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LongText Report for: 5ye9-pdb

Name Class
5ye9-pdb
HEADER    HYDROLASE/HYDROLASE INHIBITOR           15-SEP-17   5YE9              
TITLE     THE CRYSTAL STRUCTURE OF LP-PLA2 IN COMPLEX WITH A NOVEL INHIBITOR    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE;                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 47-429;                                       
COMPND   5 SYNONYM: LP-PLA2,PAF ACETYLHYDROLASE,1-ALKYL-2-                      
COMPND   6 ACETYLGLYCEROPHOSPHOCHOLINE ESTERASE,2-ACETYL-1-                     
COMPND   7 ALKYLGLYCEROPHOSPHOCHOLINE ESTERASE,GROUP-VIIA PHOSPHOLIPASE A2,     
COMPND   8 GVIIA-PLA2,LDL-ASSOCIATED PHOSPHOLIPASE A2,LDL-PLA(2),PAF 2-         
COMPND   9 ACYLHYDROLASE;                                                       
COMPND  10 EC: 3.1.1.47;                                                        
COMPND  11 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: PLA2G7, PAFAH;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE INHIBITOR, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.F.LIU,Y.C.XU                                                        
REVDAT   1   25-JUL-18 5YE9    0                                                
JRNL        AUTH   Q.LIU,F.HUANG,X.YUAN,K.WANG,Y.ZOU,J.SHEN,Y.XU                
JRNL        TITL   STRUCTURE-GUIDED DISCOVERY OF NOVEL, POTENT, AND ORALLY      
JRNL        TITL 2 BIOAVAILABLE INHIBITORS OF LIPOPROTEIN-ASSOCIATED            
JRNL        TITL 3 PHOSPHOLIPASE A2.                                            
JRNL        REF    J. MED. CHEM.                 V.  60 10231 2017              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29193967                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.7B01530                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.88 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 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) : 1.88                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.74                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 66566                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.201                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3333                            
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 29.7401 -  5.3998    0.99     2758   132  0.1633 0.1875        
REMARK   3     2  5.3998 -  4.2901    1.00     2731   128  0.1385 0.1436        
REMARK   3     3  4.2901 -  3.7490    0.95     2590   129  0.1416 0.1541        
REMARK   3     4  3.7490 -  3.4068    0.91     2467   136  0.1498 0.1808        
REMARK   3     5  3.4068 -  3.1629    1.00     2700   150  0.1640 0.1965        
REMARK   3     6  3.1629 -  2.9766    1.00     2675   136  0.1748 0.2307        
REMARK   3     7  2.9766 -  2.8276    1.00     2700   138  0.1733 0.2365        
REMARK   3     8  2.8276 -  2.7046    1.00     2709   134  0.1773 0.2120        
REMARK   3     9  2.7046 -  2.6006    1.00     2657   146  0.1722 0.2144        
REMARK   3    10  2.6006 -  2.5109    1.00     2729   128  0.1714 0.2243        
REMARK   3    11  2.5109 -  2.4324    1.00     2691   153  0.1729 0.2161        
REMARK   3    12  2.4324 -  2.3629    1.00     2650   147  0.1685 0.2192        
REMARK   3    13  2.3629 -  2.3007    1.00     2668   140  0.1739 0.2406        
REMARK   3    14  2.3007 -  2.2446    1.00     2682   138  0.1743 0.1931        
REMARK   3    15  2.2446 -  2.1936    0.85     2266   122  0.1788 0.2396        
REMARK   3    16  2.1936 -  2.1469    1.00     2683   144  0.1694 0.1960        
REMARK   3    17  2.1469 -  2.1040    1.00     2682   140  0.1755 0.2031        
REMARK   3    18  2.1040 -  2.0643    1.00     2716   142  0.1817 0.1995        
REMARK   3    19  2.0643 -  2.0275    0.80     2105   107  0.1926 0.2427        
REMARK   3    20  2.0275 -  1.9931    1.00     2696   141  0.1887 0.2212        
REMARK   3    21  1.9931 -  1.9610    1.00     2705   141  0.1960 0.2384        
REMARK   3    22  1.9610 -  1.9308    1.00     2660   135  0.2075 0.2500        
REMARK   3    23  1.9308 -  1.9024    1.00     2655   163  0.2261 0.2610        
REMARK   3    24  1.9024 -  1.8756    1.00     2658   163  0.2509 0.3096        
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)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.050           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.74                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 25.72                          
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      :  0.007           5938                                  
REMARK   3   ANGLE     :  1.071           8063                                  
