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Database: PDB
Entry: 5YWY
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HEADER    SIGNALING PROTEIN-IMMUNE SYSTEM         30-NOV-17   5YWY              
TITLE     CRYSTAL STRUCTURE OF THE HUMAN PROSTAGLANDIN E RECEPTOR EP4 IN COMPLEX
TITLE    2 WITH FAB AND ONO-AE3-208                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROSTAGLANDIN E2 RECEPTOR EP4 SUBTYPE,PROSTAGLANDIN E2     
COMPND   3 RECEPTOR EP4 SUBTYPE;                                                
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: PGE2 RECEPTOR EP4 SUBTYPE,PROSTANOID EP4 RECEPTOR;          
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: HEAVY CHAIN OF FAB FRAGMENT;                               
COMPND  10 CHAIN: H;                                                            
COMPND  11 SYNONYM: FABH;                                                       
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: LIGHT CHAIN OF FAB FRAGMENT;                               
COMPND  15 CHAIN: L;                                                            
COMPND  16 SYNONYM: FABL;                                                       
COMPND  17 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: PTGER4, PTGER2;                                                
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  11 ORGANISM_COMMON: MOUSE;                                              
SOURCE  12 ORGANISM_TAXID: 10090;                                               
SOURCE  13 EXPRESSION_SYSTEM: HYBRID;                                           
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 37965;                                      
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_COMMON: MOUSE;                                              
SOURCE  18 ORGANISM_TAXID: 10090;                                               
SOURCE  19 EXPRESSION_SYSTEM: HYBRID;                                           
SOURCE  20 EXPRESSION_SYSTEM_TAXID: 37965                                       
KEYWDS    G-PROTEIN COUPLED RECEPTOR, LIPID MEDIATOR, FUNCTIONAL ANTIBODY,      
KEYWDS   2 SIGNALING PROTEIN-IMMUNE SYSTEM COMPLEX, MEMBRANE PROTEIN, SIGNALING 
KEYWDS   3 PROTEIN-IMMUNE SYSTEM                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.TOYODA,K.MORIMOTO,R.SUNO,S.HORITA,S.IWATA,T.KOBAYASHI               
REVDAT   3   19-DEC-18 5YWY    1       JRNL                                     
REVDAT   2   12-DEC-18 5YWY    1       TITLE                                    
REVDAT   1   05-DEC-18 5YWY    0                                                
JRNL        AUTH   Y.TOYODA,K.MORIMOTO,R.SUNO,S.HORITA,K.YAMASHITA,K.HIRATA,    
JRNL        AUTH 2 Y.SEKIGUCHI,S.YASUDA,M.SHIROISHI,T.SHIMIZU,Y.URUSHIBATA,     
JRNL        AUTH 3 Y.KAJIWARA,T.INAZUMI,Y.HOTTA,H.ASADA,T.NAKANE,Y.SHIIMURA,    
JRNL        AUTH 4 T.NAKAGITA,K.TSUGE,S.YOSHIDA,T.KURIBARA,T.HOSOYA,Y.SUGIMOTO, 
JRNL        AUTH 5 N.NOMURA,M.SATO,T.HIROKAWA,M.KINOSHITA,T.MURATA,K.TAKAYAMA,  
JRNL        AUTH 6 M.YAMAMOTO,S.NARUMIYA,S.IWATA,T.KOBAYASHI                    
JRNL        TITL   LIGAND BINDING TO HUMAN PROSTAGLANDIN E RECEPTOR EP4AT THE   
JRNL        TITL 2 LIPID-BILAYER INTERFACE.                                     
