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Database: PDB
Entry: 1ND7
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Original site: 1ND7 
HEADER    LIGASE                                  08-DEC-02   1ND7              
TITLE     CONFORMATIONAL FLEXIBILITY UNDERLIES UBIQUITIN LIGATION               
TITLE    2 MEDIATED BY THE WWP1 HECT DOMAIN E3 LIGASE                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: WW DOMAIN-CONTAINING PROTEIN 1;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: WWP1 HECT DOMAIN;                                          
COMPND   5 SYNONYM: WWP1 HECT DOMAIN, SUPPRESSOR OF DELTEX RELATED              
COMPND   6 PROTEIN 1,  NEDD-4-LIKE UBIQUITIN-PROTEIN LIGASE, ATROPHIN-          
COMPND   7 1 INTERACTING PROTEIN 5;                                             
COMPND   8 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: WWP1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);                                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A(+)                                 
KEYWDS    HECT, UBIQUITIN, LIGASE, E3, WWP1                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.A.VERDECIA,C.A.P.JOAZIERO,N.J.WELLS,J.-L.FERRER,                    
AUTHOR   2 M.E.BOWMAN,T.HUNTER,J.P.NOEL                                         
REVDAT   2   24-FEB-09 1ND7    1       VERSN                                    
REVDAT   1   23-SEP-03 1ND7    0                                                
JRNL        AUTH   M.A.VERDECIA,C.A.P.JOAZIERO,N.J.WELLS,J.-L.FERRER,           
JRNL        AUTH 2 M.E.BOWMAN,T.HUNTER,J.P.NOEL                                 
JRNL        TITL   CONFORMATIONAL FLEXIBILITY UNDERLIES UBIQUITIN               
JRNL        TITL 2 LIGATION MEDIATED BY THE WWP1 HECT DOMAIN E3 LIGASE          
JRNL        REF    MOL.CELL                      V.  11   249 2003              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   12535537                                                     
JRNL        DOI    10.1016/S1097-2765(02)00774-8                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 32.08                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 770820.650                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 94.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 21708                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE            (WORKING SET) : 0.243                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1249                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.23                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 76.80                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3231                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2840                       
REMARK   3   BIN FREE R VALUE                    : 0.2830                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.60                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 156                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.023                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3118                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 26.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 43.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.72000                                             
REMARK   3    B22 (A**2) : -3.44000                                             
REMARK   3    B33 (A**2) : 9.16000                                              
REMARK   3    B12 (A**2) : -2.37000                                             
REMARK   3    B13 (A**2) : 4.83000                                              
REMARK   3    B23 (A**2) : 2.70000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.30                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.23                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.26                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.016                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.90                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 1.43                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.580 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.720 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.820 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.850 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 34.83                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER_REP.TOP                                  
