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Database: PDB
Entry: 4PJ0
LinkDB: 4PJ0
Original site: 4PJ0 
HEADER    OXIDOREDUCTASE, ELECTRON TRANSPORT      10-MAY-14   4PJ0              
TITLE     STRUCTURE OF T.ELONGATUS PHOTOSYSTEM II, ROWS OF DIMERS CRYSTAL       
TITLE    2 PACKING                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN 1;                                
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN 1,PHOTOSYSTEM II PROTEIN  
COMPND   5 D1 1;                                                                
COMPND   6 EC: 1.10.3.9;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CP47 PROTEIN;                                              
COMPND   9 CHAIN: B, b;                                                         
COMPND  10 EC: 1.10.3.9;                                                        
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;                               
COMPND  13 CHAIN: C, c;                                                         
COMPND  14 EC: 1.10.3.9;                                                        
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  17 CHAIN: D, d;                                                         
COMPND  18 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM Q(A) PROTEIN;                   
COMPND  19 EC: 1.10.3.9;                                                        
COMPND  20 MOL_ID: 5;                                                           
COMPND  21 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  22 CHAIN: E, e;                                                         
COMPND  23 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  24 EC: 1.10.3.9;                                                        
COMPND  25 MOL_ID: 6;                                                           
COMPND  26 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  27 CHAIN: F, f;                                                         
COMPND  28 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  29 EC: 1.10.3.9;                                                        
COMPND  30 MOL_ID: 7;                                                           
COMPND  31 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  32 CHAIN: H, h;                                                         
COMPND  33 SYNONYM: PSII-H;                                                     
COMPND  34 EC: 1.10.3.9;                                                        
COMPND  35 MOL_ID: 8;                                                           
COMPND  36 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  37 CHAIN: I, i;                                                         
COMPND  38 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;                                
COMPND  39 EC: 1.10.3.9;                                                        
COMPND  40 MOL_ID: 9;                                                           
COMPND  41 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  42 CHAIN: J, j;                                                         
COMPND  43 SYNONYM: PSII-J;                                                     
COMPND  44 EC: 1.10.3.9;                                                        
COMPND  45 MOL_ID: 10;                                                          
COMPND  46 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  47 CHAIN: K, k;                                                         
COMPND  48 SYNONYM: PSII-K;                                                     
COMPND  49 EC: 1.10.3.9;                                                        
COMPND  50 MOL_ID: 11;                                                          
COMPND  51 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  52 CHAIN: L, l;                                                         
COMPND  53 SYNONYM: PSII-L,PSII 5 KDA PROTEIN;                                  
COMPND  54 EC: 1.10.3.9;                                                        
COMPND  55 MOL_ID: 12;                                                          
COMPND  56 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  57 CHAIN: M, m;                                                         
COMPND  58 SYNONYM: PSII-M;                                                     
COMPND  59 EC: 1.10.3.9;                                                        
COMPND  60 MOL_ID: 13;                                                          
COMPND  61 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  62 CHAIN: O, o;                                                         
COMPND  63 SYNONYM: MSP;                                                        
COMPND  64 EC: 1.10.3.9;                                                        
COMPND  65 MOL_ID: 14;                                                          
COMPND  66 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  67 CHAIN: T, t;                                                         
COMPND  68 SYNONYM: PSII-TC;                                                    
COMPND  69 EC: 1.10.3.9;                                                        
COMPND  70 MOL_ID: 15;                                                          
COMPND  71 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  72 CHAIN: U, u;                                                         
COMPND  73 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;              
COMPND  74 EC: 1.10.3.9;                                                        
COMPND  75 MOL_ID: 16;                                                          
COMPND  76 MOLECULE: CYTOCHROME C-550;                                          
COMPND  77 CHAIN: V, v;                                                         
COMPND  78 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND  79 EC: 1.10.3.9;                                                        
COMPND  80 MOL_ID: 17;                                                          
COMPND  81 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  82 CHAIN: Y, y;                                                         
COMPND  83 EC: 1.10.3.9;                                                        
COMPND  84 MOL_ID: 18;                                                          
COMPND  85 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  86 CHAIN: X, x;                                                         
COMPND  87 EC: 1.10.3.9;                                                        
COMPND  88 MOL_ID: 19;                                                          
COMPND  89 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  90 CHAIN: Z, z;                                                         
COMPND  91 SYNONYM: PSII-Z;                                                     
COMPND  92 EC: 1.10.3.9;                                                        
COMPND  93 MOL_ID: 20;                                                          
COMPND  94 MOLECULE: PHOTOSYSTEM II PROTEIN Y;                                  
COMPND  95 CHAIN: R, r;                                                         
COMPND  96 EC: 1.10.3.9                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   7 ORGANISM_TAXID: 146786;                                              
SOURCE   8 MOL_ID: 3;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  10 ORGANISM_TAXID: 197221;                                              
SOURCE  11 STRAIN: BP-1;                                                        
SOURCE  12 MOL_ID: 4;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  14 ORGANISM_TAXID: 197221;                                              
SOURCE  15 STRAIN: BP-1;                                                        
SOURCE  16 MOL_ID: 5;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  18 ORGANISM_TAXID: 197221;                                              
SOURCE  19 STRAIN: BP-1;                                                        
SOURCE  20 MOL_ID: 6;                                                           
SOURCE  21 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  22 ORGANISM_TAXID: 197221;                                              
SOURCE  23 STRAIN: BP-1;                                                        
SOURCE  24 MOL_ID: 7;                                                           
SOURCE  25 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  26 ORGANISM_TAXID: 197221;                                              
SOURCE  27 STRAIN: BP-1;                                                        
SOURCE  28 MOL_ID: 8;                                                           
SOURCE  29 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  30 ORGANISM_TAXID: 197221;                                              
SOURCE  31 STRAIN: BP-1;                                                        
SOURCE  32 MOL_ID: 9;                                                           
SOURCE  33 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  34 ORGANISM_TAXID: 197221;                                              
SOURCE  35 STRAIN: BP-1;                                                        
SOURCE  36 MOL_ID: 10;                                                          
SOURCE  37 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  38 ORGANISM_TAXID: 197221;                                              
SOURCE  39 STRAIN: BP-1;                                                        
SOURCE  40 MOL_ID: 11;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  42 ORGANISM_TAXID: 197221;                                              
SOURCE  43 STRAIN: BP-1;                                                        
SOURCE  44 MOL_ID: 12;                                                          
SOURCE  45 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  46 ORGANISM_TAXID: 197221;                                              
SOURCE  47 STRAIN: BP-1;                                                        
SOURCE  48 MOL_ID: 13;                                                          
SOURCE  49 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  50 ORGANISM_TAXID: 197221;                                              
SOURCE  51 STRAIN: BP-1;                                                        
SOURCE  52 MOL_ID: 14;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  54 ORGANISM_TAXID: 197221;                                              
SOURCE  55 STRAIN: BP-1;                                                        
SOURCE  56 MOL_ID: 15;                                                          
SOURCE  57 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  58 ORGANISM_TAXID: 197221;                                              
SOURCE  59 STRAIN: BP-1;                                                        
SOURCE  60 MOL_ID: 16;                                                          
SOURCE  61 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  62 ORGANISM_TAXID: 197221;                                              
SOURCE  63 STRAIN: BP-1;                                                        
SOURCE  64 MOL_ID: 17;                                                          
SOURCE  65 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  66 ORGANISM_TAXID: 197221;                                              
SOURCE  67 STRAIN: BP-1;                                                        
SOURCE  68 MOL_ID: 18;                                                          
SOURCE  69 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  70 ORGANISM_TAXID: 197221;                                              
SOURCE  71 STRAIN: BP-1;                                                        
SOURCE  72 MOL_ID: 19;                                                          
SOURCE  73 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  74 ORGANISM_TAXID: 197221;                                              
SOURCE  75 STRAIN: BP-1;                                                        
SOURCE  76 MOL_ID: 20;                                                          
SOURCE  77 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  78 ORGANISM_TAXID: 197221;                                              
SOURCE  79 STRAIN: BP-1                                                         
KEYWDS    MEMBRANE PROTEIN, PHOTOSYSTEM II, C12E8, OXIDOREDUCTASE, ELECTRON     
KEYWDS   2 TRANSPORT                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.HELLMICH,M.BOMMER,A.BURKHARDT,M.IBRAHIM,J.KERN,A.MEENTS,F.MUEH,     
AUTHOR   2 H.DOBBEK,A.ZOUNI                                                     
REVDAT   3   24-DEC-14 4PJ0    1       JRNL                                     
REVDAT   2   19-NOV-14 4PJ0    1       DBREF1 SEQRES LINK   ATOM                
REVDAT   1   22-OCT-14 4PJ0    0                                                
JRNL        AUTH   J.HELLMICH,M.BOMMER,A.BURKHARDT,M.IBRAHIM,J.KERN,A.MEENTS,   
JRNL        AUTH 2 F.MUH,H.DOBBEK,A.ZOUNI                                       
JRNL        TITL   NATIVE-LIKE PHOTOSYSTEM II SUPERSTRUCTURE AT 2.44 ANGSTROM   
JRNL        TITL 2 RESOLUTION THROUGH DETERGENT EXTRACTION FROM THE PROTEIN     
JRNL        TITL 3 CRYSTAL.                                                     
JRNL        REF    STRUCTURE                     V.  22  1607 2014              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   25438669                                                     
JRNL        DOI    10.1016/J.STR.2014.09.007                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.44 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.9_1690)                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.44                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.360                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 282177                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.218                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.256                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 14110                           
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 49.1331 -  7.5640    1.00     9593   506  0.1807 0.1865        
REMARK   3     2  7.5640 -  6.0072    1.00     9307   489  0.1812 0.2145        
REMARK   3     3  6.0072 -  5.2488    1.00     9216   485  0.1902 0.2280        
REMARK   3     4  5.2488 -  4.7694    1.00     9156   482  0.1815 0.2073        
REMARK   3     5  4.7694 -  4.4278    1.00     9161   482  0.1931 0.2252        
REMARK   3     6  4.4278 -  4.1669    1.00     9121   481  0.1931 0.2129        
REMARK   3     7  4.1669 -  3.9583    1.00     9123   480  0.2016 0.2441        
REMARK   3     8  3.9583 -  3.7860    1.00     9092   478  0.2076 0.2603        
REMARK   3     9  3.7860 -  3.6403    1.00     9057   477  0.2158 0.2503        
REMARK   3    10  3.6403 -  3.5148    1.00     9092   478  0.2163 0.2460        
REMARK   3    11  3.5148 -  3.4049    1.00     9053   477  0.2190 0.2572        
REMARK   3    12  3.4049 -  3.3076    1.00     9081   478  0.2214 0.2780        
REMARK   3    13  3.3076 -  3.2205    1.00     9050   476  0.2276 0.2720        
REMARK   3    14  3.2205 -  3.1420    1.00     9014   475  0.2323 0.2648        
REMARK   3    15  3.1420 -  3.0705    1.00     9084   478  0.2337 0.2901        
REMARK   3    16  3.0705 -  3.0052    1.00     9036   475  0.2326 0.2790        
REMARK   3    17  3.0052 -  2.9451    1.00     9059   477  0.2359 0.2965        
REMARK   3    18  2.9451 -  2.8895    1.00     9015   475  0.2427 0.2953        
REMARK   3    19  2.8895 -  2.8379    1.00     8983   473  0.2440 0.3006        
REMARK   3    20  2.8379 -  2.7898    0.99     9001   474  0.2339 0.2935        
REMARK   3    21  2.7898 -  2.7448    0.99     8951   471  0.2439 0.3109        
REMARK   3    22  2.7448 -  2.7026    0.99     8908   469  0.2591 0.3498        
REMARK   3    23  2.7026 -  2.6629    0.99     8900   468  0.2608 0.3093        
REMARK   3    24  2.6629 -  2.6254    0.98     8861   466  0.2535 0.2886        
REMARK   3    25  2.6254 -  2.5899    0.97     8713   459  0.2641 0.3247        
REMARK   3    26  2.5899 -  2.5562    0.96     8652   456  0.2731 0.3190        
REMARK   3    27  2.5562 -  2.5243    0.95     8602   453  0.2752 0.3607        
REMARK   3    28  2.5243 -  2.4939    0.94     8487   446  0.2965 0.3459        
REMARK   3    29  2.4939 -  2.4649    0.93     8368   440  0.3107 0.3678        
REMARK   3    30  2.4649 -  2.4370    0.82     7331   386  0.3214 0.3832        
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)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.670           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 39.10                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007          51856                                  
REMARK   3   ANGLE     :  0.965          71128                                  
REMARK   3   CHIRALITY :  0.036           7144                                  
REMARK   3   PLANARITY :  0.004          10897                                  
REMARK   3   DIHEDRAL  : 13.236          21036                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 4PJ0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000201491.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : OTHER                              
REMARK 200  BEAMLINE                       : P11                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.196                              
REMARK 200  MONOCHROMATOR                  : SI-111 DOUBLE CRYSTAL              
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M-F               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 282213                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.440                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.120                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.4                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.44                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.69790                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.930                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: 3ARC                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: BATCH CRYSTALLISATION: 2 MM CHL A        
REMARK 280  EQUIVALENT OF PSIICC MIXED 1:1 WITH: 0.1 M TRIS (PH 7.5), 0.1 M     
REMARK 280  (NH4)2SO4, 15 - 18 % PEG 5000 MME, POST-CRYSTALLISATION             
REMARK 280  DEHYDRATION                                                         
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       58.22350            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      151.10100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      109.44450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      151.10100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.22350            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      109.44450            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: 40-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 40-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 276330 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 177440 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1842.0 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, O, T, U, V, Y, X, Z,            
REMARK 350                    AND CHAINS: a, b, c, d, e, f, h, i, j, k,         
REMARK 350                    AND CHAINS: l, m, o, t, u, v, x, R, r,            
REMARK 350                    AND CHAINS: y, z                                  
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     THR A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LYS B   507                                                      
REMARK 465     GLU B   508                                                      
REMARK 465     ALA B   509                                                      
REMARK 465     VAL B   510                                                      
REMARK 465     MET C    13                                                      
REMARK 465     VAL C    14                                                      
REMARK 465     THR C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     THR C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ILE D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     ILE D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     PRO D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     ARG D    12                                                      
REMARK 465     MET E     1                                                      
REMARK 465     LYS E    84                                                      
REMARK 465     MET F     1                                                      
REMARK 465     THR F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     ASN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     PRO F     6                                                      
REMARK 465     ASN F     7                                                      
REMARK 465     GLN F     8                                                      
REMARK 465     GLU F     9                                                      
REMARK 465     PRO F    10                                                      
REMARK 465     VAL F    11                                                      
REMARK 465     SER F    12                                                      
REMARK 465     MET H     1                                                      
REMARK 465     LEU H    65                                                      
REMARK 465     GLY H    66                                                      
REMARK 465     ARG I    34                                                      
REMARK 465     LYS I    35                                                      
REMARK 465     ASP I    36                                                      
REMARK 465     LEU I    37                                                      
REMARK 465     GLU I    38                                                      
REMARK 465     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     GLU J     4                                                      
REMARK 465     GLY J     5                                                      
REMARK 465     GLY J     6                                                      
REMARK 465     MET K     1                                                      
REMARK 465     ILE K     2                                                      
REMARK 465     ASP K     3                                                      
REMARK 465     ALA K     4                                                      
REMARK 465     LEU K     5                                                      
REMARK 465     VAL K     6                                                      
REMARK 465     LEU K     7                                                      
REMARK 465     VAL K     8                                                      
REMARK 465     ALA K     9                                                      
REMARK 465     LYS K    10                                                      
REMARK 465     MET L     1                                                      
REMARK 465     GLN M    33                                                      
REMARK 465     LYS M    34                                                      
REMARK 465     SER M    35                                                      
REMARK 465     SER M    36                                                      
REMARK 465     MET O   -25                                                      
REMARK 465     LYS O   -24                                                      
REMARK 465     TYR O   -23                                                      
REMARK 465     ARG O   -22                                                      
REMARK 465     ILE O   -21                                                      
REMARK 465     LEU O   -20                                                      
REMARK 465     MET O   -19                                                      
REMARK 465     ALA O   -18                                                      
REMARK 465     THR O   -17                                                      
REMARK 465     LEU O   -16                                                      
REMARK 465     LEU O   -15                                                      
