GenomeNet

Database: PDB
Entry: 5KAF
LinkDB: 5KAF
Original site: 5KAF 
HEADER    ELECTRON TRANSPORT                      01-JUN-16   5KAF              
TITLE     RT XFEL STRUCTURE OF PHOTOSYSTEM II IN THE DARK STATE AT 3.0 A        
TITLE    2 RESOLUTION                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;                               
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 1-344;                                        
COMPND   5 SYNONYM: PSII D1 PROTEIN 1,PHOTOSYSTEM II Q(B) PROTEIN 1;            
COMPND   6 EC: 1.10.3.9;                                                        
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOTOSYSTEM II CP47 REACTION CENTER PROTEIN;               
COMPND   9 CHAIN: B, b;                                                         
COMPND  10 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;                          
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;               
COMPND  13 CHAIN: C, c;                                                         
COMPND  14 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;                          
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  17 CHAIN: D, d;                                                         
COMPND  18 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II 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 MOL_ID: 6;                                                           
COMPND  25 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  26 CHAIN: F, f;                                                         
COMPND  27 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  28 MOL_ID: 7;                                                           
COMPND  29 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  30 CHAIN: H, h;                                                         
COMPND  31 SYNONYM: PSII-H;                                                     
COMPND  32 MOL_ID: 8;                                                           
COMPND  33 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  34 CHAIN: I, i;                                                         
COMPND  35 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;                                
COMPND  36 MOL_ID: 9;                                                           
COMPND  37 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  38 CHAIN: J, j;                                                         
COMPND  39 SYNONYM: PSII-J;                                                     
COMPND  40 MOL_ID: 10;                                                          
COMPND  41 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  42 CHAIN: K, k;                                                         
COMPND  43 SYNONYM: PSII-K;                                                     
COMPND  44 MOL_ID: 11;                                                          
COMPND  45 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  46 CHAIN: L, l;                                                         
COMPND  47 SYNONYM: PSII-L;                                                     
COMPND  48 MOL_ID: 12;                                                          
COMPND  49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN M;                  
COMPND  50 CHAIN: M, m;                                                         
COMPND  51 SYNONYM: PSII-M;                                                     
COMPND  52 MOL_ID: 13;                                                          
COMPND  53 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  54 CHAIN: O, o;                                                         
COMPND  55 SYNONYM: MSP;                                                        
COMPND  56 MOL_ID: 14;                                                          
COMPND  57 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  58 CHAIN: T, t;                                                         
COMPND  59 SYNONYM: PSII-TC;                                                    
COMPND  60 MOL_ID: 15;                                                          
COMPND  61 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  62 CHAIN: U, u;                                                         
COMPND  63 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;              
COMPND  64 MOL_ID: 16;                                                          
COMPND  65 MOLECULE: CYTOCHROME C-550;                                          
COMPND  66 CHAIN: V, v;                                                         
COMPND  67 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND  68 MOL_ID: 17;                                                          
COMPND  69 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  70 CHAIN: Y, y;                                                         
COMPND  71 MOL_ID: 18;                                                          
COMPND  72 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  73 CHAIN: X, x;                                                         
COMPND  74 MOL_ID: 19;                                                          
COMPND  75 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  76 CHAIN: Z, z;                                                         
COMPND  77 SYNONYM: PSII-Z;                                                     
COMPND  78 MOL_ID: 20;                                                          
COMPND  79 MOLECULE: PHOTOSYSTEM II PROTEIN Y;                                  
COMPND  80 CHAIN: R, r                                                          
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   3 ORGANISM_TAXID: 197221;                                              
SOURCE   4 STRAIN: BP-1;                                                        
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE   7 ORGANISM_TAXID: 197221;                                              
SOURCE   8 STRAIN: BP-1;                                                        
SOURCE   9 MOL_ID: 3;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  11 ORGANISM_TAXID: 197221;                                              
SOURCE  12 STRAIN: BP-1;                                                        
SOURCE  13 MOL_ID: 4;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  15 ORGANISM_TAXID: 197221;                                              
SOURCE  16 STRAIN: BP-1;                                                        
SOURCE  17 MOL_ID: 5;                                                           
SOURCE  18 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  19 ORGANISM_TAXID: 197221;                                              
SOURCE  20 STRAIN: BP-1;                                                        
SOURCE  21 MOL_ID: 6;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  23 ORGANISM_TAXID: 197221;                                              
SOURCE  24 STRAIN: BP-1;                                                        
SOURCE  25 MOL_ID: 7;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  27 ORGANISM_TAXID: 197221;                                              
SOURCE  28 STRAIN: BP-1;                                                        
SOURCE  29 MOL_ID: 8;                                                           
SOURCE  30 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  31 ORGANISM_TAXID: 197221;                                              
SOURCE  32 STRAIN: BP-1;                                                        
SOURCE  33 MOL_ID: 9;                                                           
SOURCE  34 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  35 ORGANISM_TAXID: 197221;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  43 ORGANISM_TAXID: 197221;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  47 ORGANISM_TAXID: 197221;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  55 ORGANISM_TAXID: 197221;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  59 ORGANISM_TAXID: 197221;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  63 ORGANISM_TAXID: 197221;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  67 ORGANISM_TAXID: 197221;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  71 ORGANISM_TAXID: 197221;                                              
SOURCE  72 STRAIN: BP-1;                                                        
SOURCE  73 MOL_ID: 19;                                                          
SOURCE  74 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  75 ORGANISM_TAXID: 197221;                                              
SOURCE  76 STRAIN: BP-1;                                                        
SOURCE  77 MOL_ID: 20;                                                          
SOURCE  78 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  79 ORGANISM_TAXID: 197221;                                              
SOURCE  80 STRAIN: BP-1                                                         
KEYWDS    PHOTOSYSTEMS, TRANSMEMBRANE, ROOM TEMPERATURE, ELECTRON TRANSPORT     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.D.YOUNG,M.IBRAHIM,R.CHATTERJEE,S.GUL,S.KOROIDOV,A.S.BREWSTER,       
AUTHOR   2 R.TRAN,R.ALONSO-MORI,F.FULLER,T.KROLL,T.MICHELS-CLARK,H.LAKSMONO,    
AUTHOR   3 R.G.SIERRA,C.A.STAN,C.SARACINI,M.A.BEAN,I.SEUFFERT,D.SOKARAS,T.-     
AUTHOR   4 C.WENG,M.S.HUNTER,A.AQUILA,J.E.KOGLIN,J.ROBINSON,M.LIANG,S.BOUTET,   
AUTHOR   5 A.Y.LYUBIMOV,M.UERVIROJNANGKOORN,N.W.MORIARTY,D.LIEBSCHNER,          
AUTHOR   6 P.V.AFONINE,D.G.WATERMAN,G.EVANS,H.DOBBEK,W.I.WEIS,A.T.BRUNGER,      
AUTHOR   7 P.H.ZWART,P.D.ADAMS,A.ZOUNI,J.MESSINGER,U.BERGMANN,N.K.SAUTER,       
AUTHOR   8 J.KERN,V.K.YACHANDRA,J.YANO                                          
REVDAT   5   20-NOV-19 5KAF    1       REMARK                                   
REVDAT   4   27-SEP-17 5KAF    1       REMARK                                   
REVDAT   3   28-DEC-16 5KAF    1       JRNL                                     
REVDAT   2   14-DEC-16 5KAF    1       JRNL                                     
REVDAT   1   23-NOV-16 5KAF    0                                                
JRNL        AUTH   I.D.YOUNG,M.IBRAHIM,R.CHATTERJEE,S.GUL,F.D.FULLER,           
JRNL        AUTH 2 S.KOROIDOV,A.S.BREWSTER,R.TRAN,R.ALONSO-MORI,T.KROLL,        
JRNL        AUTH 3 T.MICHELS-CLARK,H.LAKSMONO,R.G.SIERRA,C.A.STAN,R.HUSSEIN,    
JRNL        AUTH 4 M.ZHANG,L.DOUTHIT,M.KUBIN,C.DE LICHTENBERG,L.VO PHAM,        
JRNL        AUTH 5 H.NILSSON,M.H.CHEAH,D.SHEVELA,C.SARACINI,M.A.BEAN,           
JRNL        AUTH 6 I.SEUFFERT,D.SOKARAS,T.C.WENG,E.PASTOR,C.WENINGER,           
JRNL        AUTH 7 T.FRANSSON,L.LASSALLE,P.BRAUER,P.ALLER,P.T.DOCKER,B.ANDI,    
JRNL        AUTH 8 A.M.ORVILLE,J.M.GLOWNIA,S.NELSON,M.SIKORSKI,D.ZHU,           
JRNL        AUTH 9 M.S.HUNTER,T.J.LANE,A.AQUILA,J.E.KOGLIN,J.ROBINSON,M.LIANG,  
JRNL        AUTH10 S.BOUTET,A.Y.LYUBIMOV,M.UERVIROJNANGKOORN,N.W.MORIARTY,      
JRNL        AUTH11 D.LIEBSCHNER,P.V.AFONINE,D.G.WATERMAN,G.EVANS,P.WERNET,      
JRNL        AUTH12 H.DOBBEK,W.I.WEIS,A.T.BRUNGER,P.H.ZWART,P.D.ADAMS,A.ZOUNI,   
JRNL        AUTH13 J.MESSINGER,U.BERGMANN,N.K.SAUTER,J.KERN,V.K.YACHANDRA,      
JRNL        AUTH14 J.YANO                                                       
JRNL        TITL   STRUCTURE OF PHOTOSYSTEM II AND SUBSTRATE BINDING AT ROOM    
JRNL        TITL 2 TEMPERATURE.                                                 
JRNL        REF    NATURE                        V. 540   453 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27871088                                                     
JRNL        DOI    10.1038/NATURE20161                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   P.V.AFONINE,R.W.GROSSE-KUNSTLEVE,N.ECHOLS,J.J.HEADD,         
REMARK   1  AUTH 2 N.W.MORIARTY,M.MUSTYAKIMOV,T.C.TERWILLIGER,A.URZHUMTSEV,     
REMARK   1  AUTH 3 P.H.ZWART,P.D.ADAMS                                          
REMARK   1  TITL   TOWARDS AUTOMATED CRYSTALLOGRAPHIC STRUCTURE REFINEMENT WITH 
REMARK   1  TITL 2 PHENIX.REFINE.                                               
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  68   352 2012              
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   22505256                                                     
REMARK   1  DOI    10.1107/S0907444912001308                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   P.D.ADAMS,P.V.AFONINE,G.BUNKOCZI,V.B.CHEN,I.W.DAVIS,         
REMARK   1  AUTH 2 N.ECHOLS,J.J.HEADD,L.W.HUNG,G.J.KAPRAL,R.W.GROSSE-KUNSTLEVE, 
REMARK   1  AUTH 3 A.J.MCCOY,N.W.MORIARTY,R.OEFFNER,R.J.READ,D.C.RICHARDSON,    
REMARK   1  AUTH 4 J.S.RICHARDSON,T.C.TERWILLIGER,P.H.ZWART                     
REMARK   1  TITL   PHENIX: A COMPREHENSIVE PYTHON-BASED SYSTEM FOR              
REMARK   1  TITL 2 MACROMOLECULAR STRUCTURE SOLUTION.                           
