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Database: PDB
Entry: 4KT0
LinkDB: 4KT0
Original site: 4KT0 
HEADER    ELECTRON TRANSPORT                      19-MAY-13   4KT0              
TITLE     CRYSTAL STRUCTURE OF A VIRUS LIKE PHOTOSYSTEM I FROM THE              
TITLE    2 CYANOBACTERIUM SYNECHOCYSTIS PCC 6803                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A1;            
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PSAA;                                                       
COMPND   5 EC: 1.97.1.12;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN A2;            
COMPND   9 CHAIN: B;                                                            
COMPND  10 SYNONYM: PSAB;                                                       
COMPND  11 EC: 1.97.1.12;                                                       
COMPND  12 ENGINEERED: YES;                                                     
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: PHOTOSYSTEM I IRON-SULFUR CENTER;                          
COMPND  15 CHAIN: C;                                                            
COMPND  16 SYNONYM: 9 KDA POLYPEPTIDE, PSI-C, PHOTOSYSTEM I SUBUNIT VII, PSAC;  
COMPND  17 EC: 1.97.1.12;                                                       
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: PHOTOSYSTEM I SUBUNIT II;                                  
COMPND  21 CHAIN: D;                                                            
COMPND  22 EC: 1.97.1.12;                                                       
COMPND  23 ENGINEERED: YES;                                                     
COMPND  24 MOL_ID: 5;                                                           
COMPND  25 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IV;                  
COMPND  26 CHAIN: E;                                                            
COMPND  27 EC: 1.97.1.12;                                                       
COMPND  28 ENGINEERED: YES;                                                     
COMPND  29 MOL_ID: 6;                                                           
COMPND  30 MOLECULE: PHOTOSYSTEM I SUBUNIT III;                                 
COMPND  31 CHAIN: F;                                                            
COMPND  32 EC: 1.97.1.12;                                                       
COMPND  33 ENGINEERED: YES;                                                     
COMPND  34 MOL_ID: 7;                                                           
COMPND  35 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT IX;                  
COMPND  36 CHAIN: J;                                                            
COMPND  37 EC: 1.97.1.12;                                                       
COMPND  38 ENGINEERED: YES;                                                     
COMPND  39 MOL_ID: 8;                                                           
COMPND  40 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT PSAK;                
COMPND  41 CHAIN: K;                                                            
COMPND  42 SYNONYM: PHOTOSYSTEM I SUBUNIT X;                                    
COMPND  43 EC: 1.97.1.12;                                                       
COMPND  44 ENGINEERED: YES;                                                     
COMPND  45 MOL_ID: 9;                                                           
COMPND  46 MOLECULE: PHOTOSYSTEM I REACTION CENTER SUBUNIT XII;                 
COMPND  47 CHAIN: M;                                                            
COMPND  48 SYNONYM: PSI-M;                                                      
COMPND  49 EC: 1.97.1.12;                                                       
COMPND  50 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE   3 ORGANISM_TAXID: 1148;                                                
SOURCE   4 STRAIN: SYNECHOCYSTIS SP. PCC 6803;                                  
SOURCE   5 GENE: BEST7613_2234, MYO_18690, PSAA;                                
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE   8 ORGANISM_TAXID: 1148;                                                
SOURCE   9 GENE: PSAB, BEST7613_2235, MYO_18700;                                
SOURCE  10 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  12 MOL_ID: 3;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  14 ORGANISM_TAXID: 1148;                                                
SOURCE  15 GENE: PSAC, BEST7613_5694, MYO_120930;                               
SOURCE  16 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  18 MOL_ID: 4;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  20 ORGANISM_TAXID: 1148;                                                
SOURCE  21 GENE: PSAD, BEST7613_1459, MYO_11100;                                
SOURCE  22 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  23 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  24 MOL_ID: 5;                                                           
SOURCE  25 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  26 ORGANISM_TAXID: 1148;                                                
SOURCE  27 GENE: PSAE, BEST7613_5968, MYO_118260;                               
SOURCE  28 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  29 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  30 MOL_ID: 6;                                                           
SOURCE  31 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  32 ORGANISM_TAXID: 1148;                                                
SOURCE  33 GENE: PSAF, BEST7613_2928;                                           
SOURCE  34 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  35 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  36 MOL_ID: 7;                                                           
SOURCE  37 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  38 ORGANISM_TAXID: 1148;                                                
SOURCE  39 GENE: PSAJ, BEST7613_2927, MYO_115450;                               
SOURCE  40 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  41 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  42 MOL_ID: 8;                                                           
SOURCE  43 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  44 ORGANISM_TAXID: 1148;                                                
SOURCE  45 GENE: PSAK, BEST7613_4536, MYO_129960;                               
SOURCE  46 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  47 EXPRESSION_SYSTEM_TAXID: 1148;                                       
SOURCE  48 MOL_ID: 9;                                                           
SOURCE  49 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. PCC 6803;                     
SOURCE  50 ORGANISM_TAXID: 1148;                                                
SOURCE  51 GENE: PSBM, PSAM, BEST7613_1787, MYO_14340;                          
SOURCE  52 EXPRESSION_SYSTEM: SYNECHOCYSTIS SP. PCC 6803;                       
SOURCE  53 EXPRESSION_SYSTEM_TAXID: 1148                                        
KEYWDS    PHOTOSYNTHETIC REACTION CENTER, MEMBRANE COMPLEX, PLASTOCYANIN,       
KEYWDS   2 CYTOCHROME C6, FERREDOXIN, ELECTRON TRANSPORT                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.MAZOR,D.NATAF,H.TOPORIK,N.NELSON                                    
REVDAT   2   24-SEP-14 4KT0    1       JRNL                                     
REVDAT   1   05-FEB-14 4KT0    0                                                
JRNL        AUTH   Y.MAZOR,D.NATAF,H.TOPORIK,N.NELSON                           
JRNL        TITL   CRYSTAL STRUCTURES OF VIRUS-LIKE PHOTOSYSTEM I COMPLEXES     
JRNL        TITL 2 FROM THE MESOPHILIC CYANOBACTERIUM SYNECHOCYSTIS PCC 6803.   
JRNL        REF    ELIFE                         V.   3 01496 2014              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   24473073                                                     
JRNL        DOI    10.7554/ELIFE.01496                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.98                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 91218                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4558                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 29.9788 -  8.6328    0.98     3084   144  0.2221 0.2191        
REMARK   3     2  8.6328 -  6.8793    0.99     2977   184  0.1758 0.2216        
REMARK   3     3  6.8793 -  6.0177    0.98     2929   135  0.1831 0.2157        
REMARK   3     4  6.0177 -  5.4712    1.00     2985   159  0.1818 0.2294        
REMARK   3     5  5.4712 -  5.0810    1.00     2961   137  0.1653 0.2313        
REMARK   3     6  5.0810 -  4.7827    1.00     2969   130  0.1593 0.2042        
REMARK   3     7  4.7827 -  4.5441    0.99     2914   161  0.1567 0.2045        
REMARK   3     8  4.5441 -  4.3469    0.99     2898   153  0.1611 0.2098        
REMARK   3     9  4.3469 -  4.1800    1.00     2941   157  0.1625 0.2040        
REMARK   3    10  4.1800 -  4.0361    1.00     2906   145  0.1601 0.1913        
REMARK   3    11  4.0361 -  3.9102    0.99     2918   139  0.1656 0.2041        
REMARK   3    12  3.9102 -  3.7986    1.00     2901   162  0.1794 0.2065        
REMARK   3    13  3.7986 -  3.6988    1.00     2933   146  0.1831 0.2797        
REMARK   3    14  3.6988 -  3.6087    1.00     2851   176  0.1911 0.2416        
REMARK   3    15  3.6087 -  3.5268    1.00     2883   167  0.1994 0.2721        
REMARK   3    16  3.5268 -  3.4519    0.99     2877   160  0.2135 0.2843        
REMARK   3    17  3.4519 -  3.3829    0.98     2862   145  0.2292 0.3045        
REMARK   3    18  3.3829 -  3.3192    1.00     2871   153  0.2341 0.2941        
REMARK   3    19  3.3192 -  3.2600    1.00     2907   144  0.2380 0.2759        
REMARK   3    20  3.2600 -  3.2048    1.00     2888   161  0.2385 0.3071        
REMARK   3    21  3.2048 -  3.1531    1.00     2895   156  0.2570 0.3202        
REMARK   3    22  3.1531 -  3.1047    1.00     2896   156  0.2706 0.3617        
REMARK   3    23  3.1047 -  3.0591    1.00     2888   153  0.2699 0.3428        
REMARK   3    24  3.0591 -  3.0160    1.00     2881   145  0.2741 0.3552        
REMARK   3    25  3.0160 -  2.9753    0.99     2894   156  0.2894 0.3660        
REMARK   3    26  2.9753 -  2.9367    0.99     2842   143  0.2931 0.3831        
REMARK   3    27  2.9367 -  2.9000    0.99     2912   146  0.3072 0.3454        
REMARK   3    28  2.9000 -  2.8651    0.98     2826   156  0.3133 0.3506        
REMARK   3    29  2.8651 -  2.8318    0.95     2743   149  0.3296 0.3595        
REMARK   3    30  2.8318 -  2.8000    0.85     2428   140  0.3504 0.3817        
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)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.460           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 94.61                          
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      :  0.004          23288                                  
REMARK   3   ANGLE     :  1.734          33063                                  
REMARK   3   CHIRALITY :  0.046           2902                                  
REMARK   3   PLANARITY :  0.012           3907                                  
REMARK   3   DIHEDRAL  : 28.249           9045                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A or chain B or chain C or chain D or chain E    
REMARK   3               or chain F or chain J or chain K or chain M            
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.0050  -7.8261  21.7491              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6394 T22:   0.5398                                     
REMARK   3      T33:   0.6407 T12:   0.1236                                     
REMARK   3      T13:  -0.1111 T23:  -0.0396                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0077 L22:   0.6814                                     
REMARK   3      L33:   1.5999 L12:   0.0284                                     
REMARK   3      L13:   0.0181 L23:   0.1622                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0244 S12:  -0.0161 S13:  -0.0826                       
REMARK   3      S21:   0.1128 S22:   0.0938 S23:  -0.1135                       
REMARK   3      S31:   0.2188 S32:   0.2096 S33:   0.0099                       
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 4KT0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-DEC-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB079757.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-FEB-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97625                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91895                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 4.600                              
REMARK 200  R MERGE                    (I) : 0.13900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.38200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
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: PDB ENTRY 1JB0 WITH TRUNCATED SIDE CHAINS AND        
REMARK 200  CHLOROPHYLL TAILS                                                   
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.75                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 4.5% PEG3350, 30MM TRICINE-NAOH PH8,     
REMARK 280  55MM NACL, 50MM GLYCINE, 0.005% NONYL- BETA -D-MALTOSIDE., PH       
REMARK 280  8.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 278K                
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       60.08950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       89.56800            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       86.65400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       89.56800            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.08950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       86.65400            
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 300 REMARK: AUTHOR STATED THAT THERE IS NO QUATERNARY STRUCTURE FOR      
REMARK 300 THIS ENTRY. PISA FAILED TO GENERATE ASSEMBLY. THEREFORE THE ASU IS   
REMARK 300 INDICATED AS ASSEMBLY TEMPORARILY.                                   