REMARK 465     ALA O   -14                                                      
REMARK 465     VAL O   -13                                                      
REMARK 465     CYS O   -12                                                      
REMARK 465     LEU O   -11                                                      
REMARK 465     GLY O   -10                                                      
REMARK 465     ILE O    -9                                                      
REMARK 465     PHE O    -8                                                      
REMARK 465     SER O    -7                                                      
REMARK 465     LEU O    -6                                                      
REMARK 465     SER O    -5                                                      
REMARK 465     ALA O    -4                                                      
REMARK 465     PRO O    -3                                                      
REMARK 465     ALA O    -2                                                      
REMARK 465     PHE O    -1                                                      
REMARK 465     ALA O     0                                                      
REMARK 465     ALA O     1                                                      
REMARK 465     LYS O     2                                                      
REMARK 465     GLN O     3                                                      
REMARK 465     ALA O   246                                                      
REMARK 465     THR T    30                                                      
REMARK 465     LYS T    31                                                      
REMARK 465     LYS T    32                                                      
REMARK 465     MET U   -29                                                      
REMARK 465     GLN U   -28                                                      
REMARK 465     ARG U   -27                                                      
REMARK 465     LEU U   -26                                                      
REMARK 465     GLY U   -25                                                      
REMARK 465     ARG U   -24                                                      
REMARK 465     TRP U   -23                                                      
REMARK 465     LEU U   -22                                                      
REMARK 465     ALA U   -21                                                      
REMARK 465     LEU U   -20                                                      
REMARK 465     ALA U   -19                                                      
REMARK 465     TYR U   -18                                                      
REMARK 465     PHE U   -17                                                      
REMARK 465     VAL U   -16                                                      
REMARK 465     GLY U   -15                                                      
REMARK 465     VAL U   -14                                                      
REMARK 465     SER U   -13                                                      
REMARK 465     LEU U   -12                                                      
REMARK 465     LEU U   -11                                                      
REMARK 465     GLY U   -10                                                      
REMARK 465     TRP U    -9                                                      
REMARK 465     ILE U    -8                                                      
REMARK 465     ASN U    -7                                                      
REMARK 465     TRP U    -6                                                      
REMARK 465     SER U    -5                                                      
REMARK 465     ALA U    -4                                                      
REMARK 465     PRO U    -3                                                      
REMARK 465     THR U    -2                                                      
REMARK 465     LEU U    -1                                                      
REMARK 465     ALA U     0                                                      
REMARK 465     ALA U     1                                                      
REMARK 465     THR U     2                                                      
REMARK 465     ALA U     3                                                      
REMARK 465     SER U     4                                                      
REMARK 465     THR U     5                                                      
REMARK 465     GLU U     6                                                      
REMARK 465     GLU U     7                                                      
REMARK 465     GLU U     8                                                      
REMARK 465     MET V   -25                                                      
REMARK 465     LEU V   -24                                                      
REMARK 465     LYS V   -23                                                      
REMARK 465     LYS V   -22                                                      
REMARK 465     CYS V   -21                                                      
REMARK 465     VAL V   -20                                                      
REMARK 465     TRP V   -19                                                      
REMARK 465     LEU V   -18                                                      
REMARK 465     ALA V   -17                                                      
REMARK 465     VAL V   -16                                                      
REMARK 465     ALA V   -15                                                      
REMARK 465     LEU V   -14                                                      
REMARK 465     CYS V   -13                                                      
REMARK 465     LEU V   -12                                                      
REMARK 465     CYS V   -11                                                      
REMARK 465     LEU V   -10                                                      
REMARK 465     TRP V    -9                                                      
REMARK 465     GLN V    -8                                                      
REMARK 465     PHE V    -7                                                      
REMARK 465     THR V    -6                                                      
REMARK 465     MET V    -5                                                      
REMARK 465     GLY V    -4                                                      
REMARK 465     THR V    -3                                                      
REMARK 465     ALA V    -2                                                      
REMARK 465     LEU V    -1                                                      
REMARK 465     ALA V     0                                                      
REMARK 465     MET Y     1                                                      
REMARK 465     GLY Y     2                                                      
REMARK 465     ILE Y     3                                                      
REMARK 465     PHE Y     4                                                      
REMARK 465     ASN Y     5                                                      
REMARK 465     GLY Y     6                                                      
REMARK 465     ILE Y     7                                                      
REMARK 465     ILE Y     8                                                      
REMARK 465     GLU Y     9                                                      
REMARK 465     PHE Y    10                                                      
REMARK 465     LEU Y    11                                                      
REMARK 465     SER Y    12                                                      
REMARK 465     ASN Y    13                                                      
REMARK 465     ILE Y    14                                                      
REMARK 465     ASN Y    15                                                      
REMARK 465     PHE Y    16                                                      
REMARK 465     GLU Y    17                                                      
REMARK 465     MET X     1                                                      
REMARK 465     ARG X    39                                                      
REMARK 465     SER X    40                                                      
REMARK 465     LEU X    41                                                      
REMARK 465     MET a     1                                                      
REMARK 465     THR a     2                                                      
REMARK 465     THR a     3                                                      
REMARK 465     THR a     4                                                      
REMARK 465     LEU a     5                                                      
REMARK 465     GLN a     6                                                      
REMARK 465     ARG a     7                                                      
REMARK 465     ARG a     8                                                      
REMARK 465     GLU a     9                                                      
REMARK 465     SER a    10                                                      
REMARK 465     ALA a    11                                                      
REMARK 465     MET b     1                                                      
REMARK 465     ARG b   505                                                      
REMARK 465     ARG b   506                                                      
REMARK 465     LYS b   507                                                      
REMARK 465     GLU b   508                                                      
REMARK 465     ALA b   509                                                      
REMARK 465     VAL b   510                                                      
REMARK 465     MET c    13                                                      
REMARK 465     VAL c    14                                                      
REMARK 465     THR c    15                                                      
REMARK 465     LEU c    16                                                      
REMARK 465     SER c    17                                                      
REMARK 465     SER c    18                                                      
REMARK 465     ASN c    19                                                      
REMARK 465     SER c    20                                                      
REMARK 465     ILE c    21                                                      
REMARK 465     PHE c    22                                                      
REMARK 465     ALA c    23                                                      
REMARK 465     THR c    24                                                      
REMARK 465     ASN c    25                                                      
REMARK 465     MET d     1                                                      
REMARK 465     THR d     2                                                      
REMARK 465     ILE d     3                                                      
REMARK 465     ALA d     4                                                      
REMARK 465     ILE d     5                                                      
REMARK 465     GLY d     6                                                      
REMARK 465     ARG d     7                                                      
REMARK 465     ALA d     8                                                      
REMARK 465     PRO d     9                                                      
REMARK 465     ALA d    10                                                      
REMARK 465     GLU d    11                                                      
REMARK 465     ARG d    12                                                      
REMARK 465     MET e     1                                                      
REMARK 465     ALA e     2                                                      
REMARK 465     GLY e     3                                                      
REMARK 465     THR e     4                                                      
REMARK 465     LYS e    84                                                      
REMARK 465     MET f     1                                                      
REMARK 465     THR f     2                                                      
REMARK 465     SER f     3                                                      
REMARK 465     ASN f     4                                                      
REMARK 465     THR f     5                                                      
REMARK 465     PRO f     6                                                      
REMARK 465     ASN f     7                                                      
REMARK 465     GLN f     8                                                      
REMARK 465     GLU f     9                                                      
REMARK 465     PRO f    10                                                      
REMARK 465     VAL f    11                                                      
REMARK 465     SER f    12                                                      
REMARK 465     MET h     1                                                      
REMARK 465     LEU h    65                                                      
REMARK 465     GLY h    66                                                      
REMARK 465     ASP i    36                                                      
REMARK 465     LEU i    37                                                      
REMARK 465     GLU i    38                                                      
REMARK 465     MET j     1                                                      
REMARK 465     MET j     2                                                      
REMARK 465     SER j     3                                                      
REMARK 465     GLU j     4                                                      
REMARK 465     GLY j     5                                                      
REMARK 465     GLY j     6                                                      
REMARK 465     ARG j     7                                                      
REMARK 465     MET k     1                                                      
REMARK 465     ILE k     2                                                      
REMARK 465     ASP k     3                                                      
REMARK 465     ALA k     4                                                      
REMARK 465     LEU k     5                                                      
REMARK 465     VAL k     6                                                      
REMARK 465     LEU k     7                                                      
REMARK 465     VAL k     8                                                      
REMARK 465     ALA k     9                                                      
REMARK 465     LYS k    10                                                      
REMARK 465     MET l     1                                                      
REMARK 465     GLN m    33                                                      
REMARK 465     LYS m    34                                                      
REMARK 465     SER m    35                                                      
REMARK 465     SER m    36                                                      
REMARK 465     MET o   -25                                                      
REMARK 465     LYS o   -24                                                      
REMARK 465     TYR o   -23                                                      
REMARK 465     ARG o   -22                                                      
REMARK 465     ILE o   -21                                                      
REMARK 465     LEU o   -20                                                      
REMARK 465     MET o   -19                                                      
REMARK 465     ALA o   -18                                                      
REMARK 465     THR o   -17                                                      
REMARK 465     LEU o   -16                                                      
REMARK 465     LEU o   -15                                                      
REMARK 465     ALA o   -14                                                      
REMARK 465     VAL o   -13                                                      
REMARK 465     CYS o   -12                                                      
REMARK 465     LEU o   -11                                                      
REMARK 465     GLY o   -10                                                      
REMARK 465     ILE o    -9                                                      
REMARK 465     PHE o    -8                                                      
REMARK 465     SER o    -7                                                      
REMARK 465     LEU o    -6                                                      
REMARK 465     SER o    -5                                                      
REMARK 465     ALA o    -4                                                      
REMARK 465     PRO o    -3                                                      
REMARK 465     ALA o    -2                                                      
REMARK 465     PHE o    -1                                                      
REMARK 465     ALA o     0                                                      
REMARK 465     ALA o     1                                                      
REMARK 465     LYS o     2                                                      
REMARK 465     GLN o     3                                                      
REMARK 465     THR t    30                                                      
REMARK 465     LYS t    31                                                      
REMARK 465     LYS t    32                                                      
REMARK 465     MET u   -29                                                      
REMARK 465     GLN u   -28                                                      
REMARK 465     ARG u   -27                                                      
REMARK 465     LEU u   -26                                                      
REMARK 465     GLY u   -25                                                      
REMARK 465     ARG u   -24                                                      
REMARK 465     TRP u   -23                                                      
REMARK 465     LEU u   -22                                                      
REMARK 465     ALA u   -21                                                      
REMARK 465     LEU u   -20                                                      
REMARK 465     ALA u   -19                                                      
REMARK 465     TYR u   -18                                                      
REMARK 465     PHE u   -17                                                      
REMARK 465     VAL u   -16                                                      
REMARK 465     GLY u   -15                                                      
REMARK 465     VAL u   -14                                                      
REMARK 465     SER u   -13                                                      
REMARK 465     LEU u   -12                                                      
REMARK 465     LEU u   -11                                                      
REMARK 465     GLY u   -10                                                      
REMARK 465     TRP u    -9                                                      
REMARK 465     ILE u    -8                                                      
REMARK 465     ASN u    -7                                                      
REMARK 465     TRP u    -6                                                      
REMARK 465     SER u    -5                                                      
REMARK 465     ALA u    -4                                                      
REMARK 465     PRO u    -3                                                      
REMARK 465     THR u    -2                                                      
REMARK 465     LEU u    -1                                                      
REMARK 465     ALA u     0                                                      
REMARK 465     ALA u     1                                                      
REMARK 465     THR u     2                                                      
REMARK 465     ALA u     3                                                      
REMARK 465     SER u     4                                                      
REMARK 465     THR u     5                                                      
REMARK 465     GLU u     6                                                      
REMARK 465     GLU u     7                                                      
REMARK 465     GLU u     8                                                      
REMARK 465     MET v   -25                                                      
REMARK 465     LEU v   -24                                                      
REMARK 465     LYS v   -23                                                      
REMARK 465     LYS v   -22                                                      
REMARK 465     CYS v   -21                                                      
REMARK 465     VAL v   -20                                                      
REMARK 465     TRP v   -19                                                      
REMARK 465     LEU v   -18                                                      
REMARK 465     ALA v   -17                                                      
REMARK 465     VAL v   -16                                                      
REMARK 465     ALA v   -15                                                      
REMARK 465     LEU v   -14                                                      
REMARK 465     CYS v   -13                                                      
REMARK 465     LEU v   -12                                                      
REMARK 465     CYS v   -11                                                      
REMARK 465     LEU v   -10                                                      
REMARK 465     TRP v    -9                                                      
REMARK 465     GLN v    -8                                                      
REMARK 465     PHE v    -7                                                      
REMARK 465     THR v    -6                                                      
REMARK 465     MET v    -5                                                      
REMARK 465     GLY v    -4                                                      
REMARK 465     THR v    -3                                                      
REMARK 465     ALA v    -2                                                      
REMARK 465     LEU v    -1                                                      
REMARK 465     ALA v     0                                                      
REMARK 465     MET x     1                                                      
REMARK 465     SER x    40                                                      
REMARK 465     LEU x    41                                                      
REMARK 465     MET R     1                                                      
REMARK 465     GLN R    36                                                      
REMARK 465     LYS R    37                                                      
REMARK 465     ALA R    38                                                      
REMARK 465     LYS R    39                                                      
REMARK 465     ALA R    40                                                      
REMARK 465     ALA R    41                                                      
REMARK 465     MET r     1                                                      
REMARK 465     ASP r     2                                                      
REMARK 465     GLN r    36                                                      
REMARK 465     LYS r    37                                                      
