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Database: PDB
Entry: 5H2F
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HEADER    PHOTOSYNTHESIS                          15-OCT-16   5H2F              
TITLE     CRYSTAL STRUCTURE OF THE PSBM-DELETION MUTANT OF PHOTOSYSTEM II       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM II PROTEIN D1 1;                               
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 11-344;                                       
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 FRAGMENT: UNP RESIDUES 2-506;                                        
COMPND  11 SYNONYM: PSII 47 KDA PROTEIN,PROTEIN CP-47;                          
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: PHOTOSYSTEM II CP43 REACTION CENTER PROTEIN;               
COMPND  14 CHAIN: C, c;                                                         
COMPND  15 FRAGMENT: UNP RESIDUES 7-461;                                        
COMPND  16 SYNONYM: PSII 43 KDA PROTEIN,PROTEIN CP-43;                          
COMPND  17 MOL_ID: 4;                                                           
COMPND  18 MOLECULE: PHOTOSYSTEM II D2 PROTEIN;                                 
COMPND  19 CHAIN: D, d;                                                         
COMPND  20 FRAGMENT: UNP RESIDUES 11-352;                                       
COMPND  21 SYNONYM: PSII D2 PROTEIN,PHOTOSYSTEM II Q(A) PROTEIN;                
COMPND  22 EC: 1.10.3.9;                                                        
COMPND  23 MOL_ID: 5;                                                           
COMPND  24 MOLECULE: CYTOCHROME B559 SUBUNIT ALPHA;                             
COMPND  25 CHAIN: E, e;                                                         
COMPND  26 FRAGMENT: UNP RESIDUES 5-84;                                         
COMPND  27 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  28 MOL_ID: 6;                                                           
COMPND  29 MOLECULE: CYTOCHROME B559 SUBUNIT BETA;                              
COMPND  30 CHAIN: F, f;                                                         
COMPND  31 FRAGMENT: UNP RESIDUES 13-45;                                        
COMPND  32 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  33 MOL_ID: 7;                                                           
COMPND  34 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN H;                  
COMPND  35 CHAIN: H, h;                                                         
COMPND  36 FRAGMENT: UNP RESIDUES 2-64;                                         
COMPND  37 SYNONYM: PSII-H;                                                     
COMPND  38 MOL_ID: 8;                                                           
COMPND  39 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN I;                  
COMPND  40 CHAIN: I, i;                                                         
COMPND  41 FRAGMENT: UNP RESIDUES 1-36;                                         
COMPND  42 SYNONYM: PSII-I,PSII 4.4 KDA PROTEIN;                                
COMPND  43 MOL_ID: 9;                                                           
COMPND  44 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN J;                  
COMPND  45 CHAIN: J, j;                                                         
COMPND  46 FRAGMENT: UNP RESIDUES 1-40;                                         
COMPND  47 SYNONYM: PSII-J;                                                     
COMPND  48 MOL_ID: 10;                                                          
COMPND  49 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  50 CHAIN: K, k;                                                         
COMPND  51 SYNONYM: PSII-K;                                                     
COMPND  52 MOL_ID: 11;                                                          
COMPND  53 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN L;                  
COMPND  54 CHAIN: L, l;                                                         
COMPND  55 FRAGMENT: UNP RESIDUES 3-37;                                         
COMPND  56 SYNONYM: PSII-L;                                                     
COMPND  57 MOL_ID: 12;                                                          
COMPND  58 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  59 CHAIN: O, o;                                                         
COMPND  60 FRAGMENT: UNP RESIDUES 30-272;                                       
COMPND  61 SYNONYM: MSP;                                                        
COMPND  62 MOL_ID: 13;                                                          
COMPND  63 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN T;                  
COMPND  64 CHAIN: T, t;                                                         
COMPND  65 FRAGMENT: UNP RESIDUES 1-30;                                         
COMPND  66 SYNONYM: PSII-TC;                                                    
COMPND  67 MOL_ID: 14;                                                          
COMPND  68 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  69 CHAIN: U, u;                                                         
COMPND  70 FRAGMENT: UNP RESIDUES 38-134;                                       
COMPND  71 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN,PSII-U;              
COMPND  72 MOL_ID: 15;                                                          
COMPND  73 MOLECULE: CYTOCHROME C-550;                                          
COMPND  74 CHAIN: V, v;                                                         
COMPND  75 SYNONYM: CYTOCHROME C-549,CYTOCHROME C550,LOW-POTENTIAL CYTOCHROME C;
COMPND  76 MOL_ID: 16;                                                          
COMPND  77 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN YCF12;              
COMPND  78 CHAIN: Y, y;                                                         
COMPND  79 FRAGMENT: UNP RESIDUES 18-46;                                        
COMPND  80 MOL_ID: 17;                                                          
COMPND  81 MOLECULE: PHOTOSYSTEM II REACTION CENTER X PROTEIN;                  
COMPND  82 CHAIN: X, x;                                                         
COMPND  83 FRAGMENT: UNP RESIDUES 2-38;                                         
COMPND  84 MOL_ID: 18;                                                          
COMPND  85 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN Z;                  
COMPND  86 CHAIN: Z, z;                                                         
COMPND  87 SYNONYM: PSII-Z                                                      
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;                  
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;                  
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;                  
SOURCE  35 ORGANISM_TAXID: 197221;                                              
SOURCE  36 STRAIN: BP-1;                                                        
SOURCE  37 MOL_ID: 10;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  39 ORGANISM_TAXID: 197221;                                              
SOURCE  40 STRAIN: BP-1;                                                        
SOURCE  41 MOL_ID: 11;                                                          
SOURCE  42 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  43 ORGANISM_TAXID: 197221;                                              
SOURCE  44 STRAIN: BP-1;                                                        
SOURCE  45 MOL_ID: 12;                                                          
SOURCE  46 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  47 ORGANISM_TAXID: 197221;                                              
SOURCE  48 STRAIN: BP-1;                                                        
SOURCE  49 MOL_ID: 13;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  51 ORGANISM_TAXID: 197221;                                              
SOURCE  52 STRAIN: BP-1;                                                        
SOURCE  53 MOL_ID: 14;                                                          
SOURCE  54 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  55 ORGANISM_TAXID: 197221;                                              
SOURCE  56 STRAIN: BP-1;                                                        
SOURCE  57 MOL_ID: 15;                                                          
SOURCE  58 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  59 ORGANISM_TAXID: 197221;                                              
SOURCE  60 STRAIN: BP-1;                                                        
SOURCE  61 MOL_ID: 16;                                                          
SOURCE  62 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  63 ORGANISM_TAXID: 197221;                                              
SOURCE  64 STRAIN: BP-1;                                                        
SOURCE  65 MOL_ID: 17;                                                          
SOURCE  66 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  67 ORGANISM_TAXID: 197221;                                              
SOURCE  68 STRAIN: BP-1;                                                        
SOURCE  69 MOL_ID: 18;                                                          
SOURCE  70 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS (STRAIN BP-1);    
SOURCE  71 ORGANISM_TAXID: 197221;                                              
SOURCE  72 STRAIN: BP-1                                                         
KEYWDS    PHOTOSYNTHESIS, PHOTOSYSTEM II, MUTANT, PSBM                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.UTO,K.KAWAKAMI,Y.UMENA,M.IWAI,M.IKEUCHI,J.R.SHEN,N.KAMIYA           
REVDAT   4   29-JUL-20 5H2F    1       COMPND REMARK HETNAM LINK                
REVDAT   4 2                   1       SITE                                     
REVDAT   3   02-OCT-19 5H2F    1       COMPND REMARK HET    HETNAM              
REVDAT   3 2                   1       HETSYN FORMUL LINK   ATOM                
REVDAT   2   30-AUG-17 5H2F    1       JRNL   REMARK                            
REVDAT   1   22-MAR-17 5H2F    0                                                
JRNL        AUTH   S.UTO,K.KAWAKAMI,Y.UMENA,M.IWAI,M.IKEUCHI,J.R.SHEN,N.KAMIYA  
JRNL        TITL   MUTUAL RELATIONSHIPS BETWEEN STRUCTURAL AND FUNCTIONAL       
JRNL        TITL 2 CHANGES IN A PSBM-DELETION MUTANT OF PHOTOSYSTEM II.         
JRNL        REF    FARADAY DISCUSS.              V. 198   107 2017              
JRNL        REFN                   ISSN 1359-6640                               
JRNL        PMID   28272640                                                     
JRNL        DOI    10.1039/C6FD00213G                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 365283                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 19307                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 25485                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 94.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2590                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 1291                         
REMARK   3   BIN FREE R VALUE                    : 0.3090                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 39962                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 9423                                    
REMARK   3   SOLVENT ATOMS            : 2317                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 42.03                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.00000                                              
REMARK   3    B22 (A**2) : -0.89000                                             
REMARK   3    B33 (A**2) : -2.11000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.227         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.193         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.768         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.964                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 51170 ; 0.016 ; 0.025       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 70092 ; 2.335 ; 2.534       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  5157 ; 6.068 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1750 ;33.984 ;23.074       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  6098 ;14.763 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   207 ;17.010 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  7217 ; 0.104 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 36891 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES : REFINED INDIVIDUALLY                           
REMARK   4                                                                      
REMARK   4 5H2F COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-OCT-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300001851.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.1                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL38B1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XSCALE                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.3.22                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 385629                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.7                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08300                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70500                            
REMARK 200  R SYM FOR SHELL            (I) : 0.70500                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP, MOLREP                                        
REMARK 200 STARTING MODEL: 3WU2                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.31                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG1450, SODIUM CHLORIDE, CALCIUM        
REMARK 280  CHLORIDE, MAGNESIUM SULFATE, PH 6.1, MICROBATCH, TEMPERATURE 285K   
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       60.97700            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      142.94300            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      113.49650            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      142.94300            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       60.97700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      113.49650            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, O, T, U, V, Y, X, Z                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, c, d, e, f, h, i, j, k,         
REMARK 350                    AND CHAINS: l, o, t, u, v, y, x, z                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     LYS E    84                                                      
REMARK 465     ASP I    36                                                      
REMARK 465     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     SER J     3                                                      
REMARK 465     GLU J     4                                                      
REMARK 465     GLU b   485                                                      
REMARK 465     LEU b   486                                                      
REMARK 465     SER b   487                                                      
REMARK 465     PRO b   488                                                      
REMARK 465     GLU b   489                                                      
REMARK 465     GLN b   490                                                      
REMARK 465     VAL b   491                                                      
REMARK 465     GLU b   492                                                      
REMARK 465     TRP b   493                                                      
REMARK 465     GLY b   494                                                      
REMARK 465     PHE b   495                                                      
REMARK 465     TYR b   496                                                      
REMARK 465     GLN b   497                                                      
REMARK 465     LYS b   498                                                      
REMARK 465     VAL b   499                                                      
REMARK 465     GLY b   500                                                      
REMARK 465     ASP b   501                                                      
REMARK 465     VAL b   502                                                      
REMARK 465     THR b   503                                                      
REMARK 465     THR b   504                                                      
REMARK 465     ARG b   505                                                      
REMARK 465     ARG b   506                                                      
REMARK 465     GLU d    11                                                      
REMARK 465     THR e     5                                                      
REMARK 465     TYR f    13                                                      
REMARK 465     PRO f    14                                                      
REMARK 465     ALA h    64                                                      
REMARK 465     GLN x    38                                                      
REMARK 465     VAL z    62                                                      
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     LEU A  13    CG   CD1  CD2                                       
REMARK 470     GLU A  15    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  16    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR A 228    OG1  CG2                                            
REMARK 470     GLU A 229    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 231    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 243    CG   CD   OE1  OE2                                  
REMARK 470     THR A 286    OG1  CG2                                            
REMARK 470     LYS B 227    CG   CD   CE   NZ                                   
REMARK 470     LYS B 349    CG   CD   CE   NZ                                   
REMARK 470     SER B 480    OG                                                  
REMARK 470     GLU B 485    CG   CD   OE1  OE2                                  
REMARK 470     LEU B 486    CG   CD1  CD2                                       
REMARK 470     SER B 487    OG                                                  
REMARK 470     GLU B 489    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 490    CG   CD   OE1  NE2                                  
REMARK 470     GLU B 492    CG   CD   OE1  OE2                                  
REMARK 470     GLN B 497    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 499    CG1  CG2                                            
REMARK 470     VAL B 502    CG1  CG2                                            
REMARK 470     THR B 504    OG1  CG2                                            
REMARK 470     ARG B 505    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 506    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     THR C  24    OG1  CG2                                            
REMARK 470     ASN C  25    CG   OD1  ND2                                       
REMARK 470     SER C  30    OG                                                  
REMARK 470     GLU C 142    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 207    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D  11    CG   CD   OE1  OE2                                  
REMARK 470     ARG D  12    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E  77    CG   CD   OE1  OE2                                  
REMARK 470     ARG J   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG O  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN O  61    CG   CD   OE1  NE2                                  
