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Database: PDB
Entry: 5HPS
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Original site: 5HPS 
HEADER    LIGASE                                  20-JAN-16   5HPS              
TITLE     SYSTEM-WIDE MODULATION OF HECT E3 LIGASES WITH SELECTIVE UBIQUITIN    
TITLE    2 VARIANT PROBES: WWP1 AND UBV P1.1                                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: WWP1 HECT;                                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ATROPHIN-1-INTERACTING PROTEIN 5,AIP5,TGIF-INTERACTING      
COMPND   5 UBIQUITIN LIGASE 1,TIUL1,WW DOMAIN-CONTAINING PROTEIN 1;             
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: UBIQUITIN VARIANT P1.1;                                    
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  13 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  14 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    HECT, E3 LIGASE, UBIQUITIN VARIANT, UBV, LIGASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.-P.WU,P.Y.MERCREDI,B.A.SCHULMAN                                     
REVDAT   6   25-DEC-19 5HPS    1       REMARK                                   
REVDAT   5   27-SEP-17 5HPS    1       JRNL   REMARK                            
REVDAT   4   20-APR-16 5HPS    1       JRNL                                     
REVDAT   3   13-APR-16 5HPS    1       SOURCE                                   
REVDAT   2   23-MAR-16 5HPS    1       JRNL                                     
REVDAT   1   16-MAR-16 5HPS    0                                                
JRNL        AUTH   W.ZHANG,K.P.WU,M.A.SARTORI,H.B.KAMADURAI,A.ORDUREAU,C.JIANG, 
JRNL        AUTH 2 P.Y.MERCREDI,R.MURCHIE,J.HU,A.PERSAUD,M.MUKHERJEE,N.LI,      
JRNL        AUTH 3 A.DOYE,J.R.WALKER,Y.SHENG,Z.HAO,Y.LI,K.R.BROWN,E.LEMICHEZ,   
JRNL        AUTH 4 J.CHEN,Y.TONG,J.W.HARPER,J.MOFFAT,D.ROTIN,B.A.SCHULMAN,      
JRNL        AUTH 5 S.S.SIDHU                                                    
JRNL        TITL   SYSTEM-WIDE MODULATION OF HECT E3 LIGASES WITH SELECTIVE     
JRNL        TITL 2 UBIQUITIN VARIANT PROBES.                                    
JRNL        REF    MOL.CELL                      V.  62   121 2016              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   26949039                                                     
JRNL        DOI    10.1016/J.MOLCEL.2016.02.005                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 103.37                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 34664                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.780                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1658                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1103.5056 -  4.6932    0.97     2822   149  0.1845 0.2258        
REMARK   3     2  4.6932 -  3.7250    0.99     2760   151  0.1783 0.2402        
REMARK   3     3  3.7250 -  3.2541    0.98     2757   136  0.2100 0.2468        
REMARK   3     4  3.2541 -  2.9566    0.99     2763   141  0.2261 0.3023        
REMARK   3     5  2.9566 -  2.7447    0.98     2757   130  0.2334 0.2901        
REMARK   3     6  2.7447 -  2.5828    0.99     2719   140  0.2357 0.3229        
REMARK   3     7  2.5828 -  2.4535    0.99     2778   142  0.2331 0.2945        
REMARK   3     8  2.4535 -  2.3467    0.99     2742   122  0.2234 0.3149        
REMARK   3     9  2.3467 -  2.2563    0.98     2694   136  0.2309 0.2805        
REMARK   3    10  2.2563 -  2.1784    0.99     2777   128  0.2499 0.3193        
REMARK   3    11  2.1784 -  2.1103    0.99     2727   146  0.2458 0.3175        
REMARK   3    12  2.1103 -  2.0500    0.99     2710   137  0.2681 0.3176        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.250            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.110           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009           3815                                  
REMARK   3   ANGLE     :  1.248           5146                                  
REMARK   3   CHIRALITY :  0.052            544                                  
REMARK   3   PLANARITY :  0.005            655                                  
REMARK   3   DIHEDRAL  : 14.852           1423                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5HPS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217392.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-APR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2-7.6                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 34664                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 103.500                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.06150                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1ND7                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.56                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: AMMONIUM SULFATE, GLYCEROL, PEG 3350,    
REMARK 280  PH 7.4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000      103.95700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       22.45400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000      103.95700            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       22.45400            
