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Database: PDB
Entry: 1S5L
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Original site: 1S5L 
HEADER    PHOTOSYNTHESIS                          21-JAN-04   1S5L              
TITLE     ARCHITECTURE OF THE PHOTOSYNTHETIC OXYGEN EVOLVING CENTER             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOTOSYSTEM Q(B) PROTEIN;                                  
COMPND   3 CHAIN: A, a;                                                         
COMPND   4 SYNONYM: 32 KDA THYLAKOID MEMBRANE PROTEIN, PHOTOSYSTEM II PROTEIN   
COMPND   5 D1;                                                                  
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PHOTOSYSTEM II CORE LIGHT HARVESTING PROTEIN;              
COMPND   8 CHAIN: B, b;                                                         
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: PHOTOSYSTEM II CP43 PROTEIN;                               
COMPND  11 CHAIN: C, c;                                                         
COMPND  12 MOL_ID: 4;                                                           
COMPND  13 MOLECULE: PHOTOSYSTEM II REACTION CENTER D2 PROTEIN;                 
COMPND  14 CHAIN: D, d;                                                         
COMPND  15 MOL_ID: 5;                                                           
COMPND  16 MOLECULE: CYTOCHROME B559 ALPHA SUBUNIT;                             
COMPND  17 CHAIN: E, e;                                                         
COMPND  18 SYNONYM: PSII REACTION CENTER SUBUNIT V;                             
COMPND  19 MOL_ID: 6;                                                           
COMPND  20 MOLECULE: CYTOCHROME B559 BETA SUBUNIT;                              
COMPND  21 CHAIN: F, f;                                                         
COMPND  22 SYNONYM: PSII REACTION CENTER SUBUNIT VI;                            
COMPND  23 MOL_ID: 7;                                                           
COMPND  24 MOLECULE: PHOTOSYSTEM II PSBH PROTEIN;                               
COMPND  25 CHAIN: H, h;                                                         
COMPND  26 MOL_ID: 8;                                                           
COMPND  27 MOLECULE: PHOTOSYSTEM II REACTION CENTER I PROTEIN;                  
COMPND  28 CHAIN: I, i;                                                         
COMPND  29 SYNONYM: PSII 4.4 KDA PROTEIN;                                       
COMPND  30 MOL_ID: 9;                                                           
COMPND  31 MOLECULE: PHOTOSYSTEM II REACTION CENTER J PROTEIN;                  
COMPND  32 CHAIN: J, j;                                                         
COMPND  33 MOL_ID: 10;                                                          
COMPND  34 MOLECULE: PHOTOSYSTEM II REACTION CENTER PROTEIN K;                  
COMPND  35 CHAIN: K, k;                                                         
COMPND  36 SYNONYM: PSII-K;                                                     
COMPND  37 MOL_ID: 11;                                                          
COMPND  38 MOLECULE: PHOTOSYSTEM II REACTION CENTER L PROTEIN;                  
COMPND  39 CHAIN: L, l;                                                         
COMPND  40 SYNONYM: PSII 5 KDA PROTEIN;                                         
COMPND  41 MOL_ID: 12;                                                          
COMPND  42 MOLECULE: PHOTOSYSTEM II REACTION CENTER M PROTEIN;                  
COMPND  43 CHAIN: M, m;                                                         
COMPND  44 SYNONYM: PSII-M;                                                     
COMPND  45 MOL_ID: 13;                                                          
COMPND  46 MOLECULE: PHOTOSYSTEM II MANGANESE-STABILIZING POLYPEPTIDE;          
COMPND  47 CHAIN: O, o;                                                         
COMPND  48 SYNONYM: MSP;                                                        
COMPND  49 MOL_ID: 14;                                                          
COMPND  50 MOLECULE: PHOTOSYSTEM II PSBT PROTEIN;                               
COMPND  51 CHAIN: T, t;                                                         
COMPND  52 MOL_ID: 15;                                                          
COMPND  53 MOLECULE: PHOTOSYSTEM II 12 KDA EXTRINSIC PROTEIN;                   
COMPND  54 CHAIN: U, u;                                                         
COMPND  55 SYNONYM: PS II COMPLEX 12 KDA EXTRINSIC PROTEIN, PSII-U;             
COMPND  56 MOL_ID: 16;                                                          
COMPND  57 MOLECULE: CYTOCHROME C-550;                                          
COMPND  58 CHAIN: V, v;                                                         
COMPND  59 SYNONYM: C550, LOW POTENTIAL CYTOCHROME C;                           
COMPND  60 MOL_ID: 17;                                                          
COMPND  61 MOLECULE: PHOTOSYSTEM II PSBX PROTEIN;                               
COMPND  62 CHAIN: X, x;                                                         
COMPND  63 MOL_ID: 18;                                                          
COMPND  64 MOLECULE: PHOTOSYSTEM II PSBN PROTEIN;                               
COMPND  65 CHAIN: N, n;                                                         
COMPND  66 MOL_ID: 19;                                                          
COMPND  67 MOLECULE: PHOTOSYSTEM II REACTION CENTER Z PROTEIN;                  
COMPND  68 CHAIN: Z, z;                                                         
COMPND  69 SYNONYM: PHOTOSYSTEM II PSBZ PROTEIN                                 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   3 ORGANISM_TAXID: 146786;                                              
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   6 ORGANISM_TAXID: 146786;                                              
SOURCE   7 MOL_ID: 3;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE   9 ORGANISM_TAXID: 146786;                                              
SOURCE  10 MOL_ID: 4;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  12 ORGANISM_TAXID: 146786;                                              
SOURCE  13 MOL_ID: 5;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  15 ORGANISM_TAXID: 146786;                                              
SOURCE  16 MOL_ID: 6;                                                           
SOURCE  17 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  18 ORGANISM_TAXID: 146786;                                              
SOURCE  19 MOL_ID: 7;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  21 ORGANISM_TAXID: 146786;                                              
SOURCE  22 MOL_ID: 8;                                                           
SOURCE  23 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  24 ORGANISM_TAXID: 146786;                                              
SOURCE  25 MOL_ID: 9;                                                           
SOURCE  26 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  27 ORGANISM_TAXID: 146786;                                              
SOURCE  28 MOL_ID: 10;                                                          
SOURCE  29 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  30 ORGANISM_TAXID: 146786;                                              
SOURCE  31 MOL_ID: 11;                                                          
SOURCE  32 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  33 ORGANISM_TAXID: 146786;                                              
SOURCE  34 MOL_ID: 12;                                                          
SOURCE  35 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  36 ORGANISM_TAXID: 146786;                                              
SOURCE  37 MOL_ID: 13;                                                          
SOURCE  38 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  39 ORGANISM_TAXID: 146786;                                              
SOURCE  40 MOL_ID: 14;                                                          
SOURCE  41 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  42 ORGANISM_TAXID: 146786;                                              
SOURCE  43 MOL_ID: 15;                                                          
SOURCE  44 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  45 ORGANISM_TAXID: 146786;                                              
SOURCE  46 MOL_ID: 16;                                                          
SOURCE  47 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  48 ORGANISM_TAXID: 146786;                                              
SOURCE  49 MOL_ID: 17;                                                          
SOURCE  50 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  51 ORGANISM_TAXID: 146786;                                              
SOURCE  52 MOL_ID: 18;                                                          
SOURCE  53 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  54 ORGANISM_TAXID: 146786;                                              
SOURCE  55 MOL_ID: 19;                                                          
SOURCE  56 ORGANISM_SCIENTIFIC: THERMOSYNECHOCOCCUS ELONGATUS;                  
SOURCE  57 ORGANISM_TAXID: 146786                                               
KEYWDS    PHOTOSYSTEM, PHOTOSYNTHESIS, OXYGEN-EVOLVING, TETRA-MANGANESE,        
KEYWDS   2 MEMBRANE                                                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.N.FERREIRA,T.M.IVERSON,K.MAGHLAOUI,J.BARBER,S.IWATA                 
REVDAT   6   03-MAR-21 1S5L    1       COMPND REMARK SEQADV HET                 
REVDAT   6 2                   1       HETNAM HETSYN FORMUL LINK                
REVDAT   6 3                   1       ATOM                                     
REVDAT   5   25-JUL-12 1S5L    1       FORMUL HET    HETATM HETNAM              
REVDAT   5 2                   1       LINK   REMARK SITE   VERSN               
REVDAT   4   16-FEB-10 1S5L    1       DBREF  SEQADV                            
REVDAT   3   24-FEB-09 1S5L    1       VERSN                                    
REVDAT   2   30-MAR-04 1S5L    1       JRNL                                     
REVDAT   1   24-FEB-04 1S5L    0                                                
JRNL        AUTH   K.N.FERREIRA,T.M.IVERSON,K.MAGHLAOUI,J.BARBER,S.IWATA        
JRNL        TITL   ARCHITECTURE OF THE PHOTOSYNTHETIC OXYGEN-EVOLVING CENTER    
JRNL        REF    SCIENCE                       V. 303  1831 2004              
JRNL        REFN                   ISSN 0036-8075                               
JRNL        PMID   14764885                                                     
JRNL        DOI    10.1126/SCIENCE.1093087                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 101219                         
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 SET) : 0.296                           
REMARK   3   FREE R VALUE                     : 0.342                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 981                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 39991                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 5954                                    
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.014                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.960                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1S5L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-FEB-04.                  
REMARK 100 THE DEPOSITION ID IS D_1000021395.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-JAN-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06SA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 103604                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 87.9                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.52                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 80.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.92                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 100MM (NH4)2SO4, PEG        
REMARK 280  4000, C12E8, TRIMETHYL LEAD ACETATE, PH 7.5, PSEUDO-BATCH           
REMARK 280  HANGING DROP, TEMPERATURE 291K                                      
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       67.49600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      154.97000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      114.42450            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      154.97000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       67.49600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      114.42450            
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 300 REMARK: THE BIOLOGICAL UNIT IS A DIMER, WHICH IS PRESENT IN THE      
REMARK 300 ASYMMETRIC UNIT                                                      
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: NONADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, H, I, J, K,         
REMARK 350                    AND CHAINS: L, M, O, T, U, V, X, N, 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: NONADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, b, c, d, e, f, h, i, j, k,         
REMARK 350                    AND CHAINS: l, m, o, t, u, v, x, n, z             
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     GLN A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     GLU A     9                                                      
REMARK 465     SER A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY B     2                                                      
REMARK 465     LEU B     3                                                      
REMARK 465     PRO B     4                                                      
REMARK 465     TRP B     5                                                      
REMARK 465     ILE B   482                                                      
REMARK 465     ASP B   483                                                      
REMARK 465     PRO B   484                                                      
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     LYS B   507                                                      
REMARK 465     GLU B   508                                                      
REMARK 465     ALA B   509                                                      
REMARK 465     VAL B   510                                                      
REMARK 465     MET C     1                                                      
REMARK 465     LYS C     2                                                      
REMARK 465     THR C     3                                                      
REMARK 465     LEU C     4                                                      
REMARK 465     SER C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     GLN C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     ARG C     9                                                      
REMARK 465     TYR C    10                                                      
REMARK 465     SER C    11                                                      
REMARK 465     PRO C    12                                                      
REMARK 465     VAL C    13                                                      
REMARK 465     VAL C    14                                                      
REMARK 465     THR C    15                                                      
REMARK 465     LEU C    16                                                      
REMARK 465     SER C    17                                                      
REMARK 465     SER C    18                                                      
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     ILE C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     THR C    24                                                      
REMARK 465     ASN C    25                                                      
REMARK 465     ARG C    26                                                      
REMARK 465     ASP C    27                                                      
REMARK 465     GLN C    28                                                      
REMARK 465     GLU C    29                                                      
REMARK 465     SER C    30                                                      
REMARK 465     SER C    31                                                      
REMARK 465     GLY C    32                                                      
REMARK 465     PHE C    33                                                      
REMARK 465     ALA C    34                                                      
REMARK 465     TRP C    35                                                      
REMARK 465     LYS C   457                                                      
REMARK 465     GLY C   458                                                      
REMARK 465     ILE C   459                                                      
REMARK 465     ASP C   460                                                      
REMARK 465     ARG C   461                                                      
REMARK 465     GLU C   462                                                      
REMARK 465     SER C   463                                                      
REMARK 465     GLU C   464                                                      
REMARK 465     PRO C   465                                                      
REMARK 465     VAL C   466                                                      
REMARK 465     LEU C   467                                                      
REMARK 465     SER C   468                                                      
REMARK 465     MET C   469                                                      
REMARK 465     PRO C   470                                                      
REMARK 465     SER C   471                                                      
REMARK 465     LEU C   472                                                      
REMARK 465     ASP C   473                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ILE D     3                                                      
REMARK 465     ALA D     4                                                      
REMARK 465     ILE D     5                                                      
REMARK 465     GLY D     6                                                      
REMARK 465     ARG D     7                                                      
REMARK 465     ALA D     8                                                      
REMARK 465     PRO D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     ARG D    12                                                      
REMARK 465     GLY D    13                                                      
REMARK 465     MET E     0                                                      
REMARK 465     ALA E     1                                                      
REMARK 465     GLY E     2                                                      
REMARK 465     THR E     3                                                      
REMARK 465     THR E     4                                                      
REMARK 465     GLY E     5                                                      
REMARK 465     GLU E     6                                                      
REMARK 465     ARG E     7                                                      
REMARK 465     MET F     0                                                      
REMARK 465     THR F     1                                                      
REMARK 465     SER F     2                                                      
REMARK 465     ASN F     3                                                      
REMARK 465     THR F     4                                                      
REMARK 465     PRO F     5                                                      
REMARK 465     ASN F     6                                                      
REMARK 465     GLN F     7                                                      
REMARK 465     GLU F     8                                                      
REMARK 465     PRO F     9                                                      
REMARK 465     VAL F    10                                                      
REMARK 465     SER F    11                                                      
REMARK 465     MET H     0                                                      
REMARK 465     ALA H     1                                                      
REMARK 465     ARG H     2                                                      
REMARK 465     ARG H     3                                                      
REMARK 465     THR H     4                                                      
REMARK 465     TRP H     5                                                      
REMARK 465     LEU H     6                                                      
REMARK 465     GLY H     7                                                      
REMARK 465     ASP H     8                                                      
REMARK 465     ILE H     9                                                      
REMARK 465     LEU H    10                                                      
REMARK 465     ARG H    11                                                      
REMARK 465     PRO H    12                                                      
REMARK 465     MET J     1                                                      
REMARK 465     MET J     2                                                      
REMARK 465     SER M    31                                                      
REMARK 465     GLN M    32                                                      
REMARK 465     GLN M    33                                                      
REMARK 465     LYS M    34                                                      
REMARK 465     SER M    35                                                      
REMARK 465     SER M    36                                                      
REMARK 465     LYS T    32                                                      
REMARK 465     MET U     1                                                      
REMARK 465     GLN U     2                                                      
REMARK 465     ARG U     3                                                      
REMARK 465     LEU U     4                                                      
REMARK 465     GLY U     5                                                      
REMARK 465     ARG U     6                                                      
REMARK 465     TRP U     7                                                      
REMARK 465     LEU U     8                                                      
REMARK 465     ALA U     9                                                      
REMARK 465     LEU U    10                                                      
REMARK 465     ALA U    11                                                      
REMARK 465     TYR U    12                                                      
REMARK 465     PHE U    13                                                      
REMARK 465     VAL U    14                                                      
REMARK 465     GLY U    15                                                      
REMARK 465     VAL U    16                                                      
REMARK 465     SER U    17                                                      
REMARK 465     LEU U    18                                                      
REMARK 465     LEU U    19                                                      
REMARK 465     GLY U    20                                                      
REMARK 465     TRP U    21                                                      
REMARK 465     ILE U    22                                                      
REMARK 465     ASN U    23                                                      
REMARK 465     TRP U    24                                                      
REMARK 465     SER U    25                                                      
REMARK 465     ALA U    26                                                      
REMARK 465     PRO U    27                                                      
REMARK 465     THR U    28                                                      
REMARK 465     LEU U    29                                                      
REMARK 465     MET X     1                                                      
REMARK 465     ILE X     2                                                      
REMARK 465     GLN X     3                                                      
REMARK 465     SER X     4                                                      
REMARK 465     ALA X     5                                                      
REMARK 465     SER X     6                                                      
REMARK 465     SER X     7                                                      
REMARK 465     LEU X     8                                                      
