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Database: PDB
Entry: 4XTR
LinkDB: 4XTR
Original site: 4XTR 
HEADER    HYDROLASE/TRANSPORT PROTEIN             23-JAN-15   4XTR              
TITLE     STRUCTURE OF GET3 BOUND TO THE TRANSMEMBRANE DOMAIN OF PEP12          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ATPASE GET3;                                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: ARSENICAL PUMP-DRIVING ATPASE, ARSENITE-STIMULATED ATPASE,  
COMPND   5 GOLGI TO ER TRAFFIC PROTEIN 3, GUIDED ENTRY OF TAIL-ANCHORED PROTEINS
COMPND   6 3;                                                                   
COMPND   7 EC: 3.6.-.-;                                                         
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MUTATION: YES;                                                       
COMPND  10 MOL_ID: 2;                                                           
COMPND  11 MOLECULE: ANTIBODY HEAVY CHAIN;                                      
COMPND  12 CHAIN: C, E;                                                         
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: ANTIBODY LIGHT CHAIN;                                      
COMPND  16 CHAIN: D, F;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: PEP12P;                                                    
COMPND  20 CHAIN: G;                                                            
COMPND  21 FRAGMENT: UNP RESIDUES 102-128;                                      
COMPND  22 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /  
SOURCE   3 S288C);                                                              
SOURCE   4 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE   5 ORGANISM_TAXID: 559292;                                              
SOURCE   6 STRAIN: ATCC 204508 / S288C;                                         
SOURCE   7 GENE: GET3, ARR4, YDL100C, D2371;                                    
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  10 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PRIL;                            
SOURCE  11 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PCDF1B;                                   
SOURCE  13 MOL_ID: 2;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS, SYNTHETIC CONSTRUCT;              
SOURCE  15 ORGANISM_TAXID: 9606, 32630;                                         
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PRIL;                            
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: RH2.2;                                    
SOURCE  21 OTHER_DETAILS: OBTAINED BY PHAGE DISPLAY FROM A LIBRARY OF HUMAN IGG 
SOURCE  22 ANTIBODY FRAGMENT, THE CDRS ARE COMPLETELY SYNTHETIC;                
SOURCE  23 MOL_ID: 3;                                                           
SOURCE  24 ORGANISM_SCIENTIFIC: HOMO SAPIENS, SYNTHETIC CONSTRUCT;              
SOURCE  25 ORGANISM_TAXID: 9606, 32630;                                         
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PRIL;                            
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: RH2.2;                                    
SOURCE  31 OTHER_DETAILS: OBTAINED BY PHAGE DISPLAY FROM A LIBRARY OF HUMAN IGG 
SOURCE  32 ANTIBODY FRAGMENT, THE CDRS ARE COMPLETELY SYNTHETIC;                
SOURCE  33 MOL_ID: 4;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;                       
SOURCE  35 ORGANISM_COMMON: BAKER'S YEAST;                                      
SOURCE  36 ORGANISM_TAXID: 764099;                                              
SOURCE  37 STRAIN: VIN 13;                                                      
SOURCE  38 GENE: VIN13_4407;                                                    
SOURCE  39 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  40 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  41 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)/PRIL;                            
SOURCE  42 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  43 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    MEMBRANE PROTEIN TARGETING COMPLEX, HYDROLASE-TRANSPORT PROTEIN       
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.MATEJA,M.PADUCH,H.-Y.CHANG,A.SZYDLOWSKA,A.A.KOSSIAKOFF,R.S.HEGDE,   
AUTHOR   2 R.J.KEENAN                                                           
REVDAT   2   20-SEP-17 4XTR    1       SOURCE REMARK                            
REVDAT   1   18-MAR-15 4XTR    0                                                
JRNL        AUTH   A.MATEJA,M.PADUCH,H.Y.CHANG,A.SZYDLOWSKA,A.A.KOSSIAKOFF,     
JRNL        AUTH 2 R.S.HEGDE,R.J.KEENAN                                         
JRNL        TITL   PROTEIN TARGETING. STRUCTURE OF THE GET3 TARGETING FACTOR IN 
JRNL        TITL 2 COMPLEX WITH ITS MEMBRANE PROTEIN CARGO.                     
JRNL        REF    SCIENCE                       V. 347  1152 2015              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   25745174                                                     
JRNL        DOI    10.1126/SCIENCE.1261671                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: DEV_1839)                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 53.95                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 109280                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.216                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5469                            
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 61.5920 -  6.3678    0.96     3631   206  0.1922 0.1850        
REMARK   3     2  6.3678 -  5.0550    0.97     3539   197  0.1686 0.1877        
REMARK   3     3  5.0550 -  4.4162    0.98     3540   186  0.1353 0.1666        
REMARK   3     4  4.4162 -  4.0125    0.99     3551   181  0.1459 0.1868        
REMARK   3     5  4.0125 -  3.7250    0.97     3490   161  0.1648 0.1739        
REMARK   3     6  3.7250 -  3.5054    0.99     3516   204  0.1765 0.2001        
REMARK   3     7  3.5054 -  3.3299    0.99     3454   206  0.1878 0.2165        
REMARK   3     8  3.3299 -  3.1849    0.99     3522   187  0.1967 0.2344        
REMARK   3     9  3.1849 -  3.0623    0.99     3519   174  0.1987 0.2252        
REMARK   3    10  3.0623 -  2.9566    0.97     3434   171  0.1958 0.2555        
REMARK   3    11  2.9566 -  2.8642    0.99     3505   174  0.2039 0.2295        
REMARK   3    12  2.8642 -  2.7823    0.99     3496   192  0.1990 0.2436        
REMARK   3    13  2.7823 -  2.7091    0.99     3505   173  0.2061 0.2484        
REMARK   3    14  2.7091 -  2.6430    1.00     3504   186  0.1963 0.2340        
REMARK   3    15  2.6430 -  2.5829    1.00     3555   157  0.1994 0.2392        
REMARK   3    16  2.5829 -  2.5279    0.99     3482   192  0.2065 0.2565        
REMARK   3    17  2.5279 -  2.4774    1.00     3523   175  0.2041 0.2433        
REMARK   3    18  2.4774 -  2.4306    0.98     3443   176  0.2023 0.2439        
REMARK   3    19  2.4306 -  2.3872    0.99     3505   181  0.2069 0.2398        
REMARK   3    20  2.3872 -  2.3467    1.00     3472   199  0.2174 0.2509        
REMARK   3    21  2.3467 -  2.3089    1.00     3504   194  0.2172 0.2617        
REMARK   3    22  2.3089 -  2.2733    1.00     3467   202  0.2193 0.2623        
REMARK   3    23  2.2733 -  2.2399    0.99     3469   168  0.2276 0.2583        
REMARK   3    24  2.2399 -  2.2084    0.99     3493   193  0.2340 0.2571        
REMARK   3    25  2.2084 -  2.1785    0.98     3445   181  0.2327 0.2744        
REMARK   3    26  2.1785 -  2.1502    0.99     3472   165  0.2370 0.2913        
REMARK   3    27  2.1502 -  2.1233    0.97     3383   194  0.2492 0.2894        
REMARK   3    28  2.1233 -  2.0978    0.96     3347   166  0.2639 0.2951        
REMARK   3    29  2.0978 -  2.0734    0.91     3162   181  0.2791 0.3194        
REMARK   3    30  2.0734 -  2.0500    0.82     2883   147  0.2860 0.3308        
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)     : 0.230            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.230           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 56.79                          
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          12069                                  
REMARK   3   ANGLE     :  0.762          16378                                  
REMARK   3   CHIRALITY :  0.029           1856                                  
REMARK   3   PLANARITY :  0.003           2063                                  
REMARK   3   DIHEDRAL  : 13.330           4379                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 43                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 5 THROUGH 99 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  50.7494 -18.1404 -19.4768              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2046 T22:   0.4048                                     
REMARK   3      T33:   0.7003 T12:  -0.0056                                     
REMARK   3      T13:   0.0041 T23:   0.2222                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7690 L22:   2.5708                                     
REMARK   3      L33:   1.2161 L12:  -0.7567                                     
REMARK   3      L13:  -0.2469 L23:   0.4221                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0608 S12:  -0.1095 S13:   0.1307                       
REMARK   3      S21:   0.1461 S22:  -0.3739 S23:  -0.6255                       
REMARK   3      S31:   0.0312 S32:   0.2116 S33:   0.1713                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 100 THROUGH 153 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.0510 -13.4491  -3.1934              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5350 T22:   0.5420                                     
REMARK   3      T33:   0.6384 T12:  -0.0051                                     
REMARK   3      T13:  -0.1305 T23:   0.0647                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3232 L22:   4.9517                                     
REMARK   3      L33:   3.7333 L12:  -1.0589                                     
REMARK   3      L13:  -0.1945 L23:   0.9297                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3644 S12:  -0.5441 S13:  -0.0706                       
REMARK   3      S21:   0.6770 S22:  -0.0168 S23:  -0.9136                       
REMARK   3      S31:   0.3502 S32:   0.5201 S33:   0.2986                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 154 THROUGH 178 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  47.1143 -10.2146 -14.8124              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2965 T22:   0.4260                                     
REMARK   3      T33:   0.5993 T12:  -0.0409                                     
REMARK   3      T13:  -0.0476 T23:   0.2257                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5624 L22:   3.5829                                     
REMARK   3      L33:   1.8359 L12:  -1.2506                                     
REMARK   3      L13:  -1.6735 L23:   0.8203                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1215 S12:  -0.2725 S13:   0.1665                       
REMARK   3      S21:   0.2741 S22:  -0.1866 S23:  -0.4879                       
REMARK   3      S31:  -0.2588 S32:   0.2307 S33:   0.1896                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 179 THROUGH 211 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.7786   2.2995   1.7369              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6602 T22:   0.8462                                     
REMARK   3      T33:   0.8877 T12:  -0.1670                                     
REMARK   3      T13:   0.0230 T23:  -0.1837                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2621 L22:   6.5139                                     
REMARK   3      L33:   6.8632 L12:  -0.5461                                     
