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Database: PDB
Entry: 5TIS
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HEADER    PHOTOSYNTHESIS                          03-OCT-16   5TIS              
TITLE     ROOM TEMPERATURE XFEL STRUCTURE OF THE NATIVE, DOUBLY-ILLUMINATED     
TITLE    2 PHOTOSYSTEM II COMPLEX                                               
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;                  
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;                  
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;                  
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,    
KEYWDS   2 PHOTOSYNTHESIS                                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.D.YOUNG,M.IBRAHIM,R.CHATTERJEE,S.GUL,F.FULLER,S.KOROIDOV,           
AUTHOR   2 A.S.BREWSTER,R.TRAN,R.ALONSO-MORI,T.KROLL,T.MICHELS-CLARK,           
AUTHOR   3 H.LAKSMONO,R.G.SIERRA,C.A.STAN,R.HUSSEIN,M.ZHANG,L.DOUTHIT,M.KUBIN,  
AUTHOR   4 C.DE LICHTENBERG,L.V.PHAM,H.NILSSON,M.H.CHEAH,D.SHEVELA,C.SARACINI,  
AUTHOR   5 M.A.BEAN,I.SEUFFERT,D.SOKARAS,T.-C.WENG,E.PASTOR,C.WENINGER,         
AUTHOR   6 T.FRANSSON,L.LASSALLE,P.BRAEUER,P.ALLER,P.T.DOCKER,B.ANDI,           
AUTHOR   7 A.M.ORVILLE,J.M.GLOWNIA,S.NELSON,M.SIKORSKI,D.ZHU,M.S.HUNTER,        
AUTHOR   8 A.AQUILA,J.E.KOGLIN,J.ROBINSON,M.LIANG,S.BOUTET,A.Y.LYUBIMOV,        
AUTHOR   9 M.UERVIROJNANGKOORN,N.W.MORIARTY,D.LIEBSCHNER,P.V.AFONINE,           
AUTHOR  10 D.G.WATERMANN,G.EVANS,P.WERNET,H.DOBBEK,W.I.WEIS,A.T.BRUNGER,        
AUTHOR  11 P.H.ZWART,P.D.ADAMS,A.ZOUNI,J.MESSINGER,U.BERGMANN,N.K.SAUTER,       
AUTHOR  12 J.KERN,V.K.YACHANDRA,J.YANO                                          
REVDAT   6   01-JAN-20 5TIS    1       REMARK                                   
REVDAT   5   20-NOV-19 5TIS    1       REMARK                                   
REVDAT   4   27-SEP-17 5TIS    1       REMARK                                   
REVDAT   3   28-DEC-16 5TIS    1       JRNL                                     
REVDAT   2   14-DEC-16 5TIS    1       JRNL                                     
REVDAT   1   23-NOV-16 5TIS    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.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX DEV_2481                                      
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.28                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.325                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 385545                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.889                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3426                            
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 44.2852 -  6.4836    1.00    16669   150  0.1671 0.1996        
REMARK   3     2  6.4836 -  5.1487    1.00    16221   145  0.1753 0.2027        
REMARK   3     3  5.1487 -  4.4986    1.00    16104   144  0.1539 0.1954        
REMARK   3     4  4.4986 -  4.0876    1.00    16055   145  0.1520 0.1764        
REMARK   3     5  4.0876 -  3.7948    1.00    16011   141  0.1600 0.1879        
REMARK   3     6  3.7948 -  3.5712    1.00    15927   144  0.1681 0.1990        
REMARK   3     7  3.5712 -  3.3924    1.00    15987   143  0.1788 0.2289        
REMARK   3     8  3.3924 -  3.2448    1.00    15940   143  0.1824 0.2412        
REMARK   3     9  3.2448 -  3.1199    1.00    15884   143  0.1955 0.2441        
REMARK   3    10  3.1199 -  3.0123    1.00    15888   141  0.2002 0.2329        
REMARK   3    11  3.0123 -  2.9181    1.00    15905   142  0.2007 0.2332        
REMARK   3    12  2.9181 -  2.8347    1.00    15860   144  0.2065 0.2724        
REMARK   3    13  2.8347 -  2.7601    1.00    15879   143  0.2105 0.2596        
REMARK   3    14  2.7601 -  2.6928    1.00    15846   143  0.2234 0.2686        
REMARK   3    15  2.6928 -  2.6315    1.00    15827   137  0.2368 0.2965        
REMARK   3    16  2.6315 -  2.5756    1.00    15809   146  0.2509 0.2910        
REMARK   3    17  2.5756 -  2.5240    1.00    15859   145  0.2572 0.3153        
REMARK   3    18  2.5240 -  2.4764    1.00    15823   140  0.2679 0.2714        
REMARK   3    19  2.4764 -  2.4322    1.00    15850   139  0.2870 0.3425        
REMARK   3    20  2.4322 -  2.3910    1.00    15764   140  0.3005 0.3175        
REMARK   3    21  2.3910 -  2.3524    1.00    15735   146  0.3157 0.3893        
REMARK   3    22  2.3524 -  2.3162    1.00    15806   141  0.3249 0.3876        
REMARK   3    23  2.3162 -  2.2821    1.00    15786   141  0.3369 0.3493        
REMARK   3    24  2.2821 -  2.2500    0.99    15684   140  0.3474 0.3924        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.339            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.408           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.98                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.76                          
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      :  0.006          52552                                  
REMARK   3   ANGLE     :  0.503          71877                                  
REMARK   3   CHIRALITY :  0.038           7085                                  
REMARK   3   PLANARITY :  0.004           8681                                  
REMARK   3   DIHEDRAL  : 14.902          28166                                  
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: INDEXED AND INTEGRATED IMAGES FROM THE    
REMARK   3  TWO DIFFRACTION EXPERIMENTS WERE MERGED TO GENERATE THE SINGLE      
REMARK   3  DIFFRACTION DATASET DESCRIBED HERE.                                 
REMARK   4                                                                      
REMARK   4 5TIS COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000223850.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-NOV-15; 14-JUL-16               
REMARK 200  TEMPERATURE           (KELVIN) : 293; 293                           
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N; N                               
REMARK 200  RADIATION SOURCE               : FREE ELECTRON LASER; FREE          
REMARK 200                                   ELECTRON LASER                     
REMARK 200  BEAMLINE                       : XPP; MFX                           
REMARK 200  X-RAY GENERATOR MODEL          : SLAC LCLS BEAMLINE XPP; SLAC       
REMARK 200                                   LCLS BEAMLINE MFX                  
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.3051; 1.3051                     
REMARK 200  MONOCHROMATOR                  : NONE; NONE                         
REMARK 200  OPTICS                         : COMPOUND REFRACTIVE LENSES;        
REMARK 200                                   COMPOUND REFRACTIVE LENSES         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX170-HS; RAYONIX MX170    
REMARK 200                                   -HS                                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CCTBX.XFEL                         
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 385545                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.280                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 158.4                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8340                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 6.11                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 44.28                    
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 649.0                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 120.7                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 5KAI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: OBLONG CRYSTALS 10-20 MICROMETERS IN LENGTH                  
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.49                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.46                     
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 6.5, 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       58.93500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      155.35500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      111.57000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      155.35500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       58.93500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      111.57000            
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     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     GLU Y    17                                                      
REMARK 465     VAL Y    18                                                      
REMARK 465     ILE Y    19                                                      
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 b 489    CG   CD   OE1  OE2                                  
REMARK 470     HIS d 336    O                                                   
REMARK 470     THR x   2    OG1  CG2                                            
REMARK 470     LEU r   6    CG   CD1  CD2                                       
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU A   189    MN1   OEX A   601              1.68            
REMARK 500   SG   CYS v    40     CBC  HEM v   201              2.00            
REMARK 500   SG   CYS V    40     CBC  HEM V   201              2.02            
REMARK 500   OH   TYR u    55     O    HOH u   201              2.07            
REMARK 500   O    ILE u    49     O    HOH u   201              2.07            
REMARK 500   O    GLY J    31     O    HOH J   201              2.17            
REMARK 500   O    LEU I    37     O    HOH I   201              2.17            
REMARK 500   O    HOH b   740     O    HOH b   770              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  30      -81.03    -93.74                                   
REMARK 500    ILE A 259      -97.28   -114.12                                   
REMARK 500    ASP B  49       79.36   -155.98                                   
REMARK 500    PHE B 162       67.45   -151.91                                   
REMARK 500    ASP B 313       53.42    -90.96                                   
REMARK 500    PRO B 488       35.24    -72.95                                   
REMARK 500    THR B 504       74.76   -110.23                                   
REMARK 500    ASN C  25     -114.24     55.92                                   
REMARK 500    ASP C 107      111.74   -160.57                                   
REMARK 500    TRP C 223     -135.39     57.19                                   
REMARK 500    THR C 295      -64.36    -98.93                                   
REMARK 500    THR C 355        2.25    -68.70                                   
REMARK 500    ASN C 382      -24.42   -140.08                                   
REMARK 500    SER C 416      -56.73    179.90                                   
REMARK 500    VAL D  30      -80.68   -102.64                                   
REMARK 500    SER D  65       15.60   -159.33                                   
REMARK 500    PRO D 140       40.84    -92.16                                   
REMARK 500    SER D 295       73.10   -102.55                                   
REMARK 500    ALA D 351      -57.10     67.67                                   
REMARK 500    THR E   5      -75.32    -87.85                                   
REMARK 500    ASN H  15       58.54   -118.66                                   
REMARK 500    LYS I  33      -91.34   -116.35                                   
REMARK 500    LYS I  35       79.93   -113.91                                   
REMARK 500    ASP I  36      -40.73   -157.00                                   
REMARK 500    GLN M  32      -82.81    -72.78                                   
REMARK 500    LYS O  59      -74.45     61.18                                   
REMARK 500    ARG O  73     -156.21     64.05                                   
REMARK 500    ASN O 132       75.41     58.61                                   
REMARK 500    LEU O 164      -70.22    -87.16                                   
REMARK 500    THR U  19     -168.45   -104.10                                   
REMARK 500    ASN U  99      104.72   -160.76                                   
REMARK 500    TYR U 103     -103.56   -121.91                                   
REMARK 500    ILE V  45     -167.57   -100.11                                   
REMARK 500    ASN V  49       78.05   -161.21                                   
REMARK 500    ASP V  67       35.98    -89.41                                   
REMARK 500    LEU Y  22       30.06    -99.93                                   
REMARK 500    ILE X   3       86.37     58.75                                   
REMARK 500    ASP X  35       79.23   -107.22                                   
REMARK 500    VAL a  30      -85.56    -89.40                                   
REMARK 500    LEU a 159      -54.23   -129.09                                   
REMARK 500    ILE a 259      -91.70   -116.40                                   
REMARK 500    ARG b 127      -73.13    -73.21                                   
REMARK 500    PHE b 162       67.68   -150.61                                   
REMARK 500    GLU b 485       44.31    -88.67                                   
REMARK 500    THR b 504       42.18    -95.96                                   
REMARK 500    ILE c 134      -57.95   -121.49                                   
REMARK 500    GLU c 221      -57.84   -120.57                                   
REMARK 500    TRP c 223     -134.01     58.20                                   
REMARK 500    THR c 295      -61.05   -104.24                                   
REMARK 500    THR c 355        3.33    -68.02                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      85 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH E 214        DISTANCE =  5.97 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     CLA A  609                                                       
REMARK 610     SQD A  612                                                       
REMARK 610     LHG A  614                                                       
REMARK 610     LMG B  620                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     LMG B  626                                                       
REMARK 610     LMG C  501                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     DGD C  519                                                       
REMARK 610     LMG C  520                                                       
REMARK 610     LMG C  521                                                       
REMARK 610     LMG D  407                                                       
REMARK 610     SQD D  408                                                       
REMARK 610     SQD D  409                                                       
REMARK 610     DGD H  102                                                       
REMARK 610     SQD L  101                                                       
REMARK 610     LMG a  614                                                       
REMARK 610     LHG a  616                                                       
REMARK 610     LHG a  617                                                       
REMARK 610     CLA b  616                                                       
REMARK 610     LMG b  620                                                       
REMARK 610     SQD b  621                                                       
REMARK 610     CLA c  504                                                       