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V.  66   213 2010              
REMARK   1  REFN                   ESSN 1399-0047                               
REMARK   1  PMID   20124702                                                     
REMARK   1  DOI    10.1107/S0907444909052925                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2411                                      
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 : GEOSTD + MONOMER LIBRARY + CDL V1.2           
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.12                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.326                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 168044                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.264                           
REMARK   3   R VALUE            (WORKING SET) : 0.264                           
REMARK   3   FREE R VALUE                     : 0.303                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1446                            
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 43.1275 -  6.4568    1.00    17986   156  0.2252 0.2403        
REMARK   3     2  6.4568 -  5.1276    1.00    17493   150  0.2383 0.2754        
REMARK   3     3  5.1276 -  4.4802    1.00    17370   150  0.2267 0.2744        
REMARK   3     4  4.4802 -  4.0710    1.00    17209   149  0.2466 0.3047        
REMARK   3     5  4.0710 -  3.7793    0.99    17164   148  0.2705 0.3059        
REMARK   3     6  3.7793 -  3.5566    0.99    16987   146  0.2923 0.3117        
REMARK   3     7  3.5566 -  3.3786    0.96    16534   145  0.3155 0.3789        
REMARK   3     8  3.3786 -  3.2316    0.93    16060   143  0.3362 0.3925        
REMARK   3     9  3.2316 -  3.1072    0.89    15313   131  0.3431 0.3911        
REMARK   3    10  3.1072 -  3.0000    0.84    14482   128  0.3387 0.3656        
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)     : 0.503            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.152           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 61.05                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.33                          
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      :  0.002          51870                                  
REMARK   3   ANGLE     :  0.487          71186                                  
REMARK   3   CHIRALITY :  0.037           7058                                  
REMARK   3   PLANARITY :  0.004           8596                                  
REMARK   3   DIHEDRAL  : 18.937          18203                                  
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 5KAF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000221806.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-NOV-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 293                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER                
REMARK 200  BEAMLINE                       : CXI                                
REMARK 200  X-RAY GENERATOR MODEL          : SLAC LCLS BEAMLINE CXI             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.7493                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : 1 MICRON KB MIRROR                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : CS-PAD CXI-1                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL                         
REMARK 200  DATA SCALING SOFTWARE          : CCTBX.PRIME                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 170444                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.124                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 8.480                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.5050                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.91                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.257                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PSII MONOMER COMPOSED OF 4UB6 MONOMER AND            
REMARK 200  ADDITIONAL CHAIN FROM 4PJ0                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.69                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL GROWTH WAS AS DESCRIBED IN       
REMARK 280  KERN ET AL. 2005, BIOCHIM. BIOPHYS. ACTA-BIOENERGETICS AND          
REMARK 280  IBRAHIM ET AL. 2015, STRUCT. DYN. 2 (4), 041705, SUBSTITUTING       
REMARK 280  C12E8 FOR BETA-DM AND BETAINE FOR GLYCEROL., PH 7.5, BATCH MODE,    
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       58.86550            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      165.40900            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      111.90750            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      165.40900            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.86550            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      111.90750            
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 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: R, a, b, c, d, e, f, h, i, j,         
REMARK 350                    AND CHAINS: k, l, m, o, t, u, v, y, x,            
REMARK 350                    AND CHAINS: z, r                                  
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     MET B     1                                                      
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     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     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     GLY E     3                                                      
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     MET H     1                                                      
REMARK 465     LEU H    65                                                      
REMARK 465     GLY H    66                                                      
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     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 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     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     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     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 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     MET b     1                                                      
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     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     MET e     1                                                      
REMARK 465     ALA e     2                                                      
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     MET h     1                                                      
REMARK 465     LEU h    65                                                      
REMARK 465     GLY h    66                                                      
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     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 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     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     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     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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 485    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 489    CG   CD   OE1  OE2                                  
REMARK 470     VAL B 502    CG1  CG2                                            
REMARK 470     ARG B 505    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS D 336    O                                                   
REMARK 470     LYS E  84    CG   CD   CE   NZ                                   
REMARK 470     SER F  12    OG                                                  
REMARK 470     MET L   1    CG   SD   CE                                        
REMARK 470     GLN M  33    CG   CD   OE1  NE2                                  
REMARK 470     GLN O   3    CG   CD   OE1  NE2                                  
REMARK 470     LYS O  57    CG   CD   CE   NZ                                   
REMARK 470     ASN O  58    CG   OD1  ND2                                       
REMARK 470     LYS O  59    CG   CD   CE   NZ                                   
REMARK 470     ARG O  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN O  61    CG   CD   OE1  NE2                                  
REMARK 470     GLU O  62    CG   CD   OE1  OE2                                  
REMARK 470     THR X   2    OG1  CG2                                            
REMARK 470     ARG a  16    CD   NE   CZ   NH1  NH2                             
REMARK 470     GLU a 243    CG   CD   OE1  OE2                                  
REMARK 470     GLU b 489    CG   CD   OE1  OE2                                  
REMARK 470     VAL b 502    CG1  CG2                                            
REMARK 470     ARG b 505    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG d  12    NE   CZ   NH1  NH2                                  
REMARK 470     GLU d 227    CD   OE1  OE2                                       
REMARK 470     HIS d 336    O                                                   
REMARK 470     SER f  12    OG                                                  
REMARK 470     MET l   1    CG   SD   CE                                        
REMARK 470     GLN m  33    CG   CD   OE1  NE2                                  
REMARK 470     ASN o  58    CG   OD1  ND2                                       
REMARK 470     ARG o  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN o  61    CG   CD   OE1  NE2                                  
REMARK 470     GLU o  62    CG   CD   OE1  OE2                                  
REMARK 470     GLU o 181    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     SER b  239   CA   CB   OG                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU a   333     O    HOH a   701              1.71            
REMARK 500   OH   TYR d   141     O4   LHG a   613              1.90            
REMARK 500   OH   TYR D   141     O4   LHG A   616              1.98            
REMARK 500   O    SER a   217     OG   SER a   221              2.10            
REMARK 500   OD1  ASP c    27     OG   SER c    30              2.18            
REMARK 500   OG1  THR e     5     OE1  GLU e     7              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    ASN A  12     -164.86    -77.40                                   
REMARK 500    VAL A  30      -79.67    -95.00                                   
REMARK 500    LEU A 159      -49.66   -130.35                                   
REMARK 500    LEU A 174       66.70   -102.63                                   
REMARK 500    THR A 228     -152.28   -102.86                                   
REMARK 500    ILE A 259     -104.85   -113.73                                   
REMARK 500    PHE B 156      -52.01   -127.27                                   
REMARK 500    PHE B 162       66.97   -154.05                                   
REMARK 500    ASP B 313       48.52    -90.59                                   
REMARK 500    ALA B 320       46.36   -101.96                                   
REMARK 500    GLU B 485       30.80    -96.10                                   
REMARK 500    GLU C 221      -77.47   -116.00                                   
REMARK 500    TRP C 223     -132.22     58.54                                   
REMARK 500    SER C 406       67.00     64.16                                   
REMARK 500    SER C 416      -52.34   -165.80                                   
REMARK 500    PHE C 455       34.24   -141.32                                   
REMARK 500    SER C 463       51.81   -143.59                                   
REMARK 500    VAL D  30      -83.12    -98.08                                   
REMARK 500    SER D  65       38.45   -148.54                                   
REMARK 500    HIS D  87       34.90    -91.40                                   
REMARK 500    PRO D 140       47.58    -89.54                                   
REMARK 500    LEU D 158      -55.49   -129.54                                   
REMARK 500    GLN D 164     -159.21    -89.05                                   
REMARK 500    PHE D 173       80.53    -69.57                                   
REMARK 500    ALA D 234       39.64    -86.23                                   
REMARK 500    ALA D 351      -58.63     64.13                                   
REMARK 500    LYS H  63       72.35    -63.94                                   
REMARK 500    SER I  25       45.90    -91.94                                   
REMARK 500    LYS I  33     -123.66   -101.07                                   
REMARK 500    ALA O  26       92.63    -65.51                                   
REMARK 500    LYS O  59        7.90     59.84                                   
REMARK 500    ARG O  60       57.71   -141.34                                   
REMARK 500    ARG O  73     -164.25     60.48                                   
REMARK 500    THR O  75       42.87   -144.89                                   
REMARK 500    ASN O 132       76.28     56.86                                   
REMARK 500    LEU O 164      -75.94    -97.78                                   
REMARK 500    ILE T  29       91.00    -66.09                                   
REMARK 500    THR U  19     -165.63   -107.61                                   
REMARK 500    ASN U  29      -38.30   -141.59                                   
REMARK 500    ASN U  99       97.79   -167.39                                   
REMARK 500    TYR U 103     -123.65   -122.92                                   
REMARK 500    ASN V  49       84.04   -165.84                                   
REMARK 500    ASP V  67       30.63    -86.57                                   
REMARK 500    VAL Y  18     -115.05     76.25                                   
REMARK 500    THR Z   2      -33.77   -162.52                                   
REMARK 500    PRO Z  30       45.75    -83.75                                   
REMARK 500    GLN Z  31     -158.15    -77.22                                   
REMARK 500    ASP Z  32       80.29    -58.80                                   
REMARK 500    VAL a  30      -84.38    -90.55                                   
REMARK 500    ASN a  76     -169.68   -110.20                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     103 RAMACHANDRAN OUTLIERS.                        
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     SQD A  603                                                       
REMARK 610     CLA A  607                                                       
REMARK 610     LMG A  612                                                       
REMARK 610     LMG A  613                                                       
REMARK 610     SQD A  619                                                       
REMARK 610     LMG B  620                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     LMG B  625                                                       
REMARK 610     DGD C  516                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     LMG C  519                                                       
REMARK 610     LMG C  520                                                       
REMARK 610     LMG D  405                                                       
REMARK 610     SQD D  408                                                       
REMARK 610     SQD D  409                                                       
REMARK 610     DGD H  103                                                       
REMARK 610     SQD I  101                                                       
REMARK 610     CLA a  607                                                       
REMARK 610     LHG a  614                                                       
REMARK 610     LHG a  615                                                       
REMARK 610     LMG b  623                                                       
REMARK 610     LMG b  624                                                       
REMARK 610     LMG b  625                                                       
REMARK 610     LMG c  502                                                       
REMARK 610     CLA c  510                                                       
REMARK 610     DGD c  518                                                       
REMARK 610     DGD c  519                                                       
REMARK 610     DGD c  520                                                       
REMARK 610     LMG c  521                                                       
REMARK 610     LMG c  522                                                       
REMARK 610     LMG d  406                                                       
REMARK 610     LMG d  409                                                       
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  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 601   O1  172.2                                              
REMARK 620 3 OEX A 601   O2  110.4  65.9                                        
REMARK 620 4 OEX A 601   O5  106.4  79.6  73.9                                  
REMARK 620 5 GLU A 189   OE1 111.6  73.1 137.4  88.3                            
REMARK 620 6 ALA A 344   O    87.5  84.8  73.3 147.1 114.7                      
REMARK 620 7 HOH A 706   O    63.1 124.8 125.7  59.5  70.4 148.5                
REMARK 620 N                    1     2     3     4     5     6                 
