GenomeNet

Database: PDB
Entry: 5HPT
LinkDB: 5HPT
Original site: 5HPT 
HEADER    LIGASE/TRANSFERASE                      20-JAN-16   5HPT              
TITLE     SYSTEM-WIDE MODULATION OF HECT E3 LIGASES WITH SELECTIVE UBIQUITIN    
TITLE    2 VARIANT PROBES: WWP1, UBV P2.3 AND UBCH7                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: NEDD4-LIKE E3 UBIQUITIN-PROTEIN LIGASE WWP1;               
COMPND   3 CHAIN: A, D, G;                                                      
COMPND   4 FRAGMENT: HECT DOMAIN (UNP RESIDUES 537-917);                        
COMPND   5 SYNONYM: ATROPHIN-1-INTERACTING PROTEIN 5,AIP5,TGIF-INTERACTING      
COMPND   6 UBIQUITIN LIGASE 1,TIUL1,WW DOMAIN-CONTAINING PROTEIN 1;             
COMPND   7 EC: 6.3.2.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: UBIQUITIN VARIANT P2.3;                                    
COMPND  11 CHAIN: B, E, H;                                                      
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 L3;                        
COMPND  15 CHAIN: C, F;                                                         
COMPND  16 SYNONYM: E2 UBIQUITIN-CONJUGATING ENZYME L3,L-UBC,UBCH7,UBIQUITIN    
COMPND  17 CARRIER PROTEIN L3,UBIQUITIN-CONJUGATING ENZYME E2-F1,UBIQUITIN-     
COMPND  18 PROTEIN LIGASE L3;                                                   
COMPND  19 EC: 2.3.2.23;                                                        
COMPND  20 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;                                 
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: PGEX;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  17 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  18 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  19 EXPRESSION_SYSTEM_PLASMID: PGEX;                                     
SOURCE  20 MOL_ID: 3;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  22 ORGANISM_COMMON: HUMAN;                                              
SOURCE  23 ORGANISM_TAXID: 9606;                                                
SOURCE  24 GENE: UBE2L3, UBCE7, UBCH7;                                          
SOURCE  25 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  27 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  29 EXPRESSION_SYSTEM_PLASMID: PGEX                                      
KEYWDS    HECT E3, WWP1, UBIQUITIN, UBV, UBCH7, LIGASE-TRANSFERASE COMPLEX      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.-P.WU,B.A.SCHULMAN                                                  
REVDAT   5   25-DEC-19 5HPT    1       REMARK                                   
REVDAT   4   27-SEP-17 5HPT    1       JRNL   REMARK                            
REVDAT   3   20-APR-16 5HPT    1       JRNL                                     
REVDAT   2   23-MAR-16 5HPT    1       JRNL                                     
REVDAT   1   16-MAR-16 5HPT    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.    2.84 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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.15                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 97828                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.218                           
REMARK   3   FREE R VALUE                     : 0.237                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3811                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 95.1998 -  8.5181    0.99     3456   148  0.1784 0.1772        
REMARK   3     2  8.5181 -  6.7616    0.99     3477   132  0.2080 0.2305        
REMARK   3     3  6.7616 -  5.9071    1.00     3495   128  0.2111 0.2330        
REMARK   3     4  5.9071 -  5.3670    1.00     3493   156  0.2100 0.2139        
REMARK   3     5  5.3670 -  4.9824    0.99     3439   137  0.1870 0.1951        
REMARK   3     6  4.9824 -  4.6886    1.00     3505   139  0.1799 0.2053        
REMARK   3     7  4.6886 -  4.4538    1.00     3483   145  0.1794 0.2224        
REMARK   3     8  4.4538 -  4.2600    1.00     3470   137  0.1881 0.2205        
REMARK   3     9  4.2600 -  4.0960    0.99     3499   140  0.1955 0.2243        
REMARK   3    10  4.0960 -  3.9546    0.99     3452   133  0.2058 0.2790        
REMARK   3    11  3.9546 -  3.8310    0.99     3450   151  0.2190 0.1992        
REMARK   3    12  3.8310 -  3.7214    1.00     3535   145  0.2157 0.2178        
REMARK   3    13  3.7214 -  3.6235    1.00     3442   148  0.2156 0.2430        
REMARK   3    14  3.6235 -  3.5351    1.00     3522   140  0.2302 0.2202        
REMARK   3    15  3.5351 -  3.4547    1.00     3485   139  0.2370 0.2296        
REMARK   3    16  3.4547 -  3.3812    1.00     3487   152  0.2508 0.2999        
REMARK   3    17  3.3812 -  3.3135    0.99     3481   127  0.2556 0.2828        
REMARK   3    18  3.3135 -  3.2510    0.98     3410   148  0.2634 0.2452        
REMARK   3    19  3.2510 -  3.1929    1.00     3564   129  0.2872 0.3395        
REMARK   3    20  3.1929 -  3.1388    1.00     3424   164  0.3057 0.3578        
REMARK   3    21  3.1388 -  3.0882    1.00     3512   137  0.3181 0.3665        
REMARK   3    22  3.0882 -  3.0407    1.00     3509   121  0.3037 0.3254        
REMARK   3    23  3.0407 -  2.9959    1.00     3458   143  0.3179 0.3235        
REMARK   3    24  2.9959 -  2.9537    1.00     3535   143  0.3103 0.3122        
REMARK   3    25  2.9537 -  2.9138    1.00     3497   128  0.3193 0.3921        
REMARK   3    26  2.9138 -  2.8760    1.00     3491   144  0.3300 0.3026        
REMARK   3    27  2.8760 -  2.8400    0.99     3446   157  0.3563 0.3728        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.240           
