN LEU GLU GLU LEU TYR GLN          
SEQRES   4 C  354  ALA VAL GLU ASN LEU CYS SER TYR LYS ILE SER ALA ASN          
SEQRES   5 C  354  LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU ASP HIS ILE          
SEQRES   6 C  354  LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP SER LEU ASP          
SEQRES   7 C  354  SER VAL LEU PHE LEU LYS LYS ILE ASP ARG CYS TRP GLN          
SEQRES   8 C  354  ASN HIS CYS ARG GLN MET ILE MET ILE ARG SER ILE PHE          
SEQRES   9 C  354  LEU PHE LEU ASP ARG THR TYR VAL LEU GLN ASN SER MET          
SEQRES  10 C  354  LEU PRO SER ILE TRP ASP MET GLY LEU GLU LEU PHE ARG          
SEQRES  11 C  354  ALA HIS ILE ILE SER ASP GLN LYS VAL GLN ASN LYS THR          
SEQRES  12 C  354  ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG GLU ARG ASN          
SEQRES  13 C  354  GLY GLU ALA ILE ASP ARG SER LEU LEU ARG SER LEU LEU          
SEQRES  14 C  354  SER MET LEU SER ASP LEU GLN ILE TYR GLN ASP SER PHE          
SEQRES  15 C  354  GLU GLN ARG PHE LEU GLU GLU THR ASN ARG LEU TYR ALA          
SEQRES  16 C  354  ALA GLU GLY GLN LYS LEU MET GLN GLU ARG GLU VAL PRO          
SEQRES  17 C  354  GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU GLU GLU GLU          
SEQRES  18 C  354  ALA ASP ARG LEU ILE THR TYR LEU ASP GLN THR THR GLN          
SEQRES  19 C  354  LYS SER LEU ILE ALA THR VAL GLU LYS GLN LEU LEU GLY          
SEQRES  20 C  354  GLU HIS LEU THR ALA ILE LEU GLN LYS GLY LEU ASN ASN          
SEQRES  21 C  354  LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU SER LEU LEU          
SEQRES  22 C  354  TYR GLN LEU PHE SER ARG VAL ARG GLY GLY VAL GLN VAL          
SEQRES  23 C  354  LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS ALA PHE GLY          
SEQRES  24 C  354  SER THR ILE VAL ILE ASN PRO GLU LYS ASP LYS THR MET          
SEQRES  25 C  354  ARG GLN GLU LEU ASP ASP PHE LYS ASP LYS VAL ASP HIS          
SEQRES  26 C  354  ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU LYS PHE ILE          
SEQRES  27 C  354  ASN ALA MET LYS GLU ALA PHE GLU THR PHE ILE ASN LYS          
SEQRES  28 C  354  ARG PRO ASN                                                  
SEQRES   1 D  354  SER MET PRO LYS LEU PRO GLU ASN TYR THR ASP GLU THR          
SEQRES   2 D  354  TRP GLN LYS LEU LYS GLU ALA VAL GLU ALA ILE GLN ASN          
SEQRES   3 D  354  SER THR SER ILE LYS TYR ASN LEU GLU GLU LEU TYR GLN          
SEQRES   4 D  354  ALA VAL GLU ASN LEU CYS SER TYR LYS ILE SER ALA ASN          
SEQRES   5 D  354  LEU TYR LYS GLN LEU ARG GLN ILE CYS GLU ASP HIS ILE          
SEQRES   6 D  354  LYS ALA GLN ILE HIS GLN PHE ARG GLU ASP SER LEU ASP          
SEQRES   7 D  354  SER VAL LEU PHE LEU LYS LYS ILE ASP ARG CYS TRP GLN          
SEQRES   8 D  354  ASN HIS CYS ARG GLN MET ILE MET ILE ARG SER ILE PHE          
SEQRES   9 D  354  LEU PHE LEU ASP ARG THR TYR VAL LEU GLN ASN SER MET          
SEQRES  10 D  354  LEU PRO SER ILE TRP ASP MET GLY LEU GLU LEU PHE ARG          
SEQRES  11 D  354  ALA HIS ILE ILE SER ASP GLN LYS VAL GLN ASN LYS THR          
SEQRES  12 D  354  ILE ASP GLY ILE LEU LEU LEU ILE GLU ARG GLU ARG ASN          
SEQRES  13 D  354  GLY GLU ALA ILE ASP ARG SER LEU LEU ARG SER LEU LEU          
SEQRES  14 D  354  SER MET LEU SER ASP LEU GLN ILE TYR GLN ASP SER PHE          
SEQRES  15 D  354  GLU GLN ARG PHE LEU GLU GLU THR ASN ARG LEU TYR ALA          
SEQRES  16 D  354  ALA GLU GLY GLN LYS LEU MET GLN GLU ARG GLU VAL PRO          
SEQRES  17 D  354  GLU TYR LEU HIS HIS VAL ASN LYS ARG LEU GLU GLU GLU          
SEQRES  18 D  354  ALA ASP ARG LEU ILE THR TYR LEU ASP GLN THR THR GLN          
SEQRES  19 D  354  LYS SER LEU ILE ALA THR VAL GLU LYS GLN LEU LEU GLY          
SEQRES  20 D  354  GLU HIS LEU THR ALA ILE LEU GLN LYS GLY LEU ASN ASN          
SEQRES  21 D  354  LEU LEU ASP GLU ASN ARG ILE GLN ASP LEU SER LEU LEU          
SEQRES  22 D  354  TYR GLN LEU PHE SER ARG VAL ARG GLY GLY VAL GLN VAL          
SEQRES  23 D  354  LEU LEU GLN GLN TRP ILE GLU TYR ILE LYS ALA PHE GLY          
SEQRES  24 D  354  SER THR ILE VAL ILE ASN PRO GLU LYS ASP LYS THR MET          
SEQRES  25 D  354  ARG GLN GLU LEU ASP ASP PHE LYS ASP LYS VAL ASP HIS          
SEQRES  26 D  354  ILE ILE ASP ILE CYS PHE LEU LYS ASN GLU LYS PHE ILE          