REMARK 465     ALA r    38                                                      
REMARK 465     LYS r    39                                                      
REMARK 465     ALA r    40                                                      
REMARK 465     ALA r    41                                                      
REMARK 465     MET y     1                                                      
REMARK 465     GLY y     2                                                      
REMARK 465     ILE y     3                                                      
REMARK 465     PHE y     4                                                      
REMARK 465     ASN y     5                                                      
REMARK 465     GLY y     6                                                      
REMARK 465     ILE y     7                                                      
REMARK 465     ILE y     8                                                      
REMARK 465     GLU y     9                                                      
REMARK 465     PHE y    10                                                      
REMARK 465     LEU y    11                                                      
REMARK 465     SER y    12                                                      
REMARK 465     ASN y    13                                                      
REMARK 465     ILE y    14                                                      
REMARK 465     ASN y    15                                                      
REMARK 465     PHE y    16                                                      
REMARK 465     GLU y    17                                                      
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   OG   SER z    29     OD2  ASP z    32              2.15            
REMARK 500   OH   TYR d   141     O4   LHG a   615              2.16            
REMARK 500   OD2  ASP u    26     OG1  THR u    85              2.17            
REMARK 500   OH   TYR D   141     O4   LHG A   613              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    VAL A  30      -77.61    -88.87                                   
REMARK 500    LEU A 159      -53.62   -123.85                                   
REMARK 500    THR A 228     -166.06   -101.40                                   
REMARK 500    ILE A 259     -102.14   -114.66                                   
REMARK 500    THR A 316     -167.02   -120.66                                   
REMARK 500    PHE B 162       72.67   -152.10                                   
REMARK 500    ASP B 313       49.84    -86.71                                   
REMARK 500    PHE B 383      -70.14    -77.38                                   
REMARK 500    TYR C 143      -62.17   -102.15                                   
REMARK 500    PHE C 182       66.37   -117.31                                   
REMARK 500    TRP C 223     -136.86     54.74                                   
REMARK 500    THR C 295      -60.42   -101.36                                   
REMARK 500    TYR C 297       73.91   -118.23                                   
REMARK 500    THR C 355        1.63    -69.83                                   
REMARK 500    PHE C 358       30.47    -99.85                                   
REMARK 500    PRO C 400       63.83    -67.93                                   
REMARK 500    SER C 416      -55.34   -165.80                                   
REMARK 500    PHE C 455       33.74   -155.07                                   
REMARK 500    SER C 463       49.71   -158.14                                   
REMARK 500    VAL D  30      -69.48   -108.96                                   
REMARK 500    SER D  57       24.17   -142.20                                   
REMARK 500    SER D  65       27.01   -154.00                                   
REMARK 500    PRO D 140       36.46    -88.89                                   
REMARK 500    ALA D 234       34.60    -89.28                                   
REMARK 500    SER D 295       56.34    -92.13                                   
REMARK 500    ALA D 351      -62.51     61.31                                   
REMARK 500    GLU E  59       56.23   -141.72                                   
REMARK 500    SER I  25       55.80    -90.70                                   
REMARK 500    PHE K  45       78.74     49.61                                   
REMARK 500    ALA O  26       63.67   -112.83                                   
REMARK 500    LYS O  57      -93.13    -54.75                                   
REMARK 500    ASN O  58       13.76   -151.77                                   
REMARK 500    ARG O  73     -161.02     60.38                                   
REMARK 500    GLU O  98      -60.17   -125.45                                   
REMARK 500    VAL O 122       33.31   -142.24                                   
REMARK 500    ASN O 132       75.13     56.18                                   
REMARK 500    LEU O 164      -68.38    -94.39                                   
REMARK 500    LEU O 174       77.13   -118.99                                   
REMARK 500    SER O 221     -156.56    -88.59                                   
REMARK 500    THR U  19     -162.21   -102.91                                   
REMARK 500    ASN U  29      -36.28   -142.59                                   
REMARK 500    TYR U 103      -99.48   -118.97                                   
REMARK 500    ASN V  13     -150.74   -118.53                                   
REMARK 500    CYS V  37      -37.58   -131.21                                   
REMARK 500    ASN V  49       78.68   -166.67                                   
REMARK 500    ASP V  67       30.63    -90.97                                   
REMARK 500    ASP X  35       73.88   -103.97                                   
REMARK 500    PRO Z  30     -113.04    -64.26                                   
REMARK 500    VAL Z  61      -16.39   -146.80                                   
REMARK 500    VAL a  30      -82.70    -84.87                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     100 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO B  222     GLN B  223                 -149.53                    
REMARK 500 GLN z   31     ASP z   32                  141.76                    
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     LMG A  603                                                       
REMARK 610     LMG A  612                                                       
REMARK 610     LMG B  620                                                       
REMARK 610     LMG B  624                                                       
REMARK 610     DGD C  516                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     LMG C  519                                                       
REMARK 610     LMG C  521                                                       
REMARK 610     LMG D  409                                                       
REMARK 610     LHG E  101                                                       
REMARK 610     SQD F  101                                                       
REMARK 610     DGD H  102                                                       
REMARK 610     LMG a  603                                                       
REMARK 610     LMG a  614                                                       
REMARK 610     LHG a  616                                                       
REMARK 610     LMG b  620                                                       
REMARK 610     LMG b  624                                                       
REMARK 610     DGD c  515                                                       
REMARK 610     DGD c  516                                                       
REMARK 610     DGD c  517                                                       
REMARK 610     LMG c  518                                                       
REMARK 610     LMG c  520                                                       
REMARK 610     LMG d  408                                                       
REMARK 610     SQD f  101                                                       
REMARK 610     DGD h  102                                                       
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                             OEX A 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 601   O5  101.3                                              
REMARK 620 3 OEX A 601   O4   91.5  92.5                                        
REMARK 620 4 GLU A 333   OE2 164.6  91.6  96.4                                  
REMARK 620 5 HOH A 728   O    85.9 100.2 167.4  83.4                            
REMARK 620 6 HOH A 729   O    77.6 171.7  95.8  88.5  71.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 OEX A 601   O1  162.2                                              
REMARK 620 3 OEX A 601   O2   91.4  75.2                                        
REMARK 620 4 OEX A 601   O5  111.9  76.8  76.7                                  
REMARK 620 5 ALA A 344   O    75.9  86.9  58.3 134.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEX A 601   O1   95.9                                              
REMARK 620 3 OEX A 601   O5   96.0  82.4                                        
REMARK 620 4 OEX A 601   O3  171.5  91.9  81.6                                  
REMARK 620 5 HIS A 332   NE2  88.1 175.0 100.3  84.3                            
REMARK 620 6 ASP A 342   OD2  95.3  88.0 165.8  88.4  88.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  94.2                                              
REMARK 620 3 HIS D 214   NE2 107.9  92.7                                        
REMARK 620 4 HIS D 268   NE2  84.5 174.4  93.0                                  
REMARK 620 5 BCT A 616   O1  158.6  94.5  91.2  84.9                            
REMARK 620 6 BCT A 616   O2   98.8  82.8 153.2  91.9  63.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEX A 601   O2  170.3                                              
REMARK 620 3 OEX A 601   O3   96.0  93.1                                        
REMARK 620 4 OEX A 601   O4   87.7  83.3 175.8                                  
REMARK 620 5 OEX A 601   O5   92.2  92.3  81.5  96.6                            
REMARK 620 6 GLU C 354   OE2  91.5  85.8  86.9  94.9 168.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 OEX A 601   O1   96.5                                              
REMARK 620 3 OEX A 601   O2  174.3  89.0                                        
REMARK 620 4 OEX A 601   O3   92.5  78.9  86.8                                  
REMARK 620 5 ALA A 344   OXT  90.7  80.3  92.0 159.2                            
REMARK 620 6 GLU C 354   OE1  94.7 168.8  79.9 101.2  99.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 511   NA  110.6                                              
REMARK 620 3 CLA C 511   NB  101.9  89.6                                        
REMARK 620 4 CLA C 511   NC   80.4 168.5  91.5                                  
REMARK 620 5 CLA C 511   ND   89.1  93.8 166.5  82.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 102  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM E 102   NA  101.0                                              
REMARK 620 3 HEM E 102   NB   97.5  90.3                                        
REMARK 620 4 HEM E 102   NC   83.4 174.5  92.5                                  
REMARK 620 5 HEM E 102   ND   87.2  87.4 175.0  89.4                            
REMARK 620 6 HIS F  24   NE2 176.9  76.7  84.6  98.8  90.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM V 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  41   NE2                                                    
REMARK 620 2 HEM V 201   NA   96.4                                              
REMARK 620 3 HEM V 201   NB   94.9  90.2                                        
REMARK 620 4 HEM V 201   NC   88.1 174.4  92.6                                  
REMARK 620 5 HEM V 201   ND   89.7  87.0 174.9  89.8                            
REMARK 620 6 HIS V  92   NE2 174.8  88.0  87.7  87.3  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 601   O5  110.4                                              
REMARK 620 3 OEX a 601   O4   90.1  96.4                                        
REMARK 620 4 GLU a 333   OE2 170.4  77.2  95.0                                  
REMARK 620 5 HOH a 721   O   105.4  85.0 162.9  68.7                            
REMARK 620 6 HOH a 722   O    89.3 158.7  91.2  82.4  82.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 601   O1  158.7                                              
REMARK 620 3 OEX a 601   O2   84.9  75.8                                        
REMARK 620 4 OEX a 601   O5  107.9  76.8  77.1                                  
REMARK 620 5 ALA a 344   O    76.8  84.7  55.4 132.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 601   O1   90.9                                              
REMARK 620 3 OEX a 601   O5  100.9  92.9                                        
REMARK 620 4 OEX a 601   O3  173.2  95.5  76.6                                  
REMARK 620 5 HIS a 332   NE2  85.0 171.4  95.3  88.9                            
REMARK 620 6 ASP a 342   OD2  87.4  85.4 171.5  95.3  86.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE a 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  88.6                                              
REMARK 620 3 HIS d 214   NE2 102.6  89.7                                        
REMARK 620 4 HIS d 268   NE2  88.2 175.2  94.5                                  
REMARK 620 5 BCT a 618   O1  163.2  95.4  93.8  86.7                            
REMARK 620 6 BCT a 618   O2  102.4  88.0 154.9  89.2  61.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 601   O2  174.5                                              
REMARK 620 3 OEX a 601   O3   88.4  91.0                                        
REMARK 620 4 OEX a 601   O4   94.2  86.7 176.3                                  
REMARK 620 5 OEX a 601   O5   87.4  97.8  78.7  98.8                            
REMARK 620 6 GLU c 354   OE2  90.6  83.8  81.4 101.2 160.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 OEX a 601   O1   91.6                                              
REMARK 620 3 OEX a 601   O2  174.8  93.5                                        
REMARK 620 4 OEX a 601   O3   97.1  80.3  84.7                                  
REMARK 620 5 ALA a 344   OXT  83.7  85.2  95.8 165.5                            
REMARK 620 6 GLU c 354   OE1  85.1 176.1  89.8  98.0  96.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 511   NA  102.7                                              
REMARK 620 3 CLA c 511   NB  103.2  89.7                                        
REMARK 620 4 CLA c 511   NC   88.5 168.1  91.5                                  
REMARK 620 5 CLA c 511   ND   88.5  93.8 166.8  82.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM e 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM e 101   NA   98.3                                              
REMARK 620 3 HEM e 101   NB  105.8  90.5                                        
REMARK 620 4 HEM e 101   NC   85.4 174.3  92.6                                  
REMARK 620 5 HEM e 101   ND   79.0  87.3 175.0  89.2                            
REMARK 620 6 HIS f  24   NE2 172.8  78.2  80.6  97.6  94.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM v 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v  41   NE2                                                    
REMARK 620 2 HEM v 201   NA   92.5                                              
REMARK 620 3 HEM v 201   NB   93.5  90.2                                        
REMARK 620 4 HEM v 201   NC   90.8 174.9  93.5                                  
REMARK 620 5 HEM v 201   ND   89.7  86.4 175.4  89.7                            
REMARK 620 6 HIS v  92   NE2 171.4  81.1  92.2  95.2  84.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 607  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 738   O                                                      
REMARK 620 2 CLA B 607   NA   91.3                                              
REMARK 620 3 CLA B 607   NB  106.3  88.6                                        
REMARK 620 4 CLA B 607   NC  100.1 167.9  91.9                                  
REMARK 620 5 CLA B 607   ND   89.3  93.6 164.2  82.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA D 403  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 501   O                                                      
REMARK 620 2 CLA D 403   NA   93.9                                              
REMARK 620 3 CLA D 403   NB  105.3  88.8                                        
REMARK 620 4 CLA D 403   NC   96.6 168.8  92.3                                  
REMARK 620 5 CLA D 403   ND   88.7  93.6 165.7  82.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a 607  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH a 705   O                                                      
REMARK 620 2 CLA a 607   NA   85.6                                              
REMARK 620 3 CLA a 607   NB  101.1  88.6                                        
REMARK 620 4 CLA a 607   NC  104.6 169.4  92.4                                  
REMARK 620 5 CLA a 607   ND   93.3  93.6 165.5  82.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 607  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 701   O                                                      
REMARK 620 2 CLA b 607   NA   99.7                                              
REMARK 620 3 CLA b 607   NB  102.8  88.7                                        
REMARK 620 4 CLA b 607   NC   92.0 167.8  92.0                                  
REMARK 620 5 CLA b 607   ND   92.6  93.4 163.9  82.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 610  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 719   O                                                      
REMARK 620 2 CLA b 610   NA   93.8                                              
REMARK 620 3 CLA b 610   NB   97.6  89.2                                        
REMARK 620 4 CLA b 610   NC   96.4 169.5  92.0                                  
REMARK 620 5 CLA b 610   ND   98.1  93.5 163.9  82.5                            
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 OEX A 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE A 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG A 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD F 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 O 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 O 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 U 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 V 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE a 602                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 605                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 a 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 d 410                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 o 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 u 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 u 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR z 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v    
REMARK 800  40                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AU1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v    
REMARK 800  37                                                                  
DBREF  4PJ0 A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  4PJ0 B    1   510  UNP    Q9F1M3   Q9F1M3_9CHRO     1    510             
DBREF  4PJ0 C   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4PJ0 D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4PJ0 E    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  4PJ0 F    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  4PJ0 H    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  4PJ0 I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4PJ0 J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4PJ0 K    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  4PJ0 L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4PJ0 M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4PJ0 O  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  4PJ0 T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4PJ0 U  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  4PJ0 V  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  4PJ0 Y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4PJ0 X    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  4PJ0 Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  4PJ0 a    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  4PJ0 b    1   510  UNP    Q9F1M3   Q9F1M3_9CHRO     1    510             
DBREF  4PJ0 c   13   473  UNP    Q8DIF8   Q8DIF8_THEEB     1    461             
DBREF  4PJ0 d    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  4PJ0 e    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  4PJ0 f    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  4PJ0 h    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  4PJ0 i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  4PJ0 j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  4PJ0 k    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  4PJ0 l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  4PJ0 m    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  4PJ0 o  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  4PJ0 t    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  4PJ0 u  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  4PJ0 v  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  4PJ0 x    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  4PJ0 R    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
DBREF  4PJ0 r    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
DBREF  4PJ0 y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  4PJ0 z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQRES   1 A  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 A  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 A  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 A  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 A  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 A  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 A  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 A  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 A  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 A  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 A  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 A  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 A  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 A  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 A  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 A  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 A  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 A  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 A  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 A  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 A  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 A  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 A  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 A  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 A  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 A  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 A  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 B  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 B  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 B  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 B  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 B  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 B  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 B  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 B  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 B  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 B  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 B  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 B  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 B  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 B  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 B  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 B  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 B  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 B  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 B  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 B  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 B  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 B  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 B  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 B  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 B  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 B  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 B  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 B  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 B  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 B  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 B  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 B  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 B  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 B  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 B  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 B  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 B  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 B  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 B  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 B  510  GLU ALA VAL                                                  