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      :  0.011          13850                                  
REMARK   3   ANGLE     :  1.612          18686                                  
REMARK   3   CHIRALITY :  0.067           1983                                  
REMARK   3   PLANARITY :  0.007           2394                                  
REMARK   3   DIHEDRAL  : 16.724           5228                                  
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 5HPT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217394.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-MAR-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.0-5.2                            
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-E                            
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 97828                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.150                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.7000                            
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: 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   (%): 55.54                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.77                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ISOPROPANOL 10%, PEG3350 8%, SODIUM      
REMARK 280  CITRATE 0.1 M, PH 5.2, VAPOR DIFFUSION, HANGING DROP,               
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
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       57.00250            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       79.33150            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       59.44850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       79.33150            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       57.00250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       59.44850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28740 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3780 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -23.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, E, F                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -17.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     ILE A   541                                                      
REMARK 465     ALA A   542                                                      
REMARK 465     TYR A   543                                                      
REMARK 465     GLU A   544                                                      
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     ARG B    77                                                      
REMARK 465     ILE B    78                                                      
REMARK 465     VAL C   153                                                      
REMARK 465     ASP C   154                                                      
REMARK 465     GLY C   155                                                      
REMARK 465     GLY C   156                                                      
REMARK 465     HIS C   157                                                      
REMARK 465     HIS C   158                                                      
REMARK 465     HIS C   159                                                      
REMARK 465     HIS C   160                                                      
REMARK 465     HIS C   161                                                      
REMARK 465     HIS C   162                                                      
REMARK 465     GLY D   535                                                      
REMARK 465     SER D   536                                                      
REMARK 465     GLY D   537                                                      
REMARK 465     GLY D   538                                                      
REMARK 465     PRO D   539                                                      
REMARK 465     GLN D   540                                                      
REMARK 465     ILE D   541                                                      
REMARK 465     ALA D   542                                                      
REMARK 465     TYR D   543                                                      
REMARK 465     GLU D   544                                                      
REMARK 465     GLN D   805                                                      
REMARK 465     TYR D   821                                                      
REMARK 465     GLY E    -4                                                      
REMARK 465     SER E    -3                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     GLY E    -1                                                      
REMARK 465     SER E     0                                                      
REMARK 465     ARG E    77                                                      
REMARK 465     ILE E    78                                                      
REMARK 465     PRO F   152                                                      
REMARK 465     VAL F   153                                                      
REMARK 465     ASP F   154                                                      
REMARK 465     GLY F   155                                                      
REMARK 465     GLY F   156                                                      
REMARK 465     HIS F   157                                                      