REMARK   3   CHIRALITY :  0.047            874                                  
REMARK   3   PLANARITY :  0.005           1034                                  
REMARK   3   DIHEDRAL  : 12.510           2197                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 55 THROUGH 86 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -35.9982 -40.9097  15.6206              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2212 T22:   0.1307                                     
REMARK   3      T33:   0.1905 T12:   0.0260                                     
REMARK   3      T13:   0.0252 T23:  -0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0797 L22:   1.0851                                     
REMARK   3      L33:   2.9316 L12:  -0.0334                                     
REMARK   3      L13:   0.3919 L23:  -0.3191                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0288 S12:   0.0987 S13:  -0.1113                       
REMARK   3      S21:  -0.2269 S22:  -0.0883 S23:  -0.0596                       
REMARK   3      S31:   0.3196 S32:   0.0718 S33:   0.0702                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 87 THROUGH 111 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -48.8331 -38.2275  20.7059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1582 T22:   0.1579                                     
REMARK   3      T33:   0.1609 T12:  -0.0257                                     
REMARK   3      T13:  -0.0190 T23:   0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1793 L22:   1.8233                                     
REMARK   3      L33:   2.2048 L12:  -0.3562                                     
REMARK   3      L13:  -1.2677 L23:  -0.3911                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0489 S12:   0.1905 S13:  -0.1603                       
REMARK   3      S21:  -0.1112 S22:  -0.0606 S23:   0.4366                       
REMARK   3      S31:   0.2931 S32:  -0.3591 S33:   0.1541                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 112 THROUGH 210 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -41.3943 -37.5244  20.2646              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1502 T22:   0.1412                                     
REMARK   3      T33:   0.1791 T12:  -0.0085                                     
REMARK   3      T13:  -0.0119 T23:  -0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2490 L22:   1.9755                                     
REMARK   3      L33:   1.6192 L12:   0.1742                                     
REMARK   3      L13:   0.0225 L23:  -0.3674                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0049 S12:   0.0146 S13:  -0.0808                       
REMARK   3      S21:  -0.0597 S22:  -0.0167 S23:   0.1059                       
REMARK   3      S31:   0.1804 S32:  -0.1719 S33:   0.0300                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 211 THROUGH 240 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.6823 -28.2066  26.8597              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1467 T22:   0.1766                                     
REMARK   3      T33:   0.1533 T12:  -0.0079                                     
REMARK   3      T13:   0.0065 T23:   0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5697 L22:   7.7870                                     
REMARK   3      L33:   3.2503 L12:  -3.5161                                     
REMARK   3      L13:  -1.4401 L23:   2.8955                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1302 S12:  -0.1364 S13:   0.0008                       
REMARK   3      S21:   0.2234 S22:   0.1102 S23:  -0.2171                       
REMARK   3      S31:   0.0663 S32:   0.0637 S33:   0.0347                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 241 THROUGH 324 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.5061 -28.0284  16.7582              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1476 T22:   0.1445                                     
REMARK   3      T33:   0.1617 T12:   0.0362                                     
REMARK   3      T13:   0.0247 T23:   0.0157                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3023 L22:   1.9656                                     
REMARK   3      L33:   1.1224 L12:   0.0999                                     
REMARK   3      L13:  -0.1330 L23:  -0.1579                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0529 S12:  -0.0254 S13:  -0.1271                       
REMARK   3      S21:  -0.0521 S22:  -0.0478 S23:  -0.2985                       
