Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 5jd4-pdb

Name Class
5jd4-pdb
HEADER    HYDROLASE                               15-APR-16   5JD4              
TITLE     CRYSTAL STRUCTURE OF LAE6, AN ALPHA/BETA HYDROLASE ENZYME FROM THE    
TITLE    2 METAGENOME OF LAKE ARREO, SPAIN                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LAE6;                                                      
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   6 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: P15TV LIC                                 
KEYWDS    ALPHA/BETA HYDROLASE, ESTERASE, METAGENOME, UNCULTURED BACTERIA,      
KEYWDS   2 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.J.STOGIOS,X.XU,M.ALCAIDE,V.YIM,H.CUI,M.MARTINEZ-MARTINEZ,M.FERRER,  
AUTHOR   2 A.SAVCHENKO                                                          
REVDAT   1   04-MAY-16 5JD4    0                                                
JRNL        AUTH   M.MARTINEZ-MARTINEZ                                          
JRNL        TITL   TO BE PUBLISHED                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.060                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 165467                         
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) : 0.169                           
REMARK   3   FREE R VALUE                     : 0.211                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 1.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1875                            
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 24.9542 -  4.8089    0.98    13980   161  0.1607 0.1758        
REMARK   3     2  4.8089 -  3.8214    0.97    13790   158  0.1270 0.1701        
REMARK   3     3  3.8214 -  3.3396    0.95    13526   156  0.1440 0.1805        
REMARK   3     4  3.3396 -  3.0349    0.94    13466   158  0.1594 0.2135        
REMARK   3     5  3.0349 -  2.8177    0.92    13112   153  0.1752 0.2291        
REMARK   3     6  2.8177 -  2.6517    0.91    12976   149  0.1736 0.2146        
REMARK   3     7  2.6517 -  2.5191    0.89    12724   150  0.1848 0.2368        
REMARK   3     8  2.5191 -  2.4095    0.87    12489   126  0.1931 0.2603        
REMARK   3     9  2.4095 -  2.3168    0.87    12280   148  0.2080 0.2666        
REMARK   3    10  2.3168 -  2.2369    0.83    11881   142  0.2236 0.2734        
REMARK   3    11  2.2369 -  2.1670    0.81    11670   120  0.2267 0.2888        
REMARK   3    12  2.1670 -  2.1051    0.79    11206   143  0.2483 0.3230        
REMARK   3    13  2.1051 -  2.0497    0.74    10492   111  0.2792 0.2995        
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)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.870           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.003          20001                                  
REMARK   3   ANGLE     :  0.730          27117                                  
REMARK   3   CHIRALITY :  0.028           2879                                  
REMARK   3   PLANARITY :  0.004           3637                                  
REMARK   3   DIHEDRAL  : 11.888           7245                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 24                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID -1:12)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  67.8775  91.8253  13.6766              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3244 T22:   0.4425                                     
REMARK   3      T33:   0.3812 T12:   0.1028                                     
REMARK   3      T13:  -0.0574 T23:  -0.1277                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6725 L22:   5.6968                                     
REMARK   3      L33:   9.3047 L12:   6.7992                                     
REMARK   3      L13:  -7.5175 L23:  -6.8546                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3626 S12:  -1.3324 S13:  -0.0307                       
REMARK   3      S21:   0.3838 S22:  -0.0529 S23:  -0.8586                       
REMARK   3      S31:  -0.2159 S32:   1.0586 S33:   0.3466                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 13:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  50.4382  77.1759   7.8238              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1692 T22:   0.3195                                     
REMARK   3      T33:   0.2219 T12:  -0.0117                                     
REMARK   3      T13:   0.0793 T23:   0.0256                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9127 L22:   3.5898                                     
REMARK   3      L33:   1.7713 L12:  -0.4280                                     
REMARK   3      L13:   0.0291 L23:   0.0972                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1147 S12:  -0.2395 S13:  -0.0790                       
REMARK   3      S21:   0.2674 S22:   0.1078 S23:  -0.0442                       
REMARK   3      S31:   0.0768 S32:  -0.0897 S33:   0.0115                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 78:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  60.4785  76.4611  -3.6326              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1496 T22:   0.2058                                     
REMARK   3      T33:   0.2422 T12:   0.0048                                     
REMARK   3      T13:   0.0177 T23:  -0.0204                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6362 L22:   1.5911                                     
REMARK   3      L33:   1.3172 L12:  -0.1918                                     
REMARK   3      L13:  -0.0502 L23:  -0.0255                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0331 S12:  -0.0200 S13:  -0.1950                       
REMARK   3      S21:  -0.0357 S22:   0.0327 S23:  -0.1570                       
REMARK   3      S31:   0.1344 S32:  -0.0034 S33:   0.0044                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID -1:55)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  47.9677  96.4077  18.1624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4652 T22:   0.2345                                     
REMARK   3      T33:   0.2549 T12:   0.0049                                     
REMARK   3      T13:  -0.0340 T23:  -0.0252                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0699 L22:   0.6617                                     
REMARK   3      L33:   2.9495 L12:  -0.5390                                     
REMARK   3      L13:  -0.7402 L23:  -0.9945                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0557 S12:   0.3940 S13:   0.3281                       
REMARK   3      S21:  -0.5708 S22:  -0.0492 S23:   0.0321                       
REMARK   3      S31:   0.0990 S32:  -0.2372 S33:  -0.0067                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 56:78)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  36.0241  85.2869  37.6551              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2852 T22:   0.2988                                     
REMARK   3      T33:   0.3522 T12:  -0.1431                                     
REMARK   3      T13:   0.0103 T23:   0.0456                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9731 L22:   8.3397                                     
REMARK   3      L33:   1.2185 L12:  -4.9298                                     
REMARK   3      L13:  -0.4094 L23:   1.8038                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0968 S12:  -0.6080 S13:  -0.5330                       
REMARK   3      S21:   0.2092 S22:  -0.0926 S23:   0.6250                       
REMARK   3      S31:   0.2080 S32:  -0.2986 S33:  -0.0422                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN B AND RESID 79:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  44.2633 101.0411  36.0433              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1802 T22:   0.1596                                     
REMARK   3      T33:   0.2244 T12:  -0.0115                                     
REMARK   3      T13:  -0.0005 T23:  -0.0229                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6608 L22:   1.9028                                     
REMARK   3      L33:   1.3333 L12:  -0.1433                                     
REMARK   3      L13:   0.0800 L23:   0.0070                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0217 S12:  -0.0817 S13:   0.2140                       
REMARK   3      S21:  -0.0634 S22:   0.0050 S23:   0.1654                       
REMARK   3      S31:  -0.0584 S32:  -0.1565 S33:   0.0107                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID -1:49)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 103.1896  74.1444  15.7003              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2116 T22:   0.3859                                     
REMARK   3      T33:   0.2443 T12:   0.0799                                     
REMARK   3      T13:  -0.0291 T23:   0.0108                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3278 L22:   7.9609                                     
REMARK   3      L33:   4.2909 L12:   0.3424                                     
REMARK   3      L13:  -0.7582 L23:   2.4214                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0614 S12:  -0.4716 S13:   0.3053                       
REMARK   3      S21:   0.3940 S22:   0.1017 S23:   0.5662                       
REMARK   3      S31:  -0.0530 S32:   0.0454 S33:  -0.0276                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 50:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 120.9167  79.6231  -4.5513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1705 T22:   0.3670                                     
REMARK   3      T33:   0.2251 T12:  -0.0585                                     
REMARK   3      T13:   0.0085 T23:   0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.4752 L22:   9.6327                                     
REMARK   3      L33:   2.0751 L12:   0.3283                                     
REMARK   3      L13:   0.4894 L23:   0.8876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1837 S12:   0.2424 S13:   0.1356                       
REMARK   3      S21:  -0.3128 S22:   0.2319 S23:  -0.1731                       
REMARK   3      S31:  -0.2753 S32:   0.4360 S33:  -0.0700                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN C AND RESID 78:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 102.5133  79.2389  -3.9697              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1701 T22:   0.2133                                     
REMARK   3      T33:   0.3041 T12:   0.0096                                     
REMARK   3      T13:  -0.0253 T23:   0.0347                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5880 L22:   1.3515                                     
REMARK   3      L33:   1.1317 L12:  -0.0148                                     
REMARK   3      L13:   0.0948 L23:   0.3514                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0406 S12:   0.0100 S13:   0.2681                       
REMARK   3      S21:  -0.0854 S22:  -0.0007 S23:   0.1704                       
