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Database: PDB
Entry: 1H88
LinkDB: 1H88
Original site: 1H88 
HEADER    TRANSCRIPTION/DNA                       29-JAN-01   1H88              
TITLE     CRYSTAL STRUCTURE OF TERNARY PROTEIN-DNA COMPLEX1                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CCAAT/ENHANCER BINDING PROTEIN BETA;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 259-336;                                          
COMPND   5 SYNONYM: C/EBP BETA, NFIL-6;                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 OTHER_DETAILS: BZIP DOMAIN;                                          
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: MYB PROTO-ONCOGENE PROTEIN;                                
COMPND  10 CHAIN: C;                                                            
COMPND  11 FRAGMENT: RESIDUES 35-193;                                           
COMPND  12 SYNONYM: C-MYB;                                                      
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MUTATION: YES;                                                       
COMPND  15 OTHER_DETAILS: DNA BINDING DOMAIN;                                   
COMPND  16 MOL_ID: 3;                                                           
COMPND  17 MOLECULE: DNA(5'-(*GP*AP*TP*GP*TP*GP*GP*CP*GP*CP*AP*                 
COMPND  18 AP*TP*CP*CP*TP*TP*AP*AP*CP*GP*GP*AP*CP*TP*G)-3');                    
COMPND  19 CHAIN: D;                                                            
COMPND  20 FRAGMENT: FRAGMENT FROM TOM-1A PROMOTER;                             
COMPND  21 ENGINEERED: YES;                                                     
COMPND  22 MOL_ID: 4;                                                           
COMPND  23 MOLECULE: DNA(5'-(*CP*CP*AP*GP*TP*CP*CP*GP*TP*TP*AP*                 
COMPND  24 AP*GP*GP*AP*TP*TP*GP*CP*GP*CP*CP*AP*CP*AP*T)-3');                    
COMPND  25 CHAIN: E;                                                            
COMPND  26 FRAGMENT: FRAGMENT FROM TOM-1A PROMOTER;                             
COMPND  27 ENGINEERED: 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_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PAR2156;                                  
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  12 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  13 ORGANISM_TAXID: 10090;                                               
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PAR2156;                                  
SOURCE  19 MOL_ID: 3;                                                           
SOURCE  20 SYNTHETIC: YES;                                                      
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_TAXID: 9606;                                                
SOURCE  23 MOL_ID: 4;                                                           
SOURCE  24 SYNTHETIC: YES;                                                      
SOURCE  25 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  26 ORGANISM_TAXID: 9606                                                 
KEYWDS    TRANSCRIPTION-DNA COMPLEX, TRANSCRIPTION REGULATION, BZIP, PROTO-     
KEYWDS   2 ONCOGENE, MYB, C-MYB, C/EBP                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.H.TAHIROV,K.OGATA                                                   
REVDAT   4   08-MAY-19 1H88    1       SOURCE REMARK                            
REVDAT   3   06-MAR-13 1H88    1       SOURCE KEYWDS JRNL   REMARK              
REVDAT   3 2                   1       VERSN  FORMUL MASTER                     
REVDAT   2   24-FEB-09 1H88    1       VERSN                                    
REVDAT   1   28-JAN-02 1H88    0                                                
JRNL        AUTH   T.H.TAHIROV,K.SATO,E.ICHIKAWA-IWATA,M.SASAKI,T.INOUE-BUNGO,  
JRNL        AUTH 2 M.SHIINA,K.KIMURA,S.TAKATA,A.FUJIKAWA,H.MORII,T.KUMASAKA,    
JRNL        AUTH 3 M.YAMAMOTO,S.ISHII,K.OGATA                                   
JRNL        TITL   MECHANISM OF C-MYB-C/EBPBETA COOPERATION FROM SEPARATED      
JRNL        TITL 2 SITES ON A PROMOTER                                          
JRNL        REF    CELL(CAMBRIDGE,MASS.)         V. 108    57 2002              
JRNL        REFN                   ISSN 0092-8674                               
JRNL        PMID   11792321                                                     
JRNL        DOI    10.1016/S0092-8674(01)00636-5                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   T.H.TAHIROV,T.INOUE,M.SASAKI,M.SHIINA,K.KIMURA,K.SATO,       
REMARK   1  AUTH 2 T.KUMASAKA,M.YAMAMOTO,N.KAMIYA,K.OGATA                       
REMARK   1  TITL   CRYSTALS OF TERNARY PROTEIN-DNA COMPLEXES COMPOSED OF        
REMARK   1  TITL 2 DNA-BINDING DOMAINS C-MYB OR V-MYB, C/EBPALPHA OR C/EBPBETA  