REMARK 470     GLU O  62    CG   CD   OE1  OE2                                  
REMARK 470     GLU O  98    CG   CD   OE1  OE2                                  
REMARK 470     ILE T  29    CG1  CG2  CD1                                       
REMARK 470     THR T  30    OG1  CG2                                            
REMARK 470     LYS V  17    CG   CD   CE   NZ                                   
REMARK 470     VAL X  37    CG1  CG2                                            
REMARK 470     GLN X  38    CG   CD   OE1  NE2                                  
REMARK 470     ILE Z   3    CG1  CG2  CD1                                       
REMARK 470     GLN Z  31    CG   CD   OE1  NE2                                  
REMARK 470     ASP Z  34    CG   OD1  OD2                                       
REMARK 470     ARG Z  35    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER Z  36    OG                                                  
REMARK 470     PHE Z  41    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     VAL Z  61    CG1  CG2                                            
REMARK 470     GLU a  15    CG   CD   OE1  OE2                                  
REMARK 470     LEU a 223    CG   CD1  CD2                                       
REMARK 470     ARG a 225    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU a 226    CG   CD   OE1  OE2                                  
REMARK 470     THR a 228    OG1  CG2                                            
REMARK 470     GLU a 229    CG   CD   OE1  OE2                                  
REMARK 470     THR a 230    OG1  CG2                                            
REMARK 470     GLU a 231    CG   CD   OE1  OE2                                  
REMARK 470     TYR a 235    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLU a 242    CG   CD   OE1  OE2                                  
REMARK 470     GLU a 243    CG   CD   OE1  OE2                                  
REMARK 470     THR a 245    OG1  CG2                                            
REMARK 470     TYR a 246    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE a 248    CG1  CG2  CD1                                       
REMARK 470     VAL a 249    CG1  CG2                                            
REMARK 470     GLN a 261    CG   CD   OE1  NE2                                  
REMARK 470     TYR a 262    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     SER a 264    OG                                                  
REMARK 470     THR a 286    OG1  CG2                                            
REMARK 470     ARG b 127    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS b 227    CG   CD   CE   NZ                                   
REMARK 470     LYS b 349    CD   CE   NZ                                        
REMARK 470     GLU b 350    CD   OE1  OE2                                       
REMARK 470     PHE b 479    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     SER b 480    OG                                                  
REMARK 470     ASN c  19    CG   OD1  ND2                                       
REMARK 470     ARG d  24    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU d 241    CG   CD   OE1  OE2                                  
REMARK 470     SER e  11    OG                                                  
REMARK 470     ARG e  61    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS e  84    CG   CD   CE   NZ                                   
REMARK 470     GLU i   2    CD   OE1  OE2                                       
REMARK 470     MET j   1    CG   SD   CE                                        
REMARK 470     MET j   2    SD   CE                                             
REMARK 470     ARG j   7    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS k  10    CG   CD   CE   NZ                                   
REMARK 470     ILE k  17    CG1  CG2  CD1                                       
REMARK 470     ARG o  27    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER o  35    OG                                                  
REMARK 470     GLU o  54    CG   CD   OE1  OE2                                  
REMARK 470     LYS o  59    CG   CD   CE   NZ                                   
REMARK 470     ARG o  60    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU o  62    CG   CD   OE1  OE2                                  
REMARK 470     ARG o 207    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE t  29    CG1  CG2  CD1                                       
REMARK 470     THR t  30    OG1  CG2                                            
REMARK 470     GLU u   8    CG   CD   OE1  OE2                                  
REMARK 470     GLU u  23    CG   CD   OE1  OE2                                  
REMARK 470     LYS v  17    CG   CD   CE   NZ                                   
REMARK 470     LYS v  24    CG   CD   CE   NZ                                   
REMARK 470     LYS v 110    CG   CD   CE   NZ                                   
REMARK 470     VAL y  18    CG1  CG2                                            
REMARK 470     ILE y  19    CG1  CG2  CD1                                       
REMARK 470     ILE y  25    CG1  CG2  CD1                                       
REMARK 470     LYS x   8    CG   CD   CE   NZ                                   
REMARK 470     GLN x  33    CG   CD   OE1  NE2                                  
REMARK 470     MET z   1    CG   SD   CE                                        
REMARK 470     THR z   2    OG1  CG2                                            
REMARK 470     ILE z   3    CG1  CG2  CD1                                       
REMARK 470     LEU z   7    CG   CD1  CD2                                       
REMARK 470     GLN z  31    CG   CD   OE1  NE2                                  
REMARK 470     ASP z  32    CG   OD1  OD2                                       
REMARK 470     ASP z  34    CG   OD1  OD2                                       
REMARK 470     ARG z  35    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU z  42    CG   CD1  CD2                                       
REMARK 470     LEU z  57    CG   CD1  CD2                                       
REMARK 470     VAL z  61    CG1  CG2                                            
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   NH2  ARG B   347     O    HOH B   701              2.09            
REMARK 500   OH   TYR V   136     O    HOH V   301              2.10            
REMARK 500   OE2  GLU c   413     O    HOH c  1001              2.11            
REMARK 500   OE2  GLU D   343     O    HOH D   501              2.11            
REMARK 500   O    GLY c   148     NZ   LYS c   156              2.14            
REMARK 500   OE2  GLU O    74     O    HOH O   401              2.16            
REMARK 500   O    PRO c   191     O    HOH c  1002              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TRP A 278   CE2   TRP A 278   CD2     0.079                       
REMARK 500    TRP A 317   CE2   TRP A 317   CD2     0.082                       
REMARK 500    TRP B   5   CE2   TRP B   5   CD2     0.073                       
REMARK 500    TRP B  56   CE2   TRP B  56   CD2     0.076                       
REMARK 500    TRP B  78   CE2   TRP B  78   CD2     0.083                       
REMARK 500    HIS B 114   CG    HIS B 114   CD2     0.058                       
REMARK 500    HIS C  56   CG    HIS C  56   CD2     0.059                       
REMARK 500    HIS C  91   CG    HIS C  91   CD2     0.055                       
REMARK 500    TRP C 387   CE2   TRP C 387   CD2     0.087                       
REMARK 500    TRP D  58   CE2   TRP D  58   CD2     0.073                       
REMARK 500    HIS D  87   CG    HIS D  87   CD2     0.088                       
REMARK 500    HIS V  41   CG    HIS V  41   CD2     0.055                       
REMARK 500    HIS a 118   CG    HIS a 118   CD2     0.057                       
REMARK 500    HIS a 195   CG    HIS a 195   CD2     0.064                       
REMARK 500    HIS a 304   CG    HIS a 304   CD2     0.057                       
REMARK 500    HIS a 332   CG    HIS a 332   CD2     0.061                       
REMARK 500    HIS b  26   CG    HIS b  26   CD2     0.058                       
REMARK 500    TRP b  33   CE2   TRP b  33   CD2     0.077                       
REMARK 500    TRP b 275   CE2   TRP b 275   CD2     0.077                       
REMARK 500    TRP c 365   CE2   TRP c 365   CD2     0.080                       
REMARK 500    TRP d  48   CE2   TRP d  48   CD2     0.075                       
REMARK 500    HIS d  61   CG    HIS d  61   CD2     0.055                       
REMARK 500    TRP d  93   CE2   TRP d  93   CD2     0.073                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP C 473   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ARG b  57   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG b  57   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.5 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    VAL A  30      -84.79    -96.05                                   
REMARK 500    LEU A 159      -55.35   -120.96                                   
REMARK 500    SER A 167      135.67   -170.13                                   
REMARK 500    ARG A 225      108.88    -55.39                                   
REMARK 500    ILE A 259      -99.19   -103.80                                   
REMARK 500    ASP B  49       80.37   -154.54                                   
REMARK 500    MET B 231       -9.48    -59.03                                   
REMARK 500    ASP B 313       47.99    -88.89                                   
REMARK 500    PHE B 383      -82.25    -94.29                                   
REMARK 500    ARG B 505      137.99    -39.38                                   
REMARK 500    THR C  24       94.64    -56.66                                   
REMARK 500    ASP C 107      114.67   -169.68                                   
REMARK 500    ASN C 201       70.85   -116.41                                   
REMARK 500    TRP C 223     -140.43     52.55                                   
REMARK 500    MET C 356      -36.57    -37.74                                   
REMARK 500    SER C 416      -47.27    173.35                                   
REMARK 500    GLU C 464      108.16    -59.43                                   
REMARK 500    ARG D  12     -116.20    139.98                                   
REMARK 500    VAL D  30      -73.01   -116.00                                   
REMARK 500    SER D  65        9.43   -156.68                                   
REMARK 500    LEU D 158      -60.20   -121.97                                   
REMARK 500    ALA D 234       37.69    -81.87                                   
REMARK 500    ASN D 292       16.41     57.64                                   
REMARK 500    PRO D 309        5.25    -64.80                                   
REMARK 500    ALA D 351      -53.00     76.17                                   
REMARK 500    LYS I  33     -120.92   -101.17                                   
REMARK 500    SER J  39       -1.64     70.25                                   
REMARK 500    ALA O  26       83.59    -64.93                                   
REMARK 500    SER O  34       -3.58    -52.49                                   
REMARK 500    ARG O  42      109.20   -162.81                                   
REMARK 500    LYS O  59       34.42    -89.68                                   
REMARK 500    ARG O  73     -164.09     70.13                                   
REMARK 500    THR O 138        1.93    -59.85                                   
REMARK 500    ASN U  29      -37.19   -137.60                                   
REMARK 500    TYR U 103     -139.51   -114.56                                   
REMARK 500    ASN V  49       79.04   -161.18                                   
REMARK 500    ASP V  67       39.42    -83.81                                   
REMARK 500    ASN V  78       71.07   -152.94                                   
REMARK 500    PHE V 101       74.64   -114.71                                   
REMARK 500    GLN Z  31      -94.87    -68.98                                   
REMARK 500    ASP Z  32       95.02    -49.60                                   
REMARK 500    VAL a  30      -84.41    -89.52                                   
REMARK 500    ASN a  76     -169.56   -109.25                                   
REMARK 500    LEU a 159      -53.52   -126.51                                   
REMARK 500    HIS a 190       -7.42   -142.73                                   
REMARK 500    ARG a 225       97.16    -57.98                                   
REMARK 500    GLU a 229       46.05    -77.24                                   
REMARK 500    THR a 230      -42.32   -154.95                                   
REMARK 500    ILE a 259      -91.82   -108.40                                   
REMARK 500    ASP b  49       83.74   -151.60                                   
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 B 956        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH H 239        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH J 215        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH O 561        DISTANCE =  6.33 ANGSTROMS                       
REMARK 525    HOH b 950        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH b 951        DISTANCE =  7.60 ANGSTROMS                       
REMARK 525    HOH c1216        DISTANCE =  6.48 ANGSTROMS                       
REMARK 525    HOH h 231        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH o 553        DISTANCE =  6.05 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  406                                                       
REMARK 610     LMG A  410                                                       
REMARK 610     LHG A  412                                                       
REMARK 610     SQD A  413                                                       
REMARK 610     CLA B  614                                                       
REMARK 610     CLA B  615                                                       
REMARK 610     CLA B  617                                                       
REMARK 610     BCR B  618                                                       
REMARK 610     BCR B  619                                                       
REMARK 610     LMG B  621                                                       
REMARK 610     LMT B  622                                                       
REMARK 610     CLA C  513                                                       
REMARK 610     DGD C  517                                                       
REMARK 610     DGD C  518                                                       
REMARK 610     DGD C  519                                                       
REMARK 610     LMG C  520                                                       
REMARK 610     LHG C  522                                                       
REMARK 610     HTG C  523                                                       
REMARK 610     LMG C  531                                                       
REMARK 610     DGD D  407                                                       
REMARK 610     SQD D  408                                                       
REMARK 610     LHG D  411                                                       
REMARK 610     LMG D  412                                                       
REMARK 610     LMT E  101                                                       
REMARK 610     DGD H  102                                                       
REMARK 610     LMG J  101                                                       
REMARK 610     LHG L  101                                                       
REMARK 610     LMT T  102                                                       
REMARK 610     HTG V  203                                                       
REMARK 610     BCR Y  101                                                       
REMARK 610     CLA a  409                                                       
REMARK 610     SQD a  418                                                       
REMARK 610     LHG a  423                                                       
REMARK 610     CLA b  614                                                       
REMARK 610     CLA b  615                                                       
REMARK 610     CLA b  617                                                       
REMARK 610     BCR b  618                                                       
REMARK 610     BCR b  619                                                       
REMARK 610     SQD b  621                                                       
REMARK 610     LMG b  622                                                       
REMARK 610     DGD c  917                                                       
REMARK 610     DGD c  918                                                       
REMARK 610     DGD c  919                                                       
REMARK 610     LMG c  920                                                       
REMARK 610     LMG c  930                                                       
REMARK 610     LMT c  931                                                       
REMARK 610     LHG d  401                                                       
REMARK 610     DGD d  406                                                       
REMARK 610     LHG d  408                                                       
REMARK 610     LMG d  409                                                       
REMARK 610     SQD f  101                                                       
REMARK 610     LMT f  102                                                       
REMARK 610     DGD h  102                                                       
REMARK 610     LMG i  101                                                       
REMARK 610     LMG j  101                                                       
REMARK 610     LMT t  101                                                       
REMARK 610     HTG v  203                                                       
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 401  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD1                                                    
REMARK 620 2 OEX A 401   O5  105.8                                              
REMARK 620 3 OEX A 401   O4   93.5  87.8                                        
REMARK 620 4 GLU A 333   OE2 168.8  82.9  93.9                                  
REMARK 620 5 HOH A 522   O    81.2 172.9  93.5  90.0                            
REMARK 620 6 HOH A 591   O    89.8  84.4 172.1  84.0  94.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 401  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 OEX A 401   O1  155.2                                              
REMARK 620 3 OEX A 401   O2   87.8  67.8                                        
REMARK 620 4 OEX A 401   O5  103.4  74.2  72.2                                  
REMARK 620 5 GLU A 189   OE1 146.5  58.3 124.9  82.9                            
REMARK 620 6 ALA A 344   O    91.6  75.3  67.2 135.9 106.7                      
REMARK 620 7 HOH A 521   O    96.4  98.4 136.4 146.2  65.9  69.4                
REMARK 620 8 HOH A 604   O    79.4 122.8 143.0  77.2  69.9 146.8  79.9          
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 401  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEX A 401   O1   89.2                                              
REMARK 620 3 OEX A 401   O5   99.1  79.2                                        
REMARK 620 4 OEX A 401   O3  168.3  99.0  74.5                                  
REMARK 620 5 HIS A 332   NE2  89.2 176.2  97.7  82.1                            