REMARK   3      S31:  -0.1932 S32:  -0.0204 S33:   0.0356                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID -1:56)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 115.0651  60.0139  18.5509              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4753 T22:   0.2208                                     
REMARK   3      T33:   0.3011 T12:   0.0059                                     
REMARK   3      T13:   0.0025 T23:   0.0309                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8506 L22:   0.1044                                     
REMARK   3      L33:   1.4802 L12:  -0.4562                                     
REMARK   3      L13:   0.4302 L23:   0.0388                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0997 S12:   0.4771 S13:  -0.4279                       
REMARK   3      S21:  -0.4119 S22:  -0.0812 S23:  -0.1271                       
REMARK   3      S31:  -0.0434 S32:   0.0269 S33:  -0.0020                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 57:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 126.8553  70.8185  37.3806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2618 T22:   0.3266                                     
REMARK   3      T33:   0.4674 T12:  -0.1035                                     
REMARK   3      T13:  -0.0337 T23:  -0.0103                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9825 L22:   4.7983                                     
REMARK   3      L33:   2.2144 L12:  -5.1593                                     
REMARK   3      L13:   0.4045 L23:  -1.4208                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0721 S12:  -0.4654 S13:   0.3829                       
REMARK   3      S21:   0.2451 S22:  -0.0674 S23:  -0.5022                       
REMARK   3      S31:  -0.1638 S32:   0.5208 S33:   0.1051                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: (CHAIN D AND RESID 78:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A): 118.6833  55.4239  36.2116              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1912 T22:   0.1654                                     
REMARK   3      T33:   0.3095 T12:  -0.0008                                     
REMARK   3      T13:  -0.0154 T23:   0.0379                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4199 L22:   1.5831                                     
REMARK   3      L33:   1.2866 L12:   0.1494                                     
REMARK   3      L13:  -0.4004 L23:   0.0171                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0407 S12:  -0.0968 S13:  -0.2688                       
REMARK   3      S21:  -0.0078 S22:   0.0040 S23:  -0.2256                       
REMARK   3      S31:   0.0951 S32:   0.2000 S33:   0.0273                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID -1:60)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  70.8284  96.4656  65.8931              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4115 T22:   0.3737                                     
REMARK   3      T33:   0.2469 T12:   0.0444                                     
REMARK   3      T13:  -0.0539 T23:  -0.0424                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8871 L22:   2.2358                                     
REMARK   3      L33:   3.8717 L12:  -0.3419                                     
REMARK   3      L13:  -0.5505 L23:   1.4465                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1227 S12:  -0.5588 S13:   0.2818                       
REMARK   3      S21:   0.5807 S22:   0.0854 S23:  -0.0925                       
REMARK   3      S31:   0.0425 S32:   0.0049 S33:   0.0165                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 61:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  80.6713  84.9395  48.3604              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2779 T22:   0.3292                                     
REMARK   3      T33:   0.3971 T12:   0.1025                                     
REMARK   3      T13:  -0.0092 T23:  -0.0888                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6905 L22:   8.0083                                     
REMARK   3      L33:   1.5280 L12:   5.4215                                     
REMARK   3      L13:   0.0687 L23:  -0.4504                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2265 S12:   0.3181 S13:  -0.5065                       
REMARK   3      S21:   0.0687 S22:  -0.1643 S23:  -0.6681                       
REMARK   3      S31:   0.1985 S32:   0.1652 S33:  -0.1142                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: (CHAIN E AND RESID 78:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  73.3471 101.1432  49.2019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2035 T22:   0.2230                                     
REMARK   3      T33:   0.3363 T12:  -0.0082                                     
REMARK   3      T13:  -0.0282 T23:  -0.0666                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8132 L22:   1.5770                                     
REMARK   3      L33:   1.5584 L12:  -0.5456                                     
REMARK   3      L13:   0.2651 L23:  -0.2580                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0923 S12:  -0.2344 S13:   0.4555                       
REMARK   3      S21:   0.1864 S22:   0.0298 S23:  -0.3654                       
REMARK   3      S31:  -0.1315 S32:   0.1795 S33:   0.0308                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID -1:65)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  96.2233  51.3428 -32.7772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5202 T22:   0.5552                                     
REMARK   3      T33:   0.3125 T12:   0.0695                                     
REMARK   3      T13:  -0.0366 T23:  -0.0321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0117 L22:   3.1082                                     
REMARK   3      L33:   0.8661 L12:   0.9220                                     
REMARK   3      L13:  -0.1821 L23:  -0.1479                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0129 S12:   0.6567 S13:   0.0038                       
REMARK   3      S21:  -0.5453 S22:  -0.0065 S23:   0.5083                       
REMARK   3      S31:  -0.0427 S32:  -0.0928 S33:  -0.0179                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 66:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A): 108.1856  42.4701 -15.2119              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3955 T22:   0.2663                                     
REMARK   3      T33:   0.3793 T12:   0.1091                                     
REMARK   3      T13:  -0.0418 T23:   0.0140                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.6347 L22:   7.1611                                     
REMARK   3      L33:   9.0143 L12:   6.8417                                     
REMARK   3      L13:   5.5941 L23:   4.1035                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.7075 S12:  -0.1913 S13:  -0.7745                       
REMARK   3      S21:   0.5853 S22:  -0.2694 S23:  -0.9311                       
REMARK   3      S31:   0.9900 S32:   0.2677 S33:  -0.5283                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: (CHAIN F AND RESID 78:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  91.2986  52.3712 -17.1912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2214 T22:   0.2584                                     
REMARK   3      T33:   0.3283 T12:   0.0039                                     
REMARK   3      T13:  -0.0753 T23:  -0.0206                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5840 L22:   1.8574                                     
REMARK   3      L33:   1.5692 L12:  -0.4527                                     
REMARK   3      L13:  -0.1211 L23:   0.3310                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0276 S12:   0.2266 S13:  -0.1658                       
REMARK   3      S21:  -0.2262 S22:  -0.1405 S23:   0.4579                       
REMARK   3      S31:   0.1450 S32:  -0.1619 S33:   0.0689                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: (CHAIN G AND RESID -1:49)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  94.2082  58.0730  69.0059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6333 T22:   0.5490                                     
REMARK   3      T33:   0.3588 T12:   0.0471                                     
REMARK   3      T13:   0.0261 T23:   0.0729                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2567 L22:   0.1184                                     
REMARK   3      L33:   3.1151 L12:   0.6736                                     
REMARK   3      L13:  -0.9994 L23:   0.0378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0510 S12:  -1.0808 S13:  -0.7450                       
REMARK   3      S21:   0.5516 S22:   0.0267 S23:   0.1500                       
REMARK   3      S31:   0.1911 S32:   0.0095 S33:   0.0314                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: (CHAIN G AND RESID 50:78)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  81.8381  72.2847  48.6605              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2510 T22:   0.2329                                     
REMARK   3      T33:   0.3511 T12:   0.0757                                     
REMARK   3      T13:   0.0306 T23:  -0.0017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6506 L22:   5.3387                                     
REMARK   3      L33:   3.0680 L12:   1.5184                                     
REMARK   3      L13:   2.2158 L23:   1.7625                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1605 S12:  -0.0785 S13:  -0.0519                       
REMARK   3      S21:   0.1808 S22:  -0.1600 S23:   0.4767                       
REMARK   3      S31:  -0.2547 S32:  -0.3646 S33:   0.2860                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: (CHAIN G AND RESID 79:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  89.6474  55.3224  49.5487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2373 T22:   0.2172                                     
REMARK   3      T33:   0.3587 T12:  -0.0202                                     
REMARK   3      T13:   0.0558 T23:   0.0524                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8427 L22:   1.8854                                     
REMARK   3      L33:   1.6336 L12:  -0.4376                                     
REMARK   3      L13:  -0.4831 L23:   0.3132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0865 S12:  -0.2216 S13:  -0.3792                       
REMARK   3      S21:   0.2661 S22:  -0.0329 S23:   0.4075                       
REMARK   3      S31:   0.1523 S32:  -0.2013 S33:   0.0588                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID -1:65)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  66.3273 104.1133 -32.7426              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5650 T22:   0.5618                                     
REMARK   3      T33:   0.3402 T12:   0.1377                                     
REMARK   3      T13:   0.1081 T23:   0.0644                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0915 L22:   2.5640                                     