JRNL        REF    NAT. CHEM. BIOL.              V.  15    18 2019              
JRNL        REFN                   ESSN 1552-4469                               
JRNL        PMID   30510193                                                     
JRNL        DOI    10.1038/S41589-018-0131-3                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2210                                      
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) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.88                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 26463                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.224                           
REMARK   3   R VALUE            (WORKING SET) : 0.222                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1324                            
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 48.8850 -  6.6514    0.99     2952   155  0.2272 0.2697        
REMARK   3     2  6.6514 -  5.2815    1.00     2823   148  0.2095 0.2020        
REMARK   3     3  5.2815 -  4.6144    1.00     2810   146  0.1702 0.1817        
REMARK   3     4  4.6144 -  4.1928    1.00     2763   144  0.1963 0.2309        
REMARK   3     5  4.1928 -  3.8924    1.00     2777   153  0.2028 0.2210        
REMARK   3     6  3.8924 -  3.6630    1.00     2764   143  0.2418 0.2750        
REMARK   3     7  3.6630 -  3.4796    1.00     2749   145  0.2521 0.3061        
REMARK   3     8  3.4796 -  3.3282    1.00     2754   145  0.2724 0.3283        
REMARK   3     9  3.3282 -  3.2001    1.00     2747   145  0.3011 0.3435        
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) : 24.130           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.01                          
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      :  0.002           5760                                  
REMARK   3   ANGLE     :  0.602           7852                                  
REMARK   3   CHIRALITY :  0.041            897                                  
REMARK   3   PLANARITY :  0.004            975                                  
REMARK   3   DIHEDRAL  : 13.211           3412                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 10                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 18 THROUGH 49 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -39.7545 -24.6641   5.2043              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.6579 T22:   0.6288                                     
REMARK   3      T33:   1.6455 T12:  -0.5614                                     
REMARK   3      T13:  -0.0234 T23:  -0.0939                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1996 L22:   6.5165                                     
REMARK   3      L33:   3.2806 L12:  -0.7797                                     
REMARK   3      L13:  -0.6926 L23:  -0.2677                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0350 S12:  -0.0315 S13:   0.9440                       
REMARK   3      S21:  -0.7116 S22:   0.0978 S23:  -0.0957                       
REMARK   3      S31:  -0.8366 S32:   0.0189 S33:  -0.0822                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 50 THROUGH 122 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -51.9652 -31.1279   5.9079              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2812 T22:   0.3105                                     
REMARK   3      T33:   1.6531 T12:   0.2148                                     
REMARK   3      T13:   0.0455 T23:  -0.3662                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5674 L22:   0.4467                                     
REMARK   3      L33:   1.1822 L12:  -0.2207                                     
REMARK   3      L13:   0.2701 L23:  -0.2638                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0860 S12:  -0.1300 S13:   1.2441                       
REMARK   3      S21:   0.0815 S22:  -0.0383 S23:   0.1864                       
REMARK   3      S31:  -0.4908 S32:  -0.1129 S33:   0.1342                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 156 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -63.8730 -22.0461   9.6586              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8618 T22:   0.7482                                     
REMARK   3      T33:   1.9022 T12:   0.4254                                     
REMARK   3      T13:   0.1048 T23:  -0.2904                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8043 L22:   2.0005                                     
REMARK   3      L33:   6.4076 L12:  -2.5408                                     
REMARK   3      L13:   0.3728 L23:  -3.4503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0698 S12:   0.5258 S13:   1.4925                       
REMARK   3      S21:  -1.0933 S22:   0.0013 S23:   0.6992                       
REMARK   3      S31:  -1.2103 S32:  -0.4161 S33:   0.0315                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 157 THROUGH 346 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -54.7367 -32.3931  -4.9065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0079 T22:   0.3683                                     