REMARK 465     LEU X     9                                                      
REMARK 465     LEU X    10                                                      
REMARK 465     PHE Z    59                                                      
REMARK 465     PHE Z    60                                                      
REMARK 465     VAL Z    61                                                      
REMARK 465     VAL Z    62                                                      
REMARK 465     MET a  2001                                                      
REMARK 465     THR a  2002                                                      
REMARK 465     THR a  2003                                                      
REMARK 465     THR a  2004                                                      
REMARK 465     LEU a  2005                                                      
REMARK 465     GLN a  2006                                                      
REMARK 465     ARG a  2007                                                      
REMARK 465     ARG a  2008                                                      
REMARK 465     GLU a  2009                                                      
REMARK 465     SER a  2010                                                      
REMARK 465     ALA a  2011                                                      
REMARK 465     MET b  2001                                                      
REMARK 465     GLY b  2002                                                      
REMARK 465     LEU b  2003                                                      
REMARK 465     PRO b  2004                                                      
REMARK 465     TRP b  2005                                                      
REMARK 465     ILE b  2482                                                      
REMARK 465     ASP b  2483                                                      
REMARK 465     PRO b  2484                                                      
REMARK 465     GLU b  2485                                                      
REMARK 465     LEU b  2486                                                      
REMARK 465     SER b  2487                                                      
REMARK 465     PRO b  2488                                                      
REMARK 465     GLU b  2489                                                      
REMARK 465     GLN b  2490                                                      
REMARK 465     VAL b  2491                                                      
REMARK 465     GLU b  2492                                                      
REMARK 465     TRP b  2493                                                      
REMARK 465     GLY b  2494                                                      
REMARK 465     PHE b  2495                                                      
REMARK 465     TYR b  2496                                                      
REMARK 465     GLN b  2497                                                      
REMARK 465     LYS b  2498                                                      
REMARK 465     VAL b  2499                                                      
REMARK 465     GLY b  2500                                                      
REMARK 465     ASP b  2501                                                      
REMARK 465     VAL b  2502                                                      
REMARK 465     THR b  2503                                                      
REMARK 465     THR b  2504                                                      
REMARK 465     ARG b  2505                                                      
REMARK 465     ARG b  2506                                                      
REMARK 465     LYS b  2507                                                      
REMARK 465     GLU b  2508                                                      
REMARK 465     ALA b  2509                                                      
REMARK 465     VAL b  2510                                                      
REMARK 465     MET c  2001                                                      
REMARK 465     LYS c  2002                                                      
REMARK 465     THR c  2003                                                      
REMARK 465     LEU c  2004                                                      
REMARK 465     SER c  2005                                                      
REMARK 465     SER c  2006                                                      
REMARK 465     GLN c  2007                                                      
REMARK 465     LYS c  2008                                                      
REMARK 465     ARG c  2009                                                      
REMARK 465     TYR c  2010                                                      
REMARK 465     SER c  2011                                                      
REMARK 465     PRO c  2012                                                      
REMARK 465     VAL c  2013                                                      
REMARK 465     VAL c  2014                                                      
REMARK 465     THR c  2015                                                      
REMARK 465     LEU c  2016                                                      
REMARK 465     SER c  2017                                                      
REMARK 465     SER c  2018                                                      
REMARK 465     ASN c  2019                                                      
REMARK 465     SER c  2020                                                      
REMARK 465     ILE c  2021                                                      
REMARK 465     PHE c  2022                                                      
REMARK 465     ALA c  2023                                                      
REMARK 465     THR c  2024                                                      
REMARK 465     ASN c  2025                                                      
REMARK 465     ARG c  2026                                                      
REMARK 465     ASP c  2027                                                      
REMARK 465     GLN c  2028                                                      
REMARK 465     GLU c  2029                                                      
REMARK 465     SER c  2030                                                      
REMARK 465     SER c  2031                                                      
REMARK 465     GLY c  2032                                                      
REMARK 465     PHE c  2033                                                      
REMARK 465     ALA c  2034                                                      
REMARK 465     TRP c  2035                                                      
REMARK 465     LYS c  2457                                                      
REMARK 465     GLY c  2458                                                      
REMARK 465     ILE c  2459                                                      
REMARK 465     ASP c  2460                                                      
REMARK 465     ARG c  2461                                                      
REMARK 465     GLU c  2462                                                      
REMARK 465     SER c  2463                                                      
REMARK 465     GLU c  2464                                                      
REMARK 465     PRO c  2465                                                      
REMARK 465     VAL c  2466                                                      
REMARK 465     LEU c  2467                                                      
REMARK 465     SER c  2468                                                      
REMARK 465     MET c  2469                                                      
REMARK 465     PRO c  2470                                                      
REMARK 465     SER c  2471                                                      
REMARK 465     LEU c  2472                                                      
REMARK 465     ASP c  2473                                                      
REMARK 465     MET d  2001                                                      
REMARK 465     THR d  2002                                                      
REMARK 465     ILE d  2003                                                      
REMARK 465     ALA d  2004                                                      
REMARK 465     ILE d  2005                                                      
REMARK 465     GLY d  2006                                                      
REMARK 465     ARG d  2007                                                      
REMARK 465     ALA d  2008                                                      
REMARK 465     PRO d  2009                                                      
REMARK 465     ALA d  2010                                                      
REMARK 465     GLU d  2011                                                      
REMARK 465     ARG d  2012                                                      
REMARK 465     GLY d  2013                                                      
REMARK 465     MET e  2000                                                      
REMARK 465     ALA e  2001                                                      
REMARK 465     GLY e  2002                                                      
REMARK 465     THR e  2003                                                      
REMARK 465     THR e  2004                                                      
REMARK 465     GLY e  2005                                                      
REMARK 465     GLU e  2006                                                      
REMARK 465     ARG e  2007                                                      
REMARK 465     MET f  2000                                                      
REMARK 465     THR f  2001                                                      
REMARK 465     SER f  2002                                                      
REMARK 465     ASN f  2003                                                      
REMARK 465     THR f  2004                                                      
REMARK 465     PRO f  2005                                                      
REMARK 465     ASN f  2006                                                      
REMARK 465     GLN f  2007                                                      
REMARK 465     GLU f  2008                                                      
REMARK 465     PRO f  2009                                                      
REMARK 465     VAL f  2010                                                      
REMARK 465     SER f  2011                                                      
REMARK 465     MET h  2000                                                      
REMARK 465     ALA h  2001                                                      
REMARK 465     ARG h  2002                                                      
REMARK 465     ARG h  2003                                                      
REMARK 465     THR h  2004                                                      
REMARK 465     TRP h  2005                                                      
REMARK 465     LEU h  2006                                                      
REMARK 465     GLY h  2007                                                      
REMARK 465     ASP h  2008                                                      
REMARK 465     ILE h  2009                                                      
REMARK 465     LEU h  2010                                                      
REMARK 465     ARG h  2011                                                      
REMARK 465     PRO h  2012                                                      
REMARK 465     MET j  2001                                                      
REMARK 465     MET j  2002                                                      
REMARK 465     SER m  2031                                                      
REMARK 465     GLN m  2032                                                      
REMARK 465     GLN m  2033                                                      
REMARK 465     LYS m  2034                                                      
REMARK 465     SER m  2035                                                      
REMARK 465     SER m  2036                                                      
REMARK 465     LYS t  2032                                                      
REMARK 465     MET u  2001                                                      
REMARK 465     GLN u  2002                                                      
REMARK 465     ARG u  2003                                                      
REMARK 465     LEU u  2004                                                      
REMARK 465     GLY u  2005                                                      
REMARK 465     ARG u  2006                                                      
REMARK 465     TRP u  2007                                                      
REMARK 465     LEU u  2008                                                      
REMARK 465     ALA u  2009                                                      
REMARK 465     LEU u  2010                                                      
REMARK 465     ALA u  2011                                                      
REMARK 465     TYR u  2012                                                      
REMARK 465     PHE u  2013                                                      
REMARK 465     VAL u  2014                                                      
REMARK 465     GLY u  2015                                                      
REMARK 465     VAL u  2016                                                      
REMARK 465     SER u  2017                                                      
REMARK 465     LEU u  2018                                                      
REMARK 465     LEU u  2019                                                      
REMARK 465     GLY u  2020                                                      
REMARK 465     TRP u  2021                                                      
REMARK 465     ILE u  2022                                                      
REMARK 465     ASN u  2023                                                      
REMARK 465     TRP u  2024                                                      
REMARK 465     SER u  2025                                                      
REMARK 465     ALA u  2026                                                      
REMARK 465     PRO u  2027                                                      
REMARK 465     THR u  2028                                                      
REMARK 465     LEU u  2029                                                      
REMARK 465     MET x  2001                                                      
REMARK 465     ILE x  2002                                                      
REMARK 465     GLN x  2003                                                      
REMARK 465     SER x  2004                                                      
REMARK 465     ALA x  2005                                                      
REMARK 465     SER x  2006                                                      
REMARK 465     SER x  2007                                                      
REMARK 465     LEU x  2008                                                      
REMARK 465     LEU x  2009                                                      
REMARK 465     LEU x  2010                                                      
REMARK 465     PHE z  2059                                                      
REMARK 465     PHE z  2060                                                      
REMARK 465     VAL z  2061                                                      
REMARK 465     VAL z  2062                                                      
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   CG1  ILE O    40     OE1  GLU O    84              2.04            
REMARK 500   O    LEU e  2035     OG1  THR e  2039              2.07            
REMARK 500   O    SER c  2216     O    GLU c  2221              2.12            
REMARK 500   O    LYS C   154     OG1  THR C   158              2.15            
REMARK 500   OD1  ASN C   293     O    TYR C   297              2.15            
REMARK 500   O    THR d  2238     N    ALA d  2240              2.16            
REMARK 500   O    LEU J    36     OG   SER J    39              2.17            
REMARK 500   O    LEU C   119     OG   SER C   122              2.17            
REMARK 500   OD2  ASP A    59     O    ILE A    63              2.17            
REMARK 500   O    SER C   216     O    GLU C   221              2.18            
REMARK 500   CD   GLU d  2096     O    ARG e  2068              2.19            
REMARK 500   O    ILE e  2021     OG1  THR e  2025              2.19            
REMARK 500   OD1  ASP B    46     OG   SER B    48              2.19            
REMARK 500   O    PRO b  2187     N    PHE b  2190              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   C    ALA O   246     O    UNK n  2035     2555     1.76            
REMARK 500   N    ALA O   246     O    UNK n  2035     2555     1.97            
REMARK 500   O    ALA O   246     O    UNK n  2035     2555     2.07            
REMARK 500   O    ALA O   246     CB   UNK n  2035     2555     2.15            
REMARK 500   N    ALA O   246     C    UNK n  2035     2555     2.17            
REMARK 500   CA   ALA O   246     O    UNK n  2035     2555     2.19            
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    PRO A  84   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    GLY A 171   N   -  CA  -  C   ANGL. DEV. = -18.2 DEGREES          
REMARK 500    GLY A 236   N   -  CA  -  C   ANGL. DEV. =  15.7 DEGREES          
REMARK 500    PRO C 137   C   -  N   -  CA  ANGL. DEV. =  10.5 DEGREES          
REMARK 500    THR D 231   N   -  CA  -  C   ANGL. DEV. = -17.0 DEGREES          
REMARK 500    PRO D 335   C   -  N   -  CA  ANGL. DEV. =  11.9 DEGREES          
REMARK 500    PRO O  31   C   -  N   -  CA  ANGL. DEV. =  10.3 DEGREES          
REMARK 500    PRO O 131   N   -  CA  -  C   ANGL. DEV. =  16.9 DEGREES          
REMARK 500    PRO O 245   C   -  N   -  CA  ANGL. DEV. =  13.2 DEGREES          
REMARK 500    PRO O 245   C   -  N   -  CD  ANGL. DEV. = -18.2 DEGREES          
REMARK 500    PRO a2084   C   -  N   -  CA  ANGL. DEV. =  11.2 DEGREES          
REMARK 500    GLY a2171   N   -  CA  -  C   ANGL. DEV. = -18.2 DEGREES          
REMARK 500    GLY a2236   N   -  CA  -  C   ANGL. DEV. =  16.0 DEGREES          
REMARK 500    PRO b2367   C   -  N   -  CA  ANGL. DEV. =   9.5 DEGREES          
REMARK 500    PRO c2137   C   -  N   -  CA  ANGL. DEV. =   9.0 DEGREES          
REMARK 500    THR d2231   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    PRO d2335   C   -  N   -  CA  ANGL. DEV. =  11.5 DEGREES          
REMARK 500    PRO o2031   C   -  N   -  CA  ANGL. DEV. =  10.0 DEGREES          
REMARK 500    PRO o2131   N   -  CA  -  C   ANGL. DEV. =  15.8 DEGREES          
REMARK 500    PRO o2245   C   -  N   -  CA  ANGL. DEV. =  10.6 DEGREES          
REMARK 500    PRO o2245   C   -  N   -  CD  ANGL. DEV. = -15.8 DEGREES          
REMARK 500    CYS v2040   CA  -  CB  -  SG  ANGL. DEV. =   8.6 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    SER A  23     -167.77   -110.88                                   
REMARK 500    ARG A  27      -54.79   -154.29                                   
REMARK 500    TRP A  32      -31.95    -31.88                                   
REMARK 500    ALA A  54      -12.67   -155.44                                   
REMARK 500    ALA A  55      145.39    -39.54                                   
REMARK 500    ASP A  61       34.68    -98.37                                   
REMARK 500    ILE A  63      162.52    -47.46                                   
REMARK 500    ARG A  64       46.55    -95.44                                   
REMARK 500    TYR A  73       35.25    -84.09                                   
REMARK 500    ALA A  81     -138.92   -150.43                                   
REMARK 500    VAL A  82      107.95    -55.53                                   
REMARK 500    PRO A  84      150.42    -44.02                                   
REMARK 500    ALA A  99     -158.46   -105.85                                   
REMARK 500    ALA A 100     -124.10   -113.08                                   
REMARK 500    GLU A 104      -76.03    -65.78                                   
REMARK 500    TRP A 105      -59.42    -26.53                                   
REMARK 500    ILE A 116      -73.91    -49.46                                   
REMARK 500    LEU A 159      -87.76   -116.45                                   
REMARK 500    ILE A 160      -51.88    -25.16                                   
REMARK 500    SER A 167      133.45    172.90                                   
REMARK 500    MET A 172      114.84   -160.05                                   
REMARK 500    LEU A 174       39.89    -93.88                                   
REMARK 500    ASN A 191       85.32     50.48                                   
REMARK 500    MET A 194       47.61    -94.61                                   
REMARK 500    HIS A 215      -79.06    -49.71                                   
REMARK 500    SER A 222       35.04    -96.15                                   
REMARK 500    ARG A 225      -27.16    -37.69                                   
REMARK 500    THR A 228       18.07     40.52                                   
REMARK 500    THR A 230     -156.16   -115.71                                   
REMARK 500    PHE A 239      -45.21    -22.25                                   
REMARK 500    GLU A 242      -87.80    -53.44                                   
REMARK 500    GLU A 243       -5.59    -44.02                                   
REMARK 500    GLU A 244      178.30     58.71                                   
REMARK 500    ILE A 259      -98.88   -136.52                                   
REMARK 500    GLN A 261      -60.89    -29.70                                   
REMARK 500    PHE A 300      175.25    -52.64                                   
REMARK 500    ASN A 301       91.81   -177.91                                   
REMARK 500    ASP A 308      -19.10    -35.15                                   
REMARK 500    TRP A 317      -38.59    -28.99                                   
REMARK 500    ARG A 334      160.27    -44.09                                   
REMARK 500    ASN A 335       40.38     32.10                                   
REMARK 500    VAL B   8      -30.88   -149.67                                   
REMARK 500    PHE B  61      -61.40    -97.03                                   
REMARK 500    LEU B  63      -56.82    -27.53                                   
REMARK 500    TRP B  78      109.23    -49.77                                   
REMARK 500    SER B  92     -155.35   -105.47                                   
REMARK 500    ALA B  99      -71.73    -57.53                                   
REMARK 500    TYR B 117       65.01   -102.82                                   
REMARK 500    GLU B 121       57.37   -100.29                                   
REMARK 500    LEU B 122     -157.44   -129.34                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     523 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    TYR A 246         0.07    SIDE CHAIN                              
REMARK 500    TYR B 273         0.07    SIDE CHAIN                              
REMARK 500    TYR O 240         0.07    SIDE CHAIN                              
REMARK 500    TYR U  51         0.08    SIDE CHAIN                              
REMARK 500    TYR U 133         0.07    SIDE CHAIN                              
REMARK 500    TYR b2273         0.08    SIDE CHAIN                              
REMARK 500    TYR l2034         0.07    SIDE CHAIN                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600 LIGAND PL9 IS MISSING TWO ISOPRENOIDS DUE TO DISORDER                
REMARK 600 IN THE ELECTRON DENSITY.                                             
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     PL9 A  353                                                       
REMARK 610     PL9 D  357                                                       
REMARK 610     PL9 a 2352                                                       
REMARK 610     PL9 d 2358                                                       
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                             CLA A 352  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 118   NE2                                                    
REMARK 620 2 CLA A 352   NA   94.1                                              
REMARK 620 3 CLA A 352   NB   98.9  91.8                                        
REMARK 620 4 CLA A 352   NC  101.2 164.6  87.5                                  