REMARK 290   SMTRY3   4  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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1650 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21090 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
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     GLY A   535                                                      
REMARK 465     SER A   536                                                      
REMARK 465     GLY A   537                                                      
REMARK 465     GLY A   538                                                      
REMARK 465     PRO A   539                                                      
REMARK 465     GLN A   540                                                      
REMARK 465     GLY A   605                                                      
REMARK 465     LEU A   606                                                      
REMARK 465     ASP A   607                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     LEU B    74                                                      
REMARK 465     ARG B    75                                                      
REMARK 465     LYS B    76                                                      
REMARK 465     SER B    77                                                      
REMARK 465     ARG B    78                                                      
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     LYS A 568    CE   NZ                                             
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1048     O    HOH A  1080              1.93            
REMARK 500   OE2  GLU A   622     O    HOH A  1001              2.05            
REMARK 500   N    ASP A   675     O    HOH A  1002              2.18            
REMARK 500   OH   TYR A   543     OE2  GLU A   915              2.19            
REMARK 500   O    HOH A  1079     O    HOH A  1080              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    SER A 565     -153.50     61.49                                   
REMARK 500    ALA A 634      -72.35    -68.43                                   
REMARK 500    LYS A 636      -93.03     60.58                                   
REMARK 500    ASN A 637      -71.43   -132.16                                   
REMARK 500    ASN A 638        7.63     58.24                                   
REMARK 500    THR A 648       -9.08    -58.46                                   
REMARK 500    ASP A 700       87.60   -159.87                                   
REMARK 500    ASN A 745      115.74   -178.27                                   
REMARK 500    SER A 867       12.19    -69.18                                   
REMARK 500    THR A 916     -158.04   -136.09                                   
REMARK 500    ASN B  60       45.29    -83.33                                   
REMARK 500    GLN B  62     -155.07   -122.28                                   
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 SER A  744     ASN A  745                 -139.79                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HPK   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HPL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5HPT   RELATED DB: PDB                                   
DBREF  5HPS A  537   917  UNP    Q9H0M0   WWP1_HUMAN     537    917             
DBREF  5HPS B   -4    78  PDB    5HPS     5HPS            -4     78             
SEQADV 5HPS GLY A  535  UNP  Q9H0M0              EXPRESSION TAG                 
SEQADV 5HPS SER A  536  UNP  Q9H0M0              EXPRESSION TAG                 
SEQRES   1 A  383  GLY SER GLY GLY PRO GLN ILE ALA TYR GLU ARG GLY PHE          
SEQRES   2 A  383  ARG TRP LYS LEU ALA HIS PHE ARG TYR LEU CYS GLN SER          
SEQRES   3 A  383  ASN ALA LEU PRO SER HIS VAL LYS ILE ASN VAL SER ARG          
SEQRES   4 A  383  GLN THR LEU PHE GLU ASP SER PHE GLN GLN ILE MET ALA          
SEQRES   5 A  383  LEU LYS PRO TYR ASP LEU ARG ARG ARG LEU TYR VAL ILE          
SEQRES   6 A  383  PHE ARG GLY GLU GLU GLY LEU ASP TYR GLY GLY LEU ALA          
SEQRES   7 A  383  ARG GLU TRP PHE PHE LEU LEU SER HIS GLU VAL LEU ASN          
SEQRES   8 A  383  PRO MET TYR CYS LEU PHE GLU TYR ALA GLY LYS ASN ASN          
SEQRES   9 A  383  TYR CYS LEU GLN ILE ASN PRO ALA SER THR ILE ASN PRO          
SEQRES  10 A  383  ASP HIS LEU SER TYR PHE CYS PHE ILE GLY ARG PHE ILE          
SEQRES  11 A  383  ALA MET ALA LEU PHE HIS GLY LYS PHE ILE ASP THR GLY          
SEQRES  12 A  383  PHE SER LEU PRO PHE TYR LYS ARG MET LEU SER LYS LYS          
SEQRES  13 A  383  LEU THR ILE LYS ASP LEU GLU SER ILE ASP THR GLU PHE          
SEQRES  14 A  383  TYR ASN SER LEU ILE TRP ILE ARG ASP ASN ASN ILE GLU          
SEQRES  15 A  383  GLU CYS GLY LEU GLU MET TYR PHE SER VAL ASP MET GLU          
SEQRES  16 A  383  ILE LEU GLY LYS VAL THR SER HIS ASP LEU LYS LEU GLY          
SEQRES  17 A  383  GLY SER ASN ILE LEU VAL THR GLU GLU ASN LYS ASP GLU          
SEQRES  18 A  383  TYR ILE GLY LEU MET THR GLU TRP ARG PHE SER ARG GLY          
SEQRES  19 A  383  VAL GLN GLU GLN THR LYS ALA PHE LEU ASP GLY PHE ASN          
SEQRES  20 A  383  GLU VAL VAL PRO LEU GLN TRP LEU GLN TYR PHE ASP GLU          
