GenomeNet

Database: PDB
Entry: 1E50
LinkDB: 1E50
Original site: 1E50 
HEADER    TRANSCRIPTION                           13-JUL-00   1E50              
TITLE     AML1/CBFBETA COMPLEX                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CORE-BINDING FACTOR ALPHA SUBUNIT;                         
COMPND   3 CHAIN: A, C, E, G, Q, R;                                             
COMPND   4 FRAGMENT: RUNT DOMAIN RESIDUES 50-183;                               
COMPND   5 SYNONYM: CBFA2/PEPBP2AB/RUNX1, AML1;                                 
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CORE-BINDING FACTOR CBF-BETA;                              
COMPND   9 CHAIN: B, D, F, H;                                                   
COMPND  10 FRAGMENT: HETERODIMERISATION DOMAIN RESIDUES 2-135;                  
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: AML1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VARIANT: C41;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PRSET;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: CBFB;                                                          
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_VARIANT: C41;                                      
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PRSET                                     
KEYWDS    TRANSCRIPTION FACTOR, TRANSCRIPTION                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.J.WARREN,J.BRAVO,R.L.WILLIAMS,T.H.RABBITS                           
REVDAT   4   24-JAN-18 1E50    1       SOURCE                                   
REVDAT   3   09-JUN-09 1E50    1       HEADER KEYWDS REMARK                     
REVDAT   2   24-FEB-09 1E50    1       VERSN                                    
REVDAT   1   12-JUL-01 1E50    0                                                
JRNL        AUTH   A.J.WARREN,J.BRAVO,R.L.WILLIAMS,T.H.RABBITS                  
JRNL        TITL   STRUCTURAL BASIS FOR THE HETERODIMERIC INTERACTION BETWEEN   
JRNL        TITL 2 THE ACUTE LEUKAEMIA-ASSOCIATED TRANSCRIPTION FACTORS AML1    
JRNL        TITL 3 AND CBFBETA                                                  
JRNL        REF    EMBO J.                       V.  19  3004 2000              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   10856244                                                     
JRNL        DOI    10.1093/EMBOJ/19.12.3004                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.82                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1357943.020                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 63323                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : SHELLS                          
REMARK   3   R VALUE            (WORKING SET) : 0.268                           
REMARK   3   FREE R VALUE                     : 0.287                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1905                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.76                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 10162                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3750                       
REMARK   3   BIN FREE R VALUE                    : 0.4510                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 3.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 320                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.025                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9539                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 157                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 66.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -8.59000                                             
REMARK   3    B22 (A**2) : 4.23000                                              
REMARK   3    B33 (A**2) : 4.36000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.96000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.39                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.35                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.46                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.49                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.400                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.80                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.770                           
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) : 2.040 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.360 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.120 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 4.600 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 41.00                                                
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  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1E50 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-JUL-00.                  
REMARK 100 THE DEPOSITION ID IS D_1290004578.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-FEB-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 110.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9366                             
REMARK 200  MONOCHROMATOR                  : DIAMOND (111)                      