REMARK   3      L13:   1.7820 L23:  -1.0677                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0783 S12:  -0.9801 S13:   0.8721                       
REMARK   3      S21:   1.1374 S22:  -0.1063 S23:   0.1742                       
REMARK   3      S31:  -1.5470 S32:   0.1385 S33:   0.2370                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 212 THROUGH 230 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  53.4050  -0.3917  -3.1184              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6827 T22:   0.7166                                     
REMARK   3      T33:   1.0298 T12:  -0.2263                                     
REMARK   3      T13:  -0.2900 T23:   0.0506                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1362 L22:   4.5774                                     
REMARK   3      L33:   5.1237 L12:  -0.5719                                     
REMARK   3      L13:  -1.4121 L23:  -1.4340                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0863 S12:  -0.7909 S13:   0.4977                       
REMARK   3      S21:   1.3904 S22:  -0.5497 S23:  -0.4679                       
REMARK   3      S31:  -0.8854 S32:   0.6878 S33:   0.4764                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 231 THROUGH 285 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4438  -7.7017 -30.2719              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3252 T22:   0.3087                                     
REMARK   3      T33:   0.5209 T12:   0.0500                                     
REMARK   3      T13:  -0.0045 T23:   0.1289                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6056 L22:   3.2960                                     
REMARK   3      L33:   2.1825 L12:   0.0331                                     
REMARK   3      L13:   0.0610 L23:  -0.6409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0140 S12:   0.2754 S13:   0.1309                       
REMARK   3      S21:  -0.3713 S22:  -0.2399 S23:  -0.0100                       
REMARK   3      S31:   0.0825 S32:   0.1182 S33:   0.2323                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 286 THROUGH 305 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0787 -10.8060 -41.1397              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6385 T22:   0.4353                                     
REMARK   3      T33:   0.4962 T12:   0.0816                                     
REMARK   3      T13:  -0.1503 T23:   0.0592                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4746 L22:   6.5530                                     
REMARK   3      L33:   2.1176 L12:   2.2054                                     
REMARK   3      L13:   1.0392 L23:   0.7599                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2350 S12:   0.2790 S13:  -0.1249                       
REMARK   3      S21:  -0.8462 S22:   0.1344 S23:   0.2884                       
REMARK   3      S31:   0.4716 S32:  -0.1338 S33:   0.1612                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 306 THROUGH 352 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  45.2205 -19.6182 -37.4060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4937 T22:   0.4746                                     
REMARK   3      T33:   0.5786 T12:   0.1430                                     
REMARK   3      T13:   0.1377 T23:   0.1601                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7821 L22:   1.9332                                     
REMARK   3      L33:   2.1743 L12:   0.1659                                     
REMARK   3      L13:   0.7710 L23:  -0.8826                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0137 S12:   0.5520 S13:  -0.0790                       
REMARK   3      S21:  -0.8362 S22:  -0.2203 S23:  -0.5158                       
REMARK   3      S31:   0.2372 S32:   0.2383 S33:   0.2149                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 4 THROUGH 89 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  15.2077 -14.5325 -16.7345              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2286 T22:   0.2667                                     
REMARK   3      T33:   0.3595 T12:   0.0184                                     
REMARK   3      T13:   0.0100 T23:   0.0425                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0084 L22:   1.6857                                     
REMARK   3      L33:   2.6753 L12:  -0.9045                                     
REMARK   3      L13:   0.2752 L23:  -0.3813                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1784 S12:  -0.0630 S13:  -0.1912                       
REMARK   3      S21:   0.0110 S22:   0.0181 S23:   0.2226                       
REMARK   3      S31:  -0.0643 S32:  -0.0784 S33:  -0.1773                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 90 THROUGH 135 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  29.1763   3.7114  -2.2068              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6615 T22:   0.5718                                     
REMARK   3      T33:   0.6292 T12:  -0.0339                                     
REMARK   3      T13:  -0.0336 T23:  -0.1320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0382 L22:   5.0443                                     
REMARK   3      L33:   5.6024 L12:  -0.4678                                     
REMARK   3      L13:  -0.2986 L23:   2.0475                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0262 S12:  -0.6931 S13:   0.9228                       
REMARK   3      S21:   0.3642 S22:   0.0696 S23:  -0.2577                       
REMARK   3      S31:  -1.2855 S32:   0.0600 S33:  -0.0679                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 136 THROUGH 154 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0444  -9.2382  -1.1873              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3442 T22:   0.3914                                     
REMARK   3      T33:   0.2721 T12:  -0.0042                                     
REMARK   3      T13:  -0.0196 T23:   0.0564                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9636 L22:   1.6155                                     
REMARK   3      L33:   2.1755 L12:   0.4042                                     
REMARK   3      L13:  -1.6172 L23:   0.3929                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0426 S12:  -0.5061 S13:   0.0275                       
REMARK   3      S21:   0.2724 S22:   0.0985 S23:   0.2354                       
REMARK   3      S31:  -0.2939 S32:   0.1260 S33:  -0.0592                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 155 THROUGH 230 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0676 -14.2701   2.8993              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4375 T22:   0.5566                                     
REMARK   3      T33:   0.4374 T12:   0.0211                                     
REMARK   3      T13:  -0.0525 T23:   0.0407                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1405 L22:   2.5785                                     
REMARK   3      L33:   2.6617 L12:  -1.3008                                     
REMARK   3      L13:  -1.4865 L23:   0.2155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1922 S12:  -0.9951 S13:  -0.0485                       
REMARK   3      S21:   0.7910 S22:   0.3085 S23:  -0.2217                       
REMARK   3      S31:   0.0468 S32:   0.5740 S33:  -0.1318                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 231 THROUGH 285 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  25.9567 -28.3847 -17.5898              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3009 T22:   0.2486                                     
REMARK   3      T33:   0.4509 T12:   0.0469                                     
REMARK   3      T13:  -0.0547 T23:   0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2526 L22:   2.3358                                     
REMARK   3      L33:   2.8990 L12:  -0.1101                                     
REMARK   3      L13:  -0.0947 L23:  -1.0027                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1285 S12:   0.0447 S13:  -0.2942                       
REMARK   3      S21:  -0.2132 S22:  -0.0591 S23:  -0.0738                       
REMARK   3      S31:   0.4106 S32:   0.2588 S33:  -0.0456                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 286 THROUGH 305 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.7634 -34.3712 -32.0621              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7787 T22:   0.3340                                     
REMARK   3      T33:   0.5663 T12:   0.1769                                     
REMARK   3      T13:  -0.0777 T23:  -0.0588                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6803 L22:   2.1846                                     
REMARK   3      L33:   6.2644 L12:  -0.1790                                     
REMARK   3      L13:  -0.6493 L23:  -1.9490                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3252 S12:   0.1585 S13:  -0.4416                       
REMARK   3      S21:  -1.1526 S22:  -0.2529 S23:   0.1214                       
REMARK   3      S31:   0.0328 S32:   0.0221 S33:  -0.1773                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 306 THROUGH 353 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.7406 -23.1457 -30.5912              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4331 T22:   0.2989                                     
REMARK   3      T33:   0.4142 T12:   0.0084                                     
REMARK   3      T13:  -0.1544 T23:  -0.0265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3712 L22:   1.3179                                     
REMARK   3      L33:   1.6668 L12:  -0.3904                                     
REMARK   3      L13:  -0.6387 L23:   1.3643                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2205 S12:   0.3891 S13:  -0.3220                       
REMARK   3      S21:  -0.9492 S22:  -0.0516 S23:   0.4637                       
REMARK   3      S31:   0.2743 S32:  -0.3460 S33:  -0.2000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 4 THROUGH 128 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  45.8463 -48.4673  -7.0416              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2414 T22:   0.2329                                     
REMARK   3      T33:   0.2857 T12:   0.0283                                     
REMARK   3      T13:  -0.0207 T23:   0.0048                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6238 L22:   2.1421                                     
REMARK   3      L33:   2.3045 L12:   0.0941                                     
REMARK   3      L13:   1.3428 L23:  -0.6176                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0915 S12:   0.1092 S13:   0.2118                       
REMARK   3      S21:  -0.0312 S22:  -0.0490 S23:  -0.0250                       
REMARK   3      S31:   0.0269 S32:   0.1516 S33:  -0.0195                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 129 THROUGH 212 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  55.3409 -81.6328  -2.5923              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7451 T22:   0.7747                                     
REMARK   3      T33:   0.4597 T12:   0.1268                                     
REMARK   3      T13:  -0.1549 T23:  -0.1417                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8257 L22:   2.3968                                     
REMARK   3      L33:   2.4029 L12:  -0.3216                                     
REMARK   3      L13:   1.5173 L23:   0.2290                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1426 S12:   1.0720 S13:  -0.4720                       
REMARK   3      S21:  -0.3657 S22:   0.1170 S23:  -0.1816                       