REMARK   3      S31:   0.1618 S32:   0.1440 S33:   0.0584                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 325 THROUGH 376 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -42.0784 -18.4384  10.8022              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1707 T22:   0.1777                                     
REMARK   3      T33:   0.1842 T12:   0.0648                                     
REMARK   3      T13:  -0.0145 T23:   0.0184                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1883 L22:   2.8954                                     
REMARK   3      L33:   1.9700 L12:   0.3292                                     
REMARK   3      L13:  -0.1753 L23:  -0.2548                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0118 S12:   0.0782 S13:   0.0965                       
REMARK   3      S21:  -0.1482 S22:  -0.0194 S23:   0.1587                       
REMARK   3      S31:  -0.0579 S32:  -0.1651 S33:   0.0275                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 377 THROUGH 425 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -34.0153 -21.4597   1.2150              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2750 T22:   0.2732                                     
REMARK   3      T33:   0.1845 T12:   0.0529                                     
REMARK   3      T13:   0.0400 T23:   0.0056                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7318 L22:   2.4815                                     
REMARK   3      L33:   1.2137 L12:  -0.8747                                     
REMARK   3      L13:   0.0279 L23:   0.0456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0947 S12:   0.3311 S13:   0.0467                       
REMARK   3      S21:  -0.5393 S22:  -0.1531 S23:  -0.0953                       
REMARK   3      S31:   0.0124 S32:  -0.0370 S33:   0.0458                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 55 THROUGH 210 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   3.6688 -26.9597  32.8792              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1338 T22:   0.1506                                     
REMARK   3      T33:   0.1236 T12:   0.0003                                     
REMARK   3      T13:  -0.0145 T23:  -0.0213                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1743 L22:   1.3667                                     
REMARK   3      L33:   1.6740 L12:   0.0480                                     
REMARK   3      L13:  -0.0959 L23:  -0.2522                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0224 S12:  -0.1301 S13:   0.0733                       
REMARK   3      S21:   0.1003 S22:   0.0209 S23:  -0.0715                       
REMARK   3      S31:  -0.0124 S32:   0.1577 S33:   0.0085                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 211 THROUGH 312 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.4600 -33.4569  23.1920              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1213 T22:   0.1452                                     
REMARK   3      T33:   0.1231 T12:  -0.0049                                     
REMARK   3      T13:  -0.0011 T23:   0.0012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8876 L22:   1.9491                                     
REMARK   3      L33:   1.5937 L12:  -0.3711                                     
REMARK   3      L13:  -0.2566 L23:   0.4226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0002 S12:   0.0192 S13:  -0.0613                       
REMARK   3      S21:   0.0551 S22:  -0.0575 S23:   0.1866                       
REMARK   3      S31:   0.0193 S32:  -0.0973 S33:   0.0459                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 313 THROUGH 376 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.1594 -37.4250  14.6264              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1633 T22:   0.1811                                     
REMARK   3      T33:   0.1492 T12:   0.0190                                     
REMARK   3      T13:   0.0053 T23:   0.0071                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6962 L22:   1.4764                                     
REMARK   3      L33:   1.1697 L12:  -0.0934                                     
REMARK   3      L13:  -0.2081 L23:   0.3714                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0114 S12:  -0.0171 S13:  -0.0502                       
REMARK   3      S21:   0.0287 S22:   0.0484 S23:  -0.0989                       
REMARK   3      S31:   0.0184 S32:   0.1305 S33:  -0.0461                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 377 THROUGH 424 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4477 -26.7921   7.9583              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1908 T22:   0.1567                                     