REMARK   1  TITL 3 AND TOM-1A PROMOTER FRAGMENT                                 
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  57  1655 2001              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   1  PMID   11679735                                                     
REMARK   1  DOI    10.1107/S0907444901011982                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   T.H.TAHIROV,H.MORII,H.UEDAIRA,M.SASAKI,A.SARAI,S.ADACHI,     
REMARK   1  AUTH 2 S.Y.PARK,N.KAMIYA,K.OGATA                                    
REMARK   1  TITL   CRYSTAL STRUCTURES OF C-MYB DNA-BINDING DOMAIN IN FREE       
REMARK   1  TITL 2 STATE: AN EVIDENCE FOR BINDING OF NA+ AND COMPARISON WITH    
REMARK   1  TITL 3 SOLUTION STRUCTURE                                           
REMARK   1  REF    TO BE PUBLISHED                                              
REMARK   1  REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 0.9                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1568847.920                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 16664                          
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 SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 818                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.97                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2424                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.4120                       
REMARK   3   BIN FREE R VALUE                    : 0.4520                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.20                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 105                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.044                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2490                                    
REMARK   3   NUCLEIC ACID ATOMS       : 1060                                    
REMARK   3   HETEROGEN ATOMS          : 1                                       
REMARK   3   SOLVENT ATOMS            : 25                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 72.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 80.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 36.22000                                             
REMARK   3    B22 (A**2) : -23.51000                                            
REMARK   3    B33 (A**2) : -12.71000                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 15.66000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.41                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.54                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 20.0                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.52                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.58                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.006                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.100                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 18.00                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.130                           
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 5.910 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 8.800 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 10.100; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 13.640; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.27                                                 
REMARK   3   BSOL        : 34.54                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : DNA-RNA_REP.PARAM                              
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : DNA-RNA.TOP                                    
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: BULK SOLVENT MODEL USED. ATOMS C, O, N,   
REMARK   3  CA AND CB ARE HARMONICALLY RESTRAINED DURING REFINEMENT WITH        
REMARK   3  HARMONIC RESTRAINT CONSTANT OF 100                                  
REMARK   4                                                                      
REMARK   4 1H88 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 29-JAN-01.                  
REMARK 100 THE DEPOSITION ID IS D_1290005841.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-FEB-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL45XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : DIAMOND                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 18605                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : 3.151                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.04600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 25.2564                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.23300                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.109                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD AND MIR                  
