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LongText Report for: 8hgw-pdb

Name Class
8hgw-pdb
HEADER    HYDROLASE                               15-NOV-22   8HGW              
TITLE     CRYSTAL STRUCTURE OF MEHPH IN COMPLEX WITH MBP                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MONOALKYL PHTHALATE HYDROLASE;                             
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GORDONIA;                                       
SOURCE   3 ORGANISM_TAXID: 2053;                                                
SOURCE   4 GENE: MEHPH;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    HYDROLASE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Z.M.ZHANG,Y.J.WANG,Y.B.CHEN                                           
REVDAT   1   15-MAR-23 8HGW    0                                                
JRNL        AUTH   Y.CHEN,Y.WANG,Y.XU,J.SUN,L.YANG,C.FENG,J.WANG,Y.ZHOU,        
JRNL        AUTH 2 Z.M.ZHANG,Y.WANG                                             
JRNL        TITL   MOLECULAR INSIGHTS INTO THE CATALYTIC MECHANISM OF           
JRNL        TITL 2 PLASTICIZER DEGRADATION BY A MONOALKYL PHTHALATE HYDROLASE.  
JRNL        REF    COMMUN CHEM                   V.   6    45 2023              
JRNL        REFN                   ESSN 2399-3669                               
JRNL        PMID   36859434                                                     
JRNL        DOI    10.1038/S42004-023-00846-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692+SVN                                  
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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.348                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 28590                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.229                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.260                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.054                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1445                            
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 10.0000 -  6.0278    0.99     2801   170  0.1804 0.2204        
REMARK   3     2  6.0278 -  4.7863    1.00     2724   153  0.2075 0.2161        
REMARK   3     3  4.7863 -  4.1818    1.00     2750   137  0.1810 0.2149        
REMARK   3     4  4.1818 -  3.7997    1.00     2696   144  0.2135 0.2286        
REMARK   3     5  3.7997 -  3.5275    1.00     2692   148  0.2218 0.2556        
REMARK   3     6  3.5275 -  3.3196    1.00     2718   143  0.2549 0.2971        
REMARK   3     7  3.3196 -  3.1534    1.00     2706   128  0.2717 0.3234        
REMARK   3     8  3.1534 -  3.0162    1.00     2685   138  0.2915 0.3245        
REMARK   3     9  3.0162 -  2.9001    1.00     2671   145  0.3130 0.3553        
REMARK   3    10  2.9001 -  2.8010    1.00     2702   139  0.3458 0.4112        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.422            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.845           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 43.90                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 53.46                          
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      :  0.005           8891                                  
REMARK   3   ANGLE     :  0.998          12133                                  
REMARK   3   CHIRALITY :  0.040           1358                                  
REMARK   3   PLANARITY :  0.008           1587                                  
REMARK   3   DIHEDRAL  : 15.733           3058                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 24 THROUGH 163 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):   2.7858   1.9486 -45.6246              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2956 T22:   0.6457                                     
REMARK   3      T33:   0.3117 T12:  -0.1146                                     
REMARK   3      T13:  -0.0625 T23:   0.0758                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4035 L22:   1.3351                                     
REMARK   3      L33:   2.7093 L12:  -0.0880                                     
REMARK   3      L13:  -0.4971 L23:   0.5394                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0215 S12:  -0.5587 S13:   0.0411                       
REMARK   3      S21:   0.2910 S22:  -0.0934 S23:  -0.0974                       
REMARK   3      S31:   0.2172 S32:   0.4164 S33:   0.0678                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 164 THROUGH 196 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1938   2.3584 -67.7862              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3001 T22:   0.5365                                     
REMARK   3      T33:   0.3974 T12:  -0.0950                                     
REMARK   3      T13:  -0.0601 T23:   0.0214                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1417 L22:   2.6235                                     
REMARK   3      L33:   4.5952 L12:  -0.0873                                     