SEQRES   1 C  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 C  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 C  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 C  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 C  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 C  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 C  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 C  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 C  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 C  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 C  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 C  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 C  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 C  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 C  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 C  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 C  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 C  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 C  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 C  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 C  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 C  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 C  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 C  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 C  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 C  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 C  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 C  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 C  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 C  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 C  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 C  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 C  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 C  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 C  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 C  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 D  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 D  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 D  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 D  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 D  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 D  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 D  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 D  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 D  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 D  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 D  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 D  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 D  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 D  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 D  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 D  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 D  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 D  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 D  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 D  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 D  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 D  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 D  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 D  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 D  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 D  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 D  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 D  352  LEU                                                          
SEQRES   1 E   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 E   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 E   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 E   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 E   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 E   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 E   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 F   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 F   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 F   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 F   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 H   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 H   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 H   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 H   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 H   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 H   66  GLY                                                          
SEQRES   1 I   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 I   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 I   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 J   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 J   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 J   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 J   40  LEU                                                          
SEQRES   1 K   46  MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU          
SEQRES   2 K   46  ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO          
SEQRES   3 K   46  VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP          
SEQRES   4 K   46  GLN ALA ALA VAL GLY PHE ARG                                  
SEQRES   1 L   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 L   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 L   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 M   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 O  272  MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL          
SEQRES   2 O  272  CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA          
SEQRES   3 O  272  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   4 O  272  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   5 O  272  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   6 O  272  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   7 O  272  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   8 O  272  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   9 O  272  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES  10 O  272  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES  11 O  272  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  12 O  272  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  13 O  272  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  14 O  272  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  15 O  272  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  16 O  272  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  17 O  272  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  18 O  272  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  19 O  272  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  20 O  272  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  21 O  272  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 T   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 U  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 U  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 U  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 U  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 U  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 U  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 U  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 U  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 U  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 U  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 U  134  GLY LEU TYR LYS                                              
SEQRES   1 V  163  MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS          
SEQRES   2 V  163  LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA          
SEQRES   3 V  163  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   4 V  163  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   5 V  163  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   6 V  163  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   7 V  163  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   8 V  163  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   9 V  163  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES  10 V  163  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES  11 V  163  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  12 V  163  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  13 V  163  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 Y   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 Y   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 Y   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 Y   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 X   41  MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY          
SEQRES   2 X   41  LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA          
SEQRES   3 X   41  VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG          
SEQRES   4 X   41  SER LEU                                                      
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 a  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 a  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 a  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 a  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 a  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 a  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 a  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 a  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 a  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 a  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 a  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 a  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 a  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 a  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 a  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 a  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 a  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 a  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 a  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 a  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 a  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 a  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 a  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 a  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 a  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 a  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 a  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 b  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 b  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 b  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 b  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 b  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 b  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 b  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 b  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 b  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 b  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 b  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 b  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 b  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 b  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 b  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 b  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 b  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 b  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 b  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 b  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 b  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 b  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 b  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 b  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 b  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 b  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 b  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 b  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 b  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 b  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 b  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 b  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 b  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 b  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 b  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 b  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 b  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 b  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 b  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 b  510  GLU ALA VAL                                                  
SEQRES   1 c  461  MET VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN          
SEQRES   2 c  461  ARG ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY          
SEQRES   3 c  461  ASN ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY          
SEQRES   4 c  461  ALA HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA          
SEQRES   5 c  461  GLY ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO          
SEQRES   6 c  461  GLU LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO          
SEQRES   7 c  461  HIS ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY          
SEQRES   8 c  461  GLU VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL          
SEQRES   9 c  461  VAL HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY          
SEQRES  10 c  461  VAL TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU          
SEQRES  11 c  461  TYR SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN          
SEQRES  12 c  461  LYS MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU          
SEQRES  13 c  461  GLY ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE          
SEQRES  14 c  461  PHE GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY          
SEQRES  15 c  461  ASP VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG          
SEQRES  16 c  461  VAL ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY          
SEQRES  17 c  461  GLU GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL          
SEQRES  18 c  461  VAL GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA          
SEQRES  19 c  461  GLY GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP          
SEQRES  20 c  461  ALA ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU          
SEQRES  21 c  461  SER TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE          
SEQRES  22 c  461  ALA THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO          
SEQRES  23 c  461  SER GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN          
SEQRES  24 c  461  ALA GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU          
SEQRES  25 c  461  GLY ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU          
SEQRES  26 c  461  GLY LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE          
SEQRES  27 c  461  PHE GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY          
SEQRES  28 c  461  PRO TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP          
SEQRES  29 c  461  LEU ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU          
SEQRES  30 c  461  ARG ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY          
SEQRES  31 c  461  SER LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN          
SEQRES  32 c  461  SER VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR          
SEQRES  33 c  461  SER HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS          
SEQRES  34 c  461  LEU TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY          
SEQRES  35 c  461  PHE GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU          
SEQRES  36 c  461  SER MET PRO SER LEU ASP                                      
SEQRES   1 d  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 d  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 d  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 d  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 d  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 d  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 d  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 d  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 d  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 d  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 d  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 d  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 d  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 d  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 d  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 d  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 d  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 d  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 d  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 d  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 d  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 d  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 d  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 d  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 d  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 d  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 d  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 d  352  LEU                                                          
SEQRES   1 e   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 e   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 e   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 e   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 e   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 e   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 e   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 f   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 f   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 f   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 f   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 h   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 h   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 h   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 h   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 h   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 h   66  GLY                                                          
SEQRES   1 i   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 i   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 i   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 j   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 j   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 j   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 j   40  LEU                                                          
SEQRES   1 k   46  MET ILE ASP ALA LEU VAL LEU VAL ALA LYS LEU PRO GLU          
SEQRES   2 k   46  ALA TYR ALA ILE PHE ASP PRO LEU VAL ASP VAL LEU PRO          
SEQRES   3 k   46  VAL ILE PRO VAL LEU PHE LEU ALA LEU ALA PHE VAL TRP          
SEQRES   4 k   46  GLN ALA ALA VAL GLY PHE ARG                                  
SEQRES   1 l   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 l   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 l   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 m   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 m   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 m   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 o  272  MET LYS TYR ARG ILE LEU MET ALA THR LEU LEU ALA VAL          
SEQRES   2 o  272  CYS LEU GLY ILE PHE SER LEU SER ALA PRO ALA PHE ALA          
SEQRES   3 o  272  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   4 o  272  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   5 o  272  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   6 o  272  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   7 o  272  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   8 o  272  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   9 o  272  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES  10 o  272  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES  11 o  272  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  12 o  272  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  13 o  272  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  14 o  272  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  15 o  272  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  16 o  272  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  17 o  272  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  18 o  272  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  19 o  272  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  20 o  272  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  21 o  272  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 t   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 t   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 t   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 u  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 u  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 u  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 u  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 u  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 u  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 u  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 u  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 u  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 u  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 u  134  GLY LEU TYR LYS                                              
SEQRES   1 v  163  MET LEU LYS LYS CYS VAL TRP LEU ALA VAL ALA LEU CYS          
SEQRES   2 v  163  LEU CYS LEU TRP GLN PHE THR MET GLY THR ALA LEU ALA          
SEQRES   3 v  163  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   4 v  163  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   5 v  163  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   6 v  163  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   7 v  163  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   8 v  163  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   9 v  163  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES  10 v  163  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES  11 v  163  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  12 v  163  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  13 v  163  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 x   41  MET THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY          
SEQRES   2 x   41  LEU LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA          
SEQRES   3 x   41  VAL LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN ARG          