REMARK 465     HIS F   158                                                      
REMARK 465     HIS F   159                                                      
REMARK 465     HIS F   160                                                      
REMARK 465     HIS F   161                                                      
REMARK 465     HIS F   162                                                      
REMARK 465     GLY G   535                                                      
REMARK 465     SER G   536                                                      
REMARK 465     GLY G   537                                                      
REMARK 465     GLY G   538                                                      
REMARK 465     PRO G   539                                                      
REMARK 465     GLN G   540                                                      
REMARK 465     ILE G   541                                                      
REMARK 465     ALA G   542                                                      
REMARK 465     TYR G   543                                                      
REMARK 465     GLU G   544                                                      
REMARK 465     ARG G   545                                                      
REMARK 465     LEU G   606                                                      
REMARK 465     ASP G   607                                                      
REMARK 465     GLY G   610                                                      
REMARK 465     HIS G   820                                                      
REMARK 465     TYR G   821                                                      
REMARK 465     GLY H    -4                                                      
REMARK 465     SER H    -3                                                      
REMARK 465     GLY H    -2                                                      
REMARK 465     GLY H    -1                                                      
REMARK 465     SER H     0                                                      
REMARK 465     GLN H    76                                                      
REMARK 465     ARG H    77                                                      
REMARK 465     ILE H    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     GLU D 903    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 906    CG   CD   CE   NZ                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN H     2     O    MSE H    63              1.49            
REMARK 500   OD1  ASP D   591     NH1  ARG D   594              1.97            
REMARK 500   O    GLU C    13     SG   CYS C    17              2.02            
REMARK 500   O    THR G   822     CB   SER G   825              2.02            
REMARK 500   NE   ARG A   573     OE2  GLU A   603              2.05            
REMARK 500   O    GLY D   879     OG1  THR D   882              2.08            
REMARK 500   O    ARG C   122     O    ASP C   124              2.09            
REMARK 500   NE2  GLN D   813     CE2  TRP D   832              2.10            
REMARK 500   OH   TYR C    46     O    TYR C    75              2.10            
REMARK 500   NE2  GLN D   813     CE3  TRP D   832              2.11            
REMARK 500   NE2  GLN D   813     CG   TRP D   832              2.13            
REMARK 500   O    MET D   865     ND2  ASN D   892              2.17            
REMARK 500   OE1  GLN D   833     OH   TYR D   902              2.19            
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    LYS C   146     NZ   LYS G   568     4445     1.99            
REMARK 500   OH   TYR D   608     NZ   LYS G   908     4455     2.00            
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    GLU D 717   CB    GLU D 717   CG      0.116                       
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    TYR A 608   CA  -  CB  -  CG  ANGL. DEV. =  11.7 DEGREES          
REMARK 500    PRO B  74   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    ASP C 124   CB  -  CA  -  C   ANGL. DEV. = -15.0 DEGREES          
REMARK 500    ASP C 124   N   -  CA  -  C   ANGL. DEV. = -23.6 DEGREES          
REMARK 500    PRO D 651   C   -  N   -  CA  ANGL. DEV. =   9.3 DEGREES          
REMARK 500    MSE E  63   N   -  CA  -  C   ANGL. DEV. =  16.6 DEGREES          
REMARK 500    GLY E  64   N   -  CA  -  C   ANGL. DEV. = -22.5 DEGREES          
REMARK 500    LYS F  16   CA  -  C   -  N   ANGL. DEV. = -14.2 DEGREES          
REMARK 500    CYS F  17   CA  -  C   -  N   ANGL. DEV. = -28.4 DEGREES          
REMARK 500    CYS F  17   O   -  C   -  N   ANGL. DEV. =  22.4 DEGREES          
REMARK 500    GLY F  18   C   -  N   -  CA  ANGL. DEV. = -27.0 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    PRO A 564     -166.83    -77.86                                   
REMARK 500    SER A 565     -154.91     56.63                                   
REMARK 500    LEU A 611     -128.72   -135.51                                   
REMARK 500    VAL A 769       19.10   -142.97                                   
REMARK 500    LYS A 880     -166.43     53.13                                   
REMARK 500    ASP A 881       14.95   -158.88                                   
REMARK 500    ALA C   3     -148.73     47.51                                   
REMARK 500    GLU C  13       22.44    -77.50                                   
REMARK 500    MET C  19       67.52     29.88                                   
REMARK 500    LEU C  32       49.81    -72.70                                   
