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Database: PDB
Entry: 5HSH
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Original site: 5HSH 
HEADER    ISOMERASE                               25-JAN-16   5HSH              
TITLE     CRYSTAL STRUCTURE OF THE G291R MUTANT OF HUMAN PHOSPHOGLUCOMUTASE 1   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHOGLUCOMUTASE-1;                                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PGM 1,GLUCOSE PHOSPHOMUTASE 1;                              
COMPND   5 EC: 5.4.2.2;                                                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PGM1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PMCSG7                                    
KEYWDS    PHOSPHOGLUCOMUTASE, ISOMERASE, ENZYME, MISSENSE MUTANT                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.M.STIERS,L.J.BEAMER                                                 
REVDAT   3   27-NOV-19 5HSH    1       REMARK                                   
REVDAT   2   13-SEP-17 5HSH    1       JRNL   REMARK                            
REVDAT   1   27-APR-16 5HSH    0                                                
JRNL        AUTH   K.M.STIERS,B.N.KAIN,A.C.GRAHAM,L.J.BEAMER                    
JRNL        TITL   INDUCED STRUCTURAL DISORDER AS A MOLECULAR MECHANISM FOR     
JRNL        TITL 2 ENZYME DYSFUNCTION IN PHOSPHOGLUCOMUTASE 1 DEFICIENCY.       
JRNL        REF    J.MOL.BIOL.                   V. 428  1493 2016              
JRNL        REFN                   ESSN 1089-8638                               
JRNL        PMID   26972339                                                     
JRNL        DOI    10.1016/J.JMB.2016.02.032                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.10.1_2155: ???)                            
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) : 2.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 60.54                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 42988                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.232                           
REMARK   3   R VALUE            (WORKING SET) : 0.230                           
REMARK   3   FREE R VALUE                     : 0.273                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.030                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2162                            
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 60.5524 -  6.5329    1.00     2942   156  0.2009 0.2309        
REMARK   3     2  6.5329 -  5.1863    1.00     2807   139  0.2455 0.2929        
REMARK   3     3  5.1863 -  4.5309    1.00     2747   160  0.1988 0.2388        
REMARK   3     4  4.5309 -  4.1168    1.00     2749   138  0.1908 0.2452        
REMARK   3     5  4.1168 -  3.8218    1.00     2732   139  0.2174 0.2452        
REMARK   3     6  3.8218 -  3.5965    1.00     2706   156  0.2213 0.2577        
REMARK   3     7  3.5965 -  3.4164    1.00     2703   143  0.2403 0.3267        
REMARK   3     8  3.4164 -  3.2677    0.99     2688   136  0.2627 0.3326        
REMARK   3     9  3.2677 -  3.1419    1.00     2698   149  0.2791 0.3140        
REMARK   3    10  3.1419 -  3.0335    1.00     2709   123  0.2864 0.3547        
REMARK   3    11  3.0335 -  2.9386    1.00     2664   160  0.2924 0.3240        
REMARK   3    12  2.9386 -  2.8546    1.00     2695   145  0.2957 0.3322        
REMARK   3    13  2.8546 -  2.7795    1.00     2690   126  0.3004 0.3618        
REMARK   3    14  2.7795 -  2.7117    0.99     2658   135  0.3301 0.3408        
REMARK   3    15  2.7117 -  2.6500    0.99     2638   157  0.3726 0.4103        
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)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.290           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.010           7561                                  
REMARK   3   ANGLE     :  1.214          10308                                  
REMARK   3   CHIRALITY :  0.065           1180                                  
REMARK   3   PLANARITY :  0.009           1375                                  
REMARK   3   DIHEDRAL  : 13.397           4425                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 183 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -33.7370  72.8111   1.8739              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9472 T22:   0.6762                                     
REMARK   3      T33:   0.5966 T12:   0.1116                                     
REMARK   3      T13:   0.2082 T23:   0.1502                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4853 L22:   3.8651                                     
REMARK   3      L33:   2.8639 L12:  -0.5793                                     
REMARK   3      L13:   0.8371 L23:   0.6278                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1199 S12:  -0.5128 S13:   0.1837                       
REMARK   3      S21:   0.4808 S22:   0.2729 S23:   0.2472                       
REMARK   3      S31:  -0.8869 S32:  -0.6691 S33:  -0.1315                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 184 THROUGH 405 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.2925  45.7433  -1.3344              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3854 T22:   0.4770                                     
REMARK   3      T33:   0.6195 T12:  -0.0506                                     
REMARK   3      T13:   0.0401 T23:   0.0768                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9451 L22:   2.0934                                     
REMARK   3      L33:   4.0345 L12:  -0.8144                                     
REMARK   3      L13:   0.2122 L23:  -0.5986                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0400 S12:   0.0609 S13:   0.0349                       
REMARK   3      S21:  -0.0154 S22:   0.1235 S23:   0.3075                       
REMARK   3      S31:   0.0250 S32:  -0.0967 S33:  -0.0830                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 406 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.1499  40.3157  23.1204              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5457 T22:   0.6416                                     
REMARK   3      T33:   0.5804 T12:  -0.0094                                     
REMARK   3      T13:   0.0744 T23:   0.0410                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0460 L22:   1.3786                                     
REMARK   3      L33:   5.5222 L12:   1.3417                                     
REMARK   3      L13:  -0.7975 L23:  -0.9087                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2685 S12:  -0.8723 S13:   0.0947                       
REMARK   3      S21:   0.3516 S22:  -0.2595 S23:   0.2457                       
REMARK   3      S31:   0.0899 S32:   0.4030 S33:  -0.0257                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 95 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):  30.0262  62.9439 -14.8334              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6984 T22:   0.8831                                     
REMARK   3      T33:   0.8307 T12:  -0.0957                                     
REMARK   3      T13:   0.1018 T23:  -0.1926                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8221 L22:   3.7551                                     
REMARK   3      L33:   5.2135 L12:   1.8984                                     
REMARK   3      L13:  -0.0031 L23:  -1.7155                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1139 S12:   0.5359 S13:  -0.2616                       
REMARK   3      S21:  -0.0601 S22:   0.1352 S23:  -0.5644                       
REMARK   3      S31:  -0.7047 S32:   1.0440 S33:  -0.3022                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 96 THROUGH 140 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  19.3596  56.8690 -12.9160              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6469 T22:   0.8107                                     