REMARK 620 6 ASP A 342   OD2 100.9  96.4 159.5  86.5  87.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 A 402  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  96.5                                              
REMARK 620 3 BCT A 421   O2  149.0 100.1                                        
REMARK 620 4 BCT A 421   O2  131.1  80.1  30.5                                  
REMARK 620 5 BCT A 421   O3   99.9  92.6  53.6  32.7                            
REMARK 620 6 BCT A 421   O3  171.7  91.0  31.0  53.7  83.2                      
REMARK 620 7 HIS D 214   NE2 106.7  85.9 100.4 121.5 153.3  70.2                
REMARK 620 8 HIS D 268   NE2  89.8 173.6  74.7  96.6  87.4  82.6  91.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 401  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEX A 401   O2  166.7                                              
REMARK 620 3 OEX A 401   O3   75.8  91.1                                        
REMARK 620 4 OEX A 401   O4   96.1  97.1 171.1                                  
REMARK 620 5 OEX A 401   O5   88.7  91.9  82.4  93.8                            
REMARK 620 6 GLU C 354   OE2  88.9  88.1  86.9  96.9 169.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX A 401  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD1                                                    
REMARK 620 2 OEX A 401   O1   99.0                                              
REMARK 620 3 OEX A 401   O2  171.4  83.5                                        
REMARK 620 4 OEX A 401   O3   96.0  84.5  92.5                                  
REMARK 620 5 ALA A 344   OXT  87.6  98.6  83.8 174.8                            
REMARK 620 6 GLU C 354   OE1  87.2 172.9  90.9  91.6  84.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 406  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 614   O                                                      
REMARK 620 2 CLA A 406   NA   91.6                                              
REMARK 620 3 CLA A 406   NB  103.3  84.9                                        
REMARK 620 4 CLA A 406   NC  106.9 159.6  98.7                                  
REMARK 620 5 CLA A 406   ND   97.2  89.8 158.9  79.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA D 401  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 578   O                                                      
REMARK 620 2 CLA D 401   NA   91.5                                              
REMARK 620 3 CLA D 401   NB  101.2  87.9                                        
REMARK 620 4 CLA D 401   NC  109.1 159.2  90.5                                  
REMARK 620 5 CLA D 401   ND  101.4  90.2 157.4  83.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN B 438   OD1                                                    
REMARK 620 2 HOH B 720   O   100.3                                              
REMARK 620 3 HOH B 850   O   154.0  94.7                                        
REMARK 620 4 HOH B 932   O   100.2 150.9  75.0                                  
REMARK 620 5 HOH O 518   O   144.9  74.0  60.0  77.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 705   O                                                      
REMARK 620 2 CLA B 602   NA   81.9                                              
REMARK 620 3 CLA B 602   NB  106.5  81.2                                        
REMARK 620 4 CLA B 602   NC  116.3 161.4  96.1                                  
REMARK 620 5 CLA B 602   ND   90.3  90.8 160.0  85.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 608  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 855   O                                                      
REMARK 620 2 CLA B 608   NA   93.4                                              
REMARK 620 3 CLA B 608   NB  106.0  88.9                                        
REMARK 620 4 CLA B 608   NC  102.8 162.8  92.1                                  
REMARK 620 5 CLA B 608   ND   95.5  85.5 158.0  87.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 611  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B 710   O                                                      
REMARK 620 2 CLA B 611   NA  100.4                                              
REMARK 620 3 CLA B 611   NB   90.8  85.8                                        
REMARK 620 4 CLA B 611   NC   96.8 159.0  81.9                                  
REMARK 620 5 CLA B 611   ND  109.6 103.8 155.0  81.5                            
REMARK 620 N                    1     2     3     4                             
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  102.8                                              
REMARK 620 3 CLA C 512   NB  102.0  81.0                                        
REMARK 620 4 CLA C 512   NC  104.2 153.0  92.9                                  
REMARK 620 5 CLA C 512   ND  107.0  91.6 150.9  81.0                            
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 722   O                                                      
REMARK 620 2 CLA C 505   NA   90.6                                              
REMARK 620 3 CLA C 505   NB  113.8  86.9                                        
REMARK 620 4 CLA C 505   NC  118.3 150.4  86.9                                  
REMARK 620 5 CLA C 505   ND  102.5  85.0 142.8  82.7                            
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 607   O                                                      
REMARK 620 2 CLA C 508   NA   88.2                                              
REMARK 620 3 CLA C 508   NB  106.4  89.6                                        
REMARK 620 4 CLA C 508   NC  111.4 160.0  88.7                                  
REMARK 620 5 CLA C 508   ND   95.2  90.7 158.4  83.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM E 102  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  23   NE2                                                    
REMARK 620 2 HEM E 102   NA   94.8                                              
REMARK 620 3 HEM E 102   NB   90.5  88.9                                        
REMARK 620 4 HEM E 102   NC   87.7 177.4  91.2                                  
REMARK 620 5 HEM E 102   ND   87.6  91.2 178.1  88.8                            
REMARK 620 6 HIS F  24   NE2 175.9  83.2  93.0  94.3  88.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG J 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH F 201   O                                                      
REMARK 620 2 GLY J  31   O   157.1                                              
REMARK 620 3 ALA J  34   O   107.9  77.6                                        
REMARK 620 4 LEU J  36   O    92.7 108.7  98.3                                  
REMARK 620 5 LMG J 101   O4   87.5  83.4 160.0  93.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K  19   OD2                                                    
REMARK 620 2 ASP K  23   OD2 102.9                                              
REMARK 620 3 HOH K 201   O    69.2  87.2                                        
REMARK 620 4 HOH K 206   O   167.7  75.8  98.5                                  
REMARK 620 5 HOH Y 206   O    99.2  94.0 168.3  93.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA O 302  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR O 138   O                                                      
REMARK 620 2 ASN O 200   OD1 147.9                                              
REMARK 620 3 VAL O 201   O    84.0  74.1                                        
REMARK 620 4 HOH O 459   O    75.4  79.6  85.2                                  
REMARK 620 5 HOH O 533   O   109.9  80.0 147.7  71.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC V 202  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  41   NE2                                                    
REMARK 620 2 HEC V 202   NA   92.3                                              
REMARK 620 3 HEC V 202   NB   88.1  91.2                                        
REMARK 620 4 HEC V 202   NC   90.1 177.4  87.9                                  
REMARK 620 5 HEC V 202   ND   90.9  90.8 177.8  90.1                            
REMARK 620 6 HIS V  92   NE2 170.5  97.1  92.0  80.5  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 403  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD1                                                    
REMARK 620 2 OEX a 403   O1  144.1                                              
REMARK 620 3 OEX a 403   O2   81.1  63.5                                        
REMARK 620 4 OEX a 403   O5   96.7  80.9  74.8                                  
REMARK 620 5 GLU a 189   OE1 147.3  68.6 131.3  89.6                            
REMARK 620 6 ALA a 344   O    80.4  75.9  58.7 133.5 117.5                      
REMARK 620 7 HOH a 506   O    94.0 103.3 129.7 154.7  69.5  71.0                
REMARK 620 8 HOH a 599   O    82.8 130.3 145.5  77.0  67.4 146.7  81.7          
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 403  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 170   OD2                                                    
REMARK 620 2 OEX a 403   O5  105.6                                              
REMARK 620 3 OEX a 403   O4   98.1  88.4                                        
REMARK 620 4 GLU a 333   OE2 161.5  90.1  91.9                                  
REMARK 620 5 HOH a 544   O    84.9 169.1  87.2  80.1                            
REMARK 620 6 HOH a 597   O    85.4  86.2 174.2  86.0  97.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 403  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 189   OE2                                                    
REMARK 620 2 OEX a 403   O1   95.8                                              
REMARK 620 3 OEX a 403   O5  105.2  88.5                                        
REMARK 620 4 OEX a 403   O3  167.5  82.4  62.4                                  
REMARK 620 5 HIS a 332   NE2  93.3 169.8  93.4  89.7                            
REMARK 620 6 ASP a 342   OD2  93.5  80.7 159.2  98.4  94.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             FE2 a 404  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a 215   NE2                                                    
REMARK 620 2 HIS a 272   NE2  93.7                                              
REMARK 620 3 BCT a 422   O2   90.2  90.6                                        
REMARK 620 4 BCT a 422   O3  141.3  94.1  51.9                                  
REMARK 620 5 HIS d 214   NE2 105.3  97.8 161.7 111.1                            
REMARK 620 6 HIS d 268   NE2  85.8 175.8  85.2  83.9  86.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 403  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a 333   OE1                                                    
REMARK 620 2 OEX a 403   O2  165.5                                              
REMARK 620 3 OEX a 403   O3   83.0  86.2                                        
REMARK 620 4 OEX a 403   O4   94.1  95.2 171.3                                  
REMARK 620 5 OEX a 403   O5   83.6 105.6  88.1  99.7                            
REMARK 620 6 GLU c 354   OE2  91.5  77.9  84.7  87.2 171.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEX a 403  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a 342   OD1                                                    
REMARK 620 2 OEX a 403   O1   88.5                                              
REMARK 620 3 OEX a 403   O2  159.6 104.2                                        
REMARK 620 4 OEX a 403   O3  109.0  89.1  87.5                                  
REMARK 620 5 ALA a 344   OXT  84.2  90.4  79.8 166.7                            
REMARK 620 6 GLU c 354   OE1  85.8 174.3  81.1  93.4  88.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a 408  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH a 567   O                                                      
REMARK 620 2 CLA a 408   NA   91.2                                              
REMARK 620 3 CLA a 408   NB  101.7  85.6                                        
REMARK 620 4 CLA a 408   NC  109.2 157.3  80.6                                  
REMARK 620 5 CLA a 408   ND  100.6  95.1 157.7  91.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a 409  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH a 602   O                                                      
REMARK 620 2 CLA a 409   NA   91.8                                              
REMARK 620 3 CLA a 409   NB  106.2  83.1                                        
REMARK 620 4 CLA a 409   NC  110.0 157.8  86.5                                  
REMARK 620 5 CLA a 409   ND  100.1  92.5 153.5  88.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA b 601  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN b 438   OD1                                                    
REMARK 620 2 HOH b 755   O    89.0                                              
REMARK 620 3 HOH b 787   O    93.4  78.4                                        
REMARK 620 4 HOH b 861   O    78.6  78.9 156.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 602  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 706   O                                                      
REMARK 620 2 CLA b 602   NA   82.5                                              
REMARK 620 3 CLA b 602   NB  108.4  85.9                                        
REMARK 620 4 CLA b 602   NC  115.4 158.8  98.1                                  
REMARK 620 5 CLA b 602   ND   87.0  82.1 159.1  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 608  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 860   O                                                      
REMARK 620 2 CLA b 608   NA   96.6                                              
REMARK 620 3 CLA b 608   NB  102.5  88.1                                        
REMARK 620 4 CLA b 608   NC  106.8 156.6  86.9                                  
REMARK 620 5 CLA b 608   ND  100.3  89.8 157.1  86.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b 611  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH b 737   O                                                      
REMARK 620 2 CLA b 611   NA  100.6                                              
REMARK 620 3 CLA b 611   NB   92.5  87.2                                        
REMARK 620 4 CLA b 611   NC   96.3 161.7  85.0                                  
REMARK 620 5 CLA b 611   ND  103.8  99.4 160.8  83.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA c 901  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 PHE c  22   O                                                      
REMARK 620 2 THR c  24   O    93.7                                              
REMARK 620 3 ASP c  27   OD1 120.8  99.1                                        
REMARK 620 4 ASP c  27   OD2  74.9  84.4  49.7                                  
REMARK 620 5 SER c  30   OG  158.0  99.1  74.8 124.0                            
REMARK 620 6 HOH c1158   O    80.0  83.1 158.6 151.1  83.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 912  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c  39   OD1                                                    
REMARK 620 2 CLA c 912   NA  100.6                                              
REMARK 620 3 CLA c 912   NB  104.9  85.6                                        
REMARK 620 4 CLA c 912   NC  103.0 156.1  92.0                                  
REMARK 620 5 CLA c 912   ND  101.6  88.0 153.5  83.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 905  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH c1166   O                                                      
REMARK 620 2 CLA c 905   NA   96.2                                              
REMARK 620 3 CLA c 905   NB   99.5  83.2                                        
REMARK 620 4 CLA c 905   NC  110.8 151.9  84.5                                  
REMARK 620 5 CLA c 905   ND  115.5  89.7 144.9  85.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c 908  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH c1017   O                                                      
REMARK 620 2 CLA c 908   NA   83.4                                              
REMARK 620 3 CLA c 908   NB  104.6  87.8                                        
REMARK 620 4 CLA c 908   NC  120.5 154.5  93.7                                  
REMARK 620 5 CLA c 908   ND   96.3  86.2 157.4  82.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM e 101  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e  23   NE2                                                    
REMARK 620 2 HEM e 101   NA   90.6                                              
REMARK 620 3 HEM e 101   NB   85.7  88.7                                        
REMARK 620 4 HEM e 101   NC   90.1 178.6  92.6                                  
REMARK 620 5 HEM e 101   ND   90.7  91.9 176.4  86.8                            
REMARK 620 6 HIS f  24   NE2 176.4  86.0  95.2  93.3  88.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG j 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH f 201   O                                                      
REMARK 620 2 GLY j  31   O   156.4                                              
REMARK 620 3 ALA j  34   O   110.3  77.9                                        
REMARK 620 4 LEU j  36   O    97.8 102.8  99.5                                  
REMARK 620 5 LMG j 101   O4   85.6  81.8 158.1  93.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG k 102  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP k  19   OD2                                                    
REMARK 620 2 ASP k  23   OD2  98.0                                              
REMARK 620 3 HOH k 201   O    69.3  91.4                                        
REMARK 620 4 HOH k 206   O   162.0  73.1  94.9                                  
REMARK 620 5 HOH k 207   O   104.5 107.9 160.5  93.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA o 301  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR o 138   O                                                      
REMARK 620 2 ASN o 200   OD1 151.3                                              
REMARK 620 3 VAL o 201   O    73.4  85.9                                        
REMARK 620 4 HOH o 416   O    80.9  77.8  85.5                                  
REMARK 620 5 HOH o 441   O   132.8  67.3  94.6 144.9                            
REMARK 620 6 HOH o 447   O    69.7 136.5 104.8 143.9  69.8                      
REMARK 620 7 HOH o 489   O   110.0  79.2 151.5  67.7 101.7 102.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC v 202  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v  41   NE2                                                    
REMARK 620 2 HEC v 202   NA   91.2                                              
REMARK 620 3 HEC v 202   NB   82.0  83.7                                        
REMARK 620 4 HEC v 202   NC   87.4 177.7  94.3                                  
REMARK 620 5 HEC v 202   ND   95.4  97.1 177.3  84.8                            
REMARK 620 6 HIS v  92   NE2 168.8  99.9  97.9  81.5  84.5                      
REMARK 620 N                    1     2     3     4     5                       
DBREF  5H2F A   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  5H2F B    2   506  UNP    Q8DIQ1   PSBB_THEEB       2    506             
DBREF  5H2F C   19   473  UNP    Q8DIF8   PSBC_THEEB       7    461             
DBREF  5H2F D   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  5H2F E    5    84  UNP    Q8DIP0   PSBE_THEEB       5     84             
DBREF  5H2F F   13    45  UNP    Q8DIN9   PSBF_THEEB      13     45             
DBREF  5H2F H    2    64  UNP    Q8DJ43   PSBH_THEEB       2     64             
DBREF  5H2F I    1    36  UNP    Q8DJZ6   PSBI_THEEB       1     36             
DBREF  5H2F J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5H2F K   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  5H2F L    3    37  UNP    Q8DIN8   PSBL_THEEB       3     37             