REMARK 500    PRO C  45       46.28    -91.34                                   
REMARK 500    LYS C  48       30.61    -96.95                                   
REMARK 500    PRO C  62       32.18    -93.37                                   
REMARK 500    PRO C 115      171.42    -57.91                                   
REMARK 500    LEU C 125      -61.79     87.95                                   
REMARK 500    SER D 565     -142.87     65.43                                   
REMARK 500    TYR D 639       66.63   -112.18                                   
REMARK 500    THR D 676      135.51     80.37                                   
REMARK 500    THR D 749     -143.26   -119.69                                   
REMARK 500    ARG D 823     -142.97     58.38                                   
REMARK 500    THR D 838     -168.06    -75.09                                   
REMARK 500    ASP D 839     -157.10    -81.45                                   
REMARK 500    PRO D 857      107.47    -57.63                                   
REMARK 500    GLU D 876      -72.11   -147.22                                   
REMARK 500    VAL D 878     -149.96     64.28                                   
REMARK 500    LEU D 910       20.50    -79.89                                   
REMARK 500    ALA E  46       49.76     39.64                                   
REMARK 500    LYS E  62     -136.88     39.87                                   
REMARK 500    MSE E  63      -82.04   -103.39                                   
REMARK 500    ALA F   3       -0.36   -159.14                                   
REMARK 500    ASN F  31       -9.53   -157.19                                   
REMARK 500    PRO F  45       33.12    -89.50                                   
REMARK 500    ASP F 132       70.96     56.21                                   
REMARK 500    SER G 565     -149.12     64.85                                   
REMARK 500    ILE G 715       57.09    -91.94                                   
REMARK 500    CYS G 718       19.08     59.12                                   
REMARK 500    LEU G 720       79.53     78.28                                   
REMARK 500    PHE G 724       35.79    -74.37                                   
REMARK 500    LEU G 741     -118.70     40.29                                   
REMARK 500    THR G 749     -148.02   -105.08                                   
REMARK 500    ASN G 824       66.68     29.03                                   
REMARK 500    ASP G 839      156.68    -49.33                                   
REMARK 500    PRO G 898       86.92    -64.82                                   
REMARK 500    LYS G 900     -157.12    -75.02                                   
REMARK 500    GLU G 903       -1.86    -56.27                                   
REMARK 500    THR G 916       36.78    -93.24                                   
REMARK 500    VAL H  17     -160.54   -128.29                                   
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 GLU A  603     GLU A  604                 -139.94                    
REMARK 500 ALA A  612     ARG A  613                  139.53                    
REMARK 500 ARG C  151     PRO C  152                  -36.17                    
REMARK 500 ASN D  714     ILE D  715                 -146.08                    
REMARK 500 GLU D  876     LYS D  877                 -147.66                    
REMARK 500 SER G  901     TYR G  902                 -146.73                    
REMARK 500 LYS H   62     MSE H   63                 -140.96                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    LYS F  16        -18.80                                           
REMARK 500    CYS F  17         10.77                                           
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: 5HPS   RELATED DB: PDB                                   
DBREF  5HPT A  537   917  UNP    Q9H0M0   WWP1_HUMAN     537    917             
DBREF  5HPT B   -4    78  PDB    5HPT     5HPT            -4     78             
DBREF  5HPT C    2   154  UNP    P68036   UB2L3_HUMAN      2    154             
DBREF  5HPT D  537   917  UNP    Q9H0M0   WWP1_HUMAN     537    917             
DBREF  5HPT E   -4    78  PDB    5HPT     5HPT            -4     78             
DBREF  5HPT F    2   154  UNP    P68036   UB2L3_HUMAN      2    154             
DBREF  5HPT G  537   917  UNP    Q9H0M0   WWP1_HUMAN     537    917             
DBREF  5HPT H   -4    78  PDB    5HPT     5HPT            -4     78             
SEQADV 5HPT GLY A  535  UNP  Q9H0M0              EXPRESSION TAG                 
SEQADV 5HPT SER A  536  UNP  Q9H0M0              EXPRESSION TAG                 
SEQADV 5HPT GLY C  155  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT GLY C  156  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS C  157  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS C  158  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS C  159  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS C  160  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS C  161  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS C  162  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT GLY D  535  UNP  Q9H0M0              EXPRESSION TAG                 
SEQADV 5HPT SER D  536  UNP  Q9H0M0              EXPRESSION TAG                 