REMARK 620 5 CLA A 352   ND   94.9  90.0 165.9  87.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 347  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 170   OD2                                                    
REMARK 620 2 OEC A 347   O4  175.9                                              
REMARK 620 3 GLU A 333   OE2  95.6  88.1                                        
REMARK 620 4 BCT A 346   O1   88.1  88.1 174.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 347  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 189   OE2                                                    
REMARK 620 2 OEC A 347   O1   56.5                                              
REMARK 620 3 OEC A 347   O2  132.7  88.3                                        
REMARK 620 4 OEC A 347   O4  121.7  91.6  85.9                                  
REMARK 620 5 HIS A 332   NE2  70.3  98.6  87.4 167.6                            
REMARK 620 6 GLU A 333   OE2 132.1 154.8  93.5  63.5 106.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA A 348  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 198   NE2                                                    
REMARK 620 2 CLA A 348   NA   99.6                                              
REMARK 620 3 CLA A 348   NB   99.4  89.9                                        
REMARK 620 4 CLA A 348   NC   95.9 164.5  88.7                                  
REMARK 620 5 CLA A 348   ND   95.1  90.2 165.2  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE A 345  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 215   NE2                                                    
REMARK 620 2 HIS A 272   NE2  87.7                                              
REMARK 620 3 HIS D 214   NE2 119.3  94.4                                        
REMARK 620 4 HIS D 268   NE2  91.5 169.1  95.4                                  
REMARK 620 5 BCT D 353   O2   86.3  93.1 153.6  76.0                            
REMARK 620 6 BCT D 353   O3  148.0  88.2  92.7  86.8  62.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 347  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 333   OE1                                                    
REMARK 620 2 OEC A 347   O2   91.7                                              
REMARK 620 3 OEC A 347   O3  178.5  87.1                                        
REMARK 620 4 OEC A 347   O4   86.2  87.2  92.8                                  
REMARK 620 5 GLU C 354   OE1  95.7  86.5  85.2 173.5                            
REMARK 620 6 GLU C 354   OE2  49.7 127.4 131.8 118.2  67.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 347  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 342   OD2                                                    
REMARK 620 2 OEC A 347   O1  101.9                                              
REMARK 620 3 OEC A 347   O2  171.8  85.1                                        
REMARK 620 4 OEC A 347   O3   90.7  92.3  84.8                                  
REMARK 620 5 GLU C 354   OE1 116.5 127.0  55.4  54.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC A 347  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA A 344   OXT                                                    
REMARK 620 2 OEC A 347   O1  111.4                                              
REMARK 620 3 OEC A 347   O3   58.4  65.5                                        
REMARK 620 4 OEC A 347   O4  116.2  64.1  64.8                                  
REMARK 620 5 ALA A 344   O    57.4 102.4 101.0 163.1                            
REMARK 620 6 BCT A 346   O2  141.6 106.9 142.6  78.8 116.3                      
REMARK 620 7 BCT A 346   O3   82.2 148.3 102.7  84.2 108.9  63.6                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 520  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B   9   NE2                                                    
REMARK 620 2 CLA B 520   NA   94.2                                              
REMARK 620 3 CLA B 520   NB   95.7  91.4                                        
REMARK 620 4 CLA B 520   NC  100.6 165.1  88.6                                  
REMARK 620 5 CLA B 520   ND   96.5  90.5 167.5  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 513  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  23   NE2                                                    
REMARK 620 2 CLA B 513   NA   80.7                                              
REMARK 620 3 CLA B 513   NB   83.5  93.3                                        
REMARK 620 4 CLA B 513   NC   86.2 166.8  87.1                                  
REMARK 620 5 CLA B 513   ND   86.9  90.6 168.9  86.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  26   NE2                                                    
REMARK 620 2 CLA B 512   NA   81.2                                              
REMARK 620 3 CLA B 512   NB   83.0  93.2                                        
REMARK 620 4 CLA B 512   NC   86.5 167.4  87.7                                  
REMARK 620 5 CLA B 512   ND   86.4  90.0 168.3  86.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 518  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 100   NE2                                                    
REMARK 620 2 CLA B 518   NA   95.3                                              
REMARK 620 3 CLA B 518   NB   97.6  90.8                                        
REMARK 620 4 CLA B 518   NC  100.1 164.6  87.5                                  
REMARK 620 5 CLA B 518   ND   94.4  91.1 167.6  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 525  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 114   NE2                                                    
REMARK 620 2 CLA B 525   NA   98.9                                              
REMARK 620 3 CLA B 525   NB  100.2  92.3                                        
REMARK 620 4 CLA B 525   NC   95.7 165.1  87.8                                  
REMARK 620 5 CLA B 525   ND   92.8  89.3 166.5  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 522  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 142   NE2                                                    
REMARK 620 2 CLA B 522   NA   84.5                                              
REMARK 620 3 CLA B 522   NB   82.5  92.0                                        
REMARK 620 4 CLA B 522   NC   83.4 167.9  88.2                                  
REMARK 620 5 CLA B 522   ND   86.6  89.9 168.7  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 515  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 157   ND1                                                    
REMARK 620 2 CLA B 515   NA  103.2                                              
REMARK 620 3 CLA B 515   NB   96.6  90.0                                        
REMARK 620 4 CLA B 515   NC   95.6 161.2  88.1                                  
REMARK 620 5 CLA B 515   ND  100.5  89.1 162.7  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 521  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 201   ND1                                                    
REMARK 620 2 CLA B 521   NA   93.8                                              
REMARK 620 3 CLA B 521   NB   77.5  89.9                                        
REMARK 620 4 CLA B 521   NC  102.6 162.6  88.0                                  
REMARK 620 5 CLA B 521   ND  118.7  90.2 163.8  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 517  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 202   NE2                                                    
REMARK 620 2 CLA B 517   NA   96.3                                              
REMARK 620 3 CLA B 517   NB   94.9  91.1                                        
REMARK 620 4 CLA B 517   NC   98.7 164.9  88.2                                  
REMARK 620 5 CLA B 517   ND   97.7  89.8 167.1  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 216   NE2                                                    
REMARK 620 2 CLA B 511   NA   92.6                                              
REMARK 620 3 CLA B 511   NB   96.4  91.1                                        
REMARK 620 4 CLA B 511   NC  102.1 165.3  88.2                                  
REMARK 620 5 CLA B 511   ND   95.8  90.6 167.5  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 516  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 455   NE2                                                    
REMARK 620 2 CLA B 516   NA   99.5                                              
REMARK 620 3 CLA B 516   NB   95.8  91.6                                        
REMARK 620 4 CLA B 516   NC   95.8 164.7  88.1                                  
REMARK 620 5 CLA B 516   ND   96.9  89.5 166.9  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 519  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 466   NE2                                                    
REMARK 620 2 CLA B 519   NA   93.0                                              
REMARK 620 3 CLA B 519   NB   99.7  91.1                                        
REMARK 620 4 CLA B 519   NC  100.6 166.4  87.8                                  
REMARK 620 5 CLA B 519   ND   91.8  90.7 168.3  87.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA B 523  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 469   NE2                                                    
REMARK 620 2 CLA B 523   NA   90.3                                              
REMARK 620 3 CLA B 523   NB   98.7  91.5                                        
REMARK 620 4 CLA B 523   NC  104.2 165.3  88.4                                  
REMARK 620 5 CLA B 523   ND   93.7  90.7 167.3  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 486  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN C  39   ND2                                                    
REMARK 620 2 CLA C 486   NA  109.2                                              
REMARK 620 3 CLA C 486   NB   80.7  90.1                                        
REMARK 620 4 CLA C 486   NC   88.8 161.3  87.7                                  
REMARK 620 5 CLA C 486   ND  114.7  89.9 163.6  87.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  53   NE2                                                    
REMARK 620 2 CLA C 478   NA   83.4                                              
REMARK 620 3 CLA C 478   NB   79.4  91.9                                        
REMARK 620 4 CLA C 478   NC   83.6 166.8  88.1                                  
REMARK 620 5 CLA C 478   ND   88.4  90.0 167.4  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C  56   NE2                                                    
REMARK 620 2 CLA C 476   NA   80.9                                              
REMARK 620 3 CLA C 476   NB   81.1  92.8                                        
REMARK 620 4 CLA C 476   NC   85.2 165.8  87.8                                  
REMARK 620 5 CLA C 476   ND   87.8  89.6 168.0  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 480  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 118   NE2                                                    
REMARK 620 2 CLA C 480   NA   98.3                                              
REMARK 620 3 CLA C 480   NB   98.5  91.1                                        
REMARK 620 4 CLA C 480   NC   96.8 164.9  87.5                                  
REMARK 620 5 CLA C 480   ND   93.6  90.4 167.5  87.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 484  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 132   NE2                                                    
REMARK 620 2 CLA C 484   NA   94.8                                              
REMARK 620 3 CLA C 484   NB   96.4  91.9                                        
REMARK 620 4 CLA C 484   NC  100.0 165.1  88.0                                  
REMARK 620 5 CLA C 484   ND   96.2  89.6 167.1  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 482  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 164   NE2                                                    
REMARK 620 2 CLA C 482   NA   82.3                                              
REMARK 620 3 CLA C 482   NB   83.2  92.0                                        
REMARK 620 4 CLA C 482   NC   84.4 166.7  86.8                                  
REMARK 620 5 CLA C 482   ND   85.0  90.2 167.6  88.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 479  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 237   NE2                                                    
REMARK 620 2 CLA C 479   NA   97.6                                              
REMARK 620 3 CLA C 479   NB   95.8  91.1                                        
REMARK 620 4 CLA C 479   NC   97.5 164.9  88.2                                  
REMARK 620 5 CLA C 479   ND   96.5  89.7 167.4  87.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 474  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 251   NE2                                                    
REMARK 620 2 CLA C 474   NA  101.2                                              
REMARK 620 3 CLA C 474   NB   94.1  91.1                                        
REMARK 620 4 CLA C 474   NC   93.5 165.2  88.3                                  
REMARK 620 5 CLA C 474   ND   98.0  90.5 167.3  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 481  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 430   NE2                                                    
REMARK 620 2 CLA C 481   NA   95.4                                              
REMARK 620 3 CLA C 481   NB   99.2  91.0                                        
REMARK 620 4 CLA C 481   NC   98.7 165.9  88.1                                  
REMARK 620 5 CLA C 481   ND   93.1  91.2 167.2  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 441   NE2                                                    
REMARK 620 2 CLA C 477   NA   98.2                                              
REMARK 620 3 CLA C 477   NB   99.2  90.5                                        
REMARK 620 4 CLA C 477   NC   97.6 164.1  88.3                                  
REMARK 620 5 CLA C 477   ND   95.3  89.0 165.4  88.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA C 483  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 444   NE2                                                    
REMARK 620 2 CLA C 483   NA   92.0                                              
REMARK 620 3 CLA C 483   NB  100.6  91.6                                        
REMARK 620 4 CLA C 483   NC  103.2 164.7  87.7                                  
REMARK 620 5 CLA C 483   ND   92.5  90.3 166.7  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA D 356  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 117   NE2                                                    
REMARK 620 2 CLA D 356   NA   92.6                                              
REMARK 620 3 CLA D 356   NB   97.5  92.5                                        
REMARK 620 4 CLA D 356   NC  101.4 165.8  87.8                                  
REMARK 620 5 CLA D 356   ND   94.9  90.6 167.1  86.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA D 354  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D 197   NE2                                                    
REMARK 620 2 CLA D 354   NA  101.3                                              
REMARK 620 3 CLA D 354   NB   95.8  91.5                                        
REMARK 620 4 CLA D 354   NC   93.5 165.1  88.1                                  
REMARK 620 5 CLA D 354   ND   98.0  89.4 165.7  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC E  84  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E  22   NE2                                                    
REMARK 620 2 HEC E  84   NA   89.0                                              
REMARK 620 3 HEC E  84   NB   88.0  89.6                                        
REMARK 620 4 HEC E  84   NC   89.2 177.8  89.0                                  
REMARK 620 5 HEC E  84   ND   91.2  88.5 177.9  92.9                            
REMARK 620 6 HIS F  23   NE2 175.8  91.8  87.9  89.9  92.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC V 138  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS V  41   NE2                                                    
REMARK 620 2 HEC V 138   NA   92.2                                              
REMARK 620 3 HEC V 138   NB   87.5  89.1                                        
REMARK 620 4 HEC V 138   NC   87.9 178.1  89.0                                  
REMARK 620 5 HEC V 138   ND   93.0  86.6 175.7  95.4                            
REMARK 620 6 HIS V  92   NE2 176.7  86.5  89.5  93.3  89.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a2351  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a2118   NE2                                                    
REMARK 620 2 CLA a2351   NA   93.1                                              
REMARK 620 3 CLA a2351   NB  100.1  91.9                                        
REMARK 620 4 CLA a2351   NC  102.3 164.5  87.2                                  
REMARK 620 5 CLA a2351   ND   93.4  90.3 166.2  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a2347  MN4                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a2170   OD2                                                    
REMARK 620 2 OEC a2347   O4  178.2                                              
REMARK 620 3 GLU a2333   OE2  90.4  90.8                                        
REMARK 620 4 GLU a2333   OE1  94.7  87.1  45.0                                  
REMARK 620 5 BCT a2346   O2   90.6  88.1 172.0 142.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a2347  MN2                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU a2189   OE2                                                    
REMARK 620 2 OEC a2347   O1   48.9                                              
REMARK 620 3 OEC a2347   O2  121.3  87.5                                        
REMARK 620 4 OEC a2347   O4  125.2  91.6  85.6                                  
REMARK 620 5 HIS a2332   NE2  69.5 100.4  86.5 165.3                            
REMARK 620 6 GLU a2333   OE2 140.9 155.5  95.8  64.6 103.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA a2348  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a2198   NE2                                                    
REMARK 620 2 CLA a2348   NA  101.1                                              
REMARK 620 3 CLA a2348   NB   97.2  89.8                                        
REMARK 620 4 CLA a2348   NC   95.6 163.3  89.2                                  
REMARK 620 5 CLA a2348   ND   97.9  89.4 164.8  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              FE a2345  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS a2215   NE2                                                    
REMARK 620 2 HIS a2272   NE2  90.4                                              
REMARK 620 3 HIS d2214   NE2 125.1  93.9                                        
REMARK 620 4 HIS d2268   NE2  89.3 172.9  92.1                                  
REMARK 620 5 BCT d2353   O2   83.3  90.8 151.1  82.1                            
REMARK 620 6 BCT d2353   O3  145.8  88.3  89.1  88.0  62.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a2347  MN1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP a2342   OD2                                                    
REMARK 620 2 OEC a2347   O1   99.0                                              
REMARK 620 3 OEC a2347   O2  175.7  85.1                                        
REMARK 620 4 OEC a2347   O3   93.3  91.9  85.1                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a2347  CA1                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA a2344   O                                                      
REMARK 620 2 OEC a2347   O1  102.5                                              
REMARK 620 3 OEC a2347   O3   99.4  64.9                                        
REMARK 620 4 OEC a2347   O4  162.1  64.4  64.5                                  
REMARK 620 5 BCT a2346   O1  119.2 106.0 141.3  77.6                            
REMARK 620 6 BCT a2346   O3  109.5 147.2 101.9  82.8  64.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             OEC a2347  MN3                           
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU c2354   OE1                                                    
REMARK 620 2 OEC a2347   O2   98.4                                              
REMARK 620 3 OEC a2347   O3   74.0  86.4                                        
REMARK 620 4 OEC a2347   O4  165.2  87.6  93.0                                  
REMARK 620 5 GLU c2354   OE2  62.9 122.2 130.2 124.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2520  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2009   NE2                                                    
REMARK 620 2 CLA b2520   NA   93.4                                              
REMARK 620 3 CLA b2520   NB   96.4  91.6                                        
REMARK 620 4 CLA b2520   NC  101.8 164.7  88.3                                  
REMARK 620 5 CLA b2520   ND   96.2  90.3 167.1  86.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2513  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2023   NE2                                                    
REMARK 620 2 CLA b2513   NA   80.8                                              
REMARK 620 3 CLA b2513   NB   84.0  93.5                                        
REMARK 620 4 CLA b2513   NC   86.0 166.6  87.3                                  
REMARK 620 5 CLA b2513   ND   86.5  90.4 169.0  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2512  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2026   NE2                                                    
REMARK 620 2 CLA b2512   NA   80.4                                              
REMARK 620 3 CLA b2512   NB   83.0  93.3                                        
REMARK 620 4 CLA b2512   NC   87.0 167.3  87.1                                  
REMARK 620 5 CLA b2512   ND   86.3  89.9 168.2  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2518  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2100   NE2                                                    
REMARK 620 2 CLA b2518   NA   95.9                                              
REMARK 620 3 CLA b2518   NB   97.9  90.9                                        
REMARK 620 4 CLA b2518   NC   99.4 164.7  87.8                                  
REMARK 620 5 CLA b2518   ND   94.1  90.7 167.7  87.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2525  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2114   NE2                                                    
REMARK 620 2 CLA b2525   NA   98.5                                              
REMARK 620 3 CLA b2525   NB  100.2  92.2                                        
REMARK 620 4 CLA b2525   NC   96.1 165.1  87.9                                  
REMARK 620 5 CLA b2525   ND   92.9  89.3 166.5  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2522  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2142   NE2                                                    
REMARK 620 2 CLA b2522   NA   85.0                                              
REMARK 620 3 CLA b2522   NB   82.3  92.3                                        
REMARK 620 4 CLA b2522   NC   82.6 167.4  88.5                                  
REMARK 620 5 CLA b2522   ND   86.4  89.7 168.2  87.1                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2515  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2157   ND1                                                    
REMARK 620 2 CLA b2515   NA  102.2                                              
REMARK 620 3 CLA b2515   NB   96.4  90.1                                        
REMARK 620 4 CLA b2515   NC   96.5 161.3  87.6                                  
REMARK 620 5 CLA b2515   ND  100.6  89.1 162.7  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2521  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2201   ND1                                                    
REMARK 620 2 CLA b2521   NA   92.7                                              
REMARK 620 3 CLA b2521   NB   77.9  90.7                                        
REMARK 620 4 CLA b2521   NC  103.9 162.7  87.8                                  
REMARK 620 5 CLA b2521   ND  118.4  89.6 163.6  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2517  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2202   NE2                                                    
REMARK 620 2 CLA b2517   NA   96.3                                              
REMARK 620 3 CLA b2517   NB   95.0  91.0                                        
REMARK 620 4 CLA b2517   NC   98.7 165.0  88.0                                  
REMARK 620 5 CLA b2517   ND   97.8  90.2 166.9  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2511  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2216   NE2                                                    
REMARK 620 2 CLA b2511   NA   91.7                                              
REMARK 620 3 CLA b2511   NB   96.4  91.0                                        
REMARK 620 4 CLA b2511   NC  102.6 165.6  88.6                                  
REMARK 620 5 CLA b2511   ND   95.7  90.8 167.7  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2516  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2455   NE2                                                    