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: NONAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, J, K, M             
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     THR A     2                                                      
REMARK 465     ILE A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     LYS A    11                                                      
REMARK 465     ALA A    12                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     GLY B   731                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     VAL D   141                                                      
REMARK 465     MET E     1                                                      
REMARK 465     GLN E    70                                                      
REMARK 465     ALA E    71                                                      
REMARK 465     ALA E    72                                                      
REMARK 465     ALA E    73                                                      
REMARK 465     LYS E    74                                                      
REMARK 465     MET F   -21                                                      
REMARK 465     LYS F   -20                                                      
REMARK 465     HIS F   -19                                                      
REMARK 465     LEU F   -18                                                      
REMARK 465     LEU F   -17                                                      
REMARK 465     ALA F   -16                                                      
REMARK 465     LEU F   -15                                                      
REMARK 465     LEU F   -14                                                      
REMARK 465     LEU F   -13                                                      
REMARK 465     ALA F   -12                                                      
REMARK 465     PHE F   -11                                                      
REMARK 465     THR F   -10                                                      
REMARK 465     LEU F    -9                                                      
REMARK 465     TRP F    -8                                                      
REMARK 465     PHE F    -7                                                      
REMARK 465     ASN F    -6                                                      
REMARK 465     PHE F    -5                                                      
REMARK 465     ALA F    -4                                                      
REMARK 465     PRO F    -3                                                      
REMARK 465     SER F    -2                                                      
REMARK 465     ALA F    -1                                                      
REMARK 465     SER F     0                                                      
REMARK 465     ALA F     1                                                      
REMARK 465     ASP F     2                                                      
REMARK 465     MET K     1                                                      
REMARK 465     THR K     2                                                      
REMARK 465     ALA K     3                                                      
REMARK 465     ILE K     4                                                      
REMARK 465     ALA K     5                                                      
REMARK 465     ARG K     6                                                      
REMARK 465     GLU K     7                                                      
REMARK 465     ARG K     8                                                      
REMARK 465     GLY K     9                                                      
REMARK 465     ARG K    10                                                      
REMARK 465     SER K    11                                                      
REMARK 465     LYS K    12                                                      
REMARK 465     ARG K    13                                                      
REMARK 465     GLY K    14                                                      
REMARK 465     ILE K    15                                                      
REMARK 465     ALA K    16                                                      
REMARK 465     LEU K    17                                                      
REMARK 465     HIS K    18                                                      
REMARK 465     ARG K    19                                                      
REMARK 465     LEU K    20                                                      
REMARK 465     GLU K    21                                                      
REMARK 465     TYR K    22                                                      
REMARK 465     LEU K    23                                                      
REMARK 465     LYS K    24                                                      
REMARK 465     GLU K    25                                                      
REMARK 465     ASN K    26                                                      
REMARK 465     GLN K    27                                                      
REMARK 465     VAL K    28                                                      
REMARK 465     PHE K    29                                                      
REMARK 465     GLU K    30                                                      
REMARK 465     ILE K    31                                                      
REMARK 465     ILE K    32                                                      
REMARK 465     PHE K    33                                                      
REMARK 465     GLY K    34                                                      
REMARK 465     GLU K    35                                                      
REMARK 465     PRO K    36                                                      
REMARK 465     LEU K    37                                                      
REMARK 465     SER K    38                                                      
REMARK 465     MET K    39                                                      
REMARK 465     PHE K    40                                                      
REMARK 465     ASN K    41                                                      
REMARK 465     THR K    42                                                      
REMARK 465     ALA K    43                                                      
REMARK 465     LEU K    44                                                      
REMARK 465     LEU K    45                                                      
REMARK 465     LEU K    46                                                      
REMARK 465     ALA K    47                                                      
REMARK 465     GLN K    48                                                      
REMARK 465     ALA K    49                                                      
REMARK 465     SER K    50                                                      
REMARK 465     PRO K    51                                                      
REMARK 465     THR K    52                                                      
REMARK 465     THR K    53                                                      
REMARK 465     ILE K    79                                                      
REMARK 465     GLN K    80                                                      
REMARK 465     LYS K    81                                                      
REMARK 465     THR K    82                                                      
REMARK 465     GLY K    83                                                      
REMARK 465     LYS K    84                                                      
REMARK 465     GLY K    85                                                      
REMARK 465     LYS K    86                                                      
REMARK 465     ASP K    87                                                      
REMARK 465     LEU K    88                                                      
REMARK 465     ALA K    89                                                      
REMARK 465     LEU K    90                                                      
REMARK 465     PRO K    91                                                      
REMARK 465     GLN K    92                                                      
REMARK 465     LEU K    93                                                      
REMARK 465     ALA K    94                                                      
REMARK 465     SER K    95                                                      
REMARK 465     LYS K    96                                                      
REMARK 465     LYS K    97                                                      
REMARK 465     THR K    98                                                      
REMARK 465     PHE K    99                                                      
REMARK 465     LEU K   128                                                      
REMARK 465     MET M     1                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU D   3    CG   CD   OE1  OE2                                  
REMARK 470     TRP K  56    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP K  56    CZ3  CH2                                            
REMARK 470     LEU M   3    CG   CD1  CD2                                       
REMARK 470     ASP M   5    CG   OD1  OD2                                       
REMARK 470     GLN M   7    CG   CD   OE1  NE2                                  
REMARK 470     ILE M   8    CG1  CG2  CD1                                       
REMARK 470     LEU M   9    CG   CD1  CD2                                       
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   CMA  CL0 A  1011     O    HOH A  9109              1.91            
REMARK 500   O    HOH B  9111     O    HOH C  9203              2.04            
REMARK 500   OD1  ASN B   582     O    HOH B  9102              2.05            
REMARK 500   NH2  ARG J    31     O1D  CLA J  1302              2.15            
REMARK 500   OBD  CLA B  1230     O    HOH B  9106              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    LYS A  96       10.14   -143.69                                   
REMARK 500    PHE A  97       19.73   -145.76                                   
REMARK 500    GLN A 115      106.05     61.29                                   
REMARK 500    VAL A 121       31.07     39.66                                   
REMARK 500    THR A 153       32.60   -143.10                                   
REMARK 500    VAL A 182      -59.98   -120.45                                   
REMARK 500    ALA A 232      170.59     86.65                                   
REMARK 500    PRO A 262       48.33    -88.56                                   
REMARK 500    LEU A 275       77.23   -115.19                                   
REMARK 500    THR A 313     -104.02   -129.01                                   
REMARK 500    TRP A 315       22.15   -146.83                                   
REMARK 500    PRO A 374      107.68    -52.21                                   
REMARK 500    ASN A 424     -169.59   -112.30                                   
REMARK 500    ARG A 466       56.99   -141.74                                   
REMARK 500    ALA A 475     -132.98   -133.35                                   
REMARK 500    LEU A 478       76.90   -103.77                                   
REMARK 500    ALA A 496      -89.03   -100.06                                   
REMARK 500    ALA A 517     -106.88     58.14                                   
REMARK 500    CYS A 574     -165.28   -164.74                                   
REMARK 500    GLN A 584       61.47     60.70                                   
REMARK 500    VAL A 617      -73.41   -126.86                                   
REMARK 500    ASN A 659       42.65   -105.74                                   
REMARK 500    ASN B  73       46.92    -98.71                                   
REMARK 500    ASP B  80       72.85   -161.67                                   
REMARK 500    ALA B 107       18.64     56.96                                   
REMARK 500    VAL B 197      -52.31   -125.42                                   
REMARK 500    LEU B 222       15.00     56.98                                   
REMARK 500    THR B 227      -74.07   -107.41                                   
REMARK 500    ASN B 229       58.22   -117.03                                   
REMARK 500    ALA B 235      -77.67    -71.36                                   
REMARK 500    GLU B 248       94.03    -68.19                                   
REMARK 500    THR B 293     -121.90   -123.90                                   
REMARK 500    PRO B 455       53.76    -67.30                                   
REMARK 500    ASP B 473       71.68     62.02                                   
REMARK 500    LEU B 475      -97.88     59.16                                   
REMARK 500    ALA B 488     -129.61     62.55                                   
REMARK 500    ALA B 489     -121.55     62.35                                   
REMARK 500    ASN B 503     -168.35   -117.80                                   
REMARK 500    MET B 544       75.97   -158.52                                   
REMARK 500    CYS B 556     -163.61   -177.49                                   
REMARK 500    ASN B 602       64.30   -119.61                                   
REMARK 500    LEU B 684      -43.25     68.07                                   
REMARK 500    ASP C   9        3.80    -67.59                                   
REMARK 500    SER D   5     -163.82   -164.82                                   
REMARK 500    LEU D  19     -167.30   -123.80                                   
REMARK 500    GLU D  25      -72.55    -98.83                                   
REMARK 500    THR D  74      -14.94   -142.76                                   
REMARK 500    LEU D  97      -53.58   -129.52                                   
REMARK 500    ARG D 120      140.92   -174.98                                   
REMARK 500    THR E  14       -1.48     84.46                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      58 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG D 121         0.19    SIDE CHAIN                              
REMARK 500    ARG F 143         0.13    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     CLA A 1801                                                       
REMARK 610     CLA A 1107                                                       
REMARK 610     CL0 A 1108                                                       
REMARK 610     CLA A 1110                                                       
REMARK 610     CLA A 1111                                                       
REMARK 610     CLA A 1112                                                       
REMARK 610     CLA A 1113                                                       
REMARK 610     CLA A 1116                                                       
REMARK 610     CLA A 1118                                                       
REMARK 610     CLA A 1119                                                       
REMARK 610     CLA A 1124                                                       
REMARK 610     CLA A 1125                                                       
REMARK 610     CLA A 1137                                                       
REMARK 610     CLA A 1114                                                       
REMARK 610     CLA A 1115                                                       