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63354                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 25.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : 0.08500                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.64                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.48000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.10                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 6.50                                  
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       39.69000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Q                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: R                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A    50                                                      
REMARK 465     MET A    51                                                      
REMARK 465     VAL A    52                                                      
REMARK 465     GLU A    53                                                      
REMARK 465     VAL A    54                                                      
REMARK 465     LEU A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     ASP A    57                                                      
REMARK 465     HIS A    58                                                      
REMARK 465     ARG A   174                                                      
REMARK 465     GLU A   175                                                      
REMARK 465     PRO A   176                                                      
REMARK 465     ARG A   177                                                      
REMARK 465     ARG A   178                                                      
REMARK 465     HIS A   179                                                      
REMARK 465     ARG A   180                                                      
REMARK 465     GLN A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     LEU A   183                                                      
REMARK 465     GLN B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     GLU B    76                                                      
REMARK 465     GLN B    77                                                      
REMARK 465     SER C    50                                                      
REMARK 465     MET C    51                                                      
REMARK 465     VAL C    52                                                      
REMARK 465     GLU C    53                                                      
REMARK 465     HIS C   179                                                      
REMARK 465     ARG C   180                                                      
REMARK 465     GLN C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     LEU C   183                                                      
REMARK 465     ALA D    71                                                      
REMARK 465     SER D    72                                                      
REMARK 465     TRP D    73                                                      
REMARK 465     GLN D    74                                                      
REMARK 465     GLY D    75                                                      
REMARK 465     GLU D    76                                                      
REMARK 465     GLN D    77                                                      
REMARK 465     ARG D    78                                                      
REMARK 465     GLN D    79                                                      
REMARK 465     SER E    50                                                      
REMARK 465     MET E    51                                                      
REMARK 465     VAL E    52                                                      
REMARK 465     GLU E    53                                                      
REMARK 465     VAL E    54                                                      
REMARK 465     LEU E    55                                                      
REMARK 465     ALA E    56                                                      
REMARK 465     PRO E   176                                                      
REMARK 465     ARG E   177                                                      
REMARK 465     ARG E   178                                                      
REMARK 465     HIS E   179                                                      
REMARK 465     ARG E   180                                                      
REMARK 465     GLN E   181                                                      
REMARK 465     LYS E   182                                                      
REMARK 465     LEU E   183                                                      
REMARK 465     ALA F    71                                                      
REMARK 465     SER F    72                                                      
REMARK 465     TRP F    73                                                      
REMARK 465     GLN F    74                                                      
REMARK 465     GLY F    75                                                      
REMARK 465     GLU F    76                                                      
REMARK 465     GLN F    77                                                      
REMARK 465     ARG F    78                                                      
REMARK 465     GLN F    79                                                      
REMARK 465     SER G    50                                                      