SEQRES   4 x   41  SER LEU                                                      
SEQRES   1 R   41  MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU          
SEQRES   2 R   41  LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR          
SEQRES   3 R   41  ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS          
SEQRES   4 R   41  ALA ALA                                                      
SEQRES   1 r   41  MET ASP TRP ARG VAL LEU VAL VAL LEU LEU PRO VAL LEU          
SEQRES   2 r   41  LEU ALA ALA GLY TRP ALA VAL ARG ASN ILE LEU PRO TYR          
SEQRES   3 r   41  ALA VAL LYS GLN VAL GLN LYS LEU LEU GLN LYS ALA LYS          
SEQRES   4 r   41  ALA ALA                                                      
SEQRES   1 y   46  MET GLY ILE PHE ASN GLY ILE ILE GLU PHE LEU SER ASN          
SEQRES   2 y   46  ILE ASN PHE GLU VAL ILE ALA GLN LEU THR MET ILE ALA          
SEQRES   3 y   46  MET ILE GLY ILE ALA GLY PRO MET ILE ILE PHE LEU LEU          
SEQRES   4 y   46  ALA VAL ARG ARG GLY ASN LEU                                  
SEQRES   1 z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
HET    OEX  A 601      10                                                       
HET     FE  A 602       1                                                       
HET    LMG  A 603      51                                                       
HET     CL  A 604       1                                                       
HET     CL  A 605       1                                                       
HET    CLA  A 606      65                                                       
HET    CLA  A 607      65                                                       
HET    CLA  A 608      65                                                       
HET    BCR  A 609      40                                                       
HET    PL9  A 610      55                                                       
HET    SQD  A 611      54                                                       
HET    LMG  A 612      51                                                       
HET    LHG  A 613      49                                                       
HET    LHG  A 614      49                                                       
HET    SO4  A 615       5                                                       
HET    BCT  A 616       4                                                       
HET    CLA  B 601      65                                                       
HET    CLA  B 602      65                                                       
HET    CLA  B 603      65                                                       
HET    CLA  B 604      65                                                       
HET    CLA  B 605      65                                                       
HET    CLA  B 606      65                                                       
HET    CLA  B 607      65                                                       
HET    CLA  B 608      65                                                       
HET    CLA  B 609      65                                                       
HET    CLA  B 610      65                                                       
HET    CLA  B 611      65                                                       
HET    CLA  B 612      65                                                       
HET    CLA  B 613      65                                                       
HET    CLA  B 614      65                                                       
HET    CLA  B 615      65                                                       
HET    CLA  B 616      65                                                       
HET    BCR  B 617      40                                                       
HET    BCR  B 618      40                                                       
HET    BCR  B 619      40                                                       
HET    LMG  B 620      51                                                       
HET    UNL  B 621      10                                                       
HET    UNL  B 622       8                                                       
HET    UNL  B 623      13                                                       
HET    LMG  B 624      51                                                       
HET    UNL  B 625      16                                                       
HET    UNL  B 626       9                                                       
HET    UNL  B 627      12                                                       
HET    CLA  C 501      65                                                       
HET    CLA  C 502      65                                                       
HET    CLA  C 503      65                                                       
HET    CLA  C 504      65                                                       
HET    CLA  C 505      65                                                       
HET    CLA  C 506      65                                                       
HET    CLA  C 507      65                                                       
HET    CLA  C 508      65                                                       
HET    CLA  C 509      65                                                       
HET    CLA  C 510      65                                                       
HET    CLA  C 511      65                                                       
HET    CLA  C 512      65                                                       
HET    CLA  C 513      65                                                       
HET    BCR  C 514      40                                                       
HET    BCR  C 515      40                                                       
HET    DGD  C 516      62                                                       
HET    DGD  C 517      62                                                       
HET    DGD  C 518      62                                                       
HET    LMG  C 519      51                                                       
HET    UNL  C 520      15                                                       
HET    LMG  C 521      51                                                       
HET    BCR  C 522      40                                                       
HET    PHO  D 401      64                                                       
HET    PHO  D 402      64                                                       
HET    CLA  D 403      65                                                       
HET    CLA  D 404      65                                                       
HET    CLA  D 405      65                                                       
HET    BCR  D 406      40                                                       
HET    PL9  D 407      55                                                       
HET    LHG  D 408      49                                                       
HET    LMG  D 409      51                                                       
HET    UNL  D 410      15                                                       
HET    LHG  E 101      42                                                       
HET    HEM  E 102      43                                                       
HET    SQD  F 101      43                                                       
HET    BCR  H 101      40                                                       
HET    DGD  H 102      62                                                       
HET    UNL  I 101      14                                                       
HET    UNL  J 101      11                                                       
HET    BCR  K 101      40                                                       
HET    SQD  L 101      54                                                       
HET    LHG  L 102      49                                                       
HET    SQD  L 103      54                                                       
HET    UNL  M 101      10                                                       
HET    UNL  M 102      16                                                       
HET    SO4  O 301       5                                                       
HET    SO4  O 302       5                                                       
HET    BCR  T 101      40                                                       
HET    UNL  T 102      15                                                       
HET    UNL  T 103      12                                                       
HET    SO4  U 201       5                                                       
HET    HEM  V 201      43                                                       
HET    SO4  V 202       5                                                       
HET    UNL  X 101      10                                                       
HET    OEX  a 601      10                                                       
HET     FE  a 602       1                                                       
HET    LMG  a 603      51                                                       
HET     CL  a 604       1                                                       
HET     CL  a 605       1                                                       
HET    CLA  a 606      65                                                       
HET    CLA  a 607      65                                                       
HET    CLA  a 608      65                                                       
HET    PHO  a 609      64                                                       
HET    CLA  a 610      65                                                       
HET    BCR  a 611      40                                                       
HET    PL9  a 612      55                                                       
HET    SQD  a 613      54                                                       
HET    LMG  a 614      51                                                       
HET    LHG  a 615      49                                                       
HET    LHG  a 616      42                                                       
HET    SO4  a 617       5                                                       
HET    BCT  a 618       4                                                       
HET    CLA  b 601      65                                                       
HET    CLA  b 602      65                                                       
HET    CLA  b 603      65                                                       
HET    CLA  b 604      65                                                       
HET    CLA  b 605      65                                                       
HET    CLA  b 606      65                                                       
HET    CLA  b 607      65                                                       
HET    CLA  b 608      65                                                       
HET    CLA  b 609      65                                                       
HET    CLA  b 610      65                                                       
HET    CLA  b 611      65                                                       
HET    CLA  b 612      65                                                       
HET    CLA  b 613      65                                                       
HET    CLA  b 614      65                                                       
HET    CLA  b 615      65                                                       
HET    CLA  b 616      65                                                       
HET    BCR  b 617      40                                                       
HET    BCR  b 618      40                                                       
HET    BCR  b 619      40                                                       
HET    LMG  b 620      51                                                       
HET    UNL  b 621      10                                                       
HET    UNL  b 622      12                                                       
HET    UNL  b 623      13                                                       
HET    LMG  b 624      51                                                       
HET    UNL  b 625      16                                                       
HET    UNL  b 626       9                                                       
HET    CLA  c 501      65                                                       
HET    CLA  c 502      65                                                       
HET    CLA  c 503      65                                                       
HET    CLA  c 504      65                                                       
HET    CLA  c 505      65                                                       
HET    CLA  c 506      65                                                       
HET    CLA  c 507      65                                                       
HET    CLA  c 508      65                                                       
HET    CLA  c 509      65                                                       
HET    CLA  c 510      65                                                       
HET    CLA  c 511      65                                                       
HET    CLA  c 512      65                                                       
HET    CLA  c 513      65                                                       
HET    BCR  c 514      40                                                       
HET    DGD  c 515      62                                                       
HET    DGD  c 516      62                                                       
HET    DGD  c 517      62                                                       
HET    LMG  c 518      51                                                       
HET    UNL  c 519      15                                                       
HET    LMG  c 520      51                                                       
HET    BCR  c 521      40                                                       
HET    CLA  d 401      65                                                       
HET    PHO  d 402      64                                                       
HET    CLA  d 403      65                                                       
HET    BCR  d 404      40                                                       
HET    PL9  d 405      55                                                       
HET    LHG  d 406      49                                                       
HET    LHG  d 407      49                                                       
HET    LMG  d 408      51                                                       
HET    UNL  d 409      15                                                       
HET    SO4  d 410       5                                                       
HET    HEM  e 101      43                                                       
HET    SQD  f 101      43                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET    UNL  i 101      16                                                       
HET    UNL  j 101      15                                                       
HET    UNL  k 101       9                                                       
HET    BCR  k 102      40                                                       
HET    LHG  l 101      49                                                       
HET    UNL  m 101      10                                                       
HET    UNL  m 102      15                                                       
HET    SO4  o 301       5                                                       
HET    UNL  t 101      15                                                       
HET    BCR  t 102      40                                                       
HET    SO4  u 201       5                                                       
HET    SO4  u 202       5                                                       
HET    HEM  v 201      43                                                       
HET    UNL  x 101      16                                                       
HET    BCR  z 101      40                                                       
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM      FE FE (III) ION                                                     
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM      CL CHLORIDE ION                                                     
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     PL9 2,3-DIMETHYL-5-(3,7,11,15,19,23,27,31,35-NONAMETHYL-2,           
HETNAM   2 PL9  6,10,14,18,22,26,30,34-HEXATRIACONTANONAENYL-2,5-               
HETNAM   3 PL9  CYCLOHEXADIENE-1,4-DIONE-2,3-DIMETHYL-5-SOLANESYL-1,4-          
HETNAM   4 PL9  BENZOQUINONE                                                    
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
FORMUL  41  OEX    2(CA MN4 O5)                                                 
FORMUL  42   FE    2(FE 3+)                                                     
FORMUL  43  LMG    14(C45 H86 O10)                                              
FORMUL  44   CL    4(CL 1-)                                                     
FORMUL  46  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  49  BCR    22(C40 H56)                                                  
FORMUL  50  PL9    4(C53 H80 O2)                                                
FORMUL  51  SQD    6(C41 H78 O12 S)                                             
FORMUL  53  LHG    10(C38 H75 O10 P)                                            
FORMUL  55  SO4    10(O4 S 2-)                                                  
FORMUL  56  BCT    2(C H O3 1-)                                                 
FORMUL  99  DGD    8(C51 H96 O15)                                               
FORMUL  06  PHO    4(C55 H74 N4 O5)                                             
FORMUL  17  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  32  HOH   *304(H2 O)                                                    
HELIX    1 AA1 LEU A   13  THR A   22  1                                  10    
HELIX    2 AA2 VAL A   30  ALA A   55  1                                  26    
HELIX    3 AA3 SER A   70  GLY A   74  5                                   5    
HELIX    4 AA4 PRO A   95  ALA A   99  5                                   5    
HELIX    5 AA5 SER A  101  ASN A  108  1                                   8    
HELIX    6 AA6 GLY A  109  GLY A  138  1                                  30    
HELIX    7 AA7 TRP A  142  LEU A  159  1                                  18    
HELIX    8 AA8 LEU A  159  GLY A  166  1                                   8    
HELIX    9 AA9 SER A  167  GLY A  171  5                                   5    
HELIX   10 AB1 ILE A  176  ASN A  191  1                                  16    
HELIX   11 AB2 ILE A  192  MET A  194  5                                   3    
HELIX   12 AB3 HIS A  195  SER A  222  1                                  28    
HELIX   13 AB4 SER A  232  TYR A  237  5                                   6    
HELIX   14 AB5 ASN A  247  ILE A  259  1                                  13    
HELIX   15 AB6 PHE A  260  SER A  264  5                                   5    
HELIX   16 AB7 ASN A  267  ALA A  294  1                                  28    
HELIX   17 AB8 THR A  316  VAL A  330  1                                  15    
HELIX   18 AB9 PRO B    4  ILE B   13  5                                  10    
HELIX   19 AC1 ASP B   15  ALA B   43  1                                  29    
HELIX   20 AC2 PRO B   54  GLN B   58  5                                   5    
HELIX   21 AC3 VAL B   62  LEU B   69  1                                   8    
HELIX   22 AC4 SER B   92  TYR B  117  1                                  26    
HELIX   23 AC5 LEU B  120  ARG B  124  5                                   5    
HELIX   24 AC6 ASP B  134  PHE B  156  1                                  23    
HELIX   25 AC7 GLY B  186  ASN B  191  5                                   6    
HELIX   26 AC8 ASN B  194  VAL B  219  1                                  26    
HELIX   27 AC9 PRO B  222  LEU B  229  1                                   8    
HELIX   28 AD1 ILE B  234  GLY B  259  1                                  26    
HELIX   29 AD2 THR B  271  SER B  277  1                                   7    
HELIX   30 AD3 SER B  278  SER B  294  1                                  17    
HELIX   31 AD4 THR B  297  ALA B  304  1                                   8    
HELIX   32 AD5 PRO B  306  ASP B  313  1                                   8    
HELIX   33 AD6 TYR B  314  ASN B  318  5                                   5    
HELIX   34 AD7 PRO B  329  GLY B  333  5                                   5    
HELIX   35 AD8 SER B  391  GLY B  396  1                                   6    
HELIX   36 AD9 ASP B  413  ILE B  425  1                                  13    
HELIX   37 AE1 SER B  446  PHE B  475  1                                  30    
HELIX   38 AE2 ARG B  476  PHE B  479  5                                   4    
HELIX   39 AE3 SER B  487  GLU B  492  1                                   6    
HELIX   40 AE4 ASP B  501  ARG B  505  5                                   5    
HELIX   41 AE5 ASP C   27  GLY C   32  1                                   6    
HELIX   42 AE6 ALA C   34  ILE C   43  5                                  10    
HELIX   43 AE7 LEU C   45  HIS C   74  1                                  30    
HELIX   44 AE8 PRO C   80  GLN C   84  5                                   5    
HELIX   45 AE9 LEU C   88  LEU C   95  1                                   8    
HELIX   46 AF1 GLY C  100  GLU C  104  5                                   5    
HELIX   47 AF2 THR C  108  ARG C  135  1                                  28    
HELIX   48 AF3 ASP C  153  PHE C  181  1                                  29    
HELIX   49 AF4 ASP C  205  LEU C  214  1                                  10    
HELIX   50 AF5 GLY C  222  VAL C  227  5                                   6    
HELIX   51 AF6 ASN C  229  THR C  254  1                                  26    
HELIX   52 AF7 PHE C  257  PHE C  264  1                                   8    
HELIX   53 AF8 SER C  267  ASN C  293  1                                  27    
HELIX   54 AF9 PRO C  298  GLY C  303  1                                   6    
HELIX   55 AG1 THR C  305  GLY C  325  1                                  21    
HELIX   56 AG2 GLY C  353  TRP C  359  5                                   7    
HELIX   57 AG3 LEU C  366  PRO C  368  5                                   3    
HELIX   58 AG4 ASP C  376  ASP C  383  1                                   8    
HELIX   59 AG5 GLN C  385  THR C  397  1                                  13    
HELIX   60 AG6 SER C  421  GLY C  454  1                                  34    
HELIX   61 AG7 ASP C  460  SER C  463  5                                   4    
HELIX   62 AG8 GLU C  464  MET C  469  1                                   6    
HELIX   63 AG9 TRP D   14  LYS D   23  1                                  10    
HELIX   64 AH1 SER D   33  THR D   52  1                                  20    
HELIX   65 AH2 SER D   66  GLY D   70  5                                   5    
HELIX   66 AH3 ALA D   82  GLY D   86  5                                   5    
HELIX   67 AH4 ASP D  100  GLY D  108  1                                   9    
HELIX   68 AH5 GLY D  108  GLY D  137  1                                  30    
HELIX   69 AH6 PRO D  140  PHE D  146  1                                   7    
HELIX   70 AH7 PHE D  146  LEU D  158  1                                  13    
HELIX   71 AH8 LEU D  158  GLN D  164  1                                   7    
HELIX   72 AH9 SER D  166  ALA D  170  5                                   5    
HELIX   73 AI1 VAL D  175  PHE D  188  1                                  14    
HELIX   74 AI2 ASN D  190  LEU D  193  5                                   4    
HELIX   75 AI3 ASN D  194  ASN D  220  1                                  27    
HELIX   76 AI4 SER D  230  ALA D  234  5                                   5    
HELIX   77 AI5 SER D  245  PHE D  257  1                                  13    
HELIX   78 AI6 ASN D  263  ALA D  290  1                                  28    
HELIX   79 AI7 PHE D  298  ASP D  308  1                                  11    