REMARK 610     CLA A 1120                                                       
REMARK 610     CLA A 1121                                                       
REMARK 610     CLA A 1129                                                       
REMARK 610     CLA A 1130                                                       
REMARK 610     CLA A 1131                                                       
REMARK 610     CLA A 1132                                                       
REMARK 610     CLA A 1133                                                       
REMARK 610     CLA A 1134                                                       
REMARK 610     CLA A 1135                                                       
REMARK 610     LHG A 5005                                                       
REMARK 610     CLA B 1240                                                       
REMARK 610     CLA B 1205                                                       
REMARK 610     CLA B 1207                                                       
REMARK 610     CLA B 1208                                                       
REMARK 610     CLA B 1209                                                       
REMARK 610     CLA B 1212                                                       
REMARK 610     CLA B 1213                                                       
REMARK 610     CLA B 1217                                                       
REMARK 610     CLA B 1218                                                       
REMARK 610     CLA B 1219                                                       
REMARK 610     CLA B 1220                                                       
REMARK 610     CLA B 1222                                                       
REMARK 610     CLA B 1227                                                       
REMARK 610     CLA B 1232                                                       
REMARK 610     CLA B 1236                                                       
REMARK 610     CLA B 1201                                                       
REMARK 610     CLA B 1204                                                       
REMARK 610     CLA B 1206                                                       
REMARK 610     CLA B 1211                                                       
REMARK 610     CLA B 1237                                                       
REMARK 610     CLA B 1238                                                       
REMARK 610     CLA B 1239                                                       
REMARK 610     CLA F 1301                                                       
REMARK 610     CLA J 1303                                                       
REMARK 610     CLA J 1302                                                       
REMARK 610     CLA K 1401                                                       
REMARK 610     CLA K 1402                                                       
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                             SF4 C3003  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  17   SG                                                     
REMARK 620 2 SF4 C3003   S1  133.3                                              
REMARK 620 3 SF4 C3003   S2  151.3  67.8                                        
REMARK 620 4 SF4 C3003   S3  132.5  68.7  68.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A3001  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 565   SG                                                     
REMARK 620 2 SF4 A3001   S1   80.0                                              
REMARK 620 3 SF4 A3001   S2  117.2  67.9                                        
REMARK 620 4 SF4 A3001   S4  142.6  67.5  67.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3002  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  48   SG                                                     
REMARK 620 2 SF4 C3002   S1  148.5                                              
REMARK 620 3 SF4 C3002   S2  130.7  67.9                                        
REMARK 620 4 SF4 C3002   S3  138.3  68.4  68.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A3001  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 583   SG                                                     
REMARK 620 2 SF4 A3001   S1  164.2                                              
REMARK 620 3 SF4 A3001   S3  105.0  68.7                                        
REMARK 620 4 SF4 A3001   S4   96.7  67.5  68.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA F1139  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A9107   O                                                      
REMARK 620 2 CLA F1139   NA   82.7                                              
REMARK 620 3 CLA F1139   NB  113.0  87.7                                        
REMARK 620 4 CLA F1139   NC  110.5 164.1  94.8                                  
REMARK 620 5 CLA F1139   ND   84.6  90.8 161.9  81.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3003  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  11   SG                                                     
REMARK 620 2 SF4 C3003   S1  128.6                                              
REMARK 620 3 SF4 C3003   S2  145.5  67.8                                        
REMARK 620 4 SF4 C3003   S4  142.9  68.1  68.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A3001  FE4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS A 574   SG                                                     
REMARK 620 2 SF4 A3001   S1  114.3                                              
REMARK 620 3 SF4 A3001   S2  132.7  67.9                                        
REMARK 620 4 SF4 A3001   S3   69.1  68.7  68.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3002  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  51   SG                                                     
REMARK 620 2 SF4 C3002   S2  145.8                                              
REMARK 620 3 SF4 C3002   S3  145.9  68.0                                        
REMARK 620 4 SF4 C3002   S4  120.0  68.1  68.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3003  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  14   SG                                                     
REMARK 620 2 SF4 C3003   S1  151.8                                              
REMARK 620 3 SF4 C3003   S3  130.9  68.7                                        
REMARK 620 4 SF4 C3003   S4  133.6  68.0  69.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3002  FE3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  54   SG                                                     
REMARK 620 2 SF4 C3002   S1  146.6                                              
REMARK 620 3 SF4 C3002   S2  132.4  67.8                                        
REMARK 620 4 SF4 C3002   S4  139.0  68.3  68.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 A3001  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS B 556   SG                                                     
REMARK 620 2 SF4 A3001   S2   77.9                                              
REMARK 620 3 SF4 A3001   S3  146.5  68.8                                        
REMARK 620 4 SF4 A3001   S4  102.3  67.7  68.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1022  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A9101   O                                                      
REMARK 620 2 CLA A1022   NA  111.1                                              
REMARK 620 3 CLA A1022   NB   92.5  87.3                                        
REMARK 620 4 CLA A1022   NC   86.1 162.7  94.5                                  
REMARK 620 5 CLA A1022   ND  103.5  91.0 163.4  82.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3002  FE2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  21   SG                                                     
REMARK 620 2 SF4 C3002   S1  145.4                                              
REMARK 620 3 SF4 C3002   S3  138.2  68.3                                        
REMARK 620 4 SF4 C3002   S4  134.4  68.3  68.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             SF4 C3003  FE1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C  58   SG                                                     
REMARK 620 2 SF4 C3003   S2  150.7                                              
REMARK 620 3 SF4 C3003   S3  129.9  68.6                                        
REMARK 620 4 SF4 C3003   S4  135.8  68.2  69.0                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1107  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 123   OE1                                                    
REMARK 620 2 CLA A1107   NA   84.1                                              
REMARK 620 3 CLA A1107   NB  119.1  87.0                                        
REMARK 620 4 CLA A1107   NC  106.1 166.0  96.0                                  
REMARK 620 5 CLA A1107   ND   77.1  91.2 163.4  81.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1106  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 115   OE1                                                    
REMARK 620 2 CLA A1106   NA   88.8                                              
REMARK 620 3 CLA A1106   NB  106.6  87.4                                        
REMARK 620 4 CLA A1106   NC  105.3 164.3  94.9                                  
REMARK 620 5 CLA A1106   ND   90.5  91.0 162.8  82.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1012  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B9102   O                                                      
REMARK 620 2 CLA A1012   NA  115.8                                              
REMARK 620 3 CLA A1012   NB  102.7  88.3                                        
REMARK 620 4 CLA A1012   NC   80.9 162.4  93.7                                  
REMARK 620 5 CLA A1012   ND   92.5  90.8 163.5  82.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1237  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B9101   O                                                      
REMARK 620 2 CLA B1237   NA   89.2                                              
REMARK 620 3 CLA B1237   NB  112.3  87.4                                        
REMARK 620 4 CLA B1237   NC  103.8 164.8  94.8                                  
REMARK 620 5 CLA B1237   ND   85.5  91.4 162.2  81.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1238  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B9110   O                                                      
REMARK 620 2 CLA B1238   NA   61.1                                              
REMARK 620 3 CLA B1238   NB  109.5  87.1                                        
REMARK 620 4 CLA B1238   NC  133.1 163.0  94.6                                  
REMARK 620 5 CLA B1238   ND   85.0  91.4 162.2  81.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1240  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG B5004   O5                                                     
REMARK 620 2 CLA B1240   NA   87.1                                              
REMARK 620 3 CLA B1240   NB  108.8  87.5                                        
REMARK 620 4 CLA B1240   NC  107.4 163.7  94.6                                  
REMARK 620 5 CLA B1240   ND   88.7  91.1 162.3  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA J1302  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU J  28   OE2                                                    
REMARK 620 2 CLA J1302   NA   67.3                                              
REMARK 620 3 CLA J1302   NB   83.4  88.3                                        
REMARK 620 4 CLA J1302   NC   97.3 163.7  95.2                                  
REMARK 620 5 CLA J1302   ND   81.1  90.7 163.5  81.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA F1410  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP F  56   O                                                      
REMARK 620 2 CLA F1410   NA   81.7                                              
REMARK 620 3 CLA F1410   NB   90.4  87.6                                        
REMARK 620 4 CLA F1410   NC   81.7 163.2  94.6                                  
REMARK 620 5 CLA F1410   ND   73.2  91.2 163.5  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1801  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LHG A5003   O5                                                     
REMARK 620 2 CLA A1801   NA   86.0                                              
REMARK 620 3 CLA A1801   NB   92.8  87.9                                        
REMARK 620 4 CLA A1801   NC  109.0 164.6  94.5                                  
REMARK 620 5 CLA A1801   ND  104.5  91.0 162.5  82.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1109  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CLA A1102   O1A                                                    
REMARK 620 2 CLA A1109   NA   69.9                                              
REMARK 620 3 CLA A1109   NB   79.3  87.4                                        
REMARK 620 4 CLA A1109   NC   96.3 165.4  95.0                                  
REMARK 620 5 CLA A1109   ND   82.8  90.8 161.5  82.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A1134  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 497   O                                                      
REMARK 620 2 CLA A1134   NA   77.7                                              
REMARK 620 3 CLA A1134   NB   91.5  87.8                                        
REMARK 620 4 CLA A1134   NC   86.1 163.7  95.1                                  
REMARK 620 5 CLA A1134   ND   71.6  91.0 162.9  81.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B1206  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B  93   OD2                                                    
REMARK 620 2 CLA B1206   NA  104.4                                              
REMARK 620 3 CLA B1206   NB   99.9  87.4                                        
REMARK 620 4 CLA B1206   NC   91.6 163.4  94.5                                  