REMARK 620 2 CLA b2516   NA  100.3                                              
REMARK 620 3 CLA b2516   NB   95.3  91.5                                        
REMARK 620 4 CLA b2516   NC   94.7 165.0  87.8                                  
REMARK 620 5 CLA b2516   ND   97.4  89.5 166.8  87.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2519  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2466   NE2                                                    
REMARK 620 2 CLA b2519   NA   91.5                                              
REMARK 620 3 CLA b2519   NB  102.8  91.0                                        
REMARK 620 4 CLA b2519   NC  105.3 163.0  88.2                                  
REMARK 620 5 CLA b2519   ND   91.5  88.9 165.7  87.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA b2523  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS b2469   NE2                                                    
REMARK 620 2 CLA b2523   NA   90.6                                              
REMARK 620 3 CLA b2523   NB   99.0  91.9                                        
REMARK 620 4 CLA b2523   NC  104.2 165.0  88.0                                  
REMARK 620 5 CLA b2523   ND   93.7  90.3 167.1  86.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2486  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN c2039   ND2                                                    
REMARK 620 2 CLA c2486   NA   96.8                                              
REMARK 620 3 CLA c2486   NB   78.9  90.2                                        
REMARK 620 4 CLA c2486   NC  100.6 161.7  87.5                                  
REMARK 620 5 CLA c2486   ND  117.0  89.9 163.9  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2478  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2053   NE2                                                    
REMARK 620 2 CLA c2478   NA   82.5                                              
REMARK 620 3 CLA c2478   NB   81.7  92.3                                        
REMARK 620 4 CLA c2478   NC   84.4 166.8  87.6                                  
REMARK 620 5 CLA c2478   ND   86.3  90.2 167.3  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2056   NE2                                                    
REMARK 620 2 CLA c2476   NA   83.5                                              
REMARK 620 3 CLA c2476   NB   82.7  92.5                                        
REMARK 620 4 CLA c2476   NC   82.4 165.7  88.2                                  
REMARK 620 5 CLA c2476   ND   85.9  89.7 168.0  86.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2480  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2118   NE2                                                    
REMARK 620 2 CLA c2480   NA   98.8                                              
REMARK 620 3 CLA c2480   NB   98.3  91.0                                        
REMARK 620 4 CLA c2480   NC   96.0 165.2  87.9                                  
REMARK 620 5 CLA c2480   ND   93.8  90.2 167.5  87.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2484  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2132   NE2                                                    
REMARK 620 2 CLA c2484   NA   95.6                                              
REMARK 620 3 CLA c2484   NB   96.9  92.0                                        
REMARK 620 4 CLA c2484   NC   98.9 165.5  87.6                                  
REMARK 620 5 CLA c2484   ND   95.0  90.0 167.6  87.3                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2482  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2164   NE2                                                    
REMARK 620 2 CLA c2482   NA   83.6                                              
REMARK 620 3 CLA c2482   NB   84.0  91.8                                        
REMARK 620 4 CLA c2482   NC   82.5 166.2  87.0                                  
REMARK 620 5 CLA c2482   ND   83.2  90.2 166.7  87.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2479  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2237   NE2                                                    
REMARK 620 2 CLA c2479   NA   94.3                                              
REMARK 620 3 CLA c2479   NB   96.5  91.1                                        
REMARK 620 4 CLA c2479   NC  100.9 164.7  88.0                                  
REMARK 620 5 CLA c2479   ND   96.0  90.5 167.3  87.2                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2474  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2251   NE2                                                    
REMARK 620 2 CLA c2474   NA  102.8                                              
REMARK 620 3 CLA c2474   NB   96.9  90.7                                        
REMARK 620 4 CLA c2474   NC   92.2 165.0  88.5                                  
REMARK 620 5 CLA c2474   ND   95.4  90.5 167.0  87.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2481  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2430   NE2                                                    
REMARK 620 2 CLA c2481   NA   95.7                                              
REMARK 620 3 CLA c2481   NB   99.7  91.0                                        
REMARK 620 4 CLA c2481   NC   98.2 166.0  88.1                                  
REMARK 620 5 CLA c2481   ND   92.6  91.1 167.3  86.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2441   NE2                                                    
REMARK 620 2 CLA c2477   NA   99.4                                              
REMARK 620 3 CLA c2477   NB   99.2  90.7                                        
REMARK 620 4 CLA c2477   NC   96.4 164.1  88.5                                  
REMARK 620 5 CLA c2477   ND   94.9  89.6 165.7  87.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA c2483  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS c2444   NE2                                                    
REMARK 620 2 CLA c2483   NA   92.2                                              
REMARK 620 3 CLA c2483   NB   97.2  92.0                                        
REMARK 620 4 CLA c2483   NC  103.0 164.7  87.9                                  
REMARK 620 5 CLA c2483   ND   95.6  89.9 167.0  86.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA d2357  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS d2117   NE2                                                    
REMARK 620 2 CLA d2357   NA   93.4                                              
REMARK 620 3 CLA d2357   NB   98.1  92.5                                        
REMARK 620 4 CLA d2357   NC  101.4 165.0  87.7                                  
REMARK 620 5 CLA d2357   ND   95.0  90.1 166.5  86.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             CLA d2354  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS d2197   NE2                                                    
REMARK 620 2 CLA d2354   NA  101.1                                              
REMARK 620 3 CLA d2354   NB   95.3  91.5                                        
REMARK 620 4 CLA d2354   NC   93.8 165.1  88.0                                  
REMARK 620 5 CLA d2354   ND   98.1  89.4 166.2  87.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC e2084  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS e2022   NE2                                                    
REMARK 620 2 HEC e2084   NA   88.0                                              
REMARK 620 3 HEC e2084   NB   92.6  89.8                                        
REMARK 620 4 HEC e2084   NC   91.3 178.9  89.4                                  
REMARK 620 5 HEC e2084   ND   87.7  89.0 178.8  91.8                            
REMARK 620 6 HIS f2023   NE2 177.9  91.2  89.2  89.6  90.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEC v2138  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS v2041   NE2                                                    
REMARK 620 2 HEC v2138   NA   90.3                                              
REMARK 620 3 HEC v2138   NB   86.6  89.7                                        
REMARK 620 4 HEC v2138   NC   89.3 177.9  88.2                                  
REMARK 620 5 HEC v2138   ND   93.8  88.3 177.9  93.8                            
REMARK 620 6 HIS v2092   NE2 177.1  88.3  90.8  92.1  88.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE A 345                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT A 346                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT D 353                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FE a 2345                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT a 2346                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCT d 2353                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC A 347                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 348                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 354                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 349                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 350                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO A 351                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO D 355                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA A 352                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA D 356                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 474                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 475                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 485                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 511                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 512                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 513                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 514                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 515                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 516                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 517                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 518                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 519                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 520                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 521                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 522                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 523                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 524                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 525                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC E 84                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC V 138                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 D 357                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 A 353                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 486                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT B 526                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA B 527                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA C 487                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR F 48                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 488                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR K 50                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR C 489                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 528                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR J 53                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR B 529                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE OEC a 2347                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 2348                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 2354                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 2355                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 2349                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO a 2350                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PHO d 2356                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA a 2351                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA d 2357                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2474                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2475                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2476                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2477                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2478                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2479                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2480                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2481                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2482                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2483                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2484                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2485                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2511                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2512                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2513                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2514                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2515                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2516                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2517                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2518                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2519                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2520                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2521                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2522                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2523                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2524                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2525                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC e 2084                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEC v 2138                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 d 2358                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PL9 a 2352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2486                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LMT d 2359                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA b 2526                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CLA c 2487                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR d 2360                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 2488                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR k 2050                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR c 2489                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 2527                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR j 2053                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: LC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BCR b 2528                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1IZL   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1FE1   RELATED DB: PDB                                   
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 BECAUSE THE ELECTRON DENSITY FOR THE TWO N CHAINS                    
REMARK 999 WAS POOR, THE AUTHORS WERE UNABLE TO ASSIGN SIDE                     
REMARK 999 CHAINS.                                                              
DBREF  1S5L A    1   344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  1S5L B    1   510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  1S5L C   14   473  UNP    Q8DIF8   Q8DIF8_THEEB     2    461             
DBREF  1S5L D    1   352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  1S5L E    0    83  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  1S5L F    0    44  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  1S5L H    0    65  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  1S5L I    1    38  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  1S5L J    1    40  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  1S5L K    1    37  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  1S5L L    1    37  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  1S5L M    1    36  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  1S5L O    1   246  UNP    P0A431   PSBO_THEEB      27    272             
DBREF  1S5L T    1    32  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  1S5L U    1   134  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  1S5L V    1   137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  1S5L X   11    50  UNP    Q9F1R6   PSBX_THEEB       2     41             
DBREF  1S5L Z    1    62  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  1S5L a 2001  2344  UNP    P0A444   PSBA1_THEEB      1    344             
DBREF  1S5L b 2001  2510  UNP    Q8DIQ1   Q8DIQ1_THEEB     1    510             
DBREF  1S5L c 2014  2473  UNP    Q8DIF8   Q8DIF8_THEEB     2    461             
DBREF  1S5L d 2001  2352  UNP    Q8CM25   PSBD_THEEB       1    352             
DBREF  1S5L e 2000  2083  UNP    Q8DIP0   PSBE_THEEB       1     84             
DBREF  1S5L f 2000  2044  UNP    Q8DIN9   PSBF_THEEB       1     45             
DBREF  1S5L h 2000  2065  UNP    Q8DJ43   PSBH_THEEB       1     66             
DBREF  1S5L i 2001  2038  UNP    Q8DJZ6   PSBI_THEEB       1     38             
DBREF  1S5L j 2001  2040  UNP    P59087   PSBJ_THEEB       1     40             
DBREF  1S5L k 2001  2037  UNP    Q9F1K9   PSBK_THEEB      10     46             
DBREF  1S5L l 2001  2037  UNP    Q8DIN8   PSBL_THEEB       1     37             
DBREF  1S5L m 2001  2036  UNP    Q8DHA7   PSBM_THEEB       1     36             
DBREF  1S5L o 2001  2246  UNP    P0A431   PSBO_THEEB      27    272             
DBREF  1S5L t 2001  2032  UNP    Q8DIQ0   PSBT_THEEB       1     32             
DBREF  1S5L u 2001  2134  UNP    Q9F1L5   PSBU_THEEB       1    134             
DBREF  1S5L v 2001  2137  UNP    P0A386   CY550_THEEB     27    163             
DBREF  1S5L x 2011  2050  UNP    Q9F1R6   PSBX_THEEB       2     41             
DBREF  1S5L z 2001  2062  UNP    Q8DHJ2   PSBZ_THEEB       1     62             
DBREF  1S5L N    1    37  PDB    1S5L     1S5L             1     37             
DBREF  1S5L n 2001  2037  PDB    1S5L     1S5L          2001   2037             
SEQADV 1S5L MET C    1  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L LYS C    2  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L THR C    3  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L LEU C    4  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L SER C    5  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L SER C    6  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L GLN C    7  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L LYS C    8  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L ARG C    9  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L TYR C   10  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L SER C   11  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L PRO C   12  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L VAL C   13  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L MET X    1  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L ILE X    2  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L GLN X    3  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L SER X    4  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L ALA X    5  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L SER X    6  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L SER X    7  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L LEU X    8  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L LEU X    9  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L LEU X   10  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L MET c 2001  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L LYS c 2002  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L THR c 2003  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L LEU c 2004  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L SER c 2005  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L SER c 2006  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L GLN c 2007  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L LYS c 2008  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L ARG c 2009  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L TYR c 2010  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L SER c 2011  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L PRO c 2012  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L VAL c 2013  UNP  Q8DIF8              INSERTION                      
SEQADV 1S5L MET x 2001  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L ILE x 2002  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L GLN x 2003  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L SER x 2004  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L ALA x 2005  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L SER x 2006  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L SER x 2007  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L LEU x 2008  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L LEU x 2009  UNP  Q9F1R6              INSERTION                      
SEQADV 1S5L LEU x 2010  UNP  Q9F1R6              INSERTION                      
SEQRES   1 A  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 A  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 A  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 A  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 A  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 A  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 A  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 A  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 A  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 A  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 A  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 A  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 A  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 A  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 A  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 A  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 A  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 A  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 A  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 A  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 A  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 A  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 A  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 A  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 A  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 A  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 A  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 B  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 B  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 B  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 B  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 B  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 B  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 B  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 B  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 B  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 B  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 B  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 B  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 B  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 B  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 B  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 B  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 B  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 B  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 B  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 B  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 B  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 B  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 B  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 B  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 B  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 B  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 B  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 B  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 B  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 B  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 B  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 B  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 B  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 B  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 B  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 B  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 B  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 B  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 B  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 B  510  GLU ALA VAL                                                  