DBREF  5H2F O    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  5H2F T    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  5H2F U    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  5H2F V    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  5H2F Y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  5H2F X    2    38  UNP    Q9F1R6   PSBX_THEEB       2     38             
DBREF  5H2F Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  5H2F a   11   344  UNP    P0A444   PSBA1_THEEB     11    344             
DBREF  5H2F b    2   506  UNP    Q8DIQ1   PSBB_THEEB       2    506             
DBREF  5H2F c   19   473  UNP    Q8DIF8   PSBC_THEEB       7    461             
DBREF  5H2F d   11   352  UNP    Q8CM25   PSBD_THEEB      11    352             
DBREF  5H2F e    5    84  UNP    Q8DIP0   PSBE_THEEB       5     84             
DBREF  5H2F f   13    45  UNP    Q8DIN9   PSBF_THEEB      13     45             
DBREF  5H2F h    2    64  UNP    Q8DJ43   PSBH_THEEB       2     64             
DBREF  5H2F i    1    36  UNP    Q8DJZ6   PSBI_THEEB       1     36             
DBREF  5H2F j    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  5H2F k   10    46  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  5H2F l    3    37  UNP    Q8DIN8   PSBL_THEEB       3     37             
DBREF  5H2F o    4   246  UNP    P0A431   PSBO_THEEB      30    272             
DBREF  5H2F t    1    30  UNP    Q8DIQ0   PSBT_THEEB       1     30             
DBREF  5H2F u    8   104  UNP    Q9F1L5   PSBU_THEEB      38    134             
DBREF  5H2F v    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  5H2F y   18    46  UNP    Q8DJI1   YCF12_THEEB     18     46             
DBREF  5H2F x    2    38  UNP    Q9F1R6   PSBX_THEEB       2     38             
DBREF  5H2F z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
SEQRES   1 A  334  ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER          
SEQRES   2 A  334  THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE          
SEQRES   3 A  334  MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL          
SEQRES   4 A  334  ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY          
SEQRES   5 A  334  ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN          
SEQRES   6 A  334  ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA          
SEQRES   7 A  334  ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER          
SEQRES   8 A  334  LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU          
SEQRES   9 A  334  ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET          
SEQRES  10 A  334  GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG          
SEQRES  11 A  334  PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER          
SEQRES  12 A  334  ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY          
SEQRES  13 A  334  SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR          
SEQRES  14 A  334  PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE          
SEQRES  15 A  334  LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL          
SEQRES  16 A  334  PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU          
SEQRES  17 A  334  VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU          
SEQRES  18 A  334  SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU          
SEQRES  19 A  334  THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG          
SEQRES  20 A  334  LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER          
SEQRES  21 A  334  LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL          
SEQRES  22 A  334  TRP PHE THR ALA LEU GLY ILE SER THR MET ALA PHE ASN          
SEQRES  23 A  334  LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA          
SEQRES  24 A  334  LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN          
SEQRES  25 A  334  ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN          
SEQRES  26 A  334  ALA HIS ASN PHE PRO LEU ASP LEU ALA                          
SEQRES   1 B  505  GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN          
SEQRES   2 B  505  ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR          
SEQRES   3 B  505  ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR          
SEQRES   4 B  505  GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN          
SEQRES   5 B  505  PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET          
SEQRES   6 B  505  ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER          
SEQRES   7 B  505  ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER          
SEQRES   8 B  505  PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY          
SEQRES   9 B  505  LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP          
SEQRES  10 B  505  ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO          
SEQRES  11 B  505  ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE          
SEQRES  12 B  505  LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS          
SEQRES  13 B  505  LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP          
SEQRES  14 B  505  PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO          
SEQRES  15 B  505  GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY          
SEQRES  16 B  505  GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY          
SEQRES  17 B  505  ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO          
SEQRES  18 B  505  GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU          
SEQRES  19 B  505  THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA          
SEQRES  20 B  505  ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA          
SEQRES  21 B  505  THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN          
SEQRES  22 B  505  TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG          
SEQRES  23 B  505  VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU          
SEQRES  24 B  505  ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP          
SEQRES  25 B  505  TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG          
SEQRES  26 B  505  THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA          
SEQRES  27 B  505  TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU          
SEQRES  28 B  505  GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER          
SEQRES  29 B  505  PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS          
SEQRES  30 B  505  ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER          
SEQRES  31 B  505  PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY          
SEQRES  32 B  505  GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL          
SEQRES  33 B  505  LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE          
SEQRES  34 B  505  GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE          
SEQRES  35 B  505  ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA          
SEQRES  36 B  505  VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS          
SEQRES  37 B  505  GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE          
SEQRES  38 B  505  ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE          
SEQRES  39 B  505  TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG                  
SEQRES   1 C  455  ASN SER ILE PHE ALA THR ASN ARG ASP GLN GLU SER SER          
SEQRES   2 C  455  GLY PHE ALA TRP TRP ALA GLY ASN ALA ARG LEU ILE ASN          
SEQRES   3 C  455  LEU SER GLY LYS LEU LEU GLY ALA HIS VAL ALA HIS ALA          
SEQRES   4 C  455  GLY LEU ILE VAL PHE TRP ALA GLY ALA MET THR LEU PHE          
SEQRES   5 C  455  GLU LEU ALA HIS PHE ILE PRO GLU LYS PRO MET TYR GLU          
SEQRES   6 C  455  GLN GLY LEU ILE LEU ILE PRO HIS ILE ALA THR LEU GLY          
SEQRES   7 C  455  TRP GLY VAL GLY PRO GLY GLY GLU VAL VAL ASP THR PHE          
SEQRES   8 C  455  PRO PHE PHE VAL VAL GLY VAL VAL HIS LEU ILE SER SER          
SEQRES   9 C  455  ALA VAL LEU GLY PHE GLY GLY VAL TYR HIS ALA ILE ARG          
SEQRES  10 C  455  GLY PRO GLU THR LEU GLU GLU TYR SER SER PHE PHE GLY          
SEQRES  11 C  455  TYR ASP TRP LYS ASP LYS ASN LYS MET THR THR ILE LEU          
SEQRES  12 C  455  GLY PHE HIS LEU ILE VAL LEU GLY ILE GLY ALA LEU LEU          
SEQRES  13 C  455  LEU VAL ALA LYS ALA MET PHE PHE GLY GLY LEU TYR ASP          
SEQRES  14 C  455  THR TRP ALA PRO GLY GLY GLY ASP VAL ARG VAL ILE THR          
SEQRES  15 C  455  ASN PRO THR LEU ASP PRO ARG VAL ILE PHE GLY TYR LEU          
SEQRES  16 C  455  LEU LYS SER PRO PHE GLY GLY GLU GLY TRP ILE VAL SER          
SEQRES  17 C  455  VAL ASN ASN LEU GLU ASP VAL VAL GLY GLY HIS ILE TRP          
SEQRES  18 C  455  ILE GLY LEU ILE CYS ILE ALA GLY GLY ILE TRP HIS ILE          
SEQRES  19 C  455  LEU THR THR PRO PHE GLY TRP ALA ARG ARG ALA PHE ILE          
SEQRES  20 C  455  TRP SER GLY GLU ALA TYR LEU SER TYR SER LEU GLY ALA          
SEQRES  21 C  455  LEU SER MET MET GLY PHE ILE ALA THR CYS PHE VAL TRP          
SEQRES  22 C  455  PHE ASN ASN THR VAL TYR PRO SER GLU PHE TYR GLY PRO          
SEQRES  23 C  455  THR GLY PRO GLU ALA SER GLN ALA GLN ALA MET THR PHE          
SEQRES  24 C  455  LEU ILE ARG ASP GLN LYS LEU GLY ALA ASN VAL GLY SER          
SEQRES  25 C  455  ALA GLN GLY PRO THR GLY LEU GLY LYS TYR LEU MET ARG          
SEQRES  26 C  455  SER PRO THR GLY GLU ILE ILE PHE GLY GLY GLU THR MET          
SEQRES  27 C  455  ARG PHE TRP ASP PHE ARG GLY PRO TRP LEU GLU PRO LEU          
SEQRES  28 C  455  ARG GLY PRO ASN GLY LEU ASP LEU ASN LYS ILE LYS ASN          
SEQRES  29 C  455  ASP ILE GLN PRO TRP GLN GLU ARG ARG ALA ALA GLU TYR          
SEQRES  30 C  455  MET THR HIS ALA PRO LEU GLY SER LEU ASN SER VAL GLY          
SEQRES  31 C  455  GLY VAL ALA THR GLU ILE ASN SER VAL ASN PHE VAL SER          
SEQRES  32 C  455  PRO ARG SER TRP LEU ALA THR SER HIS PHE VAL LEU ALA          
SEQRES  33 C  455  PHE PHE PHE LEU VAL GLY HIS LEU TRP HIS ALA GLY ARG          
SEQRES  34 C  455  ALA ARG ALA ALA ALA ALA GLY PHE GLU LYS GLY ILE ASP          
SEQRES  35 C  455  ARG GLU SER GLU PRO VAL LEU SER MET PRO SER LEU ASP          
SEQRES   1 D  342  GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS          
SEQRES   2 D  342  ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU          
SEQRES   3 D  342  LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU          
SEQRES   4 D  342  THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY          
SEQRES   5 D  342  LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR          
SEQRES   6 D  342  VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER          
SEQRES   7 D  342  LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE          
SEQRES   8 D  342  THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE          
SEQRES   9 D  342  ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU          
SEQRES  10 D  342  ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO          
SEQRES  11 D  342  TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE          
SEQRES  12 D  342  VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER          
SEQRES  13 D  342  TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE          
SEQRES  14 D  342  ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR          
SEQRES  15 D  342  LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU          
SEQRES  16 D  342  GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL          
SEQRES  17 D  342  GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR          
SEQRES  18 D  342  PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR          
SEQRES  19 D  342  SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE          
SEQRES  20 D  342  GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE          
SEQRES  21 D  342  MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA          
SEQRES  22 D  342  ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR          
SEQRES  23 D  342  ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO          
SEQRES  24 D  342  GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN          
SEQRES  25 D  342  GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO          
SEQRES  26 D  342  HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG          
SEQRES  27 D  342  GLY ASN ALA LEU                                              
SEQRES   1 E   80  THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER VAL          
SEQRES   2 E   80  ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA LEU          
SEQRES   3 E   80  PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU ALA          
SEQRES   4 E   80  TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR TYR          
SEQRES   5 E   80  ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP ARG          
SEQRES   6 E   80  PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU GLN          
SEQRES   7 E   80  LEU LYS                                                      
SEQRES   1 F   33  TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR          
SEQRES   2 F   33  LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA          
SEQRES   3 F   33  ALA MET GLN PHE ILE GLN ARG                                  
SEQRES   1 H   63  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 H   63  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 H   63  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 H   63  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 H   63  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA                  
SEQRES   1 I   36  FME GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 I   36  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 I   36  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP                      
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   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 K   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 K   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 L   35  PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN ARG THR          
SEQRES   2 L   35  SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL LEU ALA          
SEQRES   3 L   35  LEU LEU PHE SER SER TYR PHE PHE ASN                          
SEQRES   1 O  243  THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA          
SEQRES   2 O  243  ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA          
SEQRES   3 O  243  TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG          
SEQRES   4 O  243  LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU          
SEQRES   5 O  243  PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR          
SEQRES   6 O  243  LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE          
SEQRES   7 O  243  GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR          
SEQRES   8 O  243  PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR          
SEQRES   9 O  243  VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE          
SEQRES  10 O  243  THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL          
SEQRES  11 O  243  THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE          
SEQRES  12 O  243  ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO          
SEQRES  13 O  243  LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE          
SEQRES  14 O  243  ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA          
SEQRES  15 O  243  ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER          
SEQRES  16 O  243  LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE          
SEQRES  17 O  243  ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP          
SEQRES  18 O  243  MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY          
SEQRES  19 O  243  VAL PHE TYR ALA SER ILE GLU PRO ALA                          
SEQRES   1 T   30  FME GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   30  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   30  PRO ARG ILE THR                                              
SEQRES   1 U   97  GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA          
SEQRES   2 U   97  TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA          
SEQRES   3 U   97  ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA          
SEQRES   4 U   97  LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU          
SEQRES   5 U   97  ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS          
SEQRES   6 U   97  GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR          
SEQRES   7 U   97  GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR          
SEQRES   8 U   97  ASN ASN GLY LEU TYR LYS                                      
SEQRES   1 V  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 V  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 V  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 V  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 V  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 V  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 V  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 V  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 V  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 V  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 V  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 Y   29  VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE          
SEQRES   2 Y   29  ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG          
SEQRES   3 Y   29  GLY ASN LEU                                                  
SEQRES   1 X   37  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 X   37  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 X   37  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN                  
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 a  334  ALA ASN LEU TRP GLU ARG PHE CYS ASN TRP VAL THR SER          
SEQRES   2 a  334  THR ASP ASN ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE          
SEQRES   3 a  334  MET ILE PRO THR LEU LEU ALA ALA THR ILE CYS PHE VAL          
SEQRES   4 a  334  ILE ALA PHE ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY          
SEQRES   5 a  334  ILE ARG GLU PRO VAL SER GLY SER LEU LEU TYR GLY ASN          
SEQRES   6 a  334  ASN ILE ILE THR GLY ALA VAL VAL PRO SER SER ASN ALA          
SEQRES   7 a  334  ILE GLY LEU HIS PHE TYR PRO ILE TRP GLU ALA ALA SER          
SEQRES   8 a  334  LEU ASP GLU TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU          
SEQRES   9 a  334  ILE ILE PHE HIS PHE LEU LEU GLY ALA SER CYS TYR MET          
SEQRES  10 a  334  GLY ARG GLN TRP GLU LEU SER TYR ARG LEU GLY MET ARG          
SEQRES  11 a  334  PRO TRP ILE CYS VAL ALA TYR SER ALA PRO LEU ALA SER          
SEQRES  12 a  334  ALA PHE ALA VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY          
SEQRES  13 a  334  SER PHE SER ASP GLY MET PRO LEU GLY ILE SER GLY THR          
SEQRES  14 a  334  PHE ASN PHE MET ILE VAL PHE GLN ALA GLU HIS ASN ILE          
SEQRES  15 a  334  LEU MET HIS PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL          
SEQRES  16 a  334  PHE GLY GLY ALA LEU PHE CYS ALA MET HIS GLY SER LEU          
SEQRES  17 a  334  VAL THR SER SER LEU ILE ARG GLU THR THR GLU THR GLU          
SEQRES  18 a  334  SER ALA ASN TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU          
SEQRES  19 a  334  THR TYR ASN ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG          
SEQRES  20 a  334  LEU ILE PHE GLN TYR ALA SER PHE ASN ASN SER ARG SER          
SEQRES  21 a  334  LEU HIS PHE PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL          
SEQRES  22 a  334  TRP PHE THR ALA LEU GLY ILE SER THR MET ALA PHE ASN          
SEQRES  23 a  334  LEU ASN GLY PHE ASN PHE ASN HIS SER VAL ILE ASP ALA          
SEQRES  24 a  334  LYS GLY ASN VAL ILE ASN THR TRP ALA ASP ILE ILE ASN          
SEQRES  25 a  334  ARG ALA ASN LEU GLY MET GLU VAL MET HIS GLU ARG ASN          
SEQRES  26 a  334  ALA HIS ASN PHE PRO LEU ASP LEU ALA                          
SEQRES   1 b  505  GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE ASN          
SEQRES   2 b  505  ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS THR          