REMARK 620 5 CLA B1206   ND   98.5  90.9 161.4  82.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN A 2001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 A 3001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 5001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL0 A 1011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 5003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4001                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4007                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4008                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR A 4012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1801                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1022                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1101                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1102                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1103                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1104                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1105                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1106                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1107                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL0 A 1108                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1109                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1110                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1111                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1112                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1113                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1116                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1117                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1118                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1119                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1122                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1123                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1124                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1125                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1126                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1127                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1128                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1136                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1137                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1140                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1012                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1114                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1115                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1120                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1121                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1129                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1130                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1131                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1132                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1133                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1134                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 1135                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG A 5005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1240                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU B 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PQN B 2002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMG B 5002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LHG B 5004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4004                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4009                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4011                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4014                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 4017                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1021                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1202                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1203                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1205                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1207                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1208                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1209                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1210                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1212                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1213                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1214                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1215                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1216                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1217                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1218                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1219                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1220                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1221                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1222                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1223                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1224                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1225                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1226                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1227                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1228                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1229                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1230                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1231                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1232                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1234                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1235                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1236                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1201                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1204                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1206                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1211                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1237                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1238                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 1239                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 6000                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 3002                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SF4 C 3003                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1410                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 4015                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 4016                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1139                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA F 1301                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: MC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J 1303                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMU J 1304                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 4013                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA J 1302                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1401                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: NC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA K 1402                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1JB0   RELATED DB: PDB                                   
REMARK 900 PHOTOSYSTEM I FROM SYNECHOCOCCUS ELONGATUS                           
REMARK 900 RELATED ID: 3LW5   RELATED DB: PDB                                   
REMARK 900 PHOTOSYSTEM I FROM PISUM SATIVUM                                     
REMARK 900 RELATED ID: 4L6V   RELATED DB: PDB                                   
DBREF  4KT0 A    1   751  UNP    L8AHT3   L8AHT3_9SYNC     1    751             
DBREF  4KT0 B    1   731  UNP    L8AIC0   L8AIC0_9SYNC     1    731             
DBREF  4KT0 C    1    81  UNP    L8AST2   L8AST2_9SYNC     1     81             
DBREF  4KT0 D    1   141  UNP    L8AFM8   L8AFM8_9SYNC     1    141             
DBREF  4KT0 E    1    74  UNP    L8ASH8   L8ASH8_9SYNC     1     74             
DBREF  4KT0 F  -21   143  UNP    L8AII8   L8AII8_9SYNC    20    184             
DBREF  4KT0 J    1    40  UNP    L8AGL9   L8AGL9_9SYNC     1     40             
DBREF  4KT0 K    1   128  UNP    L8APJ0   L8APJ0_9SYNC     1    128             
DBREF  4KT0 M    1    31  UNP    L8ADF9   L8ADF9_9SYNC     1     31             
SEQRES   1 A  751  MET THR ILE SER PRO PRO GLU ARG GLU ALA LYS ALA LYS          
SEQRES   2 A  751  VAL SER VAL ASP ASN ASN PRO VAL PRO THR SER PHE GLU          
SEQRES   3 A  751  LYS TRP GLY LYS PRO GLY HIS PHE ASP ARG THR LEU ALA          
SEQRES   4 A  751  ARG GLY PRO LYS THR THR THR TRP ILE TRP ASN LEU HIS          
SEQRES   5 A  751  ALA ASN ALA HIS ASP PHE ASP SER GLN THR SER ASP LEU          
SEQRES   6 A  751  GLU ASP VAL SER ARG LYS ILE PHE SER ALA HIS PHE GLY          
SEQRES   7 A  751  HIS LEU ALA VAL VAL PHE VAL TRP LEU SER GLY MET TYR          
SEQRES   8 A  751  PHE HIS GLY ALA LYS PHE SER ASN TYR GLU GLY TRP LEU          
SEQRES   9 A  751  ALA ASP PRO THR HIS ILE LYS PRO SER ALA GLN VAL VAL          
SEQRES  10 A  751  TRP PRO ILE VAL GLY GLN GLY ILE LEU ASN GLY ASP VAL          
SEQRES  11 A  751  GLY GLY GLY PHE HIS GLY ILE GLN ILE THR SER GLY LEU          
SEQRES  12 A  751  PHE TYR LEU TRP ARG ALA SER GLY PHE THR ASP SER TYR          
SEQRES  13 A  751  GLN LEU TYR CYS THR ALA ILE GLY GLY LEU VAL MET ALA          
SEQRES  14 A  751  ALA LEU MET LEU PHE ALA GLY TRP PHE HIS TYR HIS VAL          
SEQRES  15 A  751  LYS ALA PRO LYS LEU GLU TRP PHE GLN ASN VAL GLU SER          
SEQRES  16 A  751  MET MET ASN HIS HIS LEU ALA GLY LEU LEU GLY LEU GLY          
SEQRES  17 A  751  SER LEU GLY TRP ALA GLY HIS GLN ILE HIS VAL SER MET          
SEQRES  18 A  751  PRO ILE ASN LYS LEU LEU ASP ALA GLY VAL ALA PRO LYS          
SEQRES  19 A  751  ASP ILE PRO LEU PRO HIS GLU PHE ILE LEU GLU PRO SER          
SEQRES  20 A  751  LYS MET ALA GLU LEU TYR PRO SER PHE ALA GLN GLY LEU          
SEQRES  21 A  751  THR PRO PHE PHE THR LEU ASN TRP GLY VAL TYR SER ASP          
SEQRES  22 A  751  PHE LEU THR PHE LYS GLY GLY LEU ASN PRO VAL THR GLY          
SEQRES  23 A  751  GLY LEU TRP LEU SER ASP THR ALA HIS HIS HIS LEU ALA          
SEQRES  24 A  751  ILE ALA VAL LEU PHE ILE ILE ALA GLY HIS MET TYR ARG          
SEQRES  25 A  751  THR ASN TRP GLY ILE GLY HIS SER MET LYS GLU ILE LEU          
SEQRES  26 A  751  GLU ALA HIS LYS GLY PRO PHE THR GLY GLU GLY HIS LYS          
SEQRES  27 A  751  GLY LEU TYR GLU ILE LEU THR THR SER TRP HIS ALA GLN          
SEQRES  28 A  751  LEU ALA ILE ASN LEU ALA LEU LEU GLY SER LEU THR ILE          
SEQRES  29 A  751  ILE VAL ALA GLN HIS MET TYR ALA MET PRO PRO TYR PRO          
SEQRES  30 A  751  TYR GLN ALA ILE ASP TYR ALA THR GLN LEU SER LEU PHE          
SEQRES  31 A  751  THR HIS HIS MET TRP ILE GLY GLY PHE LEU ILE VAL GLY          
SEQRES  32 A  751  ALA GLY ALA HIS GLY ALA ILE PHE MET VAL ARG ASP TYR          
SEQRES  33 A  751  ASP PRO ALA LYS ASN VAL ASN ASN LEU LEU ASP ARG MET          
SEQRES  34 A  751  LEU ARG HIS ARG ASP ALA ILE ILE SER HIS LEU ASN TRP          
SEQRES  35 A  751  VAL CYS ILE PHE LEU GLY PHE HIS SER PHE GLY LEU TYR          
SEQRES  36 A  751  ILE HIS ASN ASP THR MET ARG ALA LEU GLY ARG PRO GLN          
SEQRES  37 A  751  ASP MET PHE SER ASP THR ALA ILE GLN LEU GLN PRO ILE          
SEQRES  38 A  751  PHE ALA GLN TRP VAL GLN HIS LEU HIS THR LEU ALA PRO          
SEQRES  39 A  751  GLY ALA THR ALA PRO ASN ALA LEU ALA THR ALA SER TYR          
SEQRES  40 A  751  ALA PHE GLY GLY GLU THR ILE ALA VAL ALA GLY LYS VAL          
SEQRES  41 A  751  ALA MET MET PRO ILE THR LEU GLY THR ALA ASP PHE MET          
SEQRES  42 A  751  VAL HIS HIS ILE HIS ALA PHE THR ILE HIS VAL THR ALA          
SEQRES  43 A  751  LEU ILE LEU LEU LYS GLY VAL LEU TYR ALA ARG SER SER          
SEQRES  44 A  751  ARG LEU VAL PRO ASP LYS ALA ASN LEU GLY PHE ARG PHE          
SEQRES  45 A  751  PRO CYS ASP GLY PRO GLY ARG GLY GLY THR CYS GLN VAL          
SEQRES  46 A  751  SER GLY TRP ASP HIS VAL PHE LEU GLY LEU PHE TRP MET          
SEQRES  47 A  751  TYR ASN SER LEU SER ILE VAL ILE PHE HIS PHE SER TRP          
SEQRES  48 A  751  LYS MET GLN SER ASP VAL TRP GLY THR VAL SER PRO ASP          
SEQRES  49 A  751  GLY SER VAL THR HIS VAL THR LEU GLY ASN PHE ALA GLN          
SEQRES  50 A  751  SER ALA ILE THR ILE ASN GLY TRP LEU ARG ASP PHE LEU          
SEQRES  51 A  751  TRP ALA GLN ALA ALA ASN VAL ILE ASN SER TYR GLY SER          
SEQRES  52 A  751  ALA LEU SER ALA TYR GLY ILE MET PHE LEU ALA GLY HIS          
SEQRES  53 A  751  PHE VAL PHE ALA PHE SER LEU MET PHE LEU PHE SER GLY          
SEQRES  54 A  751  ARG GLY TYR TRP GLN GLU LEU ILE GLU SER ILE VAL TRP          
SEQRES  55 A  751  ALA HIS ASN LYS LEU ASN VAL ALA PRO ALA ILE GLN PRO          
SEQRES  56 A  751  ARG ALA LEU SER ILE ILE GLN GLY ARG ALA VAL GLY VAL          
SEQRES  57 A  751  ALA HIS TYR LEU LEU GLY GLY ILE VAL THR THR TRP ALA          
SEQRES  58 A  751  PHE PHE LEU ALA ARG SER LEU SER ILE GLY                      
SEQRES   1 B  731  MET ALA THR LYS PHE PRO LYS PHE SER GLN ASP LEU ALA          
SEQRES   2 B  731  GLN ASP PRO THR THR ARG ARG ILE TRP TYR GLY ILE ALA          
SEQRES   3 B  731  THR ALA HIS ASP PHE GLU THR HIS ASP GLY MET THR GLU          
SEQRES   4 B  731  GLU ASN LEU TYR GLN LYS ILE PHE ALA SER HIS PHE GLY          
SEQRES   5 B  731  HIS ILE ALA ILE ILE PHE LEU TRP THR SER GLY THR LEU          
SEQRES   6 B  731  PHE HIS VAL ALA TRP GLN GLY ASN PHE GLU GLN TRP ILE          
SEQRES   7 B  731  LYS ASP PRO LEU ASN ILE ARG PRO ILE ALA HIS ALA ILE          
SEQRES   8 B  731  TRP ASP PRO HIS PHE GLY GLU GLY ALA VAL ASN ALA PHE          
SEQRES   9 B  731  THR GLN ALA GLY ALA SER ASN PRO VAL ASN ILE ALA TYR          
SEQRES  10 B  731  SER GLY VAL TYR HIS TRP PHE TYR THR ILE GLY MET THR          
SEQRES  11 B  731  THR ASN GLN GLU LEU TYR SER GLY ALA VAL PHE LEU LEU          
SEQRES  12 B  731  VAL LEU ALA SER LEU PHE LEU PHE ALA GLY TRP LEU HIS          
SEQRES  13 B  731  LEU GLN PRO LYS PHE ARG PRO SER LEU ALA TRP PHE LYS          
SEQRES  14 B  731  ASN ALA GLU SER ARG LEU ASN HIS HIS LEU ALA GLY LEU          
SEQRES  15 B  731  PHE GLY VAL SER SER LEU ALA TRP ALA GLY HIS LEU VAL          
SEQRES  16 B  731  HIS VAL ALA ILE PRO GLU ALA ARG GLY GLN HIS VAL GLY          
SEQRES  17 B  731  TRP ASP ASN PHE LEU SER THR PRO PRO HIS PRO ALA GLY          
SEQRES  18 B  731  LEU MET PRO PHE PHE THR GLY ASN TRP GLY VAL TYR ALA          
SEQRES  19 B  731  ALA ASP PRO ASP THR ALA GLY HIS ILE PHE GLY THR SER          
SEQRES  20 B  731  GLU GLY ALA GLY THR ALA ILE LEU THR PHE LEU GLY GLY          
SEQRES  21 B  731  PHE HIS PRO GLN THR GLU SER LEU TRP LEU THR ASP ILE          
SEQRES  22 B  731  ALA HIS HIS HIS LEU ALA ILE ALA VAL ILE PHE ILE ILE          
SEQRES  23 B  731  ALA GLY HIS MET TYR ARG THR ASN TRP GLY ILE GLY HIS          
SEQRES  24 B  731  SER ILE LYS GLU ILE LEU ASN ALA HIS LYS GLY PRO LEU          
SEQRES  25 B  731  THR GLY ALA GLY HIS THR ASN LEU TYR ASP THR ILE ASN          
SEQRES  26 B  731  ASN SER LEU HIS PHE GLN LEU GLY LEU ALA LEU ALA SER          
SEQRES  27 B  731  LEU GLY VAL ILE THR SER LEU VAL ALA GLN HIS MET TYR          
SEQRES  28 B  731  SER LEU PRO SER TYR ALA PHE ILE ALA GLN ASP HIS THR          
SEQRES  29 B  731  THR GLN ALA ALA LEU TYR THR HIS HIS GLN TYR ILE ALA          
SEQRES  30 B  731  GLY PHE LEU MET VAL GLY ALA PHE ALA HIS GLY ALA ILE          
SEQRES  31 B  731  PHE PHE VAL ARG ASP TYR ASP PRO VAL ALA ASN LYS ASP          
SEQRES  32 B  731  ASN VAL LEU ALA ARG MET LEU GLU HIS LYS GLU ALA LEU          
SEQRES  33 B  731  ILE SER HIS LEU SER TRP VAL SER LEU PHE LEU GLY PHE          
SEQRES  34 B  731  HIS THR LEU GLY LEU TYR VAL HIS ASN ASP VAL VAL VAL          
SEQRES  35 B  731  ALA PHE GLY THR PRO GLU LYS GLN ILE LEU ILE GLU PRO          
SEQRES  36 B  731  VAL PHE ALA GLN TRP ILE GLN ALA THR SER GLY LYS ALA          
SEQRES  37 B  731  LEU TYR GLY PHE ASP VAL LEU LEU SER ASN PRO ASP SER          
SEQRES  38 B  731  ILE ALA SER THR THR GLY ALA ALA TRP LEU PRO GLY TRP          
SEQRES  39 B  731  LEU ASP ALA ILE ASN SER GLY THR ASN SER LEU PHE LEU          