REMARK 610     CLA c  508                                                       
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  407                                                       
REMARK 610     LMG d  408                                                       
REMARK 610     SQD f  101                                                       
REMARK 610     DGD h  102                                                       
REMARK 610     LMG m  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  139.7                                              
REMARK 620 3 OEX A 601   O2   78.0  63.3                                        
REMARK 620 4 OEX A 601   O5   95.9  81.4  69.4                                  
REMARK 620 5 GLU A 189   OE1 152.1  68.2 129.1  89.2                            
REMARK 620 6 ALA A 344   O    81.8  75.7  71.2 140.1 111.2                      
REMARK 620 7 HOH A 772   O    83.5 132.0 135.1  72.4  71.9 145.4                
REMARK 620 8 HOH A 714   O    91.4 114.7 147.2 143.3  69.1  76.6  72.8          
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   98.2                                              
REMARK 620 3 OEX A 601   O4   97.2  88.5                                        
REMARK 620 4 GLU A 333   OE2 167.0  85.6  95.4                                  
REMARK 620 5 HOH A 738   O    92.9 166.3  98.0  81.9                            
REMARK 620 6 HOH A 723   O    79.7  85.2 172.5  88.2  89.0                      
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  94.9                                              
REMARK 620 3 HIS D 214   NE2 102.4  90.4                                        
REMARK 620 4 HIS D 268   NE2  85.3 175.3  94.2                                  
REMARK 620 5 BCT A 605   O2   99.2  89.8 158.2  85.5                            
REMARK 620 6 BCT A 605   O1  159.6  90.9  97.1  87.3  61.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 332   NE2                                                    
REMARK 620 2 OEX A 601   O1  164.6                                              
REMARK 620 3 OEX A 601   O5  101.6  90.0                                        
REMARK 620 4 OEX A 601   O3   84.4  88.5  77.0                                  
REMARK 620 5 ASP A 342   OD2  81.5  83.9 157.1  80.8                            
REMARK 620 N                    1     2     3     4                             
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  157.6                                              
REMARK 620 3 OEX A 601   O3   76.2  89.6                                        
REMARK 620 4 OEX A 601   O4  103.4  89.9 177.0                                  
REMARK 620 5 OEX A 601   O5   94.9 102.1  88.8  94.2                            
REMARK 620 6 GLU C 354   OE2  84.9  77.0  86.8  90.2 175.4                      
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   88.7                                              
REMARK 620 3 OEX A 601   O2  167.7 100.5                                        
REMARK 620 4 OEX A 601   O3   94.6  90.5  93.5                                  
REMARK 620 5 ALA A 344   OXT  88.8  82.1  84.5 171.8                            
REMARK 620 6 GLU C 354   OE1  83.5 172.1  87.0  91.8  96.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   OD1                                                    
REMARK 620 2 CLA C 512   NA   96.2                                              
REMARK 620 3 CLA C 512   NB   95.1  91.7                                        
REMARK 620 4 CLA C 512   NC   88.5 174.3  91.1                                  
REMARK 620 5 CLA C 512   ND   89.6  90.5 174.6  86.3                            
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   93.7                                              
REMARK 620 3 HEM E 101   NB  106.7  89.3                                        
REMARK 620 4 HEM E 101   NC   89.9 176.3  89.3                                  
REMARK 620 5 HEM E 101   ND   68.2  91.4 174.9  90.3                            
REMARK 620 6 HIS F  24   NE2 155.4  72.6  93.8 104.2  91.2                      
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   87.8                                              
REMARK 620 3 HEM V 201   NB   91.1  90.3                                        
REMARK 620 4 HEM V 201   NC   90.8 178.6  89.8                                  
REMARK 620 5 HEM V 201   ND   84.4  89.3 175.4  90.5                            
REMARK 620 6 HIS V  92   NE2 178.7  93.0  87.9  88.5  96.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 601   O1  137.4                                              
REMARK 620 3 OEX a 601   O2   72.5  68.9                                        
REMARK 620 4 OEX a 601   O5  102.1  81.0  69.8                                  
REMARK 620 5 GLU a 189   OE1 150.2  69.8 137.2  93.0                            
REMARK 620 6 ALA a 344   O    81.4  69.7  71.2 137.5 104.5                      
REMARK 620 7 HOH a 738   O    93.0 103.7 138.0 151.9  63.9  67.8                
REMARK 620 8 HOH a 779   O    87.1 133.7 135.1  76.3  71.6 145.9  80.9          
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  100.2                                              
REMARK 620 3 OEX a 601   O4   95.7  94.6                                        
REMARK 620 4 GLU a 333   OE2 175.2  84.5  85.1                                  
REMARK 620 5 HOH a 772   O    90.0  88.1 173.1  88.9                            
REMARK 620 6 HOH a 720   O    94.0 165.6  86.3  81.3  89.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 601   O1   81.6                                              
REMARK 620 3 OEX a 601   O5  100.9  92.3                                        
REMARK 620 4 OEX a 601   O3  173.5  92.2  77.6                                  
REMARK 620 5 HIS a 332   NE2  95.9 169.5  98.2  90.6                            
REMARK 620 6 ASP a 342   OD2  93.2  84.0 164.8  87.8  86.0                      
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  96.9                                              
REMARK 620 3 HIS d 214   NE2 106.3  87.1                                        
REMARK 620 4 HIS d 268   NE2  80.9 176.9  95.5                                  
REMARK 620 5 BCT a 605   O1  151.1  93.9 100.8  87.0                            
REMARK 620 6 BCT a 605   O2   93.3  84.5 159.4  93.5  61.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 601  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 601   O2  170.1                                              
REMARK 620 3 OEX a 601   O3   79.2  97.2                                        
REMARK 620 4 OEX a 601   O4   91.9  92.2 170.5                                  
REMARK 620 5 OEX a 601   O5   95.9  93.0  87.0  90.7                            
REMARK 620 6 GLU c 354   OE2  82.5  87.9  80.7 101.6 167.7                      
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   82.3                                              
REMARK 620 3 OEX a 601   O2  177.6  97.1                                        
REMARK 620 4 OEX a 601   O3   92.6  87.4  89.6                                  
REMARK 620 5 ALA a 344   OXT  89.7  92.1  88.0 177.5                            
REMARK 620 6 GLU c 354   OE1  81.5 163.8  99.2  92.6  88.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 511   NA   95.0                                              
REMARK 620 3 CLA c 511   NB   98.7  91.6                                        
REMARK 620 4 CLA c 511   NC   90.1 174.0  90.9                                  
REMARK 620 5 CLA c 511   ND   86.7  90.7 174.0  86.4                            
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   96.7                                              
REMARK 620 3 HEM e 101   NB  101.5  89.3                                        
REMARK 620 4 HEM e 101   NC   88.4 174.9  90.3                                  
REMARK 620 5 HEM e 101   ND   73.2  89.9 174.5  90.9                            
REMARK 620 6 HIS f  24   NE2 168.5  78.5  88.9  96.4  96.2                      
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   89.9                                              
REMARK 620 3 HEM v 201   NB   90.7  89.4                                        
REMARK 620 4 HEM v 201   NC   85.9 175.7  89.8                                  
REMARK 620 5 HEM v 201   ND   81.9  89.6 172.6  90.7                            
REMARK 620 6 HIS v  92   NE2 170.9  91.2  98.3  93.1  89.0                      
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 743   O                                                      
REMARK 620 2 CLA A 607   NA   84.4                                              
REMARK 620 3 CLA A 607   NB  100.9  91.5                                        
REMARK 620 4 CLA A 607   NC   98.1 175.6  91.6                                  
REMARK 620 5 CLA A 607   ND   82.8  90.7 175.9  86.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 613  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 732   O                                                      
REMARK 620 2 CLA A 613   NA   79.1                                              
REMARK 620 3 CLA A 613   NB  100.6  91.7                                        
REMARK 620 4 CLA A 613   NC  104.6 174.8  91.0                                  
REMARK 620 5 CLA A 613   ND   84.5  90.6 174.6  86.3                            
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 733   O                                                      
REMARK 620 2 CLA B 601   NA   81.8                                              
REMARK 620 3 CLA B 601   NB   98.1  91.7                                        
REMARK 620 4 CLA B 601   NC  101.4 175.3  91.3                                  
REMARK 620 5 CLA B 601   ND   85.9  90.7 175.6  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 772   O                                                      
REMARK 620 2 CLA B 607   NA   85.3                                              
REMARK 620 3 CLA B 607   NB   97.3  91.7                                        
REMARK 620 4 CLA B 607   NC   99.1 174.5  91.0                                  
REMARK 620 5 CLA B 607   ND   87.6  90.4 174.8  86.5                            
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 723   O                                                      
REMARK 620 2 CLA B 610   NA   88.6                                              
REMARK 620 3 CLA B 610   NB   86.4  91.5                                        
REMARK 620 4 CLA B 610   NC   96.0 174.6  91.5                                  
REMARK 620 5 CLA B 610   ND   97.7  90.5 175.5  86.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 505  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 661   O                                                      
REMARK 620 2 CLA C 505   NA   83.7                                              
REMARK 620 3 CLA C 505   NB   98.3  91.6                                        
REMARK 620 4 CLA C 505   NC  100.0 175.1  91.1                                  
REMARK 620 5 CLA C 505   ND   86.3  90.4 175.2  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 508  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH C 611   O                                                      
REMARK 620 2 CLA C 508   NA   84.3                                              
REMARK 620 3 CLA C 508   NB   92.0  91.6                                        
REMARK 620 4 CLA C 508   NC  100.8 174.2  91.0                                  
REMARK 620 5 CLA C 508   ND   93.3  90.7 174.4  86.3                            
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 749   O                                                      
REMARK 620 2 CLA a 607   NA   84.3                                              
REMARK 620 3 CLA a 607   NB  100.8  91.5                                        
REMARK 620 4 CLA a 607   NC   98.9 175.3  91.3                                  
REMARK 620 5 CLA a 607   ND   83.5  90.8 175.3  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 759   O                                                      
REMARK 620 2 CLA a 615   NA   84.3                                              
REMARK 620 3 CLA a 615   NB   93.4  91.5                                        
REMARK 620 4 CLA a 615   NC   99.3 175.3  91.3                                  
REMARK 620 5 CLA a 615   ND   90.8  90.7 175.4  86.3                            
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 758   O                                                      
REMARK 620 2 CLA b 601   NA   82.2                                              
REMARK 620 3 CLA b 601   NB   89.5  91.7                                        
REMARK 620 4 CLA b 601   NC  101.1 175.6  91.3                                  
REMARK 620 5 CLA b 601   ND   94.0  90.7 176.0  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 792   O                                                      
REMARK 620 2 CLA b 607   NA   87.2                                              
REMARK 620 3 CLA b 607   NB   92.4  91.6                                        
REMARK 620 4 CLA b 607   NC   97.8 174.2  91.1                                  
REMARK 620 5 CLA b 607   ND   93.1  90.7 174.2  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 719   O                                                      
REMARK 620 2 CLA b 610   NA   93.6                                              
REMARK 620 3 CLA b 610   NB   86.8  91.7                                        
REMARK 620 4 CLA b 610   NC   90.7 174.9  91.2                                  
REMARK 620 5 CLA b 610   ND   96.7  90.7 175.6  86.1                            
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 646   O                                                      
REMARK 620 2 CLA c 504   NA   83.5                                              
REMARK 620 3 CLA c 504   NB   97.2  91.8                                        
REMARK 620 4 CLA c 504   NC   99.6 175.5  91.0                                  
REMARK 620 5 CLA c 504   ND   86.9  90.5 175.5  86.4                            
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 645   O                                                      
REMARK 620 2 CLA c 507   NA   82.5                                              
REMARK 620 3 CLA c 507   NB   90.7  92.1                                        
REMARK 620 4 CLA c 507   NC  102.1 174.5  90.8                                  