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1ND7 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-02.                  
REMARK 100 THE RCSB ID CODE IS RCSB017777.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979, 0.980, 0.972                
REMARK 200  MONOCHROMATOR                  : YALE MIRRORS                       
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21708                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.080                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.95                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM ACETATE, BETA-                  
REMARK 280  MERCAPTOETHANOL, PH 5.5, VAPOR DIFFUSION, HANGING DROP,             
REMARK 280  TEMPERATURE 277.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
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: 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 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    TYR A   608     N    GLY A   610              1.41            
REMARK 500   OG1  THR A   749     ND2  ASN A   752              1.78            
REMARK 500   CE   MET A   728     CG2  THR A   735              1.85            
REMARK 500   O    LYS A   636     N    ASN A   638              1.87            
REMARK 500   N    THR A   749     OD1  ASN A   752              1.97            
REMARK 500   OD1  ASN A   570     CD   ARG A   601              2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ASN A 637   N     ASN A 637   CA     -0.130                       
REMARK 500    MET A 728   N     MET A 728   CA      0.140                       
REMARK 500    GLU A 729   N     GLU A 729   CA      0.148                       
REMARK 500    VAL A 734   CA    VAL A 734   CB      0.129                       
REMARK 500    THR A 916   N     THR A 916   CA      0.123                       
REMARK 500    THR A 916   CA    THR A 916   CB      0.199                       
REMARK 500    THR A 916   CA    THR A 916   C       0.253                       
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    ARG A 601   NE  -  CZ  -  NH2 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    GLY A 602   CA  -  C   -  N   ANGL. DEV. = -20.6 DEGREES          
REMARK 500    GLY A 602   O   -  C   -  N   ANGL. DEV. =  22.7 DEGREES          
REMARK 500    ARG A 613   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    LYS A 636   CB  -  CA  -  C   ANGL. DEV. = -13.2 DEGREES          
REMARK 500    LYS A 636   CA  -  C   -  N   ANGL. DEV. = -19.5 DEGREES          
REMARK 500    LYS A 636   O   -  C   -  N   ANGL. DEV. =  17.9 DEGREES          
REMARK 500    TYR A 639   N   -  CA  -  C   ANGL. DEV. =  23.0 DEGREES          
REMARK 500    CYS A 640   C   -  N   -  CA  ANGL. DEV. = -15.2 DEGREES          
REMARK 500    LEU A 641   C   -  N   -  CA  ANGL. DEV. = -15.1 DEGREES          
REMARK 500    GLU A 717   CB  -  CA  -  C   ANGL. DEV. =  20.6 DEGREES          
REMARK 500    GLU A 716   CA  -  C   -  N   ANGL. DEV. = -18.8 DEGREES          
REMARK 500    GLU A 716   O   -  C   -  N   ANGL. DEV. =  18.4 DEGREES          
REMARK 500    ASP A 727   CB  -  CA  -  C   ANGL. DEV. =  24.0 DEGREES          
REMARK 500    ASP A 727   N   -  CA  -  CB  ANGL. DEV. = -12.8 DEGREES          
REMARK 500    VAL A 726   O   -  C   -  N   ANGL. DEV. =  11.7 DEGREES          
REMARK 500    MET A 728   CG  -  SD  -  CE  ANGL. DEV. =   9.7 DEGREES          
REMARK 500    ASP A 727   O   -  C   -  N   ANGL. DEV. =  12.4 DEGREES          
REMARK 500    MET A 728   C   -  N   -  CA  ANGL. DEV. =  20.2 DEGREES          
REMARK 500    THR A 916   N   -  CA  -  C   ANGL. DEV. =  20.5 DEGREES          
REMARK 500    THR A 916   CA  -  C   -  O   ANGL. DEV. = -13.7 DEGREES          
REMARK 500    GLU A 917   N   -  CA  -  CB  ANGL. DEV. =  21.1 DEGREES          
REMARK 500    THR A 916   CA  -  C   -  N   ANGL. DEV. = -13.4 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    MET A 545      -99.18   -135.41                                   