REMARK   3      L13:  -0.1518 L23:  -0.1724                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0652 S12:   0.6481 S13:   0.8189                       
REMARK   3      S21:   0.1439 S22:   0.0751 S23:  -0.7710                       
REMARK   3      S31:  -0.0500 S32:   0.5200 S33:  -0.0726                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 197 THROUGH 311 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.5765  -0.2310 -54.0149              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2454 T22:   0.3157                                     
REMARK   3      T33:   0.3105 T12:  -0.1202                                     
REMARK   3      T13:   0.0018 T23:   0.0027                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0581 L22:   0.4391                                     
REMARK   3      L33:   2.0681 L12:  -1.0722                                     
REMARK   3      L13:   0.1633 L23:  -0.0767                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0381 S12:   0.1640 S13:  -0.0901                       
REMARK   3      S21:   0.0473 S22:  -0.1164 S23:  -0.0483                       
REMARK   3      S31:  -0.0482 S32:   0.2222 S33:   0.0874                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 24 THROUGH 163 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  13.9681  14.7742 -20.2042              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4719 T22:   1.2464                                     
REMARK   3      T33:   0.3173 T12:  -0.3227                                     
REMARK   3      T13:  -0.0750 T23:   0.0487                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4802 L22:   1.3021                                     
REMARK   3      L33:   1.7401 L12:   0.1077                                     
REMARK   3      L13:   0.1363 L23:   0.5954                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0004 S12:  -0.0514 S13:   0.0162                       
REMARK   3      S21:  -0.0723 S22:   0.0449 S23:  -0.0239                       
REMARK   3      S31:   0.6108 S32:  -0.4576 S33:  -0.1166                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 164 THROUGH 207 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   7.4057  30.9758  -9.1866              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2752 T22:   1.8134                                     
REMARK   3      T33:   0.7073 T12:   0.0040                                     
REMARK   3      T13:   0.2095 T23:   0.3313                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1332 L22:   0.6790                                     
REMARK   3      L33:   0.1536 L12:   0.8658                                     
REMARK   3      L13:  -0.1638 L23:  -0.0840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3419 S12:   0.5912 S13:   0.9840                       
REMARK   3      S21:  -0.1684 S22:   0.3690 S23:   0.4898                       
REMARK   3      S31:  -0.2596 S32:  -0.2850 S33:  -0.1871                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 208 THROUGH 311 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.5789  19.2187 -12.7030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3043 T22:   1.2661                                     
REMARK   3      T33:   0.3541 T12:  -0.2074                                     
REMARK   3      T13:   0.0064 T23:   0.0126                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4642 L22:   0.9476                                     
REMARK   3      L33:   0.9043 L12:   0.6479                                     
REMARK   3      L13:  -0.7799 L23:   0.1291                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1459 S12:  -0.3350 S13:  -0.0149                       
REMARK   3      S21:  -0.0374 S22:   0.2846 S23:  -0.0779                       
REMARK   3      S31:   0.2761 S32:  -0.4067 S33:  -0.0615                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 24 THROUGH 161 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -26.7494  -6.9615 -25.7494              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4073 T22:   0.7807                                     
REMARK   3      T33:   0.3283 T12:  -0.1951                                     
REMARK   3      T13:   0.0221 T23:   0.0355                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3649 L22:   2.4917                                     
REMARK   3      L33:   3.2148 L12:   0.1607                                     
REMARK   3      L13:  -1.5551 L23:  -0.9452                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3527 S12:  -0.0378 S13:   0.1109                       
REMARK   3      S21:   0.2019 S22:  -0.2690 S23:  -0.1360                       
REMARK   3      S31:  -0.6408 S32:   0.0686 S33:  -0.0557                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 162 THROUGH 196 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -17.8050 -26.2072 -20.0410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3414 T22:   1.3684                                     
REMARK   3      T33:   0.8053 T12:  -0.0497                                     