REMARK   3      L33:   2.1571 L12:   0.2103                                     
REMARK   3      L13:  -0.4532 L23:   0.6277                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2191 S12:   0.6330 S13:   0.1643                       
REMARK   3      S21:  -0.7640 S22:  -0.1966 S23:  -0.4972                       
REMARK   3      S31:   0.0164 S32:  -0.0109 S33:  -0.0621                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 66:77)                              
REMARK   3    ORIGIN FOR THE GROUP (A):  54.6205 113.0435 -15.3595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3337 T22:   0.2418                                     
REMARK   3      T33:   0.4011 T12:   0.1156                                     
REMARK   3      T13:   0.0702 T23:   0.0151                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.6574 L22:   6.6630                                     
REMARK   3      L33:   8.3821 L12:   5.1027                                     
REMARK   3      L13:  -2.9453 L23:  -0.5045                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6660 S12:   0.1022 S13:   1.1521                       
REMARK   3      S21:   0.2770 S22:  -0.0550 S23:   1.0639                       
REMARK   3      S31:  -0.9815 S32:  -0.3657 S33:  -0.6466                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: (CHAIN H AND RESID 78:315)                             
REMARK   3    ORIGIN FOR THE GROUP (A):  71.4672 103.2290 -17.2303              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2276 T22:   0.2599                                     
REMARK   3      T33:   0.4019 T12:   0.0068                                     
REMARK   3      T13:   0.0905 T23:   0.0400                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4393 L22:   2.1079                                     
REMARK   3      L33:   1.4105 L12:  -0.3935                                     
REMARK   3      L13:   0.0068 L23:  -0.2503                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0596 S12:   0.2409 S13:   0.2508                       
REMARK   3      S21:  -0.2829 S22:  -0.1173 S23:  -0.5972                       
REMARK   3      S31:  -0.1319 S32:   0.1747 S33:   0.0204                       
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 5JD4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 18-APR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000220343.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 177343                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.952                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.9                               
REMARK 200  DATA REDUNDANCY                : 3.000                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.6600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 91.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.520                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: BALBES                                                
REMARK 200 STARTING MODEL: 1EVQ                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.56                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M TRIS PH 8.5, 0.2 M AMMONIUM        
REMARK 280  SULFATE, 25% (W/V) PEG3350. CRYOPROTECTANT: 12% GLYCEROL AND        
REMARK 280  PARATONE-N OIL., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5480 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -72.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5080 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22860 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4540 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22780 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -36.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -53.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, G                                  
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     MET A   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     ARG A    -7                                                      
REMARK 465     GLU A    -6                                                      
REMARK 465     ASN A    -5                                                      
REMARK 465     LEU A    -4                                                      
REMARK 465     TYR A    -3                                                      
REMARK 465     PHE A    -2                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     ARG B    -7                                                      
REMARK 465     GLU B    -6                                                      
REMARK 465     ASN B    -5                                                      
REMARK 465     LEU B    -4                                                      
REMARK 465     TYR B    -3                                                      
REMARK 465     PHE B    -2                                                      
REMARK 465     MET C   -20                                                      
REMARK 465     GLY C   -19                                                      
REMARK 465     SER C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     ARG C    -7                                                      
REMARK 465     GLU C    -6                                                      
REMARK 465     ASN C    -5                                                      
REMARK 465     LEU C    -4                                                      
REMARK 465     TYR C    -3                                                      
REMARK 465     PHE C    -2                                                      
REMARK 465     MET D   -20                                                      
REMARK 465     GLY D   -19                                                      
REMARK 465     SER D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     ARG D    -7                                                      
REMARK 465     GLU D    -6                                                      
REMARK 465     ASN D    -5                                                      
REMARK 465     LEU D    -4                                                      
REMARK 465     TYR D    -3                                                      
REMARK 465     PHE D    -2                                                      
REMARK 465     MET E   -20                                                      
REMARK 465     GLY E   -19                                                      
REMARK 465     SER E   -18                                                      
REMARK 465     SER E   -17                                                      
REMARK 465     HIS E   -16                                                      
REMARK 465     HIS E   -15                                                      
REMARK 465     HIS E   -14                                                      
REMARK 465     HIS E   -13                                                      
REMARK 465     HIS E   -12                                                      
REMARK 465     HIS E   -11                                                      
REMARK 465     SER E   -10                                                      
REMARK 465     SER E    -9                                                      
REMARK 465     GLY E    -8                                                      
REMARK 465     ARG E    -7                                                      
REMARK 465     GLU E    -6                                                      
REMARK 465     ASN E    -5                                                      
REMARK 465     LEU E    -4                                                      
REMARK 465     TYR E    -3                                                      
REMARK 465     PHE E    -2                                                      
REMARK 465     MET F   -20                                                      
REMARK 465     GLY F   -19                                                      
REMARK 465     SER F   -18                                                      
REMARK 465     SER F   -17                                                      
REMARK 465     HIS F   -16                                                      
REMARK 465     HIS F   -15                                                      
REMARK 465     HIS F   -14                                                      
REMARK 465     HIS F   -13                                                      
REMARK 465     HIS F   -12                                                      
REMARK 465     HIS F   -11                                                      
REMARK 465     SER F   -10                                                      
REMARK 465     SER F    -9                                                      
REMARK 465     GLY F    -8                                                      
REMARK 465     ARG F    -7                                                      
REMARK 465     GLU F    -6                                                      
REMARK 465     ASN F    -5                                                      
REMARK 465     LEU F    -4                                                      
REMARK 465     TYR F    -3                                                      
REMARK 465     PHE F    -2                                                      
REMARK 465     MET G   -20                                                      
REMARK 465     GLY G   -19                                                      
REMARK 465     SER G   -18                                                      
REMARK 465     SER G   -17                                                      
REMARK 465     HIS G   -16                                                      
REMARK 465     HIS G   -15                                                      
REMARK 465     HIS G   -14                                                      
REMARK 465     HIS G   -13                                                      
REMARK 465     HIS G   -12                                                      
REMARK 465     HIS G   -11                                                      
REMARK 465     SER G   -10                                                      
REMARK 465     SER G    -9                                                      
REMARK 465     GLY G    -8                                                      
REMARK 465     ARG G    -7                                                      
REMARK 465     GLU G    -6                                                      
REMARK 465     ASN G    -5                                                      
REMARK 465     LEU G    -4                                                      
REMARK 465     TYR G    -3                                                      
REMARK 465     PHE G    -2                                                      
REMARK 465     MET H   -20                                                      
REMARK 465     GLY H   -19                                                      
REMARK 465     SER H   -18                                                      
REMARK 465     SER H   -17                                                      
REMARK 465     HIS H   -16                                                      