REMARK   3      T33:   1.2400 T12:   0.0714                                     
REMARK   3      T13:   0.1207 T23:  -0.1311                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5431 L22:   2.5466                                     
REMARK   3      L33:   0.2177 L12:  -1.4123                                     
REMARK   3      L13:   0.2868 L23:  -0.4660                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1073 S12:   0.1613 S13:   0.6362                       
REMARK   3      S21:  -0.0824 S22:  -0.0760 S23:   0.3544                       
REMARK   3      S31:  -1.2541 S32:  -0.0720 S33:   0.1645                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 20 THROUGH 138 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -50.5780 -74.4937   1.1334              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2156 T22:   0.2233                                     
REMARK   3      T33:   0.2011 T12:   0.0468                                     
REMARK   3      T13:   0.0713 T23:  -0.0750                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3337 L22:   4.9413                                     
REMARK   3      L33:   2.5505 L12:   1.0301                                     
REMARK   3      L13:   0.4540 L23:  -0.0752                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0130 S12:  -0.2607 S13:   0.2875                       
REMARK   3      S21:   0.1935 S22:   0.0474 S23:  -0.0664                       
REMARK   3      S31:  -0.4603 S32:  -0.2338 S33:  -0.0336                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 139 THROUGH 242 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -34.2627-101.4642  14.2331              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2321 T22:   0.3884                                     
REMARK   3      T33:   0.1654 T12:   0.1005                                     
REMARK   3      T13:   0.0744 T23:   0.1333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1472 L22:   2.4571                                     
REMARK   3      L33:   3.1012 L12:   1.1858                                     
REMARK   3      L13:   0.9665 L23:   0.1078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0568 S12:  -0.5597 S13:   0.1198                       
REMARK   3      S21:   0.4203 S22:   0.1706 S23:   0.1458                       
REMARK   3      S31:  -0.0147 S32:  -0.3831 S33:  -0.1791                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 23 THROUGH 40 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -27.4970 -77.2976 -11.8225              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2976 T22:   0.4105                                     
REMARK   3      T33:   0.4762 T12:  -0.0757                                     
REMARK   3      T13:   0.1589 T23:  -0.1761                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1090 L22:   4.8212                                     
REMARK   3      L33:   8.9901 L12:  -0.9113                                     
REMARK   3      L13:   3.0442 L23:  -1.4076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1016 S12:   0.2740 S13:   0.1328                       
REMARK   3      S21:   0.0282 S22:  -0.0402 S23:  -1.0188                       
REMARK   3      S31:  -0.1104 S32:   0.8685 S33:   0.0931                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 41 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -31.0106 -69.4630  -6.4689              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3778 T22:   0.2668                                     
REMARK   3      T33:   0.3838 T12:  -0.1178                                     
REMARK   3      T13:   0.0393 T23:  -0.1297                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3340 L22:   6.3598                                     
REMARK   3      L33:   2.9520 L12:  -0.4383                                     
REMARK   3      L13:   0.2205 L23:   0.7158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1574 S12:  -0.3345 S13:   0.5426                       
REMARK   3      S21:   0.6050 S22:   0.1339 S23:  -0.5422                       
REMARK   3      S31:  -0.6569 S32:   0.6367 S33:   0.0534                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 113 THROUGH 150 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.6759 -91.6634   0.0166              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1654 T22:   0.2363                                     
REMARK   3      T33:   0.2141 T12:  -0.0231                                     
REMARK   3      T13:   0.0338 T23:  -0.0511                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6813 L22:   2.2618                                     
REMARK   3      L33:   0.9451 L12:  -2.1261                                     
REMARK   3      L13:   1.2258 L23:  -0.5028                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0217 S12:   0.0973 S13:   0.1534                       
REMARK   3      S21:  -0.0255 S22:  -0.1931 S23:  -0.1935                       