REMARK   3      T13:   0.0229 T23:   0.2736                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3325 L22:   4.7798                                     
REMARK   3      L33:   2.4407 L12:   0.5457                                     
REMARK   3      L13:   0.8032 L23:  -0.0088                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3599 S12:  -0.3805 S13:  -0.7154                       
REMARK   3      S21:  -0.3769 S22:  -0.0727 S23:   0.1725                       
REMARK   3      S31:   0.3137 S32:   0.4277 S33:   0.3074                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 197 THROUGH 311 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -29.2527 -14.6945 -18.0201              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3420 T22:   0.9875                                     
REMARK   3      T33:   0.3618 T12:  -0.1978                                     
REMARK   3      T13:   0.0191 T23:  -0.0286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8224 L22:   1.5971                                     
REMARK   3      L33:   1.0806 L12:   0.3742                                     
REMARK   3      L13:  -0.0038 L23:  -1.2401                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0381 S12:  -0.2539 S13:  -0.2150                       
REMARK   3      S21:   0.1956 S22:  -0.2301 S23:  -0.1323                       
REMARK   3      S31:  -0.1200 S32:   0.5098 S33:   0.1095                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 24 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -36.1765  26.0297 -59.6487              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4857 T22:   0.3757                                     
REMARK   3      T33:   0.5240 T12:   0.0761                                     
REMARK   3      T13:   0.0468 T23:  -0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2246 L22:   2.1702                                     
REMARK   3      L33:   2.9021 L12:  -0.0422                                     
REMARK   3      L13:  -0.2924 L23:  -0.5071                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0313 S12:  -0.0450 S13:   0.4589                       
REMARK   3      S21:   0.2218 S22:   0.1836 S23:   0.0742                       
REMARK   3      S31:  -0.8633 S32:  -0.2769 S33:  -0.2352                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 119 THROUGH 196 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -35.7276  11.6689 -59.1109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2215 T22:   0.4266                                     
REMARK   3      T33:   0.3362 T12:   0.0678                                     
REMARK   3      T13:  -0.0395 T23:   0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5195 L22:   2.5522                                     
REMARK   3      L33:   3.4466 L12:   0.6808                                     
REMARK   3      L13:  -1.1500 L23:  -0.9231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1143 S12:   0.2272 S13:  -0.1373                       
REMARK   3      S21:   0.1248 S22:   0.1226 S23:   0.1752                       
REMARK   3      S31:  -0.2064 S32:  -0.5516 S33:  -0.0093                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 197 THROUGH 311 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.5366  12.4627 -61.2733              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2721 T22:   0.3499                                     
REMARK   3      T33:   0.2874 T12:  -0.0217                                     
REMARK   3      T13:   0.0027 T23:  -0.0360                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8647 L22:   1.8476                                     
REMARK   3      L33:   2.3071 L12:  -0.2595                                     
REMARK   3      L13:   1.0589 L23:  -0.6933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0416 S12:   0.1429 S13:   0.0966                       
REMARK   3      S21:   0.1603 S22:  -0.0147 S23:   0.1855                       
REMARK   3      S31:  -0.1794 S32:  -0.3468 S33:   0.0132                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : 1                                           
REMARK   3   NCS GROUP : 1                                                      
REMARK   3    NCS OPERATOR : 1                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A'                                   
REMARK   3     SELECTION          : CHAIN 'B'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 2                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A'                                   
REMARK   3     SELECTION          : CHAIN 'C'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3    NCS OPERATOR : 3                                                  
REMARK   3     REFERENCE SELECTION: CHAIN 'A'                                   
REMARK   3     SELECTION          : CHAIN 'D'                                   
REMARK   3     ATOM PAIRS NUMBER  : NULL                                        
REMARK   3     RMSD               : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 8HGW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-NOV-22.                  