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   OD2                                                    
REMARK 620 2 OEX A 601   O5  102.5                                              
REMARK 620 3 OEX A 601   O4   87.5  86.6                                        
REMARK 620 4 GLU A 333   OE2 164.2  87.6  80.9                                  
REMARK 620 5 HOH A 702   O   117.7  89.8 154.7  73.9                            
REMARK 620 6 HOH A 709   O    84.9 172.3  95.6  85.5  85.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEX A 601   O1   88.7                                              
REMARK 620 3 OEX A 601   O5   81.9  91.8                                        
REMARK 620 4 OEX A 601   O3  160.6  91.3  78.7                                  
REMARK 620 5 HIS A 332   NE2  99.8 171.3  87.2  80.0                            
REMARK 620 6 ASP A 342   OD2 106.8  76.2 164.8  92.1 103.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  88.9                                              
REMARK 620 3 HIS D 214   NE2  99.6  89.5                                        
REMARK 620 4 HIS D 268   NE2  89.8 173.4  97.1                                  
REMARK 620 5 BCT A 620   O1  166.0 102.1  89.4  78.3                            
REMARK 620 6 BCT A 620   O2  110.7  83.7 148.7  90.8  62.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEX A 601   O2  150.9                                              
REMARK 620 3 OEX A 601   O3   87.6  90.3                                        
REMARK 620 4 OEX A 601   O4   95.8  85.2 175.4                                  
REMARK 620 5 OEX A 601   O5  109.6  99.4  88.4  93.4                            
REMARK 620 6 GLU C 354   OE2  74.2  76.8  91.4  86.6 176.2                      
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   82.1                                              
REMARK 620 3 OEX A 601   O2  164.6 104.0                                        
REMARK 620 4 OEX A 601   O3  101.1  86.1  93.5                                  
REMARK 620 5 ALA A 344   OXT  89.1  83.6  77.8 164.4                            
REMARK 620 6 GLU C 354   OE1  91.9 173.9  81.7  95.5  95.9                      
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  104.7                                              
REMARK 620 3 CLA C 511   NB   96.6  91.3                                        
REMARK 620 4 CLA C 511   NC   82.0 172.7  90.9                                  
REMARK 620 5 CLA C 511   ND   90.1  90.3 172.5  86.7                            
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   93.1                                              
REMARK 620 3 HEM E 101   NB  109.0  89.4                                        
REMARK 620 4 HEM E 101   NC   93.3 173.5  89.9                                  
REMARK 620 5 HEM E 101   ND   72.1  91.2 178.7  89.4                            
REMARK 620 6 HIS F  24   NE2 162.7  69.9  74.8 103.7 104.4                      
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   99.2                                              
REMARK 620 3 HEM V 201   NB   88.3  89.4                                        
REMARK 620 4 HEM V 201   NC   76.8 175.9  90.4                                  
REMARK 620 5 HEM V 201   ND   85.4  90.1 173.5  89.6                            
REMARK 620 6 HIS V  92   NE2 160.7  95.2 104.7  88.8  81.8                      
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   OD1                                                    
REMARK 620 2 OEX a 601   O1  168.2                                              
REMARK 620 3 OEX a 601   O2  107.1  65.9                                        
REMARK 620 4 OEX a 601   O5  108.2  79.6  73.9                                  
REMARK 620 5 GLU a 189   OE1 133.5  53.4 119.1  90.2                            
REMARK 620 6 ALA a 344   O    86.5  82.7  76.5 149.8  98.7                      
REMARK 620 7 ALA a 344   OXT 120.0  48.2  46.8 110.3  90.3  41.3                
REMARK 620 8 HOH a 711   O    76.3 114.8 148.8  75.6  67.3 134.4 157.2          
REMARK 620 N                    1     2     3     4     5     6     7           
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   OD2                                                    
REMARK 620 2 OEX a 601   O5   97.1                                              
REMARK 620 3 OEX a 601   O4   98.7  86.6                                        
REMARK 620 4 GLU a 333   OE2 174.2  88.7  81.3                                  
REMARK 620 5 HOH a 707   O    87.6 162.6 109.4  87.0                            
REMARK 620 6 HOH a 701   O   131.9  90.3 129.2  47.9  74.3                      
REMARK 620 N                    1     2     3     4     5                       
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   99.6                                              
REMARK 620 3 OEX a 601   O5  100.7  91.8                                        
REMARK 620 4 OEX a 601   O3  169.1  91.3  78.7                                  
REMARK 620 5 HIS a 332   NE2  90.4 169.5  89.4  78.7                            
REMARK 620 6 ASP a 342   OD2 100.1  70.9 154.9  83.5 104.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 602  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  93.3                                              
REMARK 620 3 HIS d 214   NE2  99.9  80.2                                        
REMARK 620 4 HIS d 268   NE2  82.4 172.1  93.9                                  
REMARK 620 5 BCT a 605   O1  164.9  92.2  95.0  93.6                            
REMARK 620 6 BCT a 605   O2  103.4  86.7 153.8 100.8  62.8                      
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  152.7                                              
REMARK 620 3 OEX a 601   O3   87.1  90.2                                        
REMARK 620 4 OEX a 601   O4   96.5  85.2 175.4                                  
REMARK 620 5 OEX a 601   O5  107.6  99.4  88.3  93.4                            
REMARK 620 6 GLU c 354   OE2  73.0  79.9  90.5  87.7 178.7                      
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   90.2                                              
REMARK 620 3 OEX a 601   O2  156.1 104.1                                        
REMARK 620 4 OEX a 601   O3  106.7  86.1  93.5                                  
REMARK 620 5 ASP a 342   OD2  51.0  57.2 152.5  67.3                            
REMARK 620 6 ALA a 344   OXT  84.0  81.7  79.3 163.8 113.7                      
REMARK 620 7 GLU c 354   OE1  84.3 173.7  82.2  92.6 116.7 100.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 513  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 513   NA   99.4                                              
REMARK 620 3 CLA c 513   NB   97.1  91.4                                        
REMARK 620 4 CLA c 513   NC   87.1 172.8  90.9                                  
REMARK 620 5 CLA c 513   ND   89.8  90.3 172.5  86.5                            
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   86.8                                              
REMARK 620 3 HEM e 101   NB  101.9  89.6                                        
REMARK 620 4 HEM e 101   NC   94.9 178.2  90.4                                  
REMARK 620 5 HEM e 101   ND   73.6  90.9 175.5  89.2                            
REMARK 620 6 HIS f  24   NE2 154.2  72.1  92.7 106.2  91.7                      
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  100.4                                              
REMARK 620 3 HEM v 201   NB   91.2  89.2                                        
REMARK 620 4 HEM v 201   NC   77.4 177.8  90.3                                  
REMARK 620 5 HEM v 201   ND   83.0  90.0 173.9  90.3                            
REMARK 620 6 HIS v  92   NE2 159.9  94.6 102.4  87.7  83.7                      
REMARK 620 N                    1     2     3     4     5                       
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 710   O                                                      
REMARK 620 2 CLA A 607   NA   93.4                                              
REMARK 620 3 CLA A 607   NB   90.6  91.5                                        
REMARK 620 4 CLA A 607   NC   91.0 174.8  91.2                                  
REMARK 620 5 CLA A 607   ND   94.7  90.7 174.1  86.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 615  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 705   O                                                      
REMARK 620 2 CLA A 615   NA   74.9                                              
REMARK 620 3 CLA A 615   NB  100.6  91.6                                        
REMARK 620 4 CLA A 615   NC  109.2 174.5  91.1                                  
REMARK 620 5 CLA A 615   ND   85.6  90.7 173.8  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 601  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 710   O                                                      
REMARK 620 2 CLA B 601   NA   90.9                                              
REMARK 620 3 CLA B 601   NB   88.2  91.5                                        
REMARK 620 4 CLA B 601   NC   94.4 174.2  91.1                                  
REMARK 620 5 CLA B 601   ND   97.6  90.7 173.7  86.2                            
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 714   O                                                      
REMARK 620 2 CLA B 607   NA   87.0                                              
REMARK 620 3 CLA B 607   NB   96.7  91.4                                        
REMARK 620 4 CLA B 607   NC   98.3 173.7  91.2                                  
REMARK 620 5 CLA B 607   ND   89.7  90.6 173.4  86.2                            
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 702   O                                                      
REMARK 620 2 CLA B 610   NA   95.4                                              
REMARK 620 3 CLA B 610   NB   80.7  91.7                                        
REMARK 620 4 CLA B 610   NC   90.0 174.3  91.1                                  
REMARK 620 5 CLA B 610   ND  104.2  90.3 174.5  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 504  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 601   O                                                      
REMARK 620 2 CLA C 504   NA   85.3                                              
REMARK 620 3 CLA C 504   NB   83.3  91.6                                        
REMARK 620 4 CLA C 504   NC  100.0 174.4  91.0                                  
REMARK 620 5 CLA C 504   ND  102.7  90.6 173.7  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 507  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 603   O                                                      
REMARK 620 2 CLA C 507   NA   83.9                                              
REMARK 620 3 CLA C 507   NB   86.2  91.7                                        
REMARK 620 4 CLA C 507   NC  101.7 174.0  90.8                                  
REMARK 620 5 CLA C 507   ND   99.9  90.6 173.7  86.4                            
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 706   O                                                      
REMARK 620 2 CLA a 607   NA   82.8                                              
REMARK 620 3 CLA a 607   NB   88.7  91.5                                        
REMARK 620 4 CLA a 607   NC  102.4 174.2  91.1                                  
REMARK 620 5 CLA a 607   ND   97.4  90.6 173.7  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a 612  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH a 710   O                                                      
REMARK 620 2 CLA a 612   NA   89.7                                              
REMARK 620 3 CLA a 612   NB   96.5  91.5                                        
REMARK 620 4 CLA a 612   NC   94.8 174.5  91.2                                  
REMARK 620 5 CLA a 612   ND   89.4  90.7 173.8  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 604  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 709   O                                                      
REMARK 620 2 CLA b 604   NA   89.0                                              
REMARK 620 3 CLA b 604   NB   88.4  91.4                                        
REMARK 620 4 CLA b 604   NC   96.6 173.9  91.1                                  
REMARK 620 5 CLA b 604   ND   97.7  90.6 173.6  86.4                            
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 705   O                                                      
REMARK 620 2 CLA b 610   NA   75.7                                              
REMARK 620 3 CLA b 610   NB   89.5  91.5                                        
REMARK 620 4 CLA b 610   NC  109.9 173.8  91.1                                  
REMARK 620 5 CLA b 610   ND   97.1  90.6 173.4  86.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 613  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 707   O                                                      
REMARK 620 2 CLA b 613   NA   83.8                                              
REMARK 620 3 CLA b 613   NB   79.2  91.6                                        
REMARK 620 4 CLA b 613   NC  101.8 174.1  91.2                                  
REMARK 620 5 CLA b 613   ND  106.2  90.2 174.4  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 506  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH c 608   O                                                      
REMARK 620 2 CLA c 506   NA   90.7                                              
REMARK 620 3 CLA c 506   NB   83.0  91.6                                        
REMARK 620 4 CLA c 506   NC   94.9 174.1  91.0                                  
REMARK 620 5 CLA c 506   ND  103.0  90.6 173.6  86.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 509  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH c 609   O                                                      
REMARK 620 2 CLA c 509   NA   91.5                                              
REMARK 620 3 CLA c 509   NB   90.1  91.6                                        
REMARK 620 4 CLA c 509   NC   94.5 173.5  90.9                                  
REMARK 620 5 CLA c 509   ND   96.1  90.6 173.4  86.3                            
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 FE2 A 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD 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 PHO A 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR A 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 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 LMG A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT A 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 627                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 103                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD I 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 101                 
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 HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR Y 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 622                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR k 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR y 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v    
REMARK 800  37                                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT5                                                 
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: AT6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Di-peptide HEM v 201 and CYS v    
REMARK 800  37                                                                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5AKI   RELATED DB: PDB                                   
REMARK 900 CORRESPONDING DOUBLY ILLUMINATED RT STRUCTURE OF PHOTOSYSTEM II      
REMARK 900 RELATED ID: 5TIS   RELATED DB: PDB                                   
DBREF  5KAF A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  5KAF B    1   510  UNP    Q8DIQ1   PSBB_THEEB       1    510             
DBREF  5KAF C   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  5KAF D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  5KAF E    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  5KAF F    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  5KAF H    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  5KAF I    2    38  UNP    Q8DJZ6   PSBI_THEEB       2     38             
DBREF  5KAF J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5KAF K    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  5KAF L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5KAF M    2    36  UNP    Q8DHA7   PSBM_THEEB       2     36             
DBREF  5KAF O  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  5KAF T    2    32  UNP    Q8DIQ0   PSBT_THEEB       2     32             
DBREF  5KAF U  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  5KAF V  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  5KAF Y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  5KAF X    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  5KAF Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5KAF R    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
DBREF  5KAF a    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  5KAF b    1   510  UNP    Q8DIQ1   PSBB_THEEB       1    510             
DBREF  5KAF c   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  5KAF d    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  5KAF e    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  5KAF f    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  5KAF h    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  5KAF i    2    38  UNP    Q8DJZ6   PSBI_THEEB       2     38             
