GenomeNet

Database: PDB
Entry: 2HE0
LinkDB: 2HE0
Original site: 2HE0 
HEADER    SIGNALING PROTEIN                       21-JUN-06   2HE0              
TITLE     CRYSTAL STRUCTURE OF A HUMAN NOTCH1 ANKYRIN DOMAIN MUTANT             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NOTCH1 PREPROPROTEIN VARIANT;                              
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ANKYRIN DOMAIN, RESIDUES 1873-2115;                        
COMPND   5 SYNONYM: HUMAN NOTCH ANKYRIN DOMAIN MUTANT;                          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: NOTCH 1;                                                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: ROSETTA (DE3);                             
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET41A                                    
KEYWDS    NOTCH, ANKYRIN, SIGNALLING, SIGNALING PROTEIN                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.GUPTA,M.T.EHEBAUER,D.Y.CHIRGADZE,A.MARTINEZ ARIAS,                  
AUTHOR   2 T.L.BLUNDELL                                                         
REVDAT   2   24-FEB-09 2HE0    1       VERSN                                    
REVDAT   1   04-JUL-06 2HE0    0                                                
JRNL        AUTH   D.GUPTA,M.T.EHEBAUER,D.Y.CHIRGADZE,                          
JRNL        AUTH 2 A.MARTINEZ ARIAS,T.L.BLUNDELL                                
JRNL        TITL   CRYSTAL STRUCTURE OF A HUMAN NOTCH1 ANKYRIN DOMAIN           
JRNL        TITL 2 MUTANT                                                       
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.51                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 43201                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2297                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3161                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.82                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2520                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 180                          
REMARK   3   BIN FREE R VALUE                    : 0.3250                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2969                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 4                                       
REMARK   3   SOLVENT ATOMS            : 416                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.124         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.127         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.089         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.961         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.949                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.924                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3017 ; 0.017 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4107 ; 1.491 ; 1.941       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   398 ; 5.659 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   152 ;29.112 ;24.276       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   489 ;13.524 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    28 ;19.929 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   484 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2328 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1572 ; 0.232 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2105 ; 0.298 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   319 ; 0.237 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    53 ; 0.325 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    41 ; 0.338 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2013 ; 3.341 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3102 ; 3.973 ; 6.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1103 ; 4.329 ; 5.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1001 ; 5.677 ; 7.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 2HE0 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-JUN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB038243.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAY-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9769                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45547                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 3.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 10.700                             
REMARK 200  R MERGE                    (I) : 0.06600                            
REMARK 200  R SYM                      (I) : 0.06600                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48800                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ENTRY 1YYH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.55M SODIUM/POTASSIUM TARTRATE, PH      
REMARK 280  8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 65                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/6                                            
REMARK 290       6555   X-Y,X,Z+5/6                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       72.47933            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       36.23967            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       54.35950            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       18.11983            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.59917            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 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 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     MET A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     VAL A     5                                                      
REMARK 465     ARG A     6                                                      
REMARK 465     GLY A     7                                                      