REMARK 100 THE DEPOSITION ID IS D_1300033596.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-OCT-22                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CAMD                               
REMARK 200  BEAMLINE                       : GCPCC                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97914                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32749                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.380                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.400                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: ALPHAFOLD2                                           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM BIS-TRIS, PH 6.2, 22% (W/V) PEG   
REMARK 280  3350 AND 250 MM MGCL2.6H2O, VAPOR DIFFUSION, HANGING DROP,          
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       4555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       28.51184            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       24.47500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      152.83811            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       28.51184            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       24.47500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000      152.83811            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21130 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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: 2630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20990 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000       76.95000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       48.95000            
REMARK 350   BIOMT3   2  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    23                                                      
REMARK 465     MET B    23                                                      
REMARK 465     GLY B   175                                                      
REMARK 465     GLY B   176                                                      
REMARK 465     MET C    23                                                      
REMARK 465     GLY C   175                                                      
REMARK 465     GLY C   176                                                      
REMARK 465     MET D    23                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  70    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  74    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 167    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 179    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 192    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 194    CG   OD1  OD2                                       
REMARK 470     GLU A 197    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 210    CG   CD   OE1  OE2                                  
REMARK 470     GLN B  86    CG   CD   OE1  NE2                                  
REMARK 470     GLU B  96    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 117    CG   CD   CE   NZ                                   
REMARK 470     GLU B 167    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 179    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 182    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 192    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 194    CG   OD1  OD2                                       
REMARK 470     GLU B 197    CG   CD   OE1  OE2                                  
REMARK 470     ASP B 198    CG   OD1  OD2                                       
REMARK 470     LYS B 205    CG   CD   CE   NZ                                   
REMARK 470     LEU B 207    CG   CD1  CD2                                       
REMARK 470     SER B 209    OG                                                  
REMARK 470     GLU B 210    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 212    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 221    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B 225    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 299    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 105    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 167    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU C 179    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 194    CG   OD1  OD2                                       
REMARK 470     GLU C 197    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 205    CG   CD   CE   NZ                                   
REMARK 470     GLU C 210    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 211    CG   CD   CE   NZ                                   
REMARK 470     LEU C 213    CG   CD1  CD2                                       