DBREF  5KAF j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5KAF k    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  5KAF l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5KAF m    2    36  UNP    Q8DHA7   PSBM_THEEB       2     36             
DBREF  5KAF o  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  5KAF t    2    32  UNP    Q8DIQ0   PSBT_THEEB       2     32             
DBREF  5KAF u  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  5KAF v  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  5KAF y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  5KAF x    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  5KAF z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5KAF r    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
SEQADV 5KAF FME I    1  UNP  Q8DJZ6              EXPRESSION TAG                 
SEQADV 5KAF FME M    1  UNP  Q8DHA7              EXPRESSION TAG                 
SEQADV 5KAF FME T    1  UNP  Q8DIQ0              EXPRESSION TAG                 
SEQADV 5KAF FME i    1  UNP  Q8DJZ6              EXPRESSION TAG                 
SEQADV 5KAF FME m    1  UNP  Q8DHA7              EXPRESSION TAG                 
SEQADV 5KAF FME t    1  UNP  Q8DIQ0              EXPRESSION TAG                 
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  FME 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  FME 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  FME 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 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 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  FME 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  FME 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  FME 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 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                                                      
MODRES 5KAF FME I    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAF FME M    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAF FME T    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAF FME i    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAF FME m    1  MET  MODIFIED RESIDUE                                   
MODRES 5KAF FME t    1  MET  MODIFIED RESIDUE                                   
HET    FME  I   1      10                                                       
HET    FME  M   1      10                                                       
HET    FME  T   1      10                                                       
HET    FME  i   1      10                                                       
HET    FME  m   1      10                                                       
HET    FME  t   1      10                                                       
HET    OEX  A 601      10                                                       
HET    FE2  A 602       1                                                       
HET    SQD  A 603      52                                                       
HET     CL  A 604       1                                                       
HET     CL  A 605       1                                                       
HET    CLA  A 606      65                                                       
HET    CLA  A 607      57                                                       
HET    PHO  A 608      64                                                       
HET    CLA  A 609      65                                                       
HET    BCR  A 610      40                                                       
HET    PL9  A 611      55                                                       
HET    LMG  A 612      51                                                       
HET    LMG  A 613      51                                                       
HET    UNL  A 614       7                                                       
HET    CLA  A 615      65                                                       
HET    LHG  A 616      49                                                       
HET    LHG  A 617      49                                                       
HET    LHG  A 618      49                                                       
HET    SQD  A 619      40                                                       
HET    BCT  A 620       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    LMG  B 621      51                                                       
HET    UNL  B 622       6                                                       
HET    UNL  B 623      11                                                       
HET    UNL  B 624      11                                                       
HET    LMG  B 625      51                                                       
HET    SQD  B 626      54                                                       
HET    BCR  B 627      40                                                       
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    LMG  C 520      51                                                       
HET    UNL  C 521       9                                                       
HET    PHO  D 401      64                                                       
HET    CLA  D 402      65                                                       
HET    CLA  D 403      65                                                       
HET    BCR  D 404      40                                                       
HET    LMG  D 405      51                                                       
HET    LHG  D 406      49                                                       
HET    PL9  D 407      55                                                       
HET    SQD  D 408      47                                                       
HET    SQD  D 409      43                                                       
HET    HEM  E 101      43                                                       
HET    UNL  H 101       8                                                       
HET    BCR  H 102      40                                                       
HET    DGD  H 103      62                                                       
HET    SQD  I 101      40                                                       
HET    BCR  K 101      40                                                       
HET    LHG  L 101      49                                                       
HET    UNL  M 101       6                                                       
HET    UNL  M 102      17                                                       
HET    BCR  T 101      40                                                       
HET    HEM  V 201      43                                                       
HET    BCR  Y 101      40                                                       
HET    OEX  a 601      10                                                       
HET    FE2  a 602       1                                                       
HET     CL  a 603       1                                                       
HET     CL  a 604       1                                                       
HET    BCT  a 605       4                                                       
HET    CLA  a 606      65                                                       
HET    CLA  a 607      59                                                       
HET    PHO  a 608      64                                                       
HET    CLA  a 609      65                                                       
HET    BCR  a 610      40                                                       
HET    PL9  a 611      55                                                       
HET    CLA  a 612      65                                                       
HET    LHG  a 613      49                                                       
HET    LHG  a 614      35                                                       
HET    LHG  a 615      42                                                       
HET    SQD  b 601      54                                                       
HET    UNL  b 602      13                                                       
HET    UNL  b 603      13                                                       
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    CLA  b 617      65                                                       
HET    CLA  b 618      65                                                       
HET    CLA  b 619      65                                                       
HET    BCR  b 620      40                                                       
HET    BCR  b 621      40                                                       
HET    BCR  b 622      40                                                       
HET    LMG  b 623      51                                                       
HET    LMG  b 624      51                                                       
HET    LMG  b 625       9                                                       
HET    SQD  c 501      54                                                       
HET    LMG  c 502      51                                                       
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      58                                                       
HET    CLA  c 511      65                                                       
HET    CLA  c 512      65                                                       
HET    CLA  c 513      65                                                       
HET    CLA  c 514      65                                                       
HET    CLA  c 515      65                                                       
HET    BCR  c 516      40                                                       
HET    BCR  c 517      40                                                       
HET    DGD  c 518      62                                                       
HET    DGD  c 519      62                                                       
HET    DGD  c 520      62                                                       
HET    LMG  c 521      51                                                       
HET    LMG  c 522      51                                                       
HET    PHO  d 401      64                                                       
HET    UNL  d 402      22                                                       
HET    CLA  d 403      65                                                       
HET    CLA  d 404      65                                                       
HET    BCR  d 405      40                                                       
HET    LMG  d 406      42                                                       
HET    LHG  d 407      49                                                       
HET    PL9  d 408      55                                                       
HET    LMG  d 409      40                                                       
HET    HEM  e 101      43                                                       
HET    SQD  f 101      43                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET    UNL  i 101      12                                                       
HET    UNL  j 101       9                                                       
HET    BCR  k 101      40                                                       
HET    LHG  l 101      49                                                       
HET    UNL  m 101       5                                                       
HET    UNL  m 102      16                                                       
HET    UNL  t 101      10                                                       
HET    HEM  v 201      43                                                       
HET    BCR  y 101      40                                                       
HET    UNL  z 101      11                                                       
HETNAM     FME N-FORMYLMETHIONINE                                               
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM     FE2 FE (II) ION                                                      
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM      CL CHLORIDE ION                                                     
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN 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     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     HEM HEME                                                             
FORMUL   8  FME    6(C6 H11 N O3 S)                                             
FORMUL  41  OEX    2(CA MN4 O5)                                                 
FORMUL  42  FE2    2(FE 2+)                                                     
FORMUL  43  SQD    9(C41 H78 O12 S)                                             
FORMUL  44   CL    4(CL 1-)                                                     
FORMUL  46  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  48  PHO    4(C55 H74 N4 O5)                                             
FORMUL  50  BCR    22(C40 H56)                                                  
FORMUL  51  PL9    4(C53 H80 O2)                                                
FORMUL  52  LMG    16(C45 H86 O10)                                              
FORMUL  56  LHG    10(C38 H75 O10 P)                                            
FORMUL  60  BCT    2(C H O3 1-)                                                 
FORMUL  03  DGD    8(C51 H96 O15)                                               
FORMUL  18  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  15  HOH   *124(H2 O)                                                    
HELIX    1 AA1 ASN A   12  THR A   22  1                                  11    
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  LEU A  137  1                                  29    
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  THR A  220  1                                  26    
HELIX   13 AB4 SER A  221  LEU A  223  5                                   3    
HELIX   14 AB5 SER A  232  TYR A  237  5                                   6    
HELIX   15 AB6 ASN A  247  ILE A  259  1                                  13    
HELIX   16 AB7 PHE A  260  SER A  264  5                                   5    
HELIX   17 AB8 ASN A  267  MET A  293  1                                  27    
HELIX   18 AB9 ALA A  294  ASN A  296  5                                   3    
HELIX   19 AC1 THR A  316  HIS A  332  1                                  17    
HELIX   20 AC2 PRO B    4  ILE B   13  5                                  10    
HELIX   21 AC3 ASP B   15  ALA B   43  1                                  29    
HELIX   22 AC4 PRO B   54  GLN B   58  5                                   5    
HELIX   23 AC5 VAL B   62  ARG B   68  1                                   7    
HELIX   24 AC6 SER B   92  TYR B  117  1                                  26    
HELIX   25 AC7 LEU B  120  ARG B  124  5                                   5    
HELIX   26 AC8 ASP B  134  PHE B  156  1                                  23    
HELIX   27 AC9 GLY B  186  ASN B  191  5                                   6    
HELIX   28 AD1 ASN B  194  VAL B  219  1                                  26    
HELIX   29 AD2 PRO B  222  LEU B  229  1                                   8    
HELIX   30 AD3 ILE B  234  GLY B  259  1                                  26    
HELIX   31 AD4 ARG B  272  SER B  277  1                                   6    
HELIX   32 AD5 SER B  278  SER B  294  1                                  17    
HELIX   33 AD6 THR B  297  ALA B  304  1                                   8    
HELIX   34 AD7 PRO B  306  ASP B  313  1                                   8    
HELIX   35 AD8 TYR B  314  ASN B  318  5                                   5    
HELIX   36 AD9 PRO B  329  GLY B  333  5                                   5    
HELIX   37 AE1 SER B  391  GLY B  396  1                                   6    
HELIX   38 AE2 ASP B  413  ILE B  425  1                                  13    
HELIX   39 AE3 SER B  446  PHE B  475  1                                  30    
HELIX   40 AE4 ARG B  476  PHE B  479  5                                   4    
HELIX   41 AE5 ASP B  501  ARG B  505  5                                   5    
HELIX   42 AE6 ASP C   27  GLY C   32  1                                   6    
HELIX   43 AE7 ALA C   34  ILE C   43  5                                  10    
HELIX   44 AE8 LEU C   45  HIS C   74  1                                  30    
HELIX   45 AE9 PRO C   80  GLN C   84  5                                   5    
HELIX   46 AF1 ILE C   87  LEU C   95  1                                   9    
HELIX   47 AF2 GLY C  100  GLU C  104  5                                   5    
HELIX   48 AF3 THR C  108  ARG C  135  1                                  28    
HELIX   49 AF4 THR C  139  SER C  144  1                                   6    
HELIX   50 AF5 ASP C  153  PHE C  182  1                                  30    
HELIX   51 AF6 ASP C  205  LEU C  214  1                                  10    
HELIX   52 AF7 GLY C  222  VAL C  227  5                                   6    
HELIX   53 AF8 ASN C  229  THR C  254  1                                  26    
HELIX   54 AF9 PHE C  257  ARG C  262  1                                   6    
HELIX   55 AG1 SER C  267  ASN C  293  1                                  27    
HELIX   56 AG2 PRO C  298  GLY C  303  1                                   6    
HELIX   57 AG3 THR C  305  LEU C  324  1                                  20    