REMARK 500    SER A 565     -156.68     63.00                                   
REMARK 500    THR A 575        8.94   -170.73                                   
REMARK 500    GLU A 603       62.22     -2.35                                   
REMARK 500    GLU A 604     -126.90    -82.88                                   
REMARK 500    LEU A 606      -72.60   -107.12                                   
REMARK 500    TYR A 608      118.89    154.38                                   
REMARK 500    ALA A 634     -118.50    -69.09                                   
REMARK 500    LYS A 636     -159.88     77.07                                   
REMARK 500    ASN A 637       49.79    -32.91                                   
REMARK 500    ASN A 638     -125.62   -128.34                                   
REMARK 500    TYR A 639       -3.88   -155.69                                   
REMARK 500    ARG A 711      -98.71    -65.37                                   
REMARK 500    ASP A 712       74.25    -66.54                                   
REMARK 500    ASN A 713      140.04    170.03                                   
REMARK 500    ILE A 715       86.58    -36.19                                   
REMARK 500    GLU A 716      157.80    157.47                                   
REMARK 500    GLU A 717       -7.93     90.53                                   
REMARK 500    CYS A 718       49.76   -146.40                                   
REMARK 500    LEU A 720     -115.25   -152.11                                   
REMARK 500    ASP A 727       69.19   -104.70                                   
REMARK 500    MET A 728     -127.27     -9.21                                   
REMARK 500    GLU A 729     -171.23   -176.12                                   
REMARK 500    ILE A 730       81.76     18.25                                   
REMARK 500    LEU A 731      138.62    163.22                                   
REMARK 500    LYS A 733      -24.67   -143.15                                   
REMARK 500    GLU A 750       35.14    -81.38                                   
REMARK 500    GLU A 751      -35.98   -144.38                                   
REMARK 500    LYS A 753      -24.51    -28.85                                   
REMARK 500    GLU A 914      -60.33    -96.68                                   
REMARK 500    GLU A 915       25.12    -68.33                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A  916     GLU A  917                  110.46                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION, C(I) - CA(I) - N(I+1) - O(I), GREATER                       
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    THR A 916         29.48                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1ND7 A  546   917  UNP    Q9H0M0   WWP1_HUMAN     546    918             
SEQADV 1ND7 HIS A  544  UNP  Q9H0M0              EXPRESSION TAG                 
SEQADV 1ND7 MET A  545  UNP  Q9H0M0              INITIATOR METHIONINE           
SEQRES   1 A  374  HIS MET GLY PHE ARG TRP LYS LEU ALA HIS PHE ARG TYR          
SEQRES   2 A  374  LEU CYS GLN SER ASN ALA LEU PRO SER HIS VAL LYS ILE          
SEQRES   3 A  374  ASN VAL SER ARG GLN THR LEU PHE GLU ASP SER PHE GLN          
SEQRES   4 A  374  GLN ILE MET ALA LEU LYS PRO TYR ASP LEU ARG ARG ARG          
SEQRES   5 A  374  LEU TYR VAL ILE PHE ARG GLY GLU GLU GLY LEU ASP TYR          
SEQRES   6 A  374  GLY GLY LEU ALA ARG GLU TRP PHE PHE LEU LEU SER HIS          
SEQRES   7 A  374  GLU VAL LEU ASN PRO MET TYR CYS LEU PHE GLU TYR ALA          
SEQRES   8 A  374  GLY LYS ASN ASN TYR CYS LEU GLN ILE ASN PRO ALA SER          
SEQRES   9 A  374  THR ILE ASN PRO ASP HIS LEU SER TYR PHE CYS PHE ILE          
SEQRES  10 A  374  GLY ARG PHE ILE ALA MET ALA LEU PHE HIS GLY LYS PHE          
SEQRES  11 A  374  ILE ASP THR GLY PHE SER LEU PRO PHE TYR LYS ARG MET          
SEQRES  12 A  374  LEU SER LYS LYS LEU THR ILE LYS ASP LEU GLU SER ILE          
SEQRES  13 A  374  ASP THR GLU PHE TYR ASN SER LEU ILE TRP ILE ARG ASP          
SEQRES  14 A  374  ASN ASN ILE GLU GLU CYS GLY LEU GLU MET TYR PHE SER          