REMARK   3      S31:   0.1326 S32:  -0.0811 S33:   0.1787                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 151 THROUGH 236 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -26.1248-108.7967   1.9795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1372 T22:   0.3796                                     
REMARK   3      T33:   0.1552 T12:  -0.0115                                     
REMARK   3      T13:  -0.0736 T23:   0.0315                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.3015 L22:   6.3328                                     
REMARK   3      L33:   3.2793 L12:   0.9683                                     
REMARK   3      L13:   0.0896 L23:   0.9766                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1080 S12:  -0.0860 S13:  -0.4914                       
REMARK   3      S21:   0.2061 S22:   0.1072 S23:   0.3081                       
REMARK   3      S31:   0.4938 S32:  -0.1006 S33:   0.0047                       
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 5YWY COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 07-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300006048.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5-6.5                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225-HS                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 26463                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 52.00                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.33                     
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 71.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.29                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 24-31% PEG 300, 150 MM POTASSIUM         
REMARK 280  SULFATE, 100 MM MES PH 5.5-6.5, 1% 1,2,3-HEPTANTORIOL, LIPIDIC      
REMARK 280  CUBIC PHASE, TEMPERATURE 293K                                       
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   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       39.68000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       39.68000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       50.49000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      195.07500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       50.49000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      195.07500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       39.68000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       50.49000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000      195.07500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       39.68000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       50.49000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000      195.07500            
REMARK 290   SMTRY3   8  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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L                               
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     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     PRO A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     LEU A    12                                                      
REMARK 465     SER A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     ARG A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     ARG A   257                                                      
REMARK 465     GLN A   258                                                      
REMARK 465     PHE A   259                                                      
REMARK 465     PHE A   260                                                      
REMARK 465     ARG A   261                                                      
REMARK 465     ARG A   262                                                      
REMARK 465     ILE A   263                                                      
REMARK 465     LEU A   347                                                      
REMARK 465     PHE A   348                                                      
REMARK 465     CYS A   349                                                      
REMARK 465     ARG A   350                                                      
REMARK 465     ILE A   351                                                      
REMARK 465     GLY A   352                                                      
REMARK 465     GLY A   353                                                      
REMARK 465     SER A   354                                                      
REMARK 465     ARG A   355                                                      
REMARK 465     ARG A   356                                                      
REMARK 465     GLU A   357                                                      
REMARK 465     ARG A   358                                                      
REMARK 465     SER A   359                                                      
REMARK 465     GLY A   360                                                      
REMARK 465     GLN A   361                                                      
REMARK 465     HIS A   362                                                      