REMARK   3      T33:   0.1472 T12:  -0.0285                                     
REMARK   3      T13:   0.0139 T23:   0.0296                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5770 L22:   2.1662                                     
REMARK   3      L33:   2.3278 L12:  -1.5577                                     
REMARK   3      L13:   0.0427 L23:  -0.6694                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0280 S12:   0.2362 S13:   0.1699                       
REMARK   3      S21:  -0.2290 S22:  -0.0143 S23:  -0.0284                       
REMARK   3      S31:  -0.1770 S32:   0.0919 S33:   0.0631                       
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 5YE9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-SEP-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300005134.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JAN-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
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 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.29                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 66597                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.876                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 87.620                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.9                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.15400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.88                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.98                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.10500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   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: NULL                                                  
REMARK 200 STARTING MODEL: 5I8P                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M MOPS PH 6.6, 0.4M LI2SO4, 27%       
REMARK 280  (W/V) (NH4)2SO4, 1M NA-AC, 1.4% 1,4-BUTANEDIOL, VAPOR DIFFUSION,    
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       57.54550            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       41.80600            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       57.54550            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       41.80600            
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                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 190 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 14130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -15.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 0 ANGSTROM**2                             
REMARK 350 SURFACE AREA OF THE COMPLEX: 14050 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 0.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    42                                                      
REMARK 465     PRO A    43                                                      
REMARK 465     LEU A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ALA A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     PHE A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     GLN A    53                                                      
REMARK 465     THR A    54                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     ASN A    90                                                      
REMARK 465     ASP A    91                                                      
REMARK 465     ARG A    92                                                      
REMARK 465     HIS A   428                                                      
REMARK 465     ILE A   429                                                      
REMARK 465     GLY B    42                                                      
REMARK 465     PRO B    43                                                      
REMARK 465     LEU B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     ALA B    47                                                      
REMARK 465     ALA B    48                                                      
REMARK 465     ALA B    49                                                      
REMARK 465     SER B    50                                                      
REMARK 465     PHE B    51                                                      
REMARK 465     GLY B    52                                                      
REMARK 465     GLN B    53                                                      
REMARK 465     THR B   425                                                      
REMARK 465     ASN B   426                                                      
REMARK 465     GLN B   427                                                      