REMARK   3      S31:   0.4289 S32:   1.0171 S33:  -0.2677                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 213 THROUGH 225 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  63.1235 -86.6133  -0.0894              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7684 T22:   1.2168                                     
REMARK   3      T33:   0.8002 T12:   0.1952                                     
REMARK   3      T13:  -0.0988 T23:  -0.2334                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1196 L22:   6.1823                                     
REMARK   3      L33:   3.0301 L12:   0.3094                                     
REMARK   3      L13:   0.1478 L23:  -0.2153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3342 S12:   0.0585 S13:  -0.7023                       
REMARK   3      S21:   0.4290 S22:  -0.0407 S23:  -0.2589                       
REMARK   3      S31:   0.1468 S32:   0.8649 S33:  -0.1331                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 2 THROUGH 19 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  25.5241 -64.9915 -10.0025              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3057 T22:   0.2868                                     
REMARK   3      T33:   0.3395 T12:  -0.0064                                     
REMARK   3      T13:  -0.0629 T23:  -0.0008                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2354 L22:   5.7481                                     
REMARK   3      L33:   4.0173 L12:   0.1242                                     
REMARK   3      L13:  -0.1456 L23:   1.9322                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0829 S12:  -0.1189 S13:   0.3744                       
REMARK   3      S21:   0.7105 S22:  -0.1514 S23:   0.3179                       
REMARK   3      S31:   0.3803 S32:  -0.2574 S33:   0.1339                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 20 THROUGH 104 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  28.5490 -57.1414 -15.1457              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2770 T22:   0.2502                                     
REMARK   3      T33:   0.3622 T12:   0.0092                                     
REMARK   3      T13:  -0.0617 T23:   0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9456 L22:   3.2351                                     
REMARK   3      L33:   1.7481 L12:   0.8814                                     
REMARK   3      L13:   0.9834 L23:   0.3021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0614 S12:   0.0507 S13:   0.2590                       
REMARK   3      S21:  -0.1520 S22:  -0.0018 S23:   0.5055                       
REMARK   3      S31:   0.1017 S32:  -0.0923 S33:  -0.0410                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 105 THROUGH 116 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6119 -79.8893 -10.7400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7217 T22:   0.3570                                     
REMARK   3      T33:   0.4567 T12:  -0.0478                                     
REMARK   3      T13:  -0.3907 T23:   0.1320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9435 L22:   3.3410                                     
REMARK   3      L33:   0.5806 L12:   0.4940                                     
REMARK   3      L13:  -0.7238 L23:  -0.4656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4577 S12:  -0.5218 S13:  -0.4614                       
REMARK   3      S21:   0.2578 S22:   0.2332 S23:  -0.1176                       
REMARK   3      S31:   0.6280 S32:  -0.0512 S33:   0.2080                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 117 THROUGH 166 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  44.3200 -84.8626   6.9754              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7966 T22:   0.7159                                     
REMARK   3      T33:   0.6293 T12:  -0.0812                                     
REMARK   3      T13:  -0.2972 T23:   0.1426                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4090 L22:   1.1123                                     
REMARK   3      L33:   1.6106 L12:  -0.6211                                     
REMARK   3      L13:   1.3643 L23:  -0.0434                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5301 S12:  -1.0393 S13:  -0.6382                       
REMARK   3      S21:   0.0645 S22:   0.1420 S23:   0.1791                       
REMARK   3      S31:   0.8556 S32:  -0.7806 S33:  -0.6123                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 167 THROUGH 191 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  45.2528 -82.3612   3.0940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6135 T22:   0.4701                                     
REMARK   3      T33:   0.4272 T12:   0.0439                                     
REMARK   3      T13:  -0.1768 T23:   0.0020                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4426 L22:   2.0401                                     
REMARK   3      L33:   2.9744 L12:  -0.0844                                     
REMARK   3      L13:   1.8387 L23:  -0.4430                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1061 S12:   0.0243 S13:  -0.3075                       
REMARK   3      S21:   0.1294 S22:  -0.3212 S23:   0.0411                       
REMARK   3      S31:   0.1804 S32:   0.5132 S33:   0.4240                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'D' AND (RESID 192 THROUGH 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  40.9419 -92.7823   9.1000              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1559 T22:   1.1599                                     
REMARK   3      T33:   0.8026 T12:  -0.4848                                     
REMARK   3      T13:  -0.6008 T23:   0.6960                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1603 L22:   0.6160                                     
REMARK   3      L33:   3.9976 L12:  -0.5960                                     
REMARK   3      L13:   2.4310 L23:  -0.7421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3469 S12:  -0.1627 S13:  -0.3959                       
REMARK   3      S21:   0.0395 S22:   0.1877 S23:   0.0732                       
REMARK   3      S31:   0.8228 S32:  -0.1536 S33:  -0.0658                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 4 THROUGH 20 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  12.8827  20.9028 -29.0548              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2917 T22:   0.2771                                     
REMARK   3      T33:   0.2456 T12:   0.0250                                     
REMARK   3      T13:   0.0622 T23:   0.0397                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0787 L22:   5.1800                                     
REMARK   3      L33:   2.3468 L12:  -1.2806                                     
REMARK   3      L13:  -0.7360 L23:   0.3014                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2444 S12:   0.1797 S13:  -0.0133                       
REMARK   3      S21:   0.0865 S22:  -0.3704 S23:   0.6345                       
REMARK   3      S31:  -0.2397 S32:  -0.3970 S33:   0.0234                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 21 THROUGH 48 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7341  14.2138 -31.0967              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2758 T22:   0.2581                                     
REMARK   3      T33:   0.1078 T12:   0.0140                                     
REMARK   3      T13:  -0.0030 T23:   0.0060                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2417 L22:   4.7560                                     
REMARK   3      L33:   1.5840 L12:  -0.6146                                     
REMARK   3      L13:  -0.4238 L23:  -0.5282                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1222 S12:   0.0583 S13:  -0.1307                       
REMARK   3      S21:  -0.0325 S22:  -0.0835 S23:   0.3839                       
REMARK   3      S31:  -0.0810 S32:  -0.0734 S33:   0.0427                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 49 THROUGH 70 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  27.2296  14.8760 -23.6968              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3999 T22:   0.2836                                     
REMARK   3      T33:   0.1607 T12:  -0.0316                                     
REMARK   3      T13:  -0.0616 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5536 L22:   3.2588                                     
REMARK   3      L33:   0.9258 L12:  -0.0541                                     
REMARK   3      L13:  -0.5426 L23:   0.1108                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1688 S12:  -0.1037 S13:  -0.1956                       
REMARK   3      S21:   0.6892 S22:  -0.1630 S23:  -0.4966                       
REMARK   3      S31:  -0.0088 S32:   0.2011 S33:   0.0745                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 71 THROUGH 86 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0372  12.1857 -23.2628              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3354 T22:   0.2800                                     
REMARK   3      T33:   0.1678 T12:  -0.0103                                     
REMARK   3      T13:   0.0554 T23:  -0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.8993 L22:   8.0310                                     
REMARK   3      L33:   3.3517 L12:   1.0601                                     
REMARK   3      L13:   0.5181 L23:   1.5636                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0704 S12:  -0.0581 S13:  -0.4781                       
REMARK   3      S21:   0.7196 S22:  -0.2248 S23:   0.3669                       
REMARK   3      S31:  -0.0240 S32:  -0.2091 S33:   0.0542                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 87 THROUGH 102 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  20.7658  23.7568 -27.9401              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3718 T22:   0.2670                                     
REMARK   3      T33:   0.1073 T12:   0.0076                                     
REMARK   3      T13:   0.0275 T23:  -0.0053                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5475 L22:   2.9923                                     
REMARK   3      L33:   1.9573 L12:  -1.6671                                     
REMARK   3      L13:  -0.9898 L23:  -0.1623                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2393 S12:  -0.0543 S13:  -0.0424                       
REMARK   3      S21:   0.5882 S22:  -0.2733 S23:  -0.1235                       
REMARK   3      S31:  -0.3049 S32:  -0.1168 S33:  -0.0690                       
REMARK   3   TLS GROUP : 30                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 103 THROUGH 115 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.3655   9.8775 -37.5222              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3387 T22:   0.3030                                     
REMARK   3      T33:   0.2638 T12:   0.0794                                     
REMARK   3      T13:  -0.0295 T23:   0.0026                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5570 L22:   7.0990                                     
REMARK   3      L33:   0.9854 L12:  -4.1720                                     
REMARK   3      L13:  -0.8569 L23:  -0.5328                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1938 S12:   0.0977 S13:  -0.5262                       
REMARK   3      S21:  -0.4616 S22:  -0.2803 S23:   0.1440                       
REMARK   3      S31:   0.1765 S32:  -0.0569 S33:   0.1284                       
REMARK   3   TLS GROUP : 31                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 116 THROUGH 128 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.3619  36.1721 -27.5105              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4871 T22:   0.3558                                     