REMARK 465     PRO A     8                                                      
REMARK 465     ASP A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     PHE A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     PRO A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     MET A    15                                                      
REMARK 465     ILE A    16                                                      
REMARK 465     ALA A    17                                                      
REMARK 465     SER A    18                                                      
REMARK 465     CYS A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     GLY A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     GLU A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     SER A    29                                                      
REMARK 465     GLU A    30                                                      
REMARK 465     GLU A    31                                                      
REMARK 465     GLU A    32                                                      
REMARK 465     GLU A    33                                                      
REMARK 465     ASP A    34                                                      
REMARK 465     ALA A    35                                                      
REMARK 465     PRO A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     VAL A    38                                                      
REMARK 465     ILE A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     ASP A    41                                                      
REMARK 465     PHE A    42                                                      
REMARK 465     ILE A    43                                                      
REMARK 465     TYR A    44                                                      
REMARK 465     GLN A    45                                                      
REMARK 465     GLY A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     SER A    48                                                      
REMARK 465     LEU A    49                                                      
REMARK 465     GLU A   245                                                      
REMARK 465     HIS A   246                                                      
REMARK 465     HIS A   247                                                      
REMARK 465     HIS A   248                                                      
REMARK 465     HIS A   249                                                      
REMARK 465     HIS A   250                                                      
REMARK 465     HIS A   251                                                      
REMARK 465     HIS A   252                                                      
REMARK 465     HIS A   253                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     VAL B     5                                                      
REMARK 465     ARG B     6                                                      
REMARK 465     GLY B     7                                                      
REMARK 465     PRO B     8                                                      
REMARK 465     ASP B     9                                                      
REMARK 465     GLY B    10                                                      
REMARK 465     PHE B    11                                                      
REMARK 465     THR B    12                                                      
REMARK 465     PRO B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     MET B    15                                                      
REMARK 465     ILE B    16                                                      
REMARK 465     ALA B    17                                                      
REMARK 465     SER B    18                                                      
REMARK 465     CYS B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     GLY B    21                                                      
REMARK 465     GLY B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     GLU B    25                                                      
REMARK 465     THR B    26                                                      
REMARK 465     GLY B    27                                                      
REMARK 465     ASN B    28                                                      
REMARK 465     SER B    29                                                      
REMARK 465     GLU B    30                                                      
REMARK 465     GLU B    31                                                      
REMARK 465     GLU B    32                                                      
REMARK 465     GLU B    33                                                      
REMARK 465     ASP B    34                                                      
REMARK 465     ALA B    35                                                      
REMARK 465     PRO B    36                                                      
REMARK 465     ALA B    37                                                      
REMARK 465     VAL B    38                                                      
REMARK 465     ILE B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     ASP B    41                                                      
REMARK 465     PHE B    42                                                      
REMARK 465     ILE B    43                                                      
REMARK 465     TYR B    44                                                      
REMARK 465     GLN B    45                                                      
REMARK 465     GLY B    46                                                      
REMARK 465     ALA B    47                                                      
REMARK 465     SER B    48                                                      