SEQRES  40 B  731  THR ILE GLY PRO GLY ASP PHE LEU VAL HIS HIS ALA ILE          
SEQRES  41 B  731  ALA LEU GLY LEU HIS THR THR ALA LEU ILE LEU ILE LYS          
SEQRES  42 B  731  GLY ALA LEU ASP ALA ARG GLY SER LYS LEU MET PRO ASP          
SEQRES  43 B  731  LYS LYS ASP PHE GLY TYR SER PHE PRO CYS ASP GLY PRO          
SEQRES  44 B  731  GLY ARG GLY GLY THR CYS ASP ILE SER ALA TRP ASP ALA          
SEQRES  45 B  731  PHE TYR LEU ALA MET PHE TRP MET LEU ASN THR LEU GLY          
SEQRES  46 B  731  TRP LEU THR PHE TYR TRP HIS TRP LYS HIS LEU GLY VAL          
SEQRES  47 B  731  TRP SER GLY ASN VAL ALA GLN PHE ASN GLU ASN SER THR          
SEQRES  48 B  731  TYR LEU MET GLY TRP PHE ARG ASP TYR LEU TRP ALA ASN          
SEQRES  49 B  731  SER ALA GLN LEU ILE ASN GLY TYR ASN PRO TYR GLY VAL          
SEQRES  50 B  731  ASN ASN LEU SER VAL TRP ALA TRP MET PHE LEU PHE GLY          
SEQRES  51 B  731  HIS LEU VAL TRP ALA THR GLY PHE MET PHE LEU ILE SER          
SEQRES  52 B  731  TRP ARG GLY TYR TRP GLN GLU LEU ILE GLU THR ILE VAL          
SEQRES  53 B  731  TRP ALA HIS GLU ARG THR PRO LEU ALA ASN LEU VAL ARG          
SEQRES  54 B  731  TRP LYS ASP LYS PRO VAL ALA LEU SER ILE VAL GLN ALA          
SEQRES  55 B  731  ARG LEU VAL GLY LEU ALA HIS PHE THR VAL GLY TYR VAL          
SEQRES  56 B  731  LEU THR TYR ALA ALA PHE LEU ILE ALA SER THR ALA GLY          
SEQRES  57 B  731  LYS PHE GLY                                                  
SEQRES   1 C   81  MET SER HIS SER VAL LYS ILE TYR ASP THR CYS ILE GLY          
SEQRES   2 C   81  CYS THR GLN CYS VAL ARG ALA CYS PRO LEU ASP VAL LEU          
SEQRES   3 C   81  GLU MET VAL PRO TRP ASP GLY CYS LYS ALA ALA GLN ILE          
SEQRES   4 C   81  ALA SER SER PRO ARG THR GLU ASP CYS VAL GLY CYS LYS          
SEQRES   5 C   81  ARG CYS GLU THR ALA CYS PRO THR ASP PHE LEU SER ILE          
SEQRES   6 C   81  ARG VAL TYR LEU GLY ALA GLU THR THR ARG SER MET GLY          
SEQRES   7 C   81  LEU ALA TYR                                                  
SEQRES   1 D  141  MET THR GLU LEU SER GLY GLN PRO PRO LYS PHE GLY GLY          
SEQRES   2 D  141  SER THR GLY GLY LEU LEU SER LYS ALA ASN ARG GLU GLU          
SEQRES   3 D  141  LYS TYR ALA ILE THR TRP THR SER ALA SER GLU GLN VAL          
SEQRES   4 D  141  PHE GLU MET PRO THR GLY GLY ALA ALA ILE MET ASN GLU          
SEQRES   5 D  141  GLY GLU ASN LEU LEU TYR LEU ALA ARG LYS GLU GLN CYS          
SEQRES   6 D  141  LEU ALA LEU GLY THR GLN LEU ARG THR LYS PHE LYS PRO          
SEQRES   7 D  141  LYS ILE GLN ASP TYR LYS ILE TYR ARG VAL TYR PRO SER          
SEQRES   8 D  141  GLY GLU VAL GLN TYR LEU HIS PRO ALA ASP GLY VAL PHE          
SEQRES   9 D  141  PRO GLU LYS VAL ASN GLU GLY ARG GLU ALA GLN GLY THR          
SEQRES  10 D  141  LYS THR ARG ARG ILE GLY GLN ASN PRO GLU PRO VAL THR          
SEQRES  11 D  141  ILE LYS PHE SER GLY LYS ALA PRO TYR GLU VAL                  
SEQRES   1 E   74  MET ALA LEU ASN ARG GLY ASP LYS VAL ARG ILE LYS ARG          
SEQRES   2 E   74  THR GLU SER TYR TRP TYR GLY ASP VAL GLY THR VAL ALA          
SEQRES   3 E   74  SER VAL GLU LYS SER GLY ILE LEU TYR PRO VAL ILE VAL          
SEQRES   4 E   74  ARG PHE ASP ARG VAL ASN TYR ASN GLY PHE SER GLY SER          
SEQRES   5 E   74  ALA SER GLY VAL ASN THR ASN ASN PHE ALA GLU ASN GLU          
SEQRES   6 E   74  LEU GLU LEU VAL GLN ALA ALA ALA LYS                          
SEQRES   1 F  165  MET LYS HIS LEU LEU ALA LEU LEU LEU ALA PHE THR LEU          
SEQRES   2 F  165  TRP PHE ASN PHE ALA PRO SER ALA SER ALA ASP ASP PHE          
SEQRES   3 F  165  ALA ASN LEU THR PRO CYS SER GLU ASN PRO ALA TYR LEU          
SEQRES   4 F  165  ALA LYS SER LYS ASN PHE LEU ASN THR THR ASN ASP PRO          
SEQRES   5 F  165  ASN SER GLY LYS ILE ARG ALA GLU ARG TYR ALA SER ALA          
SEQRES   6 F  165  LEU CYS GLY PRO GLU GLY TYR PRO HIS LEU ILE VAL ASP          
SEQRES   7 F  165  GLY ARG PHE THR HIS ALA GLY ASP PHE LEU ILE PRO SER          
SEQRES   8 F  165  ILE LEU PHE LEU TYR ILE ALA GLY TRP ILE GLY TRP VAL          
SEQRES   9 F  165  GLY ARG SER TYR LEU ILE GLU ILE ARG GLU SER LYS ASN          
SEQRES  10 F  165  PRO GLU MET GLN GLU VAL VAL ILE ASN VAL PRO LEU ALA          
SEQRES  11 F  165  ILE LYS LYS MET LEU GLY GLY PHE LEU TRP PRO LEU ALA          
SEQRES  12 F  165  ALA VAL GLY GLU TYR THR SER GLY LYS LEU VAL MET LYS          
SEQRES  13 F  165  ASP SER GLU ILE PRO THR SER PRO ARG                          
SEQRES   1 J   40  MET ASP GLY LEU LYS SER PHE LEU SER THR ALA PRO VAL          
SEQRES   2 J   40  MET ILE MET ALA LEU LEU THR PHE THR ALA GLY ILE LEU          
SEQRES   3 J   40  ILE GLU PHE ASN ARG PHE TYR PRO ASP LEU LEU PHE HIS          
SEQRES   4 J   40  PRO                                                          
SEQRES   1 K  128  MET THR ALA ILE ALA ARG GLU ARG GLY ARG SER LYS ARG          
SEQRES   2 K  128  GLY ILE ALA LEU HIS ARG LEU GLU TYR LEU LYS GLU ASN          
SEQRES   3 K  128  GLN VAL PHE GLU ILE ILE PHE GLY GLU PRO LEU SER MET          
SEQRES   4 K  128  PHE ASN THR ALA LEU LEU LEU ALA GLN ALA SER PRO THR          
SEQRES   5 K  128  THR ALA GLY TRP SER LEU SER VAL GLY ILE ILE MET CYS          
SEQRES   6 K  128  LEU CYS ASN VAL PHE ALA PHE VAL ILE GLY TYR PHE ALA          
SEQRES   7 K  128  ILE GLN LYS THR GLY LYS GLY LYS ASP LEU ALA LEU PRO          
SEQRES   8 K  128  GLN LEU ALA SER LYS LYS THR PHE GLY LEU PRO GLU LEU          
SEQRES   9 K  128  LEU ALA THR MET SER PHE GLY HIS ILE LEU GLY ALA GLY          
SEQRES  10 K  128  MET VAL LEU GLY LEU ALA SER SER GLY ILE LEU                  
SEQRES   1 M   31  MET ALA LEU SER ASP THR GLN ILE LEU ALA ALA LEU VAL          
SEQRES   2 M   31  VAL ALA LEU LEU PRO ALA PHE LEU ALA PHE ARG LEU SER          
SEQRES   3 M   31  THR GLU LEU TYR LYS                                          
HET    PQN  A2001      33                                                       
HET    SF4  A3001       8                                                       
HET    LHG  A5001      49                                                       
HET    CL0  A1011      65                                                       
HET    LHG  A5003      49                                                       
HET    BCR  A4001      40                                                       
HET    BCR  A4002      40                                                       
HET    BCR  A4003      40                                                       
HET    BCR  A4007      40                                                       
HET    BCR  A4008      40                                                       
HET    BCR  A4012      40                                                       
HET    CLA  A1801      52                                                       
HET    CLA  A1022      65                                                       
HET    CLA  A1101      65                                                       
HET    CLA  A1102      65                                                       
HET    CLA  A1103      65                                                       
HET    CLA  A1104      65                                                       
HET    CLA  A1105      65                                                       
HET    CLA  A1106      65                                                       
HET    CLA  A1107      50                                                       
HET    CL0  A1108      45                                                       
HET    CLA  A1109      65                                                       
HET    CLA  A1110      54                                                       
HET    CLA  A1111      60                                                       
HET    CLA  A1112      45                                                       
HET    CLA  A1113      45                                                       
HET    CLA  A1116      54                                                       
HET    CLA  A1117      65                                                       
HET    CLA  A1118      46                                                       
HET    CLA  A1119      64                                                       
HET    CLA  A1122      65                                                       
HET    CLA  A1123      65                                                       
HET    CLA  A1124      55                                                       
HET    CLA  A1125      52                                                       
HET    CLA  A1126      65                                                       
HET    CLA  A1127      65                                                       
HET    CLA  A1128      65                                                       
HET    CLA  A1136      65                                                       
HET    CLA  A1137      50                                                       
HET    CLA  A1138      65                                                       
HET    CLA  A1140      65                                                       
HET    CLA  A1012      65                                                       
HET    CLA  A1114      49                                                       
HET    CLA  A1115      46                                                       
HET    CLA  A1120      49                                                       
HET    CLA  A1121      46                                                       
HET    CLA  A1129      46                                                       
HET    CLA  A1130      55                                                       
HET    CLA  A1131      55                                                       
HET    CLA  A1132      62                                                       
HET    CLA  A1133      46                                                       
HET    CLA  A1134      46                                                       
HET    CLA  A1135      55                                                       
HET    LHG  A5005      36                                                       
HET    CLA  B1240      45                                                       
HET    LMU  B1301      35                                                       
HET    PQN  B2002      33                                                       
HET    LMG  B5002      55                                                       
HET    LHG  B5004      49                                                       
HET    BCR  B4004      40                                                       
HET    BCR  B4005      40                                                       
HET    BCR  B4006      40                                                       
HET    BCR  B4009      40                                                       
HET    BCR  B4010      40                                                       
HET    BCR  B4011      40                                                       
HET    BCR  B4014      40                                                       
HET    BCR  B4017      40                                                       
HET    CLA  B1013      65                                                       
HET    CLA  B1021      65                                                       
HET    CLA  B1023      65                                                       
HET    CLA  B1202      65                                                       
HET    CLA  B1203      65                                                       
HET    CLA  B1205      55                                                       
HET    CLA  B1207      46                                                       
HET    CLA  B1208      45                                                       
HET    CLA  B1209      45                                                       
HET    CLA  B1210      65                                                       
HET    CLA  B1212      45                                                       
HET    CLA  B1213      50                                                       
HET    CLA  B1214      65                                                       
HET    CLA  B1215      65                                                       
HET    CLA  B1216      65                                                       
HET    CLA  B1217      47                                                       
HET    CLA  B1218      51                                                       
HET    CLA  B1219      55                                                       
HET    CLA  B1220      56                                                       
HET    CLA  B1221      65                                                       
HET    CLA  B1222      56                                                       
HET    CLA  B1223      65                                                       
HET    CLA  B1224      65                                                       
HET    CLA  B1225      65                                                       
HET    CLA  B1226      65                                                       
HET    CLA  B1227      45                                                       
HET    CLA  B1228      65                                                       
HET    CLA  B1229      65                                                       
HET    CLA  B1230      65                                                       
HET    CLA  B1231      65                                                       
HET    CLA  B1232      45                                                       
HET    CLA  B1234      65                                                       
HET    CLA  B1235      65                                                       
HET    CLA  B1236      50                                                       
HET    CLA  B1201      46                                                       
HET    CLA  B1204      46                                                       
HET    CLA  B1206      46                                                       
HET    CLA  B1211      46                                                       
HET    CLA  B1237      55                                                       
HET    CLA  B1238      44                                                       
HET    CLA  B1239      46                                                       
HET     CL  B6000       1                                                       
HET    SF4  C3002       8                                                       
HET    SF4  C3003       8                                                       
HET    CLA  F1410      65                                                       
HET    BCR  F4015      40                                                       
HET    BCR  F4016      40                                                       
HET    CLA  F1139      65                                                       
HET    CLA  F1301      45                                                       
HET    CLA  J1303      46                                                       
HET    LMU  J1304      35                                                       
HET    BCR  J4013      40                                                       
HET    CLA  J1302      45                                                       
HET    CLA  K1401      46                                                       
HET    CLA  K1402      46                                                       
HETNAM     PQN PHYLLOQUINONE                                                    