REMARK 465     CYS A   363                                                      
REMARK 465     SER A   364                                                      
REMARK 465     ASP A   365                                                      
REMARK 465     SER A   366                                                      
REMARK 465     LEU A   367                                                      
REMARK 465     GLU A   368                                                      
REMARK 465     GLU A   369                                                      
REMARK 465     ASN A   370                                                      
REMARK 465     LEU A   371                                                      
REMARK 465     TYR A   372                                                      
REMARK 465     PHE A   373                                                      
REMARK 465     GLN A   374                                                      
REMARK 465     MET H     1                                                      
REMARK 465     GLU H     2                                                      
REMARK 465     TRP H     3                                                      
REMARK 465     ARG H     4                                                      
REMARK 465     TRP H     5                                                      
REMARK 465     ILE H     6                                                      
REMARK 465     PHE H     7                                                      
REMARK 465     LEU H     8                                                      
REMARK 465     PHE H     9                                                      
REMARK 465     LEU H    10                                                      
REMARK 465     LEU H    11                                                      
REMARK 465     SER H    12                                                      
REMARK 465     GLY H    13                                                      
REMARK 465     THR H    14                                                      
REMARK 465     THR H    15                                                      
REMARK 465     GLY H    16                                                      
REMARK 465     VAL H    17                                                      
REMARK 465     HIS H    18                                                      
REMARK 465     SER H    19                                                      
REMARK 465     THR H   243                                                      
REMARK 465     ILE H   244                                                      
REMARK 465     LYS H   245                                                      
REMARK 465     PRO H   246                                                      
REMARK 465     CYS H   247                                                      
REMARK 465     PRO H   248                                                      
REMARK 465     PRO H   249                                                      
REMARK 465     CYS H   250                                                      
REMARK 465     LYS H   251                                                      
REMARK 465     CYS H   252                                                      
REMARK 465     PRO H   253                                                      
REMARK 465     MET L     1                                                      
REMARK 465     ASP L     2                                                      
REMARK 465     MET L     3                                                      
REMARK 465     ARG L     4                                                      
REMARK 465     THR L     5                                                      
REMARK 465     PRO L     6                                                      
REMARK 465     ALA L     7                                                      
REMARK 465     GLN L     8                                                      
REMARK 465     PHE L     9                                                      
REMARK 465     LEU L    10                                                      
REMARK 465     GLY L    11                                                      
REMARK 465     ILE L    12                                                      
REMARK 465     LEU L    13                                                      
REMARK 465     LEU L    14                                                      
REMARK 465     LEU L    15                                                      
REMARK 465     TRP L    16                                                      
REMARK 465     PHE L    17                                                      
REMARK 465     PRO L    18                                                      
REMARK 465     GLY L    19                                                      
REMARK 465     ILE L    20                                                      
REMARK 465     LYS L    21                                                      
REMARK 465     CYS L    22                                                      
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   OH   TYR A    80     O21  7UR A   501              2.03            
REMARK 500   O    LEU A   135     OG1  THR A   139              2.14            
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    GLN A  49      175.83    177.38                                   
REMARK 500    ASP A 132       -2.30     85.33                                   
REMARK 500    PRO A 166       51.07    -97.12                                   
REMARK 500    TRP A 174       47.12    -83.81                                   
REMARK 500    THR A 175       -0.29   -142.92                                   
REMARK 500    ALA A 266        4.22    -69.91                                   
REMARK 500    SER A 301       -7.16     72.75                                   
REMARK 500    LEU A 302       72.35     46.40                                   
REMARK 500    LYS A 308      -71.85    -82.02                                   
REMARK 500    ASN A 309       78.63     36.53                                   
REMARK 500    LEU A 332       35.23    -95.73                                   
REMARK 500    ARG L  72       19.33     59.13                                   
REMARK 500    ALA L  73       -6.80     71.52                                   
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   48     GLN A   49                  149.74                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7UR A 501                 
DBREF  5YWY A    4   259  UNP    P35408   PE2R4_HUMAN      4    217             
DBREF  5YWY A  260   366  UNP    P35408   PE2R4_HUMAN    260    366             
DBREF  5YWY H    1   253  PDB    5YWY     5YWY             1    253             
DBREF  5YWY L    1   236  PDB    5YWY     5YWY             1    236             
SEQADV 5YWY GLY A    1  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY THR A    2  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY SER A    3  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY GLN A    7  UNP  P35408    ASN     7 ENGINEERED MUTATION            
SEQADV 5YWY LEU A   62  UNP  P35408    ALA    62 ENGINEERED MUTATION            
SEQADV 5YWY ARG A  106  UNP  P35408    GLY   106 ENGINEERED MUTATION            
SEQADV 5YWY GLN A  177  UNP  P35408    ASN   177 ENGINEERED MUTATION            
SEQADV 5YWY LEU A  367  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY GLU A  368  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY GLU A  369  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY ASN A  370  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY LEU A  371  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY TYR A  372  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY PHE A  373  UNP  P35408              EXPRESSION TAG                 
SEQADV 5YWY GLN A  374  UNP  P35408              EXPRESSION TAG                 
SEQRES   1 A  332  GLY THR SER PRO GLY VAL GLN SER SER ALA SER LEU SER          
SEQRES   2 A  332  PRO ASP ARG LEU ASN SER PRO VAL THR ILE PRO ALA VAL          
SEQRES   3 A  332  MET PHE ILE PHE GLY VAL VAL GLY ASN LEU VAL ALA ILE          
SEQRES   4 A  332  VAL VAL LEU CYS LYS SER ARG LYS GLU GLN LYS GLU THR          
SEQRES   5 A  332  THR PHE TYR THR LEU VAL CYS GLY LEU LEU VAL THR ASP          
SEQRES   6 A  332  LEU LEU GLY THR LEU LEU VAL SER PRO VAL THR ILE ALA          
SEQRES   7 A  332  THR TYR MET LYS GLY GLN TRP PRO GLY GLY GLN PRO LEU          
SEQRES   8 A  332  CYS GLU TYR SER THR PHE ILE LEU LEU PHE PHE SER LEU          
SEQRES   9 A  332  SER ARG LEU SER ILE ILE CYS ALA MET SER VAL GLU ARG          
SEQRES  10 A  332  TYR LEU ALA ILE ASN HIS ALA TYR PHE TYR SER HIS TYR          
SEQRES  11 A  332  VAL ASP LYS ARG LEU ALA GLY LEU THR LEU PHE ALA VAL          
SEQRES  12 A  332  TYR ALA SER ASN VAL LEU PHE CYS ALA LEU PRO ASN MET          
SEQRES  13 A  332  GLY LEU GLY SER SER ARG LEU GLN TYR PRO ASP THR TRP          
SEQRES  14 A  332  CYS PHE ILE ASP TRP THR THR GLN VAL THR ALA HIS ALA          
SEQRES  15 A  332  ALA TYR SER TYR MET TYR ALA GLY PHE SER SER PHE LEU          
SEQRES  16 A  332  ILE LEU ALA THR VAL LEU CYS ASN VAL LEU VAL CYS GLY          
SEQRES  17 A  332  ALA LEU LEU ARG MET HIS ARG GLN PHE PHE ARG ARG ILE          
SEQRES  18 A  332  ALA GLY ALA GLU ILE GLN MET VAL ILE LEU LEU ILE ALA          
SEQRES  19 A  332  THR SER LEU VAL VAL LEU ILE CYS SER ILE PRO LEU VAL          
SEQRES  20 A  332  VAL ARG VAL PHE VAL ASN GLN LEU TYR GLN PRO SER LEU          
SEQRES  21 A  332  GLU ARG GLU VAL SER LYS ASN PRO ASP LEU GLN ALA ILE          
SEQRES  22 A  332  ARG ILE ALA SER VAL ASN PRO ILE LEU ASP PRO TRP ILE          
SEQRES  23 A  332  TYR ILE LEU LEU ARG LYS THR VAL LEU SER LYS ALA ILE          
SEQRES  24 A  332  GLU LYS ILE LYS CYS LEU PHE CYS ARG ILE GLY GLY SER          
SEQRES  25 A  332  ARG ARG GLU ARG SER GLY GLN HIS CYS SER ASP SER LEU          
SEQRES  26 A  332  GLU GLU ASN LEU TYR PHE GLN                                  
SEQRES   1 H  253  MET GLU TRP ARG TRP ILE PHE LEU PHE LEU LEU SER GLY          
SEQRES   2 H  253  THR THR GLY VAL HIS SER GLU ILE GLN LEU GLN GLN SER          
SEQRES   3 H  253  GLY PRO GLU LEU VAL LYS PRO GLY ALA SER VAL LYS VAL          
SEQRES   4 H  253  SER CYS LYS ALA SER GLY PHE PRO PHE SER THR TYR ASN          
SEQRES   5 H  253  ILE TYR TRP VAL ILE GLN SER HIS GLY LYS SER LEU GLU          
SEQRES   6 H  253  TRP ILE GLY TYR ILE ASP PRO TYR ASN GLY GLY THR SER          
SEQRES   7 H  253  TYR ASN GLN LYS PHE ARG GLY LYS ALA THR LEU THR VAL          
SEQRES   8 H  253  ASP LYS SER SER SER THR ALA TYR MET HIS LEU ASN SER          
SEQRES   9 H  253  LEU THR SER GLU ASP SER ALA VAL TYR TYR CYS ALA ARG          
SEQRES  10 H  253  ARG TRP TYR THR TYR ASP GLY ASP TRP PHE ALA TYR TRP          
SEQRES  11 H  253  GLY GLN GLY THR LEU VAL THR VAL SER ALA ALA LYS THR          
SEQRES  12 H  253  THR ALA PRO SER VAL TYR PRO LEU ALA PRO VAL CYS GLY          
SEQRES  13 H  253  ASP THR THR GLY SER SER VAL THR LEU GLY CYS LEU VAL          
SEQRES  14 H  253  LYS GLY TYR PHE PRO GLU PRO VAL THR LEU THR TRP ASN          
SEQRES  15 H  253  SER GLY SER LEU SER SER GLY VAL HIS THR PHE PRO ALA          
SEQRES  16 H  253  VAL LEU GLN SER ASP LEU TYR THR LEU SER SER SER VAL          
SEQRES  17 H  253  THR VAL THR SER SER THR TRP PRO SER GLN SER ILE THR          
SEQRES  18 H  253  CYS ASN VAL ALA HIS PRO ALA SER SER THR LYS VAL ASP          
SEQRES  19 H  253  LYS LYS ILE GLU PRO ARG GLY PRO THR ILE LYS PRO CYS          
SEQRES  20 H  253  PRO PRO CYS LYS CYS PRO                                      
SEQRES   1 L  236  MET ASP MET ARG THR PRO ALA GLN PHE LEU GLY ILE LEU          
SEQRES   2 L  236  LEU LEU TRP PHE PRO GLY ILE LYS CYS ASP ILE LYS MET          
SEQRES   3 L  236  THR GLN SER PRO SER SER MET TYR VAL SER LEU GLY GLU          
SEQRES   4 L  236  ARG VAL THR ILE THR CYS LYS ALA SER GLN ASP ILE ASN          
SEQRES   5 L  236  ARG TYR LEU SER TRP PHE GLN GLN LYS PRO GLY LYS SER          
SEQRES   6 L  236  PRO LYS THR LEU ILE TYR ARG ALA ASN ARG MET LEU ASP          
SEQRES   7 L  236  GLY VAL PRO SER ARG PHE SER GLY SER GLY SER GLY GLN          
SEQRES   8 L  236  ASP TYR SER LEU THR ILE SER SER LEU GLU TYR GLU ASP          
SEQRES   9 L  236  MET GLY ASN TYR TYR CYS LEU GLN TYR ASP GLU PHE PRO          
SEQRES  10 L  236  PHE THR PHE GLY SER GLY THR LYS LEU GLU ILE LYS ARG          
SEQRES  11 L  236  ALA ASP ALA ALA PRO THR VAL SER ILE PHE PRO PRO SER          
SEQRES  12 L  236  SER GLU GLN LEU THR SER GLY GLY ALA SER VAL VAL CYS          
SEQRES  13 L  236  PHE LEU ASN ASN PHE TYR PRO LYS ASP ILE ASN VAL LYS          
SEQRES  14 L  236  TRP LYS ILE ASP GLY SER GLU ARG GLN ASN GLY VAL LEU          
SEQRES  15 L  236  ASN SER TRP THR ASP GLN ASP SER LYS ASP SER THR TYR          
SEQRES  16 L  236  SER MET SER SER THR LEU THR LEU THR LYS ASP GLU TYR          
SEQRES  17 L  236  GLU ARG HIS ASN SER TYR THR CYS GLU ALA THR HIS LYS          
SEQRES  18 L  236  THR SER THR SER PRO ILE VAL LYS SER PHE ASN ARG ASN          
SEQRES  19 L  236  GLU CYS                                                      
HET    7UR  A 501      30                                                       
HETNAM     7UR 4-[4-CYANO-2-[[(2R)-2-(4-FLUORANYLNAPHTHALEN-1-YL)               
HETNAM   2 7UR  PROPANOYL]AMINO]PHENYL]BUTANOIC ACID                            
FORMUL   4  7UR    C24 H21 F N2 O3                                              
HELIX    1 AA1 ASN A   18  LEU A   42  1                                  25    
HELIX    2 AA2 GLU A   51  GLY A   83  1                                  33    
HELIX    3 AA3 GLY A   88  HIS A  123  1                                  36    
HELIX    4 AA4 ALA A  124  HIS A  129  1                                   6    
HELIX    5 AA5 LYS A  133  LEU A  153  1                                  21    
HELIX    6 AA6 VAL A  178  HIS A  214  1                                  37    
HELIX    7 AA7 ALA A  266  CYS A  284  1                                  19    
HELIX    8 AA8 SER A  285  TYR A  298  1                                  14    
HELIX    9 AA9 ASN A  309  VAL A  320  1                                  12    
HELIX   10 AB1 VAL A  320  LEU A  332  1                                  13    
HELIX   11 AB2 ARG A  333  ILE A  344  1                                  12    
HELIX   12 AB3 GLN H   81  ARG H   84  5                                   4    
HELIX   13 AB4 THR H  106  SER H  110  5                                   5    
HELIX   14 AB5 SER H  183  SER H  185  5                                   3    
HELIX   15 AB6 GLU L  101  MET L  105  5                                   5    
HELIX   16 AB7 SER L  143  SER L  149  1                                   7    
HELIX   17 AB8 LYS L  205  ARG L  210  1                                   6    
SHEET    1 AA1 2 SER A 161  LEU A 163  0                                        
SHEET    2 AA1 2 CYS A 170  ILE A 172 -1  O  PHE A 171   N  ARG A 162           
SHEET    1 AA2 4 GLN H  22  GLN H  25  0                                        
SHEET    2 AA2 4 VAL H  37  SER H  44 -1  O  LYS H  42   N  GLN H  24           
SHEET    3 AA2 4 THR H  97  LEU H 102 -1  O  MET H 100   N  VAL H  39           
SHEET    4 AA2 4 ALA H  87  ASP H  92 -1  N  THR H  90   O  TYR H  99           