REMARK 465     MET G    51                                                      
REMARK 465     VAL G    52                                                      
REMARK 465     GLU G    53                                                      
REMARK 465     VAL G    54                                                      
REMARK 465     LEU G    55                                                      
REMARK 465     ALA G    56                                                      
REMARK 465     PRO G   176                                                      
REMARK 465     ARG G   177                                                      
REMARK 465     ARG G   178                                                      
REMARK 465     HIS G   179                                                      
REMARK 465     ARG G   180                                                      
REMARK 465     GLN G   181                                                      
REMARK 465     LYS G   182                                                      
REMARK 465     LEU G   183                                                      
REMARK 465     GLN H    74                                                      
REMARK 465     GLY H    75                                                      
REMARK 465     GLU H    76                                                      
REMARK 465     GLN H    77                                                      
REMARK 465     SER Q    50                                                      
REMARK 465     MET Q    51                                                      
REMARK 465     VAL Q    52                                                      
REMARK 465     GLU Q    53                                                      
REMARK 465     VAL Q    54                                                      
REMARK 465     LEU Q    55                                                      
REMARK 465     ALA Q    56                                                      
REMARK 465     ASP Q    57                                                      
REMARK 465     HIS Q    58                                                      
REMARK 465     PRO Q    59                                                      
REMARK 465     GLY Q    60                                                      
REMARK 465     GLU Q    61                                                      
REMARK 465     GLY Q   172                                                      
REMARK 465     PRO Q   173                                                      
REMARK 465     ARG Q   174                                                      
REMARK 465     GLU Q   175                                                      
REMARK 465     PRO Q   176                                                      
REMARK 465     ARG Q   177                                                      
REMARK 465     ARG Q   178                                                      
REMARK 465     HIS Q   179                                                      
REMARK 465     ARG Q   180                                                      
REMARK 465     GLN Q   181                                                      
REMARK 465     LYS Q   182                                                      
REMARK 465     LEU Q   183                                                      
REMARK 465     SER R    50                                                      
REMARK 465     MET R    51                                                      
REMARK 465     VAL R    52                                                      
REMARK 465     GLU R    53                                                      
REMARK 465     VAL R    54                                                      
REMARK 465     LEU R    55                                                      
REMARK 465     ALA R    56                                                      
REMARK 465     ASP R    57                                                      
REMARK 465     HIS R    58                                                      
REMARK 465     PRO R    59                                                      
REMARK 465     GLY R    60                                                      
REMARK 465     GLU R    61                                                      
REMARK 465     GLY R   172                                                      
REMARK 465     PRO R   173                                                      
REMARK 465     ARG R   174                                                      
REMARK 465     GLU R   175                                                      
REMARK 465     PRO R   176                                                      
REMARK 465     ARG R   177                                                      
REMARK 465     ARG R   178                                                      
REMARK 465     HIS R   179                                                      
REMARK 465     ARG R   180                                                      
REMARK 465     GLN R   181                                                      
REMARK 465     LYS R   182                                                      
REMARK 465     LEU R   183                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ARG A 142    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 144    CG   CD   CE   NZ                                   