REMARK   3      T33:   0.2781 T12:   0.0443                                     
REMARK   3      T13:   0.1359 T23:   0.0284                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5364 L22:   2.8312                                     
REMARK   3      L33:   0.5997 L12:  -1.4451                                     
REMARK   3      L13:   0.0864 L23:  -0.9765                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1368 S12:  -0.0578 S13:   0.2387                       
REMARK   3      S21:   0.5922 S22:   0.1185 S23:   0.3415                       
REMARK   3      S31:  -0.2069 S32:  -0.1764 S33:  -0.1787                       
REMARK   3   TLS GROUP : 32                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 129 THROUGH 184 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.4293  47.3161 -44.7021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2460 T22:   0.2632                                     
REMARK   3      T33:   0.2654 T12:  -0.0332                                     
REMARK   3      T13:   0.0622 T23:   0.0729                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7251 L22:   2.4315                                     
REMARK   3      L33:   3.9477 L12:  -0.9828                                     
REMARK   3      L13:   0.6635 L23:   2.0395                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2374 S12:   0.0836 S13:   0.0936                       
REMARK   3      S21:   0.1080 S22:  -0.0872 S23:   0.1473                       
REMARK   3      S31:  -0.0627 S32:   0.1115 S33:   0.2038                       
REMARK   3   TLS GROUP : 33                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 185 THROUGH 212 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   5.7865  47.3612 -47.9392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2202 T22:   0.2859                                     
REMARK   3      T33:   0.3088 T12:  -0.0229                                     
REMARK   3      T13:   0.0599 T23:   0.0023                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5680 L22:   1.9991                                     
REMARK   3      L33:   5.3747 L12:  -0.9166                                     
REMARK   3      L13:   1.3931 L23:   1.0840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3168 S12:  -0.0287 S13:  -0.0794                       
REMARK   3      S21:   0.1455 S22:  -0.1343 S23:   0.2984                       
REMARK   3      S31:  -0.1026 S32:  -0.3628 S33:   0.3335                       
REMARK   3   TLS GROUP : 34                                                     
REMARK   3    SELECTION: CHAIN 'E' AND (RESID 213 THROUGH 225 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   1.3611  53.0231 -44.1762              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3113 T22:   0.4721                                     
REMARK   3      T33:   0.4853 T12:   0.0377                                     
REMARK   3      T13:   0.0340 T23:  -0.0627                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1209 L22:   1.6129                                     
REMARK   3      L33:   6.9478 L12:  -1.7500                                     
REMARK   3      L13:   0.9107 L23:   0.9220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0709 S12:  -0.2969 S13:   0.2943                       
REMARK   3      S21:   0.2843 S22:  -0.1710 S23:   0.7271                       
REMARK   3      S31:  -0.4247 S32:  -0.4833 S33:   0.4471                       
REMARK   3   TLS GROUP : 35                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 2 THROUGH 19 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  36.6217  26.0777 -46.8103              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6086 T22:   0.7762                                     
REMARK   3      T33:   0.4310 T12:   0.2761                                     
REMARK   3      T13:   0.2266 T23:   0.3300                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5070 L22:   2.3970                                     
REMARK   3      L33:   4.3180 L12:   0.4862                                     
REMARK   3      L13:   0.6488 L23:  -1.7943                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3332 S12:   0.5776 S13:   0.2148                       
REMARK   3      S21:  -0.1758 S22:  -0.4880 S23:  -0.5882                       
REMARK   3      S31:  -0.5691 S32:   0.3763 S33:  -0.1102                       
REMARK   3   TLS GROUP : 36                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 20 THROUGH 91 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  33.0167  17.2520 -46.6909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6223 T22:   0.6589                                     
REMARK   3      T33:  -0.2777 T12:   0.4107                                     
REMARK   3      T13:   0.3525 T23:   0.1265                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3702 L22:   2.7138                                     
REMARK   3      L33:   1.5121 L12:  -0.1963                                     
REMARK   3      L13:  -1.3264 L23:  -0.5639                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.9195 S12:   0.9188 S13:  -0.2695                       
REMARK   3      S21:  -1.0758 S22:  -0.9990 S23:  -1.5122                       
REMARK   3      S31:   0.3580 S32:   0.5228 S33:   0.3970                       
REMARK   3   TLS GROUP : 37                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 92 THROUGH 104 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  35.6569  15.2986 -32.5197              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3032 T22:   0.3882                                     
REMARK   3      T33:   0.3287 T12:   0.0091                                     
REMARK   3      T13:  -0.0345 T23:   0.1469                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6191 L22:   5.8063                                     
REMARK   3      L33:   3.3703 L12:  -0.9141                                     
REMARK   3      L13:   0.7325 L23:  -1.3029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2870 S12:   0.1435 S13:  -0.0277                       
REMARK   3      S21:   0.2576 S22:  -0.6997 S23:  -1.1956                       
REMARK   3      S31:   0.0620 S32:   0.4153 S33:   0.4249                       
REMARK   3   TLS GROUP : 38                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 105 THROUGH 116 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  28.8552  36.8030 -55.9244              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4791 T22:   0.6408                                     
REMARK   3      T33:   0.3531 T12:   0.2154                                     
REMARK   3      T13:   0.1837 T23:   0.2182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6133 L22:   3.2551                                     
REMARK   3      L33:   1.3494 L12:  -0.9621                                     
REMARK   3      L13:   0.7840 L23:  -2.0374                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2206 S12:   0.3963 S13:  -0.2050                       
REMARK   3      S21:  -0.0731 S22:  -0.2123 S23:  -0.1345                       
REMARK   3      S31:   0.5566 S32:   0.7865 S33:   0.1805                       
REMARK   3   TLS GROUP : 39                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 117 THROUGH 131 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  12.3420  58.1478 -42.0327              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4045 T22:   0.3488                                     
REMARK   3      T33:   0.3218 T12:  -0.0333                                     
REMARK   3      T13:  -0.0646 T23:   0.0734                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1912 L22:   2.9951                                     
REMARK   3      L33:   6.4734 L12:   0.1031                                     
REMARK   3      L13:  -1.0217 L23:  -0.2226                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2186 S12:  -0.2413 S13:   0.2956                       
REMARK   3      S21:   0.3318 S22:  -0.0198 S23:   0.1292                       
REMARK   3      S31:  -0.6914 S32:   0.4606 S33:   0.2818                       
REMARK   3   TLS GROUP : 40                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 132 THROUGH 153 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.5338  50.6505 -46.9030              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3513 T22:   0.7245                                     
REMARK   3      T33:   0.2687 T12:  -0.0523                                     
REMARK   3      T13:  -0.0053 T23:   0.2021                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6419 L22:   2.2809                                     
REMARK   3      L33:   4.0847 L12:  -0.9592                                     
REMARK   3      L13:  -0.8342 L23:   1.5526                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3230 S12:  -0.2763 S13:  -0.0445                       
REMARK   3      S21:   0.2045 S22:   0.0122 S23:  -0.3319                       
REMARK   3      S31:  -0.1198 S32:   1.4778 S33:   0.1724                       
REMARK   3   TLS GROUP : 41                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 154 THROUGH 177 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  23.7327  46.6171 -46.4393              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2623 T22:   0.6880                                     
REMARK   3      T33:   0.2737 T12:  -0.0391                                     
REMARK   3      T13:   0.0047 T23:   0.2022                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3953 L22:   2.5442                                     
REMARK   3      L33:   3.4753 L12:   0.1440                                     
REMARK   3      L13:  -0.0532 L23:   0.3161                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1055 S12:  -0.2755 S13:  -0.0102                       
REMARK   3      S21:   0.1364 S22:  -0.3927 S23:  -0.1442                       
REMARK   3      S31:   0.0613 S32:   0.9104 S33:  -0.0060                       
REMARK   3   TLS GROUP : 42                                                     
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 178 THROUGH 217 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  22.4532  60.1487 -44.0803              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5177 T22:   0.5548                                     
REMARK   3      T33:   0.2522 T12:  -0.2447                                     
REMARK   3      T13:  -0.0601 T23:   0.1396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4121 L22:   3.7212                                     
REMARK   3      L33:   4.2918 L12:  -0.4641                                     
REMARK   3      L13:  -1.5881 L23:   0.4402                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0314 S12:  -0.3077 S13:   0.3344                       
REMARK   3      S21:   0.1531 S22:   0.0593 S23:  -0.1485                       
REMARK   3      S31:  -1.0304 S32:   1.1088 S33:  -0.0272                       
REMARK   3   TLS GROUP : 43                                                     
REMARK   3    SELECTION: CHAIN 'G' AND (RESID 266 THROUGH 287 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  38.2316  -6.7124   4.4952              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3981 T22:   1.2658                                     
REMARK   3      T33:   1.1579 T12:  -0.2267                                     
REMARK   3      T13:  -0.1808 T23:  -0.1926                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3190 L22:   0.6116                                     