REMARK 470     GLU C 233    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 240    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C 244    CG   OD1  OD2                                       
REMARK 470     GLU D  88    CG   CD   OE1  OE2                                  
REMARK 470     GLU D  96    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 143    CG   CD   CE   NZ                                   
REMARK 470     GLU D 167    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 171    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D 179    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 192    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 194    CG   OD1  OD2                                       
REMARK 470     GLU D 197    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 205    CG   CD   CE   NZ                                   
REMARK 470     GLU D 210    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 225    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 233    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 299    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    GLN D    86     OG1  THR D    89              2.05            
REMARK 500   OE1  GLU C   192     OG   SER C   295              2.17            
REMARK 500   OE1  GLU B   105     OH   TYR B   138              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    SER A 125     -121.95     52.76                                   
REMARK 500    ASP A 244      -80.65    -97.21                                   
REMARK 500    SER B 125     -120.50     52.20                                   
REMARK 500    HIS B 226      -52.50   -120.39                                   
REMARK 500    ASP B 244      -80.13    -98.63                                   
REMARK 500    SER C 125     -122.97     53.36                                   
REMARK 500    ASP C 244      -80.59    -98.55                                   
REMARK 500    SER D 125     -122.23     52.63                                   
REMARK 500    ASN D 191       75.04   -115.35                                   
REMARK 500    ASP D 244      -80.53    -98.96                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  8HGW A   24   311  UNP    Q2MHH5   Q2MHH5_9ACTN    24    311             
DBREF  8HGW B   24   311  UNP    Q2MHH5   Q2MHH5_9ACTN    24    311             
DBREF  8HGW C   24   311  UNP    Q2MHH5   Q2MHH5_9ACTN    24    311             
DBREF  8HGW D   24   311  UNP    Q2MHH5   Q2MHH5_9ACTN    24    311             
SEQADV 8HGW MET A   23  UNP  Q2MHH5              INITIATING METHIONINE          
SEQADV 8HGW ASN A  259  UNP  Q2MHH5    ASP   259 CONFLICT                       
SEQADV 8HGW MET B   23  UNP  Q2MHH5              INITIATING METHIONINE          
SEQADV 8HGW ASN B  259  UNP  Q2MHH5    ASP   259 CONFLICT                       
SEQADV 8HGW MET C   23  UNP  Q2MHH5              INITIATING METHIONINE          
SEQADV 8HGW ASN C  259  UNP  Q2MHH5    ASP   259 CONFLICT                       
SEQADV 8HGW MET D   23  UNP  Q2MHH5              INITIATING METHIONINE          
SEQADV 8HGW ASN D  259  UNP  Q2MHH5    ASP   259 CONFLICT                       
SEQRES   1 A  289  MET PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG          
SEQRES   2 A  289  TYR PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU          
SEQRES   3 A  289  ILE HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY          
SEQRES   4 A  289  ILE GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU          
SEQRES   5 A  289  TYR GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY          
SEQRES   6 A  289  GLU THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL          
SEQRES   7 A  289  ASP ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN          
SEQRES   8 A  289  LEU GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG          
SEQRES   9 A  289  GLY GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO          
SEQRES  10 A  289  GLU MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR          
SEQRES  11 A  289  ALA ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE          
SEQRES  12 A  289  TYR GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA          
SEQRES  13 A  289  GLU LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN          
SEQRES  14 A  289  GLU GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR          
SEQRES  15 A  289  LYS TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA          
SEQRES  16 A  289  GLY TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER          
SEQRES  17 A  289  LEU SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA          
SEQRES  18 A  289  ASP ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY          
SEQRES  19 A  289  VAL ASN ASN ARG SER ALA PRO VAL SER MET GLY LYS GLY          
SEQRES  20 A  289  LEU PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER          
SEQRES  21 A  289  LEU TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER          