REMARK 465     LEU B    49                                                      
REMARK 465     HIS B    50                                                      
REMARK 465     ASN B    51                                                      
REMARK 465     GLU B   245                                                      
REMARK 465     HIS B   246                                                      
REMARK 465     HIS B   247                                                      
REMARK 465     HIS B   248                                                      
REMARK 465     HIS B   249                                                      
REMARK 465     HIS B   250                                                      
REMARK 465     HIS B   251                                                      
REMARK 465     HIS B   252                                                      
REMARK 465     HIS B   253                                                      
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  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN B  52    CB   CG   CD   OE1  NE2                             
REMARK 470     THR B  53    OG1  CG2                                            
REMARK 470     ARG B  55    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLU B 137    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 178    CG   CD   CE   NZ                                   
REMARK 470     LYS B 207    CG   CD   CE   NZ                                   
REMARK 470     LEU B 244    CB   CG   CD1  CD2                                  
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    LEU A   140     O    HOH A   698              1.58            
REMARK 500   NE2  GLN A   103     O    HOH A   640              1.68            
REMARK 500   O    MET B   185     O    HOH B   351              1.71            
REMARK 500   OD2  ASP A   237     O    HOH A   662              1.72            
REMARK 500   OE1  GLN A   103     O    HOH A   641              1.73            
REMARK 500   N    ILE A   144     O    HOH A   698              1.74            
REMARK 500   OE1  GLN B   103     O    HOH B   339              1.91            
REMARK 500   O    HOH A   731     O    HOH A   749              2.04            
REMARK 500   O    HOH A   661     O    HOH A   662              2.07            
REMARK 500   CA   THR B   192     O    HOH B   351              2.11            
REMARK 500   O    HOH A   675     O    HOH A   755              2.12            
REMARK 500   O    HOH A   639     O    HOH A   733              2.12            
REMARK 500   CD1  LEU B   196     O    HOH B   416              2.14            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   752     O    HOH B   359     2555     1.64            
REMARK 500   O    HOH A   662     CB   ARG B    69     3445     2.19            
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    HIS A 147       25.83     84.12                                   
REMARK 500    ASP A 154     -166.37    -75.01                                   
REMARK 500    ASP B  54     -153.98   -107.21                                   
REMARK 500    HIS B 147       27.76     83.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 361        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH B 396        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH B 399        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH B 401        DISTANCE =  6.38 ANGSTROMS                       
REMARK 525    HOH A 669        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH B 414        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A 736        DISTANCE =  5.85 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 510                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1YYH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE WILD TYPE HUMAN NOTCH 1 ANKYRIN             
REMARK 900 DOMAIN                                                               
DBREF  2HE0 A    1   243  UNP    P46531   NOTC1_HUMAN   1873   2115             
DBREF  2HE0 B    1   243  UNP    P46531   NOTC1_HUMAN   1873   2115             
SEQADV 2HE0 ALA A   58  UNP  P46531    GLU  1930 ENGINEERED                     
SEQADV 2HE0 ALA A   66  UNP  P46531    ARG  1938 ENGINEERED                     
SEQADV 2HE0 LEU A  244  UNP  P46531              CLONING ARTIFACT               
SEQADV 2HE0 GLU A  245  UNP  P46531              CLONING ARTIFACT               
SEQADV 2HE0 HIS A  246  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS A  247  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS A  248  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS A  249  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS A  250  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS A  251  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS A  252  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS A  253  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 ALA B   58  UNP  P46531    GLU  1930 ENGINEERED                     
SEQADV 2HE0 ALA B   66  UNP  P46531    ARG  1938 ENGINEERED                     
SEQADV 2HE0 LEU B  244  UNP  P46531              CLONING ARTIFACT               
SEQADV 2HE0 GLU B  245  UNP  P46531              CLONING ARTIFACT               
SEQADV 2HE0 HIS B  246  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS B  247  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS B  248  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS B  249  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS B  250  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS B  251  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS B  252  UNP  P46531              EXPRESSION TAG                 
SEQADV 2HE0 HIS B  253  UNP  P46531              EXPRESSION TAG                 
SEQRES   1 A  253  MET ASP VAL ASN VAL ARG GLY PRO ASP GLY PHE THR PRO          