REMARK   3      L33:   0.7358 L12:   0.2088                                     
REMARK   3      L13:   0.3666 L23:   0.0757                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1605 S12:  -0.2128 S13:   0.3673                       
REMARK   3      S21:   0.0670 S22:   0.2803 S23:  -0.5964                       
REMARK   3      S31:  -0.6398 S32:   0.5828 S33:  -0.2513                       
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 4XTR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206228.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 109335                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 53.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.7000                            
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) : 2.12                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.60                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.100                              
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: 2WOJ AND 3PGF                                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2 MM ATP AND 2 MM MGCL2 WITH 15% PEG     
REMARK 280  3350, 25 MM SUCCINIC ACID PH 7.0, VAPOR DIFFUSION, HANGING DROP,    
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       51.43500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.84500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       56.01500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       76.84500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       51.43500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       56.01500            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: HEPTAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEPTAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 22920 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 61770 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -212.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, 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     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     LEU A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A   101                                                      
REMARK 465     VAL A   102                                                      
REMARK 465     SER A   103                                                      
REMARK 465     ARG A   104                                                      
REMARK 465     ALA A   105                                                      
REMARK 465     ASN A   106                                                      
REMARK 465     ASN A   107                                                      
REMARK 465     ASN A   108                                                      
REMARK 465     GLY A   109                                                      
REMARK 465     SER A   110                                                      
REMARK 465     ASP A   111                                                      
REMARK 465     GLY A   112                                                      
REMARK 465     GLN A   113                                                      
REMARK 465     GLY A   114                                                      
REMARK 465     ASP A   115                                                      
REMARK 465     ASP A   116                                                      
REMARK 465     LEU A   117                                                      
REMARK 465     GLY A   118                                                      
REMARK 465     SER A   119                                                      
REMARK 465     LEU A   120                                                      
REMARK 465     LEU A   121                                                      
REMARK 465     GLN A   122                                                      
REMARK 465     GLY A   123                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     GLY A   157                                                      
REMARK 465     GLU A   158                                                      
REMARK 465     ASN A   195                                                      
REMARK 465     LYS A   196                                                      
REMARK 465     LEU A   197                                                      
REMARK 465     GLY A   198                                                      
REMARK 465     PRO A   199                                                      
REMARK 465     MET A   200                                                      
REMARK 465     LEU A   201                                                      
REMARK 465     ASN A   202                                                      
REMARK 465     SER A   203                                                      
REMARK 465     PHE A   204                                                      
REMARK 465     MET A   205                                                      
REMARK 465     GLY A   206                                                      
REMARK 465     ALA A   207                                                      
REMARK 465     GLY A   208                                                      
REMARK 465     ASN A   209                                                      
REMARK 465     VAL A   210                                                      
REMARK 465     GLU A   282                                                      
REMARK 465     LYS A   353                                                      
REMARK 465     GLU A   354                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     ARG B   104                                                      
REMARK 465     ALA B   105                                                      
REMARK 465     ASN B   106                                                      
REMARK 465     ASN B   107                                                      
REMARK 465     ASN B   108                                                      
REMARK 465     GLY B   109                                                      
REMARK 465     SER B   110                                                      
REMARK 465     ASP B   111                                                      
REMARK 465     GLY B   112                                                      
REMARK 465     GLN B   113                                                      
REMARK 465     GLY B   114                                                      
REMARK 465     ASP B   115                                                      
REMARK 465     ASP B   116                                                      
REMARK 465     LEU B   117                                                      
REMARK 465     GLY B   118                                                      
REMARK 465     SER B   119                                                      
REMARK 465     LEU B   120                                                      
REMARK 465     LEU B   121                                                      
REMARK 465     GLN B   122                                                      
REMARK 465     LYS B   196                                                      
REMARK 465     LEU B   197                                                      
REMARK 465     GLY B   198                                                      
REMARK 465     PRO B   199                                                      
REMARK 465     MET B   200                                                      
REMARK 465     LEU B   201                                                      
REMARK 465     ASN B   202                                                      
REMARK 465     SER B   203                                                      
REMARK 465     PHE B   204                                                      
REMARK 465     MET B   205                                                      
REMARK 465     GLY B   206                                                      
REMARK 465     ALA B   207                                                      
REMARK 465     GLY B   208                                                      
REMARK 465     ASN B   209                                                      
REMARK 465     VAL B   210                                                      
REMARK 465     ASN B   279                                                      
REMARK 465     ASP B   280                                                      
REMARK 465     GLN B   281                                                      
REMARK 465     GLU B   282                                                      
REMARK 465     HIS B   283                                                      
REMARK 465     GLU B   354                                                      
REMARK 465     GLU C     1                                                      
REMARK 465     ILE C     2                                                      
REMARK 465     SER C     3                                                      
REMARK 465     LYS C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     THR C   140                                                      
REMARK 465     SER C   141                                                      
REMARK 465     GLY C   142                                                      
REMARK 465     ASP C   226                                                      
REMARK 465     LYS C   227                                                      
REMARK 465     THR C   228                                                      
REMARK 465     HIS C   229                                                      
REMARK 465     THR C   230                                                      
REMARK 465     SER D     1                                                      
REMARK 465     GLU E     1                                                      
REMARK 465     ILE E     2                                                      
REMARK 465     SER E     3                                                      
REMARK 465     ASP E   226                                                      
REMARK 465     LYS E   227                                                      
REMARK 465     THR E   228                                                      
REMARK 465     HIS E   229                                                      
REMARK 465     THR E   230                                                      
REMARK 465     SER F     1                                                      
REMARK 465     MET G   252                                                      
REMARK 465     GLY G   253                                                      
REMARK 465     SER G   254                                                      
REMARK 465     HIS G   255                                                      
REMARK 465     HIS G   256                                                      
REMARK 465     HIS G   257                                                      
REMARK 465     HIS G   258                                                      
REMARK 465     HIS G   259                                                      
REMARK 465     HIS G   260                                                      
REMARK 465     SER G   261                                                      
REMARK 465     LYS G   262                                                      
REMARK 465     ARG G   263                                                      
REMARK 465     THR G   264                                                      
REMARK 465     SER G   265                                                      
REMARK 465     LEU G   288                                                      
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     ASP A 211    CB   CG   OD1  OD2                                  