SEQRES   3 b  505  ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU TYR          
SEQRES   4 b  505  GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU ASN          
SEQRES   5 b  505  PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE MET          
SEQRES   6 b  505  ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP SER          
SEQRES   7 b  505  ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP SER          
SEQRES   8 b  505  PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER GLY          
SEQRES   9 b  505  LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR TRP          
SEQRES  10 b  505  ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU PRO          
SEQRES  11 b  505  ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU PHE          
SEQRES  12 b  505  LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE HIS          
SEQRES  13 b  505  LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER ASP          
SEQRES  14 b  505  PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA PRO          
SEQRES  15 b  505  GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO GLY          
SEQRES  16 b  505  GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL GLY          
SEQRES  17 b  505  ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO PRO          
SEQRES  18 b  505  GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE GLU          
SEQRES  19 b  505  THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE ALA          
SEQRES  20 b  505  ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER ALA          
SEQRES  21 b  505  THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR GLN          
SEQRES  22 b  505  TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG ARG          
SEQRES  23 b  505  VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU GLU          
SEQRES  24 b  505  ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR ASP          
SEQRES  25 b  505  TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE ARG          
SEQRES  26 b  505  THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN ALA          
SEQRES  27 b  505  TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY GLU          
SEQRES  28 b  505  GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU SER          
SEQRES  29 b  505  PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL LYS          
SEQRES  30 b  505  ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR SER          
SEQRES  31 b  505  PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY GLY          
SEQRES  32 b  505  GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR VAL          
SEQRES  33 b  505  LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE PHE          
SEQRES  34 b  505  GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE PHE          
SEQRES  35 b  505  ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS ALA          
SEQRES  36 b  505  VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP HIS          
SEQRES  37 b  505  GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY ILE          
SEQRES  38 b  505  ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY PHE          
SEQRES  39 b  505  TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG                  
SEQRES   1 c  455  ASN SER ILE PHE ALA THR ASN ARG ASP GLN GLU SER SER          
SEQRES   2 c  455  GLY PHE ALA TRP TRP ALA GLY ASN ALA ARG LEU ILE ASN          
SEQRES   3 c  455  LEU SER GLY LYS LEU LEU GLY ALA HIS VAL ALA HIS ALA          
SEQRES   4 c  455  GLY LEU ILE VAL PHE TRP ALA GLY ALA MET THR LEU PHE          
SEQRES   5 c  455  GLU LEU ALA HIS PHE ILE PRO GLU LYS PRO MET TYR GLU          
SEQRES   6 c  455  GLN GLY LEU ILE LEU ILE PRO HIS ILE ALA THR LEU GLY          
SEQRES   7 c  455  TRP GLY VAL GLY PRO GLY GLY GLU VAL VAL ASP THR PHE          
SEQRES   8 c  455  PRO PHE PHE VAL VAL GLY VAL VAL HIS LEU ILE SER SER          
SEQRES   9 c  455  ALA VAL LEU GLY PHE GLY GLY VAL TYR HIS ALA ILE ARG          
SEQRES  10 c  455  GLY PRO GLU THR LEU GLU GLU TYR SER SER PHE PHE GLY          
SEQRES  11 c  455  TYR ASP TRP LYS ASP LYS ASN LYS MET THR THR ILE LEU          
SEQRES  12 c  455  GLY PHE HIS LEU ILE VAL LEU GLY ILE GLY ALA LEU LEU          
SEQRES  13 c  455  LEU VAL ALA LYS ALA MET PHE PHE GLY GLY LEU TYR ASP          
SEQRES  14 c  455  THR TRP ALA PRO GLY GLY GLY ASP VAL ARG VAL ILE THR          
SEQRES  15 c  455  ASN PRO THR LEU ASP PRO ARG VAL ILE PHE GLY TYR LEU          
SEQRES  16 c  455  LEU LYS SER PRO PHE GLY GLY GLU GLY TRP ILE VAL SER          
SEQRES  17 c  455  VAL ASN ASN LEU GLU ASP VAL VAL GLY GLY HIS ILE TRP          
SEQRES  18 c  455  ILE GLY LEU ILE CYS ILE ALA GLY GLY ILE TRP HIS ILE          
SEQRES  19 c  455  LEU THR THR PRO PHE GLY TRP ALA ARG ARG ALA PHE ILE          
SEQRES  20 c  455  TRP SER GLY GLU ALA TYR LEU SER TYR SER LEU GLY ALA          
SEQRES  21 c  455  LEU SER MET MET GLY PHE ILE ALA THR CYS PHE VAL TRP          
SEQRES  22 c  455  PHE ASN ASN THR VAL TYR PRO SER GLU PHE TYR GLY PRO          
SEQRES  23 c  455  THR GLY PRO GLU ALA SER GLN ALA GLN ALA MET THR PHE          
SEQRES  24 c  455  LEU ILE ARG ASP GLN LYS LEU GLY ALA ASN VAL GLY SER          
SEQRES  25 c  455  ALA GLN GLY PRO THR GLY LEU GLY LYS TYR LEU MET ARG          
SEQRES  26 c  455  SER PRO THR GLY GLU ILE ILE PHE GLY GLY GLU THR MET          
SEQRES  27 c  455  ARG PHE TRP ASP PHE ARG GLY PRO TRP LEU GLU PRO LEU          
SEQRES  28 c  455  ARG GLY PRO ASN GLY LEU ASP LEU ASN LYS ILE LYS ASN          
SEQRES  29 c  455  ASP ILE GLN PRO TRP GLN GLU ARG ARG ALA ALA GLU TYR          
SEQRES  30 c  455  MET THR HIS ALA PRO LEU GLY SER LEU ASN SER VAL GLY          
SEQRES  31 c  455  GLY VAL ALA THR GLU ILE ASN SER VAL ASN PHE VAL SER          
SEQRES  32 c  455  PRO ARG SER TRP LEU ALA THR SER HIS PHE VAL LEU ALA          
SEQRES  33 c  455  PHE PHE PHE LEU VAL GLY HIS LEU TRP HIS ALA GLY ARG          
SEQRES  34 c  455  ALA ARG ALA ALA ALA ALA GLY PHE GLU LYS GLY ILE ASP          
SEQRES  35 c  455  ARG GLU SER GLU PRO VAL LEU SER MET PRO SER LEU ASP          
SEQRES   1 d  342  GLU ARG GLY TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS          
SEQRES   2 d  342  ARG ASP ARG PHE VAL PHE VAL GLY TRP SER GLY ILE LEU          
SEQRES   3 d  342  LEU PHE PRO CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU          
SEQRES   4 d  342  THR GLY THR THR PHE VAL THR SER TRP TYR THR HIS GLY          
SEQRES   5 d  342  LEU ALA SER SER TYR LEU GLU GLY CYS ASN PHE LEU THR          
SEQRES   6 d  342  VAL ALA VAL SER THR PRO ALA ASN SER MET GLY HIS SER          
SEQRES   7 d  342  LEU LEU LEU LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE          
SEQRES   8 d  342  THR ARG TRP CYS GLN LEU GLY GLY LEU TRP THR PHE ILE          
SEQRES   9 d  342  ALA LEU HIS GLY ALA PHE GLY LEU ILE GLY PHE MET LEU          
SEQRES  10 d  342  ARG GLN PHE GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO          
SEQRES  11 d  342  TYR ASN ALA ILE ALA PHE SER ALA PRO ILE ALA VAL PHE          
SEQRES  12 d  342  VAL SER VAL PHE LEU ILE TYR PRO LEU GLY GLN SER SER          
SEQRES  13 d  342  TRP PHE PHE ALA PRO SER PHE GLY VAL ALA ALA ILE PHE          
SEQRES  14 d  342  ARG PHE LEU LEU PHE PHE GLN GLY PHE HIS ASN TRP THR          
SEQRES  15 d  342  LEU ASN PRO PHE HIS MET MET GLY VAL ALA GLY VAL LEU          
SEQRES  16 d  342  GLY GLY ALA LEU LEU CYS ALA ILE HIS GLY ALA THR VAL          
SEQRES  17 d  342  GLU ASN THR LEU PHE GLN ASP GLY GLU GLY ALA SER THR          
SEQRES  18 d  342  PHE ARG ALA PHE ASN PRO THR GLN ALA GLU GLU THR TYR          
SEQRES  19 d  342  SER MET VAL THR ALA ASN ARG PHE TRP SER GLN ILE PHE          
SEQRES  20 d  342  GLY ILE ALA PHE SER ASN LYS ARG TRP LEU HIS PHE PHE          
SEQRES  21 d  342  MET LEU PHE VAL PRO VAL THR GLY LEU TRP MET SER ALA          
SEQRES  22 d  342  ILE GLY VAL VAL GLY LEU ALA LEU ASN LEU ARG SER TYR          
SEQRES  23 d  342  ASP PHE ILE SER GLN GLU ILE ARG ALA ALA GLU ASP PRO          
SEQRES  24 d  342  GLU PHE GLU THR PHE TYR THR LYS ASN LEU LEU LEU ASN          
SEQRES  25 d  342  GLU GLY ILE ARG ALA TRP MET ALA PRO GLN ASP GLN PRO          
SEQRES  26 d  342  HIS GLU ASN PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG          
SEQRES  27 d  342  GLY ASN ALA LEU                                              
SEQRES   1 e   80  THR GLY GLU ARG PRO PHE SER ASP ILE ILE THR SER VAL          
SEQRES   2 e   80  ARG TYR TRP VAL ILE HIS SER ILE THR ILE PRO ALA LEU          
SEQRES   3 e   80  PHE ILE ALA GLY TRP LEU PHE VAL SER THR GLY LEU ALA          
SEQRES   4 e   80  TYR ASP VAL PHE GLY THR PRO ARG PRO ASP SER TYR TYR          
SEQRES   5 e   80  ALA GLN GLU GLN ARG SER ILE PRO LEU VAL THR ASP ARG          
SEQRES   6 e   80  PHE GLU ALA LYS GLN GLN VAL GLU THR PHE LEU GLU GLN          
SEQRES   7 e   80  LEU LYS                                                      
SEQRES   1 f   33  TYR PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR          
SEQRES   2 f   33  LEU ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA          
SEQRES   3 f   33  ALA MET GLN PHE ILE GLN ARG                                  
SEQRES   1 h   63  ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO LEU          
SEQRES   2 h   63  ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY THR          
SEQRES   3 h   63  THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU VAL          
SEQRES   4 h   63  PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR LEU          
SEQRES   5 h   63  ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA                  
SEQRES   1 i   36  FME GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 i   36  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 i   36  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP                      
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   37  LYS LEU PRO GLU ALA TYR ALA ILE PHE ASP PRO LEU VAL          
SEQRES   2 k   37  ASP VAL LEU PRO VAL ILE PRO VAL LEU PHE LEU ALA LEU          
SEQRES   3 k   37  ALA PHE VAL TRP GLN ALA ALA VAL GLY PHE ARG                  
SEQRES   1 l   35  PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN ARG THR          
SEQRES   2 l   35  SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL LEU ALA          
SEQRES   3 l   35  LEU LEU PHE SER SER TYR PHE PHE ASN                          
SEQRES   1 o  243  THR LEU THR TYR ASP ASP ILE VAL GLY THR GLY LEU ALA          
SEQRES   2 o  243  ASN LYS CYS PRO THR LEU ASP ASP THR ALA ARG GLY ALA          
SEQRES   3 o  243  TYR PRO ILE ASP SER SER GLN THR TYR ARG ILE ALA ARG          
SEQRES   4 o  243  LEU CYS LEU GLN PRO THR THR PHE LEU VAL LYS GLU GLU          
SEQRES   5 o  243  PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE VAL PRO THR          
SEQRES   6 o  243  LYS LEU VAL THR ARG GLU THR THR SER LEU ASP GLN ILE          
SEQRES   7 o  243  GLN GLY GLU LEU LYS VAL ASN SER ASP GLY SER LEU THR          
SEQRES   8 o  243  PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN PRO VAL THR          
SEQRES   9 o  243  VAL GLN MET ALA GLY GLY GLU ARG ILE PRO LEU LEU PHE          
SEQRES  10 o  243  THR VAL LYS ASN LEU VAL ALA SER THR GLN PRO ASN VAL          
SEQRES  11 o  243  THR SER ILE THR THR SER THR ASP PHE LYS GLY GLU PHE          
SEQRES  12 o  243  ASN VAL PRO SER TYR ARG THR ALA ASN PHE LEU ASP PRO          
SEQRES  13 o  243  LYS GLY ARG GLY LEU ALA SER GLY TYR ASP SER ALA ILE          
SEQRES  14 o  243  ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU ALA ARG ALA          
SEQRES  15 o  243  ASN VAL LYS ARG PHE SER LEU THR LYS GLY GLN ILE SER          
SEQRES  16 o  243  LEU ASN VAL ALA LYS VAL ASP GLY ARG THR GLY GLU ILE          
SEQRES  17 o  243  ALA GLY THR PHE GLU SER GLU GLN LEU SER ASP ASP ASP          
SEQRES  18 o  243  MET GLY ALA HIS GLU PRO HIS GLU VAL LYS ILE GLN GLY          
SEQRES  19 o  243  VAL PHE TYR ALA SER ILE GLU PRO ALA                          
SEQRES   1 t   30  FME GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 t   30  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 t   30  PRO ARG ILE THR                                              
SEQRES   1 u   97  GLU LEU VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA          
SEQRES   2 u   97  TYR GLY GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA          
SEQRES   3 u   97  ALA PHE ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA          
SEQRES   4 u   97  LYS LEU ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU          
SEQRES   5 u   97  ASP VAL LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS          
SEQRES   6 u   97  GLN ILE LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR          
SEQRES   7 u   97  GLU VAL GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR          
SEQRES   8 u   97  ASN ASN GLY LEU TYR LYS                                      
SEQRES   1 v  137  ALA GLU LEU THR PRO GLU VAL LEU THR VAL PRO LEU ASN          
SEQRES   2 v  137  SER GLU GLY LYS THR ILE THR LEU THR GLU LYS GLN TYR          
SEQRES   3 v  137  LEU GLU GLY LYS ARG LEU PHE GLN TYR ALA CYS ALA SER          
SEQRES   4 v  137  CYS HIS VAL GLY GLY ILE THR LYS THR ASN PRO SER LEU          
SEQRES   5 v  137  ASP LEU ARG THR GLU THR LEU ALA LEU ALA THR PRO PRO          
SEQRES   6 v  137  ARG ASP ASN ILE GLU GLY LEU VAL ASP TYR MET LYS ASN          
SEQRES   7 v  137  PRO THR THR TYR ASP GLY GLU GLN GLU ILE ALA GLU VAL          
SEQRES   8 v  137  HIS PRO SER LEU ARG SER ALA ASP ILE PHE PRO LYS MET          
SEQRES   9 v  137  ARG ASN LEU THR GLU LYS ASP LEU VAL ALA ILE ALA GLY          
SEQRES  10 v  137  HIS ILE LEU VAL GLU PRO LYS ILE LEU GLY ASP LYS TRP          
SEQRES  11 v  137  GLY GLY GLY LYS VAL TYR TYR                                  
SEQRES   1 y   29  VAL ILE ALA GLN LEU THR MET ILE ALA MET ILE GLY ILE          
SEQRES   2 y   29  ALA GLY PRO MET ILE ILE PHE LEU LEU ALA VAL ARG ARG          
SEQRES   3 y   29  GLY ASN LEU                                                  
SEQRES   1 x   37  THR ILE THR PRO SER LEU LYS GLY PHE PHE ILE GLY LEU          
SEQRES   2 x   37  LEU SER GLY ALA VAL VAL LEU GLY LEU THR PHE ALA VAL          
SEQRES   3 x   37  LEU ILE ALA ILE SER GLN ILE ASP LYS VAL GLN                  
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                      
MODRES 5H2F FME I    1  MET  MODIFIED RESIDUE                                   
MODRES 5H2F FME T    1  MET  MODIFIED RESIDUE                                   
MODRES 5H2F FME i    1  MET  MODIFIED RESIDUE                                   
MODRES 5H2F FME t    1  MET  MODIFIED RESIDUE                                   
HET    FME  I   1      10                                                       
HET    FME  T   1      10                                                       
HET    FME  i   1      10                                                       
HET    FME  t   1      10                                                       
HET    OEX  A 401      10                                                       
HET    FE2  A 402       1                                                       
HET     CL  A 403       1                                                       
HET     CL  A 404       1                                                       
HET    CLA  A 405      65                                                       
HET    CLA  A 406      55                                                       
HET    PHO  A 407      64                                                       
HET    CLA  A 408      65                                                       
HET    BCR  A 409      40                                                       
HET    LMG  A 410      51                                                       
HET    PL9  A 411      55                                                       
HET    LHG  A 412      31                                                       
HET    SQD  A 413      49                                                       
HET    LMT  A 414      35                                                       
HET    UNL  A 415       5                                                       
HET    DMS  A 416       4                                                       
HET    DMS  A 417       4                                                       
HET    DMS  A 418       4                                                       
HET    DMS  A 419       4                                                       
HET    DMS  A 420       4                                                       
HET    BCT  A 421       8                                                       
HET     CA  B 601       1                                                       
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      61                                                       
HET    CLA  B 615      53                                                       
HET    CLA  B 616      65                                                       
HET    CLA  B 617      55                                                       
HET    BCR  B 618      19                                                       
HET    BCR  B 619      30                                                       
HET    BCR  B 620      40                                                       
HET    LMG  B 621      40                                                       
HET    LMT  B 622      24                                                       
HET    HTG  B 623      19                                                       
HET    UNL  B 624       7                                                       
HET    UNL  B 625      16                                                       
HET    HTG  B 626      19                                                       
HET    HTG  B 627      19                                                       
HET    DMS  B 628       4                                                       
HET    DMS  B 629       4                                                       
HET    DMS  B 630       4                                                       
HET    DMS  B 631       4                                                       
HET    DMS  B 632       4                                                       
HET    DMS  B 633       4                                                       
HET    DMS  B 634       4                                                       
HET    DMS  B 635       4                                                       
HET    DMS  B 636       4                                                       
HET    DMS  B 637       4                                                       
HET    DMS  B 638       4                                                       
HET    DMS  B 639       4                                                       
HET    DMS  B 640       4                                                       
HET    DMS  B 641       4                                                       
HET    DMS  B 642       4                                                       
HET    SQD  C 501      54                                                       
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      56                                                       
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      51                                                       
HET    HTG  C 521      19                                                       
HET    LHG  C 522      30                                                       
HET    HTG  C 523       9                                                       
HET    DMS  C 524       4                                                       
HET    DMS  C 525       4                                                       
HET    DMS  C 526       4                                                       
HET    DMS  C 527       4                                                       
HET    DMS  C 528       4                                                       