REMARK 620 5 CLA c 507   ND   94.2  90.4 174.7  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 CL 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 BCT 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 SQD A 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD A 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG A 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA B 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR B 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AF9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG B 623                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 624                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD B 625                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG B 626                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AG9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AH9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA C 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR C 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD C 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG C 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AI9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG D 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG D 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD D 409                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AJ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM E 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR H 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD H 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR K 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD L 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG L 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR T 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM V 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR Y 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AK9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue OEX a 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FE2 a 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 603                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL a 604                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCT a 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PHO a 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AL9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR a 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 a 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD a 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG a 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA a 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG a 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AM9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AN9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA b 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR b 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AO9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG b 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD b 621                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 507                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AP9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 508                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 509                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 510                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA c 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AQ9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD c 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG c 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR c 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CLA d 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR d 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AR9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PL9 d 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG d 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG d 408                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue HEM e 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SQD f 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR h 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DGD h 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AS9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LHG l 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue LMG m 102                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BCR t 101                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AT3                                                 
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: AT4                                                 
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: AT5                                                 
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: 5KAF   RELATED DB: PDB                                   
REMARK 900 CORRESPONDING DARK STATE RT STRUCTURE OF PHOTOSYSTEM II              
REMARK 900 RELATED ID: 5KAI   RELATED DB: PDB                                   
REMARK 900 CORRESPONDING 2F STATE, NH3-BOUND RT STRUCTURE OF PHOTOSYSTEM II     
DBREF  5TIS A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  5TIS B    1   510  UNP    Q8DIQ1   PSBB_THEEB       1    510             
DBREF  5TIS C   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  5TIS D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  5TIS E    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  5TIS F    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  5TIS H    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  5TIS I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  5TIS J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5TIS K    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  5TIS L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5TIS M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  5TIS O  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  5TIS T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  5TIS U  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  5TIS V  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  5TIS Y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  5TIS X    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  5TIS Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5TIS R    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
DBREF  5TIS a    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  5TIS b    1   510  UNP    Q8DIQ1   PSBB_THEEB       1    510             
DBREF  5TIS c   13   473  UNP    Q8DIF8   PSBC_THEEB       1    461             
DBREF  5TIS d    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  5TIS e    1    84  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  5TIS f    1    45  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  5TIS h    1    66  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  5TIS i    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  5TIS j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5TIS k    1    46  UNP    Q9F1K9   PSBK_THEEB       1     46             
DBREF  5TIS l    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  5TIS m    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  5TIS o  -25   246  UNP    P0A431   PSBO_THEEB       1    272             
DBREF  5TIS t    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  5TIS u  -29   104  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  5TIS v  -25   137  UNP    P0A386   CY550_THEEB      1    163             
DBREF  5TIS y    1    46  UNP    Q8DJI1   YCF12_THEEB      1     46             
DBREF  5TIS x    1    41  UNP    Q9F1R6   PSBX_THEEB       1     41             
DBREF  5TIS z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5TIS r    1    41  UNP    Q8DKM3   PSBY_THEEB       1     41             
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 5TIS FME I    1  MET  MODIFIED RESIDUE                                   
MODRES 5TIS FME M    1  MET  MODIFIED RESIDUE                                   
MODRES 5TIS FME T    1  MET  MODIFIED RESIDUE                                   
MODRES 5TIS FME i    1  MET  MODIFIED RESIDUE                                   
MODRES 5TIS FME m    1  MET  MODIFIED RESIDUE                                   
MODRES 5TIS 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     CL  A 603       1                                                       
HET     CL  A 604       1                                                       
HET    BCT  A 605       4                                                       
HET    CLA  A 606      65                                                       
HET    CLA  A 607      65                                                       
HET    PHO  A 608      64                                                       
HET    CLA  A 609      54                                                       
HET    BCR  A 610      40                                                       
HET    PL9  A 611      55                                                       
HET    SQD  A 612      52                                                       
HET    CLA  A 613      65                                                       
HET    LHG  A 614      47                                                       
HET    UNL  A 615       9                                                       
HET    SQD  A 616      54                                                       
HET    UNL  A 617      20                                                       
HET    LHG  A 618      49                                                       
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      11                                                       
HET    LHG  B 623      49                                                       
HET    SQD  B 624      54                                                       
HET    SQD  B 625      54                                                       
HET    LMG  B 626      51                                                       
HET    UNL  B 627      15                                                       
HET    LMG  C 501      48                                                       
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    CLA  C 514      65                                                       
HET    BCR  C 515      40                                                       
HET    BCR  C 516      40                                                       
HET    DGD  C 517      62                                                       
HET    DGD  C 518      62                                                       
HET    DGD  C 519      62                                                       
HET    LMG  C 520      48                                                       
HET    LMG  C 521      51                                                       
HET    UNL  C 522      17                                                       
HET    UNL  C 523      16                                                       
HET    PHO  D 401      64                                                       
HET    CLA  D 402      65                                                       
HET    CLA  D 403      65                                                       
HET    BCR  D 404      40                                                       
HET    PL9  D 405      55                                                       
HET    LHG  D 406      49                                                       
HET    LMG  D 407      51                                                       
HET    SQD  D 408      43                                                       
HET    SQD  D 409      47                                                       
HET    UNL  D 410      18                                                       
HET    UNL  D 411      10                                                       
HET    HEM  E 101      43                                                       
HET    UNL  E 102      12                                                       
HET    BCR  H 101      40                                                       
HET    DGD  H 102      62                                                       
HET    UNL  H 103       7                                                       
HET    UNL  I 101       7                                                       
HET    UNL  I 102      20                                                       
HET    UNL  J 101      11                                                       
HET    UNL  J 102      12                                                       
HET    BCR  K 101      40                                                       
HET    SQD  L 101      49                                                       
HET    LHG  L 102      49                                                       
HET    UNL  M 101      15                                                       
HET    UNL  M 102      17                                                       
HET    BCR  T 101      40                                                       
HET    UNL  T 102      14                                                       
HET    UNL  T 103      12                                                       
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      65                                                       
HET    PHO  a 608      64                                                       
HET    PHO  a 609      64                                                       
HET    CLA  a 610      65                                                       
HET    BCR  a 611      40                                                       
HET    PL9  a 612      55                                                       
HET    SQD  a 613      54                                                       
HET    LMG  a 614      51                                                       
HET    CLA  a 615      65                                                       
HET    LHG  a 616      39                                                       
HET    LHG  a 617      42                                                       
HET    UNL  a 618      17                                                       
HET    UNL  a 619      12                                                       
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     129                                                       
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      47                                                       
HET    BCR  b 617      40                                                       
HET    BCR  b 618      40                                                       
HET    BCR  b 619      40                                                       
HET    LMG  b 620      51                                                       
HET    SQD  b 621      40                                                       
HET    UNL  b 622      17                                                       
HET    UNL  b 623      11                                                       
HET    CLA  c 501      65                                                       
HET    CLA  c 502      65                                                       
HET    CLA  c 503      65                                                       
HET    CLA  c 504      60                                                       
HET    CLA  c 505      65                                                       
HET    CLA  c 506      65                                                       
HET    CLA  c 507      65                                                       
HET    CLA  c 508      64                                                       
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      37                                                       
HET    LMG  c 520      34                                                       
HET    BCR  c 521      40                                                       
HET    BCR  c 522      40                                                       
HET    UNL  c 523       8                                                       
HET    UNL  c 524      20                                                       
HET    UNL  c 525      12                                                       
HET    CLA  d 401      65                                                       
HET    CLA  d 402      65                                                       