SEQRES  22 A  289  ASP GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE          
SEQRES  23 A  289  ILE SER LEU                                                  
SEQRES   1 B  289  MET PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG          
SEQRES   2 B  289  TYR PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU          
SEQRES   3 B  289  ILE HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY          
SEQRES   4 B  289  ILE GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU          
SEQRES   5 B  289  TYR GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY          
SEQRES   6 B  289  GLU THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL          
SEQRES   7 B  289  ASP ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN          
SEQRES   8 B  289  LEU GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG          
SEQRES   9 B  289  GLY GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO          
SEQRES  10 B  289  GLU MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR          
SEQRES  11 B  289  ALA ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE          
SEQRES  12 B  289  TYR GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA          
SEQRES  13 B  289  GLU LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN          
SEQRES  14 B  289  GLU GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR          
SEQRES  15 B  289  LYS TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA          
SEQRES  16 B  289  GLY TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER          
SEQRES  17 B  289  LEU SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA          
SEQRES  18 B  289  ASP ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY          
SEQRES  19 B  289  VAL ASN ASN ARG SER ALA PRO VAL SER MET GLY LYS GLY          
SEQRES  20 B  289  LEU PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER          
SEQRES  21 B  289  LEU TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER          
SEQRES  22 B  289  ASP GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE          
SEQRES  23 B  289  ILE SER LEU                                                  
SEQRES   1 C  289  MET PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG          
SEQRES   2 C  289  TYR PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU          
SEQRES   3 C  289  ILE HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY          
SEQRES   4 C  289  ILE GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU          
SEQRES   5 C  289  TYR GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY          
SEQRES   6 C  289  GLU THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL          
SEQRES   7 C  289  ASP ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN          
SEQRES   8 C  289  LEU GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG          
SEQRES   9 C  289  GLY GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO          
SEQRES  10 C  289  GLU MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR          
SEQRES  11 C  289  ALA ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE          
SEQRES  12 C  289  TYR GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA          
SEQRES  13 C  289  GLU LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN          
SEQRES  14 C  289  GLU GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR          
SEQRES  15 C  289  LYS TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA          
SEQRES  16 C  289  GLY TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER          
SEQRES  17 C  289  LEU SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA          
SEQRES  18 C  289  ASP ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY          
SEQRES  19 C  289  VAL ASN ASN ARG SER ALA PRO VAL SER MET GLY LYS GLY          
SEQRES  20 C  289  LEU PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER          
SEQRES  21 C  289  LEU TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER          
SEQRES  22 C  289  ASP GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE          
SEQRES  23 C  289  ILE SER LEU                                                  
SEQRES   1 D  289  MET PHE HIS THR VAL ASP VAL LYS GLY VAL GLN THR ARG          
SEQRES   2 D  289  TYR PHE ASP ASP GLY GLN ASP LYS ASP PRO ILE LEU LEU          
SEQRES   3 D  289  ILE HIS GLY GLY HIS PHE GLY PHE PHE ILE PRO VAL GLY          
SEQRES   4 D  289  ILE GLU SER TRP GLY ASN VAL LEU GLU ASP PHE GLY GLU          
SEQRES   5 D  289  TYR GLY ARG VAL LEU ALA VAL ASP LYS LEU GLY GLN GLY          
SEQRES   6 D  289  GLU THR GLY LEU PRO LEU ASN ASP GLU ASP TRP THR VAL          
SEQRES   7 D  289  ASP ALA VAL ALA GLU HIS VAL ALA ASN PHE ALA THR GLN          
SEQRES   8 D  289  LEU GLY LEU LYS ASN LEU THR LEU VAL GLY HIS SER ARG          
SEQRES   9 D  289  GLY GLY MET THR ALA VAL LEU LEU ALA LEU LYS TYR PRO          