REMARK 465     HIS H   -15                                                      
REMARK 465     HIS H   -14                                                      
REMARK 465     HIS H   -13                                                      
REMARK 465     HIS H   -12                                                      
REMARK 465     HIS H   -11                                                      
REMARK 465     SER H   -10                                                      
REMARK 465     SER H    -9                                                      
REMARK 465     GLY H    -8                                                      
REMARK 465     ARG H    -7                                                      
REMARK 465     GLU H    -6                                                      
REMARK 465     ASN H    -5                                                      
REMARK 465     LEU H    -4                                                      
REMARK 465     TYR H    -3                                                      
REMARK 465     PHE H    -2                                                      
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     SER A 161    OG                                                  
REMARK 470     SER B 161    OG                                                  
REMARK 470     SER C 161    OG                                                  
REMARK 470     SER D 161    OG                                                  
REMARK 470     SER E 161    OG                                                  
REMARK 470     SER F 161    OG                                                  
REMARK 470     SER G 161    OG                                                  
REMARK 470     SER H 161    OG                                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C   596     O    HOH C   650              1.85            
REMARK 500   ND2  ASN B     8     O    HOH B   501              1.91            
REMARK 500   O    HOH H   695     O    HOH H   707              1.92            
REMARK 500   O    HOH F   736     O    HOH F   753              1.92            
REMARK 500   NE   ARG G   263     O3   GOL G   408              1.97            
REMARK 500   O    HOH A   672     O    HOH A   778              2.10            
REMARK 500   O    HOH C   700     O    HOH C   772              2.10            
REMARK 500   O    HOH G   718     O    HOH G   740              2.14            
REMARK 500   O    HOH D   616     O    HOH D   776              2.17            
REMARK 500   O    HOH D   653     O    HOH D   698              2.18            
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    ASN A  95     -165.78   -164.25                                   
REMARK 500    SER A 161     -113.37     61.41                                   
REMARK 500    TYR A 189       70.62     23.15                                   
REMARK 500    PHE A 209      -66.75     68.18                                   
REMARK 500    LEU A 291       44.26    -95.46                                   
REMARK 500    ASN B  95     -164.95   -163.22                                   
REMARK 500    SER B 161     -112.81     56.82                                   
REMARK 500    TYR B 189       67.35     21.19                                   
REMARK 500    PHE B 209      -67.64     65.95                                   
REMARK 500    LEU B 291       40.63    -92.97                                   
REMARK 500    ALA C  62       19.99   -142.64                                   
REMARK 500    ASN C  95     -165.61   -162.11                                   
REMARK 500    SER C 161     -117.07     59.39                                   
REMARK 500    TYR C 189       67.11     23.48                                   
REMARK 500    PHE C 209      -70.63     65.34                                   
REMARK 500    ASP C 226       -1.23     81.35                                   
REMARK 500    LEU C 291       45.60    -94.46                                   
REMARK 500    ASN D  95     -163.56   -164.97                                   
REMARK 500    SER D 161     -110.19     61.73                                   
REMARK 500    TYR D 189       66.97     20.60                                   
REMARK 500    PHE D 209      -66.17     67.73                                   
REMARK 500    LEU D 291       42.15    -96.68                                   
REMARK 500    ALA E  62       11.91   -141.72                                   
REMARK 500    ASN E  95     -164.66   -166.90                                   
REMARK 500    SER E 161     -114.60     58.85                                   
REMARK 500    TYR E 189       65.66     21.15                                   
REMARK 500    PHE E 209      -66.51     61.08                                   
REMARK 500    ASP E 226        6.80     84.51                                   
REMARK 500    LEU E 291       46.75    -88.72                                   
REMARK 500    ASN F  95     -164.49   -168.12                                   
REMARK 500    SER F 161     -115.07     54.80                                   
REMARK 500    TYR F 189       66.40     22.30                                   
REMARK 500    PHE F 209      -67.14     61.70                                   
REMARK 500    LEU F 291       43.48    -92.73                                   
REMARK 500    ASN G  95     -160.16   -165.42                                   
REMARK 500    SER G 161     -114.30     60.06                                   
REMARK 500    PHE G 184      147.01   -172.12                                   
REMARK 500    TYR G 189       65.37     21.72                                   
REMARK 500    SER G 198      176.51    -59.86                                   
REMARK 500    PHE G 209      -67.09     61.56                                   
REMARK 500    LEU G 291       42.38    -91.61                                   
REMARK 500    GLU H  75      -73.53    -84.51                                   
REMARK 500    PHE H  91       19.80     59.85                                   
REMARK 500    ASN H  95     -162.55   -166.15                                   
REMARK 500    SER H 161     -116.81     59.85                                   
REMARK 500    TYR H 189       65.99     23.59                                   
REMARK 500    PHE H 209      -65.50     60.30                                   
REMARK 500    LEU H 291       46.60    -91.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 822        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH B 815        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH B 816        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH B 817        DISTANCE =  6.95 ANGSTROMS                       
REMARK 525    HOH C 835        DISTANCE =  5.98 ANGSTROMS                       
REMARK 525    HOH C 836        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH C 837        DISTANCE =  6.11 ANGSTROMS                       
REMARK 525    HOH C 838        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH C 839        DISTANCE =  6.49 ANGSTROMS                       
REMARK 525    HOH C 841        DISTANCE =  7.83 ANGSTROMS                       
REMARK 525    HOH D 798        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH D 801        DISTANCE =  6.93 ANGSTROMS                       
REMARK 525    HOH D 803        DISTANCE =  7.22 ANGSTROMS                       
REMARK 525    HOH E 783        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH F 802        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH F 804        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH F 805        DISTANCE =  7.14 ANGSTROMS                       
REMARK 525    HOH G 780        DISTANCE =  6.77 ANGSTROMS                       
REMARK 525    HOH H 758        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH H 759        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH H 760        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH H 761        DISTANCE =  7.10 ANGSTROMS                       
REMARK 525    HOH H 762        DISTANCE =  7.16 ANGSTROMS                       
REMARK 525    HOH H 763        DISTANCE =  7.38 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PE3 A  406                                                       
REMARK 610     PE3 D  408                                                       
REMARK 610     PE3 H  405                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL B 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL B 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM B 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM C 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL D 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL E 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL E 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM E 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL F 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL F 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM F 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 G 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL G 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL G 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM G 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 H 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL H 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PE3 H 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BAM H 406                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5JD3   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5JD5   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5JD6   RELATED DB: PDB                                   
DBREF  5JD4 A  -20   315  PDB    5JD4     5JD4           -20    315             
DBREF  5JD4 B  -20   315  PDB    5JD4     5JD4           -20    315             
DBREF  5JD4 C  -20   315  PDB    5JD4     5JD4           -20    315             
DBREF  5JD4 D  -20   315  PDB    5JD4     5JD4           -20    315             
DBREF  5JD4 E  -20   315  PDB    5JD4     5JD4           -20    315             
DBREF  5JD4 F  -20   315  PDB    5JD4     5JD4           -20    315             
DBREF  5JD4 G  -20   315  PDB    5JD4     5JD4           -20    315             
DBREF  5JD4 H  -20   315  PDB    5JD4     5JD4           -20    315             
SEQRES   1 A  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  336  ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU          
SEQRES   3 A  336  THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG          
SEQRES   4 A  336  GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL          
SEQRES   5 A  336  GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU          
SEQRES   6 A  336  ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY          
SEQRES   7 A  336  PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR          
SEQRES   8 A  336  ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU          
SEQRES   9 A  336  ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE          
SEQRES  10 A  336  GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS          
SEQRES  11 A  336  SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA          