HELIX   58 AG4 GLY C  353  TRP C  359  5                                   7    
HELIX   59 AG5 LEU C  366  PRO C  368  5                                   3    
HELIX   60 AG6 ASP C  376  ASP C  383  1                                   8    
HELIX   61 AG7 GLN C  385  THR C  397  1                                  13    
HELIX   62 AG8 SER C  421  GLY C  454  1                                  34    
HELIX   63 AG9 PRO C  465  MET C  469  5                                   5    
HELIX   64 AH1 GLY D   13  LYS D   23  1                                  11    
HELIX   65 AH2 SER D   33  THR D   52  1                                  20    
HELIX   66 AH3 ALA D   82  GLY D   86  5                                   5    
HELIX   67 AH4 ASP D  100  LEU D  107  1                                   8    
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  194  ASN D  220  1                                  27    
HELIX   75 AI3 SER D  230  ALA D  234  5                                   5    
HELIX   76 AI4 SER D  245  PHE D  257  1                                  13    
HELIX   77 AI5 ASN D  263  LEU D  291  1                                  29    
HELIX   78 AI6 PHE D  298  ASP D  308  1                                  11    
HELIX   79 AI7 THR D  313  GLN D  334  1                                  22    
HELIX   80 AI8 PRO E    9  THR E   15  1                                   7    
HELIX   81 AI9 SER E   16  THR E   40  1                                  25    
HELIX   82 AJ1 GLY E   41  GLY E   48  1                                   8    
HELIX   83 AJ2 GLU E   71  GLN E   82  1                                  12    
HELIX   84 AJ3 THR F   17  GLN F   41  1                                  25    
HELIX   85 AJ4 THR H    5  LEU H   11  1                                   7    
HELIX   86 AJ5 ARG H   12  SER H   16  5                                   5    
HELIX   87 AJ6 THR H   27  ASN H   50  1                                  24    
HELIX   88 AJ7 GLU I    2  LEU I   24  1                                  23    
HELIX   89 AJ8 GLY I   26  ARG I   30  5                                   5    
HELIX   90 AJ9 PRO J    9  ALA J   32  1                                  24    
HELIX   91 AK1 TYR K   15  ILE K   17  5                                   3    
HELIX   92 AK2 PHE K   18  LEU K   25  1                                   8    
HELIX   93 AK3 VAL K   27  VAL K   43  1                                  17    
HELIX   94 AK4 ASN L   13  ASN L   37  1                                  25    
HELIX   95 AK5 LEU M    6  SER M   31  1                                  26    
HELIX   96 AK6 THR O    6  VAL O   11  1                                   6    
HELIX   97 AK7 GLY O   14  LYS O   18  5                                   5    
HELIX   98 AK8 LEU O  182  VAL O  187  1                                   6    
HELIX   99 AK9 GLU T    2  PHE T   23  1                                  22    
HELIX  100 AL1 ASN U   11  GLY U   18  1                                   8    
HELIX  101 AL2 THR U   19  GLU U   23  5                                   5    
HELIX  102 AL3 ASN U   31  TYR U   38  5                                   8    
HELIX  103 AL4 PRO U   43  ASN U   52  1                                  10    
HELIX  104 AL5 SER U   57  ILE U   64  5                                   8    
HELIX  105 AL6 THR U   68  GLU U   77  1                                  10    
HELIX  106 AL7 ASN U   78  GLU U   80  5                                   3    
HELIX  107 AL8 GLU U   88  GLU U   93  1                                   6    
HELIX  108 AL9 GLY U   94  ASP U   96  5                                   3    
HELIX  109 AM1 THR V   22  CYS V   37  1                                  16    
HELIX  110 AM2 HIS V   41  ILE V   45  5                                   5    
HELIX  111 AM3 ARG V   55  LEU V   61  1                                   7    
HELIX  112 AM4 ASN V   68  MET V   76  1                                   9    
HELIX  113 AM5 SER V   94  ALA V   98  5                                   5    
HELIX  114 AM6 PHE V  101  ARG V  105  5                                   5    
HELIX  115 AM7 THR V  108  GLY V  127  1                                  20    
HELIX  116 AM8 ASP V  128  TRP V  130  5                                   3    
HELIX  117 AM9 GLY V  132  TYR V  137  5                                   6    
HELIX  118 AN1 VAL Y   18  ALA Y   31  1                                  14    
HELIX  119 AN2 GLY Y   32  ARG Y   42  1                                  11    
HELIX  120 AN3 THR X    4  ASP X   35  1                                  32    
HELIX  121 AN4 LEU Z    4  ALA Z   28  1                                  25    
HELIX  122 AN5 ASP Z   32  PHE Z   59  1                                  28    
HELIX  123 AN6 TRP R    3  ASN R   22  1                                  20    
HELIX  124 AN7 ILE R   23  LEU R   35  1                                  13    
HELIX  125 AN8 ASN a   12  THR a   22  1                                  11    
HELIX  126 AN9 GLY a   31  ALA a   55  1                                  25    
HELIX  127 AO1 SER a   70  GLY a   74  5                                   5    
HELIX  128 AO2 SER a  101  ASN a  108  1                                   8    
HELIX  129 AO3 GLY a  109  LEU a  137  1                                  29    
HELIX  130 AO4 TRP a  142  LEU a  159  1                                  18    
HELIX  131 AO5 LEU a  159  GLY a  166  1                                   8    
HELIX  132 AO6 SER a  167  GLY a  171  5                                   5    
HELIX  133 AO7 ILE a  176  ASN a  191  1                                  16    
HELIX  134 AO8 ILE a  192  MET a  194  5                                   3    
HELIX  135 AO9 HIS a  195  SER a  222  1                                  28    
HELIX  136 AP1 SER a  232  TYR a  237  5                                   6    
HELIX  137 AP2 ASN a  247  ILE a  259  1                                  13    
HELIX  138 AP3 PHE a  260  SER a  264  5                                   5    
HELIX  139 AP4 ASN a  267  ALA a  294  1                                  28    
HELIX  140 AP5 THR a  316  HIS a  332  1                                  17    
HELIX  141 AP6 PRO b    4  ILE b   13  5                                  10    
HELIX  142 AP7 ASP b   15  ALA b   43  1                                  29    
HELIX  143 AP8 PRO b   54  GLN b   58  5                                   5    
HELIX  144 AP9 PHE b   61  LEU b   69  1                                   9    
HELIX  145 AQ1 SER b   92  TYR b  117  1                                  26    
HELIX  146 AQ2 ASP b  134  PHE b  156  1                                  23    
HELIX  147 AQ3 GLY b  186  ASN b  191  5                                   6    
HELIX  148 AQ4 ASN b  194  VAL b  219  1                                  26    
HELIX  149 AQ5 PRO b  222  LEU b  229  1                                   8    
HELIX  150 AQ6 ILE b  234  GLY b  259  1                                  26    
HELIX  151 AQ7 PRO b  264  GLY b  269  1                                   6    
HELIX  152 AQ8 ARG b  272  SER b  277  1                                   6    
HELIX  153 AQ9 SER b  278  SER b  294  1                                  17    
HELIX  154 AR1 THR b  297  ALA b  304  1                                   8    
HELIX  155 AR2 PRO b  306  ASP b  313  1                                   8    
HELIX  156 AR3 TYR b  314  ASN b  318  5                                   5    
HELIX  157 AR4 PRO b  329  GLY b  333  5                                   5    
HELIX  158 AR5 SER b  391  GLY b  396  1                                   6    
HELIX  159 AR6 ASP b  413  ILE b  425  1                                  13    
HELIX  160 AR7 SER b  446  PHE b  475  1                                  30    
HELIX  161 AR8 ARG b  476  PHE b  479  5                                   4    
HELIX  162 AR9 SER b  487  GLU b  492  1                                   6    
HELIX  163 AS1 ASP b  501  ARG b  505  5                                   5    
HELIX  164 AS2 ASP c   27  GLY c   32  1                                   6    
HELIX  165 AS3 ALA c   34  ILE c   43  5                                  10    
HELIX  166 AS4 LEU c   45  HIS c   74  1                                  30    
HELIX  167 AS5 PRO c   80  GLN c   84  5                                   5    
HELIX  168 AS6 LEU c   88  LEU c   95  1                                   8    
HELIX  169 AS7 GLY c  100  GLU c  104  5                                   5    
HELIX  170 AS8 THR c  108  ARG c  135  1                                  28    
HELIX  171 AS9 ASP c  153  PHE c  182  1                                  30    
HELIX  172 AT1 ASP c  205  PHE c  210  1                                   6    
HELIX  173 AT2 PHE c  210  LYS c  215  1                                   6    
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 PRO c  465  MET c  469  5                                   5    
HELIX  186 AU6 GLY d   13  LYS d   23  1                                  11    
HELIX  187 AU7 SER d   33  THR d   52  1                                  20    
HELIX  188 AU8 ALA d   82  GLY d   86  5                                   5    
HELIX  189 AU9 ASP d  100  LEU d  107  1                                   8    
HELIX  190 AV1 GLY d  108  GLY d  137  1                                  30    
HELIX  191 AV2 PRO d  140  PHE d  146  1                                   7    
HELIX  192 AV3 PHE d  146  LEU d  158  1                                  13    
HELIX  193 AV4 LEU d  158  GLN d  164  1                                   7    
HELIX  194 AV5 SER d  166  ALA d  170  5                                   5    
HELIX  195 AV6 VAL d  175  PHE d  188  1                                  14    
HELIX  196 AV7 ASN d  194  ASN d  220  1                                  27    
HELIX  197 AV8 SER d  245  PHE d  257  1                                  13    
HELIX  198 AV9 ASN d  263  LEU d  291  1                                  29    
HELIX  199 AW1 PHE d  298  ASP d  308  1                                  11    
HELIX  200 AW2 THR d  313  GLN d  334  1                                  22    
HELIX  201 AW3 PRO d  342  LEU d  346  5                                   5    
HELIX  202 AW4 PRO e    9  ILE e   14  1                                   6    
HELIX  203 AW5 SER e   16  THR e   40  1                                  25    
HELIX  204 AW6 GLY e   41  GLY e   48  1                                   8    
HELIX  205 AW7 GLU e   71  GLN e   82  1                                  12    
HELIX  206 AW8 THR f   17  MET f   40  1                                  24    
HELIX  207 AW9 GLN f   41  ILE f   43  5                                   3    
HELIX  208 AX1 THR h    5  LEU h   11  1                                   7    
HELIX  209 AX2 THR h   27  ASN h   50  1                                  24    
HELIX  210 AX3 GLU i    2  LEU i   24  1                                  23    
HELIX  211 AX4 GLY i   26  ARG i   30  5                                   5    
HELIX  212 AX5 PRO j    9  GLY j   31  1                                  23    
HELIX  213 AX6 PRO k   12  ILE k   17  5                                   6    
HELIX  214 AX7 PHE k   18  ASP k   23  1                                   6    
HELIX  215 AX8 VAL k   24  PRO k   26  5                                   3    
HELIX  216 AX9 VAL k   27  VAL k   43  1                                  17    
HELIX  217 AY1 ASN l   13  ASN l   37  1                                  25    
HELIX  218 AY2 LEU m    6  SER m   31  1                                  26    
HELIX  219 AY3 THR o    6  VAL o   11  1                                   6    
HELIX  220 AY4 GLY o   14  LYS o   18  5                                   5    
HELIX  221 AY5 LEU o  182  VAL o  187  1                                   6    
HELIX  222 AY6 GLU t    2  PHE t   23  1                                  22    
HELIX  223 AY7 ASN u   11  GLY u   18  1                                   8    
HELIX  224 AY8 THR u   19  GLU u   23  5                                   5    
HELIX  225 AY9 ASN u   31  GLN u   37  5                                   7    
HELIX  226 AZ1 PRO u   43  ASN u   52  1                                  10    
HELIX  227 AZ2 SER u   57  ILE u   64  5                                   8    
HELIX  228 AZ3 THR u   68  ASN u   78  1                                  11    
HELIX  229 AZ4 GLU u   88  GLU u   93  1                                   6    
HELIX  230 AZ5 GLY u   94  ASP u   96  5                                   3    
HELIX  231 AZ6 THR v   22  CYS v   37  1                                  16    
HELIX  232 AZ7 HIS v   41  ILE v   45  5                                   5    
HELIX  233 AZ8 ARG v   55  LEU v   61  1                                   7    
HELIX  234 AZ9 ASN v   68  ASN v   78  1                                  11    
HELIX  235 BA1 SER v   94  ALA v   98  5                                   5    
HELIX  236 BA2 PHE v  101  ARG v  105  5                                   5    
HELIX  237 BA3 THR v  108  GLY v  127  1                                  20    
HELIX  238 BA4 ASP v  128  TRP v  130  5                                   3    
HELIX  239 BA5 GLY v  133  TYR v  137  5                                   5    
HELIX  240 BA6 VAL y   18  ARG y   42  1                                  25    
HELIX  241 BA7 THR x    4  ASP x   35  1                                  32    
HELIX  242 BA8 THR z    2  SER z   29  1                                  28    
HELIX  243 BA9 ASP z   32  VAL z   62  1                                  31    
HELIX  244 BB1 TRP r    3  LEU r    9  1                                   7    
HELIX  245 BB2 LEU r    9  ASN r   22  1                                  14    
HELIX  246 BB3 ILE r   23  LEU r   35  1                                  13    
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 MET B 166  VAL B 168  0                                        
SHEET    2 AA2 2 SER B 177  GLN B 179 -1  O  GLN B 179   N  MET B 166           
SHEET    1 AA3 6 VAL B 377  ASP B 380  0                                        
SHEET    2 AA3 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA3 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA3 6 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA3 6 THR B 398  TYR B 402 -1  O  THR B 398   N  ARG B 347           
SHEET    6 AA3 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA4 5 VAL B 377  ASP B 380  0                                        
SHEET    2 AA4 5 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA4 5 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA4 5 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA4 5 ILE B 429  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1 AA5 2 LEU C 185  ASP C 187  0                                        
SHEET    2 AA5 2 ASP C 195  ARG C 197 -1  O  ARG C 197   N  LEU C 185           
SHEET    1 AA6 2 LEU C 341  ARG C 343  0                                        
SHEET    2 AA6 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1 AA7 2 ARG C 370  GLY C 371  0                                        
SHEET    2 AA7 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1 AA8 2 ALA D  77  VAL D  78  0                                        
SHEET    2 AA8 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1 AA9 2 TYR O  30  PRO O  31  0                                        
SHEET    2 AA9 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1 AB110 PHE O  65  PRO O  67  0                                        
SHEET    2 AB110 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3 AB110 GLU O 232  PRO O 245 -1  O  LYS O 234   N  LEU O  51           
SHEET    4 AB110 GLU O 210  LEU O 220 -1  N  ILE O 211   O  ALA O 241           
SHEET    5 AB110 THR O 193  VAL O 204 -1  N  ALA O 202   O  ALA O 212           
SHEET    6 AB110 ASP O 141  VAL O 148 -1  N  PHE O 142   O  LEU O 199           
SHEET    7 AB110 LYS O 123  SER O 128 -1  N  LYS O 123   O  ASN O 147           
SHEET    8 AB110 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9 AB110 LEU O  78  VAL O  87 -1  N  LYS O  86   O  THR O  94           
SHEET   10 AB110 TYR O  38  LYS O  53 -1  N  ILE O  40   O  GLY O  83           
SHEET    1 AB2 3 LYS O  69  LEU O  70  0                                        
SHEET    2 AB2 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3 AB2 3 ARG O 115  THR O 121 -1  O  ILE O 116   N  VAL O 108           
SHEET    1 AB3 2 ILE U  25  ASP U  26  0                                        
SHEET    2 AB3 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1 AB4 2 THR V   9  PRO V  11  0                                        
SHEET    2 AB4 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1 AB5 2 ALA a  81  VAL a  82  0                                        
SHEET    2 AB5 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1 AB6 2 LEU a 297  ASN a 298  0                                        
SHEET    2 AB6 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1 AB7 2 MET b 166  VAL b 168  0                                        
SHEET    2 AB7 2 SER b 177  GLN b 179 -1  O  SER b 177   N  VAL b 168           
SHEET    1 AB8 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AB8 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AB8 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AB8 6 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AB8 6 THR b 398  TYR b 402 -1  O  THR b 398   N  ARG b 347           
SHEET    6 AB8 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1 AB9 5 VAL b 377  ASP b 380  0                                        