HETNAM     SF4 IRON/SULFUR CLUSTER                                              
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     CL0 CHLOROPHYLL A ISOMER                                             
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     LMU DODECYL-ALPHA-D-MALTOSIDE                                        
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM      CL CHLORIDE ION                                                     
HETSYN     PQN VITAMIN K1; 2-METHYL-3-PHYTYL-1,4-NAPHTHOQUINONE                 
FORMUL  10  PQN    2(C31 H46 O2)                                                
FORMUL  11  SF4    3(FE4 S4)                                                    
FORMUL  12  LHG    4(C38 H75 O10 P)                                             
FORMUL  13  CL0    2(C55 H72 MG N4 O5 2+)                                       
FORMUL  15  BCR    17(C40 H56)                                                  
FORMUL  21  CLA    90(C55 H72 MG N4 O5 2+)                                      
FORMUL  65  LMU    2(C24 H46 O11)                                               
FORMUL  67  LMG    C45 H86 O10                                                  
FORMUL  18   CL    CL 1-                                                        
FORMUL  32  HOH   *29(H2 O)                                                     
HELIX    1   1 THR A   45  ASN A   54  1                                  10    
HELIX    2   2 ASP A   57  THR A   62  5                                   6    
HELIX    3   3 ASP A   64  PHE A   97  1                                  34    
HELIX    4   4 ASN A   99  ASP A  106  1                                   8    
HELIX    5   5 GLY A  122  ASN A  127  5                                   6    
HELIX    6   6 GLY A  142  GLY A  151  1                                  10    
HELIX    7   7 ASP A  154  VAL A  182  1                                  29    
HELIX    8   8 LYS A  186  GLN A  191  1                                   6    
HELIX    9   9 ASN A  192  GLY A  203  1                                  12    
HELIX   10  10 LEU A  204  VAL A  219  1                                  16    
HELIX   11  11 VAL A  219  ASP A  228  1                                  10    
HELIX   12  12 PRO A  239  ILE A  243  5                                   5    
HELIX   13  13 GLU A  245  TYR A  253  1                                   9    
HELIX   14  14 PRO A  254  GLN A  258  5                                   5    
HELIX   15  15 PRO A  262  LEU A  266  5                                   5    
HELIX   16  16 ASN A  267  PHE A  274  5                                   8    
HELIX   17  17 TRP A  289  GLY A  308  1                                  20    
HELIX   18  18 SER A  320  ALA A  327  1                                   8    
HELIX   19  19 GLY A  339  LEU A  344  1                                   6    
HELIX   20  20 SER A  347  MET A  373  1                                  27    
HELIX   21  21 ASP A  382  ASP A  415  1                                  34    
HELIX   22  22 ASP A  417  ASN A  421  5                                   5    
HELIX   23  23 ASN A  424  ARG A  431  1                                   8    
HELIX   24  24 HIS A  432  LEU A  464  1                                  33    
HELIX   25  25 ARG A  466  MET A  470  5                                   5    
HELIX   26  26 PRO A  480  LEU A  492  1                                  13    
HELIX   27  27 SER A  506  GLY A  510  5                                   5    
HELIX   28  28 GLY A  528  TYR A  555  1                                  28    
HELIX   29  29 ASP A  564  GLY A  569  1                                   6    
HELIX   30  30 SER A  586  VAL A  617  1                                  32    
HELIX   31  31 ASN A  634  ALA A  639  1                                   6    
HELIX   32  32 THR A  641  PHE A  649  1                                   9    
HELIX   33  33 PHE A  649  ALA A  654  1                                   6    
HELIX   34  34 ALA A  654  ASN A  659  1                                   6    
HELIX   35  35 LEU A  665  SER A  688  1                                  24    
HELIX   36  36 GLY A  689  LEU A  707  1                                  19    
HELIX   37  37 SER A  719  GLY A  751  1                                  33    
HELIX   38  38 SER B    9  GLN B   14  1                                   6    
HELIX   39  39 THR B   18  THR B   27  1                                  10    
HELIX   40  40 ASP B   30  HIS B   34  5                                   5    
HELIX   41  41 THR B   38  GLY B   72  1                                  35    
HELIX   42  42 ASN B   73  ILE B   78  1                                   6    
HELIX   43  43 GLY B   97  THR B  105  1                                   9    
HELIX   44  44 GLY B  119  ILE B  127  1                                   9    
HELIX   45  45 THR B  131  HIS B  156  1                                  26    
HELIX   46  46 SER B  164  LYS B  169  1                                   6    
HELIX   47  47 ASN B  170  GLY B  181  1                                  12    
HELIX   48  48 PHE B  183  VAL B  197  1                                  15    
HELIX   49  49 VAL B  197  ALA B  202  1                                   6    
HELIX   50  50 ASN B  211  THR B  215  5                                   5    
HELIX   51  51 ASN B  229  ALA B  235  5                                   7    
HELIX   52  52 TRP B  269  ILE B  286  1                                  18    
HELIX   53  53 ALA B  287  MET B  290  5                                   4    
HELIX   54  54 SER B  300  ASN B  306  1                                   7    
HELIX   55  55 ASN B  319  SER B  327  1                                   9    
HELIX   56  56 SER B  327  TYR B  351  1                                  25    
HELIX   57  57 ASP B  362  ASP B  395  1                                  34    
HELIX   58  58 ASN B  404  HIS B  412  1                                   9    
HELIX   59  59 HIS B  412  PHE B  444  1                                  33    
HELIX   60  60 THR B  446  GLN B  450  5                                   5    
HELIX   61  61 PRO B  455  THR B  464  1                                  10    
HELIX   62  62 VAL B  474  ASN B  478  5                                   5    
HELIX   63  63 TRP B  490  SER B  500  1                                  11    
HELIX   64  64 GLY B  510  ASP B  537  1                                  28    
HELIX   65  65 ASP B  546  PHE B  550  5                                   5    
HELIX   66  66 SER B  568  GLY B  601  1                                  34    
HELIX   67  67 VAL B  603  SER B  610  1                                   8    
HELIX   68  68 TYR B  612  TYR B  620  1                                   9    
HELIX   69  69 GLN B  627  GLY B  631  5                                   5    
HELIX   70  70 LEU B  640  SER B  663  1                                  24    
HELIX   71  71 TRP B  664  THR B  682  1                                  19    
HELIX   72  72 SER B  698  PHE B  730  1                                  33    
HELIX   73  73 ARG C   44  CYS C   48  5                                   5    
HELIX   74  74 LYS C   52  CYS C   58  1                                   7    
HELIX   75  75 SER D   20  GLU D   25  1                                   6    
HELIX   76  76 ARG D   61  ARG D   73  1                                  13    
HELIX   77  77 ARG D  121  ASN D  125  5                                   5    
HELIX   78  78 ALA E   62  ASN E   64  5                                   3    
HELIX   79  79 ASN F   13  LYS F   21  1                                   9    
HELIX   80  80 ASN F   31  TYR F   40  1                                  10    
HELIX   81  81 ARG F   58  ASP F   64  5                                   7    
HELIX   82  82 PHE F   65  ILE F   90  1                                  26    
HELIX   83  83 ARG F   91  LYS F   94  5                                   4    
HELIX   84  84 ASN F   95  GLU F  100  1                                   6    
HELIX   85  85 ASN F  104  LEU F  113  1                                  10    
HELIX   86  86 GLY F  114  PHE F  116  5                                   3    
HELIX   87  87 LEU F  117  THR F  127  1                                  11    
HELIX   88  88 ASP J    2  SER J    9  1                                   8    
HELIX   89  89 THR J   10  TYR J   33  1                                  24    
HELIX   90  90 GLY K   55  TYR K   76  1                                  22    
HELIX   91  91 LEU K  101  GLU K  103  5                                   3    
HELIX   92  92 LEU K  104  ILE K  127  1                                  24    
HELIX   93  93 ALA M   15  LYS M   31  1                                  17    
SHEET    1   A 2 VAL A  16  ASN A  18  0                                        
SHEET    2   A 2 LYS A 183  PRO A 185 -1  O  ALA A 184   N  ASP A  17           
SHEET    1   B 3 SER A 113  ALA A 114  0                                        
SHEET    2   B 3 HIS A 135  GLN A 138 -1  O  ILE A 137   N  ALA A 114           
SHEET    3   B 3 GLY A 128  ASP A 129 -1  N  GLY A 128   O  GLY A 136           
SHEET    1   C 2 ILE A 514  VAL A 516  0                                        
SHEET    2   C 2 LYS A 519  MET A 522 -1  O  LYS A 519   N  VAL A 516           
SHEET    1   D 2 GLY A 619  VAL A 621  0                                        
SHEET    2   D 2 VAL A 627  HIS A 629 -1  O  THR A 628   N  THR A 620           
SHEET    1   E 2 ILE B  87  ALA B  90  0                                        
SHEET    2   E 2 VAL B 113  ILE B 115 -1  O  ASN B 114   N  ALA B  88           
SHEET    1   F 3 ILE C  65  TYR C  68  0                                        
SHEET    2   F 3 SER C   4  TYR C   8 -1  N  SER C   4   O  TYR C  68           
SHEET    3   F 3 THR D 117  LYS D 118  1  O  LYS D 118   N  ILE C   7           
SHEET    1   G 2 GLU C  27  PRO C  30  0                                        
SHEET    2   G 2 GLN C  38  SER C  41 -1  O  ILE C  39   N  VAL C  29           
SHEET    1   H 4 GLY D  53  LEU D  59  0                                        
SHEET    2   H 4 LYS D  27  SER D  34 -1  N  TYR D  28   O  LEU D  59           
SHEET    3   H 4 LYS D  84  VAL D  88 -1  O  TYR D  86   N  ALA D  29           
SHEET    4   H 4 VAL D  94  HIS D  98 -1  O  HIS D  98   N  ILE D  85           
SHEET    1   I 2 GLN D  38  GLU D  41  0                                        
SHEET    2   I 2 ALA D  47  MET D  50 -1  O  ALA D  48   N  PHE D  40           
SHEET    1   J 5 THR E  58  PHE E  61  0                                        
SHEET    2   J 5 VAL E  37  ARG E  40 -1  N  VAL E  39   O  ASN E  59           
SHEET    3   J 5 VAL E  22  VAL E  28 -1  N  SER E  27   O  ILE E  38           
SHEET    4   J 5 LYS E   8  ILE E  11 -1  N  VAL E   9   O  GLY E  23           
SHEET    5   J 5 LEU E  66  LEU E  68 -1  O  GLU E  67   N  ARG E  10           
SHEET    1   K 3 THR F   8  PRO F   9  0                                        
SHEET    2   K 3 LEU F  44  CYS F  45 -1  O  CYS F  45   N  THR F   8           
SHEET    3   K 3 PRO F  51  HIS F  52 -1  O  HIS F  52   N  LEU F  44           
SSBOND   1 CYS F   10    CYS F   45                          1555   1555  2.03  
LINK         SG  CYS C  17                FE4  SF4 C3003     1555   1555  2.00  
LINK         SG  CYS B 565                FE3  SF4 A3001     1555   1555  2.01  
LINK         SG  CYS C  48                FE4  SF4 C3002     1555   1555  2.08  
LINK         SG  CYS A 583                FE2  SF4 A3001     1555   1555  2.08  
LINK        MG   CLA F1139                 O   HOH A9107     1555   1555  2.09  
LINK         SG  CYS C  11                FE3  SF4 C3003     1555   1555  2.10  
LINK         SG  CYS A 574                FE4  SF4 A3001     1555   1555  2.10  
LINK         SG  CYS C  51                FE1  SF4 C3002     1555   1555  2.21  
LINK         SG  CYS C  14                FE2  SF4 C3003     1555   1555  2.22  
LINK         SG  CYS C  54                FE3  SF4 C3002     1555   1555  2.25  
LINK         SG  CYS B 556                FE1  SF4 A3001     1555   1555  2.26  
LINK        MG   CLA A1022                 O   HOH A9101     1555   1555  2.31  
LINK         SG  CYS C  21                FE2  SF4 C3002     1555   1555  2.31  
LINK         SG  CYS C  58                FE1  SF4 C3003     1555   1555  2.47  
LINK         OE1 GLN A 123                MG   CLA A1107     1555   1555  2.68  
LINK         OE1 GLN A 115                MG   CLA A1106     1555   1555  2.73  
LINK        MG   CLA A1012                 O   HOH B9102     1555   1555  2.74  
LINK        MG   CLA B1237                 O   HOH B9101     1555   1555  2.83  
LINK        MG   CLA B1238                 O   HOH B9110     1555   1555  2.89  
LINK        MG   CLA B1240                 O5  LHG B5004     1555   1555  2.89  
LINK         OE2 GLU J  28                MG   CLA J1302     1555   1555  2.91  
LINK         O   ASP F  56                MG   CLA F1410     1555   1555  2.94  
LINK         O5  LHG A5003                MG   CLA A1801     1555   1555  2.95  
LINK         O1A CLA A1102                MG   CLA A1109     1555   1555  2.96  
LINK         O   THR A 497                MG   CLA A1134     1555   1555  3.00  
LINK         OD2 ASP B  93                MG   CLA B1206     1555   1555  3.00  
CISPEP   1 PHE B    5    PRO B    6          0        -2.01                     
CISPEP   2 THR B  486    GLY B  487          0         8.07                     
CISPEP   3 HIS D   98    PRO D   99          0        -4.01                     
CISPEP   4 SER E   31    GLY E   32          0         1.19                     
SITE     1 AC1 10 MET A 684  PHE A 685  SER A 688  ARG A 690                    
SITE     2 AC1 10 TRP A 693  ALA A 717  LEU A 718  CLA A1101                    
SITE     3 AC1 10 CLA A1140  CLA F1139                                          
SITE     1 AC2  8 CYS A 574  PRO A 577  CYS A 583  ILE A 720                    
SITE     2 AC2  8 CYS B 556  PRO B 559  CYS B 565  TRP B 664                    
SITE     1 AC3 14 ASN A  50  ALA A  53  ASN A  54  ARG A 571                    
SITE     2 AC3 14 TRP A 588  SER A 719  ILE A 721  GLN A 722                    
SITE     3 AC3 14 ALA A 725  CLA A1101  CLA A1104  CLA A1128                    
SITE     4 AC3 14 CLA A1140  GLY E  51                                          
SITE     1 AC4 20 TYR A 455  THR A 541  TYR A 599  ILE A 604                    
SITE     2 AC4 20 PHE A 607  TRP A 645  LEU A 650  PHE A 672                    
SITE     3 AC4 20 HIS A 676  PHE A 679  TYR A 731  THR A 738                    
SITE     4 AC4 20 THR A 739  PHE A 742  CLA A1012  CLA A1022                    
SITE     5 AC4 20 HOH A9109  PHE B 617  TRP B 622  CLA B1021                    
SITE     1 AC5 10 HIS A 328  GLY A 330  PHE A 332  THR A 333                    
SITE     2 AC5 10 HIS A 337  CLA A1122  CLA A1129  CLA A1137                    
SITE     3 AC5 10 CLA A1801  BCR A4007                                          
SITE     1 AC6 10 LEU A 210  PHE A 263  ILE A 305  HIS A 309                    
SITE     2 AC6 10 CLA A1113  CLA A1118  CLA A1120  ALA K 106                    
SITE     3 AC6 10 SER K 109  PHE K 110                                          
SITE     1 AC7  8 THR A 161  LEU A 207  CLA A1103  CLA A1112                    
SITE     2 AC7  8 CLA A1114  CLA A1118  BCR A4003  CLA K1402                    
SITE     1 AC8  8 GLY A 203  LEU A 207  GLY A 208  CLA A1103                    
SITE     2 AC8  8 CLA A1104  CLA A1117  CLA A1127  BCR A4002                    