SEQRES  12 A  336  PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE          
SEQRES  13 A  336  ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE          
SEQRES  14 A  336  GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER          
SEQRES  15 A  336  ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS          
SEQRES  16 A  336  ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU          
SEQRES  17 A  336  ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER          
SEQRES  18 A  336  ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA          
SEQRES  19 A  336  LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP          
SEQRES  20 A  336  THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA          
SEQRES  21 A  336  THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR          
SEQRES  22 A  336  ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR          
SEQRES  23 A  336  ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR          
SEQRES  24 A  336  VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU          
SEQRES  25 A  336  THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU          
SEQRES  26 A  336  ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR                  
SEQRES   1 B  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  336  ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU          
SEQRES   3 B  336  THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG          
SEQRES   4 B  336  GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL          
SEQRES   5 B  336  GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU          
SEQRES   6 B  336  ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY          
SEQRES   7 B  336  PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR          
SEQRES   8 B  336  ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU          
SEQRES   9 B  336  ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE          
SEQRES  10 B  336  GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS          
SEQRES  11 B  336  SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA          
SEQRES  12 B  336  PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE          
SEQRES  13 B  336  ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE          
SEQRES  14 B  336  GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER          
SEQRES  15 B  336  ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS          
SEQRES  16 B  336  ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU          
SEQRES  17 B  336  ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER          
SEQRES  18 B  336  ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA          
SEQRES  19 B  336  LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP          
SEQRES  20 B  336  THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA          
SEQRES  21 B  336  THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR          
SEQRES  22 B  336  ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR          
SEQRES  23 B  336  ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR          
SEQRES  24 B  336  VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU          
SEQRES  25 B  336  THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU          
SEQRES  26 B  336  ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR                  
SEQRES   1 C  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  336  ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU          
SEQRES   3 C  336  THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG          
SEQRES   4 C  336  GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL          
SEQRES   5 C  336  GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU          
SEQRES   6 C  336  ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY          
SEQRES   7 C  336  PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR          
SEQRES   8 C  336  ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU          
SEQRES   9 C  336  ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE          
SEQRES  10 C  336  GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS          
SEQRES  11 C  336  SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA          
SEQRES  12 C  336  PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE          
SEQRES  13 C  336  ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE          
SEQRES  14 C  336  GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER          
SEQRES  15 C  336  ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS          
SEQRES  16 C  336  ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU          
SEQRES  17 C  336  ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER          
SEQRES  18 C  336  ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA          
SEQRES  19 C  336  LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP          
SEQRES  20 C  336  THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA          
SEQRES  21 C  336  THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR          
SEQRES  22 C  336  ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR          
SEQRES  23 C  336  ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR          
SEQRES  24 C  336  VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU          
SEQRES  25 C  336  THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU          
SEQRES  26 C  336  ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR                  
SEQRES   1 D  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  336  ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU          
SEQRES   3 D  336  THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG          
SEQRES   4 D  336  GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL          
SEQRES   5 D  336  GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU          
SEQRES   6 D  336  ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY          
SEQRES   7 D  336  PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR          
SEQRES   8 D  336  ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU          
SEQRES   9 D  336  ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE          
SEQRES  10 D  336  GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS          
SEQRES  11 D  336  SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA          
SEQRES  12 D  336  PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE          
SEQRES  13 D  336  ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE          
SEQRES  14 D  336  GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER          
SEQRES  15 D  336  ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS          
SEQRES  16 D  336  ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU          
SEQRES  17 D  336  ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER          
SEQRES  18 D  336  ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA          
SEQRES  19 D  336  LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP          
SEQRES  20 D  336  THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA          
SEQRES  21 D  336  THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR          
SEQRES  22 D  336  ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR          
SEQRES  23 D  336  ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR          
SEQRES  24 D  336  VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU          
SEQRES  25 D  336  THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU          
SEQRES  26 D  336  ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR                  
SEQRES   1 E  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 E  336  ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU          
SEQRES   3 E  336  THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG          
SEQRES   4 E  336  GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL          
SEQRES   5 E  336  GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU          
SEQRES   6 E  336  ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY          
SEQRES   7 E  336  PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR          
SEQRES   8 E  336  ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU          
SEQRES   9 E  336  ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE          
SEQRES  10 E  336  GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS          
SEQRES  11 E  336  SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA          
SEQRES  12 E  336  PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE          
SEQRES  13 E  336  ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE          
SEQRES  14 E  336  GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER          
SEQRES  15 E  336  ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS          
SEQRES  16 E  336  ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU          
SEQRES  17 E  336  ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER          
SEQRES  18 E  336  ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA          
SEQRES  19 E  336  LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP          
SEQRES  20 E  336  THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA          
SEQRES  21 E  336  THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR          
SEQRES  22 E  336  ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR          
SEQRES  23 E  336  ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR          
SEQRES  24 E  336  VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU          
SEQRES  25 E  336  THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU          
SEQRES  26 E  336  ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR                  
SEQRES   1 F  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 F  336  ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU          
SEQRES   3 F  336  THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG          
SEQRES   4 F  336  GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL          
SEQRES   5 F  336  GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU          
SEQRES   6 F  336  ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY          
SEQRES   7 F  336  PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR          
SEQRES   8 F  336  ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU          
SEQRES   9 F  336  ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE          
SEQRES  10 F  336  GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS          
SEQRES  11 F  336  SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA          
SEQRES  12 F  336  PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE          
SEQRES  13 F  336  ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE          
SEQRES  14 F  336  GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER          
SEQRES  15 F  336  ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS          
SEQRES  16 F  336  ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU          
SEQRES  17 F  336  ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER          