HELIX   80 AI8 THR D  313  GLN D  334  1                                  22    
HELIX   81 AI9 PRO D  335  ASN D  338  5                                   4    
HELIX   82 AJ1 PRO D  342  LEU D  346  5                                   5    
HELIX   83 AJ2 PRO E    9  ILE E   14  1                                   6    
HELIX   84 AJ3 SER E   16  THR E   40  1                                  25    
HELIX   85 AJ4 GLY E   41  GLY E   48  1                                   8    
HELIX   86 AJ5 GLU E   71  GLN E   82  1                                  12    
HELIX   87 AJ6 THR F   17  GLN F   41  1                                  25    
HELIX   88 AJ7 THR H    5  ARG H   12  1                                   8    
HELIX   89 AJ8 PRO H   13  SER H   16  5                                   4    
HELIX   90 AJ9 THR H   27  ASN H   50  1                                  24    
HELIX   91 AK1 GLU I    2  LEU I   24  1                                  23    
HELIX   92 AK2 GLY I   26  ARG I   30  5                                   5    
HELIX   93 AK3 PRO J    9  GLY J   31  1                                  23    
HELIX   94 AK4 PRO K   12  ILE K   17  5                                   6    
HELIX   95 AK5 PHE K   18  ASP K   23  1                                   6    
HELIX   96 AK6 VAL K   24  PRO K   26  5                                   3    
HELIX   97 AK7 VAL K   27  VAL K   43  1                                  17    
HELIX   98 AK8 ASN L   13  ASN L   37  1                                  25    
HELIX   99 AK9 LEU M    6  SER M   31  1                                  26    
HELIX  100 AL1 THR O    6  VAL O   11  1                                   6    
HELIX  101 AL2 GLY O   14  LYS O   18  5                                   5    
HELIX  102 AL3 LEU O  182  VAL O  187  1                                   6    
HELIX  103 AL4 GLU T    2  PHE T   23  1                                  22    
HELIX  104 AL5 ASN U   11  LEU U   17  1                                   7    
HELIX  105 AL6 GLY U   18  GLU U   23  5                                   6    
HELIX  106 AL7 ASN U   31  TYR U   38  5                                   8    
HELIX  107 AL8 PRO U   43  ALA U   53  1                                  11    
HELIX  108 AL9 SER U   57  ILE U   64  5                                   8    
HELIX  109 AM1 THR U   68  GLU U   77  1                                  10    
HELIX  110 AM2 ASN U   78  GLU U   80  5                                   3    
HELIX  111 AM3 GLU U   88  GLU U   93  1                                   6    
HELIX  112 AM4 GLY U   94  ASP U   96  5                                   3    
HELIX  113 AM5 THR V    4  LEU V    8  1                                   5    
HELIX  114 AM6 THR V   22  CYS V   37  1                                  16    
HELIX  115 AM7 CYS V   37  VAL V   42  1                                   6    
HELIX  116 AM8 GLY V   43  ILE V   45  5                                   3    
HELIX  117 AM9 ARG V   55  LEU V   61  1                                   7    
HELIX  118 AN1 ASN V   68  MET V   76  1                                   9    
HELIX  119 AN2 PHE V  101  ARG V  105  5                                   5    
HELIX  120 AN3 THR V  108  GLY V  127  1                                  20    
HELIX  121 AN4 ASP V  128  TRP V  130  5                                   3    
HELIX  122 AN5 GLY V  133  TYR V  137  5                                   5    
HELIX  123 AN6 ILE Y   19  ARG Y   42  1                                  24    
HELIX  124 AN7 THR X    4  ASP X   35  1                                  32    
HELIX  125 AN8 THR Z    2  SER Z   29  1                                  28    
HELIX  126 AN9 ASP Z   32  PHE Z   59  1                                  28    
HELIX  127 AO1 LEU a   13  THR a   22  1                                  10    
HELIX  128 AO2 VAL a   30  ALA a   55  1                                  26    
HELIX  129 AO3 SER a   70  GLY a   74  5                                   5    
HELIX  130 AO4 PRO a   95  ALA a   99  5                                   5    
HELIX  131 AO5 SER a  101  ASN a  108  1                                   8    
HELIX  132 AO6 GLY a  109  LEU a  137  1                                  29    
HELIX  133 AO7 TRP a  142  LEU a  159  1                                  18    
HELIX  134 AO8 LEU a  159  GLY a  166  1                                   8    
HELIX  135 AO9 SER a  167  GLY a  171  5                                   5    
HELIX  136 AP1 ILE a  176  ASN a  191  1                                  16    
HELIX  137 AP2 ILE a  192  MET a  194  5                                   3    
HELIX  138 AP3 HIS a  195  SER a  222  1                                  28    
HELIX  139 AP4 SER a  232  TYR a  237  5                                   6    
HELIX  140 AP5 ASN a  247  ILE a  259  1                                  13    
HELIX  141 AP6 PHE a  260  SER a  264  5                                   5    
HELIX  142 AP7 ASN a  267  MET a  293  1                                  27    
HELIX  143 AP8 THR a  316  VAL a  330  1                                  15    
HELIX  144 AP9 PRO b    4  ILE b   13  5                                  10    
HELIX  145 AQ1 ASP b   15  PHE b   45  1                                  31    
HELIX  146 AQ2 PRO b   54  GLN b   58  5                                   5    
HELIX  147 AQ3 VAL b   62  LEU b   69  1                                   8    
HELIX  148 AQ4 SER b   92  TYR b  117  1                                  26    
HELIX  149 AQ5 LEU b  120  ARG b  124  5                                   5    
HELIX  150 AQ6 ASP b  134  PHE b  156  1                                  23    
HELIX  151 AQ7 GLY b  186  ASN b  191  5                                   6    
HELIX  152 AQ8 ASN b  194  VAL b  219  1                                  26    
HELIX  153 AQ9 PRO b  222  LEU b  229  1                                   8    
HELIX  154 AR1 ILE b  234  GLY b  259  1                                  26    
HELIX  155 AR2 THR b  271  SER b  277  1                                   7    
HELIX  156 AR3 SER b  278  SER b  294  1                                  17    
HELIX  157 AR4 THR b  297  ALA b  304  1                                   8    
HELIX  158 AR5 PRO b  306  ASP b  313  1                                   8    
HELIX  159 AR6 TYR b  314  ASN b  318  5                                   5    
HELIX  160 AR7 PRO b  329  GLY b  333  5                                   5    
HELIX  161 AR8 SER b  391  GLY b  396  1                                   6    
HELIX  162 AR9 ASP b  413  ILE b  425  1                                  13    
HELIX  163 AS1 SER b  446  PHE b  475  1                                  30    
HELIX  164 AS2 SER b  487  VAL b  491  5                                   5    
HELIX  165 AS3 ASP c   27  GLY c   32  1                                   6    
HELIX  166 AS4 ALA c   34  ILE c   43  5                                  10    
HELIX  167 AS5 LEU c   45  HIS c   74  1                                  30    
HELIX  168 AS6 PRO c   80  GLN c   84  5                                   5    
HELIX  169 AS7 LEU c   88  LEU c   95  1                                   8    
HELIX  170 AS8 GLY c  100  GLU c  104  5                                   5    
HELIX  171 AS9 THR c  108  ARG c  135  1                                  28    
HELIX  172 AT1 ASP c  153  PHE c  181  1                                  29    
HELIX  173 AT2 ASP c  205  LEU c  214  1                                  10    
HELIX  174 AT3 GLY c  222  VAL c  227  5                                   6    
HELIX  175 AT4 ASN c  229  THR c  254  1                                  26    
HELIX  176 AT5 PHE c  257  ARG c  262  1                                   6    
HELIX  177 AT6 SER c  267  ASN c  293  1                                  27    
HELIX  178 AT7 PRO c  298  GLY c  303  1                                   6    
HELIX  179 AT8 THR c  305  LEU c  324  1                                  20    
HELIX  180 AT9 GLY c  353  TRP c  359  5                                   7    
HELIX  181 AU1 LEU c  366  PRO c  368  5                                   3    
HELIX  182 AU2 ASP c  376  ASP c  383  1                                   8    
HELIX  183 AU3 GLN c  385  THR c  397  1                                  13    
HELIX  184 AU4 SER c  421  GLY c  454  1                                  34    
HELIX  185 AU5 GLU c  464  MET c  469  5                                   6    
HELIX  186 AU6 TRP d   14  LYS d   23  1                                  10    
HELIX  187 AU7 VAL d   30  THR d   52  1                                  23    
HELIX  188 AU8 SER d   66  GLY d   70  5                                   5    
HELIX  189 AU9 ALA d   82  GLY d   86  5                                   5    
HELIX  190 AV1 ASP d  100  LEU d  107  1                                   8    
HELIX  191 AV2 GLY d  108  GLY d  137  1                                  30    
HELIX  192 AV3 PRO d  140  PHE d  146  1                                   7    
HELIX  193 AV4 PHE d  146  LEU d  158  1                                  13    
HELIX  194 AV5 LEU d  158  GLN d  164  1                                   7    
HELIX  195 AV6 SER d  166  ALA d  170  5                                   5    
HELIX  196 AV7 VAL d  175  ASN d  190  1                                  16    
HELIX  197 AV8 TRP d  191  LEU d  193  5                                   3    
HELIX  198 AV9 ASN d  194  ASN d  220  1                                  27    
HELIX  199 AW1 SER d  230  PHE d  235  5                                   6    
HELIX  200 AW2 SER d  245  PHE d  257  1                                  13    
HELIX  201 AW3 ASN d  263  ALA d  290  1                                  28    
HELIX  202 AW4 PHE d  298  ASP d  308  1                                  11    
HELIX  203 AW5 THR d  313  GLN d  334  1                                  22    
HELIX  204 AW6 PRO d  335  ASN d  338  5                                   4    
HELIX  205 AW7 PRO d  342  LEU d  346  5                                   5    
HELIX  206 AW8 PRO e    9  ILE e   14  1                                   6    
HELIX  207 AW9 SER e   16  HIS e   23  1                                   8    
HELIX  208 AX1 ILE e   25  THR e   40  1                                  16    
HELIX  209 AX2 GLY e   41  GLY e   48  1                                   8    
HELIX  210 AX3 GLU e   71  LEU e   83  1                                  13    
HELIX  211 AX4 THR f   17  GLN f   41  1                                  25    
HELIX  212 AX5 THR h    5  ARG h   12  1                                   8    
HELIX  213 AX6 PRO h   13  SER h   16  5                                   4    
HELIX  214 AX7 THR h   27  ASN h   50  1                                  24    
HELIX  215 AX8 GLU i    2  SER i   25  1                                  24    
HELIX  216 AX9 GLY i   26  ARG i   30  5                                   5    
HELIX  217 AY1 PRO j    9  ALA j   32  1                                  24    
HELIX  218 AY2 PRO k   12  ILE k   17  5                                   6    
HELIX  219 AY3 PHE k   18  ASP k   23  1                                   6    
HELIX  220 AY4 VAL k   24  PRO k   26  5                                   3    
HELIX  221 AY5 VAL k   27  VAL k   43  1                                  17    
HELIX  222 AY6 ASN l   13  ASN l   37  1                                  25    
HELIX  223 AY7 LEU m    6  SER m   31  1                                  26    
HELIX  224 AY8 THR o    6  VAL o   11  1                                   6    
HELIX  225 AY9 GLY o   14  LYS o   18  5                                   5    
HELIX  226 AZ1 LEU o  182  VAL o  187  1                                   6    
HELIX  227 AZ2 GLU t    2  PHE t   23  1                                  22    
HELIX  228 AZ3 ASN u   11  LEU u   17  1                                   7    
HELIX  229 AZ4 GLY u   18  GLU u   23  5                                   6    
HELIX  230 AZ5 ASN u   31  GLN u   37  5                                   7    
HELIX  231 AZ6 PRO u   43  ASN u   52  1                                  10    
HELIX  232 AZ7 SER u   57  ILE u   64  5                                   8    
HELIX  233 AZ8 THR u   68  ASN u   78  1                                  11    
HELIX  234 AZ9 GLU u   88  GLU u   93  1                                   6    
HELIX  235 BA1 GLY u   94  ASP u   96  5                                   3    
HELIX  236 BA2 THR v   22  CYS v   37  1                                  16    
HELIX  237 BA3 CYS v   37  VAL v   42  1                                   6    
HELIX  238 BA4 GLY v   43  ILE v   45  5                                   3    
HELIX  239 BA5 ARG v   55  LEU v   61  1                                   7    
HELIX  240 BA6 ASN v   68  ASN v   78  1                                  11    
HELIX  241 BA7 PHE v  101  ARG v  105  5                                   5    
HELIX  242 BA8 THR v  108  GLU v  122  1                                  15    
HELIX  243 BA9 GLU v  122  GLY v  127  1                                   6    
HELIX  244 BB1 ASP v  128  TRP v  130  5                                   3    
HELIX  245 BB2 GLY v  133  TYR v  137  5                                   5    
HELIX  246 BB3 THR x    4  ASP x   35  1                                  32    
HELIX  247 BB4 TRP R    3  LEU R   35  1                                  33    
HELIX  248 BB5 ARG r    4  ASN r   22  1                                  19    
HELIX  249 BB6 ILE r   23  LEU r   35  1                                  13    
HELIX  250 BB7 ILE y   19  ARG y   42  1                                  24    
HELIX  251 BB8 THR z    2  ALA z   28  1                                  27    
HELIX  252 BB9 SER z   36  ASN z   58  1                                  23    
SHEET    1 AA1 2 ALA A  81  VAL A  82  0                                        
SHEET    2 AA1 2 LEU A 174  GLY A 175 -1  O  LEU A 174   N  VAL A  82           
SHEET    1 AA2 2 LEU A 297  ASN A 298  0                                        
SHEET    2 AA2 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1 AA3 2 MET B 166  VAL B 168  0                                        
SHEET    2 AA3 2 SER B 177  GLN B 179 -1  O  SER B 177   N  VAL B 168           
SHEET    1 AA4 2 ILE B 336  TRP B 340  0                                        
SHEET    2 AA4 2 PHE B 430  ASP B 433 -1  O  GLU B 431   N  ALA B 339           
SHEET    1 AA5 6 VAL B 377  ASP B 380  0                                        
SHEET    2 AA5 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA5 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA5 6 HIS B 343  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA5 6 THR B 398  TYR B 402 -1  O  THR B 398   N  ARG B 347           
SHEET    6 AA5 6 GLN B 409  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA6 2 LEU C 185  ASP C 187  0                                        
SHEET    2 AA6 2 ASP C 195  ARG C 197 -1  O  ASP C 195   N  ASP C 187           
SHEET    1 AA7 2 LEU C 341  ARG C 343  0                                        
SHEET    2 AA7 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1 AA8 2 ARG C 370  GLY C 371  0                                        
SHEET    2 AA8 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1 AA9 2 ALA D  77  VAL D  78  0                                        
SHEET    2 AA9 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1 AB1 2 TYR O  30  PRO O  31  0                                        
SHEET    2 AB1 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1 AB210 PHE O  65  PRO O  67  0                                        
SHEET    2 AB210 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3 AB210 GLU O 232  GLU O 244 -1  O  LYS O 234   N  LEU O  51           
SHEET    4 AB210 GLU O 210  LEU O 220 -1  N  ILE O 211   O  ALA O 241           
SHEET    5 AB210 LEU O 192  ASP O 205 -1  N  GLN O 196   O  GLU O 218           
SHEET    6 AB210 ASP O 141  PRO O 149 -1  N  PHE O 142   O  LEU O 199           
SHEET    7 AB210 VAL O 126  SER O 128 -1  N  SER O 128   O  LYS O 143           
SHEET    8 AB210 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9 AB210 LEU O  78  VAL O  87 -1  N  GLU O  84   O  VAL O  96           
SHEET   10 AB210 TYR O  38  LYS O  53 -1  N  ILE O  40   O  GLY O  83           
SHEET    1 AB3 3 LYS O  69  LEU O  70  0                                        
SHEET    2 AB3 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3 AB3 3 ARG O 115  THR O 121 -1  O  ILE O 116   N  VAL O 108           
SHEET    1 AB4 2 ILE U  25  ASP U  26  0                                        
SHEET    2 AB4 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1 AB5 2 THR V   9  PRO V  11  0                                        
SHEET    2 AB5 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1 AB6 2 ALA a  81  VAL a  82  0                                        
SHEET    2 AB6 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1 AB7 2 LEU a 297  ASN a 298  0                                        
SHEET    2 AB7 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1 AB8 2 MET b 166  VAL b 168  0                                        
SHEET    2 AB8 2 SER b 177  GLN b 179 -1  O  GLN b 179   N  MET b 166           
SHEET    1 AB9 2 ILE b 336  TRP b 340  0                                        
SHEET    2 AB9 2 PHE b 430  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1 AC1 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AC1 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC1 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC1 6 HIS b 343  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC1 6 THR b 398  TYR b 402 -1  O  THR b 398   N  ARG b 347           
SHEET    6 AC1 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1 AC2 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC2 2 ASP c 195  ARG c 197 -1  O  ARG c 197   N  LEU c 185           
SHEET    1 AC3 2 LEU c 341  ARG c 343  0                                        
SHEET    2 AC3 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1 AC4 2 ARG c 370  GLY c 371  0                                        
SHEET    2 AC4 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1 AC5 2 ALA d  77  VAL d  78  0                                        
SHEET    2 AC5 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1 AC6 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC6 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC710 PHE o  65  PRO o  67  0                                        
SHEET    2 AC710 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC710 GLU o 232  PRO o 245 -1  O  LYS o 234   N  LEU o  51           
SHEET    4 AC710 GLU o 210  LEU o 220 -1  N  GLN o 219   O  VAL o 233           
SHEET    5 AC710 LEU o 192  ASP o 205 -1  N  ALA o 202   O  ALA o 212           
SHEET    6 AC710 ASP o 141  PRO o 149 -1  N  VAL o 148   O  THR o 193           
SHEET    7 AC710 VAL o 126  SER o 128 -1  N  SER o 128   O  LYS o 143           
SHEET    8 AC710 LEU o  93  ILE o 101 -1  N  PHE o  95   O  ALA o 127           
SHEET    9 AC710 LEU o  78  VAL o  87 -1  N  LYS o  86   O  THR o  94           
SHEET   10 AC710 TYR o  38  LYS o  53 -1  N  LEU o  45   O  LEU o  78           
SHEET    1 AC8 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AC8 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AC8 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AC9 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AC9 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1 AD1 2 THR v   9  PRO v  11  0                                        
SHEET    2 AD1 2 THR v  18  THR v  20 -1  O  ILE v  19   N  VAL v  10           
SSBOND   1 CYS O   19    CYS O   44                          1555   1555  2.03  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  2.03  
LINK         OD1 ASP A 170                MN4  OEX A 601     1555   1555  2.16  
LINK         OD2 ASP A 170                CA1  OEX A 601     1555   1555  2.50  
LINK         OE2 GLU A 189                MN1  OEX A 601     1555   1555  1.88  
LINK         NE2 HIS A 215                FE    FE A 602     1555   1555  2.25  
LINK         NE2 HIS A 272                FE    FE A 602     1555   1555  2.26  
LINK         NE2 HIS A 332                MN1  OEX A 601     1555   1555  2.18  
LINK         OE1 GLU A 333                MN3  OEX A 601     1555   1555  2.09  
LINK         OE2 GLU A 333                MN4  OEX A 601     1555   1555  2.15  
LINK         OD1 ASP A 342                MN2  OEX A 601     1555   1555  2.09  
LINK         OD2 ASP A 342                MN1  OEX A 601     1555   1555  2.29  
LINK         O   ALA A 344                CA1  OEX A 601     1555   1555  2.61  
LINK         OXT ALA A 344                MN2  OEX A 601     1555   1555  1.92  
LINK         OD1 ASN C  39                MG   CLA C 511     1555   1555  2.16  
LINK         OE1 GLU C 354                MN2  OEX A 601     1555   1555  2.11  
LINK         OE2 GLU C 354                MN3  OEX A 601     1555   1555  2.22  
LINK         NE2 HIS D 214                FE    FE A 602     1555   1555  2.10  
LINK         NE2 HIS D 268                FE    FE A 602     1555   1555  2.31  
LINK         NE2 HIS E  23                FE   HEM E 102     1555   1555  2.08  
LINK         NE2 HIS F  24                FE   HEM E 102     1555   1555  2.18  
LINK         SG  CYS V  37                 CAB HEM V 201     1555   1555  1.78  
LINK         SG  CYS V  40                 CAC HEM V 201     1555   1555  1.85  
LINK         NE2 HIS V  41                FE   HEM V 201     1555   1555  2.17  
LINK         NE2 HIS V  92                FE   HEM V 201     1555   1555  2.17  
LINK         OD1 ASP a 170                MN4  OEX a 601     1555   1555  2.02  
LINK         OD2 ASP a 170                CA1  OEX a 601     1555   1555  2.65  
LINK         OE2 GLU a 189                MN1  OEX a 601     1555   1555  1.81  
LINK         NE2 HIS a 215                FE    FE a 602     1555   1555  2.28  
LINK         NE2 HIS a 272                FE    FE a 602     1555   1555  2.28  
LINK         NE2 HIS a 332                MN1  OEX a 601     1555   1555  2.19  
LINK         OE1 GLU a 333                MN3  OEX a 601     1555   1555  2.00  
LINK         OE2 GLU a 333                MN4  OEX a 601     1555   1555  2.15  
LINK         OD1 ASP a 342                MN2  OEX a 601     1555   1555  2.10  
LINK         OD2 ASP a 342                MN1  OEX a 601     1555   1555  2.28  
LINK         O   ALA a 344                CA1  OEX a 601     1555   1555  2.54  
LINK         OXT ALA a 344                MN2  OEX a 601     1555   1555  1.82  
LINK         OD1 ASN c  39                MG   CLA c 511     1555   1555  2.14  
LINK         OE1 GLU c 354                MN2  OEX a 601     1555   1555  2.16  
LINK         OE2 GLU c 354                MN3  OEX a 601     1555   1555  2.21  
LINK         NE2 HIS d 214                FE    FE a 602     1555   1555  2.34  
LINK         NE2 HIS d 268                FE    FE a 602     1555   1555  2.34  
LINK         NE2 HIS e  23                FE   HEM e 101     1555   1555  2.19  
LINK         NE2 HIS f  24                FE   HEM e 101     1555   1555  2.19  
LINK         SG  CYS v  37                 CAB HEM v 201     1555   1555  1.76  
LINK         SG  CYS v  40                 CAC HEM v 201     1555   1555  1.84  
LINK         NE2 HIS v  41                FE   HEM v 201     1555   1555  2.01  
LINK         NE2 HIS v  92                FE   HEM v 201     1555   1555  2.17  
LINK        MN4  OEX A 601                 O   HOH A 728     1555   1555  2.08  
LINK        MN4  OEX A 601                 O   HOH A 729     1555   1555  2.22  
LINK        FE    FE A 602                 O1  BCT A 616     1555   1555  2.07  
LINK        FE    FE A 602                 O2  BCT A 616     1555   1555  2.07  
LINK        MG   CLA B 607                 O   HOH B 738     1555   1555  2.09  
LINK        MG   CLA D 403                 O   HOH D 501     1555   1555  2.07  
LINK        MN4  OEX a 601                 O   HOH a 721     1555   1555  2.16  
LINK        MN4  OEX a 601                 O   HOH a 722     1555   1555  2.13  
LINK        FE    FE a 602                 O1  BCT a 618     1555   1555  2.08  
LINK        FE    FE a 602                 O2  BCT a 618     1555   1555  2.08  
LINK        MG   CLA a 607                 O   HOH a 705     1555   1555  2.07  
LINK        MG   CLA b 607                 O   HOH b 701     1555   1555  2.09  