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   OE2  GLU A   320     HH   TYR B   298              1.46            
REMARK 500   OE2  GLU D   108     HH   TYR D   176              1.48            
REMARK 500   HH   TYR A   298     OE2  GLU B   320              1.58            
REMARK 500   HE   ARG F    25     OD2  ASP F    71              1.58            
REMARK 500   H    SER F    15     OD2  ASP F    18              1.58            
REMARK 500   OE1  GLU B   320     NH1  ARG B   322              2.01            
REMARK 500   OE2  GLU B   307     O    HOH B   599              2.15            
REMARK 500   O    ALA A   277     N    ASN A   279              2.17            
REMARK 500   OE2  GLU D   108     OH   TYR D   176              2.17            
REMARK 500   O    HOH B   630     O    HOH E   437              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    GLN A 154     -164.62   -102.32                                   
REMARK 500    THR A 170      -67.08    -13.59                                   
REMARK 500    PHE A 276      -56.03     59.30                                   
REMARK 500    ALA A 277     -166.47     56.62                                   
REMARK 500    GLU A 278      -65.67     52.45                                   
REMARK 500    CYS A 285       97.70     73.12                                   
REMARK 500    TYR A 306       54.19    -99.17                                   
REMARK 500    ASN B  82       24.25   -143.40                                   
REMARK 500    THR B 170      -73.87      1.92                                   
REMARK 500    CYS B 285      107.92     91.21                                   
REMARK 500    TYR B 306       47.84    -99.92                                   
REMARK 500    SER C  59       -8.42     70.92                                   
REMARK 500    ARG C 107       40.44    -87.37                                   
REMARK 500    SER D  31     -128.21     52.34                                   
REMARK 500    ALA D  52      -41.69     73.31                                   
REMARK 500    ALA D  85     -176.83   -177.16                                   
REMARK 500    TYR D  92       58.31   -147.67                                   
REMARK 500    ASN D 141       70.55     54.29                                   
REMARK 500    ARG E 107       40.99    -93.34                                   
REMARK 500    ASP E 153       65.08     61.46                                   
REMARK 500    SER F  31     -128.89     53.72                                   
REMARK 500    ALA F  52      -29.21     73.86                                   
REMARK 500    ALA F  85     -174.57   -176.81                                   
REMARK 500    ASN F 141       74.14     51.45                                   
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 E 461        DISTANCE =  5.97 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  32   OG1                                                    
REMARK 620 2 ADP A 401   O2B  94.0                                              
REMARK 620 3 ATP A 404   O3G 177.2  85.9                                        
REMARK 620 4 ATP A 404   O2B  91.4   4.8  88.3                                  
REMARK 620 5 HOH A 506   O    85.7  83.2  91.5  79.0                            
REMARK 620 6 HOH A 559   O    86.4 172.6  93.3 168.4  89.5                      
REMARK 620 7 HOH A 505   O    87.5  98.8  95.3 102.7 173.0  88.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 403  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 285   SG                                                     
REMARK 620 2 CYS A 288   SG  116.0                                              
REMARK 620 3 CYS B 285   SG  101.4 119.5                                        
REMARK 620 4 CYS B 288   SG   97.5 100.3 120.7                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 402  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR B  32   OG1                                                    
REMARK 620 2 ADP B 401   O3B  87.2                                              
REMARK 620 3 ATP B 403   O3G 176.5  89.6                                        
REMARK 620 4 ATP B 403   O1B  88.3   5.5  88.8                                  
REMARK 620 5 HOH B 528   O    89.2  95.2  89.5 100.6                            
REMARK 620 6 HOH B 571   O    90.4 176.7  92.8 172.2  87.1                      
REMARK 620 7 HOH B 611   O    85.8  88.9  95.7  83.6 173.4  88.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ADP B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ATP B 403                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4XVU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4XWO   RELATED DB: PDB                                   
DBREF  4XTR A    1   354  UNP    Q12154   GET3_YEAST       1    354             
DBREF  4XTR B    1   354  UNP    Q12154   GET3_YEAST       1    354             
DBREF  4XTR C    1   230  PDB    4XTR     4XTR             1    230             
DBREF  4XTR D    1   217  PDB    4XTR     4XTR             1    217             
DBREF  4XTR E    1   230  PDB    4XTR     4XTR             1    230             
DBREF  4XTR F    1   217  PDB    4XTR     4XTR             1    217             
DBREF  4XTR G  262   288  UNP    E7M086   E7M086_YEASV   102    128             
SEQADV 4XTR ASN A   57  UNP  Q12154    ASP    57 ENGINEERED MUTATION            
SEQADV 4XTR ASN B   57  UNP  Q12154    ASP    57 ENGINEERED MUTATION            
SEQADV 4XTR MET G  252  UNP  E7M086              INITIATING METHIONINE          
SEQADV 4XTR GLY G  253  UNP  E7M086              EXPRESSION TAG                 
SEQADV 4XTR SER G  254  UNP  E7M086              EXPRESSION TAG                 
SEQADV 4XTR HIS G  255  UNP  E7M086              EXPRESSION TAG                 
SEQADV 4XTR HIS G  256  UNP  E7M086              EXPRESSION TAG                 
SEQADV 4XTR HIS G  257  UNP  E7M086              EXPRESSION TAG                 
SEQADV 4XTR HIS G  258  UNP  E7M086              EXPRESSION TAG                 
SEQADV 4XTR HIS G  259  UNP  E7M086              EXPRESSION TAG                 
SEQADV 4XTR HIS G  260  UNP  E7M086              EXPRESSION TAG                 
SEQADV 4XTR SER G  261  UNP  E7M086              EXPRESSION TAG                 
SEQRES   1 A  354  MET ASP LEU THR VAL GLU PRO ASN LEU HIS SER LEU ILE          
SEQRES   2 A  354  THR SER THR THR HIS LYS TRP ILE PHE VAL GLY GLY LYS          
SEQRES   3 A  354  GLY GLY VAL GLY LYS THR THR SER SER CYS SER ILE ALA          
SEQRES   4 A  354  ILE GLN MET ALA LEU SER GLN PRO ASN LYS GLN PHE LEU          
SEQRES   5 A  354  LEU ILE SER THR ASN PRO ALA HIS ASN LEU SER ASP ALA          
SEQRES   6 A  354  PHE GLY GLU LYS PHE GLY LYS ASP ALA ARG LYS VAL THR          
SEQRES   7 A  354  GLY MET ASN ASN LEU SER CYS MET GLU ILE ASP PRO SER          
SEQRES   8 A  354  ALA ALA LEU LYS ASP MET ASN ASP MET ALA VAL SER ARG          
SEQRES   9 A  354  ALA ASN ASN ASN GLY SER ASP GLY GLN GLY ASP ASP LEU          
SEQRES  10 A  354  GLY SER LEU LEU GLN GLY GLY ALA LEU ALA ASP LEU THR          
SEQRES  11 A  354  GLY SER ILE PRO GLY ILE ASP GLU ALA LEU SER PHE MET          
SEQRES  12 A  354  GLU VAL MET LYS HIS ILE LYS ARG GLN GLU GLN GLY GLU          
SEQRES  13 A  354  GLY GLU THR PHE ASP THR VAL ILE PHE ASP THR ALA PRO          
SEQRES  14 A  354  THR GLY HIS THR LEU ARG PHE LEU GLN LEU PRO ASN THR          
SEQRES  15 A  354  LEU SER LYS LEU LEU GLU LYS PHE GLY GLU ILE THR ASN          
SEQRES  16 A  354  LYS LEU GLY PRO MET LEU ASN SER PHE MET GLY ALA GLY          
SEQRES  17 A  354  ASN VAL ASP ILE SER GLY LYS LEU ASN GLU LEU LYS ALA          
SEQRES  18 A  354  ASN VAL GLU THR ILE ARG GLN GLN PHE THR ASP PRO ASP          
SEQRES  19 A  354  LEU THR THR PHE VAL CYS VAL CYS ILE SER GLU PHE LEU          
SEQRES  20 A  354  SER LEU TYR GLU THR GLU ARG LEU ILE GLN GLU LEU ILE          
SEQRES  21 A  354  SER TYR ASP MET ASP VAL ASN SER ILE ILE VAL ASN GLN          
SEQRES  22 A  354  LEU LEU PHE ALA GLU ASN ASP GLN GLU HIS ASN CYS LYS          
SEQRES  23 A  354  ARG CYS GLN ALA ARG TRP LYS MET GLN LYS LYS TYR LEU          
SEQRES  24 A  354  ASP GLN ILE ASP GLU LEU TYR GLU ASP PHE HIS VAL VAL          
SEQRES  25 A  354  LYS MET PRO LEU CYS ALA GLY GLU ILE ARG GLY LEU ASN          
SEQRES  26 A  354  ASN LEU THR LYS PHE SER GLN PHE LEU ASN LYS GLU TYR          
SEQRES  27 A  354  ASN PRO ILE THR ASP GLY LYS VAL ILE TYR GLU LEU GLU          
SEQRES  28 A  354  ASP LYS GLU                                                  
SEQRES   1 B  354  MET ASP LEU THR VAL GLU PRO ASN LEU HIS SER LEU ILE          
SEQRES   2 B  354  THR SER THR THR HIS LYS TRP ILE PHE VAL GLY GLY LYS          
SEQRES   3 B  354  GLY GLY VAL GLY LYS THR THR SER SER CYS SER ILE ALA          
SEQRES   4 B  354  ILE GLN MET ALA LEU SER GLN PRO ASN LYS GLN PHE LEU          
SEQRES   5 B  354  LEU ILE SER THR ASN PRO ALA HIS ASN LEU SER ASP ALA          
SEQRES   6 B  354  PHE GLY GLU LYS PHE GLY LYS ASP ALA ARG LYS VAL THR          
SEQRES   7 B  354  GLY MET ASN ASN LEU SER CYS MET GLU ILE ASP PRO SER          
SEQRES   8 B  354  ALA ALA LEU LYS ASP MET ASN ASP MET ALA VAL SER ARG          
SEQRES   9 B  354  ALA ASN ASN ASN GLY SER ASP GLY GLN GLY ASP ASP LEU          
SEQRES  10 B  354  GLY SER LEU LEU GLN GLY GLY ALA LEU ALA ASP LEU THR          
SEQRES  11 B  354  GLY SER ILE PRO GLY ILE ASP GLU ALA LEU SER PHE MET          
SEQRES  12 B  354  GLU VAL MET LYS HIS ILE LYS ARG GLN GLU GLN GLY GLU          
SEQRES  13 B  354  GLY GLU THR PHE ASP THR VAL ILE PHE ASP THR ALA PRO          
SEQRES  14 B  354  THR GLY HIS THR LEU ARG PHE LEU GLN LEU PRO ASN THR          
SEQRES  15 B  354  LEU SER LYS LEU LEU GLU LYS PHE GLY GLU ILE THR ASN          
SEQRES  16 B  354  LYS LEU GLY PRO MET LEU ASN SER PHE MET GLY ALA GLY          
SEQRES  17 B  354  ASN VAL ASP ILE SER GLY LYS LEU ASN GLU LEU LYS ALA          
SEQRES  18 B  354  ASN VAL GLU THR ILE ARG GLN GLN PHE THR ASP PRO ASP          
SEQRES  19 B  354  LEU THR THR PHE VAL CYS VAL CYS ILE SER GLU PHE LEU          
SEQRES  20 B  354  SER LEU TYR GLU THR GLU ARG LEU ILE GLN GLU LEU ILE          
SEQRES  21 B  354  SER TYR ASP MET ASP VAL ASN SER ILE ILE VAL ASN GLN          
SEQRES  22 B  354  LEU LEU PHE ALA GLU ASN ASP GLN GLU HIS ASN CYS LYS          
SEQRES  23 B  354  ARG CYS GLN ALA ARG TRP LYS MET GLN LYS LYS TYR LEU          
SEQRES  24 B  354  ASP GLN ILE ASP GLU LEU TYR GLU ASP PHE HIS VAL VAL          
SEQRES  25 B  354  LYS MET PRO LEU CYS ALA GLY GLU ILE ARG GLY LEU ASN          
SEQRES  26 B  354  ASN LEU THR LYS PHE SER GLN PHE LEU ASN LYS GLU TYR          
SEQRES  27 B  354  ASN PRO ILE THR ASP GLY LYS VAL ILE TYR GLU LEU GLU          
SEQRES  28 B  354  ASP LYS GLU                                                  
SEQRES   1 C  230  GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY          
SEQRES   2 C  230  LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA          
SEQRES   3 C  230  ALA SER GLY PHE ASN LEU TYR TYR TYR SER ILE HIS TRP          
SEQRES   4 C  230  VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA          
SEQRES   5 C  230  SER ILE SER PRO TYR SER SER SER THR SER TYR ALA ASP          
SEQRES   6 C  230  SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER          
SEQRES   7 C  230  LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA          
SEQRES   8 C  230  GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLY ARG TRP          
SEQRES   9 C  230  TYR ARG ARG ALA LEU ASP TYR TRP GLY GLN GLY THR LEU          
SEQRES  10 C  230  VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL          
SEQRES  11 C  230  PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY          
SEQRES  12 C  230  THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO          
SEQRES  13 C  230  GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR          
SEQRES  14 C  230  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER          
SEQRES  15 C  230  GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER          