SHEET    2 AB9 5 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AB9 5 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AB9 5 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AB9 5 ILE b 429  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1 AC1 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC1 2 ASP c 195  ARG c 197 -1  O  ASP c 195   N  ASP c 187           
SHEET    1 AC2 2 LEU c 341  ARG c 343  0                                        
SHEET    2 AC2 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1 AC3 2 ARG c 370  GLY c 371  0                                        
SHEET    2 AC3 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1 AC4 2 ALA d  77  VAL d  78  0                                        
SHEET    2 AC4 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1 AC5 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC5 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC610 PHE o  65  PRO o  67  0                                        
SHEET    2 AC610 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC610 GLU o 232  PRO o 245 -1  O  LYS o 234   N  LEU o  51           
SHEET    4 AC610 GLU o 210  LEU o 220 -1  N  GLN o 219   O  VAL o 233           
SHEET    5 AC610 THR o 193  VAL o 204 -1  N  ASN o 200   O  THR o 214           
SHEET    6 AC610 ASP o 141  VAL o 148 -1  N  VAL o 148   O  THR o 193           
SHEET    7 AC610 LYS o 123  SER o 128 -1  N  SER o 128   O  LYS o 143           
SHEET    8 AC610 LEU o  93  ILE o 101 -1  N  GLU o  97   O  LEU o 125           
SHEET    9 AC610 LEU o  78  VAL o  87 -1  N  LYS o  86   O  THR o  94           
SHEET   10 AC610 TYR o  38  LYS o  53 -1  N  LEU o  45   O  LEU o  78           
SHEET    1 AC7 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AC7 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AC7 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AC8 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AC8 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1 AC9 2 THR v   9  PRO v  11  0                                        
SHEET    2 AC9 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                CA1  OEX A 601     1555   1555  2.34  
LINK         OD2 ASP A 170                MN4  OEX A 601     1555   1555  2.05  
LINK         OE1 GLU A 189                CA1  OEX A 601     1555   1555  3.10  
LINK         OE2 GLU A 189                MN1  OEX A 601     1555   1555  1.79  
LINK         NE2 HIS A 215                FE   FE2 A 602     1555   1555  2.17  
LINK         NE2 HIS A 272                FE   FE2 A 602     1555   1555  2.19  
LINK         NE2 HIS A 332                MN1  OEX A 601     1555   1555  2.12  
LINK         OE1 GLU A 333                MN3  OEX A 601     1555   1555  2.05  
LINK         OE2 GLU A 333                MN4  OEX A 601     1555   1555  2.10  
LINK         OD1 ASP A 342                MN2  OEX A 601     1555   1555  2.16  
LINK         OD2 ASP A 342                MN1  OEX A 601     1555   1555  2.21  
LINK         O   ALA A 344                CA1  OEX A 601     1555   1555  2.42  
LINK         OXT ALA A 344                MN2  OEX A 601     1555   1555  1.89  
LINK         OD1 ASN C  39                MG   CLA C 511     1555   1555  2.21  
LINK         OE1 GLU C 354                MN2  OEX A 601     1555   1555  2.10  
LINK         OE2 GLU C 354                MN3  OEX A 601     1555   1555  2.11  
LINK         NE2 HIS D 214                FE   FE2 A 602     1555   1555  2.17  
LINK         NE2 HIS D 268                FE   FE2 A 602     1555   1555  2.19  
LINK         NE2 HIS E  23                FE   HEM E 101     1555   1555  2.18  
LINK         NE2 HIS F  24                FE   HEM E 101     1555   1555  2.17  
LINK         C   FME I   1                 N   GLU I   2     1555   1555  1.33  
LINK         C   FME M   1                 N   GLU M   2     1555   1555  1.33  
LINK         C   FME T   1                 N   GLU T   2     1555   1555  1.33  
LINK         SG  CYS V  37                 CBB HEM V 201     1555   1555  1.79  
LINK         SG  CYS V  37                 CAB HEM V 201     1555   1555  1.68  
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  2.18  
LINK         OD1 ASP a 170                CA1  OEX a 601     1555   1555  2.36  
LINK         OD2 ASP a 170                MN4  OEX a 601     1555   1555  2.03  
LINK         OE1 GLU a 189                CA1  OEX a 601     1555   1555  3.11  
LINK         OE2 GLU a 189                MN1  OEX a 601     1555   1555  1.78  
LINK         NE2 HIS a 215                FE   FE2 a 602     1555   1555  2.18  
LINK         NE2 HIS a 272                FE   FE2 a 602     1555   1555  2.19  
LINK         NE2 HIS a 332                MN1  OEX a 601     1555   1555  2.12  
LINK         OE1 GLU a 333                MN3  OEX a 601     1555   1555  2.06  
LINK         OE2 GLU a 333                MN4  OEX a 601     1555   1555  2.09  
LINK         OD1 ASP a 342                MN2  OEX a 601     1555   1555  2.18  
LINK         OD2 ASP a 342                MN1  OEX a 601     1555   1555  2.20  
LINK         OD2 ASP a 342                MN2  OEX a 601     1555   1555  2.76  
LINK         O   ALA a 344                CA1  OEX a 601     1555   1555  2.42  
LINK         OXT ALA a 344                CA1  OEX a 601     1555   1555  3.20  
LINK         OXT ALA a 344                MN2  OEX a 601     1555   1555  1.90  
LINK         OD1 ASN c  39                MG   CLA c 513     1555   1555  2.20  
LINK         OE1 GLU c 354                MN2  OEX a 601     1555   1555  2.11  
LINK         OE2 GLU c 354                MN3  OEX a 601     1555   1555  2.11  
LINK         NE2 HIS d 214                FE   FE2 a 602     1555   1555  2.17  
LINK         NE2 HIS d 268                FE   FE2 a 602     1555   1555  2.20  
LINK         NE2 HIS e  23                FE   HEM e 101     1555   1555  2.16  
LINK         NE2 HIS f  24                FE   HEM e 101     1555   1555  2.17  
LINK         C   FME i   1                 N   GLU i   2     1555   1555  1.33  
LINK         C   FME m   1                 N   GLU m   2     1555   1555  1.33  
LINK         C   FME t   1                 N   GLU t   2     1555   1555  1.33  
LINK         SG  CYS v  37                 CAB HEM v 201     1555   1555  1.68  
LINK         SG  CYS v  37                 CBB HEM v 201     1555   1555  1.56  
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  2.18  
LINK        CA1  OEX A 601                 O   HOH A 706     1555   1555  2.74  
LINK        MN4  OEX A 601                 O   HOH A 702     1555   1555  1.86  
LINK        MN4  OEX A 601                 O   HOH A 709     1555   1555  2.18  
LINK        FE   FE2 A 602                 O1  BCT A 620     1555   1555  2.15  
LINK        FE   FE2 A 602                 O2  BCT A 620     1555   1555  2.18  
LINK        MG   CLA A 607                 O   HOH A 710     1555   1555  2.15  
LINK        MG   CLA A 615                 O   HOH A 705     1555   1555  2.15  
LINK        MG   CLA B 601                 O   HOH B 710     1555   1555  2.15  
LINK        MG   CLA B 607                 O   HOH B 714     1555   1555  2.15  
LINK        MG   CLA B 610                 O   HOH B 702     1555   1555  2.15  
LINK        MG   CLA C 504                 O   HOH C 601     1555   1555  2.15  
LINK        MG   CLA C 507                 O   HOH C 603     1555   1555  2.15  
LINK        CA1  OEX a 601                 O   HOH a 711     1555   1555  2.63  
LINK        MN4  OEX a 601                 O   HOH a 707     1555   1555  2.36  
LINK        MN4  OEX a 601                 O   HOH a 701     1555   1555  2.14  
LINK        FE   FE2 a 602                 O1  BCT a 605     1555   1555  2.16  
LINK        FE   FE2 a 602                 O2  BCT a 605     1555   1555  2.17  
LINK        MG   CLA a 607                 O   HOH a 706     1555   1555  2.15  
LINK        MG   CLA a 612                 O   HOH a 710     1555   1555  2.15  
LINK        MG   CLA b 604                 O   HOH b 709     1555   1555  2.15  
LINK        MG   CLA b 610                 O   HOH b 705     1555   1555  2.15  
LINK        MG   CLA b 613                 O   HOH b 707     1555   1555  2.15  
LINK        MG   CLA c 506                 O   HOH c 608     1555   1555  2.15  
LINK        MG   CLA c 509                 O   HOH c 609     1555   1555  2.15  
CISPEP   1 GLN O    3    THR O    4          0        -1.25                     
CISPEP   2 TYR U   42    PRO U   43          0        -1.32                     
CISPEP   3 ALA U   53    PRO U   54          0        -0.79                     
CISPEP   4 THR V   63    PRO V   64          0         0.09                     
CISPEP   5 GLU Y   17    VAL Y   18          0        19.95                     
CISPEP   6 TYR u   42    PRO u   43          0        -1.90                     
CISPEP   7 ALA u   53    PRO u   54          0         0.88                     
CISPEP   8 THR v   63    PRO v   64          0        -2.50                     
SITE     1 AC1 12 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AC1 12 HIS A 337  ASP A 342  ALA A 344  HOH A 702                    
SITE     3 AC1 12 HOH A 706  HOH A 709  GLU C 354  ARG C 357                    
SITE     1 AC2  5 HIS A 215  HIS A 272  BCT A 620  HIS D 214                    
SITE     2 AC2  5 HIS D 268                                                     
SITE     1 AC3 15 LEU A 200  ASN A 267  SER A 270  PHE A 274                    
SITE     2 AC3 15 TRP A 278  GLY A 282  LHG A 617  HOH A 703                    
SITE     3 AC3 15 GLN C  28  TRP C  36  DGD C 517  PHE D 232                    
SITE     4 AC3 15 ARG D 233  ALA K  34  PHE K  37                               
SITE     1 AC4  3 HIS A 332  GLU A 333  LYS D 317                               
SITE     1 AC5  3 HIS A 337  ASN A 338  PHE A 339                               
SITE     1 AC6 20 TYR A 147  PRO A 150  SER A 153  VAL A 157                    
SITE     2 AC6 20 MET A 183  PHE A 186  ILE A 192  LEU A 193                    
SITE     3 AC6 20 HIS A 198  GLY A 201  VAL A 202  PHE A 206                    
SITE     4 AC6 20 THR A 286  ALA A 287  ILE A 290  CLA A 607                    
SITE     5 AC6 20 PHO A 608  CLA A 615  CLA D 402  PHE T  17                    
SITE     1 AC7 15 GLN A 199  VAL A 202  ALA A 203  GLY A 207                    
SITE     2 AC7 15 TRP A 278  CLA A 606  PL9 A 611  HOH A 710                    
SITE     3 AC7 15 PHE D 157  VAL D 175  ILE D 178  PHE D 179                    
SITE     4 AC7 15 LEU D 182  PHO D 401  CLA D 402                               
SITE     1 AC8 13 LEU A  41  THR A  45  TYR A 126  GLN A 130                    
SITE     2 AC8 13 TYR A 147  PRO A 279  VAL A 283  CLA A 606                    
SITE     3 AC8 13 CLA A 615  ALA D 208  LEU D 209  ILE D 213                    
SITE     4 AC8 13 TRP D 253                                                     
SITE     1 AC9 16 ILE A  36  THR A  40  PHE A  93  TYR A  94                    
SITE     2 AC9 16 PRO A  95  ILE A  96  TRP A  97  LEU A 114                    
SITE     3 AC9 16 HIS A 118  LMG A 612  CLA C 505  CLA C 506                    
SITE     4 AC9 16 VAL I  12  THR I  13  PHE I  15  VAL I  16                    
SITE     1 AD1  5 ILE A  38  LEU A  42  ALA A  43  SQD A 619                    
SITE     2 AD1  5 SQD I 101                                                     
SITE     1 AD2 14 PHE A 211  HIS A 215  LEU A 218  PHE A 255                    
SITE     2 AD2 14 ALA A 263  SER A 264  PHE A 265  LEU A 271                    
SITE     3 AD2 14 CLA A 607  LEU D  45  SQD D 409  ALA F  22                    
SITE     4 AD2 14 LEU F  26  THR X  24                                          
SITE     1 AD3 10 TRP A  97  GLU A  98  PHE A 117  CLA A 609                    
SITE     2 AD3 10 LEU C 214  PHE C 218  TRP C 223  CLA C 505                    
SITE     3 AD3 10 LYS I   5  TYR I   9                                          
SITE     1 AD4  9 ASN A  26  ARG A  27  LEU A  28  LEU A  42                    
SITE     2 AD4  9 CLA A 615  BCR T 101  TRP b 113  TYR b 117                    
SITE     3 AD4  9 BCR b 622                                                     
SITE     1 AD5 17 PHE A  48  PHE A 158  MET A 172  ILE A 176                    
SITE     2 AD5 17 THR A 179  PHE A 180  MET A 183  CLA A 606                    
SITE     3 AD5 17 PHO A 608  LMG A 613  HOH A 705  MET D 198                    
SITE     4 AD5 17 VAL D 201  ALA D 202  GLY D 206  CLA D 402                    
SITE     5 AD5 17 PL9 D 407                                                     
SITE     1 AD6 12 SER A 232  ASN A 234  TYR B   6  ARG B   7                    
SITE     2 AD6 12 PHE B 464  TRP B 468  CLA B 611  TYR D 141                    
SITE     3 AD6 12 TRP D 266  PHE D 269  LHG L 101  PHE M  14                    
SITE     1 AD7 17 ARG A 140  TRP A 142  PHE A 273  PHE A 285                    
SITE     2 AD7 17 SQD A 603  TRP C 443  ARG C 447  CLA C 504                    
SITE     3 AD7 17 CLA C 508  CLA C 510  DGD C 518  GLU D 219                    
SITE     4 AD7 17 ASN D 220  ALA D 229  SER D 230  THR D 231                    
SITE     5 AD7 17 PHE D 232                                                     
SITE     1 AD8  8 LEU A 258  TYR A 262  SER A 264  PHE A 265                    
SITE     2 AD8  8 PHE D  27  PRO E   9  PHE E  10  SER E  11                    
SITE     1 AD9  8 ASP A 103  LEU A 106  BCR A 610  SQD I 101                    
SITE     2 AD9  8 TRP b  75  GLY b  89  GLU b  94  LEU b  98                    
SITE     1 AE1  9 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 AE1  9 FE2 A 602  HIS D 214  TYR D 244  LYS D 264                    
SITE     3 AE1  9 HIS D 268                                                     
SITE     1 AE2  8 TRP B 185  GLY B 186  PHE B 190  CLA B 602                    
SITE     2 AE2  8 LMG B 621  HOH B 710  PHE H  41  BCR H 102                    
SITE     1 AE3 11 GLY B 189  GLY B 197  HIS B 201  PHE B 247                    
SITE     2 AE3 11 PHE B 250  CLA B 601  CLA B 603  LEU D 158                    
SITE     3 AE3 11 TYR H  49  BCR H 102  DGD H 103                               
SITE     1 AE4 15 ARG B  68  LEU B  69  ALA B 146  CYS B 150                    
SITE     2 AE4 15 HIS B 201  HIS B 202  ALA B 248  VAL B 252                    
SITE     3 AE4 15 THR B 262  CLA B 602  CLA B 604  CLA B 605                    
SITE     4 AE4 15 CLA B 606  CLA B 609  PHE H  38                               
SITE     1 AE5 15 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 AE5 15 VAL B 245  ALA B 248  ALA B 249  VAL B 252                    
SITE     3 AE5 15 PHE B 451  HIS B 455  PHE B 458  CLA B 603                    
SITE     4 AE5 15 CLA B 605  CLA B 607  CLA B 615                               
SITE     1 AE6 17 THR B  27  VAL B  30  ALA B  31  TRP B  33                    
SITE     2 AE6 17 ALA B  34  VAL B  62  PHE B  65  MET B  66                    
SITE     3 AE6 17 ARG B  68  LEU B  69  VAL B  96  HIS B 100                    
SITE     4 AE6 17 LEU B 103  ALA B 205  CLA B 603  CLA B 604                    
SITE     5 AE6 17 CLA B 606                                                     
SITE     1 AE7 15 LEU B  69  VAL B  71  PHE B  90  TRP B  91                    
SITE     2 AE7 15 VAL B  96  ALA B  99  HIS B 100  GLY B 152                    
SITE     3 AE7 15 PHE B 153  PHE B 156  HIS B 157  PHE B 162                    
SITE     4 AE7 15 PRO B 164  CLA B 603  CLA B 605                               
SITE     1 AE8 12 TRP B  33  TYR B  40  GLY B  59  PHE B  61                    
SITE     2 AE8 12 THR B 327  GLY B 328  TRP B 450  ALA B 454                    
SITE     3 AE8 12 CLA B 604  LMG B 620  BCR B 627  HOH B 714                    
SITE     1 AE9 13 THR B 236  SER B 239  ALA B 243  PHE B 246                    
SITE     2 AE9 13 PHE B 463  HIS B 466  CLA B 609  CLA B 610                    
SITE     3 AE9 13 PHE D 120  ILE D 123  MET D 126  CLA D 403                    
SITE     4 AE9 13 SQD D 408                                                     
SITE     1 AF1 12 PHE B 139  ALA B 212  PHE B 215  HIS B 216                    
SITE     2 AF1 12 PRO B 221  PRO B 222  CLA B 603  CLA B 608                    
SITE     3 AF1 12 CLA B 610  THR H  27  MET H  31  BCR H 102                    
SITE     1 AF2 12 LEU B 135  PHE B 139  HIS B 142  MET B 231                    
SITE     2 AF2 12 VAL B 237  SER B 240  SER B 241  CLA B 608                    
SITE     3 AF2 12 CLA B 609  CLA B 612  CLA B 615  HOH B 702                    
SITE     1 AF3 17 LHG A 616  TRP B   5  TYR B   6  ARG B   7                    
SITE     2 AF3 17 VAL B   8  HIS B   9  THR B  10  ILE B 242                    
SITE     3 AF3 17 LEU B 461  PHE B 462  GLY B 465  TRP B 468                    
SITE     4 AF3 17 HIS B 469  ARG B 472  CLA B 612  CLA B 613                    
SITE     5 AF3 17 LHG L 101                                                     
SITE     1 AF4 14 HIS B   9  LEU B  19  ALA B  22  HIS B  23                    
SITE     2 AF4 14 HIS B  26  THR B  27  VAL B 237  LEU B 238                    
SITE     3 AF4 14 SER B 241  CLA B 610  CLA B 611  CLA B 613                    
SITE     4 AF4 14 CLA B 614  CLA B 615                                          
SITE     1 AF5  8 HIS B   9  HIS B  26  VAL B  30  PHE B 462                    
SITE     2 AF5  8 CLA B 611  CLA B 612  CLA B 614  BCR B 617                    
SITE     1 AF6 11 VAL B   8  HIS B   9  CLA B 612  CLA B 613                    
SITE     2 AF6 11 BCR B 617  LMG B 620  SQD B 626  GLN L   8                    
SITE     3 AF6 11 VAL L  10  PHE M  21  LEU M  25                               
SITE     1 AF7 14 HIS B  23  LEU B  24  THR B  27  MET B 138                    