HET    BCR  d 403      40                                                       
HET    PL9  d 404      55                                                       
HET    LHG  d 405      49                                                       
HET    LHG  d 406      49                                                       
HET    LMG  d 407      51                                                       
HET    LMG  d 408      38                                                       
HET    UNL  d 409      17                                                       
HET    HEM  e 101      43                                                       
HET    SQD  f 101      41                                                       
HET    BCR  h 101      40                                                       
HET    DGD  h 102      62                                                       
HET    UNL  i 101      20                                                       
HET    UNL  j 801      15                                                       
HET    UNL  j 802      12                                                       
HET    LHG  l 101      49                                                       
HET    UNL  m 101       9                                                       
HET    LMG  m 102      51                                                       
HET    UNL  m 103      16                                                       
HET    BCR  t 101      40                                                       
HET    UNL  t 102      18                                                       
HET    HEM  v 201      43                                                       
HET    UNL  x 101      16                                                       
HETNAM     FME N-FORMYLMETHIONINE                                               
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM     FE2 FE (II) ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     BCT BICARBONATE 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     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
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   CL    4(CL 1-)                                                     
FORMUL  45  BCT    2(C H O3 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  SQD    10(C41 H78 O12 S)                                            
FORMUL  54  LHG    10(C38 H75 O10 P)                                            
FORMUL  78  LMG    14(C45 H86 O10)                                              
FORMUL  02  DGD    8(C51 H96 O15)                                               
FORMUL  20  HEM    4(C34 H32 FE N4 O4)                                          
FORMUL  30  HOH   *1179(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  SER A  222  1                                  28    
HELIX   13 AB4 SER A  232  TYR A  237  5                                   6    
HELIX   14 AB5 ASN A  247  ILE A  259  1                                  13    
HELIX   15 AB6 PHE A  260  SER A  264  5                                   5    
HELIX   16 AB7 ASN A  267  ALA A  294  1                                  28    
HELIX   17 AB8 THR A  316  HIS A  332  1                                  17    
HELIX   18 AB9 PRO B    4  ILE B   13  5                                  10    
HELIX   19 AC1 ASP B   15  PHE B   45  1                                  31    
HELIX   20 AC2 PRO B   54  GLN B   58  5                                   5    
HELIX   21 AC3 VAL B   62  LEU B   69  1                                   8    
HELIX   22 AC4 SER B   92  TYR B  117  1                                  26    
HELIX   23 AC5 LEU B  120  ARG B  124  5                                   5    
HELIX   24 AC6 ASP B  134  PHE B  156  1                                  23    
HELIX   25 AC7 GLY B  186  ASN B  191  5                                   6    
HELIX   26 AC8 ASN B  194  VAL B  219  1                                  26    
HELIX   27 AC9 PRO B  222  LEU B  229  1                                   8    
HELIX   28 AD1 ASN B  233  GLY B  259  1                                  27    
HELIX   29 AD2 PRO B  264  GLY B  269  1                                   6    
HELIX   30 AD3 ARG B  272  SER B  277  1                                   6    
HELIX   31 AD4 SER B  278  SER B  294  1                                  17    
HELIX   32 AD5 THR B  297  ALA B  304  1                                   8    
HELIX   33 AD6 PRO B  306  ASP B  313  1                                   8    
HELIX   34 AD7 TYR B  314  ASN B  318  5                                   5    
HELIX   35 AD8 PRO B  329  GLY B  333  5                                   5    
HELIX   36 AD9 SER B  391  GLY B  396  1                                   6    
HELIX   37 AE1 ASP B  413  ILE B  425  1                                  13    
HELIX   38 AE2 SER B  446  PHE B  475  1                                  30    
HELIX   39 AE3 ARG B  476  PHE B  479  5                                   4    
HELIX   40 AE4 ASP C   27  GLY C   32  1                                   6    
HELIX   41 AE5 ALA C   34  ILE C   43  5                                  10    
HELIX   42 AE6 LEU C   45  HIS C   74  1                                  30    
HELIX   43 AE7 PRO C   80  GLN C   84  5                                   5    
HELIX   44 AE8 LEU C   88  LEU C   95  1                                   8    
HELIX   45 AE9 GLY C  100  GLU C  104  5                                   5    
HELIX   46 AF1 THR C  108  ARG C  135  1                                  28    
HELIX   47 AF2 ASP C  153  PHE C  182  1                                  30    
HELIX   48 AF3 ASP C  205  LYS C  215  1                                  11    
HELIX   49 AF4 GLY C  222  VAL C  227  5                                   6    
HELIX   50 AF5 ASN C  229  THR C  254  1                                  26    
HELIX   51 AF6 PHE C  257  PHE C  264  1                                   8    
HELIX   52 AF7 SER C  267  ASN C  293  1                                  27    
HELIX   53 AF8 PRO C  298  GLY C  303  1                                   6    
HELIX   54 AF9 THR C  305  LEU C  324  1                                  20    
HELIX   55 AG1 GLY C  353  TRP C  359  5                                   7    
HELIX   56 AG2 LEU C  366  PRO C  368  5                                   3    
HELIX   57 AG3 ASP C  376  ASP C  383  1                                   8    
HELIX   58 AG4 GLN C  385  THR C  397  1                                  13    
HELIX   59 AG5 SER C  421  GLY C  454  1                                  34    
HELIX   60 AG6 ASP C  460  MET C  469  5                                  10    
HELIX   61 AG7 GLY D   13  LYS D   23  1                                  11    
HELIX   62 AG8 SER D   33  VAL D   55  1                                  23    
HELIX   63 AG9 SER D   66  GLY D   70  5                                   5    
HELIX   64 AH1 ALA D   82  GLY D   86  5                                   5    
HELIX   65 AH2 ASP D  100  LEU D  107  1                                   8    
HELIX   66 AH3 GLY D  108  GLY D  137  1                                  30    
HELIX   67 AH4 PRO D  140  PHE D  146  1                                   7    
HELIX   68 AH5 PHE D  146  LEU D  158  1                                  13    
HELIX   69 AH6 LEU D  158  GLN D  164  1                                   7    
HELIX   70 AH7 SER D  166  ALA D  170  5                                   5    
HELIX   71 AH8 VAL D  175  ASN D  190  1                                  16    
HELIX   72 AH9 TRP D  191  LEU D  193  5                                   3    
HELIX   73 AI1 ASN D  194  ASN D  220  1                                  27    
HELIX   74 AI2 SER D  245  PHE D  257  1                                  13    
HELIX   75 AI3 ASN D  263  LEU D  291  1                                  29    
HELIX   76 AI4 PHE D  298  ASP D  308  1                                  11    
HELIX   77 AI5 THR D  313  GLN D  334  1                                  22    
HELIX   78 AI6 PRO D  335  ASN D  338  5                                   4    
HELIX   79 AI7 PRO D  342  LEU D  346  5                                   5    
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  LYS E   84  1                                  14    
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 SER H   61  LEU H   65  5                                   5    
HELIX   89 AJ8 GLU I    2  SER I   25  1                                  24    
HELIX   90 AJ9 GLY I   26  ARG I   30  5                                   5    
HELIX   91 AK1 PRO J    9  ALA J   32  1                                  24    
HELIX   92 AK2 PRO K   12  ILE K   17  5                                   6    
HELIX   93 AK3 PHE K   18  ASP K   23  1                                   6    
HELIX   94 AK4 VAL K   24  PRO K   26  5                                   3    
HELIX   95 AK5 VAL K   27  GLY K   44  1                                  18    
HELIX   96 AK6 ASN L   13  ASN L   37  1                                  25    
HELIX   97 AK7 LEU M    6  SER M   31  1                                  26    
HELIX   98 AK8 THR O    6  VAL O   11  1                                   6    
HELIX   99 AK9 GLY O   14  LYS O   18  5                                   5    
HELIX  100 AL1 LEU O  182  VAL O  187  1                                   6    
HELIX  101 AL2 GLU T    2  PHE T   23  1                                  22    
HELIX  102 AL3 ASN U   11  LEU U   17  1                                   7    
HELIX  103 AL4 GLY U   18  GLU U   23  5                                   6    
HELIX  104 AL5 ASN U   31  TYR U   38  5                                   8    
HELIX  105 AL6 PRO U   43  ASN U   52  1                                  10    
HELIX  106 AL7 SER U   57  ILE U   64  5                                   8    
HELIX  107 AL8 THR U   68  GLU U   77  1                                  10    
HELIX  108 AL9 ASN U   78  GLU U   80  5                                   3    
HELIX  109 AM1 GLU U   88  GLU U   93  1                                   6    
HELIX  110 AM2 GLY U   94  ASP U   96  5                                   3    
HELIX  111 AM3 THR V   22  CYS V   37  1                                  16    
HELIX  112 AM4 CYS V   37  VAL V   42  1                                   6    
HELIX  113 AM5 GLY V   43  ILE V   45  5                                   3    
HELIX  114 AM6 ARG V   55  ALA V   62  1                                   8    
HELIX  115 AM7 ASN V   68  ASN V   78  1                                  11    
HELIX  116 AM8 PHE V  101  LEU V  107  5                                   7    
HELIX  117 AM9 THR V  108  GLY V  127  1                                  20    
HELIX  118 AN1 ASP V  128  TRP V  130  5                                   3    
HELIX  119 AN2 GLY V  133  TYR V  137  5                                   5    
HELIX  120 AN3 GLN Y   21  ARG Y   43  1                                  23    
HELIX  121 AN4 THR X    4  ASP X   35  1                                  32    
HELIX  122 AN5 THR Z    2  ALA Z   28  1                                  27    
HELIX  123 AN6 TRP Z   33  PHE Z   59  1                                  27    
HELIX  124 AN7 TRP R    3  LYS R   33  1                                  31    
HELIX  125 AN8 ASN a   12  THR a   22  1                                  11    
HELIX  126 AN9 VAL a   30  ALA a   55  1                                  26    
HELIX  127 AO1 SER a   70  GLY a   74  5                                   5    
HELIX  128 AO2 PRO a   95  ALA a   99  5                                   5    
HELIX  129 AO3 SER a  101  ASN a  108  1                                   8    
HELIX  130 AO4 GLY a  109  LEU a  137  1                                  29    
HELIX  131 AO5 TRP a  142  LEU a  159  1                                  18    
HELIX  132 AO6 LEU a  159  GLY a  166  1                                   8    
HELIX  133 AO7 SER a  167  GLY a  171  5                                   5    
HELIX  134 AO8 ILE a  176  ASN a  191  1                                  16    
HELIX  135 AO9 ILE a  192  MET a  194  5                                   3    
HELIX  136 AP1 HIS a  195  SER a  222  1                                  28    
HELIX  137 AP2 SER a  232  TYR a  237  5                                   6    
HELIX  138 AP3 ASN a  247  ILE a  259  1                                  13    
HELIX  139 AP4 PHE a  260  SER a  264  5                                   5    
HELIX  140 AP5 ASN a  267  ALA a  294  1                                  28    
HELIX  141 AP6 THR a  316  HIS a  332  1                                  17    
HELIX  142 AP7 PRO b    4  ILE b   13  5                                  10    
HELIX  143 AP8 ASP b   15  ALA b   43  1                                  29    
HELIX  144 AP9 PRO b   54  GLN b   58  5                                   5    
HELIX  145 AQ1 VAL b   62  LEU b   69  1                                   8    
HELIX  146 AQ2 SER b   92  TYR b  117  1                                  26    
HELIX  147 AQ3 LEU b  120  ARG b  124  5                                   5    
HELIX  148 AQ4 ASP b  134  PHE b  156  1                                  23    
HELIX  149 AQ5 GLY b  186  ASN b  191  5                                   6    
HELIX  150 AQ6 ASN b  194  VAL b  219  1                                  26    
HELIX  151 AQ7 PRO b  222  LEU b  229  1                                   8    
HELIX  152 AQ8 ILE b  234  GLY b  259  1                                  26    
HELIX  153 AQ9 PRO b  264  GLY b  269  1                                   6    
HELIX  154 AR1 THR b  271  SER b  277  1                                   7    
HELIX  155 AR2 SER b  278  SER b  294  1                                  17    
HELIX  156 AR3 THR b  297  ALA b  304  1                                   8    
HELIX  157 AR4 PRO b  306  ASP b  313  1                                   8    
HELIX  158 AR5 TYR b  314  ASN b  318  5                                   5    
HELIX  159 AR6 PRO b  329  GLY b  333  5                                   5    
HELIX  160 AR7 SER b  391  GLY b  396  1                                   6    
HELIX  161 AR8 ASP b  413  ILE b  425  1                                  13    
HELIX  162 AR9 SER b  446  PHE b  475  1                                  30    
HELIX  163 AS1 ARG b  476  PHE b  479  5                                   4    
HELIX  164 AS2 SER b  487  GLU b  492  1                                   6    
HELIX  165 AS3 ASP c   27  GLY c   32  1                                   6    
HELIX  166 AS4 ALA c   34  ILE c   43  5                                  10    
HELIX  167 AS5 LEU c   45  HIS c   74  1                                  30    
HELIX  168 AS6 PRO c   80  GLN c   84  5                                   5    
HELIX  169 AS7 LEU c   88  LEU c   95  1                                   8    
HELIX  170 AS8 GLY c  100  GLU c  104  5                                   5    
HELIX  171 AS9 THR c  108  ARG c  135  1                                  28    
HELIX  172 AT1 ASP c  153  PHE c  182  1                                  30    
HELIX  173 AT2 ASP c  205  PHE c  210  1                                   6    
HELIX  174 AT3 PHE c  210  LYS c  215  1                                   6    
HELIX  175 AT4 GLY c  222  VAL c  227  5                                   6    
HELIX  176 AT5 ASN c  229  THR c  254  1                                  26    
HELIX  177 AT6 PHE c  257  ARG c  262  1                                   6    
HELIX  178 AT7 SER c  267  ASN c  293  1                                  27    