SEQADV 5HPT GLY F  155  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT GLY F  156  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS F  157  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS F  158  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS F  159  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS F  160  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS F  161  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT HIS F  162  UNP  P68036              EXPRESSION TAG                 
SEQADV 5HPT GLY G  535  UNP  Q9H0M0              EXPRESSION TAG                 
SEQADV 5HPT SER G  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 MSE GLN ILE LEU VAL LYS THR PHE          
SEQRES   2 B   83  THR TRP LYS THR 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 ARG LEU ILE PHE ALA GLY          
SEQRES   5 B   83  LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN          
SEQRES   6 B   83  ILE LYS MSE GLY SER SER LEU TYR LEU VAL LEU ARG LEU          
SEQRES   7 B   83  PRO GLY GLN ARG ILE                                          
SEQRES   1 C  161  ALA ALA SER ARG ARG LEU MET LYS GLU LEU GLU GLU ILE          
SEQRES   2 C  161  ARG LYS CYS GLY MET LYS ASN PHE ARG ASN ILE GLN VAL          
SEQRES   3 C  161  ASP GLU ALA ASN LEU LEU THR TRP GLN GLY LEU ILE VAL          
SEQRES   4 C  161  PRO ASP ASN PRO PRO TYR ASP LYS GLY ALA PHE ARG ILE          
SEQRES   5 C  161  GLU ILE ASN PHE PRO ALA GLU TYR PRO PHE LYS PRO PRO          
SEQRES   6 C  161  LYS ILE THR PHE LYS THR LYS ILE TYR HIS PRO ASN ILE          
SEQRES   7 C  161  ASP GLU LYS GLY GLN VAL CYS LEU PRO VAL ILE SER ALA          
SEQRES   8 C  161  GLU ASN TRP LYS PRO ALA THR LYS THR ASP GLN VAL ILE          
SEQRES   9 C  161  GLN SER LEU ILE ALA LEU VAL ASN ASP PRO GLN PRO GLU          
SEQRES  10 C  161  HIS PRO LEU ARG ALA ASP LEU ALA GLU GLU TYR SER LYS          
SEQRES  11 C  161  ASP ARG LYS LYS PHE CYS LYS ASN ALA GLU GLU PHE THR          
SEQRES  12 C  161  LYS LYS TYR GLY GLU LYS ARG PRO VAL ASP GLY GLY HIS          
SEQRES  13 C  161  HIS HIS HIS HIS HIS                                          
SEQRES   1 D  383  GLY SER GLY GLY PRO GLN ILE ALA TYR GLU ARG GLY PHE          
SEQRES   2 D  383  ARG TRP LYS LEU ALA HIS PHE ARG TYR LEU CYS GLN SER          
SEQRES   3 D  383  ASN ALA LEU PRO SER HIS VAL LYS ILE ASN VAL SER ARG          
SEQRES   4 D  383  GLN THR LEU PHE GLU ASP SER PHE GLN GLN ILE MET ALA          
SEQRES   5 D  383  LEU LYS PRO TYR ASP LEU ARG ARG ARG LEU TYR VAL ILE          
SEQRES   6 D  383  PHE ARG GLY GLU GLU GLY LEU ASP TYR GLY GLY LEU ALA          
SEQRES   7 D  383  ARG GLU TRP PHE PHE LEU LEU SER HIS GLU VAL LEU ASN          
SEQRES   8 D  383  PRO MET TYR CYS LEU PHE GLU TYR ALA GLY LYS ASN ASN          
SEQRES   9 D  383  TYR CYS LEU GLN ILE ASN PRO ALA SER THR ILE ASN PRO          
SEQRES  10 D  383  ASP HIS LEU SER TYR PHE CYS PHE ILE GLY ARG PHE ILE          
SEQRES  11 D  383  ALA MET ALA LEU PHE HIS GLY LYS PHE ILE ASP THR GLY          
SEQRES  12 D  383  PHE SER LEU PRO PHE TYR LYS ARG MET LEU SER LYS LYS          
SEQRES  13 D  383  LEU THR ILE LYS ASP LEU GLU SER ILE ASP THR GLU PHE          
SEQRES  14 D  383  TYR ASN SER LEU ILE TRP ILE ARG ASP ASN ASN ILE GLU          
SEQRES  15 D  383  GLU CYS GLY LEU GLU MET TYR PHE SER VAL ASP MET GLU          
SEQRES  16 D  383  ILE LEU GLY LYS VAL THR SER HIS ASP LEU LYS LEU GLY          
SEQRES  17 D  383  GLY SER ASN ILE LEU VAL THR GLU GLU ASN LYS ASP GLU          
SEQRES  18 D  383  TYR ILE GLY LEU MET THR GLU TRP ARG PHE SER ARG GLY          
SEQRES  19 D  383  VAL GLN GLU GLN THR LYS ALA PHE LEU ASP GLY PHE ASN          
SEQRES  20 D  383  GLU VAL VAL PRO LEU GLN TRP LEU GLN TYR PHE ASP GLU          
SEQRES  21 D  383  LYS GLU LEU GLU VAL MET LEU CYS GLY MET GLN GLU VAL          
SEQRES  22 D  383  ASP LEU ALA ASP TRP GLN ARG ASN THR VAL TYR ARG HIS          
SEQRES  23 D  383  TYR THR ARG ASN SER LYS GLN ILE ILE TRP PHE TRP GLN          
SEQRES  24 D  383  PHE VAL LYS GLU THR ASP ASN GLU VAL ARG MET ARG LEU          
SEQRES  25 D  383  LEU GLN PHE VAL THR GLY THR CYS ARG LEU PRO LEU GLY          
SEQRES  26 D  383  GLY PHE ALA GLU LEU MET GLY SER ASN GLY PRO GLN LYS          
SEQRES  27 D  383  PHE CYS ILE GLU LYS VAL GLY LYS ASP THR TRP LEU PRO          
SEQRES  28 D  383  ARG SER HIS THR CYS PHE ASN ARG LEU ASP LEU PRO PRO          
SEQRES  29 D  383  TYR LYS SER TYR GLU GLN LEU LYS GLU LYS LEU LEU PHE          
SEQRES  30 D  383  ALA ILE GLU GLU THR GLU                                      
SEQRES   1 E   83  GLY SER GLY GLY SER MSE GLN ILE LEU VAL LYS THR PHE          
SEQRES   2 E   83  THR TRP LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP          
SEQRES   3 E   83  THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU          
SEQRES   4 E   83  GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY          
SEQRES   5 E   83  LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN          
SEQRES   6 E   83  ILE LYS MSE GLY SER SER LEU TYR LEU VAL LEU ARG LEU          
SEQRES   7 E   83  PRO GLY GLN ARG ILE                                          
SEQRES   1 F  161  ALA ALA SER ARG ARG LEU MET LYS GLU LEU GLU GLU ILE          
SEQRES   2 F  161  ARG LYS CYS GLY MET LYS ASN PHE ARG ASN ILE GLN VAL          
SEQRES   3 F  161  ASP GLU ALA ASN LEU LEU THR TRP GLN GLY LEU ILE VAL          
SEQRES   4 F  161  PRO ASP ASN PRO PRO TYR ASP LYS GLY ALA PHE ARG ILE          
SEQRES   5 F  161  GLU ILE ASN PHE PRO ALA GLU TYR PRO PHE LYS PRO PRO          
SEQRES   6 F  161  LYS ILE THR PHE LYS THR LYS ILE TYR HIS PRO ASN ILE          
SEQRES   7 F  161  ASP GLU LYS GLY GLN VAL CYS LEU PRO VAL ILE SER ALA          
SEQRES   8 F  161  GLU ASN TRP LYS PRO ALA THR LYS THR ASP GLN VAL ILE          
SEQRES   9 F  161  GLN SER LEU ILE ALA LEU VAL ASN ASP PRO GLN PRO GLU          