SEQRES  27 D  354  ASN ALA MET LYS GLU ALA PHE GLU THR PHE ILE ASN LYS          
SEQRES  28 D  354  ARG PRO ASN                                                  
HET    EDO  A1534       4                                                       
HET    EDO  A1535       4                                                       
HET    EDO  A1536       4                                                       
HET    EDO  A1537       4                                                       
HET    EDO  B1534       4                                                       
HET    EDO  C1535       4                                                       
HET    EDO  D1533       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  EDO    7(C2 H6 O2)                                                  
FORMUL  12  HOH   *253(H2 O)                                                    
HELIX    1   1 ASP A  196  ASN A  211  1                                  16    
HELIX    2   2 ASN A  218  LYS A  233  1                                  16    
HELIX    3   3 ILE A  234  GLN A  253  1                                  20    
HELIX    4   4 ILE A  254  GLU A  259  5                                   6    
HELIX    5   5 ASP A  263  PHE A  289  1                                  27    
HELIX    6   6 PHE A  289  THR A  295  1                                   7    
HELIX    7   7 SER A  305  ILE A  318  1                                  14    
HELIX    8   8 ASP A  321  ASN A  341  1                                  21    
HELIX    9   9 ASP A  346  LEU A  360  1                                  15    
HELIX   10  10 ILE A  362  PHE A  367  1                                   6    
HELIX   11  11 PHE A  367  ARG A  390  1                                  24    
HELIX   12  12 GLU A  391  TYR A  413  1                                  23    
HELIX   13  13 ASP A  415  THR A  417  5                                   3    
HELIX   14  14 THR A  418  LEU A  431  1                                  14    
HELIX   15  15 HIS A  434  GLU A  449  1                                  16    
HELIX   16  16 ARG A  451  SER A  463  1                                  13    
HELIX   17  17 GLY A  467  ASN A  490  1                                  24    
HELIX   18  18 THR A  496  PHE A  516  1                                  21    
HELIX   19  19 ASN A  519  THR A  532  1                                  14    
HELIX   20  20 ASP B  196  ASN B  211  1                                  16    
HELIX   21  21 ASN B  218  LYS B  233  1                                  16    
HELIX   22  22 ILE B  234  GLN B  253  1                                  20    
HELIX   23  23 ILE B  254  GLU B  259  5                                   6    
HELIX   24  24 ASP B  263  PHE B  289  1                                  27    
HELIX   25  25 PHE B  289  THR B  295  1                                   7    
HELIX   26  26 SER B  305  ILE B  318  1                                  14    
HELIX   27  27 ASP B  321  ASN B  341  1                                  21    
HELIX   28  28 ASP B  346  LEU B  360  1                                  15    
HELIX   29  29 ILE B  362  PHE B  367  1                                   6    
HELIX   30  30 PHE B  367  ARG B  390  1                                  24    
HELIX   31  31 GLU B  391  LEU B  414  1                                  24    
HELIX   32  32 ASP B  415  THR B  417  5                                   3    
HELIX   33  33 THR B  418  LEU B  431  1                                  14    
HELIX   34  34 HIS B  434  GLU B  449  1                                  16    
HELIX   35  35 ARG B  451  SER B  463  1                                  13    
HELIX   36  36 GLY B  467  ASN B  490  1                                  24    
HELIX   37  37 THR B  496  PHE B  516  1                                  21    
HELIX   38  38 ASN B  519  THR B  532  1                                  14    
HELIX   39  39 ASP C  196  SER C  212  1                                  17    
HELIX   40  40 ASN C  218  SER C  231  1                                  14    
HELIX   41  41 ASN C  237  GLN C  253  1                                  17    