REMARK 470     SER B  72    OG                                                  
REMARK 470     ARG B  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  79    CG   CD   OE1  NE2                                  
REMARK 470     VAL C  54    CG1  CG2                                            
REMARK 470     LEU C  55    CG   CD1  CD2                                       
REMARK 470     ASP C  57    CG   OD1  OD2                                       
REMARK 470     HIS C  58    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 144    CG   CD   CE   NZ                                   
REMARK 470     ARG C 178    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASP E  57    CG   OD1  OD2                                       
REMARK 470     HIS E  58    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS E 144    CG   CD   CE   NZ                                   
REMARK 470     ASP G  57    CG   OD1  OD2                                       
REMARK 470     HIS G  58    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS G 144    CG   CD   CE   NZ                                   
REMARK 470     SER H  72    OG                                                  
REMARK 470     ARG H  78    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN H  79    CG   CD   OE1  NE2                                  
REMARK 470     LYS Q 144    CG   CD   CE   NZ                                   
REMARK 470     LYS R 144    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    ARG E   174     N    GLU E   175              1.53            
REMARK 500   NE2  GLN B    67     O    HOH B  2005              1.95            
REMARK 500   O    GLY D    61     O    HOH D  2014              2.07            
REMARK 500   OG1  THR E   147     O    HOH E  2015              2.07            
REMARK 500   OG1  THR F    62     O    HOH F  2013              2.09            
REMARK 500   ND1  HIS F    37     O    HOH F  2006              2.12            
REMARK 500   O    GLU B    89     N    GLU B    91              2.18            
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    ARG A 139   C     ARG A 139   O       0.145                       
REMARK 500    LYS A 144   CA    LYS A 144   C       0.369                       
REMARK 500    LYS A 144   C     LYS A 144   O      -0.246                       
REMARK 500    SER A 145   N     SER A 145   CA      0.251                       
REMARK 500    ARG E 174   CA    ARG E 174   C       0.314                       
REMARK 500    GLU E 175   CB    GLU E 175   CG      0.121                       
REMARK 500    GLU H  89   CA    GLU H  89   C       0.215                       
REMARK 500    GLU H  89   C     GLU H  89   O      -0.178                       
REMARK 500    ARG H  90   N     ARG H  90   CA      0.174                       
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    LYS A 144   O   -  C   -  N   ANGL. DEV. = -11.3 DEGREES          
REMARK 500    SER A 145   N   -  CA  -  C   ANGL. DEV. =  17.1 DEGREES          
REMARK 500    ARG E 174   CA  -  C   -  O   ANGL. DEV. = -28.3 DEGREES          
REMARK 500    ARG E 174   CA  -  C   -  N   ANGL. DEV. =  45.8 DEGREES          
REMARK 500    ARG E 174   O   -  C   -  N   ANGL. DEV. = -43.8 DEGREES          
REMARK 500    GLU E 175   N   -  CA  -  CB  ANGL. DEV. =  11.6 DEGREES          
REMARK 500    GLU E 175   CA  -  CB  -  CG  ANGL. DEV. =  18.1 DEGREES          
REMARK 500    GLU H  89   CA  -  C   -  N   ANGL. DEV. =  16.8 DEGREES          
REMARK 500    GLU H  89   O   -  C   -  N   ANGL. DEV. = -11.7 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    LEU A  94      -72.65    -78.79                                   
REMARK 500    ASN A 109     -177.50   -177.54                                   
REMARK 500    SER A 114       73.79   -160.27                                   
REMARK 500    ARG A 142       76.69    -33.12                                   
REMARK 500    LYS A 144       40.74   -109.99                                   
REMARK 500    SER A 145      168.81    -32.40                                   
REMARK 500    GLU B  24      117.81    -38.18                                   
REMARK 500    GLN B  79      128.94    175.97                                   
REMARK 500    ARG B  90      -35.73    -17.00                                   
REMARK 500    GLN B 117      -61.46    -90.41                                   
REMARK 500    LEU C  55      -57.95    -21.00                                   
REMARK 500    ALA C  56      112.06     70.22                                   
REMARK 500    ASP C  57     -161.42    165.33                                   
REMARK 500    HIS C  58      -26.93    101.87                                   
REMARK 500    LEU C  94      -74.40    -76.41                                   
REMARK 500    ASN C 109     -156.33   -145.71                                   
REMARK 500    GLU C 111      -77.84    -85.32                                   
REMARK 500    ALA C 120       33.61    -96.53                                   
REMARK 500    ARG C 174     -169.65   -112.18                                   
REMARK 500    GLU C 175      -93.47     46.40                                   
REMARK 500    PRO C 176      -98.93    -18.07                                   
REMARK 500    ARG C 177     -120.59    165.47                                   
REMARK 500    ASP D   7       75.39   -119.57                                   