REMARK 200 SOFTWARE USED: CNS 0.9                                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M AMMONIUM ACETATE, 0.01 M          
REMARK 280  MAGNESIUM CHLORIDE, 10% V/V MPD, 6% V/V GLYCEROL, 0.05 M TRIS       
REMARK 280  HCL BUFFER PH 7.5 AT 24 DEGREES C, PH 7.50, VAPOR DIFFUSION,        
REMARK 280  SITTING DROP, TEMPERATURE 297K                                      
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       78.48300            
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 300 REMARK: OF C/EBP BETA AND MONOMER OF MYB PROTO-                      
REMARK 300  ONCOGENE PROTEINBOUND TO A DUPLEX DNA FRAGMENTFOR                   
REMARK 300  THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350 THE                     
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: PENTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: PENTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6360 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 34030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -14.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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 CHAIN C ENGINEERED MUTATION LYS47MET, ARG48GLY                       
REMARK 400  C/EBP BETA IS IMPORTANT TRANSCRIPTIONAL ACTIVATOR IN THE REGULATION 
REMARK 400  OF GENES INVOLVED IN IMMUNE AND INFLAMMATORY RESPONSES. SPECIFICALL 
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     VAL A   259                                                      
REMARK 465     LYS A   260                                                      
REMARK 465     SER A   261                                                      
REMARK 465     LYS A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     LYS A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     THR A   266                                                      
REMARK 465     VAL B   259                                                      
REMARK 465     LYS B   260                                                      
REMARK 465     SER B   261                                                      
REMARK 465     LYS B   262                                                      
REMARK 465     ALA B   263                                                      
REMARK 465     LYS B   264                                                      
REMARK 465     LYS B   265                                                      
REMARK 465     MET C    35                                                      
REMARK 465     GLY C    36                                                      
REMARK 465     HIS C    37                                                      
REMARK 465     LEU C    38                                                      
REMARK 465     ARG C   191                                                      
REMARK 465     LYS C   192                                                      
REMARK 465     VAL C   193                                                      
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     THR B 266    OG1  CG2                                            
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     DT D   3   O4' -  C1' -  N1  ANGL. DEV. =   2.0 DEGREES          
REMARK 500     DA D  19   O4' -  C1' -  N9  ANGL. DEV. =   2.7 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    ARG A 328      -38.66    -37.23                                   
REMARK 500    PRO A 335      -76.41    -47.44                                   
REMARK 500    SER B 271      155.67    -48.39                                   
REMARK 500    GLN B 333       34.94    -83.66                                   
REMARK 500    PRO B 335      104.98    -54.83                                   
REMARK 500    LYS C  40      -70.70    -58.89                                   
REMARK 500    PRO C  71      174.08    -57.46                                   
REMARK 500    VAL C  85      -72.39   -148.29                                   
REMARK 500    ASN C  87      107.40    -41.33                                   
REMARK 500    GLU C 141      -39.57    -38.56                                   
REMARK 500    THR C 145      154.15    -39.20                                   
REMARK 500    GLN C 157      -71.89    -55.00                                   
REMARK 500    ARG C 161      -72.03    -77.74                                   
REMARK 500    ASN C 164       35.29    -83.61                                   
REMARK 500    PRO C 174      -41.24    -28.46                                   
REMARK 500    THR C 188      -73.04    -74.74                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500     DG D   1         0.09    SIDE CHAIN                              
REMARK 500     DA D  19         0.05    SIDE CHAIN                              