SITE     1 AC9  5 ALA A 350  CLA A1119  CLA A1122  CLA A1123                    
SITE     2 AC9  5 LHG A5003                                                     
SITE     1 BC1  9 ALA A 357  SER A 361  ILE A 401  ALA A 404                    
SITE     2 BC1  9 CLA A1119  CLA A1124  CLA A1125  CLA A1133                    
SITE     3 BC1  9 CLA A1137                                                     
SITE     1 BC2  8 CLA A1012  CLA A1105  CLA A1106  CLA A1107                    
SITE     2 BC2  8 CLA A1140  CLA B1230  BCR B4011  LEU J  26                    
SITE     1 BC3  8 ALA A 327  HIS A 328  LYS A 329  PRO A 331                    
SITE     2 BC3  8 PHE A 332  CLA A1121  CLA A1122  LHG A5003                    
SITE     1 BC4 20 PHE A 452  ILE A 456  PHE A 540  TRP A 597                    
SITE     2 BC4 20 ASN A 600  ILE A 642  TYR A 731  CL0 A1011                    
SITE     3 BC4 20 HOH A9101  TRP B 645  LEU B 648  PHE B 649                    
SITE     4 BC4 20 HIS B 651  LEU B 652  TRP B 654  ALA B 655                    
SITE     5 BC4 20 CLA B1021  CLA B1023  CLA B1207  BCR B4017                    
SITE     1 BC5 17 ILE A  48  HIS A  52  CLA A1012  CLA A1102                    
SITE     2 BC5 17 CLA A1109  CLA A1126  CLA A1140  PQN A2001                    
SITE     3 BC5 17 LHG A5001  BCR B4011  BCR B4014  VAL F 101                    
SITE     4 BC5 17 CLA F1139  CLA F1301  ALA J  11  PRO J  12                    
SITE     5 BC5 17 BCR J4013                                                     
SITE     1 BC6 18 TRP A  28  HIS A  33  PHE A  34  LEU A  51                    
SITE     2 BC6 18 ALA A  55  HIS A  56  GLN A  61  ALA A  75                    
SITE     3 BC6 18 GLY A  78  HIS A  79  CLA A1101  CLA A1103                    
SITE     4 BC6 18 CLA A1104  CLA A1105  CLA A1107  CLA A1109                    
SITE     5 BC6 18 CLA A1128  BCR J4013                                          
SITE     1 BC7 20 HIS A  56  PHE A  58  ILE A  72  ALA A  75                    
SITE     2 BC7 20 HIS A  76  HIS A  79  PHE A  84  TRP A 348                    
SITE     3 BC7 20 HIS A 349  GLN A 351  LEU A 352  ASN A 355                    
SITE     4 BC7 20 LEU A 356  CLA A1102  CLA A1104  CLA A1111                    
SITE     5 BC7 20 CLA A1123  CLA A1128  BCR A4002  BCR A4003                    
SITE     1 BC8 12 HIS A  56  HIS A  79  VAL A  83  TRP A  86                    
SITE     2 BC8 12 CLA A1102  CLA A1103  CLA A1106  CLA A1126                    
SITE     3 BC8 12 CLA A1127  CLA A1128  BCR A4003  LHG A5001                    
SITE     1 BC9 14 TRP A  86  SER A  88  GLY A  89  MET A  90                    
SITE     2 BC9 14 PHE A  92  HIS A  93  PHE A  97  TRP A 118                    
SITE     3 BC9 14 CLA A1102  CLA A1106  CLA A1107  BCR A4012                    
SITE     4 BC9 14 MET J  14  BCR J4013                                          
SITE     1 CC1 19 TRP A  86  MET A  90  ALA A 114  GLN A 115                    
SITE     2 CC1 19 GLN A 138  ILE A 139  THR A 140  SER A 141                    
SITE     3 CC1 19 LEU A 143  ALA A 667  TYR A 668  CLA A1104                    
SITE     4 CC1 19 CLA A1105  CLA A1107  CLA A1109  CLA A1126                    
SITE     5 CC1 19 BCR A4012  BCR B4011  BCR J4013                               
SITE     1 CC2 14 GLN A 115  VAL A 116  VAL A 117  TRP A 118                    
SITE     2 CC2 14 GLN A 123  ILE A 137  CLA A1102  CLA A1105                    
SITE     3 CC2 14 CLA A1106  CLA A1126  BCR A4012  VAL B 440                    
SITE     4 CC2 14 CLA B1230  BCR J4013                                          
SITE     1 CC3 12 VAL A  14  VAL A  16  PHE A  77  LEU A 171                    
SITE     2 CC3 12 MET A 172  ALA A 175  PHE A 178  HIS A 179                    
SITE     3 CC3 12 LYS A 183  TRP A 189  CLA A1110  CLA A1111                    
SITE     1 CC4 14 THR A  23  SER A  24  TRP A  28  HIS A  33                    
SITE     2 CC4 14 LYS A  71  SER A  74  LEU A 173  GLY A 176                    
SITE     3 CC4 14 TRP A 177  TYR A 180  HIS A 181  CLA A1101                    
SITE     4 CC4 14 CLA A1102  CLA A1106                                          
SITE     1 CC5 11 LYS A  13  VAL A  14  TRP A 189  ASN A 192                    
SITE     2 CC5 11 SER A 195  HIS A 199  THR A 313  ASN A 314                    
SITE     3 CC5 11 CL0 A1108  CLA A1111  CLA A1118                               
SITE     1 CC6 12 HIS A  76  PHE A  77  TRP A 189  ASN A 192                    
SITE     2 CC6 12 MET A 196  HIS A 199  HIS A 200  LEU A 204                    
SITE     3 CC6 12 CLA A1103  CL0 A1108  CLA A1110  CLA A1123                    
SITE     1 CC7 15 SER A 150  GLY A 151  PHE A 152  GLN A 157                    
SITE     2 CC7 15 CYS A 160  THR A 161  GLY A 211  TRP A 212                    
SITE     3 CC7 15 HIS A 215  VAL A 219  PRO A 239  HIS A 240                    
SITE     4 CC7 15 CLA A1113  CLA A1114  BCR A4002                               
SITE     1 CC8  9 LEU A 210  ILE A 217  HIS A 218  PRO A 246                    
SITE     2 CC8  9 PHE A 256  GLN A 258  GLY A 259  CLA A1112                    
SITE     3 CC8  9 BCR A4001                                                     
SITE     1 CC9 17 GLY A 279  LEU A 288  ASP A 292  THR A 293                    
SITE     2 CC9 17 HIS A 295  HIS A 296  ALA A 299  ILE A 300                    
SITE     3 CC9 17 LEU A 303  HIS A 369  MET A 373  ALA A 505                    
SITE     4 CC9 17 CLA A1115  CLA A1117  CLA A1125  CLA A1133                    
SITE     5 CC9 17 CLA A1134                                                     
SITE     1 DC1 20 ALA A 149  SER A 150  LEU A 205  GLY A 208                    
SITE     2 DC1 20 SER A 209  TRP A 212  GLN A 216  THR A 293                    
SITE     3 DC1 20 HIS A 296  HIS A 297  ILE A 300  PHE A 304                    
SITE     4 DC1 20 LEU A 362  VAL A 366  MET A 370  PRO A 375                    
SITE     5 DC1 20 TYR A 376  CLA A1116  CLA A1127  BCR A4003                    
SITE     1 DC2 15 ASN A 198  HIS A 199  ALA A 202  GLY A 203                    
SITE     2 DC2 15 LEU A 207  HIS A 309  TYR A 311  THR A 313                    
SITE     3 DC2 15 TRP A 315  ILE A 317  CLA A1110  BCR A4001                    
SITE     4 DC2 15 BCR A4002  ALA K 106  SER K 109                               
SITE     1 DC3 14 MET A 197  LEU A 201  PHE A 304  ALA A 307                    
SITE     2 DC3 14 MET A 310  TYR A 311  VAL A 553  CLA A1120                    
SITE     3 DC3 14 CLA A1121  CLA A1122  CLA A1123  CLA A1124                    
SITE     4 DC3 14 BCR A4007  BCR A4008                                          
SITE     1 DC4 13 ILE A 324  LEU A 325  HIS A 337  LEU A 340                    
SITE     2 DC4 13 LEU A 425  MET A 429  CLA A1119  CLA A1123                    
SITE     3 DC4 13 CLA A1129  CLA A1137  CLA A1801  BCR A4007                    
SITE     4 DC4 13 LHG A5003                                                     
SITE     1 DC5 17 SER A  69  HIS A  76  LEU A 187  VAL A 193                    
SITE     2 DC5 17 HIS A 200  MET A 321  LEU A 344  TRP A 348                    
SITE     3 DC5 17 ILE A 354  ASN A 355  LEU A 358  CLA A1103                    
SITE     4 DC5 17 CLA A1111  CLA A1119  CLA A1122  CLA A1127                    
SITE     5 DC5 17 BCR A4007                                                     
SITE     1 DC6 13 SER A 361  ILE A 364  ILE A 365  GLN A 368                    
SITE     2 DC6 13 ILE A 401  ILE A 542  SER A 601  CLA A1119                    
SITE     3 DC6 13 CLA A1125  CLA A1133  CLA A1135  CLA A1137                    
SITE     4 DC6 13 BCR A4008                                                     
SITE     1 DC7 12 LEU A 358  ILE A 365  HIS A 369  ALA A 372                    
SITE     2 DC7 12 MET A 373  SER A 506  PHE A 509  CLA A1116                    
SITE     3 DC7 12 CLA A1124  CLA A1133  CLA A1135  BCR A4008                    
SITE     1 DC8 15 TRP A  86  MET A  90  SER A 141  THR A 391                    
SITE     2 DC8 15 HIS A 392  TRP A 395  TRP A 740  CLA A1101                    
SITE     3 DC8 15 CLA A1104  CLA A1106  CLA A1107  CLA A1127                    
SITE     4 DC8 15 CLA A1128  CLA B1230  BCR B4011                               
SITE     1 DC9 17 LEU A  87  SER A 141  GLY A 142  LEU A 146                    
SITE     2 DC9 17 LEU A 362  THR A 363  MET A 370  TYR A 376                    
SITE     3 DC9 17 LEU A 389  HIS A 392  HIS A 393  ILE A 396                    
SITE     4 DC9 17 CLA A1104  CLA A1117  CLA A1123  CLA A1126                    
SITE     5 DC9 17 BCR A4003                                                     
SITE     1 EC1 19 HIS A  52  ALA A  53  HIS A  56  ASP A  57                    
SITE     2 EC1 19 LEU A 356  PHE A 399  GLY A 403  HIS A 407                    
SITE     3 EC1 19 ILE A 410  ARG A 414  PHE A 570  ARG A 571                    
SITE     4 EC1 19 TRP A 588  CLA A1102  CLA A1103  CLA A1104                    
SITE     5 EC1 19 CLA A1126  CLA A1140  LHG A5001                               
SITE     1 EC2 13 PHE A 446  LEU A 447  PRO A 480  ILE A 481                    
SITE     2 EC2 13 PHE A 482  ALA A 483  PHE A 532  HIS A 535                    
SITE     3 EC2 13 HIS A 536  HIS A 543  CLA A1131  CLA A1135                    
SITE     4 EC2 13 CLA A1137                                                     
SITE     1 EC3 12 ILE A 436  LEU A 440  TRP A 442  VAL A 443                    
SITE     2 EC3 12 HIS A 543  CLA A1122  CLA A1124  CLA A1129                    
SITE     3 EC3 12 CLA A1135  CLA A1136  BCR A4008  LHG A5003                    
SITE     1 EC4 13 ILE A 700  HIS A 704  LEU A 707  SER B 418                    
SITE     2 EC4 13 SER B 421  TRP B 422  LEU B 425  CLA B1228                    
SITE     3 EC4 13 CLA B1229  BCR B4014  GLY F  80  TYR F  86                    
SITE     4 EC4 13 CLA F1139                                                     
SITE     1 EC5 17 TRP A  49  PHE A 677  PHE A 681  GLN A 722                    
SITE     2 EC5 17 ALA A 725  VAL A 726  ALA A 729  HIS A 730                    
SITE     3 EC5 17 CLA A1101  CLA A1128  PQN A2001  BCR A4012                    
SITE     4 EC5 17 LHG A5001  CLA B1013  BCR B4011  CLA F1301                    
SITE     5 EC5 17 LEU J  19                                                     
SITE     1 EC6 19 LEU A 673  ALA A 674  PHE A 677  ALA A 680                    
SITE     2 EC6 19 CL0 A1011  CLA A1101  BCR A4012  VAL B 436                    
SITE     3 EC6 19 PHE B 578  TRP B 579  ASN B 582  TRP B 586                    
SITE     4 EC6 19 LEU B 613  PHE B 617  CLA B1013  CLA B1021                    
SITE     5 EC6 19 CLA B1230  BCR B4011  HOH B9102                               
SITE     1 EC7  5 TYR A 156  CYS A 160  HIS A 240  CLA A1112                    
SITE     2 EC7  5 BCR A4002                                                     
SITE     1 EC8 12 TRP A 268  TYR A 271  LEU A 275  PHE A 277                    
SITE     2 EC8 12 HIS A 295  LEU A 298  ALA A 299  VAL A 302                    
SITE     3 EC8 12 ASN A 500  CLA A1116  CLA A1134  CLA K1401                    
SITE     1 EC9 11 ILE A 306  HIS A 309  MET A 310  ARG A 312                    
SITE     2 EC9 11 GLY A 318  HIS A 319  CLA A1119  CLA A1121                    
SITE     3 EC9 11 BCR A4001  PHE K  72  ALA K  78                               
SITE     1 FC1  6 HIS A 319  ALA A 327  HIS A 328  CLA A1119                    
SITE     2 FC1  6 CLA A1120  CLA A1801                                          
SITE     1 FC2 12 PHE A 332  THR A 333  LEU A 425  ARG A 428                    
SITE     2 FC2 12 MET A 429  HIS A 432  ILE A 436  HIS A 439                    
SITE     3 FC2 12 CLA A1122  CLA A1130  CLA A1137  LHG A5003                    
SITE     1 FC3  5 ALA A 435  HIS A 439  TRP A 442  CLA A1129                    
SITE     2 FC3  5 THR B 682                                                     
SITE     1 FC4 11 TRP A 442  ILE A 445  PHE A 446  PHE A 449                    
SITE     2 FC4 11 HIS A 450  CLA A1132  CLA A1136  LHG A5005                    
SITE     3 FC4 11 CLA B1237  PQN B2002  BCR B4017                               
SITE     1 FC5 11 PHE A 449  GLY A 453  HIS A 457  THR A 460                    
SITE     2 FC5 11 MET A 461  ARG A 466  ASP A 469  CLA A1131                    
SITE     3 FC5 11 CLA B1023  CLA B1206  CLA B1207                               
SITE     1 FC6 12 TRP A 485  VAL A 486  HIS A 490  ALA A 493                    
SITE     2 FC6 12 THR A 497  ALA A 498  CLA A1116  CLA A1124                    
SITE     3 FC6 12 CLA A1125  CLA A1134  CLA A1135  BCR A4008                    
SITE     1 FC7  7 THR A 497  PRO A 499  ASN A 500  CLA A1115                    
SITE     2 FC7  7 CLA A1116  CLA A1133  CLA K1401                               
SITE     1 FC8 19 GLN A 368  TYR A 371  PHE A 482  ALA A 483                    
SITE     2 FC8 19 VAL A 486  GLN A 487  HIS A 490  PHE A 509                    
SITE     3 FC8 19 ILE A 525  HIS A 535  HIS A 538  VAL A 605                    
SITE     4 FC8 19 HIS A 608  PHE A 609  CLA A1124  CLA A1125                    
SITE     5 FC8 19 CLA A1133  CLA A1136  CLA A1137                               
SITE     1 FC9  4 GLN A 468  ASP A 469  ILE A 476  CLA A1131                    
SITE     1 GC1  6 HIS B 308  LYS B 309  PRO B 311  CLA B1219                    
SITE     2 GC1  6 CLA B1220  LHG B5004                                          
SITE     1 GC2  6 ILE B 482  THR B 486  GLY B 487  ALA B 489                    
SITE     2 GC2  6 CLA B1213  CLA B1232                                          
SITE     1 GC3 13 CLA A1131  MET B 659  PHE B 660  SER B 663                    
SITE     2 GC3 13 ARG B 665  TRP B 668  ALA B 696  LEU B 697                    
SITE     3 GC3 13 ALA B 702  CLA B1238  CLA B1239  BCR B4017                    
SITE     4 GC3 13 LMG B5002                                                     
SITE     1 GC4 12 TYR B  23  ALA B  26  SER B 553  TRP B 570                    
SITE     2 GC4 12 VAL B 700  GLN B 701  LEU B 704  CLA B1201                    
SITE     3 GC4 12 CLA B1203  CLA B1226  CLA B1239  PQN B2002                    
SITE     1 GC5 12 HIS B 308  GLY B 310  PRO B 311  LEU B 312                    
SITE     2 GC5 12 THR B 313  HIS B 317  VAL B 405  CLA B1220                    
SITE     3 GC5 12 CLA B1227  CLA B1236  CLA B1240  BCR B4009                    
SITE     1 GC6  8 LEU B 188  PHE B 225  PHE B 226  ILE B 285                    
SITE     2 GC6  8 HIS B 289  CLA B1212  CLA B1217  CLA B1218                    
SITE     1 GC7  5 GLY B 181  SER B 186  CLA B1209  CLA B1210                    
SITE     2 GC7  5 CLA B1225                                                     
SITE     1 GC8  7 LEU B  65  MET B 129  PHE B 141  LEU B 142                    
SITE     2 GC8  7 CLA B1211  CLA B1212  CLA B1225                               
SITE     1 GC9  6 MET B 409  ILE B 532  CLA B1220  CLA B1223                    
SITE     2 GC9  6 CLA B1227  LHG B5004                                          
SITE     1 HC1  9 LEU B 334  MET B 381  PHE B 385  GLY B 388                    
SITE     2 HC1  9 CLA B1216  CLA B1222  CLA B1223  CLA B1232                    
SITE     3 HC1  9 CLA B1236                                                     
SITE     1 HC2 15 ALA A 674  PHE A 677  ILE A 736  VAL A 737                    
SITE     2 HC2 15 TRP A 740  CLA A1012  CLA A1101  CLA A1106                    
SITE     3 HC2 15 CLA A1126  CLA A1140  BCR A4012  LEU B 432                    
SITE     4 HC2 15 CLA B1013  CLA B1229  CLA B1230                               
SITE     1 HC3  9 CLA A1101  CLA A1138  PHE B 429  CLA B1229                    