HET    DMS  C 529       4                                                       
HET    DMS  C 530       4                                                       
HET    LMG  C 531      40                                                       
HET    HTG  C 532      19                                                       
HET    DMS  C 533       4                                                       
HET    DMS  C 534       4                                                       
HET    DMS  C 535       4                                                       
HET    DMS  C 536       4                                                       
HET    DMS  C 537       4                                                       
HET    DMS  C 538       4                                                       
HET    DMS  C 539       4                                                       
HET    DMS  C 540       4                                                       
HET    CLA  D 401      65                                                       
HET    PHO  D 402      64                                                       
HET    CLA  D 403      65                                                       
HET    CLA  D 404      65                                                       
HET    BCR  D 405      40                                                       
HET    PL9  D 406      55                                                       
HET    DGD  D 407      50                                                       
HET    SQD  D 408      20                                                       
HET    LHG  D 409      49                                                       
HET    LHG  D 410      49                                                       
HET    LHG  D 411      45                                                       
HET    LMG  D 412      46                                                       
HET    UNL  D 413      16                                                       
HET    HTG  D 414      19                                                       
HET    HTG  D 415      19                                                       
HET    DMS  D 416       4                                                       
HET    DMS  D 417       4                                                       
HET    DMS  D 418       4                                                       
HET    LMT  E 101      24                                                       
HET    HEM  E 102      43                                                       
HET    DMS  F 101       4                                                       
HET    RRX  H 101      41                                                       
HET    DGD  H 102      62                                                       
HET    DMS  H 103       4                                                       
HET    DMS  I 101       4                                                       
HET    LMT  I 102      35                                                       
HET    UNL  I 103      13                                                       
HET    UNL  I 104      16                                                       
HET    UNL  I 105      16                                                       
HET    DMS  I 106       4                                                       
HET    LMG  J 101      45                                                       
HET     MG  J 102       1                                                       
HET    UNL  J 103      16                                                       
HET    BCR  K 101      40                                                       
HET     MG  K 102       1                                                       
HET    LHG  L 101      40                                                       
HET    DMS  L 102       4                                                       
HET    UNL  O 301      16                                                       
HET     CA  O 302       1                                                       
HET    DMS  O 303       4                                                       
HET    DMS  O 304       4                                                       
HET    DMS  O 305       4                                                       
HET    DMS  O 306       4                                                       
HET    DMS  O 307       4                                                       
HET    DMS  O 308       4                                                       
HET    DMS  O 309       4                                                       
HET    DMS  O 310       4                                                       
HET    DMS  O 311       4                                                       
HET    DMS  O 312       4                                                       
HET    DMS  O 313       4                                                       
HET    DMS  O 314       4                                                       
HET    UNL  T 101      13                                                       
HET    LMT  T 102      24                                                       
HET    UNL  U 201      14                                                       
HET    DMS  U 202       4                                                       
HET    DMS  U 203       4                                                       
HET    DMS  V 201       4                                                       
HET    HEC  V 202      43                                                       
HET    HTG  V 203      14                                                       
HET    DMS  V 204       4                                                       
HET    DMS  V 205       4                                                       
HET    DMS  V 206       4                                                       
HET    DMS  V 207       4                                                       
HET    DMS  V 208       4                                                       
HET    DMS  V 209       4                                                       
HET    DMS  V 210       4                                                       
HET    DMS  V 211       4                                                       
HET    DMS  V 212       4                                                       
HET    BCR  Y 101      39                                                       
HET    UNL  X 101      16                                                       
HET    LMT  Z 101      35                                                       
HET    UNL  Z 102       9                                                       
HET    DMS  a 401       4                                                       
HET    DMS  a 402       4                                                       
HET    OEX  a 403      10                                                       
HET    FE2  a 404       1                                                       
HET     CL  a 405       1                                                       
HET     CL  a 406       1                                                       
HET    CLA  a 407      65                                                       
HET    CLA  a 408      65                                                       
HET    CLA  a 409      61                                                       
HET    PHO  a 410      64                                                       
HET    PHO  a 411      64                                                       
HET    CLA  a 412      65                                                       
HET    BCR  a 413      40                                                       
HET    SQD  a 414      54                                                       
HET    PL9  a 415      55                                                       
HET    LHG  a 416      49                                                       
HET    UNL  a 417      10                                                       
HET    SQD  a 418      51                                                       
HET    LMT  a 419      35                                                       
HET    UNL  a 420       6                                                       
HET    DMS  a 421       4                                                       
HET    BCT  a 422       4                                                       
HET    LHG  a 423      45                                                       
HET    DMS  a 424       4                                                       
HET    DMS  a 425       4                                                       
HET     CA  b 601       1                                                       
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      59                                                       
HET    CLA  b 615      52                                                       
HET    CLA  b 616      65                                                       
HET    CLA  b 617      60                                                       
HET    BCR  b 618      20                                                       
HET    BCR  b 619      31                                                       
HET    BCR  b 620      40                                                       
HET    SQD  b 621      38                                                       
HET    LMG  b 622      43                                                       
HET    HTG  b 623      19                                                       
HET    HTG  b 624      19                                                       
HET    UNL  b 625      16                                                       
HET    HTG  b 626      19                                                       
HET    HTG  b 627      19                                                       
HET    UNL  b 628      11                                                       
HET    DMS  b 629       4                                                       
HET    DMS  b 630       4                                                       
HET    DMS  b 631       4                                                       
HET    HTG  b 632      19                                                       
HET    DMS  b 633       4                                                       
HET    DMS  b 634       4                                                       
HET    DMS  b 635       4                                                       
HET    DMS  b 636       4                                                       
HET    DMS  b 637       4                                                       
HET    DMS  b 638       4                                                       
HET     CA  c 901       1                                                       
HET    CLA  c 902      65                                                       
HET    CLA  c 903      65                                                       
HET    CLA  c 904      65                                                       
HET    CLA  c 905      65                                                       
HET    CLA  c 906      65                                                       
HET    CLA  c 907      65                                                       
HET    CLA  c 908      65                                                       
HET    CLA  c 909      65                                                       
HET    CLA  c 910      65                                                       
HET    CLA  c 911      65                                                       
HET    CLA  c 912      65                                                       
HET    CLA  c 913      65                                                       
HET    CLA  c 914      65                                                       
HET    BCR  c 915      40                                                       
HET    BCR  c 916      40                                                       
HET    DGD  c 917      62                                                       
HET    DGD  c 918      62                                                       
HET    DGD  c 919      62                                                       
HET    LMG  c 920      51                                                       
HET    LMT  c 921      35                                                       
HET    HTG  c 922      19                                                       
HET    DMS  c 923       4                                                       
HET    DMS  c 924       4                                                       
HET    DMS  c 925       4                                                       
HET    DMS  c 926       4                                                       
HET    DMS  c 927       4                                                       
HET    DMS  c 928       4                                                       
HET    DMS  c 929       4                                                       
HET    LMG  c 930      49                                                       
HET    LMT  c 931      24                                                       
HET    UNL  c 932      10                                                       
HET    DMS  c 933       4                                                       
HET    DMS  c 934       4                                                       
HET    DMS  c 935       4                                                       
HET    DMS  c 936       4                                                       
HET    DMS  c 937       4                                                       
HET    DMS  c 938       4                                                       
HET    DMS  c 939       4                                                       
HET    DMS  c 940       4                                                       
HET    DMS  c 941       4                                                       
HET    DMS  c 942       4                                                       
HET    DMS  c 943       4                                                       
HET    DMS  c 944       4                                                       
HET    LHG  d 401      33                                                       
HET    CLA  d 402      65                                                       
HET    CLA  d 403      65                                                       
HET    BCR  d 404      40                                                       
HET    PL9  d 405      55                                                       
HET    DGD  d 406      43                                                       
HET    LHG  d 407      49                                                       
HET    LHG  d 408      46                                                       
HET    LMG  d 409      47                                                       
HET    UNL  d 410      16                                                       
HET    DMS  d 411       4                                                       
HET    DMS  d 412       4                                                       
HET    DMS  d 413       4                                                       
HET    DMS  d 414       4                                                       
HET    DMS  d 415       4                                                       
HET    HEM  e 101      43                                                       
HET    SQD  f 101      14                                                       
HET    LMT  f 102      25                                                       
HET    DMS  f 103       4                                                       
HET    RRX  h 101      41                                                       
HET    DGD  h 102      62                                                       
HET    LMG  i 101      51                                                       
HET    UNL  i 102      16                                                       
HET    UNL  i 103      16                                                       
HET    UNL  i 104      16                                                       
HET    UNL  i 105      10                                                       
HET    DMS  i 106       4                                                       
HET    LMG  j 101      47                                                       
HET     MG  j 102       1                                                       
HET    UNL  j 103      16                                                       
HET    BCR  k 101      40                                                       
HET     MG  k 102       1                                                       
HET    SQD  l 101      54                                                       
HET    LHG  l 102      49                                                       
HET    DMS  l 103       4                                                       
HET    DMS  l 104       4                                                       
HET    DMS  l 105       4                                                       
HET    HTG  l 106      19                                                       
HET     CA  o 301       1                                                       
HET    DMS  o 302       4                                                       
HET    DMS  o 303       4                                                       
HET    DMS  o 304       4                                                       
HET    DMS  o 305       4                                                       
HET    DMS  o 306       4                                                       
HET    DMS  o 307       4                                                       
HET    DMS  o 308       4                                                       
HET    LMT  t 101      24                                                       
HET    UNL  t 102      16                                                       
HET    DMS  t 103       4                                                       
HET    DMS  t 104       4                                                       
HET    DMS  t 105       4                                                       
HET    UNL  u 201      11                                                       
HET    DMS  u 202       4                                                       
HET    DMS  u 203       4                                                       
HET    DMS  u 204       4                                                       
HET    DMS  u 205       4                                                       
HET    DMS  v 201       4                                                       
HET    HEC  v 202      43                                                       
HET    HTG  v 203      16                                                       
HET    DMS  v 204       4                                                       
HET    DMS  v 205       4                                                       
HET    DMS  v 206       4                                                       
HET    DMS  v 207       4                                                       
HET    DMS  v 208       4                                                       
HET    DMS  v 209       4                                                       
HET    DMS  v 210       4                                                       
HET    DMS  v 211       4                                                       
HET    BCR  y 101      40                                                       
HET    UNL  x 101      15                                                       
HETNAM     FME N-FORMYLMETHIONINE                                               