REMARK 465     HIS B   428                                                      
REMARK 465     ILE B   429                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LYS A  55    CG   CD   CE   NZ                                   
REMARK 470     ARG A  58    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLN A  88    CG   CD   OE1  NE2                                  
REMARK 470     LEU A  93    CG   CD1  CD2                                       
REMARK 470     LYS A 109    CG   CD   CE   NZ                                   
REMARK 470     HIS A 114    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP A 115    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 115    CZ3  CH2                                            
REMARK 470     LEU A 116    CG   CD1  CD2                                       
REMARK 470     LEU A 123    CG   CD1  CD2                                       
REMARK 470     ASN A 133    OD1  ND2                                            
REMARK 470     GLU A 142    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 143    CG   CD   CE   NZ                                   
REMARK 470     GLN A 193    CD   OE1  NE2                                       
REMARK 470     GLU A 197    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 210    CG   CD   CE   NZ                                   
REMARK 470     GLN A 211    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 212    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 227    CD   CE   NZ                                        
REMARK 470     LYS A 246    CG   CD   CE   NZ                                   
REMARK 470     LYS A 252    CG   CD   CE   NZ                                   
REMARK 470     GLU A 256    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 304    CG   OD1  OD2                                       
REMARK 470     GLU A 340    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 363    CG   CD   CE   NZ                                   
REMARK 470     MET A 368    CG   SD   CE                                        
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     ASP A 374    CG   OD1  OD2                                       
REMARK 470     ASP A 401    CG   OD1  OD2                                       
REMARK 470     GLU A 414    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 426    CG   OD1  ND2                                       
REMARK 470     GLN A 427    CG   CD   OE1  NE2                                  
REMARK 470     LYS B  55    CG   CD   CE   NZ                                   
REMARK 470     GLN B  88    CG   CD   OE1  NE2                                  
REMARK 470     ASP B  89    CG   OD1  OD2                                       
REMARK 470     ASP B  91    CG   OD1  OD2                                       
REMARK 470     ARG B  92    CZ   NH1  NH2                                       
REMARK 470     LYS B 101    CD   CE   NZ                                        
REMARK 470     THR B 113    OG1  CG2                                            
REMARK 470     HIS B 114    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP B 115    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B 115    CZ3  CH2                                            
REMARK 470     LEU B 116    CG   CD1  CD2                                       
REMARK 470     LEU B 123    CG   CD1  CD2                                       
REMARK 470     GLN B 193    CD   OE1  NE2                                       
REMARK 470     LYS B 210    CG   CD   CE   NZ                                   
REMARK 470     GLN B 211    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 212    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 227    CD   CE   NZ                                        
REMARK 470     LYS B 246    CD   CE   NZ                                        
REMARK 470     ASP B 250    CG   OD1  OD2                                       
REMARK 470     LYS B 252    CG   CD   CE   NZ                                   
REMARK 470     GLU B 256    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 265    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 285    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 304    CG   OD1  OD2                                       
REMARK 470     LYS B 363    CG   CD   CE   NZ                                   
REMARK 470     MET B 368    CG   SD   CE                                        
REMARK 470     LYS B 370    CG   CD   CE   NZ                                   
REMARK 470     ASP B 412    CG   OD1  OD2                                       
REMARK 470     GLU B 414    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 423    CG   OD1  ND2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  73     -167.02    -72.64                                   
REMARK 500    HIS A 114     -157.73    -95.77                                   
REMARK 500    ASP A 250       71.08   -104.35                                   
REMARK 500    LYS A 252       46.05    -82.45                                   
REMARK 500    SER A 273     -117.98     67.59                                   
REMARK 500    HIS A 399       63.94   -104.66                                   
REMARK 500    ASP B  73     -168.94    -75.91                                   
REMARK 500    LYS B 252       36.37    -81.70                                   
REMARK 500    LYS B 266       76.97   -117.01                                   
REMARK 500    SER B 273     -114.57     65.65                                   
REMARK 500    HIS B 399       64.13   -102.12                                   
REMARK 500    LYS B 400     -167.33   -120.81                                   
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 8U6 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 8U6 B 501                 
DBREF  5YE9 A   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
DBREF  5YE9 B   47   429  UNP    Q13093   PAFA_HUMAN      47    429             
SEQADV 5YE9 GLY A   42  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 PRO A   43  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 LEU A   44  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 GLY A   45  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 SER A   46  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 GLY B   42  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 PRO B   43  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 LEU B   44  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 GLY B   45  UNP  Q13093              EXPRESSION TAG                 
SEQADV 5YE9 SER B   46  UNP  Q13093              EXPRESSION TAG                 
SEQRES   1 A  388  GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR          
SEQRES   2 A  388  LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS          
SEQRES   3 A  388  THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE          
SEQRES   4 A  388  LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU          
SEQRES   5 A  388  ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY          
SEQRES   6 A  388  LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN          
SEQRES   7 A  388  ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA          
SEQRES   8 A  388  ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO          
SEQRES   9 A  388  LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR          
SEQRES  10 A  388  LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY          
SEQRES  11 A  388  PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA          
SEQRES  12 A  388  SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU          
SEQRES  13 A  388  ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS          
SEQRES  14 A  388  GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG          
SEQRES  15 A  388  GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE          
SEQRES  16 A  388  LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU          
SEQRES  17 A  388  ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE          
SEQRES  18 A  388  ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY          
SEQRES  19 A  388  GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG          
SEQRES  20 A  388  PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO          
SEQRES  21 A  388  LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU          
SEQRES  22 A  388  PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN          
SEQRES  23 A  388  ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU          
SEQRES  24 A  388  ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN          
SEQRES  25 A  388  PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY          
SEQRES  26 A  388  HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL          
SEQRES  27 A  388  ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU          
SEQRES  28 A  388  GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP          
SEQRES  29 A  388  ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO          
SEQRES  30 A  388  GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE                  
SEQRES   1 B  388  GLY PRO LEU GLY SER ALA ALA ALA SER PHE GLY GLN THR          
SEQRES   2 B  388  LYS ILE PRO ARG GLY ASN GLY PRO TYR SER VAL GLY CYS          
SEQRES   3 B  388  THR ASP LEU MET PHE ASP HIS THR ASN LYS GLY THR PHE          
SEQRES   4 B  388  LEU ARG LEU TYR TYR PRO SER GLN ASP ASN ASP ARG LEU          