REMARK 500    ARG D  35      139.29   -172.36                                   
REMARK 500    SER D  82     -167.93    -65.47                                   
REMARK 500    GLU D  89      -73.05    -94.04                                   
REMARK 500    ARG D  90      -55.82     -9.99                                   
REMARK 500    HIS E  58      -46.92    106.95                                   
REMARK 500    LEU E  94      -72.33    -85.45                                   
REMARK 500    ASN E 109     -159.07   -138.09                                   
REMARK 500    GLU E 111      -76.00    -88.49                                   
REMARK 500    SER E 114       85.45   -153.13                                   
REMARK 500    PRO E 173     -174.24    -57.38                                   
REMARK 500    GLU F  24      129.21    -33.78                                   
REMARK 500    ARG F  35      142.59   -173.89                                   
REMARK 500    SER F  82     -162.86    -69.13                                   
REMARK 500    GLU F  89      -70.92    -96.14                                   
REMARK 500    ARG F  90      -48.28    -14.00                                   
REMARK 500    ASN F 104       53.61     38.14                                   
REMARK 500    GLN F 117      -61.03    -91.78                                   
REMARK 500    HIS G  58      -66.15     98.08                                   
REMARK 500    LEU G  94      -73.60    -81.36                                   
REMARK 500    GLU G 111      -78.95    -72.69                                   
REMARK 500    SER G 114       77.59   -164.75                                   
REMARK 500    LYS G 144      173.57    -57.66                                   
REMARK 500    ARG G 174      -99.79    -88.31                                   
REMARK 500    PHE H  32       55.30     21.85                                   
REMARK 500    ASP H  34       73.28   -100.79                                   
REMARK 500    SER H  53      163.31    171.38                                   
REMARK 500    GLN H  79      134.17   -177.85                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      73 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LYS A  144     SER A  145                 -148.53                    
REMARK 500 ARG E  174     GLU E  175                  131.54                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LYS A 144        -27.31                                           
REMARK 500    ARG E 174        113.67                                           
REMARK 500    GLU F 129         12.62                                           
REMARK 500    ARG H  35         12.11                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1E50 A   50   183  UNP    Q01196   AML1_HUMAN      50    183             
DBREF  1E50 B    2   135  UNP    Q13951   PEBB_HUMAN       2    135             
DBREF  1E50 C   50   183  UNP    Q01196   AML1_HUMAN      50    183             
DBREF  1E50 D    2   135  UNP    Q13951   PEBB_HUMAN       2    135             
DBREF  1E50 E   50   183  UNP    Q01196   AML1_HUMAN      50    183             
DBREF  1E50 F    2   135  UNP    Q13951   PEBB_HUMAN       2    135             
DBREF  1E50 G   50   183  UNP    Q01196   AML1_HUMAN      50    183             
DBREF  1E50 H    2   135  UNP    Q13951   PEBB_HUMAN       2    135             
DBREF  1E50 Q   50   183  UNP    Q01196   AML1_HUMAN      50    183             
DBREF  1E50 R   50   183  UNP    Q01196   AML1_HUMAN      50    183             
SEQRES   1 A  134  SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU          
SEQRES   2 A  134  VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU          
SEQRES   3 A  134  PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA          
SEQRES   4 A  134  PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR          
SEQRES   5 A  134  LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER          
SEQRES   6 A  134  ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN          
SEQRES   7 A  134  VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER          
SEQRES   8 A  134  GLY ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE          
SEQRES   9 A  134  THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE          
SEQRES  10 A  134  LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS          
SEQRES  11 A  134  ARG GLN LYS LEU                                              
SEQRES   1 B  134  PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU ASN          
SEQRES   2 B  134  GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU ILE          
SEQRES   3 B  134  LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU ARG          
SEQRES   4 B  134  GLN ALA ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG SER          
SEQRES   5 B  134  GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER LEU          
SEQRES   6 B  134  GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG GLN          
SEQRES   7 B  134  THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU ALA          
SEQRES   8 B  134  GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN GLY          
SEQRES   9 B  134  VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU GLN ARG          
SEQRES  10 B  134  LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU ARG          
SEQRES  11 B  134  ALA GLN GLN GLU                                              