SEQRES   1 C  473  MET LYS THR LEU SER SER GLN LYS ARG TYR SER PRO VAL          
SEQRES   2 C  473  VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN ARG          
SEQRES   3 C  473  ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY ASN          
SEQRES   4 C  473  ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY ALA          
SEQRES   5 C  473  HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA GLY          
SEQRES   6 C  473  ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO GLU          
SEQRES   7 C  473  LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO HIS          
SEQRES   8 C  473  ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY GLU          
SEQRES   9 C  473  VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL VAL          
SEQRES  10 C  473  HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY VAL          
SEQRES  11 C  473  TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU TYR          
SEQRES  12 C  473  SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN LYS          
SEQRES  13 C  473  MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU GLY          
SEQRES  14 C  473  ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE PHE          
SEQRES  15 C  473  GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY ASP          
SEQRES  16 C  473  VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG VAL          
SEQRES  17 C  473  ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY GLU          
SEQRES  18 C  473  GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL VAL          
SEQRES  19 C  473  GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA GLY          
SEQRES  20 C  473  GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP ALA          
SEQRES  21 C  473  ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU SER          
SEQRES  22 C  473  TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE ALA          
SEQRES  23 C  473  THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO SER          
SEQRES  24 C  473  GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN ALA          
SEQRES  25 C  473  GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU GLY          
SEQRES  26 C  473  ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU GLY          
SEQRES  27 C  473  LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE PHE          
SEQRES  28 C  473  GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY PRO          
SEQRES  29 C  473  TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP LEU          
SEQRES  30 C  473  ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU ARG          
SEQRES  31 C  473  ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY SER          
SEQRES  32 C  473  LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN SER          
SEQRES  33 C  473  VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR SER          
SEQRES  34 C  473  HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS LEU          
SEQRES  35 C  473  TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY PHE          
SEQRES  36 C  473  GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU SER          
SEQRES  37 C  473  MET PRO SER LEU ASP                                          
SEQRES   1 D  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 D  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 D  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 D  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 D  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 D  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 D  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 D  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 D  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 D  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 D  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 D  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 D  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 D  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 D  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 D  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 D  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 D  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 D  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 D  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 D  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 D  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 D  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 D  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 D  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 D  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 D  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 D  352  LEU                                                          
SEQRES   1 E   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 E   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 E   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 E   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 E   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 E   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 E   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 F   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 F   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 F   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 F   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 H   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 H   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 H   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 H   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 H   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 H   66  GLY                                                          
SEQRES   1 I   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 I   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 I   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 J   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 J   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 J   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 J   40  LEU                                                          
SEQRES   1 K   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   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 L   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 L   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 M   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 M   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 M   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 O  246  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   2 O  246  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   3 O  246  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   4 O  246  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   5 O  246  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   6 O  246  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   7 O  246  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES   8 O  246  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES   9 O  246  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  10 O  246  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  11 O  246  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  12 O  246  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  13 O  246  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  14 O  246  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  15 O  246  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  16 O  246  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  17 O  246  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  18 O  246  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  19 O  246  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 T   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 T   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 T   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 U  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 U  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 U  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 U  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 U  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 U  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 U  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 U  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 U  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 U  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 U  134  GLY LEU TYR LYS                                              
SEQRES   1 V  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 X   50  MET ILE GLN SER ALA SER SER LEU LEU LEU THR ILE THR          
SEQRES   2 X   50  PRO SER LEU LYS GLY PHE PHE ILE GLY LEU LEU SER GLY          
SEQRES   3 X   50  ALA VAL VAL LEU GLY LEU THR PHE ALA VAL LEU ILE ALA          
SEQRES   4 X   50  ILE SER GLN ILE ASP LYS VAL GLN ARG SER LEU                  
SEQRES   1 N   37  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 N   37  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 N   37  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK                  
SEQRES   1 Z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 Z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 Z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 Z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 Z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
SEQRES   1 a  344  MET THR THR THR LEU GLN ARG ARG GLU SER ALA ASN LEU          
SEQRES   2 a  344  TRP GLU ARG PHE CYS ASN TRP VAL THR SER THR ASP ASN          
SEQRES   3 a  344  ARG LEU TYR VAL GLY TRP PHE GLY VAL ILE MET ILE PRO          
SEQRES   4 a  344  THR LEU LEU ALA ALA THR ILE CYS PHE VAL ILE ALA PHE          
SEQRES   5 a  344  ILE ALA ALA PRO PRO VAL ASP ILE ASP GLY ILE ARG GLU          
SEQRES   6 a  344  PRO VAL SER GLY SER LEU LEU TYR GLY ASN ASN ILE ILE          
SEQRES   7 a  344  THR GLY ALA VAL VAL PRO SER SER ASN ALA ILE GLY LEU          
SEQRES   8 a  344  HIS PHE TYR PRO ILE TRP GLU ALA ALA SER LEU ASP GLU          
SEQRES   9 a  344  TRP LEU TYR ASN GLY GLY PRO TYR GLN LEU ILE ILE PHE          
SEQRES  10 a  344  HIS PHE LEU LEU GLY ALA SER CYS TYR MET GLY ARG GLN          
SEQRES  11 a  344  TRP GLU LEU SER TYR ARG LEU GLY MET ARG PRO TRP ILE          
SEQRES  12 a  344  CYS VAL ALA TYR SER ALA PRO LEU ALA SER ALA PHE ALA          
SEQRES  13 a  344  VAL PHE LEU ILE TYR PRO ILE GLY GLN GLY SER PHE SER          
SEQRES  14 a  344  ASP GLY MET PRO LEU GLY ILE SER GLY THR PHE ASN PHE          
SEQRES  15 a  344  MET ILE VAL PHE GLN ALA GLU HIS ASN ILE LEU MET HIS          
SEQRES  16 a  344  PRO PHE HIS GLN LEU GLY VAL ALA GLY VAL PHE GLY GLY          
SEQRES  17 a  344  ALA LEU PHE CYS ALA MET HIS GLY SER LEU VAL THR SER          
SEQRES  18 a  344  SER LEU ILE ARG GLU THR THR GLU THR GLU SER ALA ASN          
SEQRES  19 a  344  TYR GLY TYR LYS PHE GLY GLN GLU GLU GLU THR TYR ASN          
SEQRES  20 a  344  ILE VAL ALA ALA HIS GLY TYR PHE GLY ARG LEU ILE PHE          
SEQRES  21 a  344  GLN TYR ALA SER PHE ASN ASN SER ARG SER LEU HIS PHE          
SEQRES  22 a  344  PHE LEU ALA ALA TRP PRO VAL VAL GLY VAL TRP PHE THR          
SEQRES  23 a  344  ALA LEU GLY ILE SER THR MET ALA PHE ASN LEU ASN GLY          
SEQRES  24 a  344  PHE ASN PHE ASN HIS SER VAL ILE ASP ALA LYS GLY ASN          
SEQRES  25 a  344  VAL ILE ASN THR TRP ALA ASP ILE ILE ASN ARG ALA ASN          
SEQRES  26 a  344  LEU GLY MET GLU VAL MET HIS GLU ARG ASN ALA HIS ASN          
SEQRES  27 a  344  PHE PRO LEU ASP LEU ALA                                      
SEQRES   1 b  510  MET GLY LEU PRO TRP TYR ARG VAL HIS THR VAL LEU ILE          
SEQRES   2 b  510  ASN ASP PRO GLY ARG LEU ILE ALA ALA HIS LEU MET HIS          
SEQRES   3 b  510  THR ALA LEU VAL ALA GLY TRP ALA GLY SER MET ALA LEU          
SEQRES   4 b  510  TYR GLU LEU ALA THR PHE ASP PRO SER ASP PRO VAL LEU          
SEQRES   5 b  510  ASN PRO MET TRP ARG GLN GLY MET PHE VAL LEU PRO PHE          
SEQRES   6 b  510  MET ALA ARG LEU GLY VAL THR GLY SER TRP SER GLY TRP          
SEQRES   7 b  510  SER ILE THR GLY GLU THR GLY ILE ASP PRO GLY PHE TRP          
SEQRES   8 b  510  SER PHE GLU GLY VAL ALA LEU ALA HIS ILE VAL LEU SER          
SEQRES   9 b  510  GLY LEU LEU PHE LEU ALA ALA CYS TRP HIS TRP VAL TYR          
SEQRES  10 b  510  TRP ASP LEU GLU LEU PHE ARG ASP PRO ARG THR GLY GLU          
SEQRES  11 b  510  PRO ALA LEU ASP LEU PRO LYS MET PHE GLY ILE HIS LEU          
SEQRES  12 b  510  PHE LEU ALA GLY LEU LEU CYS PHE GLY PHE GLY ALA PHE          
SEQRES  13 b  510  HIS LEU THR GLY LEU PHE GLY PRO GLY MET TRP VAL SER          
SEQRES  14 b  510  ASP PRO TYR GLY LEU THR GLY SER VAL GLN PRO VAL ALA          
SEQRES  15 b  510  PRO GLU TRP GLY PRO ASP GLY PHE ASN PRO TYR ASN PRO          
SEQRES  16 b  510  GLY GLY VAL VAL ALA HIS HIS ILE ALA ALA GLY ILE VAL          
SEQRES  17 b  510  GLY ILE ILE ALA GLY LEU PHE HIS ILE LEU VAL ARG PRO          
SEQRES  18 b  510  PRO GLN ARG LEU TYR LYS ALA LEU ARG MET GLY ASN ILE          
SEQRES  19 b  510  GLU THR VAL LEU SER SER SER ILE ALA ALA VAL PHE PHE          
SEQRES  20 b  510  ALA ALA PHE VAL VAL ALA GLY THR MET TRP TYR GLY SER          
SEQRES  21 b  510  ALA THR THR PRO ILE GLU LEU PHE GLY PRO THR ARG TYR          
SEQRES  22 b  510  GLN TRP ASP SER SER TYR PHE GLN GLN GLU ILE ASN ARG          
SEQRES  23 b  510  ARG VAL GLN ALA SER LEU ALA SER GLY ALA THR LEU GLU          
SEQRES  24 b  510  GLU ALA TRP SER ALA ILE PRO GLU LYS LEU ALA PHE TYR          
SEQRES  25 b  510  ASP TYR ILE GLY ASN ASN PRO ALA LYS GLY GLY LEU PHE          
SEQRES  26 b  510  ARG THR GLY PRO MET ASN LYS GLY ASP GLY ILE ALA GLN          
SEQRES  27 b  510  ALA TRP LYS GLY HIS ALA VAL PHE ARG ASN LYS GLU GLY          
SEQRES  28 b  510  GLU GLU LEU PHE VAL ARG ARG MET PRO ALA PHE PHE GLU          
SEQRES  29 b  510  SER PHE PRO VAL ILE LEU THR ASP LYS ASN GLY VAL VAL          
SEQRES  30 b  510  LYS ALA ASP ILE PRO PHE ARG ARG ALA GLU SER LYS TYR          
SEQRES  31 b  510  SER PHE GLU GLN GLN GLY VAL THR VAL SER PHE TYR GLY          
SEQRES  32 b  510  GLY GLU LEU ASN GLY GLN THR PHE THR ASP PRO PRO THR          
SEQRES  33 b  510  VAL LYS SER TYR ALA ARG LYS ALA ILE PHE GLY GLU ILE          
SEQRES  34 b  510  PHE GLU PHE ASP THR GLU THR LEU ASN SER ASP GLY ILE          
SEQRES  35 b  510  PHE ARG THR SER PRO ARG GLY TRP PHE THR PHE ALA HIS          
SEQRES  36 b  510  ALA VAL PHE ALA LEU LEU PHE PHE PHE GLY HIS ILE TRP          
SEQRES  37 b  510  HIS GLY ALA ARG THR LEU PHE ARG ASP VAL PHE SER GLY          
SEQRES  38 b  510  ILE ASP PRO GLU LEU SER PRO GLU GLN VAL GLU TRP GLY          
SEQRES  39 b  510  PHE TYR GLN LYS VAL GLY ASP VAL THR THR ARG ARG LYS          
SEQRES  40 b  510  GLU ALA VAL                                                  
SEQRES   1 c  473  MET LYS THR LEU SER SER GLN LYS ARG TYR SER PRO VAL          
SEQRES   2 c  473  VAL THR LEU SER SER ASN SER ILE PHE ALA THR ASN ARG          
SEQRES   3 c  473  ASP GLN GLU SER SER GLY PHE ALA TRP TRP ALA GLY ASN          
SEQRES   4 c  473  ALA ARG LEU ILE ASN LEU SER GLY LYS LEU LEU GLY ALA          
SEQRES   5 c  473  HIS VAL ALA HIS ALA GLY LEU ILE VAL PHE TRP ALA GLY          
SEQRES   6 c  473  ALA MET THR LEU PHE GLU LEU ALA HIS PHE ILE PRO GLU          
SEQRES   7 c  473  LYS PRO MET TYR GLU GLN GLY LEU ILE LEU ILE PRO HIS          
SEQRES   8 c  473  ILE ALA THR LEU GLY TRP GLY VAL GLY PRO GLY GLY GLU          
SEQRES   9 c  473  VAL VAL ASP THR PHE PRO PHE PHE VAL VAL GLY VAL VAL          
SEQRES  10 c  473  HIS LEU ILE SER SER ALA VAL LEU GLY PHE GLY GLY VAL          
SEQRES  11 c  473  TYR HIS ALA ILE ARG GLY PRO GLU THR LEU GLU GLU TYR          
SEQRES  12 c  473  SER SER PHE PHE GLY TYR ASP TRP LYS ASP LYS ASN LYS          
SEQRES  13 c  473  MET THR THR ILE LEU GLY PHE HIS LEU ILE VAL LEU GLY          
SEQRES  14 c  473  ILE GLY ALA LEU LEU LEU VAL ALA LYS ALA MET PHE PHE          
SEQRES  15 c  473  GLY GLY LEU TYR ASP THR TRP ALA PRO GLY GLY GLY ASP          
SEQRES  16 c  473  VAL ARG VAL ILE THR ASN PRO THR LEU ASP PRO ARG VAL          
SEQRES  17 c  473  ILE PHE GLY TYR LEU LEU LYS SER PRO PHE GLY GLY GLU          
SEQRES  18 c  473  GLY TRP ILE VAL SER VAL ASN ASN LEU GLU ASP VAL VAL          
SEQRES  19 c  473  GLY GLY HIS ILE TRP ILE GLY LEU ILE CYS ILE ALA GLY          
SEQRES  20 c  473  GLY ILE TRP HIS ILE LEU THR THR PRO PHE GLY TRP ALA          
SEQRES  21 c  473  ARG ARG ALA PHE ILE TRP SER GLY GLU ALA TYR LEU SER          
SEQRES  22 c  473  TYR SER LEU GLY ALA LEU SER MET MET GLY PHE ILE ALA          
SEQRES  23 c  473  THR CYS PHE VAL TRP PHE ASN ASN THR VAL TYR PRO SER          
SEQRES  24 c  473  GLU PHE TYR GLY PRO THR GLY PRO GLU ALA SER GLN ALA          
SEQRES  25 c  473  GLN ALA MET THR PHE LEU ILE ARG ASP GLN LYS LEU GLY          
SEQRES  26 c  473  ALA ASN VAL GLY SER ALA GLN GLY PRO THR GLY LEU GLY          
SEQRES  27 c  473  LYS TYR LEU MET ARG SER PRO THR GLY GLU ILE ILE PHE          
SEQRES  28 c  473  GLY GLY GLU THR MET ARG PHE TRP ASP PHE ARG GLY PRO          
SEQRES  29 c  473  TRP LEU GLU PRO LEU ARG GLY PRO ASN GLY LEU ASP LEU          
SEQRES  30 c  473  ASN LYS ILE LYS ASN ASP ILE GLN PRO TRP GLN GLU ARG          
SEQRES  31 c  473  ARG ALA ALA GLU TYR MET THR HIS ALA PRO LEU GLY SER          
SEQRES  32 c  473  LEU ASN SER VAL GLY GLY VAL ALA THR GLU ILE ASN SER          
SEQRES  33 c  473  VAL ASN PHE VAL SER PRO ARG SER TRP LEU ALA THR SER          
SEQRES  34 c  473  HIS PHE VAL LEU ALA PHE PHE PHE LEU VAL GLY HIS LEU          
SEQRES  35 c  473  TRP HIS ALA GLY ARG ALA ARG ALA ALA ALA ALA GLY PHE          
SEQRES  36 c  473  GLU LYS GLY ILE ASP ARG GLU SER GLU PRO VAL LEU SER          
SEQRES  37 c  473  MET PRO SER LEU ASP                                          
SEQRES   1 d  352  MET THR ILE ALA ILE GLY ARG ALA PRO ALA GLU ARG GLY          
SEQRES   2 d  352  TRP PHE ASP ILE LEU ASP ASP TRP LEU LYS ARG ASP ARG          
SEQRES   3 d  352  PHE VAL PHE VAL GLY TRP SER GLY ILE LEU LEU PHE PRO          
SEQRES   4 d  352  CYS ALA TYR LEU ALA LEU GLY GLY TRP LEU THR GLY THR          
SEQRES   5 d  352  THR PHE VAL THR SER TRP TYR THR HIS GLY LEU ALA SER          
SEQRES   6 d  352  SER TYR LEU GLU GLY CYS ASN PHE LEU THR VAL ALA VAL          
SEQRES   7 d  352  SER THR PRO ALA ASN SER MET GLY HIS SER LEU LEU LEU          
SEQRES   8 d  352  LEU TRP GLY PRO GLU ALA GLN GLY ASP PHE THR ARG TRP          
SEQRES   9 d  352  CYS GLN LEU GLY GLY LEU TRP THR PHE ILE ALA LEU HIS          
SEQRES  10 d  352  GLY ALA PHE GLY LEU ILE GLY PHE MET LEU ARG GLN PHE          
SEQRES  11 d  352  GLU ILE ALA ARG LEU VAL GLY VAL ARG PRO TYR ASN ALA          
SEQRES  12 d  352  ILE ALA PHE SER ALA PRO ILE ALA VAL PHE VAL SER VAL          
SEQRES  13 d  352  PHE LEU ILE TYR PRO LEU GLY GLN SER SER TRP PHE PHE          
SEQRES  14 d  352  ALA PRO SER PHE GLY VAL ALA ALA ILE PHE ARG PHE LEU          
SEQRES  15 d  352  LEU PHE PHE GLN GLY PHE HIS ASN TRP THR LEU ASN PRO          
SEQRES  16 d  352  PHE HIS MET MET GLY VAL ALA GLY VAL LEU GLY GLY ALA          
SEQRES  17 d  352  LEU LEU CYS ALA ILE HIS GLY ALA THR VAL GLU ASN THR          
SEQRES  18 d  352  LEU PHE GLN ASP GLY GLU GLY ALA SER THR PHE ARG ALA          
SEQRES  19 d  352  PHE ASN PRO THR GLN ALA GLU GLU THR TYR SER MET VAL          
SEQRES  20 d  352  THR ALA ASN ARG PHE TRP SER GLN ILE PHE GLY ILE ALA          
SEQRES  21 d  352  PHE SER ASN LYS ARG TRP LEU HIS PHE PHE MET LEU PHE          
SEQRES  22 d  352  VAL PRO VAL THR GLY LEU TRP MET SER ALA ILE GLY VAL          
SEQRES  23 d  352  VAL GLY LEU ALA LEU ASN LEU ARG SER TYR ASP PHE ILE          
SEQRES  24 d  352  SER GLN GLU ILE ARG ALA ALA GLU ASP PRO GLU PHE GLU          
SEQRES  25 d  352  THR PHE TYR THR LYS ASN LEU LEU LEU ASN GLU GLY ILE          
SEQRES  26 d  352  ARG ALA TRP MET ALA PRO GLN ASP GLN PRO HIS GLU ASN          
SEQRES  27 d  352  PHE VAL PHE PRO GLU GLU VAL LEU PRO ARG GLY ASN ALA          
SEQRES  28 d  352  LEU                                                          
SEQRES   1 e   84  MET ALA GLY THR THR GLY GLU ARG PRO PHE SER ASP ILE          
SEQRES   2 e   84  ILE THR SER VAL ARG TYR TRP VAL ILE HIS SER ILE THR          
SEQRES   3 e   84  ILE PRO ALA LEU PHE ILE ALA GLY TRP LEU PHE VAL SER          
SEQRES   4 e   84  THR GLY LEU ALA TYR ASP VAL PHE GLY THR PRO ARG PRO          
SEQRES   5 e   84  ASP SER TYR TYR ALA GLN GLU GLN ARG SER ILE PRO LEU          
SEQRES   6 e   84  VAL THR ASP ARG PHE GLU ALA LYS GLN GLN VAL GLU THR          
SEQRES   7 e   84  PHE LEU GLU GLN LEU LYS                                      
SEQRES   1 f   45  MET THR SER ASN THR PRO ASN GLN GLU PRO VAL SER TYR          
SEQRES   2 f   45  PRO ILE PHE THR VAL ARG TRP VAL ALA VAL HIS THR LEU          
SEQRES   3 f   45  ALA VAL PRO THR ILE PHE PHE LEU GLY ALA ILE ALA ALA          
SEQRES   4 f   45  MET GLN PHE ILE GLN ARG                                      
SEQRES   1 h   66  MET ALA ARG ARG THR TRP LEU GLY ASP ILE LEU ARG PRO          
SEQRES   2 h   66  LEU ASN SER GLU TYR GLY LYS VAL ALA PRO GLY TRP GLY          
SEQRES   3 h   66  THR THR PRO LEU MET ALA VAL PHE MET GLY LEU PHE LEU          
SEQRES   4 h   66  VAL PHE LEU LEU ILE ILE LEU GLU ILE TYR ASN SER THR          
SEQRES   5 h   66  LEU ILE LEU ASP GLY VAL ASN VAL SER TRP LYS ALA LEU          
SEQRES   6 h   66  GLY                                                          
SEQRES   1 i   38  MET GLU THR LEU LYS ILE THR VAL TYR ILE VAL VAL THR          
SEQRES   2 i   38  PHE PHE VAL LEU LEU PHE VAL PHE GLY PHE LEU SER GLY          
SEQRES   3 i   38  ASP PRO ALA ARG ASN PRO LYS ARG LYS ASP LEU GLU              
SEQRES   1 j   40  MET MET SER GLU GLY GLY ARG ILE PRO LEU TRP ILE VAL          
SEQRES   2 j   40  ALA THR VAL ALA GLY MET GLY VAL ILE VAL ILE VAL GLY          
SEQRES   3 j   40  LEU PHE PHE TYR GLY ALA TYR ALA GLY LEU GLY SER SER          
SEQRES   4 j   40  LEU                                                          
SEQRES   1 k   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   37  MET GLU PRO ASN PRO ASN ARG GLN PRO VAL GLU LEU ASN          
SEQRES   2 l   37  ARG THR SER LEU TYR LEU GLY LEU LEU LEU ILE LEU VAL          
SEQRES   3 l   37  LEU ALA LEU LEU PHE SER SER TYR PHE PHE ASN                  
SEQRES   1 m   36  MET GLU VAL ASN GLN LEU GLY LEU ILE ALA THR ALA LEU          
SEQRES   2 m   36  PHE VAL LEU VAL PRO SER VAL PHE LEU ILE ILE LEU TYR          
SEQRES   3 m   36  VAL GLN THR GLU SER GLN GLN LYS SER SER                      
SEQRES   1 o  246  ALA LYS GLN THR LEU THR TYR ASP ASP ILE VAL GLY THR          
SEQRES   2 o  246  GLY LEU ALA ASN LYS CYS PRO THR LEU ASP ASP THR ALA          
SEQRES   3 o  246  ARG GLY ALA TYR PRO ILE ASP SER SER GLN THR TYR ARG          
SEQRES   4 o  246  ILE ALA ARG LEU CYS LEU GLN PRO THR THR PHE LEU VAL          
SEQRES   5 o  246  LYS GLU GLU PRO LYS ASN LYS ARG GLN GLU ALA GLU PHE          
SEQRES   6 o  246  VAL PRO THR LYS LEU VAL THR ARG GLU THR THR SER LEU          
SEQRES   7 o  246  ASP GLN ILE GLN GLY GLU LEU LYS VAL ASN SER ASP GLY          
SEQRES   8 o  246  SER LEU THR PHE VAL GLU GLU ASP GLY ILE ASP PHE GLN          
SEQRES   9 o  246  PRO VAL THR VAL GLN MET ALA GLY GLY GLU ARG ILE PRO          
SEQRES  10 o  246  LEU LEU PHE THR VAL LYS ASN LEU VAL ALA SER THR GLN          
SEQRES  11 o  246  PRO ASN VAL THR SER ILE THR THR SER THR ASP PHE LYS          
SEQRES  12 o  246  GLY GLU PHE ASN VAL PRO SER TYR ARG THR ALA ASN PHE          
SEQRES  13 o  246  LEU ASP PRO LYS GLY ARG GLY LEU ALA SER GLY TYR ASP          
SEQRES  14 o  246  SER ALA ILE ALA LEU PRO GLN ALA LYS GLU GLU GLU LEU          
SEQRES  15 o  246  ALA ARG ALA ASN VAL LYS ARG PHE SER LEU THR LYS GLY          
SEQRES  16 o  246  GLN ILE SER LEU ASN VAL ALA LYS VAL ASP GLY ARG THR          
SEQRES  17 o  246  GLY GLU ILE ALA GLY THR PHE GLU SER GLU GLN LEU SER          
SEQRES  18 o  246  ASP ASP ASP MET GLY ALA HIS GLU PRO HIS GLU VAL LYS          
SEQRES  19 o  246  ILE GLN GLY VAL PHE TYR ALA SER ILE GLU PRO ALA              
SEQRES   1 t   32  MET GLU THR ILE THR TYR VAL PHE ILE PHE ALA CYS ILE          
SEQRES   2 t   32  ILE ALA LEU PHE PHE PHE ALA ILE PHE PHE ARG GLU PRO          
SEQRES   3 t   32  PRO ARG ILE THR LYS LYS                                      
SEQRES   1 u  134  MET GLN ARG LEU GLY ARG TRP LEU ALA LEU ALA TYR PHE          
SEQRES   2 u  134  VAL GLY VAL SER LEU LEU GLY TRP ILE ASN TRP SER ALA          
SEQRES   3 u  134  PRO THR LEU ALA ALA THR ALA SER THR GLU GLU GLU LEU          
SEQRES   4 u  134  VAL ASN VAL VAL ASP GLU LYS LEU GLY THR ALA TYR GLY          
SEQRES   5 u  134  GLU LYS ILE ASP LEU ASN ASN THR ASN ILE ALA ALA PHE          
SEQRES   6 u  134  ILE GLN TYR ARG GLY LEU TYR PRO THR LEU ALA LYS LEU          
SEQRES   7 u  134  ILE VAL LYS ASN ALA PRO TYR GLU SER VAL GLU ASP VAL          
SEQRES   8 u  134  LEU ASN ILE PRO GLY LEU THR GLU ARG GLN LYS GLN ILE          
SEQRES   9 u  134  LEU ARG GLU ASN LEU GLU HIS PHE THR VAL THR GLU VAL          
SEQRES  10 u  134  GLU THR ALA LEU VAL GLU GLY GLY ASP ARG TYR ASN ASN          
SEQRES  11 u  134  GLY LEU TYR LYS                                              
SEQRES   1 v  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 x   50  MET ILE GLN SER ALA SER SER LEU LEU LEU THR ILE THR          
SEQRES   2 x   50  PRO SER LEU LYS GLY PHE PHE ILE GLY LEU LEU SER GLY          
SEQRES   3 x   50  ALA VAL VAL LEU GLY LEU THR PHE ALA VAL LEU ILE ALA          
SEQRES   4 x   50  ILE SER GLN ILE ASP LYS VAL GLN ARG SER LEU                  
SEQRES   1 n   37  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   2 n   37  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK          
SEQRES   3 n   37  UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK UNK                  
SEQRES   1 z   62  MET THR ILE LEU PHE GLN LEU ALA LEU ALA ALA LEU VAL          
SEQRES   2 z   62  ILE LEU SER PHE VAL MET VAL ILE GLY VAL PRO VAL ALA          
SEQRES   3 z   62  TYR ALA SER PRO GLN ASP TRP ASP ARG SER LYS GLN LEU          
SEQRES   4 z   62  ILE PHE LEU GLY SER GLY LEU TRP ILE ALA LEU VAL LEU          
SEQRES   5 z   62  VAL VAL GLY VAL LEU ASN PHE PHE VAL VAL                      
HET     FE  A 345       1                                                       
HET    BCT  A 346       4                                                       
HET    OEC  A 347       9                                                       
HET    CLA  A 348      65                                                       
HET    CLA  A 349      65                                                       
HET    CLA  A 350      65                                                       
HET    PHO  A 351      64                                                       
HET    CLA  A 352      65                                                       
HET    PL9  A 353      45                                                       
HET    CLA  B 511      65                                                       
HET    CLA  B 512      65                                                       
HET    CLA  B 513      65                                                       
HET    CLA  B 514      65                                                       
HET    CLA  B 515      65                                                       
HET    CLA  B 516      65                                                       
HET    CLA  B 517      65                                                       
HET    CLA  B 518      65                                                       
HET    CLA  B 519      65                                                       
HET    CLA  B 520      65                                                       
HET    CLA  B 521      65                                                       
HET    CLA  B 522      65                                                       
HET    CLA  B 523      65                                                       
HET    CLA  B 524      65                                                       
HET    CLA  B 525      65                                                       
HET    LMT  B 526      35                                                       
HET    CLA  B 527      65                                                       
HET    BCR  B 528      40                                                       
HET    BCR  B 529      40                                                       
HET    CLA  C 474      65                                                       
HET    CLA  C 475      65                                                       
HET    CLA  C 476      65                                                       
HET    CLA  C 477      65                                                       
HET    CLA  C 478      65                                                       
HET    CLA  C 479      65                                                       
HET    CLA  C 480      65                                                       
HET    CLA  C 481      65                                                       
HET    CLA  C 482      65                                                       
HET    CLA  C 483      65                                                       
HET    CLA  C 484      65                                                       
HET    CLA  C 485      65                                                       
HET    CLA  C 486      65                                                       
HET    CLA  C 487      65                                                       
HET    BCR  C 488      40                                                       
HET    BCR  C 489      40                                                       
HET    BCT  D 353       4                                                       
HET    CLA  D 354      65                                                       
HET    PHO  D 355      64                                                       
HET    CLA  D 356      65                                                       
HET    PL9  D 357      45                                                       
HET    HEC  E  84      43                                                       
HET    BCR  F  48      40                                                       
HET    BCR  J  53      40                                                       
HET    BCR  K  50      40                                                       
HET    HEC  V 138      43                                                       
HET     FE  a2345       1                                                       
HET    BCT  a2346       4                                                       
HET    OEC  a2347       9                                                       
HET    CLA  a2348      65                                                       
HET    CLA  a2349      65                                                       
HET    PHO  a2350      64                                                       
HET    CLA  a2351      65                                                       
HET    PL9  a2352      45                                                       
HET    CLA  b2511      65                                                       
HET    CLA  b2512      65                                                       
HET    CLA  b2513      65                                                       
HET    CLA  b2514      65                                                       
HET    CLA  b2515      65                                                       
HET    CLA  b2516      65                                                       
HET    CLA  b2517      65                                                       
HET    CLA  b2518      65                                                       
HET    CLA  b2519      65                                                       
HET    CLA  b2520      65                                                       
HET    CLA  b2521      65                                                       
HET    CLA  b2522      65                                                       
HET    CLA  b2523      65                                                       
HET    CLA  b2524      65                                                       
HET    CLA  b2525      65                                                       
HET    CLA  b2526      65                                                       
HET    BCR  b2527      40                                                       
HET    BCR  b2528      40                                                       
HET    CLA  c2474      65                                                       
HET    CLA  c2475      65                                                       
HET    CLA  c2476      65                                                       
HET    CLA  c2477      65                                                       
HET    CLA  c2478      65                                                       
HET    CLA  c2479      65                                                       
HET    CLA  c2480      65                                                       
HET    CLA  c2481      65                                                       
HET    CLA  c2482      65                                                       
HET    CLA  c2483      65                                                       
HET    CLA  c2484      65                                                       
HET    CLA  c2485      65                                                       
HET    CLA  c2486      65                                                       
HET    CLA  c2487      65                                                       
HET    BCR  c2488      40                                                       
HET    BCR  c2489      40                                                       
HET    BCT  d2353       4                                                       
HET    CLA  d2354      65                                                       
HET    CLA  d2355      65                                                       
HET    PHO  d2356      64                                                       
HET    CLA  d2357      65                                                       
HET    PL9  d2358      45                                                       
HET    LMT  d2359      35                                                       
HET    BCR  d2360      40                                                       
HET    HEC  e2084      43                                                       
HET    BCR  j2053      40                                                       
HET    BCR  k2050      40                                                       
HET    HEC  v2138      43                                                       
HETNAM      FE FE (III) ION                                                     
HETNAM     BCT BICARBONATE ION                                                  
HETNAM     OEC OXYGEN EVOLVING SYSTEM                                           
HETNAM     CLA CHLOROPHYLL A                                                    
HETNAM     PHO PHEOPHYTIN A                                                     
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     LMT DODECYL-BETA-D-MALTOSIDE                                         
HETNAM     BCR BETA-CAROTENE                                                    
HETNAM     HEC HEME C                                                           
HETSYN     PL9 PLASTOQUINONE 9                                                  
FORMUL  39   FE    2(FE 3+)                                                     
FORMUL  40  BCT    4(C H O3 1-)                                                 
FORMUL  41  OEC    2(CA MN4 O4)                                                 
FORMUL  42  CLA    72(C55 H72 MG N4 O5 2+)                                      
FORMUL  45  PHO    4(C55 H74 N4 O5)                                             
FORMUL  47  PL9    4(C53 H80 O2)                                                
FORMUL  63  LMT    2(C24 H46 O11)                                               
FORMUL  65  BCR    14(C40 H56)                                                  
FORMUL  88  HEC    4(C34 H34 FE N4 O4)                                          
HELIX    1   1 ASN A   12  SER A   23  1                                  12    
HELIX    2   2 PHE A   33  ALA A   55  1                                  23    
HELIX    3   3 ASN A   76  GLY A   80  5                                   5    
HELIX    4   4 SER A  101  ASN A  108  1                                   8    
HELIX    5   5 GLY A  109  LEU A  137  1                                  29    
HELIX    6   6 TRP A  142  LEU A  159  1                                  18    
HELIX    7   7 LEU A  159  GLY A  166  1                                   8    
HELIX    8   8 GLY A  175  HIS A  190  1                                  16    
HELIX    9   9 HIS A  195  SER A  222  1                                  28    
HELIX   10  10 ASN A  247  ILE A  259  1                                  13    
HELIX   11  11 ASN A  267  MET A  293  1                                  27    
HELIX   12  12 ALA A  318  HIS A  332  1                                  15    
HELIX   13  13 VAL B    8  ILE B   13  5                                   6    
HELIX   14  14 ASP B   15  PHE B   45  1                                  31    
HELIX   15  15 PRO B   54  GLY B   59  1                                   6    
HELIX   16  16 VAL B   62  LEU B   69  1                                   8    
HELIX   17  17 SER B   92  VAL B  116  1                                  25    
HELIX   18  18 ASP B  134  PHE B  156  1                                  23    
HELIX   19  19 ASN B  194  LEU B  218  1                                  25    
HELIX   20  20 GLN B  223  ALA B  228  1                                   6    
HELIX   21  21 ILE B  234  GLY B  259  1                                  26    
HELIX   22  22 PRO B  264  GLY B  269  1                                   6    
HELIX   23  23 THR B  271  SER B  277  1                                   7    
HELIX   24  24 SER B  278  ALA B  293  1                                  16    
HELIX   25  25 THR B  297  SER B  303  1                                   7    
HELIX   26  26 PRO B  306  TYR B  312  1                                   7    
HELIX   27  27 ASP B  313  ASN B  318  5                                   6    
HELIX   28  28 PRO B  329  GLY B  333  5                                   5    
HELIX   29  29 SER B  391  GLY B  396  1                                   6    
HELIX   30  30 GLY B  404  GLY B  408  5                                   5    
HELIX   31  31 ASP B  413  ILE B  425  1                                  13    
HELIX   32  32 ASP B  433  LEU B  437  5                                   5    
HELIX   33  33 SER B  446  PHE B  475  1                                  30    
HELIX   34  34 PHE B  475  SER B  480  1                                   6    
HELIX   35  35 ALA C   37  LEU C   42  1                                   6    
HELIX   36  36 LEU C   45  PHE C   75  1                                  31    
HELIX   37  37 PRO C   80  GLY C   85  1                                   6    
HELIX   38  38 LEU C   88  LEU C   95  1                                   8    
HELIX   39  39 PHE C  109  ARG C  135  1                                  27    
HELIX   40  40 GLU C  141  PHE C  146  1                                   6    
HELIX   41  41 ASP C  153  PHE C  181  1                                  29    
HELIX   42  42 ASP C  205  TYR C  212  1                                   8    
HELIX   43  43 LEU C  213  LYS C  215  5                                   3    
HELIX   44  44 TRP C  223  VAL C  227  5                                   5    
HELIX   45  45 ASN C  229  THR C  254  1                                  26    
HELIX   46  46 PHE C  257  PHE C  264  1                                   8    
HELIX   47  47 SER C  267  PHE C  292  1                                  26    
HELIX   48  48 PRO C  298  GLY C  303  1                                   6    
HELIX   49  49 THR C  305  LYS C  323  1                                  19    
HELIX   50  50 GLY C  353  ARG C  357  5                                   5    
HELIX   51  51 LEU C  366  PRO C  368  5                                   3    
HELIX   52  52 ASP C  376  ASP C  383  1                                   8    
HELIX   53  53 PRO C  386  HIS C  398  1                                  13    
HELIX   54  54 SER C  421  ARG C  447  1                                  27    
HELIX   55  55 TRP D   14  ARG D   24  1                                  11    
HELIX   56  56 SER D   33  VAL D   55  1                                  23    
HELIX   57  57 ALA D   82  GLY D   86  5                                   5    
HELIX   58  58 ASP D  100  LEU D  107  1                                   8    
HELIX   59  59 GLY D  108  VAL D  136  1                                  29    
HELIX   60  60 PRO D  140  PHE D  146  1                                   7    
HELIX   61  61 PHE D  146  LEU D  158  1                                  13    
HELIX   62  62 LEU D  158  GLN D  164  1                                   7    
HELIX   63  63 VAL D  175  HIS D  189  1                                  15    
HELIX   64  64 ASN D  190  LEU D  193  5                                   4    
HELIX   65  65 ASN D  194  LEU D  222  1                                  29    
HELIX   66  66 SER D  245  PHE D  257  1                                  13    
HELIX   67  67 LYS D  264  ALA D  290  1                                  27    
HELIX   68  68 PHE D  298  ASP D  308  1                                  11    
HELIX   69  69 THR D  313  GLN D  334  1                                  22    
HELIX   70  70 PRO D  342  LEU D  346  5                                   5    
HELIX   71  71 SER E   10  SER E   15  1                                   6    
HELIX   72  72 SER E   15  ILE E   24  1                                  10    
HELIX   73  73 ILE E   26  THR E   39  1                                  14    
HELIX   74  74 GLY E   40  GLY E   47  1                                   8    
HELIX   75  75 ARG E   50  TYR E   54  5                                   5    
HELIX   76  76 GLU E   70  LYS E   83  1                                  14    
HELIX   77  77 PHE F   15  GLN F   40  1                                  26    
HELIX   78  78 THR H   26  ASN H   49  1                                  24    
HELIX   79  79 MET I    1  LEU I   24  1                                  24    
HELIX   80  80 ILE J   12  GLY J   35  1                                  24    
HELIX   81  81 LEU J   36  SER J   39  5                                   4    
HELIX   82  82 PRO K    3  ILE K    8  5                                   6    
HELIX   83  83 PHE K    9  LEU K   16  1                                   8    
HELIX   84  84 VAL K   18  VAL K   34  1                                  17    
HELIX   85  85 ASN L   13  ASN L   37  1                                  25    
HELIX   86  86 GLN M    5  GLU M   30  1                                  26    
HELIX   87  87 THR O    6  VAL O   11  1                                   6    
HELIX   88  88 ILE O   32  THR O   37  1                                   6    
HELIX   89  89 LYS O  178  VAL O  187  1                                  10    
HELIX   90  90 THR T    3  PHE T   23  1                                  21    
HELIX   91  91 THR U   32  VAL U   40  1                                   9    
HELIX   92  92 ASN U   61  TYR U   68  5                                   8    
HELIX   93  93 TYR U   72  ASN U   82  1                                  11    
HELIX   94  94 SER U   87  ILE U   94  5                                   8    
HELIX   95  95 THR U   98  GLU U  110  1                                  13    
HELIX   96  96 GLU U  118  GLU U  123  1                                   6    
HELIX   97  97 THR V    4  LEU V    8  1                                   5    
HELIX   98  98 THR V   22  CYS V   37  1                                  16    
HELIX   99  99 CYS V   37  VAL V   42  1                                   6    
HELIX  100 100 ARG V   55  LEU V   61  1                                   7    
HELIX  101 101 ASN V   68  ASN V   78  1                                  11    
HELIX  102 102 GLU V   87  VAL V   91  5                                   5    
HELIX  103 103 SER V   94  PHE V  101  5                                   8    
HELIX  104 104 THR V  108  GLY V  127  1                                  20    
HELIX  105 105 ASP V  128  GLY V  133  1                                   6    
HELIX  106 106 PRO X   14  ASP X   44  1                                  31    
HELIX  107 107 UNK N    1  UNK N   31  1                                  31    
HELIX  108 108 MET Z    1  ALA Z   26  1                                  26    
HELIX  109 109 ASP Z   32  ASN Z   58  1                                  27    
HELIX  110 110 ASN a 2012  SER a 2023  1                                  12    
HELIX  111 111 PHE a 2033  ALA a 2055  1                                  23    
HELIX  112 112 ASN a 2076  GLY a 2080  5                                   5    
HELIX  113 113 SER a 2101  ASN a 2108  1                                   8    
HELIX  114 114 GLY a 2109  LEU a 2137  1                                  29    
HELIX  115 115 TRP a 2142  LEU a 2159  1                                  18    
HELIX  116 116 LEU a 2159  GLY a 2166  1                                   8    
HELIX  117 117 GLY a 2175  HIS a 2190  1                                  16    
HELIX  118 118 HIS a 2195  SER a 2222  1                                  28    
HELIX  119 119 ASN a 2247  ILE a 2259  1                                  13    
HELIX  120 120 ASN a 2267  MET a 2293  1                                  27    
HELIX  121 121 ALA a 2318  HIS a 2332  1                                  15    
HELIX  122 122 VAL b 2008  ILE b 2013  5                                   6    
HELIX  123 123 ASP b 2015  PHE b 2045  1                                  31    
HELIX  124 124 PRO b 2054  GLY b 2059  1                                   6    
HELIX  125 125 VAL b 2062  LEU b 2069  1                                   8    
HELIX  126 126 SER b 2092  VAL b 2116  1                                  25    
HELIX  127 127 ASP b 2134  PHE b 2156  1                                  23    
HELIX  128 128 ASN b 2194  LEU b 2218  1                                  25    
HELIX  129 129 GLN b 2223  ALA b 2228  1                                   6    
HELIX  130 130 ILE b 2234  GLY b 2259  1                                  26    
HELIX  131 131 PRO b 2264  GLY b 2269  1                                   6    
HELIX  132 132 THR b 2271  SER b 2277  1                                   7    
HELIX  133 133 SER b 2278  ALA b 2293  1                                  16    
HELIX  134 134 THR b 2297  SER b 2303  1                                   7    
HELIX  135 135 PRO b 2306  TYR b 2314  1                                   9    
HELIX  136 136 ILE b 2315  ASN b 2318  5                                   4    
HELIX  137 137 PRO b 2329  GLY b 2333  5                                   5    
HELIX  138 138 SER b 2391  GLY b 2396  1                                   6    
HELIX  139 139 GLY b 2404  GLY b 2408  5                                   5    
HELIX  140 140 ASP b 2413  ILE b 2425  1                                  13    
HELIX  141 141 ASP b 2433  LEU b 2437  5                                   5    
HELIX  142 142 SER b 2446  PHE b 2475  1                                  30    
HELIX  143 143 PHE b 2475  SER b 2480  1                                   6    
HELIX  144 144 ALA c 2037  LEU c 2042  1                                   6    
HELIX  145 145 LEU c 2045  PHE c 2075  1                                  31    
HELIX  146 146 PRO c 2080  GLY c 2085  1                                   6    
HELIX  147 147 LEU c 2088  LEU c 2095  1                                   8    
HELIX  148 148 PHE c 2109  ARG c 2135  1                                  27    
HELIX  149 149 GLU c 2141  PHE c 2146  1                                   6    
HELIX  150 150 ASP c 2153  PHE c 2181  1                                  29    
HELIX  151 151 ASP c 2205  TYR c 2212  1                                   8    
HELIX  152 152 TRP c 2223  VAL c 2227  5                                   5    
HELIX  153 153 ASN c 2229  THR c 2254  1                                  26    
HELIX  154 154 PHE c 2257  PHE c 2264  1                                   8    
HELIX  155 155 SER c 2267  PHE c 2292  1                                  26    
HELIX  156 156 PRO c 2298  GLY c 2303  1                                   6    
HELIX  157 157 THR c 2305  LYS c 2323  1                                  19    
HELIX  158 158 GLY c 2353  ARG c 2357  5                                   5    
HELIX  159 159 LEU c 2366  PRO c 2368  5                                   3    
HELIX  160 160 ASP c 2376  ASP c 2383  1                                   8    
HELIX  161 161 PRO c 2386  HIS c 2398  1                                  13    
HELIX  162 162 SER c 2421  ARG c 2447  1                                  27    
HELIX  163 163 TRP d 2014  ARG d 2024  1                                  11    
HELIX  164 164 SER d 2033  VAL d 2055  1                                  23    
HELIX  165 165 ALA d 2082  GLY d 2086  5                                   5    
HELIX  166 166 ASP d 2100  LEU d 2107  1                                   8    
HELIX  167 167 GLY d 2108  VAL d 2136  1                                  29    
HELIX  168 168 PRO d 2140  PHE d 2146  1                                   7    
HELIX  169 169 PHE d 2146  LEU d 2158  1                                  13    