SEQRES  18 F  336  ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA          
SEQRES  19 F  336  LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP          
SEQRES  20 F  336  THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA          
SEQRES  21 F  336  THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR          
SEQRES  22 F  336  ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR          
SEQRES  23 F  336  ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR          
SEQRES  24 F  336  VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU          
SEQRES  25 F  336  THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU          
SEQRES  26 F  336  ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR                  
SEQRES   1 G  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 G  336  ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU          
SEQRES   3 G  336  THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG          
SEQRES   4 G  336  GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL          
SEQRES   5 G  336  GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU          
SEQRES   6 G  336  ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY          
SEQRES   7 G  336  PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR          
SEQRES   8 G  336  ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU          
SEQRES   9 G  336  ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE          
SEQRES  10 G  336  GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS          
SEQRES  11 G  336  SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA          
SEQRES  12 G  336  PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE          
SEQRES  13 G  336  ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE          
SEQRES  14 G  336  GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER          
SEQRES  15 G  336  ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS          
SEQRES  16 G  336  ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU          
SEQRES  17 G  336  ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER          
SEQRES  18 G  336  ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA          
SEQRES  19 G  336  LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP          
SEQRES  20 G  336  THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA          
SEQRES  21 G  336  THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR          
SEQRES  22 G  336  ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR          
SEQRES  23 G  336  ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR          
SEQRES  24 G  336  VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU          
SEQRES  25 G  336  THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU          
SEQRES  26 G  336  ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR                  
SEQRES   1 H  336  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 H  336  ARG GLU ASN LEU TYR PHE GLN GLY MET LEU LEU PRO GLU          
SEQRES   3 H  336  THR ARG ASN LEU LEU ASP LEU MET ASP ALA ALA THR ARG          
SEQRES   4 H  336  GLY GLY ARG PRO ARG LEU GLU THR LEU PRO HIS ALA VAL          
SEQRES   5 H  336  GLY ARG LYS ALA VAL ASP LYS MET SER GLU ASP GLY GLU          
SEQRES   6 H  336  ALA ASP PRO PRO GLU VAL ALA GLU VAL ALA ASN GLY GLY          
SEQRES   7 H  336  PHE ALA GLY PRO ALA SER GLU ILE ARG PHE ARG ARG TYR          
SEQRES   8 H  336  ARG PRO LEU GLY GLU ALA ALA GLY LEU LEU PRO THR LEU          
SEQRES   9 H  336  ILE TYR TYR HIS GLY GLY GLY PHE VAL ILE GLY ASN ILE          
SEQRES  10 H  336  GLU THR HIS ASP SER THR CYS ARG ARG LEU ALA ASN LYS          
SEQRES  11 H  336  SER ARG CYS GLN VAL ILE SER ILE ASP TYR ARG LEU ALA          
SEQRES  12 H  336  PRO GLU HIS PRO PHE PRO ALA PRO ILE ASP ASP GLY ILE          
SEQRES  13 H  336  ALA ALA PHE ARG HIS ILE ARG ASP ASN ALA GLU SER PHE          
SEQRES  14 H  336  GLY ALA ASP ALA ALA ARG LEU ALA VAL GLY GLY ASP SER          
SEQRES  15 H  336  ALA GLY GLY ALA MET ALA ALA VAL VAL CYS GLN ALA CYS          
SEQRES  16 H  336  ARG ASP ALA GLY GLU THR GLY PRO ALA PHE GLN MET LEU          
SEQRES  17 H  336  ILE TYR PRO ALA THR ASP SER SER ARG GLU SER ALA SER          
SEQRES  18 H  336  ARG VAL ALA PHE ALA GLU GLY TYR PHE LEU SER LYS ALA          
SEQRES  19 H  336  LEU MET ASP TRP PHE TRP GLU ALA TYR VAL PRO GLU ASP          
SEQRES  20 H  336  THR ASP LEU THR ASP LEU ARG LEU SER PRO LEU LEU ALA          
SEQRES  21 H  336  THR ASP PHE THR GLY LEU PRO PRO ALA PHE VAL LEU THR          
SEQRES  22 H  336  ALA GLY TYR ASP PRO LEU ARG ASP GLU GLY ARG ALA TYR          
SEQRES  23 H  336  ALA ASP ARG LEU ILE GLU ALA GLY ILE LYS THR THR TYR          
SEQRES  24 H  336  VAL ASN TYR PRO GLY THR ILE HIS GLY PHE PHE SER LEU          
SEQRES  25 H  336  THR ARG PHE LEU SER GLN GLY LEU LYS ALA ASN ASP GLU          
SEQRES  26 H  336  ALA ALA ALA VAL MET GLY ALA HIS PHE GLY THR                  
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    GOL  A 403       6                                                       
HET     CL  A 404       1                                                       
HET    GOL  A 405       6                                                       
HET    PE3  A 406      12                                                       
HET    BAM  A 407       9                                                       
HET    SO4  B 401       5                                                       
HET    SO4  B 402       5                                                       
HET    GOL  B 403       6                                                       
HET     CL  B 404       1                                                       
HET    GOL  B 405       6                                                       
HET    GOL  B 406       6                                                       
HET    GOL  B 407       6                                                       
HET    BAM  B 408       9                                                       
HET    SO4  C 401       5                                                       
HET    SO4  C 402       5                                                       
HET    GOL  C 403       6                                                       
HET    GOL  C 404       6                                                       
HET     CL  C 405       1                                                       
HET    BAM  C 406       9                                                       
HET    SO4  D 401       5                                                       
HET    GOL  D 402       6                                                       
HET     CL  D 403       1                                                       
HET    GOL  D 404       6                                                       
HET    GOL  D 405       6                                                       
HET    GOL  D 406       6                                                       
HET     CL  D 407       1                                                       
HET    PE3  D 408      13                                                       
HET    BAM  D 409       9                                                       
HET     CL  E 401       1                                                       
HET    GOL  E 402       6                                                       
HET    GOL  E 403       6                                                       
HET    GOL  E 404       6                                                       
HET    GOL  E 405       6                                                       
HET    BAM  E 406       9                                                       
HET    GOL  F 401       6                                                       
HET    GOL  F 402       6                                                       
HET    GOL  F 403       6                                                       
HET     CL  F 404       1                                                       
HET    BAM  F 405       9                                                       
HET    SO4  G 401       5                                                       
HET    GOL  G 402       6                                                       
HET    GOL  G 403       6                                                       
HET     CL  G 404       1                                                       
HET    GOL  G 405       6                                                       
HET    GOL  G 406       6                                                       
HET    GOL  G 407       6                                                       
HET    GOL  G 408       6                                                       
HET    BAM  G 409       9                                                       
HET    SO4  H 401       5                                                       
HET    SO4  H 402       5                                                       
HET    GOL  H 403       6                                                       
HET    GOL  H 404       6                                                       
HET    PE3  H 405       7                                                       
HET    BAM  H 406       9                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PE3 3,6,9,12,15,18,21,24,27,30,33,36,39-                             
HETNAM   2 PE3  TRIDECAOXAHENTETRACONTANE-1,41-DIOL                             
HETNAM     BAM BENZAMIDINE                                                      
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     PE3 POLYETHYLENE GLYCOL                                              
FORMUL   9  SO4    10(O4 S 2-)                                                  
FORMUL  11  GOL    27(C3 H8 O3)                                                 
FORMUL  12   CL    8(CL 1-)                                                     
FORMUL  14  PE3    3(C28 H58 O15)                                               
FORMUL  15  BAM    8(C7 H9 N2 1+)                                               
FORMUL  65  HOH   *2409(H2 O)                                                   
HELIX    1 AA1 LEU A    3  GLY A   20  1                                  18    
HELIX    2 AA2 ARG A   23  LEU A   27  5                                   5    
HELIX    3 AA3 PRO A   28  GLU A   44  1                                  17    
HELIX    4 AA4 ILE A   96  THR A   98  5                                   3    
HELIX    5 AA5 HIS A   99  ARG A  111  1                                  13    
HELIX    6 AA6 PRO A  128  ASN A  144  1                                  17    
HELIX    7 AA7 ALA A  145  PHE A  148  5                                   4    
HELIX    8 AA8 SER A  161  GLY A  178  1                                  18    
HELIX    9 AA9 SER A  198  PHE A  204  1                                   7    
HELIX   10 AB1 SER A  211  VAL A  223  1                                  13    
HELIX   11 AB2 SER A  235  ALA A  239  5                                   5    
HELIX   12 AB3 LEU A  258  ALA A  272  1                                  15    
HELIX   13 AB4 LEU A  295  GLY A  314  1                                  20    
HELIX   14 AB5 LEU B    3  GLY B   20  1                                  18    