SEQRES   1 C  134  SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU          
SEQRES   2 C  134  VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU          
SEQRES   3 C  134  PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA          
SEQRES   4 C  134  PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR          
SEQRES   5 C  134  LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER          
SEQRES   6 C  134  ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN          
SEQRES   7 C  134  VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER          
SEQRES   8 C  134  GLY ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE          
SEQRES   9 C  134  THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE          
SEQRES  10 C  134  LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS          
SEQRES  11 C  134  ARG GLN LYS LEU                                              
SEQRES   1 D  134  PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU ASN          
SEQRES   2 D  134  GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU ILE          
SEQRES   3 D  134  LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU ARG          
SEQRES   4 D  134  GLN ALA ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG SER          
SEQRES   5 D  134  GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER LEU          
SEQRES   6 D  134  GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG GLN          
SEQRES   7 D  134  THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU ALA          
SEQRES   8 D  134  GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN GLY          
SEQRES   9 D  134  VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU GLN ARG          
SEQRES  10 D  134  LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU ARG          
SEQRES  11 D  134  ALA GLN GLN GLU                                              
SEQRES   1 E  134  SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU          
SEQRES   2 E  134  VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU          
SEQRES   3 E  134  PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA          
SEQRES   4 E  134  PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR          
SEQRES   5 E  134  LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER          
SEQRES   6 E  134  ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN          
SEQRES   7 E  134  VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER          
SEQRES   8 E  134  GLY ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE          
SEQRES   9 E  134  THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE          
SEQRES  10 E  134  LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS          
SEQRES  11 E  134  ARG GLN LYS LEU                                              
SEQRES   1 F  134  PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU ASN          
SEQRES   2 F  134  GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU ILE          
SEQRES   3 F  134  LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU ARG          
SEQRES   4 F  134  GLN ALA ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG SER          
SEQRES   5 F  134  GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER LEU          
SEQRES   6 F  134  GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG GLN          
SEQRES   7 F  134  THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU ALA          
SEQRES   8 F  134  GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN GLY          
SEQRES   9 F  134  VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU GLN ARG          
SEQRES  10 F  134  LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU ARG          
SEQRES  11 F  134  ALA GLN GLN GLU                                              
SEQRES   1 G  134  SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU          
SEQRES   2 G  134  VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU          
SEQRES   3 G  134  PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA          
SEQRES   4 G  134  PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR          
SEQRES   5 G  134  LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER          
SEQRES   6 G  134  ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN          
SEQRES   7 G  134  VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER          
SEQRES   8 G  134  GLY ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE          
SEQRES   9 G  134  THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE          
SEQRES  10 G  134  LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS          
SEQRES  11 G  134  ARG GLN LYS LEU                                              
SEQRES   1 H  134  PRO ARG VAL VAL PRO ASP GLN ARG SER LYS PHE GLU ASN          
SEQRES   2 H  134  GLU GLU PHE PHE ARG LYS LEU SER ARG GLU CYS GLU ILE          
SEQRES   3 H  134  LYS TYR THR GLY PHE ARG ASP ARG PRO HIS GLU GLU ARG          
SEQRES   4 H  134  GLN ALA ARG PHE GLN ASN ALA CYS ARG ASP GLY ARG SER          
SEQRES   5 H  134  GLU ILE ALA PHE VAL ALA THR GLY THR ASN LEU SER LEU          
SEQRES   6 H  134  GLN PHE PHE PRO ALA SER TRP GLN GLY GLU GLN ARG GLN          
SEQRES   7 H  134  THR PRO SER ARG GLU TYR VAL ASP LEU GLU ARG GLU ALA          
SEQRES   8 H  134  GLY LYS VAL TYR LEU LYS ALA PRO MET ILE LEU ASN GLY          
SEQRES   9 H  134  VAL CYS VAL ILE TRP LYS GLY TRP ILE ASP LEU GLN ARG          