SEQRES  10 D  289  GLU MET VAL LYS LYS LEU VAL ILE ILE SER SER ALA THR          
SEQRES  11 D  289  ALA ALA PRO ALA PRO PRO VAL GLY THR ASP MET ASP PHE          
SEQRES  12 D  289  TYR GLU ARG VAL GLU ARG THR ALA PRO GLY GLY SER ALA          
SEQRES  13 D  289  GLU LEU ILE ARG HIS TYR HIS ALA ALA GLN ALA VAL ASN          
SEQRES  14 D  289  GLU GLY ASP LEU PRO GLU ASP TYR ILE GLY ILE ALA THR          
SEQRES  15 D  289  LYS TRP LEU GLU SER GLU LYS GLN LEU ASP ALA VAL ALA          
SEQRES  16 D  289  GLY TYR ALA ARG ASN ALA GLU GLU HIS TRP LEU PRO SER          
SEQRES  17 D  289  LEU SER GLU GLY ARG ARG TRP VAL GLN GLU ARG LEU ALA          
SEQRES  18 D  289  ASP ALA GLY ILE PRO VAL PRO THR LEU VAL VAL TRP GLY          
SEQRES  19 D  289  VAL ASN ASN ARG SER ALA PRO VAL SER MET GLY LYS GLY          
SEQRES  20 D  289  LEU PHE ASP LEU ILE ALA ALA ASN THR LEU ASP SER SER          
SEQRES  21 D  289  LEU TYR LEU ILE ASN ASN ALA GLY HIS HIS VAL PHE SER          
SEQRES  22 D  289  ASP GLN ARG GLU LYS PHE ASN ALA ALA VAL GLY ALA PHE          
SEQRES  23 D  289  ILE SER LEU                                                  
HET    1BO  A 401       5                                                       
HET    PHT  A1000      12                                                       
HET    PHT  B1000      12                                                       
HET    PHT  C1000      12                                                       
HET    PHT  D1000      12                                                       
HETNAM     1BO 1-BUTANOL                                                        
HETNAM     PHT PHTHALIC ACID                                                    
HETSYN     1BO BUTAN-1-OL                                                       
FORMUL   5  1BO    C4 H10 O                                                     
FORMUL   6  PHT    4(C8 H6 O4)                                                  
HELIX    1 AA1 GLY A   61  GLY A   66  5                                   6    
HELIX    2 AA2 ASN A   67  PHE A   72  1                                   6    
HELIX    3 AA3 ASN A   94  TRP A   98  5                                   5    
HELIX    4 AA4 THR A   99  LEU A  114  1                                  16    
HELIX    5 AA5 SER A  125  TYR A  138  1                                  14    
HELIX    6 AA6 MET A  163  THR A  172  1                                  10    
HELIX    7 AA7 GLY A  176  ALA A  189  1                                  14    
HELIX    8 AA8 PRO A  196  SER A  209  1                                  14    
HELIX    9 AA9 SER A  209  ALA A  223  1                                  15    
HELIX   10 AB1 HIS A  226  ALA A  245  1                                  20    
HELIX   11 AB2 PRO A  263  ALA A  276  1                                  14    
HELIX   12 AB3 HIS A  292  GLN A  297  1                                   6    
HELIX   13 AB4 GLN A  297  SER A  310  1                                  14    
HELIX   14 AB5 GLY B   61  TRP B   65  5                                   5    
HELIX   15 AB6 GLY B   66  PHE B   72  1                                   7    
HELIX   16 AB7 ASN B   94  TRP B   98  5                                   5    
HELIX   17 AB8 THR B   99  LEU B  114  1                                  16    
HELIX   18 AB9 SER B  125  TYR B  138  1                                  14    
HELIX   19 AC1 MET B  163  THR B  172  1                                  10    
HELIX   20 AC2 ALA B  178  ALA B  189  1                                  12    
HELIX   21 AC3 PRO B  196  SER B  209  1                                  14    
HELIX   22 AC4 SER B  209  ALA B  223  1                                  15    
HELIX   23 AC5 HIS B  226  ALA B  243  1                                  18    
HELIX   24 AC6 PRO B  263  ALA B  276  1                                  14    
HELIX   25 AC7 HIS B  292  GLN B  297  1                                   6    
HELIX   26 AC8 GLN B  297  SER B  310  1                                  14    
HELIX   27 AC9 GLY C   61  TRP C   65  5                                   5    
HELIX   28 AD1 GLY C   66  PHE C   72  1                                   7    
HELIX   29 AD2 ASN C   94  TRP C   98  5                                   5    
HELIX   30 AD3 THR C   99  LEU C  114  1                                  16    
HELIX   31 AD4 SER C  125  TYR C  138  1                                  14    
HELIX   32 AD5 MET C  163  THR C  172  1                                  10    
HELIX   33 AD6 ALA C  178  ALA C  189  1                                  12    
HELIX   34 AD7 PRO C  196  SER C  209  1                                  14    
HELIX   35 AD8 SER C  209  ALA C  223  1                                  15    
HELIX   36 AD9 HIS C  226  ALA C  245  1                                  20    
HELIX   37 AE1 PRO C  263  THR C  278  1                                  16    