HELIX  179 AT8 PRO c  298  GLY c  303  1                                   6    
HELIX  180 AT9 THR c  305  LEU c  324  1                                  20    
HELIX  181 AU1 GLY c  353  TRP c  359  5                                   7    
HELIX  182 AU2 LEU c  366  PRO c  368  5                                   3    
HELIX  183 AU3 ASP c  376  ASP c  383  1                                   8    
HELIX  184 AU4 GLN c  385  THR c  397  1                                  13    
HELIX  185 AU5 SER c  421  GLY c  454  1                                  34    
HELIX  186 AU6 ASP c  460  GLU c  464  5                                   5    
HELIX  187 AU7 PRO c  465  MET c  469  5                                   5    
HELIX  188 AU8 GLY d   13  LYS d   23  1                                  11    
HELIX  189 AU9 SER d   33  VAL d   55  1                                  23    
HELIX  190 AV1 SER d   66  GLY d   70  5                                   5    
HELIX  191 AV2 ALA d   82  GLY d   86  5                                   5    
HELIX  192 AV3 ASP d  100  LEU d  107  1                                   8    
HELIX  193 AV4 GLY d  108  GLY d  137  1                                  30    
HELIX  194 AV5 PRO d  140  PHE d  146  1                                   7    
HELIX  195 AV6 PHE d  146  LEU d  158  1                                  13    
HELIX  196 AV7 LEU d  158  GLN d  164  1                                   7    
HELIX  197 AV8 SER d  166  ALA d  170  5                                   5    
HELIX  198 AV9 VAL d  175  ASN d  190  1                                  16    
HELIX  199 AW1 TRP d  191  LEU d  193  5                                   3    
HELIX  200 AW2 ASN d  194  ASN d  220  1                                  27    
HELIX  201 AW3 SER d  230  ALA d  234  5                                   5    
HELIX  202 AW4 SER d  245  GLY d  258  1                                  14    
HELIX  203 AW5 ASN d  263  LEU d  291  1                                  29    
HELIX  204 AW6 PHE d  298  ASP d  308  1                                  11    
HELIX  205 AW7 THR d  313  GLN d  334  1                                  22    
HELIX  206 AW8 PRO d  342  LEU d  346  5                                   5    
HELIX  207 AW9 PRO e    9  ILE e   14  1                                   6    
HELIX  208 AX1 SER e   16  THR e   40  1                                  25    
HELIX  209 AX2 GLY e   41  GLY e   48  1                                   8    
HELIX  210 AX3 GLU e   71  GLN e   82  1                                  12    
HELIX  211 AX4 THR f   17  GLN f   41  1                                  25    
HELIX  212 AX5 THR h    5  ARG h   12  1                                   8    
HELIX  213 AX6 PRO h   13  SER h   16  5                                   4    
HELIX  214 AX7 THR h   27  ASN h   50  1                                  24    
HELIX  215 AX8 GLU i    2  LEU i   24  1                                  23    
HELIX  216 AX9 GLY i   26  ARG i   30  5                                   5    
HELIX  217 AY1 PRO j    9  ALA j   32  1                                  24    
HELIX  218 AY2 PRO k   12  ILE k   17  5                                   6    
HELIX  219 AY3 PHE k   18  ASP k   23  1                                   6    
HELIX  220 AY4 VAL k   27  GLY k   44  1                                  18    
HELIX  221 AY5 ASN l   13  ASN l   37  1                                  25    
HELIX  222 AY6 LEU m    6  GLN m   32  1                                  27    
HELIX  223 AY7 THR o    6  VAL o   11  1                                   6    
HELIX  224 AY8 GLY o   14  LYS o   18  5                                   5    
HELIX  225 AY9 GLU o  179  GLU o  181  5                                   3    
HELIX  226 AZ1 LEU o  182  VAL o  187  1                                   6    
HELIX  227 AZ2 GLU t    2  PHE t   23  1                                  22    
HELIX  228 AZ3 ASN u   11  GLY u   18  1                                   8    
HELIX  229 AZ4 THR u   19  GLU u   23  5                                   5    
HELIX  230 AZ5 ASN u   31  TYR u   38  5                                   8    
HELIX  231 AZ6 PRO u   43  ASN u   52  1                                  10    
HELIX  232 AZ7 SER u   57  ILE u   64  5                                   8    
HELIX  233 AZ8 THR u   68  GLU u   77  1                                  10    
HELIX  234 AZ9 ASN u   78  GLU u   80  5                                   3    
HELIX  235 BA1 GLU u   88  GLU u   93  1                                   6    
HELIX  236 BA2 GLY u   94  ASP u   96  5                                   3    
HELIX  237 BA3 THR v   22  CYS v   37  1                                  16    
HELIX  238 BA4 CYS v   37  VAL v   42  1                                   6    
HELIX  239 BA5 GLY v   43  ILE v   45  5                                   3    
HELIX  240 BA6 ARG v   55  LEU v   61  1                                   7    
HELIX  241 BA7 ASN v   68  ASN v   78  1                                  11    
HELIX  242 BA8 PHE v  101  ARG v  105  5                                   5    
HELIX  243 BA9 THR v  108  GLY v  127  1                                  20    
HELIX  244 BB1 ASP v  128  TRP v  130  5                                   3    
HELIX  245 BB2 GLY v  133  TYR v  137  5                                   5    
HELIX  246 BB3 VAL y   18  ARG y   42  1                                  25    
HELIX  247 BB4 THR x    4  ASP x   35  1                                  32    
HELIX  248 BB5 ILE z    3  ALA z   28  1                                  26    
HELIX  249 BB6 ASP z   32  PHE z   59  1                                  28    
HELIX  250 BB7 TRP r    3  LYS r   33  1                                  31    
SHEET    1 AA1 2 ALA A  81  VAL A  82  0                                        
SHEET    2 AA1 2 LEU A 174  GLY A 175 -1  O  LEU A 174   N  VAL A  82           
SHEET    1 AA2 2 LEU A 297  ASN A 298  0                                        
SHEET    2 AA2 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1 AA3 2 MET B 166  VAL B 168  0                                        
SHEET    2 AA3 2 SER B 177  GLN B 179 -1  O  SER B 177   N  VAL B 168           
SHEET    1 AA4 2 ILE B 336  TRP B 340  0                                        
SHEET    2 AA4 2 PHE B 430  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1 AA5 6 VAL B 377  ASP B 380  0                                        
SHEET    2 AA5 6 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA5 6 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA5 6 HIS B 343  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA5 6 THR B 398  TYR B 402 -1  O  SER B 400   N  VAL B 345           
SHEET    6 AA5 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA6 2 LEU C 185  ASP C 187  0                                        
SHEET    2 AA6 2 ASP C 195  ARG C 197 -1  O  ARG C 197   N  LEU C 185           
SHEET    1 AA7 2 LEU C 341  ARG C 343  0                                        
SHEET    2 AA7 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1 AA8 2 ARG C 370  GLY C 371  0                                        
SHEET    2 AA8 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1 AA9 2 ALA D  77  VAL D  78  0                                        
SHEET    2 AA9 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1 AB1 2 TYR O  30  PRO O  31  0                                        
SHEET    2 AB1 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1 AB210 PHE O  65  PRO O  67  0                                        
SHEET    2 AB210 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3 AB210 GLU O 232  PRO O 245 -1  O  LYS O 234   N  LEU O  51           
SHEET    4 AB210 GLU O 210  LEU O 220 -1  N  GLN O 219   O  VAL O 233           
SHEET    5 AB210 LEU O 192  VAL O 204 -1  N  ASN O 200   O  THR O 214           
SHEET    6 AB210 ASP O 141  PRO O 149 -1  N  VAL O 148   O  THR O 193           
SHEET    7 AB210 LYS O 123  SER O 128 -1  N  LYS O 123   O  ASN O 147           
SHEET    8 AB210 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9 AB210 LEU O  78  VAL O  87 -1  N  LYS O  86   O  THR O  94           
SHEET   10 AB210 TYR O  38  LYS O  53 -1  N  LEU O  45   O  LEU O  78           
SHEET    1 AB3 3 LYS O  69  LEU O  70  0                                        
SHEET    2 AB3 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3 AB3 3 ARG O 115  THR O 121 -1  O  ILE O 116   N  VAL O 108           
SHEET    1 AB4 2 ILE U  25  ASP U  26  0                                        
SHEET    2 AB4 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1 AB5 2 THR V   9  PRO V  11  0                                        
SHEET    2 AB5 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1 AB6 2 ALA a  81  VAL a  82  0                                        
SHEET    2 AB6 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1 AB7 2 LEU a 297  ASN a 298  0                                        
SHEET    2 AB7 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1 AB8 2 MET b 166  VAL b 168  0                                        
SHEET    2 AB8 2 SER b 177  GLN b 179 -1  O  SER b 177   N  VAL b 168           
SHEET    1 AB9 2 ILE b 336  TRP b 340  0                                        
SHEET    2 AB9 2 PHE b 430  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1 AC1 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AC1 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC1 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC1 6 HIS b 343  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC1 6 THR b 398  TYR b 402 -1  O  SER b 400   N  VAL b 345           
SHEET    6 AC1 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1 AC2 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC2 2 ASP c 195  ARG c 197 -1  O  ARG c 197   N  LEU c 185           
SHEET    1 AC3 2 LEU c 341  ARG c 343  0                                        
SHEET    2 AC3 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1 AC4 2 ARG c 370  GLY c 371  0                                        
SHEET    2 AC4 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1 AC5 2 ALA d  77  VAL d  78  0                                        
SHEET    2 AC5 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1 AC6 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC6 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC710 VAL o  66  PRO o  67  0                                        
SHEET    2 AC710 TYR o  38  VAL o  52 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC710 GLU o 232  PRO o 245 -1  O  LYS o 234   N  LEU o  51           
SHEET    4 AC710 GLU o 210  LEU o 220 -1  N  SER o 217   O  ILE o 235           
SHEET    5 AC710 LEU o 192  ASP o 205 -1  N  ASN o 200   O  THR o 214           
SHEET    6 AC710 ASP o 141  PRO o 149 -1  N  VAL o 148   O  THR o 193           
SHEET    7 AC710 LYS o 123  SER o 128 -1  N  LYS o 123   O  ASN o 147           
SHEET    8 AC710 LEU o  93  ILE o 101 -1  N  GLU o  97   O  LEU o 125           
SHEET    9 AC710 LEU o  78  VAL o  87 -1  N  GLN o  82   O  ASP o  99           
SHEET   10 AC710 TYR o  38  VAL o  52 -1  N  ILE o  40   O  GLY o  83           
SHEET    1 AC8 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AC8 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AC8 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AC9 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AC9 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SHEET    1 AD1 2 THR v   9  PRO v  11  0                                        
SHEET    2 AD1 2 THR v  18  THR v  20 -1  O  ILE v  19   N  VAL v  10           
SSBOND   1 CYS O   19    CYS O   44                          1555   1555  2.03  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  2.03  
LINK         OD1 ASP A 170                CA1  OEX A 601     1555   1555  2.69  
LINK         OD2 ASP A 170                MN4  OEX A 601     1555   1555  1.95  
LINK         OE1 GLU A 189                CA1  OEX A 601     1555   1555  3.19  
LINK         NE2 HIS A 215                FE   FE2 A 602     1555   1555  2.16  
LINK         NE2 HIS A 272                FE   FE2 A 602     1555   1555  2.20  
LINK         NE2 HIS A 332                MN1  OEX A 601     1555   1555  2.21  
LINK         OE1 GLU A 333                MN3  OEX A 601     1555   1555  2.16  
LINK         OE2 GLU A 333                MN4  OEX A 601     1555   1555  2.03  
LINK         OD1 ASP A 342                MN2  OEX A 601     1555   1555  2.12  
LINK         OD2 ASP A 342                MN1  OEX A 601     1555   1555  2.15  
LINK         O   ALA A 344                CA1  OEX A 601     1555   1555  2.40  
LINK         OXT ALA A 344                MN2  OEX A 601     1555   1555  1.85  
LINK         OD1 ASN C  39                MG   CLA C 512     1555   1555  2.18  
LINK         OE1 GLU C 354                MN2  OEX A 601     1555   1555  2.12  
LINK         OE2 GLU C 354                MN3  OEX A 601     1555   1555  2.00  
LINK         NE2 HIS D 214                FE   FE2 A 602     1555   1555  2.17  
LINK         NE2 HIS D 268                FE   FE2 A 602     1555   1555  2.21  
LINK         NE2 HIS E  23                FE   HEM E 101     1555   1555  2.15  
LINK         NE2 HIS F  24                FE   HEM E 101     1555   1555  2.16  
LINK         C   FME I   1                 N   GLU I   2     1555   1555  1.33  
LINK         C   FME M   1                 N  AGLU M   2     1555   1555  1.33  
LINK         C   FME M   1                 N  BGLU 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  1.70  
LINK         SG  CYS V  37                 CBB HEM V 201     1555   1555  1.72  
LINK         SG  CYS V  40                 CAC HEM V 201     1555   1555  1.87  
LINK         NE2 HIS V  41                FE   HEM V 201     1555   1555  2.15  
LINK         NE2 HIS V  92                FE   HEM V 201     1555   1555  2.15  
LINK         OD1 ASP a 170                CA1  OEX a 601     1555   1555  2.82  
LINK         OD2 ASP a 170                MN4  OEX a 601     1555   1555  2.00  
LINK         OE1 GLU a 189                CA1  OEX a 601     1555   1555  3.06  
LINK         OE2 GLU a 189                MN1  OEX a 601     1555   1555  1.77  
LINK         NE2 HIS a 215                FE   FE2 a 602     1555   1555  2.15  
LINK         NE2 HIS a 272                FE   FE2 a 602     1555   1555  2.20  
LINK         NE2 HIS a 332                MN1  OEX a 601     1555   1555  2.17  
LINK         OE1 GLU a 333                MN3  OEX a 601     1555   1555  2.09  
LINK         OE2 GLU a 333                MN4  OEX a 601     1555   1555  1.98  
LINK         OD1 ASP a 342                MN2  OEX a 601     1555   1555  2.18  
LINK         OD2 ASP a 342                MN1  OEX a 601     1555   1555  2.12  
LINK         O   ALA a 344                CA1  OEX a 601     1555   1555  2.52  
LINK         OXT ALA a 344                MN2  OEX a 601     1555   1555  1.79  
LINK         OD1 ASN c  39                MG   CLA c 511     1555   1555  2.20  
LINK         OE1 GLU c 354                MN2  OEX a 601     1555   1555  2.15  
LINK         OE2 GLU c 354                MN3  OEX a 601     1555   1555  2.09  
LINK         NE2 HIS d 214                FE   FE2 a 602     1555   1555  2.18  
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  2.16  
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  1.70  
LINK         SG  CYS v  37                 CBB HEM v 201     1555   1555  1.66  
LINK         SG  CYS v  40                 CAC HEM v 201     1555   1555  1.86  
LINK         NE2 HIS v  41                FE   HEM v 201     1555   1555  2.13  
