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Database: PDB
Entry: 1IR2
LinkDB: 1IR2
Original site: 1IR2 
HEADER    LYASE                                   03-SEP-01   1IR2              
TITLE     CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE              
TITLE    2 CARBOXYLASE/OXYGENASE (RUBISCO) FROM GREEN ALGA, CHLAMYDOMONAS       
TITLE    3 REINHARDTII COMPLEXED WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (2-  
TITLE    4 CABP)                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LARGE SUBUNIT OF RUBISCO;                                  
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, S, T, U, V, W, X, Y, Z;               
COMPND   4 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;              
COMPND   5 EC: 4.1.1.39;                                                        
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: SMALL SUBUNIT OF RUBISCO;                                  
COMPND   8 CHAIN: I, J, K, L, M, N, O, P, 1, 2, 3, 4, 5, 6, 7, 8;               
COMPND   9 SYNONYM: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 2;            
COMPND  10 EC: 4.1.1.39                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   3 ORGANISM_TAXID: 3055;                                                
SOURCE   4 STRAIN: 137C MT+;                                                    
SOURCE   5 MOL_ID: 2;                                                           
SOURCE   6 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   7 ORGANISM_TAXID: 3055;                                                
SOURCE   8 STRAIN: 137C MT+                                                     
KEYWDS    N-METHYLMETHIONINE, 4-HYDROXYPROLINE, S-METHYLCYSTEINE, ALPHA/BETA    
KEYWDS   2 BARREL, LYASE                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.MIZOHATA,H.MATSUMURA,Y.OKANO,M.KUMEI,H.TAKUMA,J.ONODERA,K.KATO,     
AUTHOR   2 N.SHIBATA,T.INOUE,A.YOKOTA,Y.KAI                                     
REVDAT   4   13-JUL-11 1IR2    1       VERSN                                    
REVDAT   3   24-FEB-09 1IR2    1       VERSN                                    
REVDAT   2   14-JAN-03 1IR2    1       REMARK                                   
REVDAT   1   20-MAR-02 1IR2    0                                                
JRNL        AUTH   E.MIZOHATA,H.MATSUMURA,Y.OKANO,M.KUMEI,H.TAKUMA,J.ONODERA,   
JRNL        AUTH 2 K.KATO,N.SHIBATA,T.INOUE,A.YOKOTA,Y.KAI                      
JRNL        TITL   CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5-BISPHOSPHATE     
JRNL        TITL 2 CARBOXYLASE/OXYGENASE FROM GREEN ALGA CHLAMYDOMONAS          
JRNL        TITL 3 REINHARDTII COMPLEXED WITH                                   
JRNL        TITL 4 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE.                        
JRNL        REF    J.MOL.BIOL.                   V. 316   679 2002              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   11866526                                                     
JRNL        DOI    10.1006/JMBI.2001.5381                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.84 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
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) : 1.84                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 39.89                          
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)   (%) : 90.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 762301                         
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) : 0.152                           
REMARK   3   FREE R VALUE                     : 0.181                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 37921                           
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) : 1.84                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.91                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2450                       
REMARK   3   BIN FREE R VALUE                    : 0.2610                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 2859                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.005                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 76496                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 592                                     
REMARK   3   SOLVENT ATOMS            : 9999                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.10                          
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) : 0.17                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.21                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.20                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.22                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.32                            
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 1IR2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-OCT-01.                  