SHEET    1 AA3 6 GLU H  29  VAL H  31  0                                        
SHEET    2 AA3 6 THR H 134  VAL H 138  1  O  THR H 137   N  GLU H  29           
SHEET    3 AA3 6 ALA H 111  THR H 121 -1  N  ALA H 111   O  VAL H 136           
SHEET    4 AA3 6 ILE H  53  GLN H  58 -1  N  GLN H  58   O  VAL H 112           
SHEET    5 AA3 6 LEU H  64  ASP H  71 -1  O  GLU H  65   N  ILE H  57           
SHEET    6 AA3 6 GLY H  76  TYR H  79 -1  O  GLY H  76   N  ASP H  71           
SHEET    1 AA4 4 GLU H  29  VAL H  31  0                                        
SHEET    2 AA4 4 THR H 134  VAL H 138  1  O  THR H 137   N  GLU H  29           
SHEET    3 AA4 4 ALA H 111  THR H 121 -1  N  ALA H 111   O  VAL H 136           
SHEET    4 AA4 4 GLY H 124  TRP H 130 -1  O  TRP H 126   N  TRP H 119           
SHEET    1 AA5 4 SER H 147  LEU H 151  0                                        
SHEET    2 AA5 4 SER H 162  TYR H 172 -1  O  LEU H 168   N  TYR H 149           
SHEET    3 AA5 4 LEU H 201  THR H 211 -1  O  TYR H 202   N  TYR H 172           
SHEET    4 AA5 4 VAL H 190  THR H 192 -1  N  HIS H 191   O  SER H 207           
SHEET    1 AA6 4 SER H 147  LEU H 151  0                                        
SHEET    2 AA6 4 SER H 162  TYR H 172 -1  O  LEU H 168   N  TYR H 149           
SHEET    3 AA6 4 LEU H 201  THR H 211 -1  O  TYR H 202   N  TYR H 172           
SHEET    4 AA6 4 VAL H 196  GLN H 198 -1  N  VAL H 196   O  THR H 203           
SHEET    1 AA7 3 THR H 178  TRP H 181  0                                        
SHEET    2 AA7 3 THR H 221  HIS H 226 -1  O  ASN H 223   N  THR H 180           
SHEET    3 AA7 3 THR H 231  LYS H 236 -1  O  VAL H 233   N  VAL H 224           
SHEET    1 AA8 4 MET L  26  SER L  29  0                                        
SHEET    2 AA8 4 VAL L  41  ALA L  47 -1  O  THR L  44   N  SER L  29           
SHEET    3 AA8 4 ASP L  92  ILE L  97 -1  O  LEU L  95   N  ILE L  43           
SHEET    4 AA8 4 PHE L  84  SER L  89 -1  N  SER L  87   O  SER L  94           
SHEET    1 AA9 6 SER L  32  VAL L  35  0                                        
SHEET    2 AA9 6 THR L 124  ILE L 128  1  O  GLU L 127   N  VAL L  35           
SHEET    3 AA9 6 GLY L 106  GLN L 112 -1  N  GLY L 106   O  LEU L 126           
SHEET    4 AA9 6 LEU L  55  GLN L  60 -1  N  PHE L  58   O  TYR L 109           
SHEET    5 AA9 6 PRO L  66  TYR L  71 -1  O  LEU L  69   N  TRP L  57           
SHEET    6 AA9 6 ARG L  75  MET L  76 -1  O  ARG L  75   N  TYR L  71           
SHEET    1 AB1 4 SER L  32  VAL L  35  0                                        
SHEET    2 AB1 4 THR L 124  ILE L 128  1  O  GLU L 127   N  VAL L  35           
SHEET    3 AB1 4 GLY L 106  GLN L 112 -1  N  GLY L 106   O  LEU L 126           
SHEET    4 AB1 4 THR L 119  PHE L 120 -1  O  THR L 119   N  GLN L 112           
SHEET    1 AB2 4 THR L 136  PHE L 140  0                                        
SHEET    2 AB2 4 GLY L 151  PHE L 161 -1  O  VAL L 155   N  PHE L 140           
SHEET    3 AB2 4 TYR L 195  THR L 204 -1  O  LEU L 201   N  VAL L 154           
SHEET    4 AB2 4 VAL L 181  TRP L 185 -1  N  SER L 184   O  SER L 198           
SHEET    1 AB3 4 SER L 175  ARG L 177  0                                        
SHEET    2 AB3 4 ASN L 167  ILE L 172 -1  N  ILE L 172   O  SER L 175           
SHEET    3 AB3 4 SER L 213  THR L 219 -1  O  THR L 219   N  ASN L 167           
SHEET    4 AB3 4 ILE L 227  ASN L 232 -1  O  PHE L 231   N  TYR L 214           
SSBOND   1 CYS A   92    CYS A  170                          1555   1555  2.03  
SSBOND   2 CYS H   41    CYS H  115                          1555   1555  2.03  
SSBOND   3 CYS H  155    CYS L  236                          1555   1555  2.03  
SSBOND   4 CYS H  167    CYS H  222                          1555   1555  2.03  
SSBOND   5 CYS L   45    CYS L  110                          1555   1555  2.03  
SSBOND   6 CYS L  156    CYS L  216                          1555   1555  2.03  
CISPEP   1 TYR A  165    PRO A  166          0         0.67                     
CISPEP   2 PHE H  173    PRO H  174          0        -4.51                     
CISPEP   3 GLU H  175    PRO H  176          0        -1.23                     
CISPEP   4 TRP H  215    PRO H  216          0         2.94                     
CISPEP   5 SER L   29    PRO L   30          0        -3.83                     
CISPEP   6 PHE L  116    PRO L  117          0         3.89                     
CISPEP   7 TYR L  162    PRO L  163          0         1.82                     
SITE     1 AC1 11 PRO A  24  THR A  76  TYR A  80  LEU A  99                    
SITE     2 AC1 11 THR A 168  TRP A 169  LEU A 312  ILE A 315                    
SITE     3 AC1 11 ARG A 316  SER A 319  VAL A 320                               
CRYST1  100.980  390.150   79.360  90.00  90.00  90.00 C 2 2 21      8          
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      0.009903  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002563  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012601        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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