LINK         NE2 HIS v  92                FE   HEM v 201     1555   1555  2.15  
LINK        CA1  OEX A 601                 O   HOH A 772     1555   1555  2.58  
LINK        CA1  OEX A 601                 O   HOH A 714     1555   1555  2.46  
LINK        MN4  OEX A 601                 O   HOH A 738     1555   1555  2.12  
LINK        MN4  OEX A 601                 O   HOH A 723     1555   1555  2.17  
LINK        FE   FE2 A 602                 O2  BCT A 605     1555   1555  2.18  
LINK        FE   FE2 A 602                 O1  BCT A 605     1555   1555  2.17  
LINK        MG   CLA A 607                 O   HOH A 743     1555   1555  2.14  
LINK        MG   CLA A 613                 O   HOH A 732     1555   1555  2.16  
LINK        MG   CLA B 601                 O   HOH B 733     1555   1555  2.15  
LINK        MG   CLA B 607                 O   HOH B 772     1555   1555  2.16  
LINK        MG   CLA B 610                 O   HOH B 723     1555   1555  2.15  
LINK        MG   CLA C 505                 O   HOH C 661     1555   1555  2.15  
LINK        MG   CLA C 508                 O   HOH C 611     1555   1555  2.15  
LINK        CA1  OEX a 601                 O   HOH a 738     1555   1555  2.45  
LINK        CA1  OEX a 601                 O   HOH a 779     1555   1555  2.62  
LINK        MN4  OEX a 601                 O   HOH a 772     1555   1555  2.24  
LINK        MN4  OEX a 601                 O   HOH a 720     1555   1555  2.27  
LINK        FE   FE2 a 602                 O1  BCT a 605     1555   1555  2.17  
LINK        FE   FE2 a 602                 O2  BCT a 605     1555   1555  2.18  
LINK        MG   CLA a 607                 O   HOH a 749     1555   1555  2.15  
LINK        MG   CLA a 615                 O   HOH a 759     1555   1555  2.16  
LINK        MG   CLA b 601                 O   HOH b 758     1555   1555  2.15  
LINK        MG   CLA b 607                 O   HOH b 792     1555   1555  2.17  
LINK        MG   CLA b 610                 O   HOH b 719     1555   1555  2.15  
LINK        MG   CLA c 504                 O   HOH c 646     1555   1555  2.15  
LINK        MG   CLA c 507                 O   HOH c 645     1555   1555  2.16  
CISPEP   1 TYR U   42    PRO U   43          0        -1.96                     
CISPEP   2 ALA U   53    PRO U   54          0        -0.29                     
CISPEP   3 THR V   63    PRO V   64          0        -3.04                     
CISPEP   4 GLN o    3    THR o    4          0         0.48                     
CISPEP   5 GLU o   54    GLU o   55          0         1.49                     
CISPEP   6 PRO o   56    LYS o   57          0         5.48                     
CISPEP   7 TYR u   42    PRO u   43          0        -0.91                     
CISPEP   8 ALA u   53    PRO u   54          0         3.79                     
CISPEP   9 THR v   63    PRO v   64          0        -1.70                     
SITE     1 AC1 14 ASP A 170  GLU A 189  HIS A 332  GLU A 333                    
SITE     2 AC1 14 HIS A 337  ASP A 342  ALA A 344  HOH A 710                    
SITE     3 AC1 14 HOH A 714  HOH A 723  HOH A 738  HOH A 772                    
SITE     4 AC1 14 GLU C 354  ARG C 357                                          
SITE     1 AC2  5 HIS A 215  HIS A 272  BCT A 605  HIS D 214                    
SITE     2 AC2  5 HIS D 268                                                     
SITE     1 AC3  4 ASN A 181  GLU A 333  HOH A 734  LYS D 317                    
SITE     1 AC4  4 ASN A 338  PHE A 339  HOH A 773  GLU C 354                    
SITE     1 AC5  8 HIS A 215  GLU A 244  TYR A 246  HIS A 272                    
SITE     2 AC5  8 FE2 A 602  HIS D 214  TYR D 244  HIS D 268                    
SITE     1 AC6 16 PRO A 150  SER A 153  VAL A 157  MET A 183                    
SITE     2 AC6 16 PHE A 186  ILE A 192  LEU A 193  HIS A 198                    
SITE     3 AC6 16 GLY A 201  THR A 286  ALA A 287  ILE A 290                    
SITE     4 AC6 16 CLA A 607  CLA A 613  PHO D 401  CLA D 402                    
SITE     1 AC7 14 GLN A 199  VAL A 202  ALA A 203  CLA A 606                    
SITE     2 AC7 14 PHO A 608  PL9 A 611  HOH A 743  PHE D 157                    
SITE     3 AC7 14 VAL D 175  ILE D 178  PHE D 179  LEU D 182                    
SITE     4 AC7 14 CLA D 402  LMG D 407                                          
SITE     1 AC8 16 PHE A 206  LEU A 210  MET A 214  LEU A 258                    
SITE     2 AC8 16 CLA A 607  TRP D  48  ILE D 114  GLY D 121                    
SITE     3 AC8 16 PHE D 125  GLN D 129  ASN D 142  PHE D 146                    
SITE     4 AC8 16 PHE D 153  GLY D 174  LEU D 279  CLA D 402                    
SITE     1 AC9 12 ILE A  36  THR A  40  PHE A  93  PRO A  95                    
SITE     2 AC9 12 ILE A  96  TRP A  97  LEU A 114  HIS A 118                    
SITE     3 AC9 12 LEU A 121  LMG C 501  VAL I  12  PHE I  15                    
SITE     1 AD1  1 ALA A  43                                                     
SITE     1 AD2 10 MET A 214  HIS A 215  LEU A 218  HIS A 252                    
SITE     2 AD2 10 PHE A 255  SER A 264  PHE A 265  LEU A 271                    
SITE     3 AD2 10 CLA A 607  TYR D  42                                          
SITE     1 AD3 16 ASN A 267  SER A 270  PHE A 273  PHE A 274                    
SITE     2 AD3 16 LHG A 618  HOH A 713  GLN C  28  ALA C  34                    
SITE     3 AD3 16 TRP C  36  CLA C 509  DGD C 519  SER D 230                    
SITE     4 AD3 16 PHE D 232  ARG D 233  PHE K  37  BCR Y 101                    
SITE     1 AD4 15 PHE A 158  MET A 172  ILE A 176  THR A 179                    
SITE     2 AD4 15 PHE A 180  MET A 183  CLA A 606  HOH A 732                    
SITE     3 AD4 15 HOH A 741  HOH A 767  MET D 198  VAL D 201                    
SITE     4 AD4 15 ALA D 202  PHO D 401  PL9 D 405                               
SITE     1 AD5 14 ARG A 140  TRP A 142  PHE A 273  HOH A 750                    
SITE     2 AD5 14 TRP C  36  TRP C 443  ARG C 447  CLA C 505                    
SITE     3 AD5 14 CLA C 509  GLU D 219  ASN D 220  ALA D 229                    
SITE     4 AD5 14 THR D 231  PHE D 232                                          
SITE     1 AD6  9 ASP A  25  ARG A  27  LEU A  28  ILE A  38                    
SITE     2 AD6  9 THR A  45  PHE T  22  TRP b 113  TYR b 117                    
SITE     3 AD6  9 BCR b 619                                                     
SITE     1 AD7  5 TYR A 262  SQD A 612  HOH A 769  PHE E  10                    
SITE     2 AD7  5 SER E  11                                                     
SITE     1 AD8  9 TRP B 185  GLY B 186  PHE B 190  CLA B 602                    
SITE     2 AD8  9 LMG B 621  HOH B 733  PHE C 181  PHE H  41                    
SITE     3 AD8  9 BCR H 101                                                     
SITE     1 AD9 15 GLY B 189  PHE B 190  GLY B 197  HIS B 201                    
SITE     2 AD9 15 VAL B 208  PHE B 247  CLA B 601  CLA B 603                    
SITE     3 AD9 15 HOH B 788  ILE D 159  LEU D 162  PHE H  38                    
SITE     4 AD9 15 ILE H  45  TYR H  49  DGD H 102                               
SITE     1 AE1 17 ARG B  68  LEU B  69  ALA B 146  CYS B 150                    
SITE     2 AE1 17 PHE B 153  HIS B 201  HIS B 202  VAL B 252                    
SITE     3 AE1 17 THR B 262  CLA B 602  CLA B 604  CLA B 605                    
SITE     4 AE1 17 CLA B 606  CLA B 609  CLA B 610  HOH B 724                    
SITE     5 AE1 17 MET H  35                                                     
SITE     1 AE2 18 TRP B  33  PHE B  61  PHE B  65  ARG B  68                    
SITE     2 AE2 18 LEU B 149  VAL B 245  ALA B 248  ALA B 249                    
SITE     3 AE2 18 VAL B 252  PHE B 451  HIS B 455  PHE B 458                    
SITE     4 AE2 18 CLA B 603  CLA B 605  CLA B 607  CLA B 612                    
SITE     5 AE2 18 CLA B 613  CLA B 615                                          
SITE     1 AE3 16 THR B  27  VAL B  30  ALA B  34  VAL B  62                    
SITE     2 AE3 16 MET B  66  ARG B  68  HIS B 100  LEU B 103                    
SITE     3 AE3 16 ALA B 205  CLA B 603  CLA B 604  CLA B 606                    
SITE     4 AE3 16 CLA B 609  CLA B 610  CLA B 615  HOH B 718                    
SITE     1 AE4 16 LEU B  69  VAL B  71  PHE B  90  TRP B  91                    
SITE     2 AE4 16 VAL B  96  HIS B 100  LEU B 106  GLY B 152                    
SITE     3 AE4 16 PHE B 153  PHE B 156  HIS B 157  PHE B 162                    
SITE     4 AE4 16 PRO B 164  CLA B 603  CLA B 605  BCR B 619                    
SITE     1 AE5 12 TRP B  33  TYR B  40  GLN B  58  GLY B  59                    
SITE     2 AE5 12 PHE B  61  THR B 327  GLY B 328  PRO B 329                    
SITE     3 AE5 12 TRP B 450  CLA B 604  LMG B 620  HOH B 772                    
SITE     1 AE6 14 THR B 236  SER B 239  SER B 240  ALA B 243                    
SITE     2 AE6 14 PHE B 247  PHE B 463  HIS B 466  CLA B 609                    
SITE     3 AE6 14 CLA B 610  HOH B 767  PHE D 120  ILE D 123                    
SITE     4 AE6 14 MET D 126  SQD D 409                                          
SITE     1 AE7 16 PHE B 139  VAL B 208  ALA B 212  PHE B 215                    
SITE     2 AE7 16 HIS B 216  VAL B 219  PRO B 221  PRO B 222                    
SITE     3 AE7 16 CLA B 603  CLA B 605  CLA B 608  CLA B 610                    
SITE     4 AE7 16 THR H  27  MET H  31  LEU H  39  BCR H 101                    
SITE     1 AE8 13 PHE B 139  HIS B 142  MET B 231  VAL B 237                    
SITE     2 AE8 13 SER B 240  SER B 241  CLA B 603  CLA B 605                    
SITE     3 AE8 13 CLA B 608  CLA B 609  CLA B 612  CLA B 615                    
SITE     4 AE8 13 HOH B 723                                                     
SITE     1 AE9 17 TRP B   5  TYR B   6  ARG B   7  VAL B   8                    
SITE     2 AE9 17 HIS B   9  LEU B 238  LEU B 461  PHE B 462                    
SITE     3 AE9 17 GLY B 465  TRP B 468  HIS B 469  ARG B 472                    
SITE     4 AE9 17 CLA B 612  CLA B 613  CLA B 614  LHG B 623                    
SITE     5 AE9 17 HOH B 739                                                     
SITE     1 AF1 16 HIS B   9  LEU B  12  LEU B  19  HIS B  23                    
SITE     2 AF1 16 HIS B  26  THR B  27  VAL B 237  LEU B 238                    
SITE     3 AF1 16 SER B 241  CLA B 604  CLA B 610  CLA B 611                    
SITE     4 AF1 16 CLA B 613  CLA B 614  CLA B 615  HOH B 730                    
SITE     1 AF2 11 HIS B   9  HIS B  26  VAL B  30  PHE B 462                    
SITE     2 AF2 11 CLA B 604  CLA B 611  CLA B 612  CLA B 614                    
SITE     3 AF2 11 BCR B 617  LMG B 620  LHG B 623                               
SITE     1 AF3 11 VAL B   8  HIS B   9  CLA B 611  CLA B 612                    
SITE     2 AF3 11 CLA B 613  BCR B 617  LMG B 620  SQD B 624                    
SITE     3 AF3 11 GLN L   8  VAL L  10  PHE M  21                               
SITE     1 AF4 12 HIS B  23  MET B 138  HIS B 142  LEU B 145                    
SITE     2 AF4 12 CLA B 604  CLA B 605  CLA B 610  CLA B 612                    
SITE     3 AF4 12 CLA B 616  BCR B 619  LEU H  11  LEU H  14                    
SITE     1 AF5  9 ILE B  20  LEU B  24  ALA B 110  TRP B 113                    
SITE     2 AF5  9 HIS B 114  CLA B 615  BCR B 619  THR H   5                    
SITE     3 AF5  9 LEU H   7                                                     
SITE     1 AF6  7 MET B  25  CLA B 613  CLA B 614  BCR B 618                    
SITE     2 AF6  7 SQD B 624  PHE t  19  BCR t 101                               
SITE     1 AF7  8 LEU B  29  GLY B  32  SER B  36  VAL B 102                    
SITE     2 AF7  8 GLY B 105  BCR B 617  LMG B 626  BCR t 101                    
SITE     1 AF8  6 LEU B 109  TRP B 113  CLA B 606  CLA B 615                    
SITE     2 AF8  6 CLA B 616  SQD B 625                                          
SITE     1 AF9  9 THR B 327  PRO B 329  PHE B 453  CLA B 607                    
SITE     2 AF9  9 CLA B 613  CLA B 614  LHG L 102  ASN M   4                    
SITE     3 AF9  9 ALA M  10                                                     
SITE     1 AG1  6 PRO B 183  GLU B 184  TRP B 185  CLA B 601                    
SITE     2 AG1  6 HOH B 705  LEU C 204                                          
SITE     1 AG2 14 ASN A 234  TYR B   6  ARG B   7  PHE B 464                    
SITE     2 AG2 14 TRP B 468  CLA B 611  CLA B 613  HOH B 739                    
SITE     3 AG2 14 TYR D 141  TRP D 266  PHE D 269  LHG L 102                    
SITE     4 AG2 14 PHE M  14  PRO M  18                                          
SITE     1 AG3 12 ARG B  18  SER B 104  PHE B 108  TRP B 115                    
SITE     2 AG3 12 CLA B 614  BCR B 617  HOH B 708  ARG L   7                    
SITE     3 AG3 12 ARG l  14  TYR l  18  TYR m  26  PHE t  23                    
SITE     1 AG4  9 TRP B 113  TYR B 117  BCR B 619  TRP a  20                    
SITE     2 AG4  9 ASN a  26  LEU a  28  LEU a  42  THR a  45                    
SITE     3 AG4  9 PHE t  22                                                     
SITE     1 AG5  9 SER B  76  TRP B  78  BCR B 618  ALA a  54                    
SITE     2 AG5  9 ASP a 103  GLY o 112  GLY o 113  PHE t  10                    
SITE     3 AG5  9 ALA t  11                                                     
SITE     1 AG6 13 TRP A  97  GLU A  98  CLA A 609  LEU C 214                    
SITE     2 AG6 13 SER C 216  PHE C 218  GLU C 221  TRP C 223                    
SITE     3 AG6 13 CLA C 506  DGD C 517  HOH C 601  LYS I   5                    
SITE     4 AG6 13 TYR I   9                                                     
SITE     1 AG7 17 THR C  94  LEU C  95  LEU C 168  GLY C 171                    
SITE     2 AG7 17 ALA C 172  LEU C 175  VAL C 233  HIS C 237                    
SITE     3 AG7 17 ILE C 240  MET C 282  PHE C 289  TYR C 297                    
SITE     4 AG7 17 CLA C 503  CLA C 504  CLA C 507  CLA C 508                    
SITE     5 AG7 17 BCR C 516                                                     
SITE     1 AG8 14 TRP C  63  HIS C  91  LEU C 279  MET C 282                    
SITE     2 AG8 14 ALA C 286  TYR C 297  HIS C 430  LEU C 433                    
SITE     3 AG8 14 PHE C 437  CLA C 502  CLA C 504  CLA C 511                    
SITE     4 AG8 14 CLA C 513  HOH C 663                                          
SITE     1 AG9 12 ILE C  60  VAL C  61  THR C  68  LEU C  88                    
SITE     2 AG9 12 HIS C  91  VAL C 114  HIS C 118  CLA C 502                    
SITE     3 AG9 12 CLA C 503  CLA C 508  CLA C 511  CLA C 513                    
SITE     1 AH1 16 PHE A 285  LHG A 614  TRP C  63  PHE C  70                    
SITE     2 AH1 16 GLN C  84  GLY C  85  TRP C 425  SER C 429                    
SITE     3 AH1 16 CLA C 509  DGD C 518  DGD C 519  LMG C 520                    
SITE     4 AH1 16 HOH C 608  HOH C 661  PRO K  26  VAL K  30                    
SITE     1 AH2 11 PHE A  33  TRP A 131  PHE C 264  TYR C 274                    
SITE     2 AH2 11 HIS C 441  LEU C 442  ALA C 445  ARG C 449                    
SITE     3 AH2 11 LMG C 501  CLA C 508  HOH C 615                               
SITE     1 AH3 12 LEU C 165  ILE C 243  GLY C 247  TRP C 250                    
SITE     2 AH3 12 HIS C 251  THR C 255  PRO C 256  PHE C 257                    
SITE     3 AH3 12 TRP C 259  ALA C 260  CLA C 502  CLA C 508                    
SITE     1 AH4 14 MET C 157  LEU C 161  HIS C 164  TRP C 266                    
SITE     2 AH4 14 TYR C 271  TYR C 274  SER C 275  MET C 282                    