REMARK 100 THE RCSB ID CODE IS RCSB005202.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUN-00                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PHOTON FACTORY                     
REMARK 200  BEAMLINE                       : BL-18B                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : WEISSENBERG                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 763078                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.840                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : 6.500                              
REMARK 200  R MERGE                    (I) : 0.06800                            
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) : 1.84                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.91                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 72.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.22900                            
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: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: PDB ID: 1BUR                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG4000, HEPES-KOH, GLYCEROL, NAHCO3,    
REMARK 280  MGCL2, DTT, 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (2-CABP), EDTA,    
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       87.37500            
REMARK 290   SMTRY3   2  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 ASSEMBLY IS A HEXADECAMER COMPRISED OF 8      
REMARK 300 LARGE AND 8 SMALL SUBUNITS. TWO HEXADECAMER EXIST IN THE ASYMMETRIC  
REMARK 300 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: HEXADECAMERIC                     
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 123440 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 115880 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -617.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I, B, J, C, K, D, L, E,            
REMARK 350                    AND CHAINS: M, F, N, G, O, H, P                   
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: HEXADECAMERIC                     
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXADECAMERIC              
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 123270 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 116460 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -611.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: S, 1, T, 2, U, 3, V, 4, W,            
REMARK 350                    AND CHAINS: 5, X, 6, Y, 7, Z, 8                   
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     VAL A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLU A     6                                                      
REMARK 465     THR A     7                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLN B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLU B     6                                                      
REMARK 465     THR B     7                                                      
REMARK 465     LYS B     8                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLN C     4                                                      
REMARK 465     THR C     5                                                      
REMARK 465     GLU C     6                                                      
REMARK 465     THR C     7                                                      
REMARK 465     LYS C     8                                                      
REMARK 465     ALA C     9                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     GLN D     4                                                      
REMARK 465     THR D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     THR D     7                                                      
REMARK 465     LYS D     8                                                      
REMARK 465     MET E     1                                                      
REMARK 465     VAL E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     GLN E     4                                                      
REMARK 465     THR E     5                                                      
REMARK 465     GLU E     6                                                      
REMARK 465     THR E     7                                                      
REMARK 465     LYS E     8                                                      
REMARK 465     ALA E     9                                                      
REMARK 465     GLY E    10                                                      
REMARK 465     MET F     1                                                      
REMARK 465     VAL F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     GLN F     4                                                      
REMARK 465     THR F     5                                                      
REMARK 465     GLU F     6                                                      
REMARK 465     THR F     7                                                      
REMARK 465     LYS F     8                                                      
REMARK 465     ALA F     9                                                      
REMARK 465     GLY F    10                                                      
REMARK 465     MET G     1                                                      
REMARK 465     VAL G     2                                                      
REMARK 465     PRO G     3                                                      
REMARK 465     GLN G     4                                                      
REMARK 465     THR G     5                                                      
REMARK 465     GLU G     6                                                      
REMARK 465     THR G     7                                                      
REMARK 465     LYS G     8                                                      
REMARK 465     ALA G     9                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     GLN H     4                                                      
REMARK 465     THR H     5                                                      
REMARK 465     GLU H     6                                                      
REMARK 465     THR H     7                                                      
REMARK 465     MET S     1                                                      
REMARK 465     VAL S     2                                                      
REMARK 465     PRO S     3                                                      
REMARK 465     GLN S     4                                                      
REMARK 465     THR S     5                                                      
REMARK 465     GLU S     6                                                      
REMARK 465     THR S     7                                                      
REMARK 465     LYS S     8                                                      
REMARK 465     ALA S     9                                                      
REMARK 465     GLY S    10                                                      
REMARK 465     MET T     1                                                      
REMARK 465     VAL T     2                                                      
REMARK 465     PRO T     3                                                      