SEQRES  10 F  161  HIS PRO LEU ARG ALA ASP LEU ALA GLU GLU TYR SER LYS          
SEQRES  11 F  161  ASP ARG LYS LYS PHE CYS LYS ASN ALA GLU GLU PHE THR          
SEQRES  12 F  161  LYS LYS TYR GLY GLU LYS ARG PRO VAL ASP GLY GLY HIS          
SEQRES  13 F  161  HIS HIS HIS HIS HIS                                          
SEQRES   1 G  383  GLY SER GLY GLY PRO GLN ILE ALA TYR GLU ARG GLY PHE          
SEQRES   2 G  383  ARG TRP LYS LEU ALA HIS PHE ARG TYR LEU CYS GLN SER          
SEQRES   3 G  383  ASN ALA LEU PRO SER HIS VAL LYS ILE ASN VAL SER ARG          
SEQRES   4 G  383  GLN THR LEU PHE GLU ASP SER PHE GLN GLN ILE MET ALA          
SEQRES   5 G  383  LEU LYS PRO TYR ASP LEU ARG ARG ARG LEU TYR VAL ILE          
SEQRES   6 G  383  PHE ARG GLY GLU GLU GLY LEU ASP TYR GLY GLY LEU ALA          
SEQRES   7 G  383  ARG GLU TRP PHE PHE LEU LEU SER HIS GLU VAL LEU ASN          
SEQRES   8 G  383  PRO MET TYR CYS LEU PHE GLU TYR ALA GLY LYS ASN ASN          
SEQRES   9 G  383  TYR CYS LEU GLN ILE ASN PRO ALA SER THR ILE ASN PRO          
SEQRES  10 G  383  ASP HIS LEU SER TYR PHE CYS PHE ILE GLY ARG PHE ILE          
SEQRES  11 G  383  ALA MET ALA LEU PHE HIS GLY LYS PHE ILE ASP THR GLY          
SEQRES  12 G  383  PHE SER LEU PRO PHE TYR LYS ARG MET LEU SER LYS LYS          
SEQRES  13 G  383  LEU THR ILE LYS ASP LEU GLU SER ILE ASP THR GLU PHE          
SEQRES  14 G  383  TYR ASN SER LEU ILE TRP ILE ARG ASP ASN ASN ILE GLU          
SEQRES  15 G  383  GLU CYS GLY LEU GLU MET TYR PHE SER VAL ASP MET GLU          
SEQRES  16 G  383  ILE LEU GLY LYS VAL THR SER HIS ASP LEU LYS LEU GLY          
SEQRES  17 G  383  GLY SER ASN ILE LEU VAL THR GLU GLU ASN LYS ASP GLU          
SEQRES  18 G  383  TYR ILE GLY LEU MET THR GLU TRP ARG PHE SER ARG GLY          
SEQRES  19 G  383  VAL GLN GLU GLN THR LYS ALA PHE LEU ASP GLY PHE ASN          
SEQRES  20 G  383  GLU VAL VAL PRO LEU GLN TRP LEU GLN TYR PHE ASP GLU          
SEQRES  21 G  383  LYS GLU LEU GLU VAL MET LEU CYS GLY MET GLN GLU VAL          
SEQRES  22 G  383  ASP LEU ALA ASP TRP GLN ARG ASN THR VAL TYR ARG HIS          
SEQRES  23 G  383  TYR THR ARG ASN SER LYS GLN ILE ILE TRP PHE TRP GLN          
SEQRES  24 G  383  PHE VAL LYS GLU THR ASP ASN GLU VAL ARG MET ARG LEU          
SEQRES  25 G  383  LEU GLN PHE VAL THR GLY THR CYS ARG LEU PRO LEU GLY          
SEQRES  26 G  383  GLY PHE ALA GLU LEU MET GLY SER ASN GLY PRO GLN LYS          
SEQRES  27 G  383  PHE CYS ILE GLU LYS VAL GLY LYS ASP THR TRP LEU PRO          
SEQRES  28 G  383  ARG SER HIS THR CYS PHE ASN ARG LEU ASP LEU PRO PRO          
SEQRES  29 G  383  TYR LYS SER TYR GLU GLN LEU LYS GLU LYS LEU LEU PHE          
SEQRES  30 G  383  ALA ILE GLU GLU THR GLU                                      
SEQRES   1 H   83  GLY SER GLY GLY SER MSE GLN ILE LEU VAL LYS THR PHE          
SEQRES   2 H   83  THR TRP LYS THR ILE THR LEU GLU VAL GLU PRO SER ASP          
SEQRES   3 H   83  THR ILE GLU ASN VAL LYS ALA LYS ILE GLN ASP LYS GLU          
SEQRES   4 H   83  GLY ILE PRO PRO ASP GLN GLN ARG LEU ILE PHE ALA GLY          
SEQRES   5 H   83  LYS GLN LEU GLU ASP GLY ARG THR LEU SER ASP TYR ASN          
SEQRES   6 H   83  ILE LYS MSE GLY SER SER LEU TYR LEU VAL LEU ARG LEU          
SEQRES   7 H   83  PRO GLY GLN ARG ILE                                          
HET    MSE  B   1       8                                                       
HET    MSE  B  63       8                                                       
HET    MSE  E   1       8                                                       
HET    MSE  E  63       8                                                       
HET    MSE  H   1       8                                                       
HET    MSE  H  63       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   2  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   9  HOH   *5(H2 O)                                                      
HELIX    1 AA1 GLY A  546  SER A  560  1                                  15    
HELIX    2 AA2 SER A  572  GLN A  574  5                                   3    
HELIX    3 AA3 THR A  575  ALA A  586  1                                  12    
HELIX    4 AA4 LYS A  588  ARG A  594  5                                   7    
HELIX    5 AA5 ARG A  613  LEU A  624  1                                  12    
HELIX    6 AA6 ASN A  625  CYS A  629  5                                   5    
HELIX    7 AA7 PRO A  645  ASN A  650  5                                   6    
HELIX    8 AA8 ASP A  652  GLY A  671  1                                  20    
HELIX    9 AA9 SER A  679  LEU A  687  1                                   9    
HELIX   10 AB1 THR A  692  ASP A  700  1                                   9    
HELIX   11 AB2 ASP A  700  ASN A  713  1                                  14    
HELIX   12 AB3 GLY A  742  ILE A  746  5                                   5    
HELIX   13 AB4 ASN A  752  ARG A  767  1                                  16    
HELIX   14 AB5 VAL A  769  VAL A  784  1                                  16    
HELIX   15 AB6 PRO A  785  GLN A  790  5                                   6    
HELIX   16 AB7 ASP A  793  CYS A  802  1                                  10    
HELIX   17 AB8 ASP A  808  ASN A  815  1                                   8    
HELIX   18 AB9 SER A  825  THR A  838  1                                  14    
HELIX   19 AC1 ASP A  839  GLY A  852  1                                  14    
HELIX   20 AC2 GLY A  860  LEU A  864  5                                   5    
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    