SITE     3 AH4 14 CLA C 502  CLA C 504  CLA C 506  CLA C 507                    
SITE     4 AH4 14 CLA C 510  HOH C 611                                          
SITE     1 AH5 18 SQD A 612  LHG A 614  PHE C  33  TRP C  36                    
SITE     2 AH5 18 ALA C  37  GLY C  38  ASN C  39  LEU C 272                    
SITE     3 AH5 18 PHE C 436  PHE C 437  GLY C 440  TRP C 443                    
SITE     4 AH5 18 HIS C 444  CLA C 505  CLA C 510  CLA C 511                    
SITE     5 AH5 18 CLA C 512  DGD C 518                                          
SITE     1 AH6 16 ASN C  39  LEU C  49  ALA C  52  HIS C  53                    
SITE     2 AH6 16 HIS C  56  TYR C 149  GLY C 268  TYR C 271                    
SITE     3 AH6 16 LEU C 272  SER C 275  LEU C 279  CLA C 508                    
SITE     4 AH6 16 CLA C 509  CLA C 511  CLA C 512  CLA C 513                    
SITE     1 AH7 12 ASN C  39  HIS C  56  LEU C  59  PHE C 436                    
SITE     2 AH7 12 PHE C 437  CLA C 503  CLA C 504  CLA C 509                    
SITE     3 AH7 12 CLA C 510  CLA C 512  PRO K  29  LEU K  33                    
SITE     1 AH8 19 THR C  24  ARG C  26  TRP C  35  GLY C  38                    
SITE     2 AH8 19 ASN C  39  ARG C  41  LEU C  42  LYS C  48                    
SITE     3 AH8 19 GLY C 126  PHE C 127  ILE C 134  CLA C 509                    
SITE     4 AH8 19 CLA C 510  CLA C 511  TRP K  39  GLN K  40                    
SITE     5 AH8 19 BCR K 101  ASN Y  45  VAL Z  20                               
SITE     1 AH9 11 HIS C  53  PHE C 146  PHE C 147  PHE C 163                    
SITE     2 AH9 11 HIS C 164  VAL C 167  ILE C 170  CLA C 503                    
SITE     3 AH9 11 CLA C 504  CLA C 510  CLA C 514                               
SITE     1 AI1  8 LEU C  50  VAL C 124  GLY C 128  TYR C 131                    
SITE     2 AI1  8 HIS C 132  TYR C 143  CLA C 513  BCR C 515                    
SITE     1 AI2  5 SER C 121  CLA C 514  TYR K  15  GLY Z  55                    
SITE     2 AI2  5 ASN Z  58                                                     
SITE     1 AI3  5 ILE C 209  LEU C 213  ASP C 232  PHE C 264                    
SITE     2 AI3  5 CLA C 502                                                     
SITE     1 AI4 21 LEU A  91  PRO C 217  GLY C 219  GLY C 220                    
SITE     2 AI4 21 GLU C 221  GLY C 222  TRP C 223  SER C 226                    
SITE     3 AI4 21 VAL C 227  CYS C 288  PHE C 292  ASN C 293                    
SITE     4 AI4 21 ASN C 294  THR C 295  ASP C 360  PHE C 361                    
SITE     5 AI4 21 ARG C 362  LEU C 438  LMG C 501  HOH C 644                    
SITE     6 AI4 21 HOH C 651                                                     
SITE     1 AI5 16 PHE A 197  GLU C  83  GLN C  84  GLY C  85                    
SITE     2 AI5 16 SER C 406  ASN C 418  PHE C 419  VAL C 420                    
SITE     3 AI5 16 TRP C 425  CLA C 505  CLA C 509  DGD C 519                    
SITE     4 AI5 16 LMG C 520  HOH C 620  TYR J  33  HOH J 203                    
SITE     1 AI6 17 PHE A 300  ASN A 301  SER A 305  SQD A 612                    
SITE     2 AI6 17 ASN C 405  SER C 406  VAL C 407  ASN C 415                    
SITE     3 AI6 17 SER C 416  ASN C 418  CLA C 505  DGD C 518                    
SITE     4 AI6 17 ALA J  32  TYR J  33  GLY J  37  SER J  38                    
SITE     5 AI6 17 SER J  39                                                     
SITE     1 AI7  4 HIS C  74  CLA C 505  DGD C 518  HOH C 647                    
SITE     1 AI8 11 PHE B 151  ALA B 155  PHE B 156  THR B 159                    
SITE     2 AI8 11 LEU B 161  PRO B 183  LEU C 204  ASP C 205                    
SITE     3 AI8 11 PRO C 206  TRP C 239  HOH C 609                               
SITE     1 AI9 13 LEU A  41  THR A  45  TYR A 126  GLN A 130                    
SITE     2 AI9 13 TYR A 147  PRO A 279  VAL A 283  CLA A 606                    
SITE     3 AI9 13 CLA A 613  ALA D 208  LEU D 209  ILE D 213                    
SITE     4 AI9 13 TRP D 253                                                     
SITE     1 AJ1 17 CLA A 606  CLA A 607  PHO A 608  PRO D 149                    
SITE     2 AJ1 17 VAL D 152  VAL D 156  LEU D 182  PHE D 185                    
SITE     3 AJ1 17 GLN D 186  TRP D 191  THR D 192  HIS D 197                    
SITE     4 AJ1 17 GLY D 200  VAL D 201  SER D 282  ALA D 283                    
SITE     5 AJ1 17 VAL D 286                                                     
SITE     1 AJ2 18 ILE D  35  PRO D  39  LEU D  43  LEU D  89                    
SITE     2 AJ2 18 LEU D  90  LEU D  91  LEU D  92  TRP D  93                    
SITE     3 AJ2 18 THR D 112  PHE D 113  LEU D 116  HIS D 117                    
SITE     4 AJ2 18 VAL H  40  HOH H 203  GLY X  13  LEU X  14                    
SITE     5 AJ2 18 LEU X  15  GLY X  17                                          
SITE     1 AJ3 10 TYR D  42  GLY D  46  GLY D  47  LEU D  49                    
SITE     2 AJ3 10 THR D  50  LMG D 407  PRO F  29  THR F  30                    
SITE     3 AJ3 10 PHE F  33  VAL J  25                                          
SITE     1 AJ4 13 PHE A  52  CLA A 613  MET D 198  MET D 199                    
SITE     2 AJ4 13 HIS D 214  THR D 217  TRP D 253  ALA D 260                    
SITE     3 AJ4 13 PHE D 261  LEU D 267  LHG D 406  LEU L  29                    
SITE     4 AJ4 13 LHG L 102                                                     
SITE     1 AJ5 15 ILE D 256  PHE D 257  ALA D 260  PHE D 261                    
SITE     2 AJ5 15 SER D 262  ASN D 263  TRP D 266  PL9 D 405                    
SITE     3 AJ5 15 HOH D 501  HOH D 554  ASN L  13  THR L  15                    
SITE     4 AJ5 15 TYR L  18  LEU L  19  PHE T  17                               
SITE     1 AJ6 17 CLA A 607  TYR D  67  GLY D  70  CYS D  71                    
SITE     2 AJ6 17 ASN D  72  PHE D  73  BCR D 404  HOH D 521                    
SITE     3 AJ6 17 THR F  30  ILE F  37  MET F  40  GLN F  41                    
SITE     4 AJ6 17 PHE J  28  GLY J  31  ALA J  32  LEU J  36                    
SITE     5 AJ6 17 HOH J 201                                                     
SITE     1 AJ7  9 ARG D  24  ARG D  26  HOH E 202  PHE F  16                    
SITE     2 AJ7  9 THR F  17  VAL F  18  GLN R  30  LEU R  34                    
SITE     3 AJ7  9 ASP X  35                                                     
SITE     1 AJ8  9 ARG B 230  CLA B 608  ASP D  16  ASP D  19                    
SITE     2 AJ8  9 LYS D  23  TRP D  32  LEU D 127  ARG D 134                    
SITE     3 AJ8  9 HOH D 504                                                     
SITE     1 AJ9 16 ILE E  13  ARG E  18  TYR E  19  HIS E  23                    
SITE     2 AJ9 16 LEU E  30  HOH E 204  HOH E 208  ARG F  19                    
SITE     3 AJ9 16 TRP F  20  VAL F  23  HIS F  24  ALA F  27                    
SITE     4 AJ9 16 ILE F  31  HOH F 101  ALA R  19  ILE R  23                    
SITE     1 AK1  7 CLA B 601  CLA B 609  PHE H  34  MET H  35                    
SITE     2 AK1  7 LEU H  37  PHE H  38  PHE H  41                               
SITE     1 AK2 17 TYR B 193  TRP B 257  TYR B 258  TYR B 273                    
SITE     2 AK2 17 GLN B 274  SER B 277  CLA B 602  HOH B 719                    
SITE     3 AK2 17 HIS D  87  LEU D 162  HOH D 527  TYR H  49                    
SITE     4 AK2 17 ASN H  50  VAL H  60  SER H  61  TRP H  62                    
SITE     5 AK2 17 HOH H 207                                                     
SITE     1 AK3  8 ALA C  55  GLY C  58  LEU C  59  SER C 122                    
SITE     2 AK3  8 GLY C 126  CLA C 512  PHE K  32  SER Z  16                    
SITE     1 AK4 11 ARG L  14  TYR L  18  HOH L 201  TYR M  26                    
SITE     2 AK4 11 PHE T  23  ARG b  18  PHE b 108  TRP b 115                    
SITE     3 AK4 11 CLA b 614  BCR b 617  BCR b 618                               
SITE     1 AK5 16 SER A 232  ASN A 234  PRO B   4  TRP B   5                    
SITE     2 AK5 16 TYR B   6  LMG B 620  LHG B 623  TRP D 266                    
SITE     3 AK5 16 PHE D 273  PL9 D 405  HOH D 501  GLU L  11                    
SITE     4 AK5 16 LEU L  12  ASN L  13  SER L  16  PHE M  21                    
SITE     1 AK6  3 PHE T  18  TRP b  33  BCR b 618                               
SITE     1 AK7 18 ALA V  36  CYS V  37  CYS V  40  HIS V  41                    
SITE     2 AK7 18 THR V  46  THR V  48  LEU V  52  ASP V  53                    
SITE     3 AK7 18 LEU V  54  THR V  58  LEU V  59  TYR V  75                    
SITE     4 AK7 18 TYR V  82  HIS V  92  HOH V 304  HOH V 306                    
SITE     5 AK7 18 HOH V 313  HOH V 321                                          
SITE     1 AK8 11 SQD A 612  PHE C  62  THR J  15  LEU K  31                    
SITE     2 AK8 11 ALA K  34  VAL K  38  ILE Y  28  GLY Y  29                    
SITE     3 AK8 11 GLY Y  32  PRO Y  33  SER Z  16                               
SITE     1 AK9 16 ASP a  61  ASP a 170  GLU a 189  HIS a 332                    
SITE     2 AK9 16 GLU a 333  HIS a 337  ASP a 342  ALA a 344                    
SITE     3 AK9 16 HOH a 720  HOH a 734  HOH a 738  HOH a 739                    
SITE     4 AK9 16 HOH a 772  HOH a 779  GLU c 354  ARG c 357                    
SITE     1 AL1  5 HIS a 215  HIS a 272  BCT a 605  HIS d 214                    
SITE     2 AL1  5 HIS d 268                                                     
SITE     1 AL2  5 ASN a 181  HIS a 332  GLU a 333  HOH a 746                    
SITE     2 AL2  5 LYS d 317                                                     
SITE     1 AL3  4 ASN a 338  PHE a 339  GLU c 354  HOH c 667                    
SITE     1 AL4  9 HIS a 215  GLU a 244  TYR a 246  HIS a 272                    
SITE     2 AL4  9 FE2 a 602  HOH a 713  HIS d 214  TYR d 244                    
SITE     3 AL4  9 HIS d 268                                                     
SITE     1 AL5 16 PRO a 150  SER a 153  VAL a 157  MET a 183                    
SITE     2 AL5 16 PHE a 186  ILE a 192  LEU a 193  HIS a 198                    
SITE     3 AL5 16 GLY a 201  THR a 286  ALA a 287  ILE a 290                    
SITE     4 AL5 16 CLA a 607  PHO a 608  CLA a 615  CLA d 401                    
SITE     1 AL6 17 GLN a 199  VAL a 202  ALA a 203  LEU a 210                    
SITE     2 AL6 17 CLA a 606  PHO a 609  PL9 a 612  LHG a 617                    
SITE     3 AL6 17 HOH a 749  HOH a 751  PHE d 157  VAL d 175                    
SITE     4 AL6 17 ILE d 178  PHE d 179  LEU d 182  CLA d 401                    
SITE     5 AL6 17 LMG d 407                                                     
SITE     1 AL7 15 LEU a  41  ALA a  44  THR a  45  TYR a 126                    
SITE     2 AL7 15 GLN a 130  TYR a 147  PRO a 279  VAL a 283                    
SITE     3 AL7 15 CLA a 606  CLA a 615  ALA d 208  LEU d 209                    
SITE     4 AL7 15 ILE d 213  TRP d 253  PHE d 257                               
SITE     1 AL8 14 LEU a 210  MET a 214  CLA a 607  ALA d  41                    
SITE     2 AL8 14 TRP d  48  GLY d 121  LEU d 122  PHE d 125                    
SITE     3 AL8 14 GLN d 129  ASN d 142  PHE d 146  PHE d 153                    
SITE     4 AL8 14 LEU d 279  CLA d 401                                          
SITE     1 AL9 13 ILE a  36  THR a  40  PHE a  93  PRO a  95                    
SITE     2 AL9 13 ILE a  96  TRP a  97  LEU a 114  HIS a 118                    
SITE     3 AL9 13 LMG a 614  TYR i   9  VAL i  12  THR i  13                    
SITE     4 AL9 13 PHE i  15                                                     
SITE     1 AM1  2 LEU a  42  ALA a  43                                          
SITE     1 AM2 13 MET a 214  HIS a 215  LEU a 218  HIS a 252                    
SITE     2 AM2 13 PHE a 255  ALA a 263  SER a 264  PHE a 265                    
SITE     3 AM2 13 LEU a 271  CLA a 607  LHG a 617  PRO d  39                    
SITE     4 AM2 13 LEU d  45                                                     
SITE     1 AM3 12 ASN a 267  SER a 270  TRP a 278  VAL a 281                    
SITE     2 AM3 12 HOH a 701  HOH a 741  GLN c  28  TRP c  36                    
SITE     3 AM3 12 SER d 230  PHE d 232  ARG d 233  PHE k  37                    
SITE     1 AM4 12 TRP a  97  GLU a  98  CLA a 610  LYS c 215                    
SITE     2 AM4 12 SER c 216  PHE c 218  GLU c 221  TRP c 223                    
SITE     3 AM4 12 CLA c 505  DGD c 516  LYS i   5  TYR i   9                    
SITE     1 AM5 15 PHE a 158  MET a 172  ILE a 176  THR a 179                    
SITE     2 AM5 15 MET a 183  CLA a 606  PHO a 608  HOH a 759                    
SITE     3 AM5 15 MET d 198  VAL d 201  ALA d 202  CLA d 401                    
SITE     4 AM5 15 PL9 d 404  LHG d 406  PHE t  10                               
SITE     1 AM6 13 ARG a 140  TRP a 142  PHE a 273  PHE c  33                    
SITE     2 AM6 13 TRP c  36  TRP c 443  ARG c 447  CLA c 508                    
SITE     3 AM6 13 GLU d 219  ASN d 220  ALA d 229  THR d 231                    
SITE     4 AM6 13 PHE d 232                                                     
SITE     1 AM7  7 TYR a 262  CLA a 607  PL9 a 612  LEU d  37                    
SITE     2 AM7  7 PRO e   9  PHE e  10  SER e  11                               
SITE     1 AM8  9 GLY b 186  PRO b 187  PHE b 190  CLA b 602                    
SITE     2 AM8  9 LMG b 620  HOH b 758  PHE h  41  LEU h  55                    
SITE     3 AM8  9 BCR h 101                                                     
SITE     1 AM9 16 GLY b 189  PHE b 190  PRO b 192  GLY b 197                    
SITE     2 AM9 16 HIS b 201  ALA b 205  PHE b 247  CLA b 601                    
SITE     3 AM9 16 CLA b 603  HOH b 795  ILE d 159  PHE h  38                    
SITE     4 AM9 16 PHE h  41  ILE h  45  TYR h  49  DGD h 102                    
SITE     1 AN1 14 ARG b  68  LEU b  69  ALA b 146  CYS b 150                    
SITE     2 AN1 14 PHE b 153  HIS b 201  HIS b 202  VAL b 252                    
SITE     3 AN1 14 THR b 262  CLA b 602  CLA b 604  CLA b 605                    
SITE     4 AN1 14 CLA b 606  HOH b 766                                          
SITE     1 AN2 20 TRP b  33  PHE b  61  PHE b  65  ARG b  68                    
SITE     2 AN2 20 LEU b 149  VAL b 245  ALA b 248  ALA b 249                    
SITE     3 AN2 20 VAL b 252  PHE b 451  HIS b 455  PHE b 458                    
SITE     4 AN2 20 CLA b 603  CLA b 605  CLA b 607  CLA b 610                    
SITE     5 AN2 20 CLA b 611  CLA b 612  CLA b 613  CLA b 615                    
SITE     1 AN3 17 THR b  27  VAL b  30  ALA b  31  ALA b  34                    
SITE     2 AN3 17 VAL b  62  MET b  66  ARG b  68  VAL b  96                    
SITE     3 AN3 17 HIS b 100  LEU b 103  ALA b 205  GLY b 209                    
SITE     4 AN3 17 CLA b 603  CLA b 604  CLA b 606  CLA b 612                    
SITE     5 AN3 17 HOH b 755                                                     
SITE     1 AN4 17 LEU b  69  GLY b  70  VAL b  71  TRP b  91                    
SITE     2 AN4 17 VAL b  96  ALA b  99  HIS b 100  VAL b 102                    
SITE     3 AN4 17 GLY b 152  PHE b 153  PHE b 156  HIS b 157                    
SITE     4 AN4 17 PHE b 162  PRO b 164  CLA b 603  CLA b 605                    
SITE     5 AN4 17 BCR b 619                                                     
SITE     1 AN5 15 TRP b  33  TYR b  40  GLN b  58  GLY b  59                    
SITE     2 AN5 15 PHE b  61  THR b 327  GLY b 328  TRP b 450                    
SITE     3 AN5 15 PHE b 451  CLA b 604  HOH b 792  PHE d 196                    