REMARK 465     GLN T     4                                                      
REMARK 465     THR T     5                                                      
REMARK 465     GLU T     6                                                      
REMARK 465     THR T     7                                                      
REMARK 465     LYS T     8                                                      
REMARK 465     ALA T     9                                                      
REMARK 465     MET U     1                                                      
REMARK 465     VAL U     2                                                      
REMARK 465     PRO U     3                                                      
REMARK 465     GLN U     4                                                      
REMARK 465     THR U     5                                                      
REMARK 465     GLU U     6                                                      
REMARK 465     MET V     1                                                      
REMARK 465     VAL V     2                                                      
REMARK 465     PRO V     3                                                      
REMARK 465     GLN V     4                                                      
REMARK 465     THR V     5                                                      
REMARK 465     GLU V     6                                                      
REMARK 465     MET W     1                                                      
REMARK 465     VAL W     2                                                      
REMARK 465     PRO W     3                                                      
REMARK 465     GLN W     4                                                      
REMARK 465     THR W     5                                                      
REMARK 465     GLU W     6                                                      
REMARK 465     THR W     7                                                      
REMARK 465     LYS W     8                                                      
REMARK 465     ALA W     9                                                      
REMARK 465     MET X     1                                                      
REMARK 465     VAL X     2                                                      
REMARK 465     PRO X     3                                                      
REMARK 465     GLN X     4                                                      
REMARK 465     THR X     5                                                      
REMARK 465     GLU X     6                                                      
REMARK 465     THR X     7                                                      
REMARK 465     LYS X     8                                                      
REMARK 465     ALA X     9                                                      
REMARK 465     MET Y     1                                                      
REMARK 465     VAL Y     2                                                      
REMARK 465     PRO Y     3                                                      
REMARK 465     GLN Y     4                                                      
REMARK 465     THR Y     5                                                      
REMARK 465     GLU Y     6                                                      
REMARK 465     THR Y     7                                                      
REMARK 465     LYS Y     8                                                      
REMARK 465     ALA Y     9                                                      
REMARK 465     GLY Y    10                                                      
REMARK 465     MET Z     1                                                      
REMARK 465     VAL Z     2                                                      
REMARK 465     PRO Z     3                                                      
REMARK 465     GLN Z     4                                                      
REMARK 465     THR Z     5                                                      
REMARK 465     GLU Z     6                                                      
REMARK 465     THR Z     7                                                      
REMARK 465     LYS Z     8                                                      
REMARK 465     ALA Z     9                                                      
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    GLY M  61   N   -  CA  -  C   ANGL. DEV. = -15.1 DEGREES          
REMARK 500    GLY 3  61   N   -  CA  -  C   ANGL. DEV. = -15.1 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    ALA A   9      114.60    155.16                                   
REMARK 500    SER A  62      -77.91   -141.00                                   
REMARK 500    THR A  75     -164.11   -124.95                                   
REMARK 500    HIS A 153      -57.72   -133.23                                   
REMARK 500    CYS A 172      123.04   -175.53                                   
REMARK 500    ASN A 207      -91.21   -121.53                                   
REMARK 500    MET A 212      109.31   -165.94                                   
REMARK 500    MET A 297      -10.72     86.29                                   
REMARK 500    VAL A 331      -50.45     78.53                                   
REMARK 500    ASP A 357       91.40   -160.97                                   
REMARK 500    THR A 406      -56.56   -121.87                                   
REMARK 500    PHE I  12       49.18   -140.05                                   
REMARK 500    GLU I  13     -149.71     60.14                                   
REMARK 500    PHE I  15       -2.28     80.98                                   
REMARK 500    LYS I  77     -122.09     52.60                                   
REMARK 500    SER B  62      -78.26   -142.45                                   
REMARK 500    THR B  75     -168.20   -124.09                                   
REMARK 500    ASN B  95       21.88   -149.30                                   
REMARK 500    HIS B 153      -51.96   -135.56                                   
REMARK 500    CYS B 172      124.47   -174.70                                   
REMARK 500    ASN B 207      -92.17   -120.42                                   
REMARK 500    MET B 212      109.66   -165.39                                   
REMARK 500    ARG B 295       30.87    -94.66                                   
REMARK 500    MET B 297      -10.64     89.91                                   
REMARK 500    VAL B 331      -53.05     78.75                                   
REMARK 500    ASP B 357       91.52   -163.26                                   
REMARK 500    THR B 406      -55.69   -124.79                                   
REMARK 500    GLU J  13     -149.68     60.66                                   
REMARK 500    THR J  14      120.05    -39.05                                   
REMARK 500    LYS J  77     -120.43     56.08                                   
REMARK 500    GLN J 115       74.67     48.71                                   
REMARK 500    ALA C  11     -106.56     39.47                                   
REMARK 500    SER C  62      -74.78   -143.52                                   
REMARK 500    THR C  75     -164.69   -125.51                                   