SITE     2 AF7 14 ILE B 141  HIS B 142  LEU B 145  CLA B 604                    
SITE     3 AF7 14 CLA B 610  CLA B 612  CLA B 616  LEU H  11                    
SITE     4 AF7 14 LEU H  14  ASN H  15                                          
SITE     1 AF8  8 ILE B  20  LEU B  24  ALA B 110  TRP B 113                    
SITE     2 AF8  8 HIS B 114  CLA B 615  BCR B 619  THR H   5                    
SITE     1 AF9 10 MET B  25  LEU B  29  TRP B 115  CLA B 613                    
SITE     2 AF9 10 CLA B 614  BCR B 618  LMG B 620  SQD B 626                    
SITE     3 AF9 10 BCR B 627  LEU M  13                                          
SITE     1 AG1  9 LEU B  29  GLY B  32  SER B  36  VAL B 102                    
SITE     2 AG1  9 SER B 104  GLY B 105  BCR B 617  LMG B 625                    
SITE     3 AG1  9 BCR B 627                                                     
SITE     1 AG2  6 LEU B 109  ALA B 110  CYS B 112  TRP B 113                    
SITE     2 AG2  6 CLA B 616  LMG B 625                                          
SITE     1 AG3 10 THR B 327  GLY B 328  PRO B 329  CLA B 607                    
SITE     2 AG3 10 CLA B 614  BCR B 617  LHG L 101  ASN M   4                    
SITE     3 AG3 10 GLN M   5  VAL M  17                                          
SITE     1 AG4  6 PRO B 183  GLU B 184  TRP B 185  CLA B 601                    
SITE     2 AG4  6 LEU C 204  PHE H  34                                          
SITE     1 AG5  7 TYR B 117  BCR B 618  BCR B 619  BCR B 627                    
SITE     2 AG5  7 LEU a  41  LEU a  42  THR a  45                               
SITE     1 AG6 11 ARG B  18  TRP B 115  CLA B 614  BCR B 617                    
SITE     2 AG6 11 ARG L   7  ARG l  14  TYR l  18  CYS t  12                    
SITE     3 AG6 11 LEU t  16  PHE t  19  PHE t  23                               
SITE     1 AG7  9 TRP B  33  SER B  36  MET B  37  CLA B 607                    
SITE     2 AG7  9 BCR B 617  BCR B 618  LMG B 625  PHE t  18                    
SITE     3 AG7  9 PHE t  22                                                     
SITE     1 AG8 15 LEU C  95  LEU C 168  GLY C 171  ALA C 172                    
SITE     2 AG8 15 LEU C 175  HIS C 237  ILE C 240  MET C 282                    
SITE     3 AG8 15 PHE C 289  TYR C 297  CLA C 502  CLA C 503                    
SITE     4 AG8 15 CLA C 506  CLA C 507  BCR C 515                               
SITE     1 AG9 15 TRP C  63  HIS C  91  LEU C 174  LYS C 178                    
SITE     2 AG9 15 LEU C 279  MET C 282  ALA C 286  TYR C 297                    
SITE     3 AG9 15 HIS C 430  LEU C 433  PHE C 437  CLA C 501                    
SITE     4 AG9 15 CLA C 503  CLA C 504  CLA C 510                               
SITE     1 AH1 11 VAL C  61  THR C  68  LEU C  88  HIS C  91                    
SITE     2 AH1 11 ILE C  92  VAL C 114  HIS C 118  MET C 282                    
SITE     3 AH1 11 CLA C 501  CLA C 502  CLA C 510                               
SITE     1 AH2 18 LHG A 617  TRP C  63  PHE C  70  GLN C  84                    
SITE     2 AH2 18 GLY C  85  ILE C  87  TRP C 425  SER C 429                    
SITE     3 AH2 18 HIS C 430  PHE C 436  CLA C 502  CLA C 508                    
SITE     4 AH2 18 DGD C 517  DGD C 518  LMG C 519  HOH C 601                    
SITE     5 AH2 18 PRO K  26  VAL K  30                                          
SITE     1 AH3 16 PHE A  33  LEU A 121  TRP A 131  CLA A 609                    
SITE     2 AH3 16 LMG A 612  PHE C 264  TYR C 274  GLY C 277                    
SITE     3 AH3 16 HIS C 441  LEU C 442  ALA C 445  ARG C 449                    
SITE     4 AH3 16 CLA C 507  BCR C 515  VAL I  16  PHE I  23                    
SITE     1 AH4 15 CLA A 609  LEU C 161  LEU C 165  ILE C 243                    
SITE     2 AH4 15 GLY C 247  TRP C 250  HIS C 251  THR C 255                    
SITE     3 AH4 15 PHE C 257  TRP C 259  PHE C 264  CLA C 501                    
SITE     4 AH4 15 CLA C 507  BCR C 515  DGD C 516                               
SITE     1 AH5 15 MET C 157  LEU C 161  HIS C 164  LEU C 168                    
SITE     2 AH5 15 PHE C 264  TRP C 266  TYR C 271  TYR C 274                    
SITE     3 AH5 15 SER C 275  LEU C 279  CLA C 501  CLA C 505                    
SITE     4 AH5 15 CLA C 506  CLA C 509  HOH C 603                               
SITE     1 AH6 21 LHG A 617  PHE C  33  TRP C  36  ALA C  37                    
SITE     2 AH6 21 GLY C  38  ASN C  39  ALA C  40  LEU C 272                    
SITE     3 AH6 21 LEU C 276  PHE C 436  PHE C 437  GLY C 440                    
SITE     4 AH6 21 TRP C 443  HIS C 444  CLA C 504  CLA C 509                    
SITE     5 AH6 21 CLA C 510  CLA C 511  DGD C 517  LMG C 519                    
SITE     6 AH6 21 LEU K  33                                                     
SITE     1 AH7 16 LEU C  49  ALA C  52  HIS C  53  HIS C  56                    
SITE     2 AH7 16 ILE C 160  HIS C 164  GLY C 268  TYR C 271                    
SITE     3 AH7 16 LEU C 272  SER C 275  LEU C 279  CLA C 507                    
SITE     4 AH7 16 CLA C 508  CLA C 510  CLA C 511  CLA C 512                    
SITE     1 AH8 14 LHG A 617  ASN C  39  HIS C  56  LEU C  59                    
SITE     2 AH8 14 LEU C 279  PHE C 436  PHE C 437  CLA C 502                    
SITE     3 AH8 14 CLA C 503  CLA C 508  CLA C 509  CLA C 511                    
SITE     4 AH8 14 PRO K  29  LEU K  33                                          
SITE     1 AH9 19 ASN C  25  TRP C  35  GLY C  38  ASN C  39                    
SITE     2 AH9 19 ARG C  41  LEU C  42  LEU C  45  LYS C  48                    
SITE     3 AH9 19 HIS C  56  CLA C 508  CLA C 509  CLA C 510                    
SITE     4 AH9 19 PHE K  32  TRP K  39  GLN K  40  BCR K 101                    
SITE     5 AH9 19 VAL Z  20  PRO Z  24  ALA Z  28                               
SITE     1 AI1  9 HIS C  53  ALA C  57  PHE C 147  PHE C 163                    
SITE     2 AI1  9 HIS C 164  VAL C 167  CLA C 509  CLA C 513                    
SITE     3 AI1  9 BCR C 514                                                     
SITE     1 AI2 11 LEU C  50  VAL C  54  VAL C 124  GLY C 128                    
SITE     2 AI2 11 TYR C 131  HIS C 132  LEU C 140  TYR C 143                    
SITE     3 AI2 11 PHE C 147  CLA C 512  BCR C 514                               
SITE     1 AI3  6 ILE C 120  SER C 121  VAL C 124  CLA C 512                    
SITE     2 AI3  6 CLA C 513  GLY Z  55                                          
SITE     1 AI4 10 ILE C 209  TYR C 212  LEU C 213  ASP C 232                    
SITE     2 AI4 10 GLY C 236  HIS C 237  PHE C 264  CLA C 501                    
SITE     3 AI4 10 CLA C 505  CLA C 506                                          
SITE     1 AI5 20 LEU A  91  PHE A 155  ILE A 163  PRO C 217                    
SITE     2 AI5 20 PHE C 218  GLY C 219  GLY C 220  GLU C 221                    
SITE     3 AI5 20 GLY C 222  TRP C 223  VAL C 227  CYS C 288                    
SITE     4 AI5 20 PHE C 292  ASN C 293  ASN C 294  THR C 295                    
SITE     5 AI5 20 ASP C 360  PHE C 361  ARG C 362  CLA C 506                    
SITE     1 AI6 16 PHE A 197  SQD A 603  GLU C  83  GLN C  84                    
SITE     2 AI6 16 GLY C  85  LEU C 404  SER C 406  ASN C 418                    
SITE     3 AI6 16 PHE C 419  VAL C 420  TRP C 425  SER C 429                    
SITE     4 AI6 16 CLA C 504  CLA C 508  DGD C 518  LMG C 519                    
SITE     1 AI7 21 PRO A 196  GLN A 199  ASN A 301  PHE A 302                    
SITE     2 AI7 21 SER A 305  LHG A 617  ASN C 405  SER C 406                    
SITE     3 AI7 21 VAL C 407  ASN C 415  SER C 416  ASN C 418                    
SITE     4 AI7 21 CLA C 504  DGD C 517  PHE J  29  ALA J  32                    
SITE     5 AI7 21 TYR J  33  GLY J  37  SER J  38  SER J  39                    
SITE     6 AI7 21 GLN V  34                                                     
SITE     1 AI8  7 HIS C  74  CLA C 504  CLA C 508  DGD C 517                    
SITE     2 AI8  7 ILE J  22  VAL K  27  GLN Y  21                               
SITE     1 AI9  6 ALA B 155  THR B 159  PRO B 183  LEU C 204                    
SITE     2 AI9  6 PRO C 206  HOH C 607                                          
SITE     1 AJ1 20 LEU A 210  MET A 214  LEU A 258  CLA A 607                    
SITE     2 AJ1 20 ALA D  41  ALA D  44  TRP D  48  ILE D 114                    
SITE     3 AJ1 20 GLY D 121  LEU D 122  PHE D 125  GLN D 129                    
SITE     4 AJ1 20 ASN D 142  PHE D 146  PRO D 149  PHE D 153                    
SITE     5 AJ1 20 GLY D 174  PRO D 275  LEU D 279  CLA D 402                    
SITE     1 AJ2 20 MET A 183  CLA A 606  CLA A 607  CLA A 615                    
SITE     2 AJ2 20 TRP D  48  PRO D 149  VAL D 152  VAL D 156                    
SITE     3 AJ2 20 LEU D 182  PHE D 185  GLN D 186  TRP D 191                    
SITE     4 AJ2 20 THR D 192  HIS D 197  GLY D 200  VAL D 201                    
SITE     5 AJ2 20 VAL D 204  SER D 282  ALA D 283  PHO D 401                    
SITE     1 AJ3 14 CLA B 608  ILE D  35  PRO D  39  LEU D  43                    
SITE     2 AJ3 14 LEU D  89  LEU D  90  LEU D  91  LEU D  92                    
SITE     3 AJ3 14 TRP D  93  THR D 112  PHE D 113  LEU D 116                    
SITE     4 AJ3 14 HIS D 117  GLY X  13                                          
SITE     1 AJ4 10 TYR D  42  LEU D  43  GLY D  46  GLY D  47                    
SITE     2 AJ4 10 LEU D  49  THR D  50  PHE D 101  LMG D 405                    
SITE     3 AJ4 10 PRO F  29  PHE F  33                                          
SITE     1 AJ5 12 TYR D  67  CYS D  71  ASN D  72  PHE D  73                    
SITE     2 AJ5 12 BCR D 404  THR F  30  MET F  40  GLN F  41                    
SITE     3 AJ5 12 PHE J  28  GLY J  31  ALA J  32  LEU J  36                    
SITE     1 AJ6 13 PHE D 257  ILE D 259  ALA D 260  PHE D 261                    
SITE     2 AJ6 13 SER D 262  ASN D 263  TRP D 266  ASN L  13                    
SITE     3 AJ6 13 THR L  15  LEU L  19  LHG L 101  PHE T  17                    
SITE     4 AJ6 13 ALA T  20                                                     
SITE     1 AJ7 17 PHE A  52  ILE A  77  CLA A 615  MET D 199                    
SITE     2 AJ7 17 LEU D 210  ILE D 213  HIS D 214  THR D 217                    
SITE     3 AJ7 17 TRP D 253  ILE D 259  ALA D 260  PHE D 261                    
SITE     4 AJ7 17 LEU D 267  VAL D 274  LEU L  23  LEU L  29                    
SITE     5 AJ7 17 LHG L 101                                                     
SITE     1 AJ8  9 ALA B 228  ARG B 230  LYS B 498  CLA B 608                    
SITE     2 AJ8  9 ASP D  19  LYS D  23  TRP D  32  ARG D 134                    
SITE     3 AJ8  9 LEU D 135                                                     
SITE     1 AJ9 13 PL9 A 611  ARG D  24  ARG D  26  GLU E   7                    
SITE     2 AJ9 13 PHE F  16  THR F  17  VAL F  18  GLN R  30                    
SITE     3 AJ9 13 LEU R  34  THR X  24  ILE X  31  ASP X  35                    
SITE     4 AJ9 13 HOH X 101                                                     
SITE     1 AK1 12 PHE E  10  ILE E  13  ARG E  18  TYR E  19                    
SITE     2 AK1 12 HIS E  23  LEU E  30  ILE F  15  ARG F  19                    
SITE     3 AK1 12 TRP F  20  HIS F  24  ALA F  27  ILE F  31                    
SITE     1 AK2  5 CLA B 601  CLA B 602  CLA B 609  LEU H  37                    
SITE     2 AK2  5 PHE H  38                                                     
SITE     1 AK3 15 TYR B 193  PHE B 250  TYR B 258  TYR B 273                    
SITE     2 AK3 15 GLN B 274  SER B 277  CLA B 602  HIS D  87                    
SITE     3 AK3 15 LEU D 162  LEU H  46  TYR H  49  ASN H  50                    
SITE     4 AK3 15 VAL H  60  SER H  61  TRP H  62                               
SITE     1 AK4  7 LEU A 102  BCR A 610  SQD A 619  FME I   1                    
SITE     2 AK4  7 THR I   3  LEU I   4  PHE I  15                               
SITE     1 AK5  6 LEU C  59  PHE C  62  ALA C 123  CLA C 511                    
SITE     2 AK5  6 PHE K  32  SER Z  16                                          
SITE     1 AK6 19 SER A 232  ASN A 234  LHG A 616  PRO B   4                    
SITE     2 AK6 19 TRP B   5  TYR B   6  CLA B 611  LMG B 620                    
SITE     3 AK6 19 TRP D 266  PHE D 273  LHG D 406  PL9 D 407                    
SITE     4 AK6 19 GLU L  11  LEU L  12  ASN L  13  SER L  16                    
SITE     5 AK6 19 GLY L  20  LEU L  23  PHE M  21                               
SITE     1 AK7 10 LMG A 613  PHE T   8  ALA T  15  PHE T  18                    
SITE     2 AK7 10 PHE T  22  TRP b  33  SER b  36  SQD b 601                    
SITE     3 AK7 10 CLA b 610  BCR b 621                                          
SITE     1 AK8 15 ALA V  36  CYS V  37  SER V  39  CYS V  40                    
SITE     2 AK8 15 HIS V  41  THR V  46  THR V  48  LEU V  52                    
SITE     3 AK8 15 ASP V  53  THR V  58  LEU V  59  TYR V  75                    
SITE     4 AK8 15 MET V  76  TYR V  82  HIS V  92                               
SITE     1 AK9 13 PHE C  62  THR J  15  LEU K  25  ILE K  28                    
SITE     2 AK9 13 LEU K  31  ALA K  34  VAL K  38  ILE Y  28                    
SITE     3 AK9 13 GLY Y  29  GLY Y  32  VAL Z  13  SER Z  16                    
SITE     4 AK9 13 PHE Z  17                                                     
SITE     1 AL1 12 ASP a 170  GLU a 189  HIS a 332  GLU a 333                    
SITE     2 AL1 12 HIS a 337  ASP a 342  ALA a 344  HOH a 701                    
SITE     3 AL1 12 HOH a 707  HOH a 711  GLU c 354  ARG c 357                    
SITE     1 AL2  5 HIS a 215  HIS a 272  BCT a 605  HIS d 214                    
SITE     2 AL2  5 HIS d 268                                                     
SITE     1 AL3  3 HIS a 332  GLU a 333  LYS d 317                               
SITE     1 AL4  2 ASN a 338  PHE a 339                                          
SITE     1 AL5  8 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 AL5  8 FE2 a 602  HIS d 214  TYR d 244  HIS d 268                    
SITE     1 AL6 18 PRO a 150  SER a 153  VAL a 157  MET a 183                    
SITE     2 AL6 18 PHE a 186  ILE a 192  LEU a 193  HIS a 198                    
SITE     3 AL6 18 GLY a 201  VAL a 202  THR a 286  ILE a 290                    
SITE     4 AL6 18 CLA a 607  PHO a 608  CLA a 612  CLA d 403                    
SITE     5 AL6 18 LHG d 407  PHE t  17                                          
SITE     1 AL7 15 GLN a 199  VAL a 202  ALA a 203  PHE a 206                    
SITE     2 AL7 15 GLY a 207  TRP a 278  CLA a 606  HOH a 706                    
SITE     3 AL7 15 PHE d 157  VAL d 175  ILE d 178  PHE d 179                    
SITE     4 AL7 15 LEU d 182  PHO d 401  CLA d 403                               
SITE     1 AL8 17 LEU a  41  ALA a  44  THR a  45  PHE a  48                    
SITE     2 AL8 17 TYR a 126  GLN a 130  ALA a 146  TYR a 147                    
SITE     3 AL8 17 PRO a 279  VAL a 283  CLA a 606  CLA a 612                    
SITE     4 AL8 17 ALA d 208  LEU d 209  ILE d 213  TRP d 253                    
SITE     5 AL8 17 PHE d 257                                                     
SITE     1 AL9 14 PRO a  39  PHE a  93  TYR a  94  PRO a  95                    
SITE     2 AL9 14 ILE a  96  TRP a  97  LEU a 114  PHE a 117                    
SITE     3 AL9 14 HIS a 118  BCR a 610  CLA c 507  CLA c 508                    
SITE     4 AL9 14 TYR i   9  PHE i  15                                          
SITE     1 AM1  3 ALA a  43  ILE a  50  CLA a 609                               
SITE     1 AM2 12 HIS a 215  LEU a 218  ALA a 263  SER a 264                    
SITE     2 AM2 12 PHE a 265  LEU a 271  LEU a 275  LHG a 615                    
SITE     3 AM2 12 PHE d  38  PHO d 401  ALA f  22  THR x  24                    
SITE     1 AM3 18 VAL a 157  PHE a 158  MET a 172  ILE a 176                    
SITE     2 AM3 18 THR a 179  PHE a 180  MET a 183  CLA a 606                    
SITE     3 AM3 18 PHO a 608  HOH a 710  MET d 198  VAL d 201                    
SITE     4 AM3 18 ALA d 202  GLY d 206  CLA d 403  LHG d 407                    
SITE     5 AM3 18 PL9 d 408  LHG l 101                                          
SITE     1 AM4 13 SER a 232  ASN a 234  TYR b   6  ARG b   7                    
SITE     2 AM4 13 TRP b 468  CLA b 610  CLA b 614  TYR d 141                    
SITE     3 AM4 13 TRP d 266  PHE d 269  LHG l 101  PHE m  14                    
SITE     4 AM4 13 PRO m  18                                                     
SITE     1 AM5 12 ARG a 140  TRP a 142  PHE a 273  TRP c  36                    
SITE     2 AM5 12 TRP c 443  ARG c 447  CLA c 510  GLU d 219                    
SITE     3 AM5 12 ASN d 220  ALA d 229  THR d 231  PHE d 232                    
SITE     1 AM6 10 LEU a 258  PHE a 260  TYR a 262  ALA a 263                    
SITE     2 AM6 10 PL9 a 611  PHE d  27  VAL d  28  PRO e   9                    
SITE     3 AM6 10 PHE e  10  SER e  11                                          
SITE     1 AM7  9 ARG L  14  TYR L  18  TYR M  26  CYS T  12                    
SITE     2 AM7  9 PHE T  23  BCR T 101  ARG b  18  CLA b 617                    
SITE     3 AM7  9 ARG l   7                                                     
SITE     1 AM8  7 PHE b 190  CLA b 605  LMG b 624  HOH b 709                    
SITE     2 AM8  7 PHE h  41  LEU h  55  BCR h 101                               
SITE     1 AM9 15 GLY b 189  PHE b 190  PRO b 192  GLY b 197                    