SITE     4 AN5 15 MET d 199  LHG d 405  LMG m 102                               
SITE     1 AN6 10 THR b 236  SER b 239  ALA b 243  PHE b 463                    
SITE     2 AN6 10 HIS b 466  CLA b 609  CLA b 610  PHE d 120                    
SITE     3 AN6 10 CLA d 402  LMG d 408                                          
SITE     1 AN7 14 PHE b 139  VAL b 208  ALA b 212  PHE b 215                    
SITE     2 AN7 14 HIS b 216  PRO b 221  PRO b 222  LEU b 229                    
SITE     3 AN7 14 CLA b 608  CLA b 610  THR h  27  MET h  31                    
SITE     4 AN7 14 LEU h  39  BCR h 101                                          
SITE     1 AN8 14 HIS b  23  PHE b 139  HIS b 142  LEU b 143                    
SITE     2 AN8 14 MET b 231  THR b 236  VAL b 237  SER b 241                    
SITE     3 AN8 14 CLA b 604  CLA b 608  CLA b 609  CLA b 612                    
SITE     4 AN8 14 CLA b 615  HOH b 719                                          
SITE     1 AN9 18 TRP b   5  TYR b   6  ARG b   7  VAL b   8                    
SITE     2 AN9 18 HIS b   9  LEU b 461  PHE b 462  PHE b 464                    
SITE     3 AN9 18 GLY b 465  TRP b 468  HIS b 469  ARG b 472                    
SITE     4 AN9 18 CLA b 604  CLA b 612  CLA b 613  CLA b 614                    
SITE     5 AN9 18 HOH b 746  LHG d 405                                          
SITE     1 AO1 16 HIS b   9  LEU b  19  HIS b  23  HIS b  26                    
SITE     2 AO1 16 THR b  27  VAL b 237  LEU b 238  SER b 241                    
SITE     3 AO1 16 CLA b 604  CLA b 605  CLA b 610  CLA b 611                    
SITE     4 AO1 16 CLA b 613  CLA b 614  CLA b 615  HOH b 768                    
SITE     1 AO2 10 HIS b  26  VAL b  30  PHE b 462  CLA b 604                    
SITE     2 AO2 10 CLA b 611  CLA b 612  CLA b 614  BCR b 617                    
SITE     3 AO2 10 BCR b 618  LHG d 405                                          
SITE     1 AO3 11 SQD L 101  VAL b   8  HIS b   9  TRP b 115                    
SITE     2 AO3 11 CLA b 611  CLA b 612  CLA b 613  BCR b 617                    
SITE     3 AO3 11 HOH b 800  GLN l   8  PHE m  21                               
SITE     1 AO4 10 HIS b  23  LEU b  24  MET b 138  HIS b 142                    
SITE     2 AO4 10 LEU b 145  CLA b 604  CLA b 610  CLA b 612                    
SITE     3 AO4 10 CLA b 616  LEU h  11                                          
SITE     1 AO5  8 ILE b  20  LEU b  24  TRP b 113  HIS b 114                    
SITE     2 AO5  8 CLA b 615  BCR b 619  HOH b 787  THR h   5                    
SITE     1 AO6  7 SQD L 101  MET b  25  TRP b 115  CLA b 613                    
SITE     2 AO6  7 CLA b 614  BCR b 618  LEU m  13                               
SITE     1 AO7 11 SQD L 101  BCR T 101  LEU b  29  GLY b  32                    
SITE     2 AO7 11 TRP b  33  SER b  36  ILE b 101  VAL b 102                    
SITE     3 AO7 11 GLY b 105  CLA b 613  BCR b 617                               
SITE     1 AO8  5 SQD A 616  LEU b 109  TRP b 113  CLA b 606                    
SITE     2 AO8  5 CLA b 616                                                     
SITE     1 AO9  6 GLU b 184  TRP b 185  CLA b 601  MET c 180                    
SITE     2 AO9  6 LEU c 204  LMG c 520                                          
SITE     1 AP1  7 ILE A  50  LEU A 102  ASP A 103  LEU A 106                    
SITE     2 AP1  7 HOH A 701  TRP b  75  LEU b  98                               
SITE     1 AP2 13 LEU c  95  LEU c 168  GLY c 171  ALA c 172                    
SITE     2 AP2 13 LEU c 175  HIS c 237  PHE c 289  TYR c 297                    
SITE     3 AP2 13 CLA c 502  CLA c 503  CLA c 507  BCR c 515                    
SITE     4 AP2 13 HOH c 666                                                     
SITE     1 AP3 14 TRP c  63  HIS c  91  LEU c  95  LEU c 279                    
SITE     2 AP3 14 MET c 282  ALA c 286  TYR c 297  HIS c 430                    
SITE     3 AP3 14 LEU c 433  PHE c 437  CLA c 501  CLA c 503                    
SITE     4 AP3 14 CLA c 510  CLA c 512                                          
SITE     1 AP4 11 ILE c  60  VAL c  61  ALA c  64  THR c  68                    
SITE     2 AP4 11 LEU c  88  HIS c  91  VAL c 114  HIS c 118                    
SITE     3 AP4 11 LEU c 279  CLA c 501  CLA c 502                               
SITE     1 AP5 15 TRP c  63  MET c  67  PHE c  70  GLN c  84                    
SITE     2 AP5 15 GLY c  85  ILE c  87  TRP c 425  SER c 429                    
SITE     3 AP5 15 CLA c 508  DGD c 517  LMG c 519  HOH c 634                    
SITE     4 AP5 15 HOH c 646  PRO k  26  VAL k  30                               
SITE     1 AP6 11 TRP a 131  LMG a 614  PHE c 264  TYR c 274                    
SITE     2 AP6 11 HIS c 441  LEU c 442  ALA c 445  ARG c 449                    
SITE     3 AP6 11 CLA c 507  BCR c 515  HOH c 632                               
SITE     1 AP7 13 LEU c 165  ILE c 243  GLY c 247  TRP c 250                    
SITE     2 AP7 13 HIS c 251  THR c 255  PRO c 256  PHE c 257                    
SITE     3 AP7 13 TRP c 259  PHE c 264  CLA c 507  LEU i  24                    
SITE     4 AP7 13 SER i  25                                                     
SITE     1 AP8 17 MET c 157  THR c 158  LEU c 161  HIS c 164                    
SITE     2 AP8 17 LEU c 168  PHE c 264  TRP c 266  TYR c 271                    
SITE     3 AP8 17 TYR c 274  SER c 275  LEU c 279  CLA c 501                    
SITE     4 AP8 17 CLA c 505  CLA c 506  CLA c 509  HOH c 602                    
SITE     5 AP8 17 HOH c 645                                                     
SITE     1 AP9 18 LHG a 616  PHE c  33  TRP c  36  ALA c  37                    
SITE     2 AP9 18 GLY c  38  ASN c  39  ALA c  40  LEU c 272                    
SITE     3 AP9 18 LEU c 276  PHE c 436  GLY c 440  TRP c 443                    
SITE     4 AP9 18 HIS c 444  ARG c 447  CLA c 504  CLA c 509                    
SITE     5 AP9 18 CLA c 510  CLA c 511                                          
SITE     1 AQ1 15 ASN c  39  LEU c  49  ALA c  52  HIS c  53                    
SITE     2 AQ1 15 HIS c  56  GLY c 268  TYR c 271  LEU c 272                    
SITE     3 AQ1 15 SER c 275  LEU c 279  CLA c 507  CLA c 508                    
SITE     4 AQ1 15 CLA c 510  CLA c 511  CLA c 512                               
SITE     1 AQ2 11 ASN c  39  HIS c  56  LEU c  59  PHE c 437                    
SITE     2 AQ2 11 CLA c 502  CLA c 508  CLA c 509  CLA c 511                    
SITE     3 AQ2 11 LMG c 519  PRO k  29  LEU k  33                               
SITE     1 AQ3 18 ARG c  26  TRP c  35  GLY c  38  ASN c  39                    
SITE     2 AQ3 18 ARG c  41  LEU c  42  LYS c  48  PHE c 127                    
SITE     3 AQ3 18 CLA c 508  CLA c 509  CLA c 510  BCR c 522                    
SITE     4 AQ3 18 TRP k  39  GLN k  40  ASN y  45  LEU y  46                    
SITE     5 AQ3 18 MET z  19  VAL z  20                                          
SITE     1 AQ4 11 HIS c  53  PHE c 146  PHE c 147  ILE c 160                    
SITE     2 AQ4 11 PHE c 163  HIS c 164  ILE c 170  CLA c 502                    
SITE     3 AQ4 11 CLA c 509  CLA c 513  BCR c 514                               
SITE     1 AQ5 10 LEU c  50  VAL c  54  VAL c 124  GLY c 128                    
SITE     2 AQ5 10 TYR c 131  HIS c 132  LEU c 140  TYR c 143                    
SITE     3 AQ5 10 CLA c 512  BCR c 514                                          
SITE     1 AQ6  6 SER c 121  VAL c 124  CLA c 512  CLA c 513                    
SITE     2 AQ6  6 TYR k  15  VAL z  51                                          
SITE     1 AQ7  7 ILE c 209  LEU c 213  GLY c 236  ILE c 240                    
SITE     2 AQ7  7 PHE c 264  CLA c 501  CLA c 505                               
SITE     1 AQ8 21 LEU a  91  PHE a 155  LMG a 614  PRO c 217                    
SITE     2 AQ8 21 GLY c 219  GLY c 220  GLU c 221  GLY c 222                    
SITE     3 AQ8 21 TRP c 223  SER c 226  PHE c 284  PHE c 292                    
SITE     4 AQ8 21 ASN c 293  ASN c 294  THR c 295  ASP c 360                    
SITE     5 AQ8 21 PHE c 361  ARG c 362  HOH c 604  HOH c 651                    
SITE     6 AQ8 21 HOH c 659                                                     
SITE     1 AQ9 15 PHE a 197  GLU c  83  GLN c  84  GLY c  85                    
SITE     2 AQ9 15 SER c 406  ASN c 418  PHE c 419  VAL c 420                    
SITE     3 AQ9 15 TRP c 425  CLA c 504  DGD c 518  LMG c 519                    
SITE     4 AQ9 15 HOH c 624  LMG d 407  TYR j  33                               
SITE     1 AR1 17 GLN a 199  PHE a 300  ASN a 301  SER a 305                    
SITE     2 AR1 17 ASN c 405  SER c 406  ASN c 415  SER c 416                    
SITE     3 AR1 17 VAL c 417  ASN c 418  DGD c 517  LMG d 407                    
SITE     4 AR1 17 ALA j  32  TYR j  33  GLY j  37  SER j  38                    
SITE     5 AR1 17 SER j  39                                                     
SITE     1 AR2  7 HIS c  74  CLA c 504  CLA c 510  DGD c 517                    
SITE     2 AR2  7 HOH c 660  ASP k  23  GLN y  21                               
SITE     1 AR3  9 ALA b 155  THR b 159  LEU b 161  PRO b 183                    
SITE     2 AR3  9 TRP b 185  LMG b 620  LEU c 204  ASP c 205                    
SITE     3 AR3  9 HOH c 606                                                     
SITE     1 AR4 12 PHE c  62  BCR c 522  THR j  15  ILE k  28                    
SITE     2 AR4 12 LEU k  31  ALA k  34  VAL k  38  ILE y  28                    
SITE     3 AR4 12 GLY y  29  GLY y  32  SER z  16  PHE z  17                    
SITE     1 AR5  8 ALA c  55  GLY c  58  LEU c  59  SER c 122                    
SITE     2 AR5  8 ALA c 123  CLA c 511  BCR c 521  PHE k  32                    
SITE     1 AR6 19 PHE a 206  CLA a 606  CLA a 607  PHO a 609                    
SITE     2 AR6 19 CLA a 615  PRO d 149  VAL d 152  VAL d 156                    
SITE     3 AR6 19 LEU d 182  PHE d 185  GLN d 186  TRP d 191                    
SITE     4 AR6 19 THR d 192  HIS d 197  GLY d 200  VAL d 201                    
SITE     5 AR6 19 SER d 282  ALA d 283  VAL d 286                               
SITE     1 AR7 15 CLA b 608  CYS d  40  LEU d  43  LEU d  89                    
SITE     2 AR7 15 LEU d  90  LEU d  91  LEU d  92  TRP d  93                    
SITE     3 AR7 15 THR d 112  PHE d 113  LEU d 116  HIS d 117                    
SITE     4 AR7 15 GLY x  13  LEU x  14  LEU x  15                               
SITE     1 AR8 12 TYR d  42  LEU d  43  GLY d  46  GLY d  47                    
SITE     2 AR8 12 LEU d  49  THR d  50  LMG d 407  PRO f  29                    
SITE     3 AR8 12 THR f  30  PHE f  33  VAL j  21  VAL j  25                    
SITE     1 AR9 14 PHE a  52  CLA a 615  MET d 198  MET d 199                    
SITE     2 AR9 14 HIS d 214  THR d 217  TRP d 253  ALA d 260                    
SITE     3 AR9 14 PHE d 261  LEU d 267  VAL d 274  VAL l  26                    
SITE     4 AR9 14 LHG l 101  PHE t  10                                          
SITE     1 AS1 14 ASN a 234  TYR b   6  ARG b   7  PHE b 464                    
SITE     2 AS1 14 TRP b 468  CLA b 607  CLA b 611  CLA b 613                    
SITE     3 AS1 14 HOH b 746  TYR d 141  ILE d 144  PHE d 269                    
SITE     4 AS1 14 HOH d 520  LHG l 101                                          
SITE     1 AS2 15 CLA a 615  ILE d 256  PHE d 257  ALA d 260                    
SITE     2 AS2 15 PHE d 261  SER d 262  ASN d 263  TRP d 266                    
SITE     3 AS2 15 HOH d 527  ASN l  13  LEU l  19  LHG l 101                    
SITE     4 AS2 15 HOH l 203  PHE t  17  ALA t  20                               
SITE     1 AS3 18 CLA a 607  DGD c 517  DGD c 518  TYR d  67                    
SITE     2 AS3 18 GLY d  70  CYS d  71  ASN d  72  PHE d  73                    
SITE     3 AS3 18 BCR d 403  THR f  30  ILE f  37  MET f  40                    
SITE     4 AS3 18 GLN f  41  PHE j  28  GLY j  31  ALA j  32                    
SITE     5 AS3 18 LEU j  36  HOH j 901                                          
SITE     1 AS4  6 ALA b 228  ARG b 230  CLA b 608  ASP d  19                    
SITE     2 AS4  6 LYS d  23  TRP d  32                                          
SITE     1 AS5 13 ILE e  13  ARG e  18  TYR e  19  HIS e  23                    
SITE     2 AS5 13 THR e  26  LEU e  30  HOH e 201  ARG f  19                    
SITE     3 AS5 13 TRP f  20  VAL f  23  HIS f  24  VAL f  28                    
SITE     4 AS5 13 ALA r  19                                                     
SITE     1 AS6  8 ARG d  24  ARG d  26  HOH e 203  PHE f  16                    
SITE     2 AS6  8 THR f  17  VAL f  18  LEU r  34  ASP x  35                    
SITE     1 AS7  4 CLA b 601  CLA b 609  LEU h  37  PHE h  38                    
SITE     1 AS8 15 TYR b 193  PHE b 250  TYR b 258  TYR b 273                    
SITE     2 AS8 15 SER b 277  CLA b 602  HIS d  87  LEU d 162                    
SITE     3 AS8 15 TYR h  49  ASN h  50  VAL h  60  SER h  61                    
SITE     4 AS8 15 TRP h  62  HOH h 202  HOH h 203                               
SITE     1 AS9 14 SER a 232  ASN a 234  PRO b   4  TRP b   5                    
SITE     2 AS9 14 TYR b   6  TRP d 266  PHE d 273  PL9 d 404                    
SITE     3 AS9 14 LHG d 405  LHG d 406  GLU l  11  LEU l  12                    
SITE     4 AS9 14 ASN l  13  SER l  16                                          
SITE     1 AT1 10 THR b 327  LYS b 332  VAL b 457  CLA b 607                    
SITE     2 AT1 10 PHE l  35  ASN m   4  LEU m   6  ALA m  10                    
SITE     3 AT1 10 HOH m 202  HOH m 204                                          
SITE     1 AT2  6 TRP B  33  MET B  37  BCR B 617  BCR B 618                    
SITE     2 AT2  6 PHE t  18  PHE t  22                                          
SITE     1 AT3 21 PHE v  33  ALA v  36  ALA v  38  SER v  39                    
SITE     2 AT3 21 CYS v  40  HIS v  41  THR v  46  THR v  48                    
SITE     3 AT3 21 LEU v  52  ASP v  53  LEU v  54  THR v  58                    
SITE     4 AT3 21 TYR v  75  TYR v  82  HIS v  92  PRO v  93                    
SITE     5 AT3 21 HOH v 306  HOH v 307  HOH v 309  HOH v 319                    
SITE     6 AT3 21 HOH v 322                                                     
SITE     1 AT4 23 ALA v  36  CYS v  37  ALA v  38  SER v  39                    
SITE     2 AT4 23 HIS v  41  VAL v  42  ILE v  45  THR v  46                    
SITE     3 AT4 23 LYS v  47  THR v  48  LEU v  52  ASP v  53                    
SITE     4 AT4 23 LEU v  54  THR v  58  TYR v  75  TYR v  82                    
SITE     5 AT4 23 HIS v  92  PRO v  93  HOH v 306  HOH v 307                    
SITE     6 AT4 23 HOH v 309  HOH v 319  HOH v 322                               
SITE     1 AT5 21 PHE v  33  ALA v  36  ALA v  38  SER v  39                    
SITE     2 AT5 21 CYS v  40  HIS v  41  THR v  46  THR v  48                    
SITE     3 AT5 21 LEU v  52  ASP v  53  LEU v  54  THR v  58                    
SITE     4 AT5 21 TYR v  75  TYR v  82  HIS v  92  PRO v  93                    
SITE     5 AT5 21 HOH v 306  HOH v 307  HOH v 309  HOH v 319                    
SITE     6 AT5 21 HOH v 322                                                     
CRYST1  117.870  223.140  310.710  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      0.008484  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004481  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003218        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system