REMARK   3      T33:   0.8076 T12:   0.0686                                     
REMARK   3      T13:  -0.0115 T23:  -0.0956                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2347 L22:   2.8358                                     
REMARK   3      L33:   5.7471 L12:   2.6133                                     
REMARK   3      L13:   0.3876 L23:  -1.6656                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0115 S12:   1.0074 S13:  -0.2316                       
REMARK   3      S21:  -0.1992 S22:   0.3330 S23:   0.0694                       
REMARK   3      S31:  -0.2881 S32:   0.0322 S33:  -0.5005                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 141 THROUGH 170 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.8119  65.6995 -16.1738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9478 T22:   0.9167                                     
REMARK   3      T33:   0.7557 T12:  -0.1503                                     
REMARK   3      T13:   0.1823 T23:  -0.1363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2770 L22:   1.7981                                     
REMARK   3      L33:   4.6465 L12:   0.8905                                     
REMARK   3      L13:   0.4782 L23:   0.2731                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0634 S12:   0.5477 S13:   0.3248                       
REMARK   3      S21:  -0.5644 S22:   0.4731 S23:  -0.5196                       
REMARK   3      S31:  -0.8810 S32:   0.7015 S33:  -0.5119                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 212 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1180  54.1077   0.8531              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6611 T22:   0.6622                                     
REMARK   3      T33:   0.7726 T12:   0.0711                                     
REMARK   3      T13:  -0.0548 T23:   0.0047                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2155 L22:   2.5821                                     
REMARK   3      L33:   2.5381 L12:   1.7653                                     
REMARK   3      L13:  -0.7551 L23:   0.6942                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4745 S12:  -0.1543 S13:  -0.0188                       
REMARK   3      S21:   0.5905 S22:  -0.0111 S23:  -0.2200                       
REMARK   3      S31:  -0.4641 S32:   0.1226 S33:  -0.4054                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 213 THROUGH 293 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  20.1426  33.0860  -6.0776              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7353 T22:   0.7540                                     
REMARK   3      T33:   1.1582 T12:   0.2002                                     
REMARK   3      T13:  -0.2331 T23:  -0.1326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4521 L22:   3.3536                                     
REMARK   3      L33:   3.0054 L12:   0.6033                                     
REMARK   3      L13:   0.4314 L23:   0.8867                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3216 S12:  -0.0735 S13:  -0.8469                       
REMARK   3      S21:   0.1023 S22:   0.0292 S23:  -1.2805                       
REMARK   3      S31:   0.6867 S32:   0.5928 S33:  -0.5780                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 294 THROUGH 434 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.9597  39.2374 -16.8837              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3844 T22:   0.8244                                     
REMARK   3      T33:   0.6630 T12:  -0.0280                                     
REMARK   3      T13:  -0.0079 T23:   0.0194                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5013 L22:   3.7128                                     
REMARK   3      L33:   4.3601 L12:   0.0099                                     
REMARK   3      L13:   1.1573 L23:  -0.1484                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0986 S12:   0.4551 S13:  -0.1312                       
REMARK   3      S21:  -0.1770 S22:   0.2822 S23:  -0.0320                       
REMARK   3      S31:   0.3280 S32:  -0.2895 S33:  -0.3412                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 435 THROUGH 473 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   3.2770  38.8007 -44.7228              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4193 T22:   1.6049                                     
REMARK   3      T33:   0.9917 T12:  -0.1409                                     
REMARK   3      T13:  -0.0811 T23:   0.0228                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6499 L22:   4.3615                                     
REMARK   3      L33:   4.8726 L12:  -0.5617                                     
REMARK   3      L13:   1.1503 L23:   0.4855                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5198 S12:   1.9450 S13:  -1.1735                       
REMARK   3      S21:  -1.9073 S22:  -0.6260 S23:  -0.4482                       
REMARK   3      S31:  -0.3230 S32:   0.2873 S33:  -0.3569                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 474 THROUGH 522 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):   4.7584  44.2343 -33.2566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7656 T22:   1.2324                                     
REMARK   3      T33:   0.7195 T12:  -0.1007                                     
REMARK   3      T13:   0.1009 T23:   0.0500                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5993 L22:   3.4852                                     
REMARK   3      L33:   3.5745 L12:  -1.7214                                     
REMARK   3      L13:   0.5735 L23:   1.1009                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0296 S12:   0.6352 S13:   0.3169                       
REMARK   3      S21:  -1.1911 S22:   0.3195 S23:  -0.0087                       
REMARK   3      S31:  -0.4219 S32:  -0.2082 S33:  -0.2705                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 523 THROUGH 562 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.0629  28.1837 -36.4664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8911 T22:   1.0601                                     
REMARK   3      T33:   1.1838 T12:   0.0675                                     
REMARK   3      T13:   0.0179 T23:  -0.4567                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1554 L22:   4.0042                                     
REMARK   3      L33:   4.5005 L12:  -0.8687                                     
REMARK   3      L13:   1.9101 L23:   0.2351                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3044 S12:   0.5732 S13:  -0.2020                       
REMARK   3      S21:  -0.9912 S22:   0.5309 S23:  -1.1871                       
REMARK   3      S31:   1.0430 S32:   1.0501 S33:  -0.7740                       
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 5HSH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000217660.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-OCT-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 9.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 4.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00003                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CMOS                               
REMARK 200  DETECTOR MANUFACTURER          : RDI CMOS_8M                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48369                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.650                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.537                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 14.00                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.65                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.75                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.10                              