HELIX   38 AE2 HIS C  292  GLN C  297  1                                   6    
HELIX   39 AE3 GLN C  297  SER C  310  1                                  14    
HELIX   40 AE4 GLY D   61  GLY D   66  5                                   6    
HELIX   41 AE5 ASN D   67  PHE D   72  1                                   6    
HELIX   42 AE6 ASN D   94  TRP D   98  5                                   5    
HELIX   43 AE7 THR D   99  LEU D  114  1                                  16    
HELIX   44 AE8 SER D  125  TYR D  138  1                                  14    
HELIX   45 AE9 MET D  163  THR D  172  1                                  10    
HELIX   46 AF1 GLY D  176  ALA D  189  1                                  14    
HELIX   47 AF2 PRO D  196  SER D  209  1                                  14    
HELIX   48 AF3 SER D  209  ALA D  223  1                                  15    
HELIX   49 AF4 HIS D  226  ALA D  245  1                                  20    
HELIX   50 AF5 PRO D  263  THR D  278  1                                  16    
HELIX   51 AF6 HIS D  292  GLN D  297  1                                   6    
HELIX   52 AF7 GLN D  297  SER D  310  1                                  14    
SHEET    1 AA116 HIS A  25  VAL A  29  0                                        
SHEET    2 AA116 VAL A  32  ASP A  38 -1  O  THR A  34   N  VAL A  27           
SHEET    3 AA116 ARG A  77  VAL A  81 -1  O  ALA A  80   N  PHE A  37           
SHEET    4 AA116 PRO A  45  ILE A  49  1  N  ILE A  46   O  LEU A  79           
SHEET    5 AA116 LEU A 119  HIS A 124  1  O  VAL A 122   N  LEU A  47           
SHEET    6 AA116 VAL A 142  ILE A 148  1  O  VAL A 146   N  LEU A 121           
SHEET    7 AA116 THR A 251  GLY A 256  1  O  VAL A 254   N  ILE A 147           
SHEET    8 AA116 SER A 281  ILE A 286  1  O  TYR A 284   N  VAL A 253           
SHEET    9 AA116 SER D 281  ILE D 286 -1  O  LEU D 283   N  LEU A 285           
SHEET   10 AA116 THR D 251  GLY D 256  1  N  VAL D 253   O  TYR D 284           
SHEET   11 AA116 VAL D 142  ILE D 148  1  N  ILE D 147   O  VAL D 254           
SHEET   12 AA116 LEU D 119  HIS D 124  1  N  LEU D 121   O  VAL D 146           
SHEET   13 AA116 PRO D  45  ILE D  49  1  N  LEU D  47   O  THR D 120           
SHEET   14 AA116 ARG D  77  VAL D  81  1  O  LEU D  79   N  ILE D  46           
SHEET   15 AA116 VAL D  32  ASP D  38 -1  N  PHE D  37   O  ALA D  80           
SHEET   16 AA116 HIS D  25  VAL D  29 -1  N  VAL D  27   O  THR D  34           
SHEET    1 AA2 8 HIS B  25  VAL B  29  0                                        
SHEET    2 AA2 8 VAL B  32  ASP B  38 -1  O  THR B  34   N  VAL B  27           
SHEET    3 AA2 8 ARG B  77  VAL B  81 -1  O  ALA B  80   N  PHE B  37           
SHEET    4 AA2 8 PRO B  45  ILE B  49  1  N  ILE B  46   O  LEU B  79           
SHEET    5 AA2 8 LEU B 119  HIS B 124  1  O  VAL B 122   N  ILE B  49           
SHEET    6 AA2 8 VAL B 142  ILE B 148  1  O  VAL B 146   N  LEU B 121           
SHEET    7 AA2 8 THR B 251  GLY B 256  1  O  VAL B 254   N  ILE B 147           
SHEET    8 AA2 8 SER B 281  ILE B 286  1  O  TYR B 284   N  VAL B 253           
SHEET    1 AA3 8 HIS C  25  VAL C  29  0                                        
SHEET    2 AA3 8 VAL C  32  ASP C  38 -1  O  THR C  34   N  VAL C  27           
SHEET    3 AA3 8 ARG C  77  VAL C  81 -1  O  ALA C  80   N  PHE C  37           
SHEET    4 AA3 8 PRO C  45  ILE C  49  1  N  ILE C  46   O  LEU C  79           
SHEET    5 AA3 8 LEU C 119  HIS C 124  1  O  VAL C 122   N  LEU C  47           
SHEET    6 AA3 8 VAL C 142  ILE C 148  1  O  VAL C 146   N  LEU C 121           
SHEET    7 AA3 8 THR C 251  GLY C 256  1  O  VAL C 254   N  ILE C 147           
SHEET    8 AA3 8 SER C 281  ILE C 286  1  O  TYR C 284   N  VAL C 253           
LINK         CB  SER A 125                 O11 PHT A1000     1555   1555  1.39  
LINK         CB  SER B 125                 O11 PHT B1000     1555   1555  1.42  
LINK         CB  SER C 125                 O12 PHT C1000     1555   1555  1.41  
LINK         CB  SER D 125                 O11 PHT D1000     1555   1555  1.40  
CRYST1   76.950   48.950  306.325  90.00  93.73  90.00 I 1 2 1      16          
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      0.012995  0.000000  0.000847        0.00000                         
SCALE2      0.000000  0.020429  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003271        0.00000                         
TER    2180      LEU A 311                                                      
TER    4313      LEU B 311                                                      
TER    6465      LEU C 311                                                      
TER    8625      LEU D 311                                                      
MASTER      528    0    5   52   32    0    0    6 8674    4   57   92          
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
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