SEQRES  15 A  374  VAL ASP MET GLU ILE LEU GLY LYS VAL THR SER HIS ASP          
SEQRES  16 A  374  LEU LYS LEU GLY GLY SER ASN ILE LEU VAL THR GLU GLU          
SEQRES  17 A  374  ASN LYS ASP GLU TYR ILE GLY LEU MET THR GLU TRP ARG          
SEQRES  18 A  374  PHE SER ARG GLY VAL GLN GLU GLN THR LYS ALA PHE LEU          
SEQRES  19 A  374  ASP GLY PHE ASN GLU VAL VAL PRO LEU GLN TRP LEU GLN          
SEQRES  20 A  374  TYR PHE ASP GLU LYS GLU LEU GLU VAL MET LEU CYS GLY          
SEQRES  21 A  374  MET GLN GLU VAL ASP LEU ALA ASP TRP GLN ARG ASN THR          
SEQRES  22 A  374  VAL TYR ARG HIS TYR THR ARG ASN SER LYS GLN ILE ILE          
SEQRES  23 A  374  TRP PHE TRP GLN PHE VAL LYS GLU THR ASP ASN GLU VAL          
SEQRES  24 A  374  ARG MET ARG LEU LEU GLN PHE VAL THR GLY THR CYS ARG          
SEQRES  25 A  374  LEU PRO LEU GLY GLY PHE ALA GLU LEU MET GLY SER ASN          
SEQRES  26 A  374  GLY PRO GLN LYS PHE CYS ILE GLU LYS VAL GLY LYS ASP          
SEQRES  27 A  374  THR TRP LEU PRO ARG SER HIS THR CYS PHE ASN ARG LEU          
SEQRES  28 A  374  ASP LEU PRO PRO TYR LYS SER TYR GLU GLN LEU LYS GLU          
SEQRES  29 A  374  LYS LEU LEU PHE ALA ILE GLU GLU THR GLU                      
HELIX    1   1 GLY A  546  ASN A  561  1                                  16    
HELIX    2   2 THR A  575  ALA A  586  1                                  12    
HELIX    3   3 LYS A  588  ARG A  594  5                                   7    
HELIX    4   4 GLY A  609  LEU A  624  1                                  16    
HELIX    5   5 ASN A  625  CYS A  629  5                                   5    
HELIX    6   6 PRO A  645  ASN A  650  5                                   6    
HELIX    7   7 ASP A  652  HIS A  670  1                                  19    
HELIX    8   8 SER A  679  LEU A  687  1                                   9    
HELIX    9   9 THR A  692  SER A  698  1                                   7    
HELIX   10  10 ASP A  700  ASP A  712  1                                  13    
HELIX   11  11 GLY A  742  ILE A  746  5                                   5    
HELIX   12  12 ASN A  752  ARG A  767  1                                  16    
HELIX   13  13 VAL A  769  VAL A  784  1                                  16    
HELIX   14  14 PRO A  785  GLN A  790  5                                   6    
HELIX   15  15 ASP A  793  GLY A  803  1                                  11    
HELIX   16  16 ASP A  808  ASN A  815  1                                   8    
HELIX   17  17 SER A  825  THR A  838  1                                  14    
HELIX   18  18 ASP A  839  GLY A  852  1                                  14    
HELIX   19  19 GLY A  860  GLU A  863  5                                   4    
HELIX   20  20 THR A  889  PHE A  891  5                                   3    
HELIX   21  21 SER A  901  GLU A  915  1                                  15    
SHEET    1   A 2 HIS A 566  VAL A 571  0                                        
SHEET    2   A 2 ARG A 595  PHE A 600  1  O  ARG A 595   N  VAL A 567           
SHEET    1   B 2 PHE A 631  TYR A 633  0                                        
SHEET    2   B 2 LEU A 641  ILE A 643 -1  O  GLN A 642   N  GLU A 632           
SHEET    1   C 2 SER A 725  VAL A 726  0                                        
SHEET    2   C 2 HIS A 737  ASP A 738 -1  O  HIS A 737   N  VAL A 726           
SHEET    1   D 4 THR A 816  ARG A 819  0                                        
SHEET    2   D 4 PHE A 873  GLU A 876  1  O  PHE A 873   N  VAL A 817           
SHEET    3   D 4 ARG A 893  ASP A 895  1  O  LEU A 894   N  CYS A 874           
SHEET    4   D 4 ARG A 886  HIS A 888 -1  N  ARG A 886   O  ASP A 895           
SHEET    1   E 2 MET A 865  GLY A 866  0                                        
SHEET    2   E 2 GLY A 869  PRO A 870 -1  O  GLY A 869   N  GLY A 866           
CRYST1   45.200   50.850   58.430 113.47  99.21 102.26 P 1           1          
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      0.022124  0.004808  0.006423        0.00000                         
SCALE2      0.000000  0.020125  0.010088        0.00000                         
SCALE3      0.000000  0.000000  0.019394        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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