REMARK 200  R MERGE FOR SHELL          (I) : 2.81000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 5EPC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ~1.0M SODIUM CITRATE, 0.1M CHES BUFFER   
REMARK 280  PH 9.7., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 292K            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.64350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       85.39000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       85.39000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       24.82175            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       85.39000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       85.39000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.46525            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       85.39000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       85.39000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       24.82175            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       85.39000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       85.39000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.46525            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       49.64350            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A    64                                                      
REMARK 465     PHE A    65                                                      
REMARK 465     SER A   117                                                      
REMARK 465     HIS A   118                                                      
REMARK 465     ASN A   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     GLY A   121                                                      
REMARK 465     GLY A   122                                                      
REMARK 465     PRO A   123                                                      
REMARK 465     ASN A   124                                                      
REMARK 465     GLY A   125                                                      
REMARK 465     ASP A   256                                                      
REMARK 465     PHE A   257                                                      
REMARK 465     GLY A   258                                                      
REMARK 465     GLY A   259                                                      
REMARK 465     HIS A   260                                                      
REMARK 465     HIS A   261                                                      
REMARK 465     PRO A   262                                                      
REMARK 465     ASP A   263                                                      
REMARK 465     PRO A   264                                                      
REMARK 465     ASN A   265                                                      
REMARK 465     LEU A   266                                                      
REMARK 465     THR A   267                                                      
REMARK 465     GLY A   506                                                      
REMARK 465     THR A   507                                                      
REMARK 465     GLY A   508                                                      
REMARK 465     SER A   509                                                      
REMARK 465     ARG B    64                                                      
REMARK 465     PHE B    65                                                      
REMARK 465     HIS B   118                                                      
REMARK 465     ASN B   119                                                      
REMARK 465     PRO B   120                                                      
REMARK 465     GLY B   121                                                      
REMARK 465     GLY B   122                                                      
REMARK 465     PRO B   123                                                      
REMARK 465     ASN B   124                                                      
REMARK 465     GLY B   125                                                      
REMARK 465     PRO B   253                                                      
REMARK 465     LEU B   254                                                      
REMARK 465     GLU B   255                                                      
REMARK 465     ASP B   256                                                      
REMARK 465     PHE B   257                                                      
REMARK 465     GLY B   258                                                      
REMARK 465     GLY B   259                                                      
REMARK 465     HIS B   260                                                      
REMARK 465     HIS B   261                                                      
REMARK 465     PRO B   262                                                      
REMARK 465     ASP B   263                                                      
REMARK 465     PRO B   264                                                      
REMARK 465     ASN B   265                                                      
REMARK 465     LEU B   266                                                      
REMARK 465     THR B   267                                                      
REMARK 465     TYR B   268                                                      
REMARK 465     SER B   505                                                      
REMARK 465     GLY B   506                                                      
REMARK 465     THR B   507                                                      
REMARK 465     GLY B   508                                                      
REMARK 465     SER B   509                                                      
REMARK 465     ALA B   510                                                      
REMARK 465     GLY B   511                                                      
REMARK 465     ALA B   512                                                      
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     VAL A   2    CG1  CG2                                            
REMARK 470     LYS A   3    CG   CD   CE   NZ                                   
REMARK 470     VAL A   5    CG1  CG2                                            
REMARK 470     LYS A   8    CG   CD   CE   NZ                                   
REMARK 470     GLN A  10    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  16    CG   CD   CE   NZ                                   
REMARK 470     THR A  19    OG1  CG2                                            
REMARK 470     SER A  20    OG                                                  
REMARK 470     LEU A  22    CG   CD1  CD2                                       
REMARK 470     ARG A  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     ARG A  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A  26    CG1  CG2                                            
REMARK 470     LYS A  27    CG   CD   CE   NZ                                   
REMARK 470     VAL A  28    CG1  CG2                                            
REMARK 470     GLN A  30    CG   CD   OE1  NE2                                  
REMARK 470     SER A  31    OG                                                  
REMARK 470     ILE A  40    CG1  CG2  CD1                                       
REMARK 470     ILE A  43    CG1  CG2  CD1                                       
REMARK 470     VAL A  47    CG1  CG2                                            
REMARK 470     GLU A  48    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  51    CG   CD   OE1  NE2                                  