LINK        MG   CLA b 610                 O   HOH b 719     1555   1555  2.07  
CISPEP   1 TYR U   42    PRO U   43          0        -1.65                     
CISPEP   2 ALA U   53    PRO U   54          0         1.80                     
CISPEP   3 THR V   63    PRO V   64          0        -1.67                     
CISPEP   4 TYR u   42    PRO u   43          0        -0.86                     
CISPEP   5 ALA u   53    PRO u   54          0         1.38                     
CISPEP   6 THR v   63    PRO v   64          0        -2.08                     
SITE     1 AC1 13 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AC1 13 HIS A 337  ASP A 342  ALA A 344  HOH A 726                    
SITE     3 AC1 13 HOH A 728  HOH A 729  HOH A 730  GLU C 354                    
SITE     4 AC1 13 ARG C 357                                                     
SITE     1 AC2  5 HIS A 215  HIS A 272  BCT A 616  HIS D 214                    
SITE     2 AC2  5 HIS D 268                                                     
SITE     1 AC3 13 TRP A  20  ASN A  26  ARG A  27  LEU A  28                    
SITE     2 AC3 13 VAL A  30  LEU A  42  THR A  45  ILE A  46                    
SITE     3 AC3 13 CLA D 403  PHE T  22  BCR T 101  TRP b 113                    
SITE     4 AC3 13 BCR b 619                                                     
SITE     1 AC4  3 ASN A 181  GLU A 333  LYS D 317                               
SITE     1 AC5  4 ASN A 338  PHE A 339  GLU C 354  HOH C 923                    
SITE     1 AC6 21 TYR A 147  PRO A 150  SER A 153  VAL A 157                    
SITE     2 AC6 21 MET A 183  PHE A 186  GLN A 187  ILE A 192                    
SITE     3 AC6 21 LEU A 193  HIS A 198  GLY A 201  PHE A 206                    
SITE     4 AC6 21 THR A 286  ALA A 287  ILE A 290  CLA A 607                    
SITE     5 AC6 21 PHE D 257  PHO D 401  CLA D 403  CLA D 404                    
SITE     6 AC6 21 PHE T  17                                                     
SITE     1 AC7 16 GLN A 199  VAL A 202  ALA A 203  PHE A 206                    
SITE     2 AC7 16 GLY A 207  LEU A 210  TRP A 278  CLA A 606                    
SITE     3 AC7 16 DGD C 518  PHE D 157  VAL D 175  ILE D 178                    
SITE     4 AC7 16 PHE D 179  LEU D 182  PHO D 402  CLA D 404                    
SITE     1 AC8 20 ILE A  36  PRO A  39  PHE A  93  TYR A  94                    
SITE     2 AC8 20 PRO A  95  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC8 20 PHE A 117  HIS A 118  BCR A 609  LMG A 612                    
SITE     4 AC8 20 CLA C 505  CLA C 506  DGD C 516  VAL I   8                    
SITE     5 AC8 20 TYR I   9  VAL I  12  PHE I  15  VAL I  16                    
SITE     1 AC9  4 LEU A  42  ALA A  43  ILE A  50  CLA A 608                    
SITE     1 AD1 19 PHE A 211  HIS A 215  LEU A 218  HIS A 252                    
SITE     2 AD1 19 PHE A 255  ALA A 263  SER A 264  PHE A 265                    
SITE     3 AD1 19 LEU A 271  PHE A 274  LEU A 275  PHE D  38                    
SITE     4 AD1 19 PRO D  39  LEU D  45  PHO D 402  LHG E 101                    
SITE     5 AD1 19 LEU F  26  THR X  24  LEU X  28                               
SITE     1 AD2 12 LEU A 200  SER A 270  PHE A 273  ALA A 277                    
SITE     2 AD2 12 TRP A 278  LHG A 614  GLN C  28  ALA C  34                    
SITE     3 AD2 12 TRP C  36  CLA C 508  PHE D 232  PHE K  37                    
SITE     1 AD3 18 PHE A  93  TRP A  97  GLU A  98  PHE A 117                    
SITE     2 AD3 18 LEU A 120  LEU A 121  PHE A 155  CLA A 608                    
SITE     3 AD3 18 LEU C 214  SER C 216  PHE C 218  GLU C 221                    
SITE     4 AD3 18 TRP C 223  PHE C 284  CLA C 505  DGD C 516                    
SITE     5 AD3 18 LYS I   5  TYR I   9                                          
SITE     1 AD4 16 SER A 232  ALA A 233  ASN A 234  HOH A 731                    
SITE     2 AD4 16 TRP B   5  TYR B   6  ARG B   7  PHE B 464                    
SITE     3 AD4 16 TRP B 468  CLA B 607  CLA B 611  CLA B 613                    
SITE     4 AD4 16 TYR D 141  PHE D 269  LHG L 102  PHE M  14                    
SITE     1 AD5 16 ARG A 140  TRP A 142  PHE A 273  SQD A 611                    
SITE     2 AD5 16 TRP C  36  TRP C 443  ARG C 447  CLA C 508                    
SITE     3 AD5 16 CLA C 510  DGD C 518  GLU D 219  ASN D 220                    
SITE     4 AD5 16 ALA D 229  SER D 230  THR D 231  PHE D 232                    
SITE     1 AD6  3 PRO A  57  PRO A  66  ARG O 115                               
SITE     1 AD7  8 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 AD7  8  FE A 602  HIS D 214  TYR D 244  HIS D 268                    
SITE     1 AD8  7 TRP B 185  PHE B 190  CLA B 602  LMG B 624                    
SITE     2 AD8  7 PHE H  41  LEU H  55  BCR H 101                               
SITE     1 AD9 13 GLY B 189  PHE B 190  PRO B 192  GLY B 197                    
SITE     2 AD9 13 HIS B 201  ALA B 204  VAL B 208  PHE B 247                    
SITE     3 AD9 13 PHE B 250  CLA B 601  CLA B 603  LEU D 158                    
SITE     4 AD9 13 PHE H  38                                                     
SITE     1 AE1 21 ARG B  68  LEU B  69  ALA B 146  LEU B 149                    
SITE     2 AE1 21 CYS B 150  PHE B 153  VAL B 198  HIS B 201                    
SITE     3 AE1 21 HIS B 202  PHE B 247  ALA B 248  VAL B 252                    
SITE     4 AE1 21 THR B 262  CLA B 602  CLA B 604  CLA B 605                    
SITE     5 AE1 21 CLA B 606  CLA B 608  CLA B 609  MET H  35                    
SITE     6 AE1 21 PHE H  38                                                     
SITE     1 AE2 19 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 AE2 19 LEU B 149  VAL B 245  ALA B 248  ALA B 249                    
SITE     3 AE2 19 VAL B 252  PHE B 451  HIS B 455  PHE B 458                    
SITE     4 AE2 19 CLA B 603  CLA B 605  CLA B 606  CLA B 607                    
SITE     5 AE2 19 CLA B 612  CLA B 613  CLA B 615                               
SITE     1 AE3 18 THR B  27  VAL B  30  ALA B  31  ALA B  34                    
SITE     2 AE3 18 VAL B  62  MET B  66  ARG B  68  VAL B  96                    
SITE     3 AE3 18 HIS B 100  LEU B 103  ALA B 205  CLA B 603                    
SITE     4 AE3 18 CLA B 604  CLA B 606  CLA B 609  CLA B 610                    
SITE     5 AE3 18 CLA B 612  HOH B 725                                          
SITE     1 AE4 17 LEU B  69  VAL B  71  PHE B  90  TRP B  91                    
SITE     2 AE4 17 VAL B  96  HIS B 100  LEU B 106  GLY B 152                    
SITE     3 AE4 17 PHE B 153  PHE B 156  HIS B 157  PHE B 162                    
SITE     4 AE4 17 PRO B 164  CLA B 603  CLA B 604  CLA B 605                    
SITE     5 AE4 17 BCR B 619                                                     
SITE     1 AE5 16 LHG A 613  TRP B  33  TYR B  40  GLN B  58                    
SITE     2 AE5 16 GLY B  59  PHE B  61  THR B 327  GLY B 328                    
SITE     3 AE5 16 PRO B 329  TRP B 450  CLA B 604  LMG B 620                    
SITE     4 AE5 16 HOH B 738  THR D 277  PHE M  14  BCR t 102                    
SITE     1 AE6 14 THR B 236  SER B 239  ALA B 243  PHE B 463                    
SITE     2 AE6 14 HIS B 466  ILE B 467  LEU B 474  CLA B 603                    
SITE     3 AE6 14 CLA B 609  CLA B 610  ILE D 123  MET D 126                    
SITE     4 AE6 14 CLA D 405  LEU H  43                                          
SITE     1 AE7 18 PHE B 139  VAL B 208  ALA B 212  PHE B 215                    
SITE     2 AE7 18 HIS B 216  VAL B 219  PRO B 221  PRO B 222                    
SITE     3 AE7 18 LEU B 229  CLA B 603  CLA B 605  CLA B 608                    
SITE     4 AE7 18 CLA B 610  THR H  27  MET H  31  LEU H  42                    
SITE     5 AE7 18 LEU H  43  BCR H 101                                          
SITE     1 AE8 13 LEU B 135  PHE B 139  HIS B 142  LEU B 143                    
SITE     2 AE8 13 MET B 231  VAL B 237  SER B 240  SER B 241                    
SITE     3 AE8 13 CLA B 605  CLA B 608  CLA B 609  CLA B 612                    
SITE     4 AE8 13 CLA B 615                                                     
SITE     1 AE9 19 LHG A 613  HOH A 731  TRP B   5  TYR B   6                    
SITE     2 AE9 19 ARG B   7  VAL B   8  HIS B   9  THR B  10                    
SITE     3 AE9 19 LEU B 238  LEU B 461  PHE B 462  GLY B 465                    
SITE     4 AE9 19 TRP B 468  HIS B 469  ARG B 472  CLA B 612                    
SITE     5 AE9 19 CLA B 613  CLA B 614  LHG L 102                               
SITE     1 AF1 17 HIS B   9  LEU B  19  HIS B  23  HIS B  26                    
SITE     2 AF1 17 THR B  27  VAL B 237  LEU B 238  SER B 241                    
SITE     3 AF1 17 VAL B 245  CLA B 604  CLA B 605  CLA B 610                    
SITE     4 AF1 17 CLA B 611  CLA B 613  CLA B 614  CLA B 615                    
SITE     5 AF1 17 HOH B 717                                                     
SITE     1 AF2 11 LHG A 613  HIS B   9  HIS B  26  VAL B  30                    
SITE     2 AF2 11 PHE B 462  CLA B 604  CLA B 611  CLA B 612                    
SITE     3 AF2 11 CLA B 614  BCR B 617  BCR B 618                               
SITE     1 AF3 13 VAL B   8  HIS B   9  LEU B  29  CLA B 611                    
SITE     2 AF3 13 CLA B 612  CLA B 613  BCR B 617  LMG B 620                    
SITE     3 AF3 13 GLN L   8  VAL L  10  SQD L 101  PHE M  21                    
SITE     4 AF3 13 PHE t   8                                                     
SITE     1 AF4 12 ILE B  20  HIS B  23  LEU B  24  MET B 138                    
SITE     2 AF4 12 HIS B 142  LEU B 145  CLA B 604  CLA B 610                    
SITE     3 AF4 12 CLA B 612  CLA B 616  LEU H  11  LEU H  14                    
SITE     1 AF5 10 ILE B  20  LEU B  24  TRP B 113  HIS B 114                    
SITE     2 AF5 10 CLA B 615  BCR B 619  THR H   5  LEU H   7                    
SITE     3 AF5 10 GLY H   8  HOH H 202                                          
SITE     1 AF6 11 MET B  25  LEU B  29  CLA B 613  CLA B 614                    
SITE     2 AF6 11 BCR B 618  LMG B 620  SQD L 101  LHG L 102                    
SITE     3 AF6 11 LEU M  13  PHE t  19  BCR t 102                               
SITE     1 AF7  9 LEU B  29  GLY B  32  SER B  36  SER B 104                    
SITE     2 AF7  9 GLY B 105  CLA B 613  BCR B 617  LMG a 603                    
SITE     3 AF7  9 BCR t 102                                                     
SITE     1 AF8  6 LEU B 106  LEU B 109  ALA B 110  CLA B 606                    
SITE     2 AF8  6 CLA B 616  LMG a 603                                          
SITE     1 AF9 11 THR B 327  GLY B 328  PRO B 329  CLA B 607                    
SITE     2 AF9 11 CLA B 614  BCR B 617  ILE D 284  PHE L  35                    
SITE     3 AF9 11 LHG L 102  ASN M   4  VAL M  17                               
SITE     1 AG1 10 PRO B 183  GLU B 184  TRP B 185  ILE B 207                    
SITE     2 AG1 10 CLA B 601  ILE C 170  MET C 180  LEU C 204                    
SITE     3 AG1 10 ILE C 238  CLA C 512                                          
SITE     1 AG2 17 THR C  94  LEU C  95  LEU C 168  GLY C 171                    
SITE     2 AG2 17 ALA C 172  LEU C 175  VAL C 233  HIS C 237                    
SITE     3 AG2 17 ALA C 278  MET C 282  PHE C 289  TYR C 297                    
SITE     4 AG2 17 CLA C 502  CLA C 503  CLA C 506  CLA C 507                    
SITE     5 AG2 17 BCR C 515                                                     
SITE     1 AG3 17 TRP C  63  HIS C  91  LEU C 174  LEU C 279                    
SITE     2 AG3 17 MET C 282  ALA C 286  VAL C 290  TYR C 297                    
SITE     3 AG3 17 LEU C 426  HIS C 430  LEU C 433  PHE C 437                    
SITE     4 AG3 17 CLA C 501  CLA C 503  CLA C 504  CLA C 510                    
SITE     5 AG3 17 CLA C 512                                                     
SITE     1 AG4 14 ILE C  60  VAL C  61  THR C  68  LEU C  88                    
SITE     2 AG4 14 HIS C  91  ILE C  92  VAL C 114  HIS C 118                    
SITE     3 AG4 14 CLA C 501  CLA C 502  CLA C 507  CLA C 509                    
SITE     4 AG4 14 CLA C 510  CLA C 512                                          
SITE     1 AG5 14 TRP C  63  MET C  67  PHE C  70  GLN C  84                    
SITE     2 AG5 14 GLY C  85  TRP C 425  SER C 429  PHE C 436                    
SITE     3 AG5 14 CLA C 502  DGD C 517  DGD C 518  LMG C 519                    
SITE     4 AG5 14 PRO K  26  VAL K  30                                          
SITE     1 AG6 16 PHE A  33  ILE A  36  TRP A 131  CLA A 608                    
SITE     2 AG6 16 LMG A 612  PHE C 264  TYR C 274  GLY C 277                    
SITE     3 AG6 16 HIS C 441  LEU C 442  ALA C 445  ARG C 449                    
SITE     4 AG6 16 CLA C 507  BCR C 515  HOH C 913  VAL I  16                    
SITE     1 AG7 15 CLA A 608  LEU C 165  ILE C 243  GLY C 247                    
SITE     2 AG7 15 TRP C 250  HIS C 251  THR C 255  PRO C 256                    
SITE     3 AG7 15 PHE C 257  TRP C 259  PHE C 264  CLA C 501                    
SITE     4 AG7 15 CLA C 507  BCR C 515  DGD C 516                               
SITE     1 AG8 17 MET C 157  THR C 158  LEU C 161  HIS C 164                    
SITE     2 AG8 17 LEU C 168  PHE C 264  TRP C 266  TYR C 271                    
SITE     3 AG8 17 TYR C 274  SER C 275  LEU C 279  CLA C 501                    
SITE     4 AG8 17 CLA C 503  CLA C 505  CLA C 506  CLA C 509                    
SITE     5 AG8 17 BCR C 515                                                     
SITE     1 AG9 21 SQD A 611  LHG A 614  PHE C  33  TRP C  36                    
SITE     2 AG9 21 ALA C  37  GLY C  38  ASN C  39  ALA C  40                    
SITE     3 AG9 21 LEU C 272  LEU C 276  PHE C 436  GLY C 440                    
SITE     4 AG9 21 TRP C 443  HIS C 444  ARG C 447  CLA C 509                    
SITE     5 AG9 21 CLA C 510  CLA C 511  DGD C 517  DGD C 518                    
SITE     6 AG9 21 LMG C 519                                                     
SITE     1 AH1 20 ASN C  39  LEU C  42  LEU C  49  ALA C  52                    
SITE     2 AH1 20 HIS C  53  HIS C  56  TYR C 149  ILE C 160                    
SITE     3 AH1 20 GLY C 268  GLU C 269  TYR C 271  LEU C 272                    
SITE     4 AH1 20 SER C 275  LEU C 279  CLA C 503  CLA C 507                    
SITE     5 AH1 20 CLA C 508  CLA C 510  CLA C 511  CLA C 512                    
SITE     1 AH2 15 LHG A 614  ASN C  39  HIS C  56  LEU C 279                    
SITE     2 AH2 15 PHE C 436  PHE C 437  CLA C 502  CLA C 503                    
SITE     3 AH2 15 CLA C 508  CLA C 509  CLA C 511  LMG C 519                    
SITE     4 AH2 15 PRO K  29  VAL K  30  LEU K  33                               
SITE     1 AH3 16 ARG C  26  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 AH3 16 ARG C  41  LEU C  42  LEU C  45  LYS C  48                    
SITE     3 AH3 16 PHE C 127  CLA C 508  CLA C 509  CLA C 510                    
SITE     4 AH3 16 BCR C 522  TRP K  39  GLN K  40  VAL Z  20                    
SITE     1 AH4 15 LMG B 624  HIS C  53  ALA C  57  PHE C 147                    
SITE     2 AH4 15 ILE C 160  PHE C 163  HIS C 164  ILE C 166                    
SITE     3 AH4 15 VAL C 167  GLY C 171  CLA C 502  CLA C 503                    
SITE     4 AH4 15 CLA C 509  CLA C 513  BCR C 514                               
SITE     1 AH5 10 LEU C  50  VAL C  54  VAL C 124  GLY C 128                    
SITE     2 AH5 10 TYR C 131  HIS C 132  LEU C 140  TYR C 143                    
SITE     3 AH5 10 CLA C 512  BCR C 514                                          
SITE     1 AH6  9 PHE C 112  ILE C 120  SER C 121  CLA C 512                    
SITE     2 AH6  9 CLA C 513  TYR K  15  GLY Z  55  ASN Z  58                    
SITE     3 AH6  9 PHE Z  59                                                     
SITE     1 AH7 10 ILE C 209  GLY C 236  HIS C 237  ILE C 240                    
SITE     2 AH7 10 PHE C 264  CLA C 501  CLA C 505  CLA C 506                    
SITE     3 AH7 10 CLA C 507  LEU I  24                                          
SITE     1 AH8 23 LEU A  91  PHE A 155  ILE A 163  CLA A 608                    
SITE     2 AH8 23 LMG A 612  PRO C 217  GLY C 219  GLY C 220                    
SITE     3 AH8 23 GLY C 222  TRP C 223  VAL C 225  SER C 226                    
SITE     4 AH8 23 VAL C 227  CYS C 288  ASN C 293  ASN C 294                    
SITE     5 AH8 23 THR C 295  ASP C 360  PHE C 361  ARG C 362                    
SITE     6 AH8 23 LEU C 438  CLA C 506  HOH C 903                               
SITE     1 AH9 16 PHE A 197  GLU C  83  GLN C  84  GLY C  85                    
SITE     2 AH9 16 SER C 406  ASN C 418  PHE C 419  VAL C 420                    
SITE     3 AH9 16 TRP C 425  THR C 428  SER C 429  CLA C 504                    
SITE     4 AH9 16 CLA C 508  DGD C 518  LMG C 519  TYR J  33                    
SITE     1 AI1 25 PRO A 196  GLN A 199  PHE A 300  ASN A 301                    
SITE     2 AI1 25 PHE A 302  SER A 305  CLA A 607  LHG A 614                    
SITE     3 AI1 25 ASN C 405  SER C 406  VAL C 407  ASN C 415                    
SITE     4 AI1 25 SER C 416  ASN C 418  CLA C 504  CLA C 508                    
SITE     5 AI1 25 DGD C 517  LMG D 409  HOH D 526  ALA J  32                    
SITE     6 AI1 25 TYR J  33  GLY J  37  SER J  38  SER J  39                    
SITE     7 AI1 25 GLN V  34                                                     
SITE     1 AI2  7 HIS C  74  CLA C 504  CLA C 508  CLA C 510                    
SITE     2 AI2  7 DGD C 517  GLN Y  21  ILE Y  25                               
SITE     1 AI3 10 ALA B 155  PHE B 156  THR B 159  LEU B 161                    
SITE     2 AI3 10 TRP B 185  LEU C 204  ASP C 205  PRO C 206                    
SITE     3 AI3 10 ALA C 246  TRP C 250                                          
SITE     1 AI4  6 SER C 122  ALA C 123  CLA C 511  PHE K  18                    
SITE     2 AI4  6 PHE K  32  LEU Z   9                                          
SITE     1 AI5 16 LEU A  41  ALA A  44  THR A  45  TYR A 126                    
SITE     2 AI5 16 GLN A 130  TYR A 147  GLY A 175  PRO A 279                    
SITE     3 AI5 16 VAL A 283  CLA A 606  ALA D 208  LEU D 209                    
SITE     4 AI5 16 ILE D 213  TRP D 253  PHE D 257  CLA D 403                    
SITE     1 AI6 23 ALA A 209  LEU A 210  MET A 214  PHE A 255                    
SITE     2 AI6 23 LEU A 258  CLA A 607  PL9 A 610  ALA D  41                    
SITE     3 AI6 23 ALA D  44  TRP D  48  ILE D 114  GLY D 121                    
SITE     4 AI6 23 LEU D 122  PHE D 125  GLN D 129  ASN D 142                    
SITE     5 AI6 23 PHE D 146  PHE D 153  PHE D 173  GLY D 174                    
SITE     6 AI6 23 PRO D 275  LEU D 279  CLA D 404                               
SITE     1 AI7 21 THR A  45  PHE A  48  PHE A 158  MET A 172                    
SITE     2 AI7 21 ILE A 176  THR A 179  PHE A 180  MET A 183                    
SITE     3 AI7 21 LMG A 603  CLA A 606  MET D 198  VAL D 201                    
SITE     4 AI7 21 ALA D 202  LEU D 205  LEU D 209  PHO D 401                    
SITE     5 AI7 21 CLA D 404  PL9 D 407  LHG D 408  HOH D 501                    
SITE     6 AI7 21 LHG L 102                                                     
SITE     1 AI8 22 MET A 183  PHE A 206  CLA A 606  CLA A 607                    
SITE     2 AI8 22 LEU D  45  TRP D  48  PRO D 149  VAL D 152                    
SITE     3 AI8 22 VAL D 156  PHE D 181  LEU D 182  PHE D 185                    
SITE     4 AI8 22 GLN D 186  TRP D 191  THR D 192  HIS D 197                    
SITE     5 AI8 22 GLY D 200  SER D 282  ALA D 283  VAL D 286                    
SITE     6 AI8 22 PHO D 402  CLA D 403                                          
SITE     1 AI9 14 CLA B 608  ILE D  35  PRO D  39  LEU D  43                    
SITE     2 AI9 14 LEU D  89  LEU D  90  LEU D  91  LEU D  92                    
SITE     3 AI9 14 TRP D  93  THR D 112  PHE D 113  LEU D 116                    
SITE     4 AI9 14 HIS D 117  GLY X  13                                          
SITE     1 AJ1 11 TYR D  42  LEU D  43  GLY D  46  LEU D  49                    
SITE     2 AJ1 11 THR D  50  LMG D 409  PRO F  29  THR F  30                    
SITE     3 AJ1 11 PHE F  33  VAL J  21  VAL J  25                               
SITE     1 AJ2 19 PHE A  52  MET D 199  LEU D 209  LEU D 210                    
SITE     2 AJ2 19 ILE D 213  HIS D 214  THR D 217  MET D 246                    
SITE     3 AJ2 19 TRP D 253  ALA D 260  PHE D 261  LEU D 267                    
SITE     4 AJ2 19 PHE D 270  PHE D 273  VAL D 274  CLA D 403                    
SITE     5 AJ2 19 VAL L  26  LHG L 102  PHE T  10                               
SITE     1 AJ3 18 ILE D 256  PHE D 257  ALA D 260  PHE D 261                    
SITE     2 AJ3 18 SER D 262  ASN D 263  TRP D 266  PHE D 270                    
SITE     3 AJ3 18 CLA D 403  HOH D 527  ASN L  13  THR L  15                    
SITE     4 AJ3 18 SER L  16  TYR L  18  LEU L  19  LHG L 102                    
SITE     5 AJ3 18 PHE T  17  ALA T  20                                          
SITE     1 AJ4 14 DGD C 518  TYR D  67  GLY D  70  ASN D  72                    
SITE     2 AJ4 14 PHE D  73  BCR D 406  HOH D 526  THR F  30                    
SITE     3 AJ4 14 MET F  40  GLN F  41  PHE J  28  GLY J  31                    
SITE     4 AJ4 14 ALA J  32  LEU J  36                                          
SITE     1 AJ5 10 LEU A 258  TYR A 262  ALA A 263  PL9 A 610                    
SITE     2 AJ5 10 PHE D  27  GLU E   7  PRO E   9  PHE E  10                    
SITE     3 AJ5 10 SER E  11  ARG F  19                                          
SITE     1 AJ6 16 PHE E  10  ILE E  13  ARG E  18  TYR E  19                    
SITE     2 AJ6 16 HIS E  23  THR E  26  LEU E  30  ILE F  15                    
SITE     3 AJ6 16 PHE F  16  ARG F  19  TRP F  20  HIS F  24                    
SITE     4 AJ6 16 ALA F  27  ILE F  31  ALA R  19  ILE R  23                    
SITE     1 AJ7  8 ARG D  24  ARG D  26  PHE F  16  THR F  17                    
SITE     2 AJ7  8 VAL F  18  VAL F  21  GLN R  30  THR X  24                    
SITE     1 AJ8  6 CLA B 601  CLA B 609  PHE H  34  LEU H  37                    
SITE     2 AJ8  6 PHE H  38  LEU X   7                                          
SITE     1 AJ9 16 TYR B 193  TYR B 258  TYR B 273  GLN B 274                    
SITE     2 AJ9 16 SER B 277  TYR B 279  THR B 452  HOH B 713                    
SITE     3 AJ9 16 HIS D  87  LEU D 162  TYR H  49  ASN H  50                    
SITE     4 AJ9 16 VAL H  60  SER H  61  TRP H  62  HOH H 207                    
SITE     1 AK1 13 PHE C  62  ALA J  14  THR J  15  LEU K  25                    
SITE     2 AK1 13 ILE K  28  LEU K  31  ALA K  34  VAL K  38                    
SITE     3 AK1 13 ILE Y  28  GLY Y  29  GLY Y  32  SER Z  16                    
SITE     4 AK1 13 PHE Z  17                                                     
SITE     1 AK2 11 ARG B  18  LEU B  29  SER B 104  PHE B 108                    
SITE     2 AK2 11 CLA B 614  BCR B 617  ASN L   4  ARG L   7                    
SITE     3 AK2 11 ARG l  14  TYR l  18  TYR m  26                               
SITE     1 AK3 20 SER A 232  ASN A 234  LHG A 613  PRO B   4                    
SITE     2 AK3 20 TRP B   5  TYR B   6  CLA B 611  BCR B 617                    
SITE     3 AK3 20 LMG B 620  TRP D 266  PHE D 273  CLA D 403                    
SITE     4 AK3 20 PL9 D 407  LHG D 408  GLU L  11  LEU L  12                    
SITE     5 AK3 20 ASN L  13  SER L  16  LEU L  22  LEU M  22                    
SITE     1 AK4 17 ARG L  14  LEU L  17  TYR L  18  TYR M  26                    
SITE     2 AK4 17 CYS T  12  LEU T  16  PHE T  19  PHE T  23                    
SITE     3 AK4 17 ARG b  18  SER b 104  PHE b 108  TRP b 115                    
SITE     4 AK4 17 CLA b 614  BCR b 617  BCR b 618  ASN l   4                    
SITE     5 AK4 17 ARG l   7                                                     
SITE     1 AK5  2 LYS O  69  LEU O  70                                          
SITE     1 AK6  2 PRO O  20  THR O  21                                          
SITE     1 AK7 11 LMG A 603  PHE T   8  ALA T  11  ALA T  15                    
SITE     2 AK7 11 PHE T  18  PHE T  22  TRP b  33  TYR b  40                    
SITE     3 AK7 11 CLA b 607  BCR b 617  BCR b 618                               