SEQRES  10 H  134  LEU ASP GLY MET GLY CYS LEU GLU PHE ASP GLU GLU ARG          
SEQRES  11 H  134  ALA GLN GLN GLU                                              
SEQRES   1 Q  134  SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU          
SEQRES   2 Q  134  VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU          
SEQRES   3 Q  134  PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA          
SEQRES   4 Q  134  PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR          
SEQRES   5 Q  134  LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER          
SEQRES   6 Q  134  ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN          
SEQRES   7 Q  134  VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER          
SEQRES   8 Q  134  GLY ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE          
SEQRES   9 Q  134  THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE          
SEQRES  10 Q  134  LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS          
SEQRES  11 Q  134  ARG GLN LYS LEU                                              
SEQRES   1 R  134  SER MET VAL GLU VAL LEU ALA ASP HIS PRO GLY GLU LEU          
SEQRES   2 R  134  VAL ARG THR ASP SER PRO ASN PHE LEU CYS SER VAL LEU          
SEQRES   3 R  134  PRO THR HIS TRP ARG CYS ASN LYS THR LEU PRO ILE ALA          
SEQRES   4 R  134  PHE LYS VAL VAL ALA LEU GLY ASP VAL PRO ASP GLY THR          
SEQRES   5 R  134  LEU VAL THR VAL MET ALA GLY ASN ASP GLU ASN TYR SER          
SEQRES   6 R  134  ALA GLU LEU ARG ASN ALA THR ALA ALA MET LYS ASN GLN          
SEQRES   7 R  134  VAL ALA ARG PHE ASN ASP LEU ARG PHE VAL GLY ARG SER          
SEQRES   8 R  134  GLY ARG GLY LYS SER PHE THR LEU THR ILE THR VAL PHE          
SEQRES   9 R  134  THR ASN PRO PRO GLN VAL ALA THR TYR HIS ARG ALA ILE          
SEQRES  10 R  134  LYS ILE THR VAL ASP GLY PRO ARG GLU PRO ARG ARG HIS          
SEQRES  11 R  134  ARG GLN LYS LEU                                              
FORMUL  11  HOH   *157(H2 O)                                                    
HELIX    1   1 ASP B    7  GLU B   15  1                                   9    
HELIX    2   2 GLU B   15  LYS B   20  1                                   6    
HELIX    3   3 PRO B   36  ASP B   50  1                                  15    
HELIX    4   4 ASP B  128  GLU B  135  1                                   8    
HELIX    5   5 ASP D    7  GLU D   15  1                                   9    
HELIX    6   6 GLU D   15  ARG D   23  1                                   9    
HELIX    7   7 PRO D   36  ASP D   50  1                                  15    
HELIX    8   8 ASP D  128  GLN D  134  1                                   7    
HELIX    9   9 ASP F    7  GLU F   15  1                                   9    
HELIX   10  10 GLU F   15  ARG F   23  1                                   9    
HELIX   11  11 PRO F   36  ASP F   50  1                                  15    
HELIX   12  12 ASP F  128  GLN F  134  1                                   7    
HELIX   13  13 ASP H    7  GLU H   15  1                                   9    
HELIX   14  14 GLU H   15  ARG H   23  1                                   9    
HELIX   15  15 PRO H   36  ASP H   50  1                                  15    
HELIX   16  16 ASP H  128  GLN H  134  1                                   7    
SHEET    1   A 4 LEU A  62  ARG A  64  0                                        
SHEET    2   A 4 PHE A  70  SER A  73 -1  N  CYS A  72   O  VAL A  63           
SHEET    3   A 4 LYS A  90  ALA A  93 -1  N  VAL A  92   O  LEU A  71           
SHEET    4   A 4 VAL A 128  ARG A 130 -1  N  ALA A 129   O  VAL A  91           
SHEET    1   B 2 HIS A  78  ARG A  80  0                                        
SHEET    2   B 2 LYS A 167  THR A 169  1  N  LYS A 167   O  TRP A  79           
SHEET    1   C 4 THR A 121  ALA A 123  0                                        
SHEET    2   C 4 LEU A 102  GLY A 108 -1  N  VAL A 103   O  ALA A 122           
SHEET    3   C 4 THR A 147  VAL A 152 -1  N  THR A 151   O  THR A 104           
SHEET    4   C 4 GLN A 158  TYR A 162 -1  N  TYR A 162   O  LEU A 148           
SHEET    1   D 5 ILE B  55  PHE B  57  0                                        
SHEET    2   D 5 CYS B  25  TYR B  29 -1  N  LYS B  28   O  ALA B  56           
SHEET    3   D 5 ASP B 120  PHE B 127 -1  N  GLY B 123   O  CYS B  25           
SHEET    4   D 5 VAL B 106  ASP B 115 -1  N  TRP B 113   O  MET B 122           
SHEET    5   D 5 LYS B  94  LEU B 103 -1  N  LEU B 103   O  VAL B 106           
SHEET    1   E 2 ARG B  52  GLU B  54  0                                        
SHEET    2   E 2 SER B  65  GLN B  67 -1  N  LEU B  66   O  SER B  53           
SHEET    1   F 4 LEU C  62  ARG C  64  0                                        
SHEET    2   F 4 PHE C  70  SER C  73 -1  N  CYS C  72   O  VAL C  63           
SHEET    3   F 4 LYS C  90  ALA C  93 -1  N  VAL C  92   O  LEU C  71           
SHEET    4   F 4 VAL C 128  ARG C 130 -1  N  ALA C 129   O  VAL C  91           
SHEET    1   G 2 HIS C  78  ARG C  80  0                                        
SHEET    2   G 2 LYS C 167  THR C 169  1  N  LYS C 167   O  TRP C  79           
SHEET    1   H 4 THR C 121  ALA C 123  0                                        
SHEET    2   H 4 LEU C 102  GLY C 108 -1  N  VAL C 103   O  ALA C 122           
SHEET    3   H 4 THR C 147  VAL C 152 -1  N  THR C 151   O  THR C 104           