REMARK 470     GLN A  53    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  54    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  62    CG   OD1  OD2                                       
REMARK 470     TYR A  66    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     MET A  67    CG   SD   CE                                        
REMARK 470     LEU A  73    CG   CD1  CD2                                       
REMARK 470     ILE A  74    CG1  CG2  CD1                                       
REMARK 470     LYS A 105    CG   CD   CE   NZ                                   
REMARK 470     LYS A 107    CG   CD   CE   NZ                                   
REMARK 470     ASP A 126    CG   OD1  OD2                                       
REMARK 470     ILE A 143    CG1  CG2  CD1                                       
REMARK 470     THR A 144    OG1  CG2                                            
REMARK 470     LYS A 146    CG   CD   CE   NZ                                   
REMARK 470     ILE A 147    CG1  CG2  CD1                                       
REMARK 470     PHE A 148    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A 149    CG   CD   OE1  NE2                                  
REMARK 470     ILE A 150    CG1  CG2  CD1                                       
REMARK 470     LYS A 152    CG   CD   CE   NZ                                   
REMARK 470     THR A 153    OG1  CG2                                            
REMARK 470     ILE A 154    CG1  CG2  CD1                                       
REMARK 470     GLU A 155    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 156    CG   CD   OE1  OE2                                  
REMARK 470     VAL A 159    CG1  CG2                                            
REMARK 470     ASP A 162    CG   OD1  OD2                                       
REMARK 470     LYS A 164    CG   CD   CE   NZ                                   
REMARK 470     VAL A 169    CG1  CG2                                            
REMARK 470     LYS A 172    CG   CD   CE   NZ                                   
REMARK 470     LYS A 180    CG   CD   CE   NZ                                   
REMARK 470     LYS A 182    CG   CD   CE   NZ                                   
REMARK 470     LYS A 209    CG   CD   CE   NZ                                   
REMARK 470     PRO A 215    CG   CD                                             
REMARK 470     ASN A 216    CG   OD1  ND2                                       
REMARK 470     VAL A 228    CG1  CG2                                            
REMARK 470     LYS A 234    CG   CD   CE   NZ                                   
REMARK 470     VAL A 249    CG1  CG2                                            
REMARK 470     VAL A 252    CG1  CG2                                            
REMARK 470     LEU A 254    CG   CD1  CD2                                       
REMARK 470     GLU A 255    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 268    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     VAL A 273    CG1  CG2                                            
REMARK 470     GLU A 274    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 277    CG   CD   CE   NZ                                   
REMARK 470     GLU A 280    CG   CD   OE1  OE2                                  
REMARK 470     GLN A 325    CG   CD   OE1  NE2                                  
REMARK 470     SER A 346    OG                                                  
REMARK 470     LYS A 360    CG   CD   CE   NZ                                   
REMARK 470     LYS A 370    CG   CD   CE   NZ                                   
REMARK 470     LYS A 406    CG   CD   CE   NZ                                   
REMARK 470     VAL A 433    CG1  CG2                                            
REMARK 470     GLU A 436    CG   CD   OE1  OE2                                  
REMARK 470     ASN A 439    CG   OD1  ND2                                       
REMARK 470     LYS A 440    CG   CD   CE   NZ                                   
REMARK 470     LYS A 443    CG   CD   CE   NZ                                   
REMARK 470     PHE A 450    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP A 451    CG   OD1  OD2                                       
REMARK 470     ARG A 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER A 453    OG                                                  
REMARK 470     VAL A 455    CG1  CG2                                            
REMARK 470     LYS A 457    CG   CD   CE   NZ                                   
REMARK 470     GLN A 458    CG   CD   OE1  NE2                                  
REMARK 470     SER A 460    OG                                                  
REMARK 470     ASN A 462    CG   OD1  ND2                                       
REMARK 470     ASP A 463    CG   OD1  OD2                                       
REMARK 470     LYS A 464    CG   CD   CE   NZ                                   
REMARK 470     VAL A 465    CG1  CG2                                            
REMARK 470     VAL A 468    CG1  CG2                                            
REMARK 470     LYS A 470    CG   CD   CE   NZ                                   
REMARK 470     GLU A 475    CG   CD   OE1  OE2                                  
REMARK 470     SER A 477    OG                                                  
REMARK 470     VAL A 480    CG1  CG2                                            
REMARK 470     SER A 483    OG                                                  
REMARK 470     ILE A 484    CG1  CG2  CD1                                       
REMARK 470     ARG A 486    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 487    CG   OD1  ND2                                       
REMARK 470     VAL A 501    CG1  CG2                                            
REMARK 470     LEU A 504    CG   CD1  CD2                                       
REMARK 470     SER A 505    OG                                                  
REMARK 470     ILE A 514    CG1  CG2  CD1                                       
REMARK 470     LYS A 523    CG   CD   CE   NZ                                   
REMARK 470     ASP A 524    CG   OD1  OD2                                       
REMARK 470     VAL A 525    CG1  CG2                                            
REMARK 470     LYS A 527    CG   CD   CE   NZ                                   
REMARK 470     ILE A 528    CG1  CG2  CD1                                       
REMARK 470     ASN A 529    CG   OD1  ND2                                       
REMARK 470     LEU A 536    CG   CD1  CD2                                       
REMARK 470     LYS A 545    CG   CD   CE   NZ                                   
REMARK 470     VAL A 546    CG1  CG2                                            
REMARK 470     GLN A 548    CG   CD   OE1  NE2                                  
REMARK 470     THR A 553    OG1  CG2                                            
REMARK 470     VAL B   2    CG1  CG2                                            
REMARK 470     LYS B   3    CG   CD   CE   NZ                                   
REMARK 470     VAL B   5    CG1  CG2                                            
REMARK 470     THR B   6    OG1  CG2                                            
REMARK 470     LYS B   8    CG   CD   CE   NZ                                   
REMARK 470     THR B   9    OG1  CG2                                            
REMARK 470     GLN B  10    CG   CD   OE1  NE2                                  
REMARK 470     ASP B  14    CG   OD1  OD2                                       
REMARK 470     LYS B  16    CG   CD   CE   NZ                                   
REMARK 470     THR B  19    OG1  CG2                                            
REMARK 470     SER B  20    OG                                                  