HELIX  170 170 LEU d 2158  GLN d 2164  1                                   7    
HELIX  171 171 VAL d 2175  HIS d 2189  1                                  15    
HELIX  172 172 ASN d 2190  LEU d 2193  5                                   4    
HELIX  173 173 ASN d 2194  LEU d 2222  1                                  29    
HELIX  174 174 SER d 2245  PHE d 2257  1                                  13    
HELIX  175 175 LYS d 2264  ALA d 2290  1                                  27    
HELIX  176 176 PHE d 2298  ASP d 2308  1                                  11    
HELIX  177 177 THR d 2313  GLN d 2334  1                                  22    
HELIX  178 178 PRO d 2342  LEU d 2346  5                                   5    
HELIX  179 179 SER e 2010  SER e 2015  1                                   6    
HELIX  180 180 SER e 2015  ILE e 2024  1                                  10    
HELIX  181 181 ILE e 2026  THR e 2039  1                                  14    
HELIX  182 182 GLY e 2040  GLY e 2047  1                                   8    
HELIX  183 183 ARG e 2050  TYR e 2054  5                                   5    
HELIX  184 184 GLU e 2070  LYS e 2083  1                                  14    
HELIX  185 185 PHE f 2015  GLN f 2040  1                                  26    
HELIX  186 186 THR h 2026  ASN h 2049  1                                  24    
HELIX  187 187 MET i 2001  LEU i 2024  1                                  24    
HELIX  188 188 ILE j 2012  GLY j 2037  1                                  26    
HELIX  189 189 PRO k 2003  ILE k 2008  5                                   6    
HELIX  190 190 PHE k 2009  LEU k 2016  1                                   8    
HELIX  191 191 VAL k 2018  VAL k 2034  1                                  17    
HELIX  192 192 ASN l 2013  ASN l 2037  1                                  25    
HELIX  193 193 GLN m 2005  GLU m 2030  1                                  26    
HELIX  194 194 THR o 2006  VAL o 2011  1                                   6    
HELIX  195 195 ILE o 2032  THR o 2037  1                                   6    
HELIX  196 196 LYS o 2178  VAL o 2187  1                                  10    
HELIX  197 197 THR t 2003  PHE t 2023  1                                  21    
HELIX  198 198 THR u 2032  VAL u 2040  1                                   9    
HELIX  199 199 VAL u 2042  LEU u 2047  1                                   6    
HELIX  200 200 ASN u 2061  TYR u 2068  5                                   8    
HELIX  201 201 TYR u 2072  ASN u 2082  1                                  11    
HELIX  202 202 SER u 2087  ILE u 2094  5                                   8    
HELIX  203 203 THR u 2098  GLU u 2110  1                                  13    
HELIX  204 204 GLU u 2118  GLU u 2123  1                                   6    
HELIX  205 205 THR v 2004  LEU v 2008  1                                   5    
HELIX  206 206 THR v 2022  CYS v 2037  1                                  16    
HELIX  207 207 CYS v 2037  VAL v 2042  1                                   6    
HELIX  208 208 ARG v 2055  LEU v 2061  1                                   7    
HELIX  209 209 ASN v 2068  ASN v 2078  1                                  11    
HELIX  210 210 GLU v 2087  VAL v 2091  5                                   5    
HELIX  211 211 SER v 2094  PHE v 2101  5                                   8    
HELIX  212 212 THR v 2108  GLY v 2127  1                                  20    
HELIX  213 213 ASP v 2128  GLY v 2133  1                                   6    
HELIX  214 214 PRO x 2014  ASP x 2044  1                                  31    
HELIX  215 215 UNK n 2001  UNK n 2031  1                                  31    
HELIX  216 216 MET z 2001  TYR z 2027  1                                  27    
HELIX  217 217 ASP z 2032  ASN z 2058  1                                  27    
SHEET    1   A 2 LEU A 297  ASN A 298  0                                        
SHEET    2   A 2 GLY C 402  SER C 403  1  O  GLY C 402   N  ASN A 298           
SHEET    1   B 2 SER A 305  VAL A 306  0                                        
SHEET    2   B 2 VAL A 313  ILE A 314 -1  O  ILE A 314   N  SER A 305           
SHEET    1   C 2 MET B 166  TRP B 167  0                                        
SHEET    2   C 2 VAL B 178  GLN B 179 -1  O  GLN B 179   N  MET B 166           
SHEET    1   D 5 VAL B 377  ASP B 380  0                                        
SHEET    2   D 5 ILE B 369  THR B 371 -1  N  LEU B 370   O  ALA B 379           
SHEET    3   D 5 GLU B 353  VAL B 356 -1  N  PHE B 355   O  THR B 371           
SHEET    4   D 5 ALA B 344  ARG B 347 -1  N  PHE B 346   O  LEU B 354           
SHEET    5   D 5 THR B 398  PHE B 401 -1  O  SER B 400   N  VAL B 345           
SHEET    1   E 2 LEU C 185  TYR C 186  0                                        
SHEET    2   E 2 VAL C 196  ARG C 197 -1  O  ARG C 197   N  LEU C 185           
SHEET    1   F 2 LEU C 341  ARG C 343  0                                        
SHEET    2   F 2 ILE C 349  PHE C 351 -1  O  ILE C 350   N  MET C 342           
SHEET    1   G 2 ARG C 370  GLY C 371  0                                        
SHEET    2   G 2 GLY C 374  LEU C 375 -1  O  GLY C 374   N  GLY C 371           
SHEET    1   H 2 ALA D  77  VAL D  78  0                                        
SHEET    2   H 2 PHE D 173  GLY D 174 -1  O  PHE D 173   N  VAL D  78           
SHEET    1   I 8 VAL O 126  SER O 128  0                                        
SHEET    2   I 8 LEU O  93  GLU O  97 -1  N  PHE O  95   O  ALA O 127           
SHEET    3   I 8 GLY O  83  VAL O  87 -1  N  GLU O  84   O  VAL O  96           
SHEET    4   I 8 ARG O  39  LYS O  53 -1  N  ALA O  41   O  GLY O  83           
SHEET    5   I 8 GLU O 232  ILE O 243 -1  O  GLN O 236   N  THR O  48           
SHEET    6   I 8 GLY O 209  THR O 214 -1  N  ILE O 211   O  ALA O 241           
SHEET    7   I 8 GLN O 196  VAL O 201 -1  N  ASN O 200   O  THR O 214           
SHEET    8   I 8 PHE O 142  GLY O 144 -1  N  PHE O 142   O  LEU O 199           
SHEET    1   J 8 VAL O 126  SER O 128  0                                        
SHEET    2   J 8 LEU O  93  GLU O  97 -1  N  PHE O  95   O  ALA O 127           
SHEET    3   J 8 GLY O  83  VAL O  87 -1  N  GLU O  84   O  VAL O  96           
SHEET    4   J 8 ARG O  39  LYS O  53 -1  N  ALA O  41   O  GLY O  83           
SHEET    5   J 8 GLU O 232  ILE O 243 -1  O  GLN O 236   N  THR O  48           
SHEET    6   J 8 SER O 217  GLU O 218 -1  N  SER O 217   O  ILE O 235           
SHEET    7   J 8 GLN O 196  VAL O 201 -1  N  GLN O 196   O  GLU O 218           
SHEET    8   J 8 PHE O 142  GLY O 144 -1  N  PHE O 142   O  LEU O 199           
SHEET    1   K 3 LYS O  69  LEU O  70  0                                        
SHEET    2   K 3 VAL O 106  VAL O 108 -1  O  VAL O 108   N  LYS O  69           
SHEET    3   K 3 ARG O 115  PRO O 117 -1  O  ILE O 116   N  THR O 107           
SHEET    1   L 2 ASN O 147  VAL O 148  0                                        
SHEET    2   L 2 THR O 193  LYS O 194 -1  O  THR O 193   N  VAL O 148           
SHEET    1   M 2 ILE U  55  ASP U  56  0                                        
SHEET    2   M 2 PHE U 112  THR U 113  1  O  THR U 113   N  ILE U  55           
SHEET    1   N 2 THR V   9  PRO V  11  0                                        
SHEET    2   N 2 THR V  18  THR V  20 -1  O  ILE V  19   N  VAL V  10           
SHEET    1   O 2 LEU a2297  ASN a2298  0                                        
SHEET    2   O 2 GLY c2402  SER c2403  1  O  GLY c2402   N  ASN a2298           
SHEET    1   P 2 SER a2305  VAL a2306  0                                        
SHEET    2   P 2 VAL a2313  ILE a2314 -1  O  ILE a2314   N  SER a2305           
SHEET    1   Q 2 MET b2166  TRP b2167  0                                        
SHEET    2   Q 2 VAL b2178  GLN b2179 -1  O  GLN b2179   N  MET b2166           
SHEET    1   R 5 VAL b2377  ASP b2380  0                                        
SHEET    2   R 5 ILE b2369  THR b2371 -1  N  LEU b2370   O  ALA b2379           
SHEET    3   R 5 GLU b2353  VAL b2356 -1  N  PHE b2355   O  THR b2371           
SHEET    4   R 5 ALA b2344  ARG b2347 -1  N  PHE b2346   O  LEU b2354           
SHEET    5   R 5 THR b2398  PHE b2401 -1  O  SER b2400   N  VAL b2345           
SHEET    1   S 2 LEU c2185  TYR c2186  0                                        
SHEET    2   S 2 VAL c2196  ARG c2197 -1  O  ARG c2197   N  LEU c2185           
SHEET    1   T 2 LEU c2341  ARG c2343  0                                        
SHEET    2   T 2 ILE c2349  PHE c2351 -1  O  ILE c2350   N  MET c2342           
SHEET    1   U 2 ARG c2370  GLY c2371  0                                        
SHEET    2   U 2 GLY c2374  LEU c2375 -1  O  GLY c2374   N  GLY c2371           
SHEET    1   V 2 ALA d2077  VAL d2078  0                                        
SHEET    2   V 2 PHE d2173  GLY d2174 -1  O  PHE d2173   N  VAL d2078           
SHEET    1   W12 THR o2193  VAL o2201  0                                        
SHEET    2   W12 GLY o2209  THR o2214 -1  O  THR o2214   N  ASN o2200           
SHEET    3   W12 GLU o2232  ILE o2243 -1  O  ALA o2241   N  ILE o2211           
SHEET    4   W12 THR o2193  VAL o2201  0                                        
SHEET    5   W12 PHE o2142  VAL o2148 -1  N  PHE o2142   O  LEU o2199           
SHEET    6   W12 VAL o2126  SER o2128 -1  N  SER o2128   O  LYS o2143           
SHEET    7   W12 LEU o2093  GLU o2097 -1  N  PHE o2095   O  ALA o2127           
SHEET    8   W12 GLY o2083  VAL o2087 -1  N  GLU o2084   O  VAL o2096           
SHEET    9   W12 ARG o2039  LYS o2053 -1  N  ALA o2041   O  GLY o2083           
SHEET   10   W12 GLU o2232  ILE o2243 -1  O  GLN o2236   N  THR o2048           
SHEET   11   W12 SER o2217  GLU o2218 -1  N  SER o2217   O  ILE o2235           
SHEET   12   W12 GLU o2232  ILE o2243 -1  O  ILE o2235   N  SER o2217           
SHEET    1   X 3 LYS o2069  LEU o2070  0                                        
SHEET    2   X 3 VAL o2106  VAL o2108 -1  O  VAL o2108   N  LYS o2069           
SHEET    3   X 3 ARG o2115  PRO o2117 -1  O  ILE o2116   N  THR o2107           
SHEET    1   Y 2 ILE u2055  ASP u2056  0                                        
SHEET    2   Y 2 PHE u2112  THR u2113  1  O  THR u2113   N  ILE u2055           
SHEET    1   Z 2 THR v2009  PRO v2011  0                                        
SHEET    2   Z 2 THR v2018  THR v2020 -1  O  ILE v2019   N  VAL v2010           
SSBOND   1 CYS O   19    CYS O   44                          1555   1555  2.05  
SSBOND   2 CYS o 2019    CYS o 2044                          1555   1555  2.05  
LINK         OE2 GLU A 189                 O1  OEC A 347     1555   1555  1.79  
LINK         CD1 ILE E  12                 O2D HEC E  84     1555   1555  1.96  
LINK         OE2 GLU a2189                 O1  OEC a2347     1555   1555  1.58  
LINK         CD1 ILE e2012                 O2D HEC e2084     1555   1555  1.88  
LINK         SG  CYS v2037                 CAB HEC v2138     1555   1555  1.83  
LINK         SG  CYS v2040                 CAC HEC v2138     1555   1555  1.84  
LINK         NE2 HIS A 118                MG   CLA A 352     1555   1555  2.30  
LINK         OD2 ASP A 170                MN4  OEC A 347     1555   1555  1.99  
LINK         OE2 GLU A 189                MN2  OEC A 347     1555   1555  1.98  
LINK         NE2 HIS A 198                MG   CLA A 348     1555   1555  2.25  
LINK         NE2 HIS A 215                FE    FE A 345     1555   1555  2.18  
LINK         NE2 HIS A 272                FE    FE A 345     1555   1555  2.20  
LINK         NE2 HIS A 332                MN2  OEC A 347     1555   1555  1.99  
LINK         OE2 GLU A 333                MN2  OEC A 347     1555   1555  2.94  
LINK         OE2 GLU A 333                MN4  OEC A 347     1555   1555  2.01  
LINK         OE1 GLU A 333                MN3  OEC A 347     1555   1555  3.00  
LINK         OD2 ASP A 342                MN1  OEC A 347     1555   1555  1.98  
LINK         OXT ALA A 344                CA1  OEC A 347     1555   1555  2.01  
LINK         O   ALA A 344                CA1  OEC A 347     1555   1555  2.44  
LINK        FE    FE A 345                 NE2 HIS D 214     1555   1555  2.19  
LINK        FE    FE A 345                 NE2 HIS D 268     1555   1555  2.17  
LINK        FE    FE A 345                 O2  BCT D 353     1555   1555  2.19  
LINK        FE    FE A 345                 O3  BCT D 353     1555   1555  2.21  
LINK         O2  BCT A 346                CA1  OEC A 347     1555   1555  2.26  
LINK         O3  BCT A 346                CA1  OEC A 347     1555   1555  2.26  
LINK         O1  BCT A 346                MN4  OEC A 347     1555   1555  1.89  
LINK        MN3  OEC A 347                 OE1 GLU C 354     1555   1555  1.94  
LINK        MN3  OEC A 347                 OE2 GLU C 354     1555   1555  2.00  
LINK        MN1  OEC A 347                 OE1 GLU C 354     1555   1555  3.12  
LINK         NE2 HIS B   9                MG   CLA B 520     1555   1555  2.28  
LINK         NE2 HIS B  23                MG   CLA B 513     1555   1555  2.30  
LINK         NE2 HIS B  26                MG   CLA B 512     1555   1555  2.32  
LINK         NE2 HIS B 100                MG   CLA B 518     1555   1555  2.27  
LINK         NE2 HIS B 114                MG   CLA B 525     1555   1555  2.24  
LINK         NE2 HIS B 142                MG   CLA B 522     1555   1555  2.27  
LINK         ND1 HIS B 157                MG   CLA B 515     1555   1555  2.25  
LINK         ND1 HIS B 201                MG   CLA B 521     1555   1555  2.25  
LINK         NE2 HIS B 202                MG   CLA B 517     1555   1555  2.27  
LINK         NE2 HIS B 216                MG   CLA B 511     1555   1555  2.24  
LINK         NE2 HIS B 455                MG   CLA B 516     1555   1555  2.25  
LINK         NE2 HIS B 466                MG   CLA B 519     1555   1555  2.26  
LINK         NE2 HIS B 469                MG   CLA B 523     1555   1555  2.26  
LINK         ND2 ASN C  39                MG   CLA C 486     1555   1555  2.28  
LINK         NE2 HIS C  53                MG   CLA C 478     1555   1555  2.30  
LINK         NE2 HIS C  56                MG   CLA C 476     1555   1555  2.28  
LINK         NE2 HIS C 118                MG   CLA C 480     1555   1555  2.31  
LINK         NE2 HIS C 132                MG   CLA C 484     1555   1555  2.26  
LINK         NE2 HIS C 164                MG   CLA C 482     1555   1555  2.28  
LINK         NE2 HIS C 237                MG   CLA C 479     1555   1555  2.23  
LINK         NE2 HIS C 251                MG   CLA C 474     1555   1555  2.24  
LINK         NE2 HIS C 430                MG   CLA C 481     1555   1555  2.23  
LINK         NE2 HIS C 441                MG   CLA C 477     1555   1555  2.27  
LINK         NE2 HIS C 444                MG   CLA C 483     1555   1555  2.27  
LINK         NE2 HIS D 117                MG   CLA D 356     1555   1555  2.27  
LINK         NE2 HIS D 197                MG   CLA D 354     1555   1555  2.24  
LINK         NE2 HIS E  22                FE   HEC E  84     1555   1555  2.00  
LINK        FE   HEC E  84                 NE2 HIS F  23     1555   1555  2.03  
LINK         NE2 HIS V  41                FE   HEC V 138     1555   1555  2.00  
LINK         NE2 HIS V  92                FE   HEC V 138     1555   1555  2.04  
LINK         NE2 HIS a2118                MG   CLA a2351     1555   1555  2.31  
LINK         OD2 ASP a2170                MN4  OEC a2347     1555   1555  2.00  
LINK         OE2 GLU a2189                MN2  OEC a2347     1555   1555  2.01  
LINK         NE2 HIS a2198                MG   CLA a2348     1555   1555  2.29  
LINK         NE2 HIS a2215                FE    FE a2345     1555   1555  2.19  
LINK         NE2 HIS a2272                FE    FE a2345     1555   1555  2.21  
LINK         NE2 HIS a2332                MN2  OEC a2347     1555   1555  2.02  
LINK         OE2 GLU a2333                MN2  OEC a2347     1555   1555  2.97  
LINK         OE2 GLU a2333                MN4  OEC a2347     1555   1555  2.02  
LINK         OE1 GLU a2333                MN4  OEC a2347     1555   1555  3.08  
LINK         OD2 ASP a2342                MN1  OEC a2347     1555   1555  1.98  
LINK         O   ALA a2344                CA1  OEC a2347     1555   1555  2.46  
LINK        FE    FE a2345                 NE2 HIS d2214     1555   1555  2.17  
LINK        FE    FE a2345                 NE2 HIS d2268     1555   1555  2.23  
LINK        FE    FE a2345                 O2  BCT d2353     1555   1555  2.21  
LINK        FE    FE a2345                 O3  BCT d2353     1555   1555  2.20  
LINK         O1  BCT a2346                CA1  OEC a2347     1555   1555  2.25  
LINK         O3  BCT a2346                CA1  OEC a2347     1555   1555  2.24  
LINK         O2  BCT a2346                MN4  OEC a2347     1555   1555  1.85  
LINK        MN3  OEC a2347                 OE1 GLU c2354     1555   1555  2.20  
LINK        MN3  OEC a2347                 OE2 GLU c2354     1555   1555  2.01  
LINK         NE2 HIS b2009                MG   CLA b2520     1555   1555  2.26  
LINK         NE2 HIS b2023                MG   CLA b2513     1555   1555  2.30  
LINK         NE2 HIS b2026                MG   CLA b2512     1555   1555  2.31  
LINK         NE2 HIS b2100                MG   CLA b2518     1555   1555  2.27  
LINK         NE2 HIS b2114                MG   CLA b2525     1555   1555  2.23  
LINK         NE2 HIS b2142                MG   CLA b2522     1555   1555  2.28  
LINK         ND1 HIS b2157                MG   CLA b2515     1555   1555  2.25  
LINK         ND1 HIS b2201                MG   CLA b2521     1555   1555  2.23  
LINK         NE2 HIS b2202                MG   CLA b2517     1555   1555  2.24  
LINK         NE2 HIS b2216                MG   CLA b2511     1555   1555  2.25  
LINK         NE2 HIS b2455                MG   CLA b2516     1555   1555  2.26  
LINK         NE2 HIS b2466                MG   CLA b2519     1555   1555  2.25  
LINK         NE2 HIS b2469                MG   CLA b2523     1555   1555  2.27  
LINK         ND2 ASN c2039                MG   CLA c2486     1555   1555  2.26  
LINK         NE2 HIS c2053                MG   CLA c2478     1555   1555  2.30  
LINK         NE2 HIS c2056                MG   CLA c2476     1555   1555  2.26  
LINK         NE2 HIS c2118                MG   CLA c2480     1555   1555  2.28  
LINK         NE2 HIS c2132                MG   CLA c2484     1555   1555  2.24  
LINK         NE2 HIS c2164                MG   CLA c2482     1555   1555  2.27  
LINK         NE2 HIS c2237                MG   CLA c2479     1555   1555  2.25  
LINK         NE2 HIS c2251                MG   CLA c2474     1555   1555  2.26  
LINK         NE2 HIS c2430                MG   CLA c2481     1555   1555  2.23  
LINK         NE2 HIS c2441                MG   CLA c2477     1555   1555  2.29  
LINK         NE2 HIS c2444                MG   CLA c2483     1555   1555  2.28  
LINK         NE2 HIS d2117                MG   CLA d2357     1555   1555  2.29  
LINK         NE2 HIS d2197                MG   CLA d2354     1555   1555  2.26  
LINK         NE2 HIS e2022                FE   HEC e2084     1555   1555  2.01  
LINK        FE   HEC e2084                 NE2 HIS f2023     1555   1555  2.04  
LINK         NE2 HIS v2041                FE   HEC v2138     1555   1555  2.02  
LINK         NE2 HIS v2092                FE   HEC v2138     1555   1555  2.00  
CISPEP   1 ALA C  190    PRO C  191          0        -0.24                     
CISPEP   2 ALA U   83    PRO U   84          0        -0.04                     
CISPEP   3 THR V   63    PRO V   64          0        -0.04                     
CISPEP   4 ALA c 2190    PRO c 2191          0        -0.77                     
CISPEP   5 ALA u 2083    PRO u 2084          0         0.23                     
CISPEP   6 THR v 2063    PRO v 2064          0        -0.50                     
SITE     1 AC1  5 HIS A 215  HIS A 272  HIS D 214  HIS D 268                    
SITE     2 AC1  5 BCT D 353                                                     
SITE     1 AC2  6 TYR A 161  GLN A 165  ASP A 170  ALA A 344                    
SITE     2 AC2  6 OEC A 347  ARG C 357                                          
SITE     1 AC3  9 HIS A 215  VAL A 219  TYR A 246  HIS A 272                    
SITE     2 AC3  9  FE A 345  HIS D 214  TYR D 244  LYS D 264                    
SITE     3 AC3  9 HIS D 268                                                     
SITE     1 AC4  5 HIS a2215  HIS a2272  HIS d2214  HIS d2268                    
SITE     2 AC4  5 BCT d2353                                                     
SITE     1 AC5  5 GLN a2165  ASP a2170  ALA a2344  OEC a2347                    
SITE     2 AC5  5 ARG c2357                                                     
SITE     1 AC6  8 HIS a2215  TYR a2246  HIS a2272   FE a2345                    
SITE     2 AC6  8 HIS d2214  TYR d2244  LYS d2264  HIS d2268                    
SITE     1 AC7 10 GLN A 165  ASP A 170  GLU A 189  HIS A 332                    
SITE     2 AC7 10 GLU A 333  HIS A 337  ASP A 342  ALA A 344                    
SITE     3 AC7 10 BCT A 346  GLU C 354                                          
SITE     1 AC8 23 TYR A 147  PRO A 150  SER A 153  ALA A 154                    
SITE     2 AC8 23 MET A 183  ILE A 184  PHE A 186  GLN A 187                    
SITE     3 AC8 23 ILE A 192  LEU A 193  HIS A 198  GLY A 201                    
SITE     4 AC8 23 VAL A 205  PHE A 206  THR A 286  ALA A 287                    
SITE     5 AC8 23 ILE A 290  CLA A 349  CLA A 350  PHO A 351                    
SITE     6 AC8 23 CLA D 354  PL9 D 357  PHE T  17                               
SITE     1 AC9 19 MET A 183  PHE A 206  CLA A 348  CLA A 350                    
SITE     2 AC9 19 PL9 A 353  LEU D 122  VAL D 152  VAL D 156                    
SITE     3 AC9 19 PHE D 181  PHE D 185  GLN D 186  TRP D 191                    
SITE     4 AC9 19 THR D 192  HIS D 197  VAL D 201  VAL D 204                    
SITE     5 AC9 19 SER D 282  VAL D 286  PHO D 355                               
SITE     1 BC1 14 VAL A 157  MET A 172  ILE A 176  THR A 179                    
SITE     2 BC1 14 PHE A 180  PHE A 182  MET A 183  CLA A 348                    
SITE     3 BC1 14 PHO A 351  MET D 198  VAL D 201  LEU D 209                    
SITE     4 BC1 14 ILE T  14  PHE T  17                                          
SITE     1 BC2 16 GLN A 199  VAL A 202  ALA A 203  TYR A 262                    
SITE     2 BC2 16 ALA A 263  TRP A 278  CLA A 348  PL9 A 353                    
SITE     3 BC2 16 VAL D 175  ILE D 178  PHE D 179  PHE D 181                    
SITE     4 BC2 16 LEU D 182  CLA D 354  PHO D 355  BCR J  53                    
SITE     1 BC3 15 LEU A  41  ALA A  44  THR A  45  TYR A 126                    
SITE     2 BC3 15 GLN A 130  ALA A 146  TYR A 147  PHE A 158                    
SITE     3 BC3 15 LEU A 174  CLA A 348  CLA A 349  ALA D 208                    
SITE     4 BC3 15 LEU D 209  ILE D 213  PHE D 257                               
SITE     1 BC4 16 PHE A 206  ALA A 209  LEU A 210  MET A 214                    
SITE     2 BC4 16 CLA A 350  PL9 A 353  TRP D  48  GLY D 118                    
SITE     3 BC4 16 PHE D 125  GLN D 129  ASN D 142  PHE D 146                    
SITE     4 BC4 16 PHE D 153  PHE D 173  LEU D 279  CLA D 354                    
SITE     1 BC5 12 THR A  40  PHE A  93  TYR A  94  PRO A  95                    
SITE     2 BC5 12 ILE A  96  GLN A 113  LEU A 114  HIS A 118                    
SITE     3 BC5 12 LEU A 121  SER C 216  TYR I   9  PHE I  15                    
SITE     1 BC6 16 TYR B 258  CLA B 519  CLA B 521  LMT B 526                    
SITE     2 BC6 16 LEU D  43  HIS D  87  LEU D  91  LEU D  92                    
SITE     3 BC6 16 TRP D  93  THR D 112  PHE D 113  LEU D 116                    
SITE     4 BC6 16 HIS D 117  LEU D 162  LEU H  42  TYR H  48                    
SITE     1 BC7 17 LEU C 161  LEU C 165  LEU C 213  ILE C 240                    
SITE     2 BC7 17 ILE C 243  GLY C 247  TRP C 250  HIS C 251                    
SITE     3 BC7 17 THR C 254  THR C 255  PRO C 256  PHE C 257                    
SITE     4 BC7 17 TRP C 259  ALA C 260  PHE C 264  CLA C 477                    
SITE     5 BC7 17 CLA C 485                                                     
SITE     1 BC8 15 PRO A 196  GLN A 199  PHE A 300  TRP C  63                    
SITE     2 BC8 15 PHE C  70  GLY C  85  LEU C 404  SER C 406                    
SITE     3 BC8 15 TRP C 425  SER C 429  HIS C 430  CLA C 476                    
SITE     4 BC8 15 CLA C 481  BCR J  53  PRO K  17                               
SITE     1 BC9 12 ASN C  39  HIS C  56  ILE C  60  PHE C 437                    
SITE     2 BC9 12 CLA C 475  CLA C 478  CLA C 480  CLA C 481                    
SITE     3 BC9 12 CLA C 483  CLA C 486  PRO K  20  LEU K  24                    
SITE     1 CC1 15 MET A 127  TRP A 131  TRP C 223  PHE C 264                    
SITE     2 CC1 15 SER C 273  TYR C 274  GLY C 277  ALA C 278                    
SITE     3 CC1 15 HIS C 441  ALA C 445  ARG C 449  CLA C 474                    
SITE     4 CC1 15 CLA C 485  VAL I  20  PHE I  23                               
SITE     1 CC2 13 ASN C  39  ALA C  52  HIS C  53  HIS C  56                    
SITE     2 CC2 13 HIS C 164  LEU C 272  SER C 275  CLA C 476                    
SITE     3 CC2 13 CLA C 480  CLA C 482  CLA C 483  CLA C 485                    
SITE     4 CC2 13 CLA C 486                                                     
SITE     1 CC3 19 THR C  94  LEU C  95  LEU C 168  GLY C 171                    
SITE     2 CC3 19 ALA C 172  LEU C 175  VAL C 233  HIS C 237                    
SITE     3 CC3 19 ILE C 240  ALA C 278  MET C 281  MET C 282                    
SITE     4 CC3 19 ILE C 285  PHE C 289  VAL C 296  TYR C 297                    
SITE     5 CC3 19 CLA C 480  CLA C 481  CLA C 485                               
SITE     1 CC4 16 ILE C  60  VAL C  61  TRP C  63  ALA C  64                    
SITE     2 CC4 16 THR C  68  LEU C  88  HIS C  91  LEU C  95                    
SITE     3 CC4 16 VAL C 114  HIS C 118  LEU C 279  CLA C 476                    
SITE     4 CC4 16 CLA C 478  CLA C 479  CLA C 481  CLA C 482                    
SITE     1 CC5 14 TRP C  63  ILE C  87  HIS C  91  LEU C 175                    
SITE     2 CC5 14 LYS C 178  PHE C 182  LEU C 279  TYR C 297                    
SITE     3 CC5 14 HIS C 430  LEU C 433  CLA C 475  CLA C 476                    
SITE     4 CC5 14 CLA C 479  CLA C 480                                          
SITE     1 CC6 10 LEU C  50  HIS C  53  ALA C  57  ILE C 160                    
SITE     2 CC6 10 PHE C 163  HIS C 164  VAL C 167  CLA C 478                    
SITE     3 CC6 10 CLA C 480  CLA C 484                                          
SITE     1 CC7 11 TRP C  36  ALA C  37  LEU C 276  PHE C 436                    
SITE     2 CC7 11 PHE C 437  VAL C 439  GLY C 440  TRP C 443                    
SITE     3 CC7 11 HIS C 444  CLA C 476  CLA C 478                               
SITE     1 CC8  7 VAL C  54  VAL C 124  GLY C 128  TYR C 131                    
SITE     2 CC8  7 HIS C 132  CLA C 482  BCR C 489                               
SITE     1 CC9 11 HIS C 164  ILE C 240  PHE C 264  TYR C 271                    
SITE     2 CC9 11 TYR C 274  SER C 275  MET C 282  CLA C 474                    
SITE     3 CC9 11 CLA C 477  CLA C 478  CLA C 479                               
SITE     1 DC1 11 PHE B 139  ALA B 212  HIS B 216  PRO B 222                    
SITE     2 DC1 11 LEU B 225  CLA B 524  THR H  26  MET H  30                    
SITE     3 DC1 11 PHE H  33  LEU H  36  PHE H  37                               
SITE     1 DC2 10 HIS B   9  HIS B  26  VAL B  30  LEU B 461                    
SITE     2 DC2 10 PHE B 462  CLA B 513  CLA B 516  CLA B 520                    
SITE     3 DC2 10 CLA B 523  BCR B 528                                          
SITE     1 DC3 16 HIS B   9  LEU B  19  HIS B  23  HIS B  26                    
SITE     2 DC3 16 THR B  27  ILE B 234  VAL B 237  LEU B 238                    
SITE     3 DC3 16 SER B 241  VAL B 245  CLA B 512  CLA B 516                    
SITE     4 DC3 16 CLA B 520  CLA B 522  CLA B 523  CLA B 524                    
SITE     1 DC4 16 TRP B  33  SER B  36  TYR B  40  GLN B  58                    
SITE     2 DC4 16 GLY B  59  PHE B  61  LEU B 324  PHE B 325                    
SITE     3 DC4 16 ARG B 326  THR B 327  GLY B 328  TRP B 450                    
SITE     4 DC4 16 CLA B 516  BCR B 529  MET D 199  LEU L  27                    
SITE     1 DC5 11 LEU B  69  TRP B  91  LEU B 149  GLY B 152                    
SITE     2 DC5 11 PHE B 153  PHE B 156  HIS B 157  PHE B 162                    
SITE     3 DC5 11 PRO B 164  CLA B 517  CLA B 518                               
SITE     1 DC6 15 TRP B  33  PHE B  61  ARG B  68  VAL B 245                    
SITE     2 DC6 15 ALA B 248  ALA B 249  VAL B 252  PHE B 451                    
SITE     3 DC6 15 HIS B 455  PHE B 458  PHE B 462  CLA B 512                    
SITE     4 DC6 15 CLA B 513  CLA B 514  CLA B 518                               
SITE     1 DC7 17 ARG B  68  LEU B 149  CYS B 150  PHE B 153                    
SITE     2 DC7 17 MET B 166  HIS B 201  HIS B 202  ALA B 248                    
SITE     3 DC7 17 VAL B 251  VAL B 252  THR B 262  CLA B 515                    
SITE     4 DC7 17 CLA B 518  CLA B 521  CLA B 524  PHE H  37                    
SITE     5 DC7 17 LEU H  38                                                     
SITE     1 DC8 19 THR B  27  VAL B  30  ALA B  31  TRP B  33                    
SITE     2 DC8 19 VAL B  62  PHE B  65  MET B  66  ARG B  68                    
SITE     3 DC8 19 LEU B  69  HIS B 100  LEU B 103  GLY B 147                    
SITE     4 DC8 19 ALA B 205  GLY B 209  CLA B 515  CLA B 516                    
SITE     5 DC8 19 CLA B 517  CLA B 521  CLA B 524                               
SITE     1 DC9  6 ALA B 243  HIS B 466  CLA B 524  ILE D 123                    
SITE     2 DC9  6 MET D 126  CLA D 356                                          
SITE     1 EC1 12 TYR B   6  VAL B   8  HIS B   9  VAL B  11                    
SITE     2 EC1 12 CLA B 512  CLA B 513  CLA B 523  BCR B 529                    
SITE     3 EC1 12 VAL L  10  VAL M  17  PRO M  18  PHE M  21                    
SITE     1 EC2 16 PHE B 190  GLY B 197  ALA B 200  HIS B 201                    
SITE     2 EC2 16 ALA B 204  PHE B 247  PHE B 250  CLA B 517                    
SITE     3 EC2 16 CLA B 518  CLA B 527  PHE D 120  CLA D 356                    
SITE     4 EC2 16 PHE H  37  PHE H  40  ILE H  44  TYR H  48                    
SITE     1 EC3 13 ILE B  20  HIS B  23  LEU B 106  LEU B 109                    
SITE     2 EC3 13 ALA B 110  ARG B 124  MET B 138  ILE B 141                    
SITE     3 EC3 13 HIS B 142  LEU B 145  CLA B 513  CLA B 524                    
SITE     4 EC3 13 CLA B 525                                                     
SITE     1 EC4 15 TYR B   6  ARG B   7  VAL B   8  HIS B   9                    
SITE     2 EC4 15 LEU B 461  PHE B 462  PHE B 464  GLY B 465                    
SITE     3 EC4 15 TRP B 468  HIS B 469  ARG B 472  CLA B 512                    
SITE     4 EC4 15 CLA B 513  CLA B 520  BCR B 528                               
SITE     1 EC5 17 LEU B  19  LEU B 135  PHE B 139  HIS B 142                    
SITE     2 EC5 17 LEU B 143  LEU B 225  MET B 231  ILE B 234                    
SITE     3 EC5 17 VAL B 237  SER B 240  SER B 241  CLA B 511                    
SITE     4 EC5 17 CLA B 513  CLA B 517  CLA B 518  CLA B 519                    
SITE     5 EC5 17 CLA B 522                                                     
SITE     1 EC6  8 ILE B  20  TRP B 113  HIS B 114  TYR B 117                    
SITE     2 EC6  8 LEU B 122  PHE B 123  ARG B 124  CLA B 522                    
SITE     1 EC7 12 ILE E  12  ARG E  17  TYR E  18  HIS E  22                    
SITE     2 EC7 12 THR E  25  LEU E  29  ARG F  18  TRP F  19                    
SITE     3 EC7 12 HIS F  23  ALA F  26  VAL F  27  ILE F  30                    
SITE     1 EC8 14 ALA V  36  CYS V  37  CYS V  40  HIS V  41                    
SITE     2 EC8 14 LEU V  52  ASP V  53  LEU V  54  THR V  58                    
SITE     3 EC8 14 LEU V  72  TYR V  75  MET V  76  TYR V  82                    
SITE     4 EC8 14 HIS V  92  PRO V  93                                          
SITE     1 EC9 10 CLA A 348  THR D 217  TRP D 253  PHE D 257                    
SITE     2 EC9 10 ALA D 260  PHE D 261  LEU D 267  PHE T  18                    
SITE     3 EC9 10 ILE T  21  BCR b2527                                          
SITE     1 FC1 17 PHE A 211  MET A 214  HIS A 215  LEU A 218                    
SITE     2 FC1 17 ALA A 251  HIS A 252  PHE A 255  ILE A 259                    
SITE     3 FC1 17 ALA A 263  SER A 264  PHE A 265  LEU A 271                    
SITE     4 FC1 17 PHE A 274  CLA A 350  CLA D 354  PHO D 355                    
SITE     5 FC1 17 BCR J  53                                                     
SITE     1 FC2 18 TRP C  36  GLY C  38  ASN C  39  ARG C  41                    
SITE     2 FC2 18 LEU C  42  LYS C  48  ALA C  52  ALA C 123                    
SITE     3 FC2 18 VAL C 130  ILE C 134  CLA C 476  CLA C 478                    
SITE     4 FC2 18 BCR C 488  TRP K  30  GLN K  31  MET Z  19                    
SITE     5 FC2 18 PRO Z  24  TRP Z  47                                          
SITE     1 FC3  9 TYR B 193  TYR B 258  TYR B 273  SER B 277                    
SITE     2 FC3  9 HIS D  87  CLA D 356  VAL H  59  SER H  60                    
SITE     3 FC3  9 TRP H  61                                                     
SITE     1 FC4  3 PRO B 187  PHE B 190  CLA B 521                               
SITE     1 FC5 14 ILE A  36  LEU A  91  PHE A 117  PHE A 155                    
SITE     2 FC5 14 LEU A 159  PHE A 168  PRO C 217  PHE C 218                    
SITE     3 FC5 14 GLY C 220  GLY C 222  VAL C 225  ILE C 285                    
SITE     4 FC5 14 PHE C 289  PHE C 292                                          
SITE     1 FC6  7 LEU D  43  GLY D  46  LEU D  49  THR D  50                    
SITE     2 FC6  7 THR F  29  PHE F  32  ILE F  36                               
SITE     1 FC7  9 ALA C  55  VAL C 116  SER C 122  GLY C 126                    
SITE     2 FC7  9 CLA C 486  TYR K   6  PHE K  23  BCR K  50                    
SITE     3 FC7  9 LEU Z   9                                                     
SITE     1 FC8 17 BCR C 488  ALA J  14  THR J  15  GLY J  18                    
SITE     2 FC8 17 MET J  19  LEU K  16  ILE K  19  LEU K  22                    
SITE     3 FC8 17 PHE K  23  ALA K  25  LEU K  26  PHE K  28                    
SITE     4 FC8 17 VAL K  29  UNK N  16  UNK N  20  SER Z  16                    
SITE     5 FC8 17 PHE Z  17                                                     
SITE     1 FC9  8 PHE C 109  VAL C 116  ILE C 120  CLA C 484                    
SITE     2 FC9  8 TYR K   6  VAL Z  51  VAL Z  54  GLY Z  55                    
SITE     1 GC1  6 LEU B  29  GLY B  32  GLY B 105  CLA B 512                    
SITE     2 GC1  6 CLA B 523  PL9 d2358                                          
SITE     1 GC2  5 CLA A 350  PL9 A 353  CLA C 475  PHE J  29                    
SITE     2 GC2  5 TYR J  33                                                     
SITE     1 GC3  7 MET B  25  LEU B  29  ARG B 326  THR B 327                    
SITE     2 GC3  7 CLA B 514  CLA B 520  LEU M   6                               
SITE     1 GC4 10 GLN a2165  ASP a2170  GLU a2189  HIS a2332                    
SITE     2 GC4 10 GLU a2333  HIS a2337  ASP a2342  ALA a2344                    
SITE     3 GC4 10 BCT a2346  GLU c2354                                          
SITE     1 GC5 25 TYR a2147  PRO a2150  SER a2153  ALA a2154                    
SITE     2 GC5 25 VAL a2157  MET a2183  ILE a2184  GLN a2187                    
SITE     3 GC5 25 ILE a2192  LEU a2193  HIS a2198  GLY a2201                    
SITE     4 GC5 25 VAL a2205  PHE a2206  THR a2286  ALA a2287                    
SITE     5 GC5 25 ILE a2290  CLA a2349  PHO a2350  LEU d2182                    
SITE     6 GC5 25 LEU d2205  CLA d2354  CLA d2355  PL9 d2358                    
SITE     7 GC5 25 PHE t2017                                                     
SITE     1 GC6 20 MET a2183  PHE a2206  CLA a2348  CLA a2349                    
SITE     2 GC6 20 PL9 a2352  LEU d2122  VAL d2152  VAL d2156                    
SITE     3 GC6 20 PHE d2181  LEU d2182  PHE d2185  GLN d2186                    
SITE     4 GC6 20 TRP d2191  HIS d2197  VAL d2201  VAL d2204                    
SITE     5 GC6 20 SER d2282  VAL d2286  CLA d2355  PHO d2356                    
SITE     1 GC7 12 MET a2172  ILE a2176  THR a2179  PHE a2180                    
SITE     2 GC7 12 PHE a2182  MET a2183  CLA a2348  PHO a2350                    
SITE     3 GC7 12 MET d2198  VAL d2201  LEU d2209  CLA d2354                    
SITE     1 GC8 19 GLN a2199  VAL a2202  ALA a2203  PHE a2206                    
SITE     2 GC8 19 TYR a2262  ALA a2263  PHE a2265  TRP a2278                    
SITE     3 GC8 19 CLA a2348  PL9 a2352  PHE d2157  VAL d2175                    
SITE     4 GC8 19 ILE d2178  PHE d2179  PHE d2181  LEU d2182                    
SITE     5 GC8 19 CLA d2354  PHO d2356  BCR j2053                               
SITE     1 GC9 16 LEU a2041  ALA a2044  THR a2045  TYR a2126                    
SITE     2 GC9 16 GLN a2130  ALA a2146  TYR a2147  PHE a2158                    
SITE     3 GC9 16 LEU a2174  VAL a2283  CLA a2348  ALA d2208                    
SITE     4 GC9 16 LEU d2209  ILE d2213  PHE d2257  CLA d2355                    
SITE     1 HC1 17 PHE a2206  ALA a2209  LEU a2210  MET a2214                    
SITE     2 HC1 17 LEU a2258  CLA a2349  PL9 a2352  TRP d2048                    
SITE     3 HC1 17 GLY d2118  PHE d2125  GLN d2129  ASN d2142                    
SITE     4 HC1 17 PHE d2146  PRO d2149  PHE d2153  PHE d2173                    
SITE     5 HC1 17 CLA d2354                                                     
SITE     1 HC2 12 PHE a2093  TYR a2094  PRO a2095  ILE a2096                    
SITE     2 HC2 12 TRP a2097  GLU a2098  LEU a2114  HIS a2118                    
SITE     3 HC2 12 LEU a2121  SER c2216  TYR i2009  PHE i2015                    
SITE     1 HC3 16 TYR b2258  CLA b2519  CLA b2521  CYS d2040                    
SITE     2 HC3 16 HIS d2087  LEU d2091  LEU d2092  TRP d2093                    
SITE     3 HC3 16 THR d2112  PHE d2113  LEU d2116  HIS d2117                    
SITE     4 HC3 16 LEU d2162  LMT d2359  LEU h2042  TYR h2048                    
SITE     1 HC4 15 LEU c2161  LEU c2165  LEU c2213  ILE c2240                    
SITE     2 HC4 15 ILE c2243  HIS c2251  THR c2254  THR c2255                    
SITE     3 HC4 15 PRO c2256  PHE c2257  TRP c2259  ALA c2260                    
SITE     4 HC4 15 PHE c2264  CLA c2477  CLA c2485                               
SITE     1 HC5 16 PRO a2196  GLN a2199  PHE a2300  TRP c2063                    
SITE     2 HC5 16 PHE c2070  GLY c2085  LEU c2404  SER c2406                    
SITE     3 HC5 16 TRP c2425  SER c2429  HIS c2430  CLA c2476                    
SITE     4 HC5 16 CLA c2481  BCR j2053  PRO k2017  VAL k2021                    
SITE     1 HC6 11 HIS c2056  ILE c2060  PHE c2437  CLA c2475                    
SITE     2 HC6 11 CLA c2478  CLA c2480  CLA c2481  CLA c2483                    
SITE     3 HC6 11 CLA c2486  PRO k2020  LEU k2024                               
SITE     1 HC7 14 TRP a2131  TRP c2223  PHE c2264  SER c2273                    
SITE     2 HC7 14 TYR c2274  GLY c2277  ALA c2278  HIS c2441                    
SITE     3 HC7 14 ALA c2445  ARG c2449  CLA c2474  CLA c2485                    
SITE     4 HC7 14 VAL i2020  PHE i2023                                          
SITE     1 HC8 12 ASN c2039  ALA c2052  HIS c2053  HIS c2056                    
SITE     2 HC8 12 LEU c2272  SER c2275  CLA c2476  CLA c2480                    
SITE     3 HC8 12 CLA c2482  CLA c2483  CLA c2485  CLA c2486                    
SITE     1 HC9 18 THR c2094  LEU c2095  LEU c2168  GLY c2171                    
SITE     2 HC9 18 ALA c2172  LEU c2175  HIS c2237  ILE c2240                    
SITE     3 HC9 18 ALA c2278  MET c2281  MET c2282  ILE c2285                    
SITE     4 HC9 18 PHE c2289  VAL c2296  TYR c2297  CLA c2480                    
SITE     5 HC9 18 CLA c2481  CLA c2485                                          
SITE     1 IC1 16 ILE c2060  VAL c2061  TRP c2063  ALA c2064                    
SITE     2 IC1 16 THR c2068  LEU c2088  HIS c2091  LEU c2095                    
SITE     3 IC1 16 VAL c2114  HIS c2118  LEU c2279  CLA c2476                    
SITE     4 IC1 16 CLA c2478  CLA c2479  CLA c2481  CLA c2482                    
SITE     1 IC2 15 TRP c2063  ILE c2087  HIS c2091  LEU c2175                    
SITE     2 IC2 15 LYS c2178  PHE c2182  LEU c2279  TYR c2297                    
SITE     3 IC2 15 LEU c2426  HIS c2430  LEU c2433  CLA c2475                    
SITE     4 IC2 15 CLA c2476  CLA c2479  CLA c2480                               
SITE     1 IC3  9 LEU c2050  HIS c2053  ALA c2057  PHE c2163                    
SITE     2 IC3  9 HIS c2164  VAL c2167  CLA c2478  CLA c2480                    
SITE     3 IC3  9 CLA c2484                                                     
SITE     1 IC4 10 TRP c2036  ALA c2037  LEU c2276  PHE c2436                    
SITE     2 IC4 10 PHE c2437  GLY c2440  TRP c2443  HIS c2444                    
SITE     3 IC4 10 CLA c2476  CLA c2478                                          
SITE     1 IC5  7 VAL c2054  VAL c2124  GLY c2128  TYR c2131                    
SITE     2 IC5  7 HIS c2132  CLA c2482  BCR c2489                               
SITE     1 IC6 14 LEU c2161  HIS c2164  ILE c2240  CYS c2244                    
SITE     2 IC6 14 PHE c2264  TRP c2266  TYR c2271  TYR c2274                    
SITE     3 IC6 14 SER c2275  MET c2282  CLA c2474  CLA c2477                    
SITE     4 IC6 14 CLA c2478  CLA c2479                                          
SITE     1 IC7 11 PHE b2139  ALA b2212  HIS b2216  PRO b2222                    
SITE     2 IC7 11 LEU b2225  CLA b2524  THR h2026  MET h2030                    
SITE     3 IC7 11 PHE h2033  LEU h2036  PHE h2037                               
SITE     1 IC8 11 HIS b2009  HIS b2026  VAL b2030  PHE b2458                    
SITE     2 IC8 11 LEU b2461  PHE b2462  CLA b2513  CLA b2516                    
SITE     3 IC8 11 CLA b2520  CLA b2523  BCR b2527                               
SITE     1 IC9 16 HIS b2009  LEU b2019  HIS b2023  HIS b2026                    
SITE     2 IC9 16 THR b2027  ILE b2234  VAL b2237  LEU b2238                    
SITE     3 IC9 16 SER b2241  VAL b2245  CLA b2512  CLA b2516                    
SITE     4 IC9 16 CLA b2520  CLA b2522  CLA b2523  CLA b2524                    
SITE     1 JC1 16 TRP b2033  SER b2036  TYR b2040  GLN b2058                    
SITE     2 JC1 16 GLY b2059  PHE b2061  LEU b2324  PHE b2325                    
SITE     3 JC1 16 ARG b2326  THR b2327  GLY b2328  TRP b2450                    
SITE     4 JC1 16 CLA b2516  BCR b2528  MET d2199  PHE l2031                    
SITE     1 JC2 10 LEU b2069  TRP b2091  GLY b2152  PHE b2153                    
SITE     2 JC2 10 PHE b2156  HIS b2157  PHE b2162  PRO b2164                    
SITE     3 JC2 10 CLA b2517  CLA b2518                                          
SITE     1 JC3 16 TRP b2033  PHE b2061  ARG b2068  VAL b2245                    
SITE     2 JC3 16 ALA b2248  ALA b2249  VAL b2252  PHE b2451                    
SITE     3 JC3 16 HIS b2455  PHE b2458  PHE b2462  CLA b2512                    
SITE     4 JC3 16 CLA b2513  CLA b2514  CLA b2518  CLA b2522                    
SITE     1 JC4 17 ARG b2068  LEU b2149  CYS b2150  PHE b2153                    
SITE     2 JC4 17 MET b2166  HIS b2201  HIS b2202  ALA b2248                    
SITE     3 JC4 17 VAL b2251  VAL b2252  THR b2262  CLA b2515                    
SITE     4 JC4 17 CLA b2518  CLA b2521  CLA b2524  PHE h2037                    
SITE     5 JC4 17 LEU h2038                                                     
SITE     1 JC5 17 THR b2027  VAL b2030  ALA b2031  VAL b2062                    
SITE     2 JC5 17 PHE b2065  MET b2066  ARG b2068  LEU b2069                    
SITE     3 JC5 17 HIS b2100  LEU b2103  GLY b2147  ALA b2205                    
SITE     4 JC5 17 GLY b2209  CLA b2515  CLA b2516  CLA b2517                    
SITE     5 JC5 17 CLA b2524                                                     
SITE     1 JC6  6 ALA b2243  HIS b2466  CLA b2524  ILE d2123                    
SITE     2 JC6  6 MET d2126  CLA d2357                                          
SITE     1 JC7 12 TYR b2006  VAL b2008  HIS b2009  VAL b2011                    
SITE     2 JC7 12 CLA b2512  CLA b2513  CLA b2523  BCR b2528                    
SITE     3 JC7 12 VAL l2010  VAL m2017  PRO m2018  PHE m2021                    
SITE     1 JC8 15 PHE b2190  GLY b2197  ALA b2200  HIS b2201                    
SITE     2 JC8 15 ALA b2204  PHE b2247  PHE b2250  CLA b2517                    
SITE     3 JC8 15 CLA b2526  ILE d2123  CLA d2357  PHE h2037                    
SITE     4 JC8 15 PHE h2040  ILE h2044  TYR h2048                               
SITE     1 JC9 14 ILE b2020  HIS b2023  LEU b2106  LEU b2109                    
SITE     2 JC9 14 ALA b2110  ARG b2124  MET b2138  ILE b2141                    
SITE     3 JC9 14 HIS b2142  LEU b2145  CLA b2513  CLA b2516                    
SITE     4 JC9 14 CLA b2524  CLA b2525                                          
SITE     1 KC1 15 TYR b2006  ARG b2007  VAL b2008  HIS b2009                    
SITE     2 KC1 15 LEU b2461  PHE b2462  PHE b2464  GLY b2465                    
SITE     3 KC1 15 TRP b2468  HIS b2469  ARG b2472  CLA b2512                    
SITE     4 KC1 15 CLA b2513  CLA b2520  BCR b2527                               
SITE     1 KC2 17 LEU b2019  LEU b2135  PHE b2139  HIS b2142                    
SITE     2 KC2 17 LEU b2143  LEU b2225  MET b2231  ILE b2234                    
SITE     3 KC2 17 VAL b2237  SER b2240  SER b2241  CLA b2511                    
SITE     4 KC2 17 CLA b2513  CLA b2517  CLA b2518  CLA b2519                    
SITE     5 KC2 17 CLA b2522                                                     
SITE     1 KC3  8 ILE b2020  TRP b2113  HIS b2114  TYR b2117                    
SITE     2 KC3  8 LEU b2122  PHE b2123  ARG b2124  CLA b2522                    
SITE     1 KC4 13 ILE e2012  ARG e2017  TYR e2018  ILE e2021                    
SITE     2 KC4 13 HIS e2022  THR e2025  LEU e2029  ARG f2018                    
SITE     3 KC4 13 TRP f2019  HIS f2023  ALA f2026  VAL f2027                    
SITE     4 KC4 13 ILE f2030                                                     
SITE     1 KC5 12 ALA v2036  CYS v2037  CYS v2040  HIS v2041                    
SITE     2 KC5 12 ASN v2049  LEU v2052  ASP v2053  LEU v2054                    
SITE     3 KC5 12 THR v2058  TYR v2075  TYR v2082  HIS v2092                    
SITE     1 KC6 11 BCR B 528  CLA a2348  LEU d2209  THR d2217                    
SITE     2 KC6 11 TRP d2253  PHE d2257  ALA d2260  PHE d2261                    
SITE     3 KC6 11 LEU d2267  PHE t2018  ILE t2021                               
SITE     1 KC7 17 PHE a2211  MET a2214  HIS a2215  LEU a2218                    
SITE     2 KC7 17 ALA a2251  HIS a2252  PHE a2255  PHE a2260                    
SITE     3 KC7 17 ALA a2263  SER a2264  PHE a2265  LEU a2271                    
SITE     4 KC7 17 PHE a2274  CLA a2349  CLA d2354  PHO d2356                    
SITE     5 KC7 17 BCR j2053                                                     
SITE     1 KC8 21 TRP c2036  GLY c2038  ASN c2039  ARG c2041                    
SITE     2 KC8 21 LEU c2042  LYS c2048  ALA c2123  PHE c2127                    
SITE     3 KC8 21 VAL c2130  ILE c2134  CLA c2476  CLA c2478                    
SITE     4 KC8 21 BCR c2488  LEU k2024  TRP k2030  GLN k2031                    
SITE     5 KC8 21 ARG k2037  MET z2019  VAL z2020  VAL z2023                    
SITE     6 KC8 21 TRP z2047                                                     
SITE     1 KC9  9 TYR b2193  TYR b2258  TYR b2273  SER b2277                    
SITE     2 KC9  9 HIS d2087  CLA d2357  VAL h2059  SER h2060                    
SITE     3 KC9  9 TRP h2061                                                     
SITE     1 LC1  3 PRO b2187  PHE b2190  CLA b2521                               
SITE     1 LC2 15 ILE a2036  LEU a2091  PHE a2117  PHE a2155                    
SITE     2 LC2 15 LEU a2159  ILE a2163  PHE a2168  PRO c2217                    
SITE     3 LC2 15 PHE c2218  GLY c2220  GLY c2222  VAL c2225                    
SITE     4 LC2 15 ILE c2285  PHE c2289  PHE c2292                               
SITE     1 LC3  7 LEU d2043  GLY d2046  LEU d2049  PHE d2113                    
SITE     2 LC3  7 PHE f2032  LEU f2033  ILE f2036                               
SITE     1 LC4  9 ALA c2055  LEU c2119  SER c2122  GLY c2126                    
SITE     2 LC4  9 CLA c2486  TYR k2006  PHE k2023  BCR k2050                    
SITE     3 LC4  9 LEU z2009                                                     
SITE     1 LC5 17 BCR c2488  ALA j2014  THR j2015  GLY j2018                    
SITE     2 LC5 17 MET j2019  LEU k2016  ILE k2019  LEU k2022                    
SITE     3 LC5 17 PHE k2023  ALA k2025  LEU k2026  PHE k2028                    
SITE     4 LC5 17 VAL k2029  UNK n2016  UNK n2020  SER z2016                    
SITE     5 LC5 17 PHE z2017                                                     
SITE     1 LC6  9 PHE c2109  PHE c2112  VAL c2116  ILE c2120                    
SITE     2 LC6  9 CLA c2484  TYR k2006  VAL z2051  VAL z2054                    
SITE     3 LC6  9 GLY z2055                                                     
SITE     1 LC7  6 PL9 D 357  LEU b2029  GLY b2032  GLY b2105                    
SITE     2 LC7  6 CLA b2512  CLA b2523                                          
SITE     1 LC8  5 CLA a2349  PL9 a2352  CLA c2475  PHE j2029                    
SITE     2 LC8  5 TYR j2033                                                     
SITE     1 LC9  7 MET b2025  LEU b2029  ARG b2326  THR b2327                    
SITE     2 LC9  7 CLA b2514  CLA b2520  LEU m2006                               
CRYST1  134.992  228.849  309.940  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      0.007408  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004370  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003226        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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