SHEET    4   H 4 GLN C 158  TYR C 162 -1  N  TYR C 162   O  LEU C 148           
SHEET    1   I 6 THR D  62  GLN D  67  0                                        
SHEET    2   I 6 ARG D  52  PHE D  57 -1  N  PHE D  57   O  THR D  62           
SHEET    3   I 6 CYS D  25  TYR D  29 -1  N  LYS D  28   O  ALA D  56           
SHEET    4   I 6 ASP D 120  PHE D 127 -1  N  GLY D 123   O  CYS D  25           
SHEET    5   I 6 VAL D 106  ASP D 115 -1  N  TRP D 113   O  MET D 122           
SHEET    6   I 6 LYS D  94  LEU D 103 -1  N  LEU D 103   O  VAL D 106           
SHEET    1   J 4 LEU E  62  ARG E  64  0                                        
SHEET    2   J 4 PHE E  70  SER E  73 -1  N  CYS E  72   O  VAL E  63           
SHEET    3   J 4 LYS E  90  ALA E  93 -1  N  VAL E  92   O  LEU E  71           
SHEET    4   J 4 VAL E 128  ARG E 130 -1  N  ALA E 129   O  VAL E  91           
SHEET    1   K 2 HIS E  78  ARG E  80  0                                        
SHEET    2   K 2 LYS E 167  THR E 169  1  N  LYS E 167   O  TRP E  79           
SHEET    1   L 4 THR E 121  ALA E 123  0                                        
SHEET    2   L 4 LEU E 102  GLY E 108 -1  N  VAL E 103   O  ALA E 122           
SHEET    3   L 4 THR E 147  VAL E 152 -1  N  THR E 151   O  THR E 104           
SHEET    4   L 4 GLN E 158  TYR E 162 -1  N  TYR E 162   O  LEU E 148           
SHEET    1   M 6 THR F  62  GLN F  67  0                                        
SHEET    2   M 6 ARG F  52  PHE F  57 -1  N  PHE F  57   O  THR F  62           
SHEET    3   M 6 CYS F  25  TYR F  29 -1  N  LYS F  28   O  ALA F  56           
SHEET    4   M 6 ASP F 120  PHE F 127 -1  N  GLY F 123   O  CYS F  25           
SHEET    5   M 6 VAL F 106  ASP F 115 -1  N  TRP F 113   O  MET F 122           
SHEET    6   M 6 LYS F  94  LEU F 103 -1  N  LEU F 103   O  VAL F 106           
SHEET    1   N 4 LEU G  62  ARG G  64  0                                        
SHEET    2   N 4 PHE G  70  SER G  73 -1  N  CYS G  72   O  VAL G  63           
SHEET    3   N 4 LYS G  90  ALA G  93 -1  N  VAL G  92   O  LEU G  71           
SHEET    4   N 4 VAL G 128  ARG G 130 -1  N  ALA G 129   O  VAL G  91           
SHEET    1   O 2 HIS G  78  ARG G  80  0                                        
SHEET    2   O 2 LYS G 167  THR G 169  1  N  LYS G 167   O  TRP G  79           
SHEET    1   P 4 THR G 121  ALA G 123  0                                        
SHEET    2   P 4 LEU G 102  GLY G 108 -1  N  VAL G 103   O  ALA G 122           
SHEET    3   P 4 THR G 147  VAL G 152 -1  N  THR G 151   O  THR G 104           
SHEET    4   P 4 GLN G 158  TYR G 162 -1  N  TYR G 162   O  LEU G 148           
SHEET    1   Q 5 ILE H  55  PHE H  57  0                                        
SHEET    2   Q 5 CYS H  25  TYR H  29 -1  N  LYS H  28   O  ALA H  56           
SHEET    3   Q 5 ASP H 120  PHE H 127 -1  N  GLY H 123   O  CYS H  25           
SHEET    4   Q 5 VAL H 106  ASP H 115 -1  N  TRP H 113   O  MET H 122           
SHEET    5   Q 5 LYS H  94  LEU H 103 -1  N  LEU H 103   O  VAL H 106           
SHEET    1   R 2 ARG H  52  GLU H  54  0                                        
SHEET    2   R 2 SER H  65  GLN H  67 -1  N  LEU H  66   O  SER H  53           
SHEET    1   S 3 PHE Q  70  CYS Q  72  0                                        
SHEET    2   S 3 LYS Q  90  ALA Q  93 -1  N  VAL Q  92   O  LEU Q  71           
SHEET    3   S 3 VAL Q 128  ARG Q 130 -1  N  ALA Q 129   O  VAL Q  91           
SHEET    1   T 2 HIS Q  78  ARG Q  80  0                                        
SHEET    2   T 2 LYS Q 167  THR Q 169  1  N  LYS Q 167   O  TRP Q  79           
SHEET    1   U 2 LEU Q 102  THR Q 104  0                                        
SHEET    2   U 2 THR Q 121  ALA Q 123 -1  N  ALA Q 122   O  VAL Q 103           
SHEET    1   V 2 LEU Q 148  VAL Q 152  0                                        
SHEET    2   V 2 GLN Q 158  TYR Q 162 -1  N  TYR Q 162   O  LEU Q 148           
SHEET    1   W 3 PHE R  70  CYS R  72  0                                        
SHEET    2   W 3 PHE R  89  ALA R  93 -1  N  VAL R  92   O  LEU R  71           
SHEET    3   W 3 VAL R 128  PHE R 131 -1  N  PHE R 131   O  PHE R  89           
SHEET    1   X 2 HIS R  78  ARG R  80  0                                        
SHEET    2   X 2 LYS R 167  THR R 169  1  N  LYS R 167   O  TRP R  79           
SHEET    1   Y 2 LEU R 102  THR R 104  0                                        
SHEET    2   Y 2 THR R 121  ALA R 123 -1  N  ALA R 122   O  VAL R 103           
SHEET    1   Z 2 LEU R 148  VAL R 152  0                                        
SHEET    2   Z 2 GLN R 158  TYR R 162 -1  N  TYR R 162   O  LEU R 148           
CISPEP   1 ASN A  155    PRO A  156          0         0.07                     
CISPEP   2 ASN C  155    PRO C  156          0        -0.31                     
CISPEP   3 ASN E  155    PRO E  156          0        -0.14                     
CISPEP   4 ASN G  155    PRO G  156          0         0.12                     
CISPEP   5 ASN Q  155    PRO Q  156          0         0.35                     
CISPEP   6 ASN R  155    PRO R  156          0         0.01                     
CRYST1  103.260   79.380  130.100  90.00 101.39  90.00 P 1 21 1     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009684  0.000000  0.001951        0.00000                         
SCALE2      0.000000  0.012598  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007841        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system