REMARK 500     DC E   1         0.08    SIDE CHAIN                              
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 NH4 C 1191                
DBREF  1H88 A  259   336  UNP    P17676   CEBB_HUMAN     259    336             
DBREF  1H88 B  259   336  UNP    P17676   CEBB_HUMAN     259    336             
DBREF  1H88 C   35   193  UNP    P06876   MYB_MOUSE       35    193             
DBREF  1H88 D    1    26  PDB    1H88     1H88             1     26             
DBREF  1H88 E    1    26  PDB    1H88     1H88             1     26             
SEQADV 1H88 MET C   35  UNP  P17676    LYS    35 ENGINEERED MUTATION            
SEQADV 1H88 GLY C   36  UNP  P17676    ARG    36 ENGINEERED MUTATION            
SEQRES   1 A   78  VAL LYS SER LYS ALA LYS LYS THR VAL ASP LYS HIS SER          
SEQRES   2 A   78  ASP GLU TYR LYS ILE ARG ARG GLU ARG ASN ASN ILE ALA          
SEQRES   3 A   78  VAL ARG LYS SER ARG ASP LYS ALA LYS MET ARG ASN LEU          
SEQRES   4 A   78  GLU THR GLN HIS LYS VAL LEU GLU LEU THR ALA GLU ASN          
SEQRES   5 A   78  GLU ARG LEU GLN LYS LYS VAL GLU GLN LEU SER ARG GLU          
SEQRES   6 A   78  LEU SER THR LEU ARG ASN LEU PHE LYS GLN LEU PRO GLU          
SEQRES   1 B   78  VAL LYS SER LYS ALA LYS LYS THR VAL ASP LYS HIS SER          
SEQRES   2 B   78  ASP GLU TYR LYS ILE ARG ARG GLU ARG ASN ASN ILE ALA          
SEQRES   3 B   78  VAL ARG LYS SER ARG ASP LYS ALA LYS MET ARG ASN LEU          
SEQRES   4 B   78  GLU THR GLN HIS LYS VAL LEU GLU LEU THR ALA GLU ASN          
SEQRES   5 B   78  GLU ARG LEU GLN LYS LYS VAL GLU GLN LEU SER ARG GLU          
SEQRES   6 B   78  LEU SER THR LEU ARG ASN LEU PHE LYS GLN LEU PRO GLU          
SEQRES   1 C  159  MET GLY HIS LEU GLY LYS THR ARG TRP THR ARG GLU GLU          
SEQRES   2 C  159  ASP GLU LYS LEU LYS LYS LEU VAL GLU GLN ASN GLY THR          
SEQRES   3 C  159  ASP ASP TRP LYS VAL ILE ALA ASN TYR LEU PRO ASN ARG          
SEQRES   4 C  159  THR ASP VAL GLN CYS GLN HIS ARG TRP GLN LYS VAL LEU          
SEQRES   5 C  159  ASN PRO GLU LEU ILE LYS GLY PRO TRP THR LYS GLU GLU          
SEQRES   6 C  159  ASP GLN ARG VAL ILE LYS LEU VAL GLN LYS TYR GLY PRO          
SEQRES   7 C  159  LYS ARG TRP SER VAL ILE ALA LYS HIS LEU LYS GLY ARG          
SEQRES   8 C  159  ILE GLY LYS GLN CYS ARG GLU ARG TRP HIS ASN HIS LEU          
SEQRES   9 C  159  ASN PRO GLU VAL LYS LYS THR SER TRP THR GLU GLU GLU          
SEQRES  10 C  159  ASP ARG ILE ILE TYR GLN ALA HIS LYS ARG LEU GLY ASN          
SEQRES  11 C  159  ARG TRP ALA GLU ILE ALA LYS LEU LEU PRO GLY ARG THR          
SEQRES  12 C  159  ASP ASN ALA ILE LYS ASN HIS TRP ASN SER THR MET ARG          
SEQRES  13 C  159  ARG LYS VAL                                                  
SEQRES   1 D   26   DG  DA  DT  DG  DT  DG  DG  DC  DG  DC  DA  DA  DT          
SEQRES   2 D   26   DC  DC  DT  DT  DA  DA  DC  DG  DG  DA  DC  DT  DG          
SEQRES   1 E   26   DC  DC  DA  DG  DT  DC  DC  DG  DT  DT  DA  DA  DG          
SEQRES   2 E   26   DG  DA  DT  DT  DG  DC  DG  DC  DC  DA  DC  DA  DT          
HET    NH4  C1191       1                                                       
HETNAM     NH4 AMMONIUM ION                                                     
FORMUL   6  NH4    H4 N 1+                                                      
FORMUL   7  HOH   *25(H2 O)                                                     
HELIX    1   1 SER A  271  GLN A  333  1                                  63    
HELIX    2   2 SER B  271  GLN B  333  1                                  63    
HELIX    3   3 THR C   44  GLY C   59  1                                  16    
HELIX    4   4 ASP C   62  LEU C   70  1                                   9    
HELIX    5   5 THR C   74  LYS C   84  1                                  11    
HELIX    6   6 THR C   96  GLY C  111  1                                  16    
HELIX    7   7 ARG C  114  LYS C  120  1                                   7    
HELIX    8   8 ILE C  126  HIS C  137  1                                  12    
HELIX    9   9 THR C  148  GLY C  163  1                                  16    
HELIX   10  10 ARG C  165  ALA C  170  1                                   6    
HELIX   11  11 LYS C  171  LEU C  173  5                                   3    
HELIX   12  12 THR C  177  THR C  188  1                                  12    
SITE     1 AC1  3 ALA C 119  LEU C 122  ARG C 125                               
CRYST1   41.735  156.966   55.868  90.00 100.16  90.00 P 1 21 1      4          
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      0.023961  0.000000  0.004294        0.00000                         
SCALE2      0.000000  0.006371  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.018184        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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