HETNAM     OEX CA-MN4-O5 CLUSTER                                                
HETNAM     FE2 FE (II) ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     LMG 1,2-DISTEAROYL-MONOGALACTOSYL-DIGLYCERIDE                        
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     LHG 1,2-DIPALMITOYL-PHOSPHATIDYL-GLYCEROLE                           
HETNAM     SQD 1,2-DI-O-ACYL-3-O-[6-DEOXY-6-SULFO-ALPHA-D-                      
HETNAM   2 SQD  GLUCOPYRANOSYL]-SN-GLYCEROL                                     
HETNAM     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM     UNL UNKNOWN LIGAND                                                   
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     BCT BICARBONATE ION                                                  
HETNAM      CA CALCIUM ION                                                      
HETNAM     HTG HEPTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE                             
HETNAM     DGD DIGALACTOSYL DIACYL GLYCEROL (DGDG)                              
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     RRX (3R)-BETA,BETA-CAROTEN-3-OL                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     HEC HEME C                                                           
HETSYN     PL9 PLASTOQUINONE 9                                                  
HETSYN     SQD SULFOQUINOVOSYLDIACYLGLYCEROL                                    
HETSYN     HEM HEME                                                             
HETSYN     RRX BETA-CRYPTOXANTHIN                                               
FORMUL   8  FME    4(C6 H11 N O3 S)                                             
FORMUL  37  OEX    2(CA MN4 O5)                                                 
FORMUL  38  FE2    2(FE 2+)                                                     
FORMUL  39   CL    4(CL 1-)                                                     
FORMUL  41  CLA    70(C55 H72 MG N4 O5 2+)                                      
FORMUL  43  PHO    4(C55 H74 N4 O5)                                             
FORMUL  45  BCR    18(C40 H56)                                                  
FORMUL  46  LMG    12(C45 H86 O10)                                              
FORMUL  47  PL9    4(C53 H80 O2)                                                
FORMUL  48  LHG    12(C38 H75 O10 P)                                            
FORMUL  49  SQD    8(C41 H78 O12 S)                                             
FORMUL  50  LMT    11(C24 H46 O11)                                              
FORMUL  52  DMS    133(C2 H6 O S)                                               
FORMUL  57  BCT    2(C H O3 1-)                                                 
FORMUL  58   CA    5(CA 2+)                                                     
FORMUL  80  HTG    17(C13 H26 O5 S)                                             
FORMUL  16  DGD    10(C51 H96 O15)                                              
FORMUL  59  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL  61  RRX    2(C40 H56 O)                                                 
FORMUL  71   MG    4(MG 2+)                                                     
FORMUL  97  HEC    2(C34 H34 FE N4 O4)                                          
FORMUL  88  HOH   *2317(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 PRO A   95  ALA A   99  5                                   5    
HELIX    4 AA4 SER A  101  ASN A  108  1                                   8    
HELIX    5 AA5 GLY A  109  LEU A  137  1                                  29    
HELIX    6 AA6 TRP A  142  LEU A  159  1                                  18    
HELIX    7 AA7 LEU A  159  GLY A  166  1                                   8    
HELIX    8 AA8 SER A  167  GLY A  171  5                                   5    
HELIX    9 AA9 ILE A  176  ASN A  191  1                                  16    
HELIX   10 AB1 ILE A  192  MET A  194  5                                   3    
HELIX   11 AB2 HIS A  195  SER A  222  1                                  28    
HELIX   12 AB3 SER A  232  TYR A  237  5                                   6    
HELIX   13 AB4 ASN A  247  ILE A  259  1                                  13    
HELIX   14 AB5 PHE A  260  SER A  264  5                                   5    
HELIX   15 AB6 ASN A  267  ALA A  294  1                                  28    
HELIX   16 AB7 THR A  316  HIS A  332  1                                  17    
HELIX   17 AB8 TYR B    6  ILE B   13  5                                   8    
HELIX   18 AB9 ASP B   15  PHE B   45  1                                  31    
HELIX   19 AC1 PRO B   54  GLN B   58  5                                   5    
HELIX   20 AC2 VAL B   62  LEU B   69  1                                   8    
HELIX   21 AC3 SER B   92  TYR B  117  1                                  26    
HELIX   22 AC4 LEU B  120  ARG B  124  5                                   5    
HELIX   23 AC5 ASP B  134  PHE B  156  1                                  23    
HELIX   24 AC6 GLY B  186  ASN B  191  5                                   6    
HELIX   25 AC7 ASN B  194  VAL B  219  1                                  26    
HELIX   26 AC8 PRO B  222  LEU B  229  1                                   8    
HELIX   27 AC9 ASN B  233  GLY B  259  1                                  27    
HELIX   28 AD1 PRO B  264  GLY B  269  1                                   6    
HELIX   29 AD2 THR B  271  SER B  277  1                                   7    
HELIX   30 AD3 SER B  278  SER B  294  1                                  17    
HELIX   31 AD4 THR B  297  ALA B  304  1                                   8    
HELIX   32 AD5 PRO B  306  ASP B  313  1                                   8    
HELIX   33 AD6 TYR B  314  ASN B  318  5                                   5    
HELIX   34 AD7 PRO B  329  GLY B  333  5                                   5    
HELIX   35 AD8 SER B  391  GLY B  396  1                                   6    
HELIX   36 AD9 ASP B  413  ILE B  425  1                                  13    
HELIX   37 AE1 SER B  446  PHE B  475  1                                  30    
HELIX   38 AE2 ARG B  476  PHE B  479  5                                   4    
HELIX   39 AE3 SER B  487  VAL B  491  5                                   5    
HELIX   40 AE4 ASP B  501  ARG B  505  5                                   5    
HELIX   41 AE5 ASP C   27  GLY C   32  1                                   6    
HELIX   42 AE6 ALA C   34  ILE C   43  5                                  10    
HELIX   43 AE7 LEU C   45  PHE C   75  1                                  31    
HELIX   44 AE8 PRO C   80  GLN C   84  5                                   5    
HELIX   45 AE9 LEU C   88  LEU C   95  1                                   8    
HELIX   46 AF1 GLY C  100  GLU C  104  5                                   5    
HELIX   47 AF2 THR C  108  ARG C  135  1                                  28    
HELIX   48 AF3 ASP C  153  PHE C  182  1                                  30    
HELIX   49 AF4 ASP C  205  PHE C  210  1                                   6    
HELIX   50 AF5 GLY C  211  LYS C  215  5                                   5    
HELIX   51 AF6 GLY C  222  VAL C  227  5                                   6    
HELIX   52 AF7 ASN C  229  THR C  254  1                                  26    
HELIX   53 AF8 PHE C  257  PHE C  264  1                                   8    
HELIX   54 AF9 SER C  267  ASN C  293  1                                  27    
HELIX   55 AG1 PRO C  298  GLY C  303  1                                   6    
HELIX   56 AG2 THR C  305  LEU C  324  1                                  20    
HELIX   57 AG3 GLY C  353  TRP C  359  5                                   7    
HELIX   58 AG4 LEU C  366  PRO C  368  5                                   3    
HELIX   59 AG5 ASP C  376  ASP C  383  1                                   8    
HELIX   60 AG6 GLN C  385  THR C  397  1                                  13    
HELIX   61 AG7 SER C  421  ALA C  453  1                                  33    
HELIX   62 AG8 GLU C  464  MET C  469  5                                   6    
HELIX   63 AG9 GLY D   13  LYS D   23  1                                  11    
HELIX   64 AH1 TRP D   32  VAL D   55  1                                  24    
HELIX   65 AH2 SER D   57  GLY D   62  1                                   6    
HELIX   66 AH3 SER D   66  GLY D   70  5                                   5    
HELIX   67 AH4 ALA D   82  GLY D   86  5                                   5    
HELIX   68 AH5 ASP D  100  LEU D  107  1                                   8    
HELIX   69 AH6 GLY D  108  GLY D  137  1                                  30    
HELIX   70 AH7 PRO D  140  LEU D  158  1                                  19    
HELIX   71 AH8 LEU D  158  GLN D  164  1                                   7    
HELIX   72 AH9 SER D  166  ALA D  170  5                                   5    
HELIX   73 AI1 VAL D  175  ASN D  190  1                                  16    
HELIX   74 AI2 TRP D  191  LEU D  193  5                                   3    
HELIX   75 AI3 ASN D  194  THR D  221  1                                  28    
HELIX   76 AI4 SER D  245  PHE D  257  1                                  13    
HELIX   77 AI5 ASN D  263  ALA D  290  1                                  28    
HELIX   78 AI6 PHE D  298  ASP D  308  1                                  11    
HELIX   79 AI7 THR D  313  GLN D  334  1                                  22    
HELIX   80 AI8 PRO D  335  ASN D  338  5                                   4    
HELIX   81 AI9 PRO D  342  LEU D  346  5                                   5    
HELIX   82 AJ1 PRO E    9  SER E   16  1                                   8    
HELIX   83 AJ2 SER E   16  THR E   40  1                                  25    
HELIX   84 AJ3 GLY E   41  GLY E   48  1                                   8    
HELIX   85 AJ4 GLU E   71  GLN E   82  1                                  12    
HELIX   86 AJ5 THR F   17  GLN F   41  1                                  25    
HELIX   87 AJ6 THR H    5  ARG H   12  1                                   8    
HELIX   88 AJ7 PRO H   13  SER H   16  5                                   4    
HELIX   89 AJ8 THR H   27  ASN H   50  1                                  24    
HELIX   90 AJ9 GLU I    2  SER I   25  1                                  24    
HELIX   91 AK1 GLY I   26  ARG I   30  5                                   5    
HELIX   92 AK2 PRO J    9  TYR J   33  1                                  25    
HELIX   93 AK3 PRO K   12  ILE K   17  5                                   6    
HELIX   94 AK4 PHE K   18  LEU K   25  1                                   8    
HELIX   95 AK5 VAL K   27  VAL K   43  1                                  17    
HELIX   96 AK6 ASN L   13  ASN L   37  1                                  25    
HELIX   97 AK7 THR O    6  VAL O   11  1                                   6    
HELIX   98 AK8 GLY O   14  LYS O   18  5                                   5    
HELIX   99 AK9 GLU O  179  GLU O  181  5                                   3    
HELIX  100 AL1 LEU O  182  VAL O  187  1                                   6    
HELIX  101 AL2 ASP O  223  ALA O  227  5                                   5    
HELIX  102 AL3 GLU T    2  PHE T   23  1                                  22    
HELIX  103 AL4 ASN U   11  LEU U   17  1                                   7    
HELIX  104 AL5 GLY U   18  GLU U   23  5                                   6    
HELIX  105 AL6 ASN U   31  TYR U   38  5                                   8    
HELIX  106 AL7 PRO U   43  ASN U   52  1                                  10    
HELIX  107 AL8 SER U   57  ILE U   64  5                                   8    
HELIX  108 AL9 THR U   68  LEU U   79  1                                  12    
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 SER V   94  ALA V   98  5                                   5    
HELIX  117 AM9 PHE V  101  ARG V  105  5                                   5    
HELIX  118 AN1 THR V  108  GLY V  127  1                                  20    
HELIX  119 AN2 ASP V  128  TRP V  130  5                                   3    
HELIX  120 AN3 GLY V  133  TYR V  137  5                                   5    
HELIX  121 AN4 ILE Y   19  ARG Y   42  1                                  24    
HELIX  122 AN5 THR X    4  ASP X   35  1                                  32    
HELIX  123 AN6 THR Z    2  ALA Z   28  1                                  27    
HELIX  124 AN7 TRP Z   33  VAL Z   62  1                                  30    
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 PRO a   95  ALA a   99  5                                   5    
HELIX  128 AO2 SER a  101  ASN a  108  1                                   8    
HELIX  129 AO3 GLY a  109  LEU a  137  1                                  29    
HELIX  130 AO4 TRP a  142  LEU a  159  1                                  18    
HELIX  131 AO5 LEU a  159  GLY a  166  1                                   8    
HELIX  132 AO6 SER a  167  GLY a  171  5                                   5    
HELIX  133 AO7 ILE a  176  ASN a  191  1                                  16    
HELIX  134 AO8 ILE a  192  MET a  194  5                                   3    
HELIX  135 AO9 HIS a  195  SER a  222  1                                  28    
HELIX  136 AP1 SER a  232  TYR a  237  5                                   6    
HELIX  137 AP2 ASN a  247  ILE a  259  1                                  13    
HELIX  138 AP3 ASN a  267  ALA a  294  1                                  28    
HELIX  139 AP4 THR a  316  HIS a  332  1                                  17    
HELIX  140 AP5 TYR b    6  ILE b   13  5                                   8    
HELIX  141 AP6 ASP b   15  PHE b   45  1                                  31    
HELIX  142 AP7 PRO b   54  GLN b   58  5                                   5    
HELIX  143 AP8 VAL b   62  LEU b   69  1                                   8    
HELIX  144 AP9 SER b   92  TYR b  117  1                                  26    
HELIX  145 AQ1 LEU b  120  ARG b  124  5                                   5    
HELIX  146 AQ2 ASP b  134  PHE b  156  1                                  23    
HELIX  147 AQ3 GLY b  186  ASN b  191  5                                   6    
HELIX  148 AQ4 ASN b  194  VAL b  219  1                                  26    
HELIX  149 AQ5 PRO b  222  LEU b  229  1                                   8    
HELIX  150 AQ6 ASN b  233  GLY b  259  1                                  27    
HELIX  151 AQ7 PRO b  264  GLY b  269  1                                   6    
HELIX  152 AQ8 THR b  271  SER b  277  1                                   7    
HELIX  153 AQ9 SER b  278  SER b  294  1                                  17    
HELIX  154 AR1 THR b  297  ALA b  304  1                                   8    
HELIX  155 AR2 PRO b  306  ASP b  313  1                                   8    
HELIX  156 AR3 TYR b  314  ASN b  318  5                                   5    
HELIX  157 AR4 PRO b  329  GLY b  333  5                                   5    
HELIX  158 AR5 ASP b  413  ILE b  425  1                                  13    
HELIX  159 AR6 SER b  446  PHE b  475  1                                  30    
HELIX  160 AR7 ARG b  476  PHE b  479  5                                   4    
HELIX  161 AR8 ASP c   27  GLY c   32  1                                   6    
HELIX  162 AR9 ALA c   34  ILE c   43  5                                  10    
HELIX  163 AS1 LEU c   45  PHE c   75  1                                  31    
HELIX  164 AS2 PRO c   80  GLN c   84  5                                   5    
HELIX  165 AS3 ILE c   87  LEU c   95  1                                   9    
HELIX  166 AS4 GLY c  100  GLU c  104  5                                   5    
HELIX  167 AS5 THR c  108  ARG c  135  1                                  28    
HELIX  168 AS6 ASP c  153  PHE c  182  1                                  30    
HELIX  169 AS7 ASP c  205  PHE c  210  1                                   6    
HELIX  170 AS8 GLY c  211  LYS c  215  5                                   5    
HELIX  171 AS9 GLY c  222  VAL c  227  5                                   6    
HELIX  172 AT1 ASN c  229  LEU c  253  1                                  25    
HELIX  173 AT2 PHE c  257  PHE c  264  1                                   8    
HELIX  174 AT3 SER c  267  ASN c  293  1                                  27    
HELIX  175 AT4 PRO c  298  GLY c  303  1                                   6    
HELIX  176 AT5 THR c  305  LEU c  324  1                                  20    
HELIX  177 AT6 GLY c  353  TRP c  359  5                                   7    
HELIX  178 AT7 LEU c  366  PRO c  368  5                                   3    
HELIX  179 AT8 ASP c  376  ASP c  383  1                                   8    
HELIX  180 AT9 GLN c  385  THR c  397  1                                  13    
HELIX  181 AU1 SER c  421  ALA c  453  1                                  33    
HELIX  182 AU2 ASP c  460  MET c  469  5                                  10    
HELIX  183 AU3 GLY d   13  LYS d   23  1                                  11    
HELIX  184 AU4 VAL d   30  VAL d   55  1                                  26    
HELIX  185 AU5 SER d   57  GLY d   62  1                                   6    
HELIX  186 AU6 SER d   66  GLY d   70  5                                   5    
HELIX  187 AU7 ALA d   82  GLY d   86  5                                   5    
HELIX  188 AU8 ASP d  100  GLY d  108  1                                   9    
HELIX  189 AU9 GLY d  108  GLY d  137  1                                  30    
HELIX  190 AV1 PRO d  140  LEU d  158  1                                  19    
HELIX  191 AV2 LEU d  158  GLN d  164  1                                   7    
HELIX  192 AV3 SER d  166  ALA d  170  5                                   5    
HELIX  193 AV4 VAL d  175  ASN d  190  1                                  16    
HELIX  194 AV5 TRP d  191  LEU d  193  5                                   3    
HELIX  195 AV6 ASN d  194  ASN d  220  1                                  27    
HELIX  196 AV7 SER d  245  PHE d  257  1                                  13    
HELIX  197 AV8 ASN d  263  LEU d  291  1                                  29    
HELIX  198 AV9 PHE d  298  ASP d  308  1                                  11    
HELIX  199 AW1 THR d  313  GLN d  334  1                                  22    
HELIX  200 AW2 PRO d  335  ASN d  338  5                                   4    
HELIX  201 AW3 PRO d  342  LEU d  346  5                                   5    
HELIX  202 AW4 PRO e    9  ILE e   14  1                                   6    
HELIX  203 AW5 SER e   16  THR e   40  1                                  25    
HELIX  204 AW6 GLY e   41  GLY e   48  1                                   8    
HELIX  205 AW7 GLU e   71  GLN e   82  1                                  12    
HELIX  206 AW8 THR f   17  GLN f   41  1                                  25    
HELIX  207 AW9 THR h    5  ARG h   12  1                                   8    
HELIX  208 AX1 PRO h   13  SER h   16  5                                   4    
HELIX  209 AX2 THR h   27  ASN h   50  1                                  24    
HELIX  210 AX3 GLU i    2  SER i   25  1                                  24    
HELIX  211 AX4 GLY i   26  ARG i   30  5                                   5    
HELIX  212 AX5 PRO j    9  TYR j   33  1                                  25    
HELIX  213 AX6 PRO k   12  ILE k   17  5                                   6    
HELIX  214 AX7 PHE k   18  ASP k   23  1                                   6    
HELIX  215 AX8 VAL k   24  PRO k   26  5                                   3    
HELIX  216 AX9 VAL k   27  VAL k   43  1                                  17    
HELIX  217 AY1 ASN l   13  ASN l   37  1                                  25    
HELIX  218 AY2 THR o    6  VAL o   11  1                                   6    