REMARK 500    HIS C 153      -55.64   -135.46                                   
REMARK 500    CYS C 172      125.76   -172.89                                   
REMARK 500    ASN C 207      -90.55   -121.08                                   
REMARK 500    MET C 212      108.85   -163.83                                   
REMARK 500    MET C 297      -12.38     86.29                                   
REMARK 500    VAL C 331      -52.28     77.65                                   
REMARK 500    ASP C 357       89.55   -158.12                                   
REMARK 500    GLU K  13     -149.43     61.10                                   
REMARK 500    PHE K  15       -1.01     81.10                                   
REMARK 500    LYS K  77     -124.78     55.47                                   
REMARK 500    GLN K 115       73.91     49.67                                   
REMARK 500    ARG K 130       27.63   -143.52                                   
REMARK 500    SER D  62      -75.63   -143.90                                   
REMARK 500    THR D  75     -164.18   -124.09                                   
REMARK 500    ASN D  95       19.16   -147.91                                   
REMARK 500    HIS D 153      -55.85   -136.21                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     250 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH 18710        DISTANCE =  6.07 ANGSTROMS                       
REMARK 525    HOH 19717        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH 19718        DISTANCE =  7.08 ANGSTROMS                       
REMARK 525    HOH 2 269        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH 2 294        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH 2 295        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH 2 297        DISTANCE =  5.47 ANGSTROMS                       
REMARK 525    HOH 2 313        DISTANCE =  6.66 ANGSTROMS                       
REMARK 525    HOH 3 228        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH 3 301        DISTANCE =  7.05 ANGSTROMS                       
REMARK 525    HOH 4 249        DISTANCE =  6.57 ANGSTROMS                       
REMARK 525    HOH 4 280        DISTANCE =  5.39 ANGSTROMS                       
REMARK 525    HOH 4 294        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH 5 307        DISTANCE =  6.76 ANGSTROMS                       
REMARK 525    HOH 6 273        DISTANCE =  6.75 ANGSTROMS                       
REMARK 525    HOH 79297        DISTANCE =  5.80 ANGSTROMS                       
REMARK 525    HOH 86709        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH 87845        DISTANCE =  6.15 ANGSTROMS                       
REMARK 525    HOH A 881        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A 927        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH A 980        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A 983        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A1005        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A1015        DISTANCE =  5.06 ANGSTROMS                       
REMARK 525    HOH A1029        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH A1067        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH A1071        DISTANCE =  5.90 ANGSTROMS                       
REMARK 525    HOH B 909        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH B 966        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH B 983        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH B 995        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH B 997        DISTANCE =  5.10 ANGSTROMS                       
REMARK 525    HOH B 999        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH B1002        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH B1011        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH B1014        DISTANCE =  5.85 ANGSTROMS                       
REMARK 525    HOH C 969        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH C 987        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH C1006        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH C1007        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH C1034        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH C1038        DISTANCE =  5.57 ANGSTROMS                       
REMARK 525    HOH C1048        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH C1063        DISTANCE =  5.30 ANGSTROMS                       
REMARK 525    HOH C1076        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH C1078        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH C1086        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH C1091        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH D 852        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH D 889        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH D 999        DISTANCE =  5.67 ANGSTROMS                       
REMARK 525    HOH D1000        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH D1008        DISTANCE =  6.28 ANGSTROMS                       
REMARK 525    HOH D1010        DISTANCE =  5.07 ANGSTROMS                       
REMARK 525    HOH D1031        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH D1042        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH D1047        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH D1062        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH D1088        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH E 780        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH E 945        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH E 949        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH E 970        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH E 993        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH E1020        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH E1038        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH E1055        DISTANCE =  6.30 ANGSTROMS                       
REMARK 525    HOH E1059        DISTANCE =  7.04 ANGSTROMS                       
REMARK 525    HOH E1074        DISTANCE =  9.90 ANGSTROMS                       
REMARK 525    HOH F 866        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH F 914        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH F1018        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH F1020        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH F1044        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH F1049        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH F1050        DISTANCE =  6.92 ANGSTROMS                       
REMARK 525    HOH F1058        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH F1061        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH F1066        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH G 813        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH G 899        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH G 943        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH G 955        DISTANCE =  5.26 ANGSTROMS                       