SEQRES   2 A  253  LEU MET ILE ALA SER CYS SER GLY GLY GLY LEU GLU THR          
SEQRES   3 A  253  GLY ASN SER GLU GLU GLU GLU ASP ALA PRO ALA VAL ILE          
SEQRES   4 A  253  SER ASP PHE ILE TYR GLN GLY ALA SER LEU HIS ASN GLN          
SEQRES   5 A  253  THR ASP ARG THR GLY ALA THR ALA LEU HIS LEU ALA ALA          
SEQRES   6 A  253  ALA TYR SER ARG SER ASP ALA ALA LYS ARG LEU LEU GLU          
SEQRES   7 A  253  ALA SER ALA ASP ALA ASN ILE GLN ASP ASN MET GLY ARG          
SEQRES   8 A  253  THR PRO LEU HIS ALA ALA VAL SER ALA ASP ALA GLN GLY          
SEQRES   9 A  253  VAL PHE GLN ILE LEU ILE ARG ASN ARG ALA THR ASP LEU          
SEQRES  10 A  253  ASP ALA ARG MET HIS ASP GLY THR THR PRO LEU ILE LEU          
SEQRES  11 A  253  ALA ALA ARG LEU ALA VAL GLU GLY MET LEU GLU ASP LEU          
SEQRES  12 A  253  ILE ASN SER HIS ALA ASP VAL ASN ALA VAL ASP ASP LEU          
SEQRES  13 A  253  GLY LYS SER ALA LEU HIS TRP ALA ALA ALA VAL ASN ASN          
SEQRES  14 A  253  VAL ASP ALA ALA VAL VAL LEU LEU LYS ASN GLY ALA ASN          
SEQRES  15 A  253  LYS ASP MET GLN ASN ASN ARG GLU GLU THR PRO LEU PHE          
SEQRES  16 A  253  LEU ALA ALA ARG GLU GLY SER TYR GLU THR ALA LYS VAL          
SEQRES  17 A  253  LEU LEU ASP HIS PHE ALA ASN ARG ASP ILE THR ASP HIS          
SEQRES  18 A  253  MET ASP ARG LEU PRO ARG ASP ILE ALA GLN GLU ARG MET          
SEQRES  19 A  253  HIS HIS ASP ILE VAL ARG LEU LEU ASP LEU GLU HIS HIS          
SEQRES  20 A  253  HIS HIS HIS HIS HIS HIS                                      
SEQRES   1 B  253  MET ASP VAL ASN VAL ARG GLY PRO ASP GLY PHE THR PRO          
SEQRES   2 B  253  LEU MET ILE ALA SER CYS SER GLY GLY GLY LEU GLU THR          
SEQRES   3 B  253  GLY ASN SER GLU GLU GLU GLU ASP ALA PRO ALA VAL ILE          
SEQRES   4 B  253  SER ASP PHE ILE TYR GLN GLY ALA SER LEU HIS ASN GLN          
SEQRES   5 B  253  THR ASP ARG THR GLY ALA THR ALA LEU HIS LEU ALA ALA          
SEQRES   6 B  253  ALA TYR SER ARG SER ASP ALA ALA LYS ARG LEU LEU GLU          
SEQRES   7 B  253  ALA SER ALA ASP ALA ASN ILE GLN ASP ASN MET GLY ARG          
SEQRES   8 B  253  THR PRO LEU HIS ALA ALA VAL SER ALA ASP ALA GLN GLY          
SEQRES   9 B  253  VAL PHE GLN ILE LEU ILE ARG ASN ARG ALA THR ASP LEU          
SEQRES  10 B  253  ASP ALA ARG MET HIS ASP GLY THR THR PRO LEU ILE LEU          
SEQRES  11 B  253  ALA ALA ARG LEU ALA VAL GLU GLY MET LEU GLU ASP LEU          
SEQRES  12 B  253  ILE ASN SER HIS ALA ASP VAL ASN ALA VAL ASP ASP LEU          
SEQRES  13 B  253  GLY LYS SER ALA LEU HIS TRP ALA ALA ALA VAL ASN ASN          
SEQRES  14 B  253  VAL ASP ALA ALA VAL VAL LEU LEU LYS ASN GLY ALA ASN          
SEQRES  15 B  253  LYS ASP MET GLN ASN ASN ARG GLU GLU THR PRO LEU PHE          
SEQRES  16 B  253  LEU ALA ALA ARG GLU GLY SER TYR GLU THR ALA LYS VAL          
SEQRES  17 B  253  LEU LEU ASP HIS PHE ALA ASN ARG ASP ILE THR ASP HIS          
SEQRES  18 B  253  MET ASP ARG LEU PRO ARG ASP ILE ALA GLN GLU ARG MET          
SEQRES  19 B  253  HIS HIS ASP ILE VAL ARG LEU LEU ASP LEU GLU HIS HIS          
SEQRES  20 B  253  HIS HIS HIS HIS HIS HIS                                      
HET    EDO  A 510       4                                                       
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  EDO    C2 H6 O2                                                     
FORMUL   4  HOH   *416(H2 O)                                                    
HELIX    1   1 THR A   59  TYR A   67  1                                   9    
HELIX    2   2 ARG A   69  ALA A   79  1                                  11    
HELIX    3   3 THR A   92  ALA A  100  1                                   9    
HELIX    4   4 ALA A  102  ASN A  112  1                                  11    
HELIX    5   5 THR A  126  ALA A  135  1                                  10    
HELIX    6   6 GLY A  138  SER A  146  1                                   9    
HELIX    7   7 SER A  159  ASN A  168  1                                  10    
HELIX    8   8 ASN A  169  ASN A  179  1                                  11    
HELIX    9   9 THR A  192  GLY A  201  1                                  10    
HELIX   10  10 SER A  202  HIS A  212  1                                  11    
HELIX   11  11 LEU A  225  ARG A  233  1                                   9    
HELIX   12  12 HIS A  235  LEU A  244  1                                  10    
HELIX   13  13 THR B   59  TYR B   67  1                                   9    
HELIX   14  14 ARG B   69  ALA B   79  1                                  11    
HELIX   15  15 THR B   92  ALA B  100  1                                   9    
HELIX   16  16 ALA B  102  ARG B  111  1                                  10    
HELIX   17  17 THR B  126  ALA B  135  1                                  10    
HELIX   18  18 GLY B  138  SER B  146  1                                   9    
HELIX   19  19 SER B  159  ASN B  168  1                                  10    
HELIX   20  20 ASN B  169  ASN B  179  1                                  11    
HELIX   21  21 THR B  192  GLY B  201  1                                  10    
HELIX   22  22 SER B  202  HIS B  212  1                                  11    
HELIX   23  23 LEU B  225  ARG B  233  1                                   9    
HELIX   24  24 HIS B  235  ASP B  243  1                                   9    
CISPEP   1 GLN B   52    THR B   53          0         5.29                     
SITE     1 AC1  7 ARG A 120  MET A 121  HIS A 122  GLY A 124                    
SITE     2 AC1  7 ASP A 155  HOH A 585  HOH A 747                               
CRYST1   96.982   96.982  108.719  90.00  90.00 120.00 P 65         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      0.010311  0.005953  0.000000        0.00000                         
SCALE2      0.000000  0.011906  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009198        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system