HELIX   24 AC6 SER C    4  LYS C   16  1                                  13    
HELIX   25 AC7 LEU C   87  SER C   91  5                                   5    
HELIX   26 AC8 LYS C  100  ASP C  114  1                                  15    
HELIX   27 AC9 ARG C  122  LYS C  131  1                                  10    
HELIX   28 AD1 ASP C  132  GLY C  148  1                                  17    
HELIX   29 AD2 GLY D  546  ASN D  561  1                                  16    
HELIX   30 AD3 SER D  572  GLN D  574  5                                   3    
HELIX   31 AD4 THR D  575  MET D  585  1                                  11    
HELIX   32 AD5 LYS D  588  ARG D  594  5                                   7    
HELIX   33 AD6 GLU D  604  TYR D  608  5                                   5    
HELIX   34 AD7 ARG D  613  LEU D  624  1                                  12    
HELIX   35 AD8 ASN D  625  CYS D  629  5                                   5    
HELIX   36 AD9 ALA D  646  ASN D  650  5                                   5    
HELIX   37 AE1 ASP D  652  HIS D  670  1                                  19    
HELIX   38 AE2 SER D  679  LEU D  687  1                                   9    
HELIX   39 AE3 ASP D  695  ASP D  700  1                                   6    
HELIX   40 AE4 ASP D  700  ASN D  713  1                                  14    
HELIX   41 AE5 GLY D  742  ILE D  746  5                                   5    
HELIX   42 AE6 ASN D  752  ARG D  767  1                                  16    
HELIX   43 AE7 VAL D  769  VAL D  784  1                                  16    
HELIX   44 AE8 PRO D  785  GLN D  790  5                                   6    
HELIX   45 AE9 ASP D  793  CYS D  802  1                                  10    
HELIX   46 AF1 ALA D  810  ASN D  815  1                                   6    
HELIX   47 AF2 SER D  825  THR D  838  1                                  14    
HELIX   48 AF3 ASN D  840  GLY D  852  1                                  13    
HELIX   49 AF4 GLY D  860  LEU D  864  5                                   5    
HELIX   50 AF5 SER D  901  ILE D  913  1                                  13    
HELIX   51 AF6 THR E   22  GLY E   35  1                                  14    
HELIX   52 AF7 PRO E   37  ASP E   39  5                                   3    
HELIX   53 AF8 ALA F    3  LYS F   16  1                                  14    
HELIX   54 AF9 LEU F   87  SER F   91  5                                   5    
HELIX   55 AG1 LYS F  100  ASP F  114  1                                  15    
HELIX   56 AG2 ARG F  122  LYS F  131  1                                  10    
HELIX   57 AG3 ASP F  132  TYR F  147  1                                  16    
HELIX   58 AG4 PHE G  547  ASN G  561  1                                  15    
HELIX   59 AG5 SER G  572  GLN G  574  5                                   3    
HELIX   60 AG6 THR G  575  ALA G  586  1                                  12    
HELIX   61 AG7 LYS G  588  ARG G  594  5                                   7    
HELIX   62 AG8 ALA G  612  LEU G  624  1                                  13    
HELIX   63 AG9 ASN G  625  CYS G  629  5                                   5    
HELIX   64 AH1 PRO G  645  ASN G  650  5                                   6    
HELIX   65 AH2 ASP G  652  GLY G  671  1                                  20    
HELIX   66 AH3 SER G  679  LEU G  687  1                                   9    
HELIX   67 AH4 THR G  692  ASP G  700  1                                   9    
HELIX   68 AH5 ASP G  700  ASN G  713  1                                  14    
HELIX   69 AH6 GLY G  742  ILE G  746  5                                   5    
HELIX   70 AH7 ASN G  752  ARG G  767  1                                  16    
HELIX   71 AH8 VAL G  769  VAL G  784  1                                  16    
HELIX   72 AH9 PRO G  785  GLN G  790  5                                   6    
HELIX   73 AI1 ASP G  793  CYS G  802  1                                  10    
HELIX   74 AI2 ASP G  808  ASN G  815  1                                   8    
HELIX   75 AI3 SER G  825  GLU G  837  1                                  13    
HELIX   76 AI4 ASP G  839  GLY G  852  1                                  14    
HELIX   77 AI5 GLY G  860  LEU G  864  5                                   5    
HELIX   78 AI6 SER G  901  GLU G  903  5                                   3    
HELIX   79 AI7 GLN G  904  GLU G  915  1                                  12    
HELIX   80 AI8 THR H   22  GLY H   35  1                                  14    
HELIX   81 AI9 PRO H   37  ASP H   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  TYR A 597   N  VAL A 567           
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  THR A 735   N  MET A 728           
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 5 THR B  12  GLU B  16  0                                        
SHEET    2 AA5 5 GLN B   2  THR B   7 -1  N  VAL B   5   O  ILE B  13           
SHEET    3 AA5 5 SER B  66  LEU B  71  1  O  LEU B  67   N  LEU B   4           
SHEET    4 AA5 5 GLN B  41  PHE B  45 -1  N  ARG B  42   O  VAL B  70           
SHEET    5 AA5 5 LYS B  48  GLN B  49 -1  O  LYS B  48   N  PHE B  45           
SHEET    1 AA6 4 PHE C  22  VAL C  27  0                                        
SHEET    2 AA6 4 THR C  34  ILE C  39 -1  O  GLN C  36   N  GLN C  26           
SHEET    3 AA6 4 PHE C  51  ASN C  56 -1  O  ILE C  55   N  TRP C  35           
SHEET    4 AA6 4 LYS C  67  PHE C  70 -1  O  LYS C  67   N  ASN C  56           