SEQRES  16 C  230  SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN          
SEQRES  17 C  230  HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU          
SEQRES  18 C  230  PRO LYS SER CYS ASP LYS THR HIS THR                          
SEQRES   1 D  217  SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER          
SEQRES   2 D  217  ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA          
SEQRES   3 D  217  SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN          
SEQRES   4 D  217  LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA          
SEQRES   5 D  217  SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY          
SEQRES   6 D  217  SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER          
SEQRES   7 D  217  LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN          
SEQRES   8 D  217  TYR PRO TYR TYR SER SER LEU ILE THR PHE GLY GLN GLY          
SEQRES   9 D  217  THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER          
SEQRES  10 D  217  VAL PHE ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER          
SEQRES  11 D  217  GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR          
SEQRES  12 D  217  PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA          
SEQRES  13 D  217  LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN          
SEQRES  14 D  217  ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU          
SEQRES  15 D  217  THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR          
SEQRES  16 D  217  ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL          
SEQRES  17 D  217  THR LYS SER PHE ASN ARG GLY GLU CYS                          
SEQRES   1 E  230  GLU ILE SER GLU VAL GLN LEU VAL GLU SER GLY GLY GLY          
SEQRES   2 E  230  LEU VAL GLN PRO GLY GLY SER LEU ARG LEU SER CYS ALA          
SEQRES   3 E  230  ALA SER GLY PHE ASN LEU TYR TYR TYR SER ILE HIS TRP          
SEQRES   4 E  230  VAL ARG GLN ALA PRO GLY LYS GLY LEU GLU TRP VAL ALA          
SEQRES   5 E  230  SER ILE SER PRO TYR SER SER SER THR SER TYR ALA ASP          
SEQRES   6 E  230  SER VAL LYS GLY ARG PHE THR ILE SER ALA ASP THR SER          
SEQRES   7 E  230  LYS ASN THR ALA TYR LEU GLN MET ASN SER LEU ARG ALA          
SEQRES   8 E  230  GLU ASP THR ALA VAL TYR TYR CYS ALA ARG GLY ARG TRP          
SEQRES   9 E  230  TYR ARG ARG ALA LEU ASP TYR TRP GLY GLN GLY THR LEU          
SEQRES  10 E  230  VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER VAL          
SEQRES  11 E  230  PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY GLY          
SEQRES  12 E  230  THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO          
SEQRES  13 E  230  GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU THR          
SEQRES  14 E  230  SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER          
SEQRES  15 E  230  GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SER          
SEQRES  16 E  230  SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN          
SEQRES  17 E  230  HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU          
SEQRES  18 E  230  PRO LYS SER CYS ASP LYS THR HIS THR                          
SEQRES   1 F  217  SER ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER          
SEQRES   2 F  217  ALA SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA          
SEQRES   3 F  217  SER GLN SER VAL SER SER ALA VAL ALA TRP TYR GLN GLN          
SEQRES   4 F  217  LYS PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR SER ALA          
SEQRES   5 F  217  SER SER LEU TYR SER GLY VAL PRO SER ARG PHE SER GLY          
SEQRES   6 F  217  SER ARG SER GLY THR ASP PHE THR LEU THR ILE SER SER          
SEQRES   7 F  217  LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN          
SEQRES   8 F  217  TYR PRO TYR TYR SER SER LEU ILE THR PHE GLY GLN GLY          
SEQRES   9 F  217  THR LYS VAL GLU ILE LYS ARG THR VAL ALA ALA PRO SER          
SEQRES  10 F  217  VAL PHE ILE PHE PRO PRO SER ASP SER GLN LEU LYS SER          
SEQRES  11 F  217  GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR          
SEQRES  12 F  217  PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA          
SEQRES  13 F  217  LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN          
SEQRES  14 F  217  ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU          
SEQRES  15 F  217  THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR          
SEQRES  16 F  217  ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL          
SEQRES  17 F  217  THR LYS SER PHE ASN ARG GLY GLU CYS                          
SEQRES   1 G   37  MET GLY SER HIS HIS HIS HIS HIS HIS SER LYS ARG THR          
SEQRES   2 G   37  SER ARG TRP ARG VAL TYR LEU LEU ILE VAL LEU LEU VAL          
SEQRES   3 G   37  MET LEU LEU PHE ILE PHE LEU ILE MET LYS LEU                  
HET    ADP  A 401      38                                                       
HET     MG  A 402       1                                                       
HET     ZN  A 403       1                                                       
HET    ATP  A 404      42                                                       
HET    ADP  B 401      39                                                       
HET     MG  B 402       1                                                       
HET    ATP  B 403      43                                                       
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      ZN ZINC ION                                                         
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
FORMUL   8  ADP    2(C10 H15 N5 O10 P2)                                         
FORMUL   9   MG    2(MG 2+)                                                     
FORMUL  10   ZN    ZN 2+                                                        
FORMUL  11  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL  15  HOH   *928(H2 O)                                                    
HELIX    1 AA1 LEU A    9  THR A   14  1                                   6    
HELIX    2 AA2 GLY A   30  GLN A   46  1                                  17    
HELIX    3 AA3 ASN A   61  GLY A   67  1                                   7    
HELIX    4 AA4 ASP A   89  MET A  100  1                                  12    
HELIX    5 AA5 ALA A  125  GLY A  131  1                                   7    
HELIX    6 AA6 GLY A  135  GLN A  154  1                                  20    
HELIX    7 AA7 PRO A  169  GLN A  178  1                                  10    
HELIX    8 AA8 GLN A  178  THR A  194  1                                  17    
HELIX    9 AA9 ILE A  212  THR A  231  1                                  20    
HELIX   10 AB1 GLU A  245  TYR A  262  1                                  18    
HELIX   11 AB2 CYS A  285  TYR A  306  1                                  22    
HELIX   12 AB3 GLY A  323  LYS A  336  1                                  14    
HELIX   13 AB4 THR A  342  GLU A  349  5                                   8    
HELIX   14 AB5 LEU B    9  THR B   14  1                                   6    
HELIX   15 AB6 GLY B   30  GLN B   46  1                                  17    
HELIX   16 AB7 ASN B   61  GLY B   67  1                                   7    
HELIX   17 AB8 ASP B   89  SER B  103  1                                  15    
HELIX   18 AB9 ALA B  125  GLY B  131  1                                   7    
HELIX   19 AC1 GLY B  135  GLY B  155  1                                  21    
HELIX   20 AC2 PRO B  169  GLN B  178  1                                  10    
HELIX   21 AC3 GLN B  178  ASN B  195  1                                  18    
HELIX   22 AC4 ILE B  212  THR B  231  1                                  20    
HELIX   23 AC5 GLU B  245  TYR B  262  1                                  18    
HELIX   24 AC6 CYS B  285  TYR B  306  1                                  22    
HELIX   25 AC7 GLY B  323  LYS B  336  1                                  14    
HELIX   26 AC8 ASP B  343  GLU B  349  5                                   7    
HELIX   27 AC9 ASN C   31  TYR C   33  5                                   3    
HELIX   28 AD1 ARG C   90  THR C   94  5                                   5    
HELIX   29 AD2 SER C  165  ALA C  167  5                                   3    
HELIX   30 AD3 SER C  196  GLN C  201  1                                   6    
HELIX   31 AD4 LYS C  210  ASN C  213  5                                   4    
HELIX   32 AD5 GLN D   80  PHE D   84  5                                   5    
HELIX   33 AD6 SER D  124  GLY D  131  1                                   8    
HELIX   34 AD7 LYS D  186  GLU D  190  1                                   5    
HELIX   35 AD8 ASN E   31  TYR E   33  5                                   3    
HELIX   36 AD9 PRO E   56  SER E   59  5                                   4    
HELIX   37 AE1 ARG E   90  THR E   94  5                                   5    
HELIX   38 AE2 SER E  165  ALA E  167  5                                   3    
HELIX   39 AE3 SER E  196  LEU E  198  5                                   3    
HELIX   40 AE4 LYS E  210  ASN E  213  5                                   4    
HELIX   41 AE5 GLN F   80  PHE F   84  5                                   5    
HELIX   42 AE6 SER F  124  LYS F  129  1                                   6    
HELIX   43 AE7 LYS F  186  HIS F  192  1                                   7    
HELIX   44 AE8 TRP G  267  MET G  286  1                                  20    
SHEET    1 AA1 8 ARG A  75  LYS A  76  0                                        
SHEET    2 AA1 8 LEU A  83  GLU A  87 -1  O  CYS A  85   N  ARG A  75           
SHEET    3 AA1 8 PHE A  51  SER A  55  1  N  LEU A  53   O  SER A  84           
SHEET    4 AA1 8 THR A 162  ASP A 166  1  O  ILE A 164   N  LEU A  52           
SHEET    5 AA1 8 TRP A  20  GLY A  25  1  N  ILE A  21   O  PHE A 165           
SHEET    6 AA1 8 THR A 236  ILE A 243  1  O  VAL A 239   N  PHE A  22           
SHEET    7 AA1 8 SER A 268  LEU A 274  1  O  ILE A 270   N  CYS A 240           
SHEET    8 AA1 8 HIS A 310  PRO A 315  1  O  HIS A 310   N  ILE A 269           
SHEET    1 AA2 8 ARG B  75  LYS B  76  0                                        
SHEET    2 AA2 8 LEU B  83  MET B  86 -1  O  CYS B  85   N  ARG B  75           
SHEET    3 AA2 8 PHE B  51  SER B  55  1  N  LEU B  53   O  SER B  84           
SHEET    4 AA2 8 THR B 162  ASP B 166  1  O  ILE B 164   N  LEU B  52           
SHEET    5 AA2 8 TRP B  20  GLY B  25  1  N  ILE B  21   O  PHE B 165           
SHEET    6 AA2 8 THR B 236  ILE B 243  1  O  VAL B 239   N  PHE B  22           
SHEET    7 AA2 8 SER B 268  LEU B 274  1  O  ILE B 270   N  CYS B 240           
SHEET    8 AA2 8 HIS B 310  PRO B 315  1  O  HIS B 310   N  ILE B 269           
SHEET    1 AA3 4 GLN C   6  SER C  10  0                                        
SHEET    2 AA3 4 LEU C  21  SER C  28 -1  O  SER C  24   N  SER C  10           
SHEET    3 AA3 4 THR C  81  MET C  86 -1  O  ALA C  82   N  CYS C  25           
SHEET    4 AA3 4 PHE C  71  ASP C  76 -1  N  ASP C  76   O  THR C  81           
SHEET    1 AA4 6 LEU C  14  VAL C  15  0                                        
SHEET    2 AA4 6 THR C 116  VAL C 120  1  O  THR C 119   N  VAL C  15           
SHEET    3 AA4 6 ALA C  95  ARG C 103 -1  N  TYR C  97   O  THR C 116           
SHEET    4 AA4 6 TYR C  35  GLN C  42 -1  N  VAL C  40   O  TYR C  98           
SHEET    5 AA4 6 LEU C  48  ILE C  54 -1  O  GLU C  49   N  ARG C  41           
SHEET    6 AA4 6 THR C  61  TYR C  63 -1  O  SER C  62   N  SER C  53           
SHEET    1 AA5 4 LEU C  14  VAL C  15  0                                        
SHEET    2 AA5 4 THR C 116  VAL C 120  1  O  THR C 119   N  VAL C  15           
SHEET    3 AA5 4 ALA C  95  ARG C 103 -1  N  TYR C  97   O  THR C 116           
SHEET    4 AA5 4 ARG C 106  TRP C 112 -1  O  ARG C 106   N  ARG C 103           
SHEET    1 AA6 4 SER C 129  LEU C 133  0                                        