HELIX   15 AB6 ARG B   23  LEU B   27  5                                   5    
HELIX   16 AB7 PRO B   28  GLU B   44  1                                  17    
HELIX   17 AB8 ILE B   96  THR B   98  5                                   3    
HELIX   18 AB9 HIS B   99  ARG B  111  1                                  13    
HELIX   19 AC1 PRO B  128  ASN B  144  1                                  17    
HELIX   20 AC2 ALA B  145  PHE B  148  5                                   4    
HELIX   21 AC3 SER B  161  GLY B  178  1                                  18    
HELIX   22 AC4 SER B  198  PHE B  204  1                                   7    
HELIX   23 AC5 SER B  211  VAL B  223  1                                  13    
HELIX   24 AC6 SER B  235  ALA B  239  5                                   5    
HELIX   25 AC7 LEU B  258  ALA B  272  1                                  15    
HELIX   26 AC8 LEU B  295  GLY B  314  1                                  20    
HELIX   27 AC9 LEU C    3  GLY C   20  1                                  18    
HELIX   28 AD1 ARG C   23  LEU C   27  5                                   5    
HELIX   29 AD2 PRO C   28  GLU C   44  1                                  17    
HELIX   30 AD3 ILE C   96  THR C   98  5                                   3    
HELIX   31 AD4 HIS C   99  ARG C  111  1                                  13    
HELIX   32 AD5 PRO C  128  ASN C  144  1                                  17    
HELIX   33 AD6 ALA C  145  PHE C  148  5                                   4    
HELIX   34 AD7 SER C  161  ALA C  177  1                                  17    
HELIX   35 AD8 SER C  198  PHE C  204  1                                   7    
HELIX   36 AD9 SER C  211  VAL C  223  1                                  13    
HELIX   37 AE1 SER C  235  ALA C  239  5                                   5    
HELIX   38 AE2 LEU C  258  ALA C  272  1                                  15    
HELIX   39 AE3 LEU C  295  PHE C  313  1                                  19    
HELIX   40 AE4 LEU D    3  GLY D   20  1                                  18    
HELIX   41 AE5 ARG D   23  LEU D   27  5                                   5    
HELIX   42 AE6 PRO D   28  GLU D   44  1                                  17    
HELIX   43 AE7 ILE D   96  THR D   98  5                                   3    
HELIX   44 AE8 HIS D   99  ARG D  111  1                                  13    
HELIX   45 AE9 PRO D  128  ASN D  144  1                                  17    
HELIX   46 AF1 ALA D  145  PHE D  148  5                                   4    
HELIX   47 AF2 SER D  161  ALA D  177  1                                  17    
HELIX   48 AF3 SER D  198  PHE D  204  1                                   7    
HELIX   49 AF4 SER D  211  VAL D  223  1                                  13    
HELIX   50 AF5 SER D  235  ALA D  239  5                                   5    
HELIX   51 AF6 LEU D  258  ALA D  272  1                                  15    
HELIX   52 AF7 LEU D  295  PHE D  313  1                                  19    
HELIX   53 AF8 LEU E    3  GLY E   19  1                                  17    
HELIX   54 AF9 ARG E   23  LEU E   27  5                                   5    
HELIX   55 AG1 PRO E   28  GLU E   44  1                                  17    
HELIX   56 AG2 ILE E   96  THR E   98  5                                   3    
HELIX   57 AG3 HIS E   99  ARG E  111  1                                  13    
HELIX   58 AG4 PRO E  128  ASN E  144  1                                  17    
HELIX   59 AG5 ALA E  145  PHE E  148  5                                   4    
HELIX   60 AG6 SER E  161  GLY E  178  1                                  18    
HELIX   61 AG7 SER E  198  PHE E  204  1                                   7    
HELIX   62 AG8 SER E  211  VAL E  223  1                                  13    
HELIX   63 AG9 SER E  235  ALA E  239  5                                   5    
HELIX   64 AH1 LEU E  258  ALA E  272  1                                  15    
HELIX   65 AH2 LEU E  295  GLY E  314  1                                  20    
HELIX   66 AH3 LEU F    3  GLY F   20  1                                  18    
HELIX   67 AH4 ARG F   23  LEU F   27  5                                   5    
HELIX   68 AH5 PRO F   28  GLU F   44  1                                  17    
HELIX   69 AH6 ILE F   96  THR F   98  5                                   3    
HELIX   70 AH7 HIS F   99  ARG F  111  1                                  13    
HELIX   71 AH8 PRO F  128  ASN F  144  1                                  17    
HELIX   72 AH9 ALA F  145  PHE F  148  5                                   4    
HELIX   73 AI1 SER F  161  GLY F  178  1                                  18    
HELIX   74 AI2 SER F  198  PHE F  204  1                                   7    
HELIX   75 AI3 SER F  211  VAL F  223  1                                  13    
HELIX   76 AI4 SER F  235  ALA F  239  5                                   5    
HELIX   77 AI5 LEU F  258  ALA F  272  1                                  15    
HELIX   78 AI6 LEU F  295  GLY F  314  1                                  20    
HELIX   79 AI7 LEU G    3  GLY G   20  1                                  18    
HELIX   80 AI8 ARG G   23  LEU G   27  5                                   5    
HELIX   81 AI9 PRO G   28  GLU G   44  1                                  17    
HELIX   82 AJ1 ILE G   96  THR G   98  5                                   3    
HELIX   83 AJ2 HIS G   99  ARG G  111  1                                  13    
HELIX   84 AJ3 PRO G  128  ASN G  144  1                                  17    
HELIX   85 AJ4 ALA G  145  PHE G  148  5                                   4    
HELIX   86 AJ5 SER G  161  ALA G  177  1                                  17    
HELIX   87 AJ6 SER G  198  PHE G  204  1                                   7    
HELIX   88 AJ7 SER G  211  VAL G  223  1                                  13    
HELIX   89 AJ8 SER G  235  ALA G  239  5                                   5    
HELIX   90 AJ9 LEU G  258  ALA G  272  1                                  15    
HELIX   91 AK1 LEU G  295  PHE G  313  1                                  19    
HELIX   92 AK2 LEU H    3  GLY H   20  1                                  18    
HELIX   93 AK3 ARG H   23  LEU H   27  5                                   5    
HELIX   94 AK4 PRO H   28  GLU H   44  1                                  17    
HELIX   95 AK5 ILE H   96  THR H   98  5                                   3    
HELIX   96 AK6 HIS H   99  ARG H  111  1                                  13    
HELIX   97 AK7 PRO H  128  ASN H  144  1                                  17    
HELIX   98 AK8 ALA H  145  PHE H  148  5                                   4    
HELIX   99 AK9 SER H  161  GLY H  178  1                                  18    
HELIX  100 AL1 SER H  198  PHE H  204  1                                   7    
HELIX  101 AL2 SER H  211  VAL H  223  1                                  13    
HELIX  102 AL3 SER H  235  ALA H  239  5                                   5    
HELIX  103 AL4 LEU H  258  ALA H  272  1                                  15    
HELIX  104 AL5 LEU H  295  GLY H  314  1                                  20    
SHEET    1 AA116 GLU A  52  ALA A  59  0                                        
SHEET    2 AA116 GLU A  64  ARG A  71 -1  O  ILE A  65   N  PHE A  58           
SHEET    3 AA116 GLN A 113  ASP A 118 -1  O  VAL A 114   N  TYR A  70           
SHEET    4 AA116 LEU A  80  TYR A  86  1  N  LEU A  83   O  GLN A 113           
SHEET    5 AA116 ALA A 150  ASP A 160  1  O  ALA A 156   N  THR A  82           
SHEET    6 AA116 PHE A 184  ILE A 188  1  O  ILE A 188   N  GLY A 159           
SHEET    7 AA116 ALA A 248  ALA A 253  1  O  PHE A 249   N  LEU A 187           
SHEET    8 AA116 THR A 276  TYR A 281  1  O  THR A 277   N  VAL A 250           
SHEET    9 AA116 THR H 276  TYR H 281 -1  O  TYR H 278   N  TYR A 278           
SHEET   10 AA116 ALA H 248  ALA H 253  1  N  VAL H 250   O  THR H 277           
SHEET   11 AA116 PHE H 184  ILE H 188  1  N  LEU H 187   O  PHE H 249           
SHEET   12 AA116 ALA H 150  ASP H 160  1  N  GLY H 159   O  ILE H 188           
SHEET   13 AA116 LEU H  80  TYR H  86  1  N  THR H  82   O  ALA H 156           
SHEET   14 AA116 GLN H 113  ASP H 118  1  O  ILE H 115   N  TYR H  85           
SHEET   15 AA116 GLU H  64  ARG H  71 -1  N  TYR H  70   O  VAL H 114           
SHEET   16 AA116 GLU H  52  ALA H  59 -1  N  GLY H  56   O  PHE H  67           
SHEET    1 AA232 GLU B  52  ALA B  59  0                                        
SHEET    2 AA232 GLU B  64  ARG B  71 -1  O  ILE B  65   N  PHE B  58           
SHEET    3 AA232 GLN B 113  ASP B 118 -1  O  ASP B 118   N  ARG B  66           
SHEET    4 AA232 LEU B  80  TYR B  86  1  N  LEU B  83   O  GLN B 113           
SHEET    5 AA232 ALA B 150  ASP B 160  1  O  ALA B 156   N  THR B  82           
SHEET    6 AA232 PHE B 184  ILE B 188  1  O  MET B 186   N  VAL B 157           
SHEET    7 AA232 ALA B 248  ALA B 253  1  O  PHE B 249   N  LEU B 187           
SHEET    8 AA232 THR B 276  TYR B 281  1  O  THR B 277   N  VAL B 250           
SHEET    9 AA232 THR E 276  TYR E 281 -1  O  TYR E 278   N  TYR B 278           
SHEET   10 AA232 ALA E 248  ALA E 253  1  N  VAL E 250   O  THR E 277           
SHEET   11 AA232 PHE E 184  ILE E 188  1  N  LEU E 187   O  PHE E 249           
SHEET   12 AA232 ALA E 150  ASP E 160  1  N  GLY E 159   O  ILE E 188           
SHEET   13 AA232 LEU E  80  TYR E  86  1  N  THR E  82   O  ALA E 156           
SHEET   14 AA232 GLN E 113  ASP E 118  1  O  GLN E 113   N  LEU E  83           
SHEET   15 AA232 GLU E  64  ARG E  71 -1  N  TYR E  70   O  VAL E 114           
SHEET   16 AA232 GLU E  52  ALA E  59 -1  N  PHE E  58   O  ILE E  65           
SHEET   17 AA232 GLU G  52  ALA G  59 -1  O  ASN G  55   N  VAL E  53           
SHEET   18 AA232 GLU G  64  ARG G  71 -1  O  ILE G  65   N  PHE G  58           
SHEET   19 AA232 GLN G 113  ASP G 118 -1  O  VAL G 114   N  TYR G  70           
SHEET   20 AA232 LEU G  80  TYR G  86  1  N  LEU G  83   O  GLN G 113           
SHEET   21 AA232 ALA G 150  ASP G 160  1  O  ALA G 156   N  ILE G  84           
SHEET   22 AA232 PHE G 184  ILE G 188  1  O  ILE G 188   N  GLY G 159           
SHEET   23 AA232 ALA G 248  ALA G 253  1  O  PHE G 249   N  LEU G 187           
SHEET   24 AA232 THR G 276  TYR G 281  1  O  THR G 277   N  VAL G 250           
SHEET   25 AA232 THR D 276  TYR D 281 -1  N  TYR D 278   O  TYR G 278           
SHEET   26 AA232 ALA D 248  ALA D 253  1  N  VAL D 250   O  THR D 277           
SHEET   27 AA232 PHE D 184  ILE D 188  1  N  LEU D 187   O  PHE D 249           
SHEET   28 AA232 ALA D 150  ASP D 160  1  N  VAL D 157   O  MET D 186           
SHEET   29 AA232 LEU D  80  TYR D  86  1  N  THR D  82   O  ALA D 156           
SHEET   30 AA232 GLN D 113  ASP D 118  1  O  GLN D 113   N  LEU D  83           
SHEET   31 AA232 GLU D  64  ARG D  71 -1  N  TYR D  70   O  VAL D 114           
SHEET   32 AA232 GLU D  52  ALA D  59 -1  N  PHE D  58   O  ILE D  65           
SHEET    1 AA316 GLU C  52  ALA C  59  0                                        
SHEET    2 AA316 GLU C  64  ARG C  71 -1  O  ILE C  65   N  PHE C  58           
SHEET    3 AA316 GLN C 113  ASP C 118 -1  O  ASP C 118   N  ARG C  66           