SEQRES   5 B  388  ASP THR LEU TRP ILE PRO ASN LYS GLU TYR PHE TRP GLY          
SEQRES   6 B  388  LEU SER LYS PHE LEU GLY THR HIS TRP LEU MET GLY ASN          
SEQRES   7 B  388  ILE LEU ARG LEU LEU PHE GLY SER MET THR THR PRO ALA          
SEQRES   8 B  388  ASN TRP ASN SER PRO LEU ARG PRO GLY GLU LYS TYR PRO          
SEQRES   9 B  388  LEU VAL VAL PHE SER HIS GLY LEU GLY ALA PHE ARG THR          
SEQRES  10 B  388  LEU TYR SER ALA ILE GLY ILE ASP LEU ALA SER HIS GLY          
SEQRES  11 B  388  PHE ILE VAL ALA ALA VAL GLU HIS ARG ASP ARG SER ALA          
SEQRES  12 B  388  SER ALA THR TYR TYR PHE LYS ASP GLN SER ALA ALA GLU          
SEQRES  13 B  388  ILE GLY ASP LYS SER TRP LEU TYR LEU ARG THR LEU LYS          
SEQRES  14 B  388  GLN GLU GLU GLU THR HIS ILE ARG ASN GLU GLN VAL ARG          
SEQRES  15 B  388  GLN ARG ALA LYS GLU CYS SER GLN ALA LEU SER LEU ILE          
SEQRES  16 B  388  LEU ASP ILE ASP HIS GLY LYS PRO VAL LYS ASN ALA LEU          
SEQRES  17 B  388  ASP LEU LYS PHE ASP MET GLU GLN LEU LYS ASP SER ILE          
SEQRES  18 B  388  ASP ARG GLU LYS ILE ALA VAL ILE GLY HIS SER PHE GLY          
SEQRES  19 B  388  GLY ALA THR VAL ILE GLN THR LEU SER GLU ASP GLN ARG          
SEQRES  20 B  388  PHE ARG CYS GLY ILE ALA LEU ASP ALA TRP MET PHE PRO          
SEQRES  21 B  388  LEU GLY ASP GLU VAL TYR SER ARG ILE PRO GLN PRO LEU          
SEQRES  22 B  388  PHE PHE ILE ASN SER GLU TYR PHE GLN TYR PRO ALA ASN          
SEQRES  23 B  388  ILE ILE LYS MET LYS LYS CYS TYR SER PRO ASP LYS GLU          
SEQRES  24 B  388  ARG LYS MET ILE THR ILE ARG GLY SER VAL HIS GLN ASN          
SEQRES  25 B  388  PHE ALA ASP PHE THR PHE ALA THR GLY LYS ILE ILE GLY          
SEQRES  26 B  388  HIS MET LEU LYS LEU LYS GLY ASP ILE ASP SER ASN VAL          
SEQRES  27 B  388  ALA ILE ASP LEU SER ASN LYS ALA SER LEU ALA PHE LEU          
SEQRES  28 B  388  GLN LYS HIS LEU GLY LEU HIS LYS ASP PHE ASP GLN TRP          
SEQRES  29 B  388  ASP CYS LEU ILE GLU GLY ASP ASP GLU ASN LEU ILE PRO          
SEQRES  30 B  388  GLY THR ASN ILE ASN THR THR ASN GLN HIS ILE                  
HET    8U6  A 501      33                                                       
HET    SO4  A 502       5                                                       
HET    SO4  A 503       5                                                       
HET    SO4  A 504       5                                                       
HET    8U6  B 501      33                                                       
HETNAM     8U6 N-[4-[(3-CYANO-4-NAPHTHALEN-2-YLOXY-PHENYL)                      
HETNAM   2 8U6  SULFAMOYL]PHENYL]ETHANAMIDE                                     
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  8U6    2(C25 H19 N3 O4 S)                                           
FORMUL   4  SO4    3(O4 S 2-)                                                   
FORMUL   8  HOH   *223(H2 O)                                                    
HELIX    1 AA1 ASN A  100  GLY A  112  1                                  13    
HELIX    2 AA2 HIS A  114  GLY A  126  1                                  13    
HELIX    3 AA3 TYR A  160  HIS A  170  1                                  11    
HELIX    4 AA4 ASP A  192  ILE A  198  1                                   7    
HELIX    5 AA5 LYS A  210  GLU A  212  5                                   3    
HELIX    6 AA6 GLU A  213  HIS A  241  1                                  29    
HELIX    7 AA7 ASP A  254  LYS A  259  5                                   6    
HELIX    8 AA8 SER A  273  ASP A  286  1                                  14    
HELIX    9 AA9 GLY A  303  TYR A  307  5                                   5    
HELIX   10 AB1 TYR A  324  CYS A  334  1                                  11    
HELIX   11 AB2 VAL A  350  ALA A  360  5                                  11    
HELIX   12 AB3 GLY A  362  LEU A  369  1                                   8    
HELIX   13 AB4 ASP A  376  GLY A  397  1                                  22    
HELIX   14 AB5 ASP A  401  GLN A  404  5                                   4    
HELIX   15 AB6 TRP A  405  GLU A  410  1                                   6    
HELIX   16 AB7 ASN B  100  GLY B  112  1                                  13    
HELIX   17 AB8 TRP B  115  GLY B  126  1                                  12    
HELIX   18 AB9 TYR B  160  HIS B  170  1                                  11    
HELIX   19 AC1 ASP B  192  GLY B  199  1                                   8    
HELIX   20 AC2 LYS B  210  GLU B  212  5                                   3    
HELIX   21 AC3 GLU B  213  HIS B  241  1                                  29    
HELIX   22 AC4 ASP B  254  LYS B  259  5                                   6    
HELIX   23 AC5 SER B  273  ASP B  286  1                                  14    
HELIX   24 AC6 GLY B  303  ARG B  309  5                                   7    
HELIX   25 AC7 TYR B  324  LYS B  333  1                                  10    
HELIX   26 AC8 VAL B  350  ALA B  360  5                                  11    
HELIX   27 AC9 GLY B  362  LEU B  369  1                                   8    
HELIX   28 AD1 ASP B  376  GLY B  397  1                                  22    
HELIX   29 AD2 ASP B  401  GLN B  404  5                                   4    
HELIX   30 AD3 TRP B  405  GLU B  410  1                                   6    
SHEET    1 AA110 ASN A 133  TRP A 134  0                                        
SHEET    2 AA110 VAL A  65  PHE A  72  1  N  VAL A  65   O  ASN A 133           
SHEET    3 AA110 THR A  79  PRO A  86 -1  O  TYR A  85   N  GLY A  66           
SHEET    4 AA110 ILE A 173  VAL A 177 -1  O  VAL A 174   N  TYR A  84           
SHEET    5 AA110 TYR A 144  SER A 150  1  N  VAL A 147   O  ALA A 175           
SHEET    6 AA110 ILE A 262  HIS A 272  1  O  ASP A 263   N  TYR A 144           
SHEET    7 AA110 CYS A 291  LEU A 295  1  O  LEU A 295   N  GLY A 271           
SHEET    8 AA110 LEU A 314  SER A 319  1  O  PHE A 315   N  ALA A 294           
SHEET    9 AA110 ARG A 341  ILE A 346  1  O  ILE A 344   N  ASN A 318           
SHEET   10 AA110 LEU A 416  PRO A 418 -1  O  ILE A 417   N  THR A 345           
SHEET    1 AA2 2 THR A  95  LEU A  96  0                                        
SHEET    2 AA2 2 THR A 129  THR A 130 -1  O  THR A 130   N  THR A  95           
SHEET    1 AA3 2 ALA A 186  TYR A 189  0                                        
SHEET    2 AA3 2 SER A 202  TYR A 205 -1  O  LEU A 204   N  THR A 187           
SHEET    1 AA410 ASN B 133  TRP B 134  0                                        
SHEET    2 AA410 VAL B  65  PHE B  72  1  N  VAL B  65   O  ASN B 133           
SHEET    3 AA410 THR B  79  PRO B  86 -1  O  TYR B  85   N  GLY B  66           
SHEET    4 AA410 ILE B 173  VAL B 177 -1  O  ALA B 176   N  ARG B  82           
SHEET    5 AA410 TYR B 144  SER B 150  1  N  VAL B 147   O  ALA B 175           
SHEET    6 AA410 ILE B 262  HIS B 272  1  O  ASP B 263   N  TYR B 144           
SHEET    7 AA410 CYS B 291  LEU B 295  1  O  LEU B 295   N  GLY B 271           
SHEET    8 AA410 LEU B 314  SER B 319  1  O  PHE B 315   N  ALA B 294           
SHEET    9 AA410 ARG B 341  ILE B 346  1  O  LYS B 342   N  PHE B 316           
SHEET   10 AA410 LEU B 416  PRO B 418 -1  O  ILE B 417   N  THR B 345           
SHEET    1 AA5 2 THR B  95  LEU B  96  0                                        
SHEET    2 AA5 2 THR B 129  THR B 130 -1  O  THR B 130   N  THR B  95           
SHEET    1 AA6 2 ALA B 186  TYR B 189  0                                        
SHEET    2 AA6 2 SER B 202  TYR B 205 -1  O  LEU B 204   N  THR B 187           
CISPEP   1 PHE A   72    ASP A   73          0        -8.79                     
CISPEP   2 PHE B   72    ASP B   73          0        -5.73                     
SITE     1 AC1 11 LEU A 107  PHE A 110  GLY A 152  LEU A 153                    
SITE     2 AC1 11 GLY A 154  ALA A 155  HIS A 272  SER A 273                    
SITE     3 AC1 11 GLN A 352  ALA A 355  PHE A 357                               
SITE     1 AC2  5 TYR A 321  PHE A 322  VAL A 350  HIS A 351                    
SITE     2 AC2  5 HOH A 610                                                     
SITE     1 AC3  6 ASN A 100  LYS A 101  ARG A 122  ASP B  89                    
SITE     2 AC3  6 ASN B  90  HOH B 676                                          
SITE     1 AC4  8 SER A 308  ILE A 310  PRO A 311  LYS A 339                    
SITE     2 AC4  8 LYS B 143  HIS B 241  ARG B 264  HOH B 607                    
SITE     1 AC5 13 LEU B 107  PHE B 110  GLY B 152  LEU B 153                    
SITE     2 AC5 13 GLY B 154  ALA B 155  HIS B 272  SER B 273                    
SITE     3 AC5 13 GLN B 352  ALA B 355  ASP B 356  PHE B 357                    
SITE     4 AC5 13 LEU B 371                                                     
CRYST1  115.091   83.612   96.601  90.00 114.90  90.00 C 1 2 1       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      0.008689  0.000000  0.004034        0.00000                         
SCALE2      0.000000  0.011960  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011413        0.00000                         
TER    2842      GLN A 427                                                      
TER    5715      THR B 424                                                      
MASTER      554    0    5   30   28    0   13    6 6017    2   81   60          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
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