SHEET    2 AA6 4 THR C 144  TYR C 154 -1  O  GLY C 148   N  LEU C 133           
SHEET    3 AA6 4 TYR C 185  PRO C 194 -1  O  TYR C 185   N  TYR C 154           
SHEET    4 AA6 4 VAL C 172  THR C 174 -1  N  HIS C 173   O  VAL C 190           
SHEET    1 AA7 4 SER C 129  LEU C 133  0                                        
SHEET    2 AA7 4 THR C 144  TYR C 154 -1  O  GLY C 148   N  LEU C 133           
SHEET    3 AA7 4 TYR C 185  PRO C 194 -1  O  TYR C 185   N  TYR C 154           
SHEET    4 AA7 4 VAL C 178  LEU C 179 -1  N  VAL C 178   O  SER C 186           
SHEET    1 AA8 3 THR C 160  TRP C 163  0                                        
SHEET    2 AA8 3 ILE C 204  HIS C 209 -1  O  ASN C 208   N  THR C 160           
SHEET    3 AA8 3 THR C 214  LYS C 219 -1  O  VAL C 216   N  VAL C 207           
SHEET    1 AA9 4 MET D   5  SER D   8  0                                        
SHEET    2 AA9 4 VAL D  20  ALA D  26 -1  O  THR D  23   N  SER D   8           
SHEET    3 AA9 4 ASP D  71  ILE D  76 -1  O  LEU D  74   N  ILE D  22           
SHEET    4 AA9 4 PHE D  63  SER D  68 -1  N  SER D  64   O  THR D  75           
SHEET    1 AB1 6 SER D  11  ALA D  14  0                                        
SHEET    2 AB1 6 THR D 105  ILE D 109  1  O  GLU D 108   N  ALA D  14           
SHEET    3 AB1 6 THR D  86  GLN D  91 -1  N  TYR D  87   O  THR D 105           
SHEET    4 AB1 6 VAL D  34  GLN D  39 -1  N  ALA D  35   O  GLN D  90           
SHEET    5 AB1 6 LYS D  46  TYR D  50 -1  O  LEU D  48   N  TRP D  36           
SHEET    6 AB1 6 SER D  54  LEU D  55 -1  O  SER D  54   N  TYR D  50           
SHEET    1 AB2 4 SER D  11  ALA D  14  0                                        
SHEET    2 AB2 4 THR D 105  ILE D 109  1  O  GLU D 108   N  ALA D  14           
SHEET    3 AB2 4 THR D  86  GLN D  91 -1  N  TYR D  87   O  THR D 105           
SHEET    4 AB2 4 THR D 100  PHE D 101 -1  O  THR D 100   N  GLN D  91           
SHEET    1 AB3 4 SER D 117  PHE D 121  0                                        
SHEET    2 AB3 4 THR D 132  PHE D 142 -1  O  LEU D 138   N  PHE D 119           
SHEET    3 AB3 4 TYR D 176  SER D 185 -1  O  SER D 180   N  CYS D 137           
SHEET    4 AB3 4 SER D 162  VAL D 166 -1  N  SER D 165   O  SER D 179           
SHEET    1 AB4 4 ALA D 156  LEU D 157  0                                        
SHEET    2 AB4 4 LYS D 148  VAL D 153 -1  N  VAL D 153   O  ALA D 156           
SHEET    3 AB4 4 VAL D 194  THR D 200 -1  O  ALA D 196   N  LYS D 152           
SHEET    4 AB4 4 VAL D 208  ASN D 213 -1  O  VAL D 208   N  VAL D 199           
SHEET    1 AB5 4 GLN E   6  SER E  10  0                                        
SHEET    2 AB5 4 LEU E  21  SER E  28 -1  O  SER E  24   N  SER E  10           
SHEET    3 AB5 4 THR E  81  MET E  86 -1  O  MET E  86   N  LEU E  21           
SHEET    4 AB5 4 PHE E  71  ASP E  76 -1  N  ASP E  76   O  THR E  81           
SHEET    1 AB6 6 GLY E  13  VAL E  15  0                                        
SHEET    2 AB6 6 THR E 116  VAL E 120  1  O  THR E 119   N  VAL E  15           
SHEET    3 AB6 6 ALA E  95  ARG E 103 -1  N  TYR E  97   O  THR E 116           
SHEET    4 AB6 6 TYR E  35  GLN E  42 -1  N  VAL E  40   O  TYR E  98           
SHEET    5 AB6 6 LEU E  48  SER E  55 -1  O  GLU E  49   N  ARG E  41           
SHEET    6 AB6 6 SER E  60  TYR E  63 -1  O  SER E  60   N  SER E  55           
SHEET    1 AB7 4 GLY E  13  VAL E  15  0                                        
SHEET    2 AB7 4 THR E 116  VAL E 120  1  O  THR E 119   N  VAL E  15           
SHEET    3 AB7 4 ALA E  95  ARG E 103 -1  N  TYR E  97   O  THR E 116           
SHEET    4 AB7 4 ARG E 106  TRP E 112 -1  O  ARG E 106   N  ARG E 103           
SHEET    1 AB8 4 SER E 129  LEU E 133  0                                        
SHEET    2 AB8 4 THR E 144  TYR E 154 -1  O  LEU E 150   N  PHE E 131           
SHEET    3 AB8 4 TYR E 185  PRO E 194 -1  O  VAL E 193   N  ALA E 145           
SHEET    4 AB8 4 VAL E 172  THR E 174 -1  N  HIS E 173   O  VAL E 190           
SHEET    1 AB9 4 SER E 129  LEU E 133  0                                        
SHEET    2 AB9 4 THR E 144  TYR E 154 -1  O  LEU E 150   N  PHE E 131           
SHEET    3 AB9 4 TYR E 185  PRO E 194 -1  O  VAL E 193   N  ALA E 145           
SHEET    4 AB9 4 VAL E 178  LEU E 179 -1  N  VAL E 178   O  SER E 186           
SHEET    1 AC1 3 THR E 160  TRP E 163  0                                        
SHEET    2 AC1 3 ILE E 204  HIS E 209 -1  O  ASN E 206   N  SER E 162           
SHEET    3 AC1 3 THR E 214  LYS E 219 -1  O  VAL E 216   N  VAL E 207           
SHEET    1 AC2 4 MET F   5  SER F   8  0                                        
SHEET    2 AC2 4 VAL F  20  ALA F  26 -1  O  ARG F  25   N  THR F   6           
SHEET    3 AC2 4 ASP F  71  ILE F  76 -1  O  LEU F  74   N  ILE F  22           
SHEET    4 AC2 4 PHE F  63  SER F  68 -1  N  SER F  64   O  THR F  75           
SHEET    1 AC3 6 SER F  11  ALA F  14  0                                        
SHEET    2 AC3 6 THR F 105  ILE F 109  1  O  GLU F 108   N  LEU F  12           
SHEET    3 AC3 6 THR F  86  GLN F  91 -1  N  TYR F  87   O  THR F 105           
SHEET    4 AC3 6 VAL F  34  GLN F  39 -1  N  ALA F  35   O  GLN F  90           
SHEET    5 AC3 6 LYS F  46  TYR F  50 -1  O  LYS F  46   N  GLN F  38           
SHEET    6 AC3 6 SER F  54  LEU F  55 -1  O  SER F  54   N  TYR F  50           
SHEET    1 AC4 4 SER F  11  ALA F  14  0                                        
SHEET    2 AC4 4 THR F 105  ILE F 109  1  O  GLU F 108   N  LEU F  12           
SHEET    3 AC4 4 THR F  86  GLN F  91 -1  N  TYR F  87   O  THR F 105           
SHEET    4 AC4 4 THR F 100  PHE F 101 -1  O  THR F 100   N  GLN F  91           
SHEET    1 AC5 4 SER F 117  PHE F 121  0                                        
SHEET    2 AC5 4 THR F 132  PHE F 142 -1  O  LEU F 138   N  PHE F 119           
SHEET    3 AC5 4 TYR F 176  SER F 185 -1  O  LEU F 182   N  VAL F 135           
SHEET    4 AC5 4 SER F 162  VAL F 166 -1  N  SER F 165   O  SER F 179           
SHEET    1 AC6 4 ALA F 156  LEU F 157  0                                        
SHEET    2 AC6 4 LYS F 148  VAL F 153 -1  N  VAL F 153   O  ALA F 156           
SHEET    3 AC6 4 VAL F 194  THR F 200 -1  O  GLU F 198   N  GLN F 150           
SHEET    4 AC6 4 VAL F 208  ASN F 213 -1  O  VAL F 208   N  VAL F 199           
SSBOND   1 CYS C   25    CYS C   99                          1555   1555  2.04  
SSBOND   2 CYS C  149    CYS C  205                          1555   1555  2.03  
SSBOND   3 CYS C  225    CYS D  217                          1555   1555  2.03  
SSBOND   4 CYS D   24    CYS D   89                          1555   1555  2.04  
SSBOND   5 CYS D  137    CYS D  197                          1555   1555  2.03  
SSBOND   6 CYS E   25    CYS E   99                          1555   1555  2.04  
SSBOND   7 CYS E  149    CYS E  205                          1555   1555  2.03  
SSBOND   8 CYS E  225    CYS F  217                          1555   1555  2.03  
SSBOND   9 CYS F   24    CYS F   89                          1555   1555  2.04  
SSBOND  10 CYS F  137    CYS F  197                          1555   1555  2.04  
LINK         OG1 THR A  32                MG    MG A 402     1555   1555  2.11  
LINK         SG  CYS A 285                ZN    ZN A 403     1555   1555  2.24  
LINK         SG  CYS A 288                ZN    ZN A 403     1555   1555  2.35  
LINK         OG1 THR B  32                MG    MG B 402     1555   1555  2.10  
LINK         SG  CYS B 285                ZN    ZN A 403     1555   1555  2.31  
LINK         SG  CYS B 288                ZN    ZN A 403     1555   1555  2.31  
LINK         O2BBADP A 401                MG    MG A 402     1555   1555  2.08  
LINK        MG    MG A 402                 O3GAATP A 404     1555   1555  2.13  
LINK        MG    MG A 402                 O2BAATP A 404     1555   1555  2.15  
LINK        MG    MG A 402                 O   HOH A 506     1555   1555  2.12  
LINK        MG    MG A 402                 O   HOH A 559     1555   1555  2.17  
LINK        MG    MG A 402                 O   HOH A 505     1555   1555  2.37  
LINK         O3BBADP B 401                MG    MG B 402     1555   1555  2.12  
LINK        MG    MG B 402                 O3GAATP B 403     1555   1555  2.07  
LINK        MG    MG B 402                 O1BAATP B 403     1555   1555  2.12  
LINK        MG    MG B 402                 O   HOH B 528     1555   1555  2.26  
LINK        MG    MG B 402                 O   HOH B 571     1555   1555  2.14  
LINK        MG    MG B 402                 O   HOH B 611     1555   1555  2.10  
CISPEP   1 PHE C  155    PRO C  156          0        -6.38                     
CISPEP   2 GLU C  157    PRO C  158          0        -1.41                     
CISPEP   3 SER D    8    PRO D    9          0        -6.74                     
CISPEP   4 TYR D  143    PRO D  144          0         1.22                     
CISPEP   5 PHE E  155    PRO E  156          0        -5.29                     
CISPEP   6 GLU E  157    PRO E  158          0        -3.63                     
CISPEP   7 SER F    8    PRO F    9          0        -3.80                     
CISPEP   8 TYR F  143    PRO F  144          0         0.15                     
SITE     1 AC1 19 GLY A  28  VAL A  29  GLY A  30  LYS A  31                    
SITE     2 AC1 19 THR A  32  THR A  33  ASN A 272  PRO A 315                    
SITE     3 AC1 19 CYS A 317  ILE A 321  PHE A 330   MG A 402                    
SITE     4 AC1 19 ATP A 404  HOH A 506  HOH A 509  HOH A 592                    
SITE     5 AC1 19 LYS B  26  GLU B 245  LEU B 247                               
SITE     1 AC2  6 THR A  32  ADP A 401  ATP A 404  HOH A 505                    
SITE     2 AC2  6 HOH A 506  HOH A 559                                          
SITE     1 AC3  4 CYS A 285  CYS A 288  CYS B 285  CYS B 288                    
SITE     1 AC4 25 GLY A  27  GLY A  28  VAL A  29  GLY A  30                    
SITE     2 AC4 25 LYS A  31  THR A  32  THR A  33  ASN A  57                    
SITE     3 AC4 25 PRO A 169  ASN A 272  PRO A 315  LEU A 316                    
SITE     4 AC4 25 CYS A 317  ILE A 321  PHE A 330  ADP A 401                    
SITE     5 AC4 25  MG A 402  HOH A 506  HOH A 509  HOH A 592                    
SITE     6 AC4 25 HOH A 595  LYS B  26  GLY B  27  GLU B 245                    
SITE     7 AC4 25 LEU B 247                                                     
SITE     1 AC5 21 LYS A  26  GLU A 245  PHE A 246  LEU A 247                    
SITE     2 AC5 21 GLY B  28  VAL B  29  GLY B  30  LYS B  31                    
SITE     3 AC5 21 THR B  32  THR B  33  ASN B 272  PRO B 315                    
SITE     4 AC5 21 LEU B 316  CYS B 317  ILE B 321  PHE B 330                    
SITE     5 AC5 21  MG B 402  ATP B 403  HOH B 545  HOH B 557                    
SITE     6 AC5 21 HOH B 611                                                     
SITE     1 AC6  6 THR B  32  ADP B 401  ATP B 403  HOH B 528                    
SITE     2 AC6  6 HOH B 571  HOH B 611                                          
SITE     1 AC7 27 LYS A  26  GLY A  27  GLU A 245  PHE A 246                    
SITE     2 AC7 27 LEU A 247  GLY B  27  GLY B  28  VAL B  29                    
SITE     3 AC7 27 GLY B  30  LYS B  31  THR B  32  THR B  33                    
SITE     4 AC7 27 ASN B  57  ASN B 272  PRO B 315  LEU B 316                    
SITE     5 AC7 27 CYS B 317  ILE B 321  PHE B 330  ADP B 401                    
SITE     6 AC7 27  MG B 402  HOH B 528  HOH B 545  HOH B 557                    
SITE     7 AC7 27 HOH B 571  HOH B 611  HOH B 619                               
CRYST1  102.870  112.030  153.690  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.009721  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008926  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006507        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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