REMARK 470     ARG B  23    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B  24    CG   CD   CE   NZ                                   
REMARK 470     ARG B  25    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B  26    CG1  CG2                                            
REMARK 470     LYS B  27    CG   CD   CE   NZ                                   
REMARK 470     VAL B  28    CG1  CG2                                            
REMARK 470     SER B  31    OG                                                  
REMARK 470     ASN B  38    CG   OD1  ND2                                       
REMARK 470     ILE B  40    CG1  CG2  CD1                                       
REMARK 470     VAL B  47    CG1  CG2                                            
REMARK 470     GLU B  48    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  54    CG   CD   OE1  OE2                                  
REMARK 470     TYR B  66    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU B  69    CG   CD   OE1  OE2                                  
REMARK 470     LEU B  73    CG   CD1  CD2                                       
REMARK 470     ILE B  77    CG1  CG2  CD1                                       
REMARK 470     LYS B 105    CG   CD   CE   NZ                                   
REMARK 470     LYS B 107    CG   CD   CE   NZ                                   
REMARK 470     ILE B 109    CG1  CG2  CD1                                       
REMARK 470     ASP B 126    CG   OD1  OD2                                       
REMARK 470     ILE B 143    CG1  CG2  CD1                                       
REMARK 470     LYS B 146    CG   CD   CE   NZ                                   
REMARK 470     ILE B 147    CG1  CG2  CD1                                       
REMARK 470     PHE B 148    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN B 149    CG   CD   OE1  NE2                                  
REMARK 470     ILE B 150    CG1  CG2  CD1                                       
REMARK 470     LYS B 152    CG   CD   CE   NZ                                   
REMARK 470     ILE B 154    CG1  CG2  CD1                                       
REMARK 470     GLU B 155    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 156    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 159    CG1  CG2                                            
REMARK 470     ASP B 162    CG   OD1  OD2                                       
REMARK 470     LYS B 164    CG   CD   CE   NZ                                   
REMARK 470     VAL B 165    CG1  CG2                                            
REMARK 470     VAL B 169    CG1  CG2                                            
REMARK 470     LYS B 172    CG   CD   CE   NZ                                   
REMARK 470     ASP B 176    CG   OD1  OD2                                       
REMARK 470     LEU B 177    CG   CD1  CD2                                       
REMARK 470     ASN B 179    CG   OD1  ND2                                       
REMARK 470     LYS B 180    CG   CD   CE   NZ                                   
REMARK 470     LYS B 182    CG   CD   CE   NZ                                   
REMARK 470     VAL B 186    CG1  CG2                                            
REMARK 470     SER B 206    OG                                                  
REMARK 470     LYS B 209    CG   CD   CE   NZ                                   
REMARK 470     SER B 213    OG                                                  
REMARK 470     PRO B 215    CG   CD                                             
REMARK 470     ASN B 216    CG   OD1  ND2                                       
REMARK 470     LYS B 219    CG   CD   CE   NZ                                   
REMARK 470     ILE B 220    CG1  CG2  CD1                                       
REMARK 470     ARG B 221    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL B 228    CG1  CG2                                            
REMARK 470     VAL B 229    CG1  CG2                                            
REMARK 470     VAL B 233    CG1  CG2                                            
REMARK 470     LYS B 234    CG   CD   CE   NZ                                   
REMARK 470     VAL B 249    CG1  CG2                                            
REMARK 470     VAL B 252    CG1  CG2                                            
REMARK 470     ASP B 271    CG   OD1  OD2                                       
REMARK 470     VAL B 273    CG1  CG2                                            
REMARK 470     GLU B 274    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 277    CG   CD   CE   NZ                                   
REMARK 470     SER B 278    OG                                                  
REMARK 470     GLU B 280    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 291    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 293    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B 299    CG   CD   CE   NZ                                   
REMARK 470     VAL B 304    CG1  CG2                                            
REMARK 470     VAL B 310    CG1  CG2                                            
REMARK 470     SER B 319    OG                                                  
REMARK 470     ARG B 329    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 343    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 348    OG1  CG2                                            
REMARK 470     LYS B 360    CG   CD   CE   NZ                                   
REMARK 470     LYS B 370    CG   CD   CE   NZ                                   
REMARK 470     LYS B 406    CG   CD   CE   NZ                                   
REMARK 470     GLN B 418    CG   CD   OE1  NE2                                  
REMARK 470     LYS B 419    CG   CD   CE   NZ                                   
REMARK 470     THR B 426    OG1  CG2                                            
REMARK 470     GLU B 431    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 432    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 433    CG1  CG2                                            
REMARK 470     GLU B 434    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 436    CG   CD   OE1  OE2                                  
REMARK 470     ASN B 439    CG   OD1  ND2                                       
REMARK 470     LYS B 440    CG   CD   CE   NZ                                   
REMARK 470     LYS B 443    CG   CD   CE   NZ                                   
REMARK 470     ASP B 444    CG   OD1  OD2                                       
REMARK 470     LEU B 445    CG   CD1  CD2                                       
REMARK 470     GLU B 446    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 448    CG   CD1  CD2                                       
REMARK 470     PHE B 450    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG B 452    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER B 453    OG                                                  
REMARK 470     VAL B 455    CG1  CG2                                            
REMARK 470     LYS B 457    CG   CD   CE   NZ                                   
REMARK 470     GLN B 458    CG   CD   OE1  NE2                                  
REMARK 470     PHE B 459    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER B 460    OG                                                  
REMARK 470     ASN B 462    CG   OD1  ND2                                       
REMARK 470     ASP B 463    CG   OD1  OD2                                       
REMARK 470     LYS B 464    CG   CD   CE   NZ                                   
REMARK 470     VAL B 465    CG1  CG2                                            
REMARK 470     THR B 467    OG1  CG2                                            
REMARK 470     VAL B 468    CG1  CG2                                            
REMARK 470     LYS B 470    CG   CD   CE   NZ                                   