SHEET    1 AA7 2 HIS D 566  VAL D 571  0                                        
SHEET    2 AA7 2 ARG D 595  PHE D 600  1  O  ILE D 599   N  VAL D 571           
SHEET    1 AA8 2 PHE D 631  TYR D 633  0                                        
SHEET    2 AA8 2 LEU D 641  ILE D 643 -1  O  GLN D 642   N  GLU D 632           
SHEET    1 AA9 2 SER D 725  ILE D 730  0                                        
SHEET    2 AA9 2 LYS D 733  ASP D 738 -1  O  HIS D 737   N  VAL D 726           
SHEET    1 AB1 4 VAL D 817  TYR D 818  0                                        
SHEET    2 AB1 4 CYS D 874  ILE D 875  1  O  ILE D 875   N  VAL D 817           
SHEET    3 AB1 4 ARG D 893  ASP D 895  1  O  LEU D 894   N  CYS D 874           
SHEET    4 AB1 4 ARG D 886  HIS D 888 -1  N  HIS D 888   O  ARG D 893           
SHEET    1 AB2 5 THR E  12  GLU E  16  0                                        
SHEET    2 AB2 5 GLN E   2  LYS E   6 -1  N  ILE E   3   O  LEU E  15           
SHEET    3 AB2 5 SER E  66  LEU E  71  1  O  LEU E  67   N  LEU E   4           
SHEET    4 AB2 5 GLN E  41  PHE E  45 -1  N  ILE E  44   O  TYR E  68           
SHEET    5 AB2 5 LYS E  48  LEU E  50 -1  O  LEU E  50   N  LEU E  43           
SHEET    1 AB3 4 GLN F  26  VAL F  27  0                                        
SHEET    2 AB3 4 THR F  34  ILE F  39 -1  O  GLN F  36   N  GLN F  26           
SHEET    3 AB3 4 PHE F  51  ASN F  56 -1  O  ILE F  55   N  TRP F  35           
SHEET    4 AB3 4 LYS F  67  PHE F  70 -1  O  THR F  69   N  GLU F  54           
SHEET    1 AB4 2 HIS G 566  VAL G 571  0                                        
SHEET    2 AB4 2 ARG G 595  PHE G 600  1  O  TYR G 597   N  ILE G 569           
SHEET    1 AB5 2 PHE G 631  TYR G 633  0                                        
SHEET    2 AB5 2 LEU G 641  ILE G 643 -1  O  GLN G 642   N  GLU G 632           
SHEET    1 AB6 2 SER G 725  ILE G 730  0                                        
SHEET    2 AB6 2 LYS G 733  ASP G 738 -1  O  HIS G 737   N  VAL G 726           
SHEET    1 AB7 4 THR G 816  TYR G 818  0                                        
SHEET    2 AB7 4 PHE G 873  GLU G 876  1  O  ILE G 875   N  VAL G 817           
SHEET    3 AB7 4 ARG G 893  ASP G 895  1  O  LEU G 894   N  CYS G 874           
SHEET    4 AB7 4 ARG G 886  HIS G 888 -1  N  ARG G 886   O  ASP G 895           
SHEET    1 AB8 5 THR H  12  GLU H  16  0                                        
SHEET    2 AB8 5 GLN H   2  LYS H   6 -1  N  VAL H   5   O  ILE H  13           
SHEET    3 AB8 5 SER H  66  LEU H  71  1  O  LEU H  67   N  LYS H   6           
SHEET    4 AB8 5 GLN H  41  PHE H  45 -1  N  ILE H  44   O  TYR H  68           
SHEET    5 AB8 5 LYS H  48  GLN H  49 -1  O  LYS H  48   N  PHE H  45           
LINK         C   MSE B   1                 N   GLN B   2     1555   1555  1.32  
LINK         C   LYS B  62                 N   MSE B  63     1555   1555  1.31  
LINK         C   MSE B  63                 N   GLY B  64     1555   1555  1.32  
LINK         NE2 GLN D 813                 CD2 TRP D 832     1555   1555  1.58  
LINK         C   MSE E   1                 N   GLN E   2     1555   1555  1.34  
LINK         C   LYS E  62                 N   MSE E  63     1555   1555  1.33  
LINK         C   MSE E  63                 N   GLY E  64     1555   1555  1.33  
LINK         NH1 ARG F 133                 SG  CYS F 137     1555   1555  1.77  
LINK         C   MSE H   1                 N   GLN H   2     1555   1555  1.33  
LINK         C   LYS H  62                 N   MSE H  63     1555   1555  1.34  
LINK         C   MSE H  63                 N   GLY H  64     1555   1555  1.31  
CISPEP   1 LEU A  606    ASP A  607          0        -4.69                     
CISPEP   2 ASP A  607    TYR A  608          0        17.14                     
CISPEP   3 TYR A  608    GLY A  609          0        -1.63                     
CISPEP   4 GLY A  610    LEU A  611          0       -17.18                     
CISPEP   5 ALA C    2    ALA C    3          0        -5.74                     
CISPEP   6 PRO C   44    PRO C   45          0         2.20                     
CISPEP   7 TYR C   61    PRO C   62          0         1.86                     
CISPEP   8 LYS C  150    ARG C  151          0        13.38                     
CISPEP   9 ARG D  601    GLY D  602          0       -21.41                     
CISPEP  10 GLY D  602    GLU D  603          0       -10.35                     
CISPEP  11 GLU D  603    GLU D  604          0        24.63                     
CISPEP  12 GLY D  609    GLY D  610          0        12.78                     
CISPEP  13 GLU D  806    VAL D  807          0         1.25                     
CISPEP  14 VAL D  878    GLY D  879          0        -0.78                     
CISPEP  15 PRO E   74    GLY E   75          0       -14.19                     
CISPEP  16 GLY E   75    GLN E   76          0        -3.40                     
CISPEP  17 PRO F   44    PRO F   45          0         2.04                     
CISPEP  18 TYR F   61    PRO F   62          0         6.85                     
CISPEP  19 TYR G  608    GLY G  609          0        13.80                     
CISPEP  20 THR G  822    ARG G  823          0       -20.58                     
CISPEP  21 ARG G  823    ASN G  824          0       -10.01                     
CRYST1  114.005  118.897  158.663  90.00  90.00  90.00 P 21 21 21   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      0.008772  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008411  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006303        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system