HELIX   42  42 ILE C  254  GLU C  259  5                                   6    
HELIX   43  43 ASP C  263  PHE C  289  1                                  27    
HELIX   44  44 PHE C  289  LEU C  298  1                                  10    
HELIX   45  45 SER C  305  ILE C  318  1                                  14    
HELIX   46  46 ASP C  321  ASN C  341  1                                  21    
HELIX   47  47 ASP C  346  LEU C  360  1                                  15    
HELIX   48  48 ILE C  362  PHE C  367  1                                   6    
HELIX   49  49 PHE C  367  ARG C  390  1                                  24    
HELIX   50  50 GLU C  391  LEU C  414  1                                  24    
HELIX   51  51 ASP C  415  THR C  417  5                                   3    
HELIX   52  52 THR C  418  LEU C  431  1                                  14    
HELIX   53  53 HIS C  434  GLU C  449  1                                  16    
HELIX   54  54 ARG C  451  SER C  463  1                                  13    
HELIX   55  55 GLY C  467  ASN C  490  1                                  24    
HELIX   56  56 THR C  496  CYS C  515  1                                  20    
HELIX   57  57 ASN C  519  GLU C  531  1                                  13    
HELIX   58  58 ASP D  196  ASN D  211  1                                  16    
HELIX   59  59 ASN D  218  CYS D  230  1                                  13    
HELIX   60  60 ASN D  237  GLN D  253  1                                  17    
HELIX   61  61 ILE D  254  GLU D  259  5                                   6    
HELIX   62  62 ASP D  263  PHE D  289  1                                  27    
HELIX   63  63 PHE D  289  GLN D  299  1                                  11    
HELIX   64  64 SER D  305  ILE D  318  1                                  14    
HELIX   65  65 ASP D  321  ASN D  341  1                                  21    
HELIX   66  66 ASP D  346  LEU D  360  1                                  15    
HELIX   67  67 ILE D  362  PHE D  367  1                                   6    
HELIX   68  68 PHE D  367  ARG D  390  1                                  24    
HELIX   69  69 GLU D  391  LEU D  414  1                                  24    
HELIX   70  70 ASP D  415  THR D  417  5                                   3    
HELIX   71  71 THR D  418  LEU D  431  1                                  14    
HELIX   72  72 HIS D  434  GLU D  449  1                                  16    
HELIX   73  73 ARG D  451  SER D  463  1                                  13    
HELIX   74  74 GLY D  467  ILE D  489  1                                  23    
HELIX   75  75 GLU D  500  CYS D  515  1                                  16    
HELIX   76  76 ASN D  519  GLU D  531  1                                  13    
CISPEP   1 ASP A  260    SER A  261          0         2.03                     
CISPEP   2 ASP B  260    SER B  261          0         2.91                     
SITE     1 AC1  3 ARG A 243  GLU A 312  ALA A 316                               
SITE     1 AC2  5 ILE A 345  ASP A 346  ARG A 347  GLN B 460                    
SITE     2 AC2  5 SER B 463                                                     
SITE     1 AC3  3 ASP A 272  GLN A 276  SER A 348                               
SITE     1 AC4  5 GLN A 210  ILE A 250  HIS A 278  GLN A 281                    
SITE     2 AC4  5 MET A 282                                                     
SITE     1 AC5  5 GLN B 210  ILE B 250  HIS B 278  GLN B 281                    
SITE     2 AC5  5 MET B 282                                                     
SITE     1 AC6  4 ARG C 243  GLU C 247  ALA C 316  LYS D 323                    
SITE     1 AC7  5 GLN C 460  ILE D 345  ASP D 346  ARG D 347                    
SITE     2 AC7  5 SER D 348                                                     
CRYST1   64.248  157.091   92.916  90.00  95.71  90.00 P 1 21 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      0.015565  0.000000  0.001556        0.00000                         
SCALE2      0.000000  0.006366  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010816        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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