SITE     1 AK8  2 ASN C 327  TYR U  98                                          
SITE     1 AK9 19 ALA V  36  CYS V  37  SER V  39  CYS V  40                    
SITE     2 AK9 19 HIS V  41  THR V  46  THR V  48  ASN V  49                    
SITE     3 AK9 19 LEU V  52  ASP V  53  THR V  58  LEU V  59                    
SITE     4 AK9 19 TYR V  75  MET V  76  TYR V  82  ILE V  88                    
SITE     5 AK9 19 HIS V  92  MET V 104  HOH V 303                               
SITE     1 AL1  4 ILE V  19  THR V  20  LYS u  24  GLU u  80                    
SITE     1 AL2 12 ASP a 170  GLU a 189  HIS a 332  GLU a 333                    
SITE     2 AL2 12 HIS a 337  ASP a 342  ALA a 344  HOH a 720                    
SITE     3 AL2 12 HOH a 721  HOH a 722  GLU c 354  ARG c 357                    
SITE     1 AL3  5 HIS a 215  HIS a 272  BCT a 618  HIS d 214                    
SITE     2 AL3  5 HIS d 268                                                     
SITE     1 AL4 10 TRP B 113  BCR B 618  BCR B 619  TRP a  20                    
SITE     2 AL4 10 ASN a  26  ARG a  27  LEU a  28  THR a  45                    
SITE     3 AL4 10 CLA a 607  PHE t  22                                          
SITE     1 AL5  3 ASN a 181  GLU a 333  HOH a 719                               
SITE     1 AL6  4 HIS a 337  ASN a 338  PHE a 339  GLU c 354                    
SITE     1 AL7 19 TYR a 147  PRO a 150  SER a 153  VAL a 157                    
SITE     2 AL7 19 MET a 183  PHE a 186  GLN a 187  ILE a 192                    
SITE     3 AL7 19 HIS a 198  GLY a 201  VAL a 202  PHE a 206                    
SITE     4 AL7 19 THR a 286  ALA a 287  ILE a 290  CLA a 607                    
SITE     5 AL7 19 PHO a 609  PHE d 257  CLA d 401                               
SITE     1 AL8 20 PHE a 158  MET a 172  ILE a 176  THR a 179                    
SITE     2 AL8 20 MET a 183  LMG a 603  CLA a 606  PHO a 609                    
SITE     3 AL8 20 HOH a 705  HOH a 713  HOH a 724  MET d 198                    
SITE     4 AL8 20 VAL d 201  ALA d 202  LEU d 205  LEU d 209                    
SITE     5 AL8 20 CLA d 401  PL9 d 405  LHG d 406  LHG l 101                    
SITE     1 AL9 15 GLN a 199  VAL a 202  ALA a 203  PHE a 206                    
SITE     2 AL9 15 GLY a 207  TRP a 278  HOH a 703  DGD c 517                    
SITE     3 AL9 15 VAL d 175  ILE d 178  PHE d 179  LEU d 182                    
SITE     4 AL9 15 CLA d 401  PHO d 402  LMG d 408                               
SITE     1 AM1 17 LEU a  41  ALA a  44  THR a  45  TYR a 126                    
SITE     2 AM1 17 GLN a 130  ALA a 146  TYR a 147  GLY a 175                    
SITE     3 AM1 17 VAL a 283  CLA a 606  CLA a 607  LEU d 205                    
SITE     4 AM1 17 ALA d 208  LEU d 209  ILE d 213  TRP d 253                    
SITE     5 AM1 17 PHE d 257                                                     
SITE     1 AM2 15 PHE a  93  PRO a  95  ILE a  96  LEU a 114                    
SITE     2 AM2 15 PHE a 117  HIS a 118  LEU a 121  BCR a 611                    
SITE     3 AM2 15 CLA c 505  CLA c 506  TYR i   9  VAL i  12                    
SITE     4 AM2 15 THR i  13  PHE i  15  VAL i  16                               
SITE     1 AM3  4 ILE a  38  ALA a  43  ILE a  50  CLA a 610                    
SITE     1 AM4 19 HIS a 215  LEU a 218  HIS a 252  PHE a 255                    
SITE     2 AM4 19 SER a 264  PHE a 265  LEU a 271  LEU a 275                    
SITE     3 AM4 19 LHG a 616  PHE d  38  PRO d  39  CLA d 401                    
SITE     4 AM4 19 PHO d 402  ALA f  22  THR f  25  LEU f  26                    
SITE     5 AM4 19 SQD f 101  THR x  24  LEU x  28                               
SITE     1 AM5 16 LEU a 200  PHE a 265  SER a 270  PHE a 273                    
SITE     2 AM5 16 TRP a 278  VAL a 281  GLY a 282  GLN c  28                    
SITE     3 AM5 16 ALA c  34  TRP c  35  TRP c  36  CLA c 508                    
SITE     4 AM5 16 PHE d 232  ARG d 233  LHG d 407  ALA k  34                    
SITE     1 AM6 16 TRP a  97  GLU a  98  PHE a 117  LEU a 120                    
SITE     2 AM6 16 PHE a 155  LEU c 213  LEU c 214  LYS c 215                    
SITE     3 AM6 16 PHE c 218  GLU c 221  TRP c 223  PHE c 284                    
SITE     4 AM6 16 CLA c 505  DGD c 515  LYS i   5  TYR i   9                    
SITE     1 AM7 16 SER a 232  ALA a 233  ASN a 234  TRP b   5                    
SITE     2 AM7 16 TYR b   6  ARG b   7  PHE b 464  TRP b 468                    
SITE     3 AM7 16 CLA b 607  CLA b 611  CLA b 613  TYR d 141                    
SITE     4 AM7 16 TRP d 266  PHE d 269  LEU d 272  LHG l 101                    
SITE     1 AM8  8 LEU a 258  ILE a 259  TYR a 262  PL9 a 612                    
SITE     2 AM8  8 THR e   5  PRO e   9  PHE e  10  SER e  11                    
SITE     1 AM9  3 PRO a  57  PRO a  66  ARG o 115                               
SITE     1 AN1  8 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 AN1  8  FE a 602  HIS d 214  TYR d 244  HIS d 268                    
SITE     1 AN2  8 TRP b 185  GLY b 186  PHE b 190  CLA b 602                    
SITE     2 AN2  8 LMG b 624  PHE h  41  LEU h  55  BCR h 101                    
SITE     1 AN3 12 GLY b 189  PHE b 190  GLY b 197  HIS b 201                    
SITE     2 AN3 12 ALA b 205  VAL b 208  PHE b 250  CLA b 601                    
SITE     3 AN3 12 CLA b 603  PHE h  38  ILE h  45  DGD h 102                    
SITE     1 AN4 20 ARG b  68  LEU b  69  ALA b 146  CYS b 150                    
SITE     2 AN4 20 PHE b 153  VAL b 198  HIS b 201  HIS b 202                    
SITE     3 AN4 20 PHE b 247  ALA b 248  VAL b 252  THR b 262                    
SITE     4 AN4 20 CLA b 602  CLA b 604  CLA b 605  CLA b 606                    
SITE     5 AN4 20 CLA b 609  MET h  35  PHE h  38  BCR h 101                    
SITE     1 AN5 18 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 AN5 18 VAL b 245  ALA b 248  ALA b 249  VAL b 252                    
SITE     3 AN5 18 PHE b 451  HIS b 455  PHE b 458  PHE b 462                    
SITE     4 AN5 18 CLA b 603  CLA b 605  CLA b 607  CLA b 612                    
SITE     5 AN5 18 CLA b 613  CLA b 615                                          
SITE     1 AN6 20 THR b  27  VAL b  30  ALA b  31  TRP b  33                    
SITE     2 AN6 20 ALA b  34  VAL b  62  MET b  66  ARG b  68                    
SITE     3 AN6 20 LEU b  69  VAL b  96  HIS b 100  LEU b 103                    
SITE     4 AN6 20 LEU b 143  ALA b 205  GLY b 209  CLA b 603                    
SITE     5 AN6 20 CLA b 604  CLA b 606  CLA b 610  CLA b 612                    
SITE     1 AN7 16 LEU b  69  VAL b  71  PHE b  90  TRP b  91                    
SITE     2 AN7 16 VAL b  96  ALA b  99  HIS b 100  GLY b 152                    
SITE     3 AN7 16 PHE b 153  PHE b 156  HIS b 157  PHE b 162                    
SITE     4 AN7 16 PRO b 164  CLA b 603  CLA b 605  BCR b 619                    
SITE     1 AN8 19 BCR T 101  LHG a 615  TRP b  33  TYR b  40                    
SITE     2 AN8 19 GLN b  58  GLY b  59  PHE b  61  LEU b 324                    
SITE     3 AN8 19 THR b 327  GLY b 328  PRO b 329  TRP b 450                    
SITE     4 AN8 19 CLA b 604  BCR b 618  LMG b 620  HOH b 701                    
SITE     5 AN8 19 THR d 277  MET d 281  PHE m  14                               
SITE     1 AN9 14 THR b 236  SER b 239  ALA b 243  PHE b 463                    
SITE     2 AN9 14 HIS b 466  CLA b 609  CLA b 610  PHE d 120                    
SITE     3 AN9 14 ILE d 123  MET d 126  LEU d 127  CLA d 403                    
SITE     4 AN9 14 LEU h  43  DGD h 102                                          
SITE     1 AO1 14 PHE b 139  ALA b 212  PHE b 215  HIS b 216                    
SITE     2 AO1 14 VAL b 219  PRO b 221  PRO b 222  LEU b 229                    
SITE     3 AO1 14 CLA b 603  CLA b 608  CLA b 610  THR h  27                    
SITE     4 AO1 14 MET h  31  BCR h 101                                          
SITE     1 AO2 14 LEU b 135  PHE b 139  HIS b 142  LEU b 143                    
SITE     2 AO2 14 MET b 231  VAL b 237  SER b 240  SER b 241                    
SITE     3 AO2 14 CLA b 605  CLA b 608  CLA b 609  CLA b 612                    
SITE     4 AO2 14 CLA b 615  HOH b 719                                          
SITE     1 AO3 17 LHG a 615  TRP b   5  TYR b   6  ARG b   7                    
SITE     2 AO3 17 VAL b   8  HIS b   9  THR b  10  LEU b 461                    
SITE     3 AO3 17 PHE b 462  GLY b 465  TRP b 468  HIS b 469                    
SITE     4 AO3 17 ARG b 472  CLA b 612  CLA b 613  CLA b 614                    
SITE     5 AO3 17 LHG l 101                                                     
SITE     1 AO4 17 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 AO4 17 THR b  27  VAL b 237  LEU b 238  SER b 241                    
SITE     3 AO4 17 VAL b 245  CLA b 604  CLA b 605  CLA b 610                    
SITE     4 AO4 17 CLA b 611  CLA b 613  CLA b 614  CLA b 615                    
SITE     5 AO4 17 HOH b 703                                                     
SITE     1 AO5 12 LHG a 615  HIS b   9  HIS b  26  VAL b  30                    
SITE     2 AO5 12 PHE b 462  CLA b 604  CLA b 611  CLA b 612                    
SITE     3 AO5 12 CLA b 614  BCR b 618  LMG b 620  PHE m  14                    
SITE     1 AO6 12 SQD L 103  PHE T   8  VAL b   8  HIS b   9                    
SITE     2 AO6 12 LEU b  29  CLA b 611  CLA b 612  CLA b 613                    
SITE     3 AO6 12 BCR b 617  LMG b 620  VAL l  10  PHE m  21                    
SITE     1 AO7 12 HIS b  23  LEU b  24  MET b 138  ILE b 141                    
SITE     2 AO7 12 HIS b 142  LEU b 145  CLA b 604  CLA b 610                    
SITE     3 AO7 12 CLA b 612  CLA b 616  BCR b 619  LEU h  14                    
SITE     1 AO8  8 ILE b  20  LEU b  24  ALA b 110  TRP b 113                    
SITE     2 AO8  8 HIS b 114  CLA b 615  BCR b 619  THR h   5                    
SITE     1 AO9  8 SQD L 103  PHE T  19  BCR T 101  MET b  25                    
SITE     2 AO9  8 LEU b  29  TRP b 115  CLA b 614  LMG b 620                    
SITE     1 AP1  8 SQD L 103  BCR T 101  LEU b  29  GLY b  32                    
SITE     2 AP1  8 SER b  36  GLY b 105  CLA b 607  CLA b 613                    
SITE     1 AP2  8 LMG A 603  LEU b 106  LEU b 109  ALA b 110                    
SITE     2 AP2  8 TYR b 117  CLA b 606  CLA b 615  CLA b 616                    
SITE     1 AP3 13 THR b 327  GLY b 328  PRO b 329  LYS b 332                    
SITE     2 AP3 13 CLA b 607  CLA b 613  CLA b 614  BCR b 617                    
SITE     3 AP3 13 LHG l 101  ASN m   4  LEU m   6  ALA m  10                    
SITE     4 AP3 13 PHE m  14                                                     
SITE     1 AP4 10 PRO b 183  GLU b 184  TRP b 185  ALA b 204                    
SITE     2 AP4 10 CLA b 601  MET c 180  THR c 200  LEU c 204                    
SITE     3 AP4 10 ILE c 238  LMG c 520                                          
SITE     1 AP5 17 THR c  94  LEU c  95  LEU c 168  GLY c 171                    
SITE     2 AP5 17 ALA c 172  LEU c 175  VAL c 233  HIS c 237                    
SITE     3 AP5 17 ILE c 240  MET c 282  VAL c 296  TYR c 297                    
SITE     4 AP5 17 CLA c 502  CLA c 503  CLA c 506  CLA c 507                    
SITE     5 AP5 17 BCR c 514                                                     
SITE     1 AP6 16 TRP c  63  HIS c  91  LEU c 174  LEU c 279                    
SITE     2 AP6 16 MET c 282  ALA c 286  VAL c 290  TYR c 297                    
SITE     3 AP6 16 HIS c 430  LEU c 433  PHE c 437  CLA c 501                    
SITE     4 AP6 16 CLA c 503  CLA c 504  CLA c 510  CLA c 512                    
SITE     1 AP7 14 VAL c  61  ALA c  64  THR c  68  LEU c  88                    
SITE     2 AP7 14 HIS c  91  ILE c  92  VAL c 114  HIS c 118                    
SITE     3 AP7 14 CLA c 501  CLA c 502  CLA c 507  CLA c 509                    
SITE     4 AP7 14 CLA c 510  CLA c 513                                          
SITE     1 AP8 17 TRP c  63  MET c  67  PHE c  70  GLN c  84                    
SITE     2 AP8 17 GLY c  85  TRP c 425  SER c 429  VAL c 432                    
SITE     3 AP8 17 PHE c 436  CLA c 502  CLA c 508  DGD c 516                    
SITE     4 AP8 17 DGD c 517  LMG c 518  LHG d 407  PRO k  26                    
SITE     5 AP8 17 VAL k  30                                                     
SITE     1 AP9 14 PHE a  33  TRP a 131  CLA a 610  LMG a 614                    
SITE     2 AP9 14 PHE c 264  TYR c 274  GLY c 277  HIS c 441                    
SITE     3 AP9 14 ALA c 445  ARG c 449  CLA c 507  BCR c 514                    
SITE     4 AP9 14 HOH c 607  VAL i  16                                          
SITE     1 AQ1 16 CLA a 610  LEU c 165  LEU c 213  ILE c 243                    
SITE     2 AQ1 16 GLY c 247  TRP c 250  HIS c 251  THR c 255                    
SITE     3 AQ1 16 PRO c 256  PHE c 257  TRP c 259  ALA c 260                    
SITE     4 AQ1 16 PHE c 264  CLA c 501  CLA c 507  BCR c 514                    
SITE     1 AQ2 19 MET c 157  LEU c 161  HIS c 164  LEU c 165                    
SITE     2 AQ2 19 LEU c 168  CYS c 244  PHE c 264  TRP c 266                    
SITE     3 AQ2 19 TYR c 271  TYR c 274  SER c 275  ALA c 278                    
SITE     4 AQ2 19 LEU c 279  MET c 282  CLA c 501  CLA c 503                    
SITE     5 AQ2 19 CLA c 505  CLA c 506  CLA c 509                               
SITE     1 AQ3 21 SQD a 613  PHE c  33  TRP c  36  ALA c  37                    
SITE     2 AQ3 21 GLY c  38  ASN c  39  ALA c  40  LEU c 272                    
SITE     3 AQ3 21 LEU c 276  PHE c 436  PHE c 437  GLY c 440                    
SITE     4 AQ3 21 TRP c 443  HIS c 444  ARG c 447  CLA c 504                    
SITE     5 AQ3 21 CLA c 509  CLA c 510  CLA c 511  LMG c 518                    
SITE     6 AQ3 21 LHG d 407                                                     
SITE     1 AQ4 19 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 AQ4 19 HIS c  56  TYR c 149  TRP c 151  ILE c 160                    
SITE     3 AQ4 19 GLY c 268  TYR c 271  LEU c 272  SER c 275                    
SITE     4 AQ4 19 LEU c 279  CLA c 503  CLA c 507  CLA c 508                    
SITE     5 AQ4 19 CLA c 510  CLA c 511  CLA c 512                               
SITE     1 AQ5 14 ASN c  39  HIS c  56  LEU c  59  LEU c 279                    
SITE     2 AQ5 14 PHE c 436  PHE c 437  CLA c 502  CLA c 503                    
SITE     3 AQ5 14 CLA c 508  CLA c 509  CLA c 511  LHG d 407                    
SITE     4 AQ5 14 PRO k  29  LEU k  33                                          
SITE     1 AQ6 20 ARG c  26  TRP c  35  GLY c  38  ASN c  39                    
SITE     2 AQ6 20 ARG c  41  LEU c  42  LEU c  45  LYS c  48                    
SITE     3 AQ6 20 ALA c  52  GLY c 126  PHE c 127  ILE c 134                    
SITE     4 AQ6 20 CLA c 508  CLA c 509  CLA c 510  BCR c 521                    
SITE     5 AQ6 20 TRP k  39  GLN k  40  ASN y  45  ALA z  28                    
SITE     1 AQ7 12 HIS c  53  ALA c  57  PHE c 147  ILE c 160                    
SITE     2 AQ7 12 PHE c 163  HIS c 164  VAL c 167  GLY c 171                    
SITE     3 AQ7 12 CLA c 502  CLA c 509  CLA c 513  BCR z 101                    
SITE     1 AQ8 13 LEU c  50  VAL c  54  VAL c 124  LEU c 125                    
SITE     2 AQ8 13 GLY c 128  TYR c 131  HIS c 132  LEU c 140                    
SITE     3 AQ8 13 TYR c 143  PHE c 147  CLA c 503  CLA c 512                    
SITE     4 AQ8 13 BCR z 101                                                     
SITE     1 AQ9 11 ILE c 209  LEU c 213  ASP c 232  GLY c 236                    
SITE     2 AQ9 11 HIS c 237  PHE c 264  CLA c 501  CLA c 505                    
SITE     3 AQ9 11 CLA c 506  VAL i  20  LEU i  24                               
SITE     1 AR1 22 LEU a  91  SER a 148  ALA a 152  PHE a 155                    
SITE     2 AR1 22 ILE a 163  LMG a 614  PRO c 217  GLY c 219                    
SITE     3 AR1 22 GLY c 220  GLU c 221  GLY c 222  TRP c 223                    
SITE     4 AR1 22 VAL c 225  VAL c 227  CYS c 288  PHE c 292                    
SITE     5 AR1 22 ASN c 293  ASN c 294  THR c 295  ASP c 360                    
SITE     6 AR1 22 PHE c 361  ARG c 362                                          
SITE     1 AR2 17 HIS a 195  PHE a 197  GLU c  83  GLN c  84                    
SITE     2 AR2 17 GLY c  85  LEU c 404  SER c 406  ASN c 418                    
SITE     3 AR2 17 PHE c 419  VAL c 420  TRP c 425  THR c 428                    
SITE     4 AR2 17 CLA c 504  DGD c 517  LMG c 518  PHE j  29                    
SITE     5 AR2 17 TYR j  33                                                     
SITE     1 AR3 18 LEU a 200  ASN a 301  PHE a 302  SER a 305                    
SITE     2 AR3 18 CLA a 608  ASN c 405  ASN c 415  SER c 416                    
SITE     3 AR3 18 ASN c 418  CLA c 504  DGD c 516  LMG d 408                    
SITE     4 AR3 18 ALA j  32  TYR j  33  GLY j  37  SER j  38                    
SITE     5 AR3 18 SER j  39  GLN v  34                                          
SITE     1 AR4  5 HIS c  74  CLA c 504  CLA c 508  DGD c 516                    
SITE     2 AR4  5 ASP k  23                                                     
SITE     1 AR5 11 ALA b 155  THR b 159  TRP b 185  LMG b 624                    
SITE     2 AR5 11 LEU c 204  ASP c 205  PRO c 206  ARG c 207                    
SITE     3 AR5 11 TRP c 239  ILE c 243  HOH c 602                               
SITE     1 AR6  7 SER c 122  ALA c 123  CLA c 511  PHE k  18                    
SITE     2 AR6  7 PHE k  32  BCR k 102  LEU z   9                               
SITE     1 AR7 21 MET a 183  PHE a 206  CLA a 606  CLA a 607                    
SITE     2 AR7 21 CLA a 608  PL9 a 612  TRP d  48  PRO d 149                    
SITE     3 AR7 21 VAL d 152  VAL d 156  LEU d 182  PHE d 185                    
SITE     4 AR7 21 GLN d 186  TRP d 191  THR d 192  HIS d 197                    
SITE     5 AR7 21 GLY d 200  SER d 282  ALA d 283  VAL d 286                    
SITE     6 AR7 21 PHO d 402                                                     
SITE     1 AR8 23 PHE a 206  ALA a 209  LEU a 210  MET a 214                    
SITE     2 AR8 23 LEU a 258  CLA a 608  PL9 a 612  ALA d  41                    
SITE     3 AR8 23 LEU d  45  ILE d 114  GLY d 121  LEU d 122                    
SITE     4 AR8 23 PHE d 125  GLN d 129  ASN d 142  PHE d 146                    
SITE     5 AR8 23 PRO d 149  PHE d 153  PHE d 173  GLY d 174                    
SITE     6 AR8 23 PRO d 275  LEU d 279  CLA d 401                               
SITE     1 AR9 15 CLA b 608  CYS d  40  LEU d  43  LEU d  89                    
SITE     2 AR9 15 LEU d  90  LEU d  91  LEU d  92  TRP d  93                    
SITE     3 AR9 15 THR d 112  PHE d 113  LEU d 116  HIS d 117                    
SITE     4 AR9 15 VAL h  33  LEU h  37  GLY x  13                               
SITE     1 AS1 11 TYR d  42  LEU d  43  GLY d  46  LEU d  49                    
SITE     2 AS1 11 THR d  50  LMG d 408  PRO f  29  THR f  30                    
SITE     3 AS1 11 PHE f  33  VAL j  21  VAL j  25                               
SITE     1 AS2 17 ILE a  77  CLA a 607  MET d 198  MET d 199                    
SITE     2 AS2 17 LEU d 210  HIS d 214  THR d 217  TRP d 253                    
SITE     3 AS2 17 ALA d 260  PHE d 261  VAL d 274  LHG d 406                    
SITE     4 AS2 17 VAL l  26  LEU l  27  LEU l  29  LHG l 101                    
SITE     5 AS2 17 PHE t  10                                                     
SITE     1 AS3 17 CLA a 607  PHE d 257  ALA d 260  PHE d 261                    
SITE     2 AS3 17 SER d 262  ASN d 263  TRP d 266  PHE d 270                    
SITE     3 AS3 17 PL9 d 405  ASN l  13  THR l  15  SER l  16                    
SITE     4 AS3 17 TYR l  18  LEU l  19  LHG l 101  PHE t  17                    
SITE     5 AS3 17 ALA t  20                                                     
SITE     1 AS4 19 ARG a 140  TRP a 142  ALA a 146  PHE a 273                    
SITE     2 AS4 19 TRP a 284  SQD a 613  TRP c  36  TRP c 443                    
SITE     3 AS4 19 ARG c 447  CLA c 504  CLA c 508  CLA c 510                    
SITE     4 AS4 19 GLU d 219  ASN d 220  ALA d 229  SER d 230                    
SITE     5 AS4 19 THR d 231  PHE d 232  HOH d 508                               
SITE     1 AS5 14 CLA a 608  DGD c 517  TYR d  67  GLY d  70                    
SITE     2 AS5 14 ASN d  72  PHE d  73  BCR d 404  THR f  30                    
SITE     3 AS5 14 MET f  40  GLN f  41  PHE j  28  GLY j  31                    
SITE     4 AS5 14 ALA j  32  LEU j  36                                          
SITE     1 AS6  3 GLY d 226  GLU d 227  GLY d 228                               
SITE     1 AS7 16 PHE e  10  ILE e  13  ARG e  18  TYR e  19                    
SITE     2 AS7 16 ILE e  22  HIS e  23  THR e  26  ILE f  15                    
SITE     3 AS7 16 PHE f  16  ARG f  19  TRP f  20  HIS f  24                    
SITE     4 AS7 16 ALA f  27  ILE f  31  ALA r  19  ILE r  23                    
SITE     1 AS8 10 PL9 a 612  TRP d  21  ARG d  24  ARG d  26                    
SITE     2 AS8 10 PHE f  16  THR f  17  VAL f  18  GLN r  30                    
SITE     3 AS8 10 LEU r  34  ASP x  35                                          
SITE     1 AS9 11 CLA b 601  CLA b 603  CLA b 609  MET h  35                    
SITE     2 AS9 11 LEU h  37  PHE h  38  PHE h  41  LEU h  55                    
SITE     3 AS9 11 THR x   2  ILE x   3  LEU x   7                               
SITE     1 AT1 19 TYR b 193  PHE b 250  TYR b 258  TYR b 273                    
SITE     2 AT1 19 GLN b 274  SER b 277  TYR b 279  PHE b 463                    
SITE     3 AT1 19 CLA b 602  CLA b 608  HOH b 723  HIS d  87                    
SITE     4 AT1 19 LEU d 162  GLY d 163  TYR h  49  ASN h  50                    
SITE     5 AT1 19 VAL h  60  SER h  61  TRP h  62                               
SITE     1 AT2 14 PHE c  62  BCR c 521  ALA j  14  THR j  15                    
SITE     2 AT2 14 ILE k  28  LEU k  31  ALA k  34  VAL k  38                    
SITE     3 AT2 14 ILE y  28  GLY y  29  GLY y  32  SER z  16                    
SITE     4 AT2 14 PHE z  17  VAL z  20                                          
SITE     1 AT3 20 SER a 232  ASN a 234  CLA a 607  LHG a 615                    
SITE     2 AT3 20 PRO b   4  TRP b   5  TYR b   6  CLA b 611                    
SITE     3 AT3 20 LMG b 620  TRP d 266  PHE d 273  PL9 d 405                    
SITE     4 AT3 20 LHG d 406  GLU l  11  LEU l  12  ASN l  13                    
SITE     5 AT3 20 SER l  16  GLY l  20  VAL l  26  PHE m  21                    
SITE     1 AT4  2 PRO o  20  THR o  21                                          
SITE     1 AT5  8 TRP B  33  SER B  36  CLA B 607  BCR B 617                    
SITE     2 AT5  8 BCR B 618  ALA t  11  PHE t  17  PHE t  18                    
SITE     1 AT6  3 ASN c 327  LYS u  51  TYR u  98                               
SITE     1 AT7  1 GLU u  23                                                     
SITE     1 AT8  9 PHE c 112  ILE c 120  SER c 121  LEU c 125                    
SITE     2 AT8  9 PHE c 147  CLA c 512  CLA c 513  VAL z  51                    
SITE     3 AT8  9 GLY z  55                                                     
SITE     1 AT9 20 ALA v  36  CYS v  37  ALA v  38  SER v  39                    
SITE     2 AT9 20 HIS v  41  VAL v  42  ILE v  45  THR v  46                    
SITE     3 AT9 20 LYS v  47  THR v  48  ASN v  49  LEU v  52                    
SITE     4 AT9 20 ASP v  53  THR v  58  LEU v  72  TYR v  75                    
SITE     5 AT9 20 MET v  76  TYR v  82  HIS v  92  MET v 104                    
SITE     1 AU1 18 PHE v  33  ALA v  36  ALA v  38  SER v  39                    
SITE     2 AU1 18 CYS v  40  HIS v  41  THR v  46  THR v  48                    
SITE     3 AU1 18 ASN v  49  LEU v  52  ASP v  53  THR v  58                    
SITE     4 AU1 18 LEU v  72  TYR v  75  MET v  76  TYR v  82                    
SITE     5 AU1 18 HIS v  92  MET v 104                                          
CRYST1  116.447  218.889  302.202  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.008588  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004569  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003309        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system