REMARK 470     VAL B 480    CG1  CG2                                            
REMARK 470     ILE B 484    CG1  CG2  CD1                                       
REMARK 470     LEU B 490    CG   CD1  CD2                                       
REMARK 470     ILE B 493    CG1  CG2  CD1                                       
REMARK 470     THR B 495    OG1  CG2                                            
REMARK 470     ILE B 500    CG1  CG2  CD1                                       
REMARK 470     VAL B 501    CG1  CG2                                            
REMARK 470     PHE B 502    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU B 504    CG   CD1  CD2                                       
REMARK 470     ILE B 514    CG1  CG2  CD1                                       
REMARK 470     LEU B 516    CG   CD1  CD2                                       
REMARK 470     ILE B 518    CG1  CG2  CD1                                       
REMARK 470     LYS B 523    CG   CD   CE   NZ                                   
REMARK 470     ASP B 524    CG   OD1  OD2                                       
REMARK 470     VAL B 525    CG1  CG2                                            
REMARK 470     LYS B 527    CG   CD   CE   NZ                                   
REMARK 470     ILE B 528    CG1  CG2  CD1                                       
REMARK 470     ASN B 529    CG   OD1  ND2                                       
REMARK 470     GLN B 530    CG   CD   OE1  NE2                                  
REMARK 470     PRO B 532    CG   CD                                             
REMARK 470     GLN B 533    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 534    CG1  CG2                                            
REMARK 470     LEU B 536    CG   CD1  CD2                                       
REMARK 470     LEU B 539    CG   CD1  CD2                                       
REMARK 470     ILE B 540    CG1  CG2  CD1                                       
REMARK 470     ILE B 542    CG1  CG2  CD1                                       
REMARK 470     LEU B 544    CG   CD1  CD2                                       
REMARK 470     LYS B 545    CG   CD   CE   NZ                                   
REMARK 470     VAL B 546    CG1  CG2                                            
REMARK 470     GLN B 548    CG   CD   OE1  NE2                                  
REMARK 470     LEU B 549    CG   CD1  CD2                                       
REMARK 470     GLN B 550    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 551    CG   CD   OE1  OE2                                  
REMARK 470     ARG B 552    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR B 553    OG1  CG2                                            
REMARK 470     VAL B 560    CG1  CG2                                            
REMARK 470     ILE B 561    CG1  CG2  CD1                                       
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   NH1  ARG B   333     O    THR B   337              2.00            
REMARK 500   OD2  ASP A   444     NH1  ARG A   552              2.12            
REMARK 500   OD2  ASP A   271     O    HOH A   701              2.15            
REMARK 500   O    ASN A   462     O    HOH A   702              2.15            
REMARK 500   O    THR B   348     N    ILE B   350              2.16            
REMARK 500   OD1  ASP A   411     O    HOH A   703              2.17            
REMARK 500   OD2  ASP A   519     O    HOH A   704              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    MET A 441   CB  -  CG  -  SD  ANGL. DEV. =  19.4 DEGREES          
REMARK 500    ARG A 552   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.3 DEGREES          
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    ASP A  14       31.99    -87.77                                   
REMARK 500    GLN A  15       50.44   -109.69                                   
REMARK 500    CYS A 160       79.89   -102.19                                   
REMARK 500    ASN A 179       19.81     53.67                                   
REMARK 500    PRO A 215      -90.54    -49.22                                   
REMARK 500    ASN A 216       43.24    -89.62                                   
REMARK 500    CYS A 238      -62.92    -91.06                                   
REMARK 500    CYS A 251       44.31    -88.55                                   
REMARK 500    ASP A 290      -76.10    135.95                                   
REMARK 500    ARG A 291       29.62   -141.34                                   
REMARK 500    THR A 348       -8.48   -150.17                                   
REMARK 500    LYS A 349       -3.68     75.47                                   
REMARK 500    SER A 378       42.36    -75.64                                   
REMARK 500    ALA A 461      130.42     87.29                                   
REMARK 500    ALA B 116     -131.58    -93.26                                   
REMARK 500    CYS B 160       79.28   -102.55                                   
REMARK 500    ASN B 179       18.17     55.62                                   
REMARK 500    ASN B 216       36.66    -86.98                                   
REMARK 500    CYS B 251       46.99    -85.11                                   
REMARK 500    ASP B 290      -80.66    144.90                                   
REMARK 500    ARG B 291       26.40   -141.63                                   
REMARK 500    THR B 348      105.53   -166.43                                   
REMARK 500    LYS B 349        0.82    -23.33                                   
REMARK 500    SER B 378       41.05    -77.18                                   
REMARK 500    ALA B 461      159.86    151.76                                   
REMARK 500    ASP B 463      -38.46   -178.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 601                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5EPC   RELATED DB: PDB                                   
REMARK 900 HUMAN PHOSPHOGLUCOMUTASE 1                                           
REMARK 900 RELATED ID: 5F9C   RELATED DB: PDB                                   
REMARK 900 MUTANT OF HUMAN PHOSPHOGLUCOMUTASE 1                                 
DBREF  5HSH A    1   562  UNP    P36871   PGM1_HUMAN       1    562             
DBREF  5HSH B    1   562  UNP    P36871   PGM1_HUMAN       1    562             
SEQADV 5HSH ARG A  291  UNP  P36871    GLY   291 ENGINEERED MUTATION            
SEQADV 5HSH ARG B  291  UNP  P36871    GLY   291 ENGINEERED MUTATION            
SEQRES   1 A  562  MET VAL LYS ILE VAL THR VAL LYS THR GLN ALA TYR GLN          
SEQRES   2 A  562  ASP GLN LYS PRO GLY THR SER GLY LEU ARG LYS ARG VAL          
SEQRES   3 A  562  LYS VAL PHE GLN SER SER ALA ASN TYR ALA GLU ASN PHE          
SEQRES   4 A  562  ILE GLN SER ILE ILE SER THR VAL GLU PRO ALA GLN ARG          
SEQRES   5 A  562  GLN GLU ALA THR LEU VAL VAL GLY GLY ASP GLY ARG PHE          
SEQRES   6 A  562  TYR MET LYS GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA          
SEQRES   7 A  562  ALA ALA ASN GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN          
SEQRES   8 A  562  GLY ILE LEU SER THR PRO ALA VAL SER CYS ILE ILE ARG          
SEQRES   9 A  562  LYS ILE LYS ALA ILE GLY GLY ILE ILE LEU THR ALA SER          
SEQRES  10 A  562  HIS ASN PRO GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS          
SEQRES  11 A  562  PHE ASN ILE SER ASN GLY GLY PRO ALA PRO GLU ALA ILE          
SEQRES  12 A  562  THR ASP LYS ILE PHE GLN ILE SER LYS THR ILE GLU GLU          
SEQRES  13 A  562  TYR ALA VAL CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL          
SEQRES  14 A  562  LEU GLY LYS GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS          
SEQRES  15 A  562  PRO PHE THR VAL GLU ILE VAL ASP SER VAL GLU ALA TYR          
SEQRES  16 A  562  ALA THR MET LEU ARG SER ILE PHE ASP PHE SER ALA LEU          
SEQRES  17 A  562  LYS GLU LEU LEU SER GLY PRO ASN ARG LEU LYS ILE ARG          