HELIX  219 AY3 GLY o   14  LYS o   18  5                                   5    
HELIX  220 AY4 GLU o  179  GLU o  181  5                                   3    
HELIX  221 AY5 LEU o  182  VAL o  187  1                                   6    
HELIX  222 AY6 GLU t    2  PHE t   23  1                                  22    
HELIX  223 AY7 ASN u   11  LEU u   17  1                                   7    
HELIX  224 AY8 GLY u   18  GLU u   23  5                                   6    
HELIX  225 AY9 ASN u   31  TYR u   38  5                                   8    
HELIX  226 AZ1 PRO u   43  ALA u   53  1                                  11    
HELIX  227 AZ2 SER u   57  ILE u   64  5                                   8    
HELIX  228 AZ3 THR u   68  LEU u   79  1                                  12    
HELIX  229 AZ4 GLU u   88  GLU u   93  1                                   6    
HELIX  230 AZ5 GLY u   94  ASP u   96  5                                   3    
HELIX  231 AZ6 THR v   22  CYS v   37  1                                  16    
HELIX  232 AZ7 CYS v   37  VAL v   42  1                                   6    
HELIX  233 AZ8 GLY v   43  ILE v   45  5                                   3    
HELIX  234 AZ9 ARG v   55  LEU v   61  1                                   7    
HELIX  235 BA1 ASN v   68  ASN v   78  1                                  11    
HELIX  236 BA2 SER v   94  ALA v   98  5                                   5    
HELIX  237 BA3 PHE v  101  ARG v  105  5                                   5    
HELIX  238 BA4 THR v  108  GLY v  127  1                                  20    
HELIX  239 BA5 ASP v  128  TRP v  130  5                                   3    
HELIX  240 BA6 GLY v  133  TYR v  137  5                                   5    
HELIX  241 BA7 ILE y   19  ARG y   42  1                                  24    
HELIX  242 BA8 THR x    4  ASP x   35  1                                  32    
HELIX  243 BA9 THR z    2  ALA z   28  1                                  27    
HELIX  244 BB1 ASP z   32  PHE z   59  1                                  28    
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 LEU B   3  PRO B   4  0                                        
SHEET    2 AA3 2 VAL L  10  GLU L  11  1  O  GLU L  11   N  LEU B   3           
SHEET    1 AA4 2 MET B 166  VAL B 168  0                                        
SHEET    2 AA4 2 SER B 177  GLN B 179 -1  O  SER B 177   N  VAL B 168           
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 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA5 6 THR B 398  TYR B 402 -1  O  TYR B 402   N  HIS B 343           
SHEET    6 AA5 6 THR B 410  PHE B 411 -1  O  PHE B 411   N  VAL B 399           
SHEET    1 AA6 5 VAL B 377  ASP B 380  0                                        
SHEET    2 AA6 5 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3 AA6 5 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4 AA6 5 ILE B 336  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5 AA6 5 ILE B 429  ASP B 433 -1  O  GLU B 431   N  GLN B 338           
SHEET    1 AA7 2 LEU C 185  ASP C 187  0                                        
SHEET    2 AA7 2 ASP C 195  ARG C 197 -1  O  ASP C 195   N  ASP C 187           
SHEET    1 AA8 2 LEU C 341  ARG C 343  0                                        
SHEET    2 AA8 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1 AA9 2 ARG C 370  GLY C 371  0                                        
SHEET    2 AA9 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1 AB1 2 ALA D  77  VAL D  78  0                                        
SHEET    2 AB1 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1 AB2 2 TYR O  30  PRO O  31  0                                        
SHEET    2 AB2 2 SER O 135  ILE O 136 -1  O  ILE O 136   N  TYR O  30           
SHEET    1 AB310 PHE O  65  PRO O  67  0                                        
SHEET    2 AB310 TYR O  38  LYS O  53 -1  N  VAL O  52   O  VAL O  66           
SHEET    3 AB310 GLU O 232  PRO O 245 -1  O  LYS O 234   N  LEU O  51           
SHEET    4 AB310 GLU O 210  LEU O 220 -1  N  GLN O 219   O  VAL O 233           
SHEET    5 AB310 LEU O 192  VAL O 204 -1  N  ASN O 200   O  THR O 214           
SHEET    6 AB310 ASP O 141  PRO O 149 -1  N  GLY O 144   O  ILE O 197           
SHEET    7 AB310 VAL O 126  SER O 128 -1  N  SER O 128   O  LYS O 143           
SHEET    8 AB310 LEU O  93  ILE O 101 -1  N  PHE O  95   O  ALA O 127           
SHEET    9 AB310 LEU O  78  VAL O  87 -1  N  GLN O  82   O  GLU O  98           
SHEET   10 AB310 TYR O  38  LYS O  53 -1  N  LEU O  45   O  LEU O  78           
SHEET    1 AB4 3 LYS O  69  LEU O  70  0                                        
SHEET    2 AB4 3 PHE O 103  GLN O 109 -1  O  GLN O 109   N  LYS O  69           
SHEET    3 AB4 3 ARG O 115  THR O 121 -1  O  ILE O 116   N  VAL O 108           
SHEET    1 AB5 2 ILE U  25  ASP U  26  0                                        
SHEET    2 AB5 2 PHE U  82  THR U  83  1  O  THR U  83   N  ILE U  25           
SHEET    1 AB6 2 THR V   9  PRO V  11  0                                        
SHEET    2 AB6 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1 AB7 2 ALA a  81  VAL a  82  0                                        
SHEET    2 AB7 2 LEU a 174  GLY a 175 -1  O  LEU a 174   N  VAL a  82           
SHEET    1 AB8 2 LEU a 297  ASN a 298  0                                        
SHEET    2 AB8 2 GLY c 402  SER c 403  1  O  GLY c 402   N  ASN a 298           
SHEET    1 AB9 2 LEU b   3  PRO b   4  0                                        
SHEET    2 AB9 2 VAL l  10  GLU l  11  1  O  GLU l  11   N  LEU b   3           
SHEET    1 AC1 2 MET b 166  VAL b 168  0                                        
SHEET    2 AC1 2 SER b 177  GLN b 179 -1  O  GLN b 179   N  MET b 166           
SHEET    1 AC2 6 VAL b 377  ASP b 380  0                                        
SHEET    2 AC2 6 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC2 6 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC2 6 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC2 6 THR b 398  TYR b 402 -1  O  SER b 400   N  VAL b 345           
SHEET    6 AC2 6 THR b 410  PHE b 411 -1  O  PHE b 411   N  VAL b 399           
SHEET    1 AC3 5 VAL b 377  ASP b 380  0                                        
SHEET    2 AC3 5 ILE b 369  THR b 371 -1  N  LEU b 370   O  ALA b 379           
SHEET    3 AC3 5 GLU b 353  VAL b 356 -1  N  PHE b 355   O  THR b 371           
SHEET    4 AC3 5 ILE b 336  ARG b 347 -1  N  PHE b 346   O  LEU b 354           
SHEET    5 AC3 5 ILE b 429  ASP b 433 -1  O  GLU b 431   N  GLN b 338           
SHEET    1 AC4 2 LEU c 185  ASP c 187  0                                        
SHEET    2 AC4 2 ASP c 195  ARG c 197 -1  O  ARG c 197   N  LEU c 185           
SHEET    1 AC5 2 LEU c 341  ARG c 343  0                                        
SHEET    2 AC5 2 ILE c 349  PHE c 351 -1  O  ILE c 350   N  MET c 342           
SHEET    1 AC6 2 ARG c 370  GLY c 371  0                                        
SHEET    2 AC6 2 GLY c 374  LEU c 375 -1  O  GLY c 374   N  GLY c 371           
SHEET    1 AC7 2 ALA d  77  VAL d  78  0                                        
SHEET    2 AC7 2 PHE d 173  GLY d 174 -1  O  PHE d 173   N  VAL d  78           
SHEET    1 AC8 2 TYR o  30  PRO o  31  0                                        
SHEET    2 AC8 2 SER o 135  ILE o 136 -1  O  ILE o 136   N  TYR o  30           
SHEET    1 AC9 4 PHE o  65  PRO o  67  0                                        
SHEET    2 AC9 4 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AC9 4 LEU o  78  VAL o  87 -1  O  LEU o  78   N  LEU o  45           
SHEET    4 AC9 4 ASP o  99  ILE o 101 -1  O  ASP o  99   N  GLN o  82           
SHEET    1 AD110 PHE o  65  PRO o  67  0                                        
SHEET    2 AD110 TYR o  38  LYS o  53 -1  N  VAL o  52   O  VAL o  66           
SHEET    3 AD110 GLU o 232  PRO o 245 -1  O  LYS o 234   N  LEU o  51           
SHEET    4 AD110 GLU o 210  LEU o 220 -1  N  SER o 217   O  ILE o 235           
SHEET    5 AD110 LEU o 192  ASP o 205 -1  N  ASP o 205   O  GLU o 210           
SHEET    6 AD110 ASP o 141  PRO o 149 -1  N  VAL o 148   O  THR o 193           
SHEET    7 AD110 VAL o 126  SER o 128 -1  N  SER o 128   O  LYS o 143           
SHEET    8 AD110 LEU o  93  VAL o  96 -1  N  PHE o  95   O  ALA o 127           
SHEET    9 AD110 LEU o  78  VAL o  87 -1  N  GLU o  84   O  VAL o  96           
SHEET   10 AD110 ASP o  99  ILE o 101 -1  O  ASP o  99   N  GLN o  82           
SHEET    1 AD2 3 LYS o  69  LEU o  70  0                                        
SHEET    2 AD2 3 PHE o 103  GLN o 109 -1  O  GLN o 109   N  LYS o  69           
SHEET    3 AD2 3 ARG o 115  THR o 121 -1  O  ILE o 116   N  VAL o 108           
SHEET    1 AD3 2 ILE u  25  ASP u  26  0                                        
SHEET    2 AD3 2 PHE u  82  THR u  83  1  O  THR u  83   N  ILE u  25           
SSBOND   1 CYS O   19    CYS O   44                          1555   1555  2.03  
SSBOND   2 CYS o   19    CYS o   44                          1555   1555  1.98  
LINK         C   FME I   1                 N   GLU I   2     1555   1555  1.34  
LINK         C   FME T   1                 N   GLU T   2     1555   1555  1.34  
LINK         SG  CYS V  37                 CAB HEC V 202     1555   1555  1.84  
LINK         SG  CYS V  40                 CAC HEC V 202     1555   1555  1.94  
LINK         C   FME i   1                 N   GLU i   2     1555   1555  1.35  
LINK         C   FME t   1                 N   GLU t   2     1555   1555  1.34  
LINK         SG  CYS v  37                 CAB HEC v 202     1555   1555  1.82  
LINK         SG  CYS v  40                 CAC HEC v 202     1555   1555  1.97  
LINK         OD1 ASP A 170                MN4  OEX A 401     1555   1555  1.98  
LINK         OD2 ASP A 170                CA1  OEX A 401     1555   1555  2.41  
LINK         OE1 GLU A 189                CA1  OEX A 401     1555   1555  2.96  
LINK         OE2 GLU A 189                MN1  OEX A 401     1555   1555  1.87  
LINK         NE2 HIS A 215                FE   FE2 A 402     1555   1555  2.05  
LINK         NE2 HIS A 272                FE   FE2 A 402     1555   1555  2.32  
LINK         NE2 HIS A 332                MN1  OEX A 401     1555   1555  2.03  
LINK         OE1 GLU A 333                MN3  OEX A 401     1555   1555  1.97  
LINK         OE2 GLU A 333                MN4  OEX A 401     1555   1555  2.13  
LINK         OD1 ASP A 342                MN2  OEX A 401     1555   1555  2.04  
LINK         OD2 ASP A 342                MN1  OEX A 401     1555   1555  2.20  
LINK         O   ALA A 344                CA1  OEX A 401     1555   1555  2.31  
LINK         OXT ALA A 344                MN2  OEX A 401     1555   1555  1.97  
LINK        CA1  OEX A 401                 O   HOH A 521     1555   1555  2.30  
LINK        MN4  OEX A 401                 O   HOH A 522     1555   1555  2.16  
LINK        MN4  OEX A 401                 O   HOH A 591     1555   1555  2.15  
LINK        CA1  OEX A 401                 O   HOH A 604     1555   1555  2.41  
LINK        MN2  OEX A 401                 OE1 GLU C 354     1555   1555  2.08  
LINK        MN3  OEX A 401                 OE2 GLU C 354     1555   1555  2.14  
LINK        FE   FE2 A 402                 O2 ABCT A 421     1555   1555  2.54  
LINK        FE   FE2 A 402                 O2 BBCT A 421     1555   1555  2.46  
LINK        FE   FE2 A 402                 O3 ABCT A 421     1555   1555  2.35  
LINK        FE   FE2 A 402                 O3 BBCT A 421     1555   1555  2.29  
LINK        FE   FE2 A 402                 NE2 HIS D 214     1555   1555  2.17  
LINK        FE   FE2 A 402                 NE2 HIS D 268     1555   1555  2.38  
LINK        MG   CLA A 406                 O   HOH A 614     1555   1555  2.12  
LINK         O   HOH A 578                MG   CLA D 401     1555   1555  2.02  
LINK         OD1 ASN B 438                CA    CA B 601     1555   1555  2.59  
LINK        CA    CA B 601                 O   HOH B 720     1555   1555  2.69  
LINK        CA    CA B 601                 O   HOH B 850     1555   1555  2.62  
LINK        CA    CA B 601                 O   HOH B 932     1555   1555  2.34  
LINK        CA    CA B 601                 O   HOH O 518     1555   1555  2.59  
LINK        MG   CLA B 602                 O   HOH B 705     1555   1555  1.97  
LINK        MG   CLA B 608                 O   HOH B 855     1555   1555  1.93  
LINK        MG   CLA B 611                 O   HOH B 710     1555   1555  2.11  
LINK         OD1 ASN C  39                MG   CLA C 512     1555   1555  1.97  
LINK        MG   CLA C 505                 O   HOH C 722     1555   1555  2.06  
LINK        MG   CLA C 508                 O   HOH C 607     1555   1555  2.08  
LINK         NE2 HIS E  23                FE   HEM E 102     1555   1555  2.04  
LINK        FE   HEM E 102                 NE2 HIS F  24     1555   1555  2.10  
LINK         O   HOH F 201                MG    MG J 102     1555   1555  2.50  
LINK         O   GLY J  31                MG    MG J 102     1555   1555  2.25  
LINK         O   ALA J  34                MG    MG J 102     1555   1555  2.31  
LINK         O   LEU J  36                MG    MG J 102     1555   1555  2.39  
LINK         O4  LMG J 101                MG    MG J 102     1555   1555  2.40  
LINK         OD2 ASP K  19                MG    MG K 102     1555   1555  2.38  
LINK         OD2 ASP K  23                MG    MG K 102     1555   1555  2.51  
LINK        MG    MG K 102                 O   HOH K 201     1555   1555  2.15  
LINK        MG    MG K 102                 O   HOH K 206     1555   1555  2.81  
LINK        MG    MG K 102                 O   HOH Y 206     1555   1555  2.79  
LINK         O   THR O 138                CA    CA O 302     1555   1555  2.46  
LINK         OD1 ASN O 200                CA    CA O 302     1555   1555  2.49  
LINK         O   VAL O 201                CA    CA O 302     1555   1555  2.33  
LINK        CA    CA O 302                 O   HOH O 459     1555   1555  2.19  
LINK        CA    CA O 302                 O   HOH O 533     1555   1555  2.93  
LINK         NE2 HIS V  41                FE   HEC V 202     1555   1555  2.00  
LINK         NE2 HIS V  92                FE   HEC V 202     1555   1555  2.02  
LINK         OD1 ASP a 170                CA1  OEX a 403     1555   1555  2.53  
LINK         OD2 ASP a 170                MN4  OEX a 403     1555   1555  2.10  
LINK         OE1 GLU a 189                CA1  OEX a 403     1555   1555  2.85  
LINK         OE2 GLU a 189                MN1  OEX a 403     1555   1555  1.78  
LINK         NE2 HIS a 215                FE   FE2 a 404     1555   1555  1.98  
LINK         NE2 HIS a 272                FE   FE2 a 404     1555   1555  2.30  
LINK         NE2 HIS a 332                MN1  OEX a 403     1555   1555  2.05  
LINK         OE1 GLU a 333                MN3  OEX a 403     1555   1555  2.06  
LINK         OE2 GLU a 333                MN4  OEX a 403     1555   1555  2.05  
LINK         OD1 ASP a 342                MN2  OEX a 403     1555   1555  2.00  
LINK         OD2 ASP a 342                MN1  OEX a 403     1555   1555  2.19  
LINK         O   ALA a 344                CA1  OEX a 403     1555   1555  2.60  
LINK         OXT ALA a 344                MN2  OEX a 403     1555   1555  1.96  
LINK        CA1  OEX a 403                 O   HOH a 506     1555   1555  2.40  
LINK        MN4  OEX a 403                 O   HOH a 544     1555   1555  2.21  
LINK        MN4  OEX a 403                 O   HOH a 597     1555   1555  2.33  
LINK        CA1  OEX a 403                 O   HOH a 599     1555   1555  2.62  
LINK        MN2  OEX a 403                 OE1 GLU c 354     1555   1555  2.11  
LINK        MN3  OEX a 403                 OE2 GLU c 354     1555   1555  2.29  
LINK        FE   FE2 a 404                 O2  BCT a 422     1555   1555  2.35  
LINK        FE   FE2 a 404                 O3  BCT a 422     1555   1555  2.59  
LINK        FE   FE2 a 404                 NE2 HIS d 214     1555   1555  2.08  
LINK        FE   FE2 a 404                 NE2 HIS d 268     1555   1555  2.33  
LINK        MG   CLA a 408                 O   HOH a 567     1555   1555  2.15  
LINK        MG   CLA a 409                 O   HOH a 602     1555   1555  2.13  
LINK         OD1 ASN b 438                CA    CA b 601     1555   1555  2.41  
LINK        CA    CA b 601                 O   HOH b 755     1555   1555  2.64  
LINK        CA    CA b 601                 O   HOH b 787     1555   1555  2.12  
LINK        CA    CA b 601                 O   HOH b 861     1555   1555  2.45  
LINK        MG   CLA b 602                 O   HOH b 706     1555   1555  2.16  
LINK        MG   CLA b 608                 O   HOH b 860     1555   1555  1.96  
LINK        MG   CLA b 611                 O   HOH b 737     1555   1555  2.01  
LINK         O   PHE c  22                CA    CA c 901     1555   1555  2.38  
LINK         O   THR c  24                CA    CA c 901     1555   1555  2.18  
LINK         OD1 ASP c  27                CA    CA c 901     1555   1555  2.76  
LINK         OD2 ASP c  27                CA    CA c 901     1555   1555  2.52  
LINK         OG  SER c  30                CA    CA c 901     1555   1555  2.30  
LINK         OD1 ASN c  39                MG   CLA c 912     1555   1555  2.04  
LINK        CA    CA c 901                 O   HOH c1158     1555   1555  2.52  
LINK        MG   CLA c 905                 O   HOH c1166     1555   1555  2.10  
LINK        MG   CLA c 908                 O   HOH c1017     1555   1555  2.04  
LINK         NE2 HIS e  23                FE   HEM e 101     1555   1555  2.11  
LINK        FE   HEM e 101                 NE2 HIS f  24     1555   1555  2.06  
LINK         O   HOH f 201                MG    MG j 102     1555   1555  2.54  
LINK         O   GLY j  31                MG    MG j 102     1555   1555  2.21  
LINK         O   ALA j  34                MG    MG j 102     1555   1555  2.49  
LINK         O   LEU j  36                MG    MG j 102     1555   1555  2.25  
LINK         O4  LMG j 101                MG    MG j 102     1555   1555  2.52  
LINK         OD2 ASP k  19                MG    MG k 102     1555   1555  2.21  
LINK         OD2 ASP k  23                MG    MG k 102     1555   1555  2.40  
LINK        MG    MG k 102                 O   HOH k 201     1555   1555  2.12  
LINK        MG    MG k 102                 O   HOH k 206     1555   1555  2.96  
LINK        MG    MG k 102                 O   HOH k 207     1555   1555  2.51  
LINK         O   THR o 138                CA    CA o 301     1555   1555  2.47  
LINK         OD1 ASN o 200                CA    CA o 301     1555   1555  2.32  
LINK         O   VAL o 201                CA    CA o 301     1555   1555  2.35  
LINK        CA    CA o 301                 O   HOH o 416     1555   1555  2.49  
LINK        CA    CA o 301                 O   HOH o 441     1555   1555  2.60  
LINK        CA    CA o 301                 O   HOH o 447     1555   1555  2.37  
LINK        CA    CA o 301                 O   HOH o 489     1555   1555  2.32  
LINK         NE2 HIS v  41                FE   HEC v 202     1555   1555  1.99  
LINK         NE2 HIS v  92                FE   HEC v 202     1555   1555  1.92  
CISPEP   1 TYR U   42    PRO U   43          0         4.19                     
CISPEP   2 ALA U   53    PRO U   54          0         1.68                     
CISPEP   3 THR V   63    PRO V   64          0       -11.67                     
CISPEP   4 TYR u   42    PRO u   43          0         3.47                     
CISPEP   5 ALA u   53    PRO u   54          0        -1.22                     
CISPEP   6 THR v   63    PRO v   64          0        -4.57                     
CRYST1  121.954  226.993  285.886  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      0.008200  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004405  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003498        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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