SHEET    4 AA316 LEU C  80  TYR C  86  1  N  LEU C  83   O  GLN C 113           
SHEET    5 AA316 ALA C 150  ASP C 160  1  O  ALA C 156   N  THR C  82           
SHEET    6 AA316 PHE C 184  ILE C 188  1  O  ILE C 188   N  GLY C 159           
SHEET    7 AA316 ALA C 248  ALA C 253  1  O  PHE C 249   N  LEU C 187           
SHEET    8 AA316 THR C 276  TYR C 281  1  O  THR C 277   N  VAL C 250           
SHEET    9 AA316 THR F 276  TYR F 281 -1  O  TYR F 278   N  TYR C 278           
SHEET   10 AA316 ALA F 248  ALA F 253  1  N  VAL F 250   O  THR F 277           
SHEET   11 AA316 PHE F 184  ILE F 188  1  N  LEU F 187   O  PHE F 249           
SHEET   12 AA316 ALA F 150  ASP F 160  1  N  GLY F 159   O  ILE F 188           
SHEET   13 AA316 LEU F  80  TYR F  86  1  N  ILE F  84   O  ALA F 156           
SHEET   14 AA316 GLN F 113  ASP F 118  1  O  GLN F 113   N  LEU F  83           
SHEET   15 AA316 GLU F  64  ARG F  71 -1  N  TYR F  70   O  VAL F 114           
SHEET   16 AA316 GLU F  52  ALA F  59 -1  N  PHE F  58   O  ILE F  65           
CISPEP   1 ALA A  122    PRO A  123          0         1.07                     
CISPEP   2 PHE A  127    PRO A  128          0         5.01                     
CISPEP   3 ALA B  122    PRO B  123          0         3.15                     
CISPEP   4 PHE B  127    PRO B  128          0         1.87                     
CISPEP   5 ALA C  122    PRO C  123          0         2.37                     
CISPEP   6 PHE C  127    PRO C  128          0         1.90                     
CISPEP   7 ALA D  122    PRO D  123          0         2.65                     
CISPEP   8 PHE D  127    PRO D  128          0         3.41                     
CISPEP   9 ALA E  122    PRO E  123          0         3.02                     
CISPEP  10 PHE E  127    PRO E  128          0         3.50                     
CISPEP  11 ALA F  122    PRO F  123          0         2.29                     
CISPEP  12 PHE F  127    PRO F  128          0         2.67                     
CISPEP  13 ALA G  122    PRO G  123          0         1.88                     
CISPEP  14 PHE G  127    PRO G  128          0         2.62                     
CISPEP  15 ALA H  122    PRO H  123          0         2.71                     
CISPEP  16 PHE H  127    PRO H  128          0         3.72                     
SITE     1 AC1  5 LYS A 275  HIS A 312  HOH A 552  GLN H 297                    
SITE     2 AC1  5 LYS H 300                                                     
SITE     1 AC2  7 ARG A 263  ASP A 267  ILE A 270  TYR A 278                    
SITE     2 AC2  7 ARG H 263  ASP H 267  ILE H 270                               
SITE     1 AC3  5 GLN A  -1  LEU A  10  ASP A  11  ASP A  14                    
SITE     2 AC3  5 GLY A 207                                                     
SITE     1 AC4  1 HIS A  29                                                     
SITE     1 AC5  8 GLU A  52  ARG A  69  ARG A  71  GLY A  78                    
SITE     2 AC5  8 HOH A 501  HOH A 533  ARG C  69  SER C 147                    
SITE     1 AC6  4 ARG A 105  LEU A 299  HOH A 562  GLY B  19                    
SITE     1 AC7  7 GLY A  89  GLY A  90  SER A 161  ALA A 162                    
SITE     2 AC7  7 LEU A 210  MET A 215  HIS A 286                               
SITE     1 AC8  5 GLN B 297  LYS B 300  HOH B 539  LYS E 275                    
SITE     2 AC8  5 HIS E 312                                                     
SITE     1 AC9  5 LYS B 275  HIS B 312  HOH B 529  GLN E 297                    
SITE     2 AC9  5 LYS E 300                                                     
SITE     1 AD1  4 GLU B  25  LEU B  27   CL B 404  HOH B 614                    
SITE     1 AD2  2 HIS B  29  GOL B 403                                          
SITE     1 AD3  5 GLN B  -1  ASP B  11  GLY B 207  HOH B 516                    
SITE     2 AD3  5 HOH B 659                                                     
SITE     1 AD4  7 ARG B  69  ARG B  71  GLY B  78  SER B 147                    
SITE     2 AD4  7 ARG D  69  GLU D 146  SER D 147                               
SITE     1 AD5  3 ARG B  21  PRO B  22  ALA B  35                               
SITE     1 AD6  6 GLY B  88  GLY B  89  GLY B  90  SER B 161                    
SITE     2 AD6  6 ALA B 162  HIS B 286                                          
SITE     1 AD7  5 LYS C 275  HIS C 312  HOH C 505  GLN F 297                    
SITE     2 AD7  5 LYS F 300                                                     
SITE     1 AD8  6 GLN C 297  LYS C 300  HOH C 508  HOH C 571                    
SITE     2 AD8  6 LYS F 275  HIS F 312                                          
SITE     1 AD9  7 ASN A  55  ARG A  66  GLU C  49  VAL C  50                    
SITE     2 AD9  7 VAL C  53  ARG C 104  HOH C 516                               
SITE     1 AE1  6 ALA C  62  ARG C 120  ALA C 129  ASP C 132                    
SITE     2 AE1  6 HOH C 503  HOH C 559                                          
SITE     1 AE2  7 GLY C  88  GLY C  89  GLY C  90  SER C 161                    
SITE     2 AE2  7 ALA C 162  LEU C 210  HIS C 286                               
SITE     1 AE3  6 LYS D 275  HIS D 312  HOH D 522  HOH D 613                    
SITE     2 AE3  6 GLN G 297  LYS G 300                                          
SITE     1 AE4  3 ARG D  21  PRO D  22  MET D  39                               
SITE     1 AE5  3 HIS D  29  GOL D 404  HOH D 555                               
SITE     1 AE6  9 GLU D  25  LEU D  27  PRO D  28  HIS D  29                    
SITE     2 AE6  9 TRP D 217   CL D 403  HOH D 541  HOH D 555                    
SITE     3 AE6  9 HOH D 736                                                     
SITE     1 AE7  5 GLN D  -1  ARG D   7  LEU D  10  ASP D  11                    
SITE     2 AE7  5 GLY D 207                                                     
SITE     1 AE8  5 ALA D  62  ARG D 120  ALA D 129  ASP D 132                    
SITE     2 AE8  5 HOH D 595                                                     
SITE     1 AE9  4 ASP D 231  LEU D 232  HOH D 750  HOH D 785                    
SITE     1 AF1  9 ALA C  45  THR C 292  ARG C 293  HOH C 565                    
SITE     2 AF1  9 LEU D  12  ARG D  21  MET D  39  PHE D 209                    
SITE     3 AF1  9 HOH D 647                                                     
SITE     1 AF2  7 GLY D  89  GLY D  90  SER D 161  ALA D 162                    
SITE     2 AF2  7 LEU D 210  MET D 215  HIS D 286                               
SITE     1 AF3  1 HIS E  29                                                     
SITE     1 AF4  8 GLU E  49  VAL E  50  VAL E  53  ARG E 104                    
SITE     2 AF4  8 HOH E 600  ASN G  55  GLY G  56  ARG G  66                    
SITE     1 AF5  2 ARG E 105  LYS E 109                                          
SITE     1 AF6  7 ASN E  55  GLY E  56  ARG E  66  PHE E  67                    
SITE     2 AF6  7 ARG E  68  ILE E  96  GLU E  97                               
SITE     1 AF7  5 GLN E  -1  ARG E   7  ASP E  11  GLY E 207                    
SITE     2 AF7  5 HOH E 647                                                     
SITE     1 AF8  5 GLY E  89  GLY E  90  SER E 161  ALA E 162                    
SITE     2 AF8  5 HIS E 286                                                     
SITE     1 AF9  7 ARG C 263  ASP C 267  ILE C 270  ARG F 263                    
SITE     2 AF9  7 ASP F 267  ILE F 270  TYR F 278                               
SITE     1 AG1  4 GLU F  49  VAL F  50  VAL F  53  ARG F 104                    
SITE     1 AG2  3 GLY F 207  HOH F 506  HOH F 636                               
SITE     1 AG3  2 ARG F 105  HOH F 673                                          
SITE     1 AG4  8 GLY F  88  GLY F  89  GLY F  90  SER F 161                    
SITE     2 AG4  8 ALA F 162  MET F 215  HIS F 286  HOH F 790                    
SITE     1 AG5  6 GLN D 297  LYS D 300  LYS G 275  HIS G 312                    
SITE     2 AG5  6 HOH G 557  HOH G 583                                          
SITE     1 AG6  6 ASN E  55  ARG E  66  GLU G  49  VAL G  50                    
SITE     2 AG6  6 VAL G  53  ARG G 104                                          
SITE     1 AG7  2 ARG G 105  LYS G 109                                          
SITE     1 AG8  1 HIS G  29                                                     
SITE     1 AG9  5 GLN G  -1  LEU G   2  ASP G  11  GLY G 207                    
SITE     2 AG9  5 HOH G 511                                                     
SITE     1 AH1  5 LEU E  79  GLU E 146  LEU G  79  GLU G 146                    
SITE     2 AH1  5 HOH G 594                                                     
SITE     1 AH2  5 ILE D 270  ARG G 259  ASP G 260  ARG G 263                    
SITE     2 AH2  5 HOH G 647                                                     
SITE     1 AH3  6 ARG D 263  ASP D 267  ARG G 263  ASP G 267                    
SITE     2 AH3  6 ILE G 270  TYR G 278                                          
SITE     1 AH4  6 GLY G  88  GLY G  89  GLY G  90  SER G 161                    
SITE     2 AH4  6 ALA G 162  HIS G 286                                          
SITE     1 AH5  5 GLN A 297  LYS A 300  LYS H 275  HIS H 312                    
SITE     2 AH5  5 HOH H 548                                                     
SITE     1 AH6  2 ARG H 105  GOL H 403                                          
SITE     1 AH7  7 GLY A 314  HOH A 528  SER H 296  LEU H 299                    
SITE     2 AH7  7 SO4 H 402  HOH H 583  HOH H 632                               
SITE     1 AH8  5 ARG H 175  LEU H 232  ALA H 239  THR H 240                    
SITE     2 AH8  5 ASP H 241                                                     
SITE     1 AH9  5 ILE A 270  ARG H 259  ASP H 260  ARG H 263                    
SITE     2 AH9  5 ASN H 280                                                     
SITE     1 AI1  6 GLY H  89  GLY H  90  SER H 161  ALA H 162                    
SITE     2 AI1  6 MET H 215  HIS H 286                                          
CRYST1   90.275   90.098  110.760  68.02  79.60  67.57 P 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      0.011077 -0.004573 -0.000528        0.00000                         
SCALE2      0.000000  0.012008 -0.004282        0.00000                         
SCALE3      0.000000  0.000000  0.009746        0.00000                         
TER    2409      THR A 315                                                      
TER    4818      THR B 315                                                      
TER    7232      THR C 315                                                      
TER    9636      THR D 315                                                      
TER   12046      THR E 315                                                      
TER   14450      THR F 315                                                      
TER   16866      THR G 315                                                      
TER   19270      THR H 315                                                      
MASTER     1113    0   56  104   64    0   96    621957    8  316  208          
END                                                                             

Send your questions or comments to :
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
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer