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Database: PDB
Entry: 1YYH
LinkDB: 1YYH
Original site: 1YYH 
HEADER    CELL CYCLE,TRANSCRIPTION                25-FEB-05   1YYH              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN NOTCH 1 ANKYRIN DOMAIN                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NOTCH 1, ANKYRIN DOMAIN;                                   
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: ANKYRIN DOMAIN;                                            
COMPND   5 SYNONYM: NEUROGENIC LOCUS NOTCH HOMOLOG PROTEIN 1; HN1;              
COMPND   6 TRANSLOCATION-ASSOCIATED NOTCH PROTEIN TAN-1;                        
COMPND   7 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: NOTCH1, TAN1;                                                  
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: PET41                                     
KEYWDS    ANKYRIN REPEATS; NOTCH 1, CELL CYCLE, TRANSCRIPTION                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.T.EHEBAUER,D.Y.CHIRGADZE,P.HAYWARD,A.MARTINEZ-ARIAS,T.L.BLUNDELL    
REVDAT   4   18-JUL-18 1YYH    1       REMARK                                   
REVDAT   3   24-FEB-09 1YYH    1       VERSN                                    
REVDAT   2   13-DEC-05 1YYH    1       JRNL                                     
REVDAT   1   16-AUG-05 1YYH    0                                                
JRNL        AUTH   M.T.EHEBAUER,D.Y.CHIRGADZE,P.HAYWARD,A.MARTINEZ-ARIAS,       
JRNL        AUTH 2 T.L.BLUNDELL                                                 
JRNL        TITL   HIGH-RESOLUTION CRYSTAL STRUCTURE OF THE HUMAN NOTCH 1       
JRNL        TITL 2 ANKYRIN DOMAIN                                               
JRNL        REF    BIOCHEM.J.                    V. 392    13 2005              
JRNL        REFN                   ISSN 0264-6021                               
JRNL        PMID   16011479                                                     
JRNL        DOI    10.1042/BJ20050515                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2                                           
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
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) : 83.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 42631                          
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) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.193                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2261                            
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) : 3138                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 181                          
REMARK   3   BIN FREE R VALUE                    : 0.2760                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2918                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 537                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.72000                                              
REMARK   3    B22 (A**2) : 0.72000                                              
REMARK   3    B33 (A**2) : -1.08000                                             
REMARK   3    B12 (A**2) : 0.36000                                              
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): 0.109         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.107         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.068         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.271         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2984 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4054 ; 1.425 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   380 ; 5.367 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   155 ;29.899 ;24.194       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   499 ;12.908 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    30 ;14.885 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   479 ; 0.112 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2292 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1520 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2091 ; 0.295 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   358 ; 0.197 ; 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):    40 ; 0.120 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    32 ; 0.195 ; 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):  1974 ; 2.888 ; 5.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3040 ; 3.487 ; 6.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1112 ; 4.011 ; 5.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1014 ; 5.779 ; 7.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 1YYH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-05.                  
REMARK 100 THE DEPOSITION ID IS D_1000032071.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SRS                                
REMARK 200  BEAMLINE                       : PX14.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.488                              
REMARK 200  MONOCHROMATOR                  : DARESBURY                          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44926                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 83.920                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 3.600                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : 0.07900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.4000                            
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     (%) : 98.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.38500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 12.40                              
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 1OT8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.70                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM HYDROGEN PHOSPHATE, SODIUM      
REMARK 280  CHLORIDE, IMIDAZOLE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 298.0K                                                  
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       72.66400            
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       36.33200            
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       54.49800            
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       18.16600            
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       90.83000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     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     HIS A    50                                                      
REMARK 465     ASN A    51                                                      
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     GLN B    52                                                      
REMARK 465     THR B    53                                                      
REMARK 465     ASP B    54                                                      
REMARK 465     LEU B   244                                                      
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     GLN A  52    CG   CD   OE1  NE2                                  
REMARK 470     THR A  53    OG1  CG2                                            
REMARK 470     ARG A  55    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A  69    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B  55    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 178    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   NE2  GLN B   103     O    HOH B   482              1.47            
REMARK 500   NH2  ARG B    75     O    HOH B   464              2.02            
REMARK 500   O    HOH B   289     O    HOH B   476              2.03            
REMARK 500   O    HOH A   435     O    HOH A   535              2.05            
REMARK 500   OE1  GLN A   103     O    HOH A   450              2.08            
REMARK 500   NH1  ARG B    75     O    HOH B   463              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   381     O    HOH B   504     2654     2.11            
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    ASP B 237   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 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    ASP A  54     -157.98    -90.41                                   
REMARK 500    ASP A  87     -169.90    -77.19                                   
REMARK 500    HIS A 147       25.34     80.84                                   
REMARK 500    HIS B 147       24.21     83.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1YYH A    1   243  UNP    P46531   NOTC1_HUMAN   1873   2115             
DBREF  1YYH B    1   243  UNP    P46531   NOTC1_HUMAN   1873   2115             
SEQADV 1YYH LEU A  244  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH GLU A  245  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS A  246  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS A  247  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS A  248  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS A  249  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS A  250  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS A  251  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS A  252  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS A  253  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH LEU B  244  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH GLU B  245  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS B  246  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS B  247  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS B  248  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS B  249  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS B  250  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS B  251  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH HIS B  252  UNP  P46531              EXPRESSION TAG                 
SEQADV 1YYH 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 GLU THR ALA LEU HIS LEU ALA ALA          
SEQRES   6 A  253  ARG 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 GLU THR ALA LEU HIS LEU ALA ALA          
SEQRES   6 B  253  ARG 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                                      
FORMUL   3  HOH   *537(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  ASP A  101  1                                  10    
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  ASP B  101  1                                  10    
HELIX   16  16 ALA B  102  ASN B  112  1                                  11    
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    
CRYST1   96.840   96.840  108.996  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      0.010326  0.005962  0.000000        0.00000                         
SCALE2      0.000000  0.011924  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009175        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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