SITE     2 HC3  9 PRO F  68  PHE F  72  ILE F  75  CLA F1301                    
SITE     3 HC3  9 BCR F4015                                                     
SITE     1 HC4  8 CLA A1022  CLA A1131  TRP B 645  PHE B 649                    
SITE     2 HC4  8 CLA B1023  CLA B1206  CLA B1239  PQN B2002                    
SITE     1 HC5 22 PHE A 677  ALA A 680  PHE A 681  MET A 684                    
SITE     2 HC5 22 PHE A 687  TYR A 692  TRP A 693  LEU A 696                    
SITE     3 HC5 22 CLA A1012  CLA A1140  SER B 421  SER B 424                    
SITE     4 HC5 22 LEU B 425  GLY B 428  PHE B 429  LEU B 522                    
SITE     5 HC5 22 LEU B 529  ILE B 530  LEU B 575  PHE B 578                    
SITE     6 HC5 22 TRP B 579  BCR B4011                                          
SITE     1 HC6 18 LEU A 646  LEU A 650  TRP A 651  CL0 A1011                    
SITE     2 HC6 18 CLA A1012  CLA A1022  ALA B 519  TRP B 586                    
SITE     3 HC6 18 PHE B 589  LEU B 613  SER B 625  PHE B 647                    
SITE     4 HC6 18 HIS B 651  TRP B 654  TYR B 714  THR B 717                    
SITE     5 HC6 18 TYR B 718  PHE B 721                                          
SITE     1 HC7 20 ASN A 441  CYS A 444  ILE A 445  GLY A 448                    
SITE     2 HC7 20 PHE A 449  ILE A 456  PHE A 540  LEU A 547                    
SITE     3 HC7 20 ILE A 548  PHE A 596  TRP A 597  CLA A1022                    
SITE     4 HC7 20 CLA A1132  ALA B 655  THR B 656  PHE B 658                    
SITE     5 HC7 20 MET B 659  TYR B 667  TRP B 668  BCR B4017                    
SITE     1 HC8 18 HIS B  29  PHE B  31  TYR B  43  ILE B  46                    
SITE     2 HC8 18 SER B  49  HIS B  50  HIS B  53  ILE B  54                    
SITE     3 HC8 18 PHE B 168  ARG B 174  LEU B 182  LEU B 328                    
SITE     4 HC8 18 LEU B 332  ALA B 335  CLA B1203  CLA B1210                    
SITE     5 HC8 18 CLA B1221  CLA B1226                                          
SITE     1 HC9 10 HIS B  29  HIS B  53  TRP B  60  ILE B 376                    
SITE     2 HC9 10 CLA B1201  CLA B1202  CLA B1224  CLA B1225                    
SITE     3 HC9 10 CLA B1226  LMG B5002                                          
SITE     1 IC1 14 ALA B  88  HIS B  89  ASN B 114  ILE B 115                    
SITE     2 IC1 14 ALA B 116  TYR B 117  SER B 118  VAL B 642                    
SITE     3 IC1 14 TRP B 643  MET B 646  CLA B1204  CLA B1206                    
SITE     4 IC1 14 CLA B1224  CLA B1226                                          
SITE     1 IC2  5 CLA A1022  CLA A1132  TRP B  92  HIS B  95                    
SITE     2 IC2  5 CLA B1206                                                     
SITE     1 IC3 10 PHE B  47  PHE B  51  LEU B 148  PHE B 151                    
SITE     2 IC3 10 ALA B 152  HIS B 156  PHE B 161  TRP B 167                    
SITE     3 IC3 10 CLA B1209  CLA B1210                                          
SITE     1 IC4  7 TRP B 167  SER B 173  HIS B 177  CLA B1208                    
SITE     2 IC4  7 CLA B1210  CLA B1217  BCR B4005                               
SITE     1 IC5 18 PHE B  47  HIS B  50  PHE B  51  ILE B  54                    
SITE     2 IC5 18 TRP B 123  TRP B 167  ASN B 170  ARG B 174                    
SITE     3 IC5 18 HIS B 177  HIS B 178  LEU B 182  TYR B 356                    
SITE     4 IC5 18 CLA B1202  CLA B1208  CLA B1209  CLA B1215                    
SITE     5 IC5 18 CLA B1225  BCR B4005                                          
SITE     1 IC6 13 LEU B 188  ALA B 191  GLY B 192  HIS B 196                    
SITE     2 IC6 13 PHE B 212  THR B 215  PRO B 216  PRO B 217                    
SITE     3 IC6 13 GLY B 221  LEU B 222  CLA B1211  BCR B4004                    
SITE     4 IC6 13 BCR B4006                                                     
SITE     1 IC7  8 TRP B 230  LEU B 255  PHE B 257  HIS B 275                    
SITE     2 IC7  8 LEU B 278  ALA B 279  CLA B1214  LMU B1301                    
SITE     1 IC8 16 THR B 256  PHE B 257  LEU B 268  ASP B 272                    
SITE     2 IC8 16 HIS B 275  HIS B 276  ILE B 280  ILE B 283                    
SITE     3 IC8 16 HIS B 349  TRP B 494  CLA B1213  CLA B1215                    
SITE     4 IC8 16 CLA B1221  CLA B1223  CLA B1231  CLA B1232                    
SITE     1 IC9 19 TRP B 123  PHE B 183  SER B 186  SER B 187                    
SITE     2 IC9 19 TRP B 190  ILE B 273  HIS B 276  HIS B 277                    
SITE     3 IC9 19 ILE B 280  ILE B 342  VAL B 346  MET B 350                    
SITE     4 IC9 19 SER B 355  TYR B 356  CLA B1210  CLA B1214                    
SITE     5 IC9 19 CLA B1221  CLA B1223  CLA B1225                               
SITE     1 JC1 15 LEU B 179  ILE B 283  PHE B 284  ILE B 286                    
SITE     2 JC1 15 ALA B 287  MET B 290  TYR B 291  ILE B 304                    
SITE     3 JC1 15 CLA B1218  CLA B1219  CLA B1220  CLA B1221                    
SITE     4 JC1 15 CLA B1223  CLA B1231  BCR B4010                               
SITE     1 JC2  8 ASN B 176  HIS B 177  ALA B 180  HIS B 289                    
SITE     2 JC2  8 THR B 293  TRP B 295  CLA B1209  BCR B4004                    
SITE     1 JC3  7 ILE B 286  MET B 290  GLY B 298  HIS B 299                    
SITE     2 JC3  7 CLA B1216  CLA B1219  BCR B4004                               
SITE     1 JC4  9 MET B 290  HIS B 299  ILE B 304  ALA B 307                    
SITE     2 JC4  9 HIS B 308  CLA B1216  CLA B1218  CLA B1220                    
SITE     3 JC4  9 CLA B1240                                                     
SITE     1 JC5 12 LEU B 305  HIS B 308  HIS B 317  ILE B 324                    
SITE     2 JC5 12 VAL B 405  CLA B1216  CLA B1219  CLA B1221                    
SITE     3 JC5 12 CLA B1227  CLA B1240  BCR B4009  LHG B5004                    
SITE     1 JC6 15 ALA B 171  ARG B 174  LEU B 175  HIS B 178                    
SITE     2 JC6 15 PHE B 284  ILE B 301  LEU B 305  LEU B 334                    
SITE     3 JC6 15 ILE B 342  CLA B1202  CLA B1214  CLA B1215                    
SITE     4 JC6 15 CLA B1216  CLA B1220  CLA B1223                               
SITE     1 JC7 14 VAL B 341  SER B 344  GLN B 348  GLN B 374                    
SITE     2 JC7 14 MET B 381  PHE B 385  LEU B 524  THR B 527                    
SITE     3 JC7 14 LEU B 531  MET B 580  CLA B1223  CLA B1234                    
SITE     4 JC7 14 CLA B1236  BCR B4010                                          
SITE     1 JC8 16 SER B 338  VAL B 341  LEU B 345  HIS B 349                    
SITE     2 JC8 16 SER B 352  LEU B 353  LEU B 505  CLA B1214                    
SITE     3 JC8 16 CLA B1215  CLA B1216  CLA B1221  CLA B1222                    
SITE     4 JC8 16 CLA B1231  CLA B1234  BCR B4009  BCR B4010                    
SITE     1 JC9  9 TRP B  60  SER B 118  THR B 371  HIS B 372                    
SITE     2 JC9  9 TYR B 375  PHE B 379  CLA B1203  CLA B1205                    
SITE     3 JC9  9 CLA B1225                                                     
SITE     1 KC1 18 THR B  61  GLY B 119  TRP B 123  ALA B 189                    
SITE     2 KC1 18 ILE B 342  THR B 343  MET B 350  TYR B 356                    
SITE     3 KC1 18 LEU B 369  HIS B 372  HIS B 373  ILE B 376                    
SITE     4 KC1 18 CLA B1203  CLA B1210  CLA B1215  CLA B1224                    
SITE     5 KC1 18 BCR B4005  BCR B4006                                          
SITE     1 KC2 17 ILE B  25  ALA B  26  HIS B  29  ASP B  30                    
SITE     2 KC2 17 LEU B 332  PHE B 379  GLY B 383  HIS B 387                    
SITE     3 KC2 17 ILE B 390  ARG B 394  TRP B 570  PHE B 573                    
SITE     4 KC2 17 VAL B 712  CLA B1202  CLA B1203  CLA B1205                    
SITE     5 KC2 17 LMG B5002                                                     
SITE     1 KC3 13 LEU B 312  THR B 313  VAL B 405  ARG B 408                    
SITE     2 KC3 13 MET B 409  HIS B 412  LEU B 416  HIS B 419                    
SITE     3 KC3 13 CLA B1220  CLA B1228  CLA B1236  BCR B4009                    
SITE     4 KC3 13 LHG B5004                                                     
SITE     1 KC4  8 LYS A 706  CLA A1138  ALA B 415  HIS B 419                    
SITE     2 KC4  8 CLA B1227  VAL F 132  ASP F 135  BCR F4016                    
SITE     1 KC5 13 CLA A1138  TRP B 422  LEU B 425  PHE B 426                    
SITE     2 KC5 13 PHE B 429  HIS B 430  CLA B1230  BCR B4011                    
SITE     3 KC5 13 BCR B4014  SER F  69  PHE F  72  ALA F  76                    
SITE     4 KC5 13 BCR F4016                                                     
SITE     1 KC6 18 VAL A 121  CLA A1012  CLA A1107  CLA A1126                    
SITE     2 KC6 18 BCR A4012  GLY B 433  HIS B 437  LYS B 449                    
SITE     3 KC6 18 CLA B1229  BCR B4011  HOH B9106  LEU F  71                    
SITE     4 KC6 18 CLA F1301  BCR F4015  ASN J  30  ASP J  35                    
SITE     5 KC6 18 LEU J  36  LEU J  37                                          
SITE     1 KC7 12 TRP B 460  ILE B 461  THR B 464  SER B 465                    
SITE     2 KC7 12 LEU B 476  TRP B 490  LEU B 491  CLA B1214                    
SITE     3 KC7 12 CLA B1216  CLA B1223  CLA B1232  CLA B1234                    
SITE     1 KC8  6 THR B 486  TRP B 490  CLA B1214  CLA B1231                    
SITE     2 KC8  6 LMU B1301  BCR B4010                                          
SITE     1 KC9 17 TYR B 351  TYR B 370  ALA B 458  ILE B 461                    
SITE     2 KC9 17 GLN B 462  LEU B 507  ILE B 509  HIS B 517                    
SITE     3 KC9 17 ILE B 520  LEU B 587  TYR B 590  TRP B 591                    
SITE     4 KC9 17 CLA B1222  CLA B1223  CLA B1231  CLA B1235                    
SITE     5 KC9 17 CLA F1410                                                     
SITE     1 LC1 18 PHE B 426  LEU B 427  GLU B 454  PRO B 455                    
SITE     2 LC1 18 VAL B 456  PHE B 457  ALA B 458  PHE B 514                    
SITE     3 LC1 18 HIS B 517  HIS B 518  HIS B 525  CLA B1234                    
SITE     4 LC1 18 CLA B1236  HOH B9105  VAL F  55  PHE F  65                    
SITE     5 LC1 18 BCR F4015  BCR F4016                                          
SITE     1 LC2 11 LEU B 420  TRP B 422  VAL B 423  ALA B 521                    
SITE     2 LC2 11 HIS B 525  ILE B 532  CLA B1222  CLA B1227                    
SITE     3 LC2 11 CLA B1235  BCR B4010  LHG B5004                               
SITE     1 LC3 10 PHE B   5  ILE B  25  ALA B  28  HIS B  29                    
SITE     2 LC3 10 HIS B  34  CLA B1203  LMG B5002  SER M  26                    
SITE     3 LC3 10 LEU M  29  TYR M  30                                          
SITE     1 LC4 13 LEU B  59  SER B  62  GLY B  63  PHE B  66                    
SITE     2 LC4 13 HIS B  67  TRP B  70  GLN B  71  TRP B  92                    
SITE     3 LC4 13 LEU B 143  CLA B1205  CLA B1206  ALA M  11                    
SITE     4 LC4 13 ALA M  15                                                     
SITE     1 LC5 16 ALA A 463  LEU A 464  CLA A1132  HIS B  89                    
SITE     2 LC5 16 ILE B  91  TRP B  92  ASP B  93  HIS B  95                    
SITE     3 LC5 16 ASN B 114  SER B 641  VAL B 642  TRP B 645                    
SITE     4 LC5 16 CLA B1204  CLA B1205  CLA B1207  BCR B4017                    
SITE     1 LC6 17 ILE B 127  GLY B 128  SER B 137  GLY B 138                    
SITE     2 LC6 17 PHE B 141  SER B 186  ALA B 189  TRP B 190                    
SITE     3 LC6 17 GLY B 192  HIS B 193  HIS B 196  VAL B 197                    
SITE     4 LC6 17 GLY B 208  TRP B 209  PHE B 212  CLA B1212                    
SITE     5 LC6 17 BCR B4006                                                     
SITE     1 LC7  8 SER A 438  ASN A 441  TRP A 442  CLA A1131                    
SITE     2 LC7  8 ALA B 678  THR B 682  CLA B1238  HOH B9101                    
SITE     1 LC8 15 ILE B  21  TRP B  22  VAL B 676  HIS B 679                    
SITE     2 LC8 15 VAL B 688  ARG B 689  TRP B 690  LYS B 691                    
SITE     3 LC8 15 ASP B 692  PRO B 694  VAL B 695  CLA B1237                    
SITE     4 LC8 15 PQN B2002  HOH B9101  HOH B9110                               
SITE     1 LC9  8 PHE B 649  VAL B 653  PHE B 660  VAL B 705                    
SITE     2 LC9  8 HIS B 709  PQN B2002  BCR B4017  LMG B5002                    
SITE     1 MC1  4 ARG A 462  THR A 641  ARG A 647  ASN B 633                    
SITE     1 MC2  6 CYS C  21  VAL C  25  CYS C  48  CYS C  51                    
SITE     2 MC2  6 LYS C  52  CYS C  54                                          
SITE     1 MC3  7 CYS C  11  GLY C  13  CYS C  14  THR C  15                    
SITE     2 MC3  7 CYS C  17  CYS C  58  PRO C  59                               
SITE     1 MC4  9 PHE B 457  TRP B 460  CLA B1234  ASP F  56                    
SITE     2 MC4  9 GLY F  57  ARG F  58  PHE F  59  LEU F  66                    
SITE     3 MC4  9 BCR F4016                                                     
SITE     1 MC5 13 PHE B 426  HIS B 430  LEU B 434  ILE B 453                    
SITE     2 MC5 13 CLA B1230  CLA B1235  BCR B4014  HOH B9105                    
SITE     3 MC5 13 PRO F  68  LEU J  37  HIS J  39  PRO J  40                    
SITE     4 MC5 13 CLA J1303                                                     
SITE     1 MC6  7 CLA B1228  CLA B1229  CLA B1235  VAL F  55                    
SITE     2 MC6  7 TRP F  81  ALA F 122  CLA F1410                               
SITE     1 MC7 22 THR A  45  ILE A  48  TRP A  49  VAL A 701                    
SITE     2 MC7 22 HIS A 704  VAL A 709  PRO A 711  PRO A 715                    
SITE     3 MC7 22 ARG A 716  CLA A1101  CLA A1138  PQN A2001                    
SITE     4 MC7 22 HOH A9107  TYR F  86  LEU F  87  GLU F 100                    
SITE     5 MC7 22 ILE F 103  MET F 112  CLA F1301  ILE J  15                    
SITE     6 MC7 22 ALA J  17  LEU J  18                                          
SITE     1 MC8 11 CLA A1101  CLA A1140  CLA B1230  BCR B4014                    
SITE     2 MC8 11 TRP F  78  ILE F  79  MET F 112  CLA F1139                    
SITE     3 MC8 11 LEU J  18  THR J  22  LEU J  26                               
SITE     1 MC9  4 ILE F  67  LEU F  71  BCR F4015  HIS J  39                    
SITE     1 NC1  4 ILE F 103  LYS J   5  SER J   6  SER J   9                    
SITE     1 NC2 13 TRP A 118  CLA A1101  CLA A1102  CLA A1105                    
SITE     2 NC2 13 CLA A1106  CLA A1107  VAL J  13  MET J  16                    
SITE     3 NC2 13 THR J  20  ILE J  27  GLU J  28  ARG J  31                    
SITE     4 NC2 13 CLA J1302                                                     
SITE     1 NC3  5 GLY J  24  GLU J  28  ARG J  31  PHE J  32                    
SITE     2 NC3  5 BCR J4013                                                     
SITE     1 NC4  6 CLA A1115  CLA A1134  LEU K 114  GLY K 117                    
SITE     2 NC4  6 MET K 118  SER K 125                                          
SITE     1 NC5  8 PHE A 264  BCR A4002  ALA K  54  SER K  59                    
SITE     2 NC5  8 ILE K  62  ILE K  63  LEU K  66  HIS K 112                    
CRYST1  120.179  173.308  179.136  90.00  90.00  90.00 P 21 21 21    4          
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      0.008321  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005770  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005582        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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