SITE     2 AM9 15 HIS b 201  ALA b 204  PHE b 247  PHE b 250                    
SITE     3 AM9 15 VAL b 251  CLA b 604  CLA b 606  LEU d 158                    
SITE     4 AM9 15 PHE h  41  ILE h  45  TYR h  49                               
SITE     1 AN1 16 ARG b  68  LEU b  69  ALA b 146  CYS b 150                    
SITE     2 AN1 16 PHE b 153  HIS b 201  HIS b 202  ALA b 248                    
SITE     3 AN1 16 VAL b 252  THR b 262  CLA b 605  CLA b 607                    
SITE     4 AN1 16 CLA b 608  CLA b 609  CLA b 612  PHE h  38                    
SITE     1 AN2 20 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 AN2 20 LEU b 145  LEU b 149  VAL b 245  ALA b 248                    
SITE     3 AN2 20 ALA b 249  VAL b 252  PHE b 451  HIS b 455                    
SITE     4 AN2 20 PHE b 458  CLA b 606  CLA b 608  CLA b 609                    
SITE     5 AN2 20 CLA b 610  CLA b 615  CLA b 616  CLA b 618                    
SITE     1 AN3 19 THR b  27  VAL b  30  ALA b  31  TRP b  33                    
SITE     2 AN3 19 ALA b  34  VAL b  62  PHE b  65  MET b  66                    
SITE     3 AN3 19 ARG b  68  VAL b  96  HIS b 100  LEU b 103                    
SITE     4 AN3 19 LEU b 143  ALA b 205  CLA b 606  CLA b 607                    
SITE     5 AN3 19 CLA b 609  CLA b 612  CLA b 613                               
SITE     1 AN4 17 LEU b  69  VAL b  71  PHE b  90  TRP b  91                    
SITE     2 AN4 17 VAL b  96  HIS b 100  LEU b 149  GLY b 152                    
SITE     3 AN4 17 PHE b 153  PHE b 156  HIS b 157  PHE b 162                    
SITE     4 AN4 17 PRO b 164  CLA b 606  CLA b 607  CLA b 608                    
SITE     5 AN4 17 BCR b 622                                                     
SITE     1 AN5 12 BCR T 101  LHG a 613  TRP b  33  TYR b  40                    
SITE     2 AN5 12 GLY b  59  PHE b  61  THR b 327  GLY b 328                    
SITE     3 AN5 12 TRP b 450  CLA b 607  LMG b 623  HOH b 705                    
SITE     1 AN6 16 THR b 236  SER b 239  ALA b 243  PHE b 247                    
SITE     2 AN6 16 PHE b 463  HIS b 466  ILE b 467  CLA b 612                    
SITE     3 AN6 16 CLA b 613  LMG b 625  PHE d 120  ILE d 123                    
SITE     4 AN6 16 MET d 126  CLA d 404  LEU h  43  DGD h 102                    
SITE     1 AN7 15 PHE b 139  VAL b 208  ALA b 212  PHE b 215                    
SITE     2 AN7 15 HIS b 216  PRO b 221  PRO b 222  CLA b 606                    
SITE     3 AN7 15 CLA b 608  CLA b 611  CLA b 613  THR h  27                    
SITE     4 AN7 15 MET h  31  LEU h  42  BCR h 101                               
SITE     1 AN8 14 LEU b 135  MET b 138  PHE b 139  HIS b 142                    
SITE     2 AN8 14 THR b 236  VAL b 237  SER b 240  SER b 241                    
SITE     3 AN8 14 CLA b 608  CLA b 611  CLA b 612  CLA b 615                    
SITE     4 AN8 14 CLA b 618  HOH b 707                                          
SITE     1 AN9 18 LHG a 613  TRP b   5  TYR b   6  ARG b   7                    
SITE     2 AN9 18 VAL b   8  HIS b   9  ILE b 242  PHE b 458                    
SITE     3 AN9 18 LEU b 461  PHE b 462  GLY b 465  TRP b 468                    
SITE     4 AN9 18 HIS b 469  ARG b 472  PHE b 479  CLA b 615                    
SITE     5 AN9 18 CLA b 616  LHG l 101                                          
SITE     1 AO1 17 HIS b   9  LEU b  12  LEU b  19  ALA b  22                    
SITE     2 AO1 17 HIS b  23  HIS b  26  THR b  27  VAL b 237                    
SITE     3 AO1 17 LEU b 238  SER b 241  VAL b 245  CLA b 607                    
SITE     4 AO1 17 CLA b 613  CLA b 614  CLA b 616  CLA b 617                    
SITE     5 AO1 17 CLA b 618                                                     
SITE     1 AO2 10 HIS b   9  HIS b  26  VAL b  30  CLA b 607                    
SITE     2 AO2 10 CLA b 614  CLA b 615  CLA b 617  BCR b 620                    
SITE     3 AO2 10 LMG b 623  PHE m  14                                          
SITE     1 AO3 13 PHE T   8  VAL b   8  HIS b   9  VAL b  11                    
SITE     2 AO3 13 TRP b 115  SQD b 601  CLA b 615  CLA b 616                    
SITE     3 AO3 13 BCR b 620  LMG b 623  GLN l   8  VAL l  10                    
SITE     4 AO3 13 PHE m  21                                                     
SITE     1 AO4 10 HIS b  23  MET b 138  HIS b 142  LEU b 145                    
SITE     2 AO4 10 CLA b 607  CLA b 613  CLA b 615  CLA b 619                    
SITE     3 AO4 10 LEU h  11  ASN h  15                                          
SITE     1 AO5  8 ILE b  20  LEU b  24  TRP b 113  HIS b 114                    
SITE     2 AO5  8 LEU b 120  CLA b 618  BCR b 622  THR h   5                    
SITE     1 AO6  8 MET b  25  LEU b  29  TRP b 115  CLA b 616                    
SITE     2 AO6  8 CLA b 617  BCR b 621  LMG b 623  LEU m  13                    
SITE     1 AO7  7 BCR T 101  LEU b  29  GLY b  32  SER b  36                    
SITE     2 AO7  7 VAL b 102  GLY b 105  BCR b 620                               
SITE     1 AO8  6 LMG A 613  LEU b 109  CYS b 112  TRP b 113                    
SITE     2 AO8  6 CLA b 609  CLA b 619                                          
SITE     1 AO9  9 THR b 327  GLY b 328  PHE b 453  CLA b 610                    
SITE     2 AO9  9 CLA b 616  CLA b 617  BCR b 620  LHG l 101                    
SITE     3 AO9  9 ASN m   4                                                     
SITE     1 AP1  4 GLU b 184  TRP b 185  CLA b 604  CLA c 514                    
SITE     1 AP2  3 ALA b 228  CLA b 611  LMG d 409                               
SITE     1 AP3  9 ASN a 267  SER a 270  PHE a 274  TRP a 278                    
SITE     2 AP3  9 GLN c  28  TRP c  36  PHE d 232  ARG d 233                    
SITE     3 AP3  9 PHE k  37                                                     
SITE     1 AP4 12 TRP a  97  GLU a  98  LEU c 213  LEU c 214                    
SITE     2 AP4 12 LYS c 215  SER c 216  PHE c 218  TRP c 223                    
SITE     3 AP4 12 PHE c 284  CLA c 507  DGD c 518  TYR i   9                    
SITE     1 AP5 15 LEU c  95  GLY c 171  ALA c 172  LEU c 175                    
SITE     2 AP5 15 VAL c 233  HIS c 237  MET c 282  PHE c 289                    
SITE     3 AP5 15 VAL c 296  TYR c 297  CLA c 504  CLA c 505                    
SITE     4 AP5 15 CLA c 508  CLA c 509  BCR c 517                               
SITE     1 AP6 15 TRP c  63  HIS c  91  LEU c 174  PHE c 182                    
SITE     2 AP6 15 LEU c 279  MET c 282  ALA c 286  TYR c 297                    
SITE     3 AP6 15 HIS c 430  LEU c 433  PHE c 437  CLA c 503                    
SITE     4 AP6 15 CLA c 505  CLA c 506  CLA c 512                               
SITE     1 AP7 12 ILE c  60  VAL c  61  THR c  68  LEU c  88                    
SITE     2 AP7 12 HIS c  91  ILE c  92  VAL c 114  HIS c 118                    
SITE     3 AP7 12 CLA c 503  CLA c 504  CLA c 512  CLA c 515                    
SITE     1 AP8 17 TRP c  63  MET c  67  PHE c  70  GLN c  84                    
SITE     2 AP8 17 GLY c  85  ILE c  87  TRP c 425  SER c 429                    
SITE     3 AP8 17 HIS c 430  PHE c 436  CLA c 504  DGD c 519                    
SITE     4 AP8 17 DGD c 520  LMG c 521  HOH c 608  PRO k  26                    
SITE     5 AP8 17 VAL k  30                                                     
SITE     1 AP9 15 PHE a  33  TRP a 131  CLA a 609  TYR c 274                    
SITE     2 AP9 15 GLY c 277  HIS c 441  LEU c 442  ALA c 445                    
SITE     3 AP9 15 ARG c 449  LMG c 502  CLA c 509  BCR c 517                    
SITE     4 AP9 15 VAL i  12  VAL i  16  PHE i  23                               
SITE     1 AQ1 13 CLA a 609  LEU c 165  ILE c 243  GLY c 247                    
SITE     2 AQ1 13 TRP c 250  HIS c 251  THR c 255  PHE c 257                    
SITE     3 AQ1 13 TRP c 259  PHE c 264  CLA c 503  CLA c 509                    
SITE     4 AQ1 13 BCR c 517                                                     
SITE     1 AQ2 19 MET c 157  LEU c 161  HIS c 164  LEU c 168                    
SITE     2 AQ2 19 TRP c 259  PHE c 264  TRP c 266  TYR c 271                    
SITE     3 AQ2 19 TYR c 274  SER c 275  ALA c 278  LEU c 279                    
SITE     4 AQ2 19 MET c 282  CLA c 503  CLA c 507  CLA c 508                    
SITE     5 AQ2 19 CLA c 511  BCR c 517  HOH c 609                               
SITE     1 AQ3 16 LHG a 614  PHE c  33  TRP c  36  ALA c  37                    
SITE     2 AQ3 16 GLY c  38  ASN c  39  LEU c 272  LEU c 276                    
SITE     3 AQ3 16 PHE c 436  PHE c 437  GLY c 440  TRP c 443                    
SITE     4 AQ3 16 HIS c 444  CLA c 511  CLA c 512  CLA c 513                    
SITE     1 AQ4 14 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 AQ4 14 HIS c  56  GLY c 268  LEU c 272  SER c 275                    
SITE     3 AQ4 14 LEU c 279  CLA c 509  CLA c 510  CLA c 512                    
SITE     4 AQ4 14 CLA c 513  CLA c 514                                          
SITE     1 AQ5 11 ASN c  39  HIS c  56  LEU c  59  PHE c 437                    
SITE     2 AQ5 11 CLA c 504  CLA c 505  CLA c 510  CLA c 511                    
SITE     3 AQ5 11 CLA c 513  PRO k  29  LEU k  33                               
SITE     1 AQ6 22 ASN c  25  ARG c  26  GLY c  38  ASN c  39                    
SITE     2 AQ6 22 ARG c  41  LEU c  42  LEU c  45  LYS c  48                    
SITE     3 AQ6 22 ILE c 134  CLA c 510  CLA c 511  CLA c 512                    
SITE     4 AQ6 22 PHE k  32  LEU k  33  ALA k  36  TRP k  39                    
SITE     5 AQ6 22 GLN k  40  BCR k 101  ASN y  45  LEU y  46                    
SITE     6 AQ6 22 VAL z  20  ALA z  28                                          
SITE     1 AQ7  9 LMG b 624  HIS c  53  PHE c 147  PHE c 163                    
SITE     2 AQ7  9 HIS c 164  ILE c 166  VAL c 167  CLA c 511                    
SITE     3 AQ7  9 CLA c 515                                                     
SITE     1 AQ8 13 LEU c  50  VAL c  54  VAL c 124  GLY c 128                    
SITE     2 AQ8 13 TYR c 131  HIS c 132  PRO c 137  LEU c 140                    
SITE     3 AQ8 13 TYR c 143  PHE c 147  CLA c 505  CLA c 514                    
SITE     4 AQ8 13 BCR c 516                                                     
SITE     1 AQ9  6 VAL c 116  SER c 121  CLA c 515  TYR k  15                    
SITE     2 AQ9  6 GLY z  55  ASN z  58                                          
SITE     1 AR1 12 ILE c 209  LEU c 213  ASP c 232  GLY c 236                    
SITE     2 AR1 12 HIS c 237  ILE c 240  PHE c 264  CLA c 503                    
SITE     3 AR1 12 CLA c 507  CLA c 508  CLA c 509  LEU i  24                    
SITE     1 AR2 17 PHE a 155  PRO c 217  GLY c 219  GLY c 220                    
SITE     2 AR2 17 GLU c 221  GLY c 222  VAL c 225  VAL c 227                    
SITE     3 AR2 17 CYS c 288  ASN c 293  ASN c 294  THR c 295                    
SITE     4 AR2 17 ASP c 360  PHE c 361  ARG c 362  LMG c 502                    
SITE     5 AR2 17 HOH c 610                                                     
SITE     1 AR3 15 LEU a 297  GLU c  83  GLN c  84  GLY c  85                    
SITE     2 AR3 15 SER c 406  ASN c 418  PHE c 419  VAL c 420                    
SITE     3 AR3 15 TRP c 425  THR c 428  CLA c 506  DGD c 520                    
SITE     4 AR3 15 LMG c 521  PHE j  29  TYR j  33                               
SITE     1 AR4 18 GLN a 199  PHE a 300  ASN a 301  SER a 305                    
SITE     2 AR4 18 ASN c 405  SER c 406  VAL c 407  ASN c 415                    
SITE     3 AR4 18 SER c 416  ASN c 418  CLA c 506  DGD c 519                    
SITE     4 AR4 18 PHE j  29  ALA j  32  TYR j  33  GLY j  37                    
SITE     5 AR4 18 SER j  38  GLN v  34                                          
SITE     1 AR5  7 HIS c  74  CLA c 506  DGD c 519  ASP k  23                    
SITE     2 AR5  7 VAL k  27  GLN y  21  ILE y  25                               
SITE     1 AR6  8 PHE b 151  ALA b 155  THR b 159  PRO b 183                    
SITE     2 AR6  8 TRP b 185  ILE b 207  LEU c 204  PRO c 206                    
SITE     1 AR7 20 ALA a 209  LEU a 210  MET a 214  LEU a 258                    
SITE     2 AR7 20 CLA a 607  PL9 a 611  ALA d  41  ALA d  44                    
SITE     3 AR7 20 TRP d  48  GLY d 121  LEU d 122  PHE d 125                    
SITE     4 AR7 20 GLN d 129  ASN d 142  PHE d 146  PHE d 153                    
SITE     5 AR7 20 GLY d 174  PRO d 275  LEU d 279  CLA d 403                    
SITE     1 AR8 19 PHE a 206  CLA a 606  CLA a 607  CLA a 612                    
SITE     2 AR8 19 PRO d 149  VAL d 152  VAL d 156  LEU d 182                    
SITE     3 AR8 19 PHE d 185  GLN d 186  TRP d 191  THR d 192                    
SITE     4 AR8 19 HIS d 197  GLY d 200  VAL d 201  VAL d 204                    
SITE     5 AR8 19 SER d 282  ALA d 283  PHO d 401                               
SITE     1 AR9 16 CLA b 611  ILE d  35  PRO d  39  CYS d  40                    
SITE     2 AR9 16 LEU d  43  LEU d  89  LEU d  90  LEU d  91                    
SITE     3 AR9 16 LEU d  92  TRP d  93  THR d 112  PHE d 113                    
SITE     4 AR9 16 HIS d 117  LEU h  39  GLY x  13  LEU x  14                    
SITE     1 AS1  9 TYR d  42  LEU d  43  GLY d  46  LEU d  49                    
SITE     2 AS1  9 LMG d 406  PRO f  29  THR f  30  PHE f  33                    
SITE     3 AS1  9 VAL j  21                                                     
SITE     1 AS2 12 TYR d  67  CYS d  71  ASN d  72  PHE d  73                    
SITE     2 AS2 12 BCR d 405  THR f  30  MET f  40  GLN f  41                    
SITE     3 AS2 12 PHE j  28  GLY j  31  ALA j  32  LEU j  36                    
SITE     1 AS3 15 CLA a 606  CLA a 612  PHE d 257  ILE d 259                    
SITE     2 AS3 15 ALA d 260  PHE d 261  SER d 262  ASN d 263                    
SITE     3 AS3 15 TRP d 266  PL9 d 408  ASN l  13  THR l  15                    
SITE     4 AS3 15 LEU l  19  LHG l 101  PHE t  17                               
SITE     1 AS4 17 PHE a  52  CLA a 612  MET d 199  LEU d 210                    
SITE     2 AS4 17 ILE d 213  HIS d 214  THR d 217  TRP d 253                    
SITE     3 AS4 17 ALA d 260  PHE d 261  VAL d 274  LHG d 407                    
SITE     4 AS4 17 LEU l  23  VAL l  26  LEU l  27  LEU l  29                    
SITE     5 AS4 17 LHG l 101                                                     
SITE     1 AS5  5 LMG b 625  ASP d  19  LYS d  23  TRP d  32                    
SITE     2 AS5  5 ARG d 134                                                     
SITE     1 AS6 11 PHE e  10  ILE e  13  ARG e  18  TYR e  19                    
SITE     2 AS6 11 HIS e  23  LEU e  30  ILE f  15  ARG f  19                    
SITE     3 AS6 11 TRP f  20  HIS f  24  ILE f  31                               
SITE     1 AS7 10 ARG d  24  ARG d  26  PHE f  16  THR f  17                    
SITE     2 AS7 10 VAL f  18  VAL f  21  GLN r  30  VAL r  31                    
SITE     3 AS7 10 LEU r  34  ASP x  35                                          
SITE     1 AS8  6 CLA b 604  CLA b 612  LEU h  37  PHE h  38                    
SITE     2 AS8  6 PHE h  41  ILE h  44                                          
SITE     1 AS9 13 PHE b 250  TYR b 258  TYR b 273  TYR b 279                    
SITE     2 AS9 13 CLA b 611  HIS d  87  LEU d 162  GLY d 163                    
SITE     3 AS9 13 TYR h  49  ASN h  50  VAL h  60  SER h  61                    
SITE     4 AS9 13 TRP h  62                                                     
SITE     1 AT1  4 ALA c 123  CLA c 513  PHE k  32  SER z  16                    
SITE     1 AT2 19 SER a 232  ASN a 234  CLA a 612  LHG a 613                    
SITE     2 AT2 19 PRO b   4  TRP b   5  TYR b   6  CLA b 614                    
SITE     3 AT2 19 LMG b 623  TRP d 266  PHE d 273  LHG d 407                    
SITE     4 AT2 19 PL9 d 408  GLU l  11  LEU l  12  ASN l  13                    
SITE     5 AT2 19 SER l  16  GLY l  20  PHE m  21                               
SITE     1 AT3 11 PHE c  62  THR j  15  ILE k  28  LEU k  31                    
SITE     2 AT3 11 ALA k  34  VAL k  38  ILE y  28  GLY y  29                    
SITE     3 AT3 11 GLY y  32  SER z  16  PHE z  17                               
SITE     1 AT4 15 PHE v  33  TYR v  35  ALA v  36  ALA v  38                    
SITE     2 AT4 15 SER v  39  CYS v  40  HIS v  41  THR v  48                    
SITE     3 AT4 15 LEU v  52  ASP v  53  THR v  58  LEU v  59                    
SITE     4 AT4 15 TYR v  75  ILE v  88  HIS v  92                               
SITE     1 AT5 17 ALA v  36  CYS v  37  ALA v  38  SER v  39                    
SITE     2 AT5 17 HIS v  41  VAL v  42  ILE v  45  THR v  46                    
SITE     3 AT5 17 LYS v  47  THR v  48  LEU v  52  ASP v  53                    
SITE     4 AT5 17 THR v  58  LEU v  59  TYR v  75  ILE v  88                    
SITE     5 AT5 17 HIS v  92                                                     
SITE     1 AT6 15 PHE v  33  TYR v  35  ALA v  36  ALA v  38                    
SITE     2 AT6 15 SER v  39  CYS v  40  HIS v  41  THR v  48                    
SITE     3 AT6 15 LEU v  52  ASP v  53  THR v  58  LEU v  59                    
SITE     4 AT6 15 TYR v  75  ILE v  88  HIS v  92                               
CRYST1  117.731  223.815  330.818  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      0.008494  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004468  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003023        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system