SEQRES  18 A  562  ILE ASP ALA MET HIS GLY VAL VAL GLY PRO TYR VAL LYS          
SEQRES  19 A  562  LYS ILE LEU CYS GLU GLU LEU GLY ALA PRO ALA ASN SER          
SEQRES  20 A  562  ALA VAL ASN CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS          
SEQRES  21 A  562  HIS PRO ASP PRO ASN LEU THR TYR ALA ALA ASP LEU VAL          
SEQRES  22 A  562  GLU THR MET LYS SER GLY GLU HIS ASP PHE GLY ALA ALA          
SEQRES  23 A  562  PHE ASP GLY ASP ARG ASP ARG ASN MET ILE LEU GLY LYS          
SEQRES  24 A  562  HIS GLY PHE PHE VAL ASN PRO SER ASP SER VAL ALA VAL          
SEQRES  25 A  562  ILE ALA ALA ASN ILE PHE SER ILE PRO TYR PHE GLN GLN          
SEQRES  26 A  562  THR GLY VAL ARG GLY PHE ALA ARG SER MET PRO THR SER          
SEQRES  27 A  562  GLY ALA LEU ASP ARG VAL ALA SER ALA THR LYS ILE ALA          
SEQRES  28 A  562  LEU TYR GLU THR PRO THR GLY TRP LYS PHE PHE GLY ASN          
SEQRES  29 A  562  LEU MET ASP ALA SER LYS LEU SER LEU CYS GLY GLU GLU          
SEQRES  30 A  562  SER PHE GLY THR GLY SER ASP HIS ILE ARG GLU LYS ASP          
SEQRES  31 A  562  GLY LEU TRP ALA VAL LEU ALA TRP LEU SER ILE LEU ALA          
SEQRES  32 A  562  THR ARG LYS GLN SER VAL GLU ASP ILE LEU LYS ASP HIS          
SEQRES  33 A  562  TRP GLN LYS TYR GLY ARG ASN PHE PHE THR ARG TYR ASP          
SEQRES  34 A  562  TYR GLU GLU VAL GLU ALA GLU GLY ALA ASN LYS MET MET          
SEQRES  35 A  562  LYS ASP LEU GLU ALA LEU MET PHE ASP ARG SER PHE VAL          
SEQRES  36 A  562  GLY LYS GLN PHE SER ALA ASN ASP LYS VAL TYR THR VAL          
SEQRES  37 A  562  GLU LYS ALA ASP ASN PHE GLU TYR SER ASP PRO VAL ASP          
SEQRES  38 A  562  GLY SER ILE SER ARG ASN GLN GLY LEU ARG LEU ILE PHE          
SEQRES  39 A  562  THR ASP GLY SER ARG ILE VAL PHE ARG LEU SER GLY THR          
SEQRES  40 A  562  GLY SER ALA GLY ALA THR ILE ARG LEU TYR ILE ASP SER          
SEQRES  41 A  562  TYR GLU LYS ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN          
SEQRES  42 A  562  VAL MET LEU ALA PRO LEU ILE SER ILE ALA LEU LYS VAL          
SEQRES  43 A  562  SER GLN LEU GLN GLU ARG THR GLY ARG THR ALA PRO THR          
SEQRES  44 A  562  VAL ILE THR                                                  
SEQRES   1 B  562  MET VAL LYS ILE VAL THR VAL LYS THR GLN ALA TYR GLN          
SEQRES   2 B  562  ASP GLN LYS PRO GLY THR SER GLY LEU ARG LYS ARG VAL          
SEQRES   3 B  562  LYS VAL PHE GLN SER SER ALA ASN TYR ALA GLU ASN PHE          
SEQRES   4 B  562  ILE GLN SER ILE ILE SER THR VAL GLU PRO ALA GLN ARG          
SEQRES   5 B  562  GLN GLU ALA THR LEU VAL VAL GLY GLY ASP GLY ARG PHE          
SEQRES   6 B  562  TYR MET LYS GLU ALA ILE GLN LEU ILE ALA ARG ILE ALA          
SEQRES   7 B  562  ALA ALA ASN GLY ILE GLY ARG LEU VAL ILE GLY GLN ASN          
SEQRES   8 B  562  GLY ILE LEU SER THR PRO ALA VAL SER CYS ILE ILE ARG          
SEQRES   9 B  562  LYS ILE LYS ALA ILE GLY GLY ILE ILE LEU THR ALA SER          
SEQRES  10 B  562  HIS ASN PRO GLY GLY PRO ASN GLY ASP PHE GLY ILE LYS          
SEQRES  11 B  562  PHE ASN ILE SER ASN GLY GLY PRO ALA PRO GLU ALA ILE          
SEQRES  12 B  562  THR ASP LYS ILE PHE GLN ILE SER LYS THR ILE GLU GLU          
SEQRES  13 B  562  TYR ALA VAL CYS PRO ASP LEU LYS VAL ASP LEU GLY VAL          
SEQRES  14 B  562  LEU GLY LYS GLN GLN PHE ASP LEU GLU ASN LYS PHE LYS          
SEQRES  15 B  562  PRO PHE THR VAL GLU ILE VAL ASP SER VAL GLU ALA TYR          
SEQRES  16 B  562  ALA THR MET LEU ARG SER ILE PHE ASP PHE SER ALA LEU          
SEQRES  17 B  562  LYS GLU LEU LEU SER GLY PRO ASN ARG LEU LYS ILE ARG          
SEQRES  18 B  562  ILE ASP ALA MET HIS GLY VAL VAL GLY PRO TYR VAL LYS          
SEQRES  19 B  562  LYS ILE LEU CYS GLU GLU LEU GLY ALA PRO ALA ASN SER          
SEQRES  20 B  562  ALA VAL ASN CYS VAL PRO LEU GLU ASP PHE GLY GLY HIS          
SEQRES  21 B  562  HIS PRO ASP PRO ASN LEU THR TYR ALA ALA ASP LEU VAL          
SEQRES  22 B  562  GLU THR MET LYS SER GLY GLU HIS ASP PHE GLY ALA ALA          
SEQRES  23 B  562  PHE ASP GLY ASP ARG ASP ARG ASN MET ILE LEU GLY LYS          
SEQRES  24 B  562  HIS GLY PHE PHE VAL ASN PRO SER ASP SER VAL ALA VAL          
SEQRES  25 B  562  ILE ALA ALA ASN ILE PHE SER ILE PRO TYR PHE GLN GLN          
SEQRES  26 B  562  THR GLY VAL ARG GLY PHE ALA ARG SER MET PRO THR SER          
SEQRES  27 B  562  GLY ALA LEU ASP ARG VAL ALA SER ALA THR LYS ILE ALA          
SEQRES  28 B  562  LEU TYR GLU THR PRO THR GLY TRP LYS PHE PHE GLY ASN          
SEQRES  29 B  562  LEU MET ASP ALA SER LYS LEU SER LEU CYS GLY GLU GLU          
SEQRES  30 B  562  SER PHE GLY THR GLY SER ASP HIS ILE ARG GLU LYS ASP          
SEQRES  31 B  562  GLY LEU TRP ALA VAL LEU ALA TRP LEU SER ILE LEU ALA          
SEQRES  32 B  562  THR ARG LYS GLN SER VAL GLU ASP ILE LEU LYS ASP HIS          
SEQRES  33 B  562  TRP GLN LYS TYR GLY ARG ASN PHE PHE THR ARG TYR ASP          
SEQRES  34 B  562  TYR GLU GLU VAL GLU ALA GLU GLY ALA ASN LYS MET MET          
SEQRES  35 B  562  LYS ASP LEU GLU ALA LEU MET PHE ASP ARG SER PHE VAL          
SEQRES  36 B  562  GLY LYS GLN PHE SER ALA ASN ASP LYS VAL TYR THR VAL          
SEQRES  37 B  562  GLU LYS ALA ASP ASN PHE GLU TYR SER ASP PRO VAL ASP          
SEQRES  38 B  562  GLY SER ILE SER ARG ASN GLN GLY LEU ARG LEU ILE PHE          
SEQRES  39 B  562  THR ASP GLY SER ARG ILE VAL PHE ARG LEU SER GLY THR          
SEQRES  40 B  562  GLY SER ALA GLY ALA THR ILE ARG LEU TYR ILE ASP SER          
SEQRES  41 B  562  TYR GLU LYS ASP VAL ALA LYS ILE ASN GLN ASP PRO GLN          
SEQRES  42 B  562  VAL MET LEU ALA PRO LEU ILE SER ILE ALA LEU LYS VAL          
SEQRES  43 B  562  SER GLN LEU GLN GLU ARG THR GLY ARG THR ALA PRO THR          
SEQRES  44 B  562  VAL ILE THR                                                  
HET    SO4  A 601       5                                                       
HET    SO4  A 602       5                                                       
HET    SO4  A 603       5                                                       
HET    SO4  A 604       5                                                       
HET    SO4  B 601       5                                                       
HETNAM     SO4 SULFATE ION                                                      
FORMUL   3  SO4    5(O4 S 2-)                                                   
FORMUL   8  HOH   *101(H2 O)                                                    
HELIX    1 AA1 ARG A   25  SER A   31  1                                   7    
HELIX    2 AA2 ASN A   34  SER A   45  1                                  12    
HELIX    3 AA3 THR A   46  VAL A   47  5                                   2    
HELIX    4 AA4 GLU A   48  ARG A   52  5                                   5    
HELIX    5 AA5 MET A   67  ASN A   81  1                                  15    
HELIX    6 AA6 ASN A   91  ILE A   93  5                                   3    
HELIX    7 AA7 SER A   95  LYS A  107  1                                  13    
HELIX    8 AA8 PRO A  140  ILE A  154  1                                  15    
HELIX    9 AA9 VAL A  192  PHE A  203  1                                  12    
HELIX   10 AB1 ASP A  204  SER A  213  1                                  10    
HELIX   11 AB2 VAL A  228  LEU A  237  1                                  10    
HELIX   12 AB3 PRO A  244  ASN A  246  5                                   3    
HELIX   13 AB4 ALA A  269  SER A  278  1                                  10    
HELIX   14 AB5 ASN A  305  ASN A  316  1                                  12    
HELIX   15 AB6 ILE A  317  SER A  319  5                                   3    
HELIX   16 AB7 ILE A  320  GLY A  327  1                                   8    
HELIX   17 AB8 GLY A  339  ALA A  347  1                                   9    
HELIX   18 AB9 TRP A  359  ALA A  368  1                                  10    
HELIX   19 AC1 ASP A  390  LYS A  406  1                                  17    