SEQRES  21 A  383  LYS GLU LEU GLU VAL MET LEU CYS GLY MET GLN GLU VAL          
SEQRES  22 A  383  ASP LEU ALA ASP TRP GLN ARG ASN THR VAL TYR ARG HIS          
SEQRES  23 A  383  TYR THR ARG ASN SER LYS GLN ILE ILE TRP PHE TRP GLN          
SEQRES  24 A  383  PHE VAL LYS GLU THR ASP ASN GLU VAL ARG MET ARG LEU          
SEQRES  25 A  383  LEU GLN PHE VAL THR GLY THR CYS ARG LEU PRO LEU GLY          
SEQRES  26 A  383  GLY PHE ALA GLU LEU MET GLY SER ASN GLY PRO GLN LYS          
SEQRES  27 A  383  PHE CYS ILE GLU LYS VAL GLY LYS ASP THR TRP LEU PRO          
SEQRES  28 A  383  ARG SER HIS THR CYS PHE ASN ARG LEU ASP LEU PRO PRO          
SEQRES  29 A  383  TYR LYS SER TYR GLU GLN LEU LYS GLU LYS LEU LEU PHE          
SEQRES  30 A  383  ALA ILE GLU GLU THR GLU                                      
SEQRES   1 B   83  GLY SER GLY GLY SER MET HIS ILE PHE VAL LYS THR LEU          
SEQRES   2 B   83  ARG GLY TRP SER ILE THR LEU GLU VAL GLU PRO SER ASP          
SEQRES   3 B   83  THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU          
SEQRES   4 B   83  GLY ILE PRO PRO ASP GLN GLN ILE LEU ILE PHE ALA ARG          
SEQRES   5 B   83  LYS LYS LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN          
SEQRES   6 B   83  ILE GLN GLU LYS SER SER LEU TYR LEU PHE LEU ARG LEU          
SEQRES   7 B   83  LEU ARG LYS SER ARG                                          
FORMUL   3  HOH   *94(H2 O)                                                     
HELIX    1 AA1 GLY A  546  SER A  560  1                                  15    
HELIX    2 AA2 THR A  575  LEU A  587  1                                  13    
HELIX    3 AA3 LYS A  588  ARG A  594  5                                   7    
HELIX    4 AA4 GLY A  610  LEU A  624  1                                  15    
HELIX    5 AA5 ASN A  625  CYS A  629  5                                   5    
HELIX    6 AA6 PRO A  645  ASN A  650  5                                   6    
HELIX    7 AA7 ASP A  652  HIS A  670  1                                  19    
HELIX    8 AA8 SER A  679  LEU A  687  1                                   9    
HELIX    9 AA9 THR A  692  ASP A  700  1                                   9    
HELIX   10 AB1 ASP A  700  ASN A  713  1                                  14    
HELIX   11 AB2 ASN A  714  GLY A  719  1                                   6    
HELIX   12 AB3 GLU A  751  SER A  766  1                                  16    
HELIX   13 AB4 VAL A  769  VAL A  784  1                                  16    
HELIX   14 AB5 PRO A  785  PHE A  792  5                                   8    
HELIX   15 AB6 ASP A  793  GLY A  803  1                                  11    
HELIX   16 AB7 ASP A  808  ASN A  815  1                                   8    
HELIX   17 AB8 SER A  825  THR A  838  1                                  14    
HELIX   18 AB9 ASP A  839  GLY A  852  1                                  14    
HELIX   19 AC1 GLY A  859  GLU A  863  5                                   5    
HELIX   20 AC2 THR A  889  PHE A  891  5                                   3    
HELIX   21 AC3 SER A  901  GLU A  915  1                                  15    
HELIX   22 AC4 THR B   22  GLY B   35  1                                  14    
HELIX   23 AC5 PRO B   37  ASP B   39  5                                   3    
SHEET    1 AA1 2 HIS A 566  VAL A 571  0                                        
SHEET    2 AA1 2 ARG A 595  PHE A 600  1  O  ILE A 599   N  ILE A 569           
SHEET    1 AA2 2 PHE A 631  TYR A 633  0                                        
SHEET    2 AA2 2 LEU A 641  ILE A 643 -1  O  GLN A 642   N  GLU A 632           
SHEET    1 AA3 2 SER A 725  ILE A 730  0                                        
SHEET    2 AA3 2 LYS A 733  ASP A 738 -1  O  LYS A 733   N  ILE A 730           
SHEET    1 AA4 4 VAL A 817  ARG A 819  0                                        
SHEET    2 AA4 4 CYS A 874  GLU A 876  1  O  ILE A 875   N  VAL A 817           
SHEET    3 AA4 4 ARG A 893  ASP A 895  1  O  LEU A 894   N  CYS A 874           
SHEET    4 AA4 4 ARG A 886  HIS A 888 -1  N  ARG A 886   O  ASP A 895           
SHEET    1 AA5 2 MET A 865  GLY A 866  0                                        
SHEET    2 AA5 2 GLY A 869  PRO A 870 -1  O  GLY A 869   N  GLY A 866           
SHEET    1 AA6 5 SER B  12  GLU B  16  0                                        
SHEET    2 AA6 5 HIS B   2  LYS B   6 -1  N  ILE B   3   O  LEU B  15           
SHEET    3 AA6 5 SER B  65  LEU B  71  1  O  LEU B  67   N  LYS B   6           
SHEET    4 AA6 5 GLN B  41  PHE B  45 -1  N  ILE B  42   O  PHE B  70           
SHEET    5 AA6 5 LYS B  48  LYS B  49 -1  O  LYS B  48   N  PHE B  45           
CISPEP   1 GLY A  609    GLY A  610          0        -6.67                     
CISPEP   2 GLU A  750    GLU A  751          0        -1.69                     
CRYST1  207.914   44.908   60.200  90.00  96.07  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004810  0.000000  0.000512        0.00000                         
SCALE2      0.000000  0.022268  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.016705        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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