HELIX   20 AC2 SER A  408  GLY A  421  1                                  14    
HELIX   21 AC3 GLU A  434  MET A  449  1                                  16    
HELIX   22 AC4 ASP A  524  ASN A  529  1                                   6    
HELIX   23 AC5 ASP A  531  GLN A  548  1                                  18    
HELIX   24 AC6 GLN A  548  GLY A  554  1                                   7    
HELIX   25 AC7 ARG B   25  SER B   31  1                                   7    
HELIX   26 AC8 ASN B   34  SER B   45  1                                  12    
HELIX   27 AC9 THR B   46  VAL B   47  5                                   2    
HELIX   28 AD1 GLU B   48  ARG B   52  5                                   5    
HELIX   29 AD2 MET B   67  ASN B   81  1                                  15    
HELIX   30 AD3 ASN B   91  ILE B   93  5                                   3    
HELIX   31 AD4 SER B   95  LYS B  107  1                                  13    
HELIX   32 AD5 PRO B  140  ILE B  154  1                                  15    
HELIX   33 AD6 VAL B  192  PHE B  203  1                                  12    
HELIX   34 AD7 ASP B  204  SER B  213  1                                  10    
HELIX   35 AD8 VAL B  228  ILE B  236  1                                   9    
HELIX   36 AD9 PRO B  244  ASN B  246  5                                   3    
HELIX   37 AE1 ALA B  270  LYS B  277  1                                   8    
HELIX   38 AE2 ASN B  305  ASN B  316  1                                  12    
HELIX   39 AE3 ILE B  317  SER B  319  5                                   3    
HELIX   40 AE4 ILE B  320  GLY B  327  1                                   8    
HELIX   41 AE5 GLY B  339  SER B  346  1                                   8    
HELIX   42 AE6 TRP B  359  ALA B  368  1                                  10    
HELIX   43 AE7 ASP B  390  LYS B  406  1                                  17    
HELIX   44 AE8 SER B  408  GLY B  421  1                                  14    
HELIX   45 AE9 GLU B  434  MET B  449  1                                  16    
HELIX   46 AF1 ASP B  524  ASN B  529  1                                   6    
HELIX   47 AF2 ASP B  531  GLN B  548  1                                  18    
HELIX   48 AF3 GLN B  548  THR B  553  1                                   6    
SHEET    1 AA1 2 VAL A   5  LYS A   8  0                                        
SHEET    2 AA1 2 GLU A 156  VAL A 159 -1  O  TYR A 157   N  VAL A   7           
SHEET    1 AA2 7 LEU A  22  LYS A  24  0                                        
SHEET    2 AA2 7 PHE A 127  ASN A 132 -1  O  ILE A 129   N  LEU A  22           
SHEET    3 AA2 7 GLY A 110  THR A 115 -1  N  THR A 115   O  GLY A 128           
SHEET    4 AA2 7 THR A  56  GLY A  60  1  N  VAL A  58   O  ILE A 112           
SHEET    5 AA2 7 ARG A  85  GLY A  89  1  O  VAL A  87   N  LEU A  57           
SHEET    6 AA2 7 PHE A 184  VAL A 189  1  O  VAL A 189   N  ILE A  88           
SHEET    7 AA2 7 GLY A 171  PHE A 175 -1  N  PHE A 175   O  PHE A 184           
SHEET    1 AA3 5 ALA A 248  VAL A 249  0                                        
SHEET    2 AA3 5 ILE A 220  ASP A 223  1  N  ILE A 222   O  VAL A 249           
SHEET    3 AA3 5 PHE A 283  PHE A 287  1  O  ALA A 285   N  ASP A 223           
SHEET    4 AA3 5 ASN A 294  GLY A 298 -1  O  LEU A 297   N  GLY A 284           
SHEET    5 AA3 5 PHE A 302  VAL A 304 -1  O  PHE A 302   N  GLY A 298           
SHEET    1 AA4 4 LEU A 352  THR A 355  0                                        
SHEET    2 AA4 4 PHE A 331  SER A 334  1  N  PHE A 331   O  TYR A 353           
SHEET    3 AA4 4 LEU A 373  GLU A 376  1  O  LEU A 373   N  ALA A 332           
SHEET    4 AA4 4 GLY A 380  SER A 383 -1  O  GLY A 380   N  GLU A 376           
SHEET    1 AA5 7 GLN A 458  SER A 460  0                                        
SHEET    2 AA5 7 VAL A 465  ASN A 473 -1  O  TYR A 466   N  PHE A 459           
SHEET    3 AA5 7 LEU A 490  PHE A 494 -1  O  ILE A 493   N  LYS A 470           
SHEET    4 AA5 7 ARG A 499  SER A 505 -1  O  PHE A 502   N  LEU A 490           
SHEET    5 AA5 7 ALA A 512  GLU A 522 -1  O  ARG A 515   N  ARG A 503           
SHEET    6 AA5 7 ARG A 422  VAL A 433 -1  N  VAL A 433   O  ALA A 512           
SHEET    7 AA5 7 VAL A 560  THR A 562 -1  O  VAL A 560   N  ASP A 429           
SHEET    1 AA6 2 TYR A 476  SER A 477  0                                        
SHEET    2 AA6 2 ILE A 484  SER A 485 -1  O  SER A 485   N  TYR A 476           
SHEET    1 AA7 2 VAL B   5  LYS B   8  0                                        
SHEET    2 AA7 2 GLU B 156  VAL B 159 -1  O  TYR B 157   N  VAL B   7           
SHEET    1 AA8 7 LEU B  22  LYS B  24  0                                        
SHEET    2 AA8 7 PHE B 127  ASN B 132 -1  O  PHE B 127   N  LYS B  24           
SHEET    3 AA8 7 GLY B 110  THR B 115 -1  N  ILE B 113   O  LYS B 130           
SHEET    4 AA8 7 THR B  56  GLY B  60  1  N  GLY B  60   O  ILE B 112           
SHEET    5 AA8 7 ARG B  85  GLY B  89  1  O  VAL B  87   N  LEU B  57           
SHEET    6 AA8 7 PHE B 184  VAL B 189  1  O  GLU B 187   N  ILE B  88           
SHEET    7 AA8 7 GLY B 171  PHE B 175 -1  N  GLN B 173   O  VAL B 186           
SHEET    1 AA9 5 ALA B 248  VAL B 249  0                                        
SHEET    2 AA9 5 ILE B 220  ASP B 223  1  N  ILE B 222   O  VAL B 249           
SHEET    3 AA9 5 PHE B 283  PHE B 287  1  O  PHE B 287   N  ASP B 223           
SHEET    4 AA9 5 ASN B 294  GLY B 298 -1  O  LEU B 297   N  GLY B 284           
SHEET    5 AA9 5 PHE B 302  VAL B 304 -1  O  PHE B 302   N  GLY B 298           
SHEET    1 AB1 4 LEU B 352  THR B 355  0                                        
SHEET    2 AB1 4 PHE B 331  SER B 334  1  N  PHE B 331   O  TYR B 353           
SHEET    3 AB1 4 LEU B 373  GLU B 376  1  O  LEU B 373   N  ALA B 332           
SHEET    4 AB1 4 GLY B 380  SER B 383 -1  O  GLY B 380   N  GLU B 376           
SHEET    1 AB2 7 GLN B 458  SER B 460  0                                        
SHEET    2 AB2 7 VAL B 465  ASN B 473 -1  O  TYR B 466   N  PHE B 459           
SHEET    3 AB2 7 LEU B 490  PHE B 494 -1  O  ARG B 491   N  ASP B 472           
SHEET    4 AB2 7 ARG B 499  ARG B 503 -1  O  PHE B 502   N  LEU B 490           
SHEET    5 AB2 7 ILE B 514  GLU B 522 -1  O  TYR B 517   N  VAL B 501           
SHEET    6 AB2 7 ARG B 422  TYR B 430 -1  N  TYR B 428   O  LEU B 516           
SHEET    7 AB2 7 VAL B 560  THR B 562 -1  O  VAL B 560   N  ASP B 429           
SHEET    1 AB3 2 TYR B 476  SER B 477  0                                        
SHEET    2 AB3 2 ILE B 484  SER B 485 -1  O  SER B 485   N  TYR B 476           
CISPEP   1 GLY A  289    ASP A  290          0       -13.21                     
CISPEP   2 ALA A  461    ASN A  462          0        -4.81                     
CISPEP   3 GLY B  289    ASP B  290          0       -11.96                     
CISPEP   4 ALA B  461    ASN B  462          0        -7.04                     
SITE     1 AC1  5 ARG A 293  SER A 378  PHE A 379  ARG A 427                    
SITE     2 AC1  5 ARG A 515                                                     
SITE     1 AC2  5 ALA A 315  ASN A 316  ILE A 317  PHE A 318                    
SITE     2 AC2  5 SER A 319                                                     
SITE     1 AC3  2 ARG A  85  GLU A 187                                          
SITE     1 AC4  6 THR A  19  PRO A 138  ARG A 291  TRP A 359                    
SITE     2 AC4  6 LYS A 360  LYS A 389                                          
SITE     1 AC5  3 SER B 378  PHE B 379  ARG B 427                               
CRYST1  170.780  170.780   99.287  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.005855  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005855  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010072        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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