REMARK 525    HOH G 982        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH G1061        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH G1068        DISTANCE =  5.41 ANGSTROMS                       
REMARK 525    HOH H 888        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH H 904        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH H 910        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH H 996        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH H1052        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH H1065        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH I 271        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH I 283        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH I 303        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH I 304        DISTANCE =  6.52 ANGSTROMS                       
REMARK 525    HOH J 241        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH J 291        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH J 297        DISTANCE =  7.20 ANGSTROMS                       
REMARK 525    HOH J 310        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH K 312        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH L 265        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH L 326        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH M 286        DISTANCE =  6.99 ANGSTROMS                       
REMARK 525    HOH M 293        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH M 296        DISTANCE =  5.44 ANGSTROMS                       
REMARK 525    HOH M 317        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH N 306        DISTANCE =  6.20 ANGSTROMS                       
REMARK 525    HOH O6586        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH O7345        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH O9444        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH O9906        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH P8008        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH P8942        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH P8948        DISTANCE =  6.84 ANGSTROMS                       
REMARK 525    HOH S 844        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH S 910        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH S 935        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH S 975        DISTANCE =  6.83 ANGSTROMS                       
REMARK 525    HOH S1009        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH S1028        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH T 891        DISTANCE =  5.92 ANGSTROMS                       
REMARK 525    HOH T 917        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH T 928        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH T1001        DISTANCE =  5.21 ANGSTROMS                       
REMARK 525    HOH T1004        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH T1015        DISTANCE =  5.45 ANGSTROMS                       
REMARK 525    HOH T1017        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH T1020        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH T1029        DISTANCE =  5.17 ANGSTROMS                       
REMARK 525    HOH T1030        DISTANCE =  5.23 ANGSTROMS                       
REMARK 525    HOH T1039        DISTANCE =  6.00 ANGSTROMS                       
REMARK 525    HOH U 957        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH U 974        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH U 978        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH U1012        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH U1019        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH U1028        DISTANCE =  7.77 ANGSTROMS                       
REMARK 525    HOH V 878        DISTANCE =  5.29 ANGSTROMS                       
REMARK 525    HOH V 905        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH V 908        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH V 915        DISTANCE =  5.01 ANGSTROMS                       
REMARK 525    HOH V 950        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH V 982        DISTANCE =  5.93 ANGSTROMS                       
REMARK 525    HOH V 990        DISTANCE =  6.04 ANGSTROMS                       
REMARK 525    HOH V1010        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH V1011        DISTANCE =  6.06 ANGSTROMS                       
REMARK 525    HOH V1023        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH V1046        DISTANCE =  5.61 ANGSTROMS                       
REMARK 525    HOH V1062        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH V1066        DISTANCE =  6.09 ANGSTROMS                       
REMARK 525    HOH V1067        DISTANCE =  7.28 ANGSTROMS                       
REMARK 525    HOH W 945        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH W 960        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH W1003        DISTANCE =  7.66 ANGSTROMS                       
REMARK 525    HOH W1004        DISTANCE =  6.87 ANGSTROMS                       
REMARK 525    HOH W1007        DISTANCE =  5.75 ANGSTROMS                       
REMARK 525    HOH W1008        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH W1017        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH W1022        DISTANCE =  5.94 ANGSTROMS                       
REMARK 525    HOH X 926        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH X 946        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH X 986        DISTANCE =  5.49 ANGSTROMS                       
REMARK 525    HOH X1010        DISTANCE =  5.14 ANGSTROMS                       
REMARK 525    HOH X1012        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH X1015        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH X1025        DISTANCE =  5.43 ANGSTROMS                       
REMARK 525    HOH X1026        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH X1040        DISTANCE =  6.21 ANGSTROMS                       
REMARK 525    HOH X1052        DISTANCE =  5.13 ANGSTROMS                       
REMARK 525    HOH X1057        DISTANCE =  6.44 ANGSTROMS                       
REMARK 525    HOH X1061        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH Y 888        DISTANCE =  5.53 ANGSTROMS                       
REMARK 525    HOH Y 909        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH Y 925        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH Y 966        DISTANCE =  5.28 ANGSTROMS                       
REMARK 525    HOH Y 967        DISTANCE =  5.40 ANGSTROMS                       
REMARK 525    HOH Y1017        DISTANCE =  5.78 ANGSTROMS                       
REMARK 525    HOH Y1032        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH Y1033        DISTANCE =  5.96 ANGSTROMS                       
REMARK 525    HOH Y1042        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH Z 870        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH Z1016        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH Z1021        DISTANCE =  5.99 ANGSTROMS                       
REMARK 525    HOH Z1050        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH Z1068        DISTANCE =  6.53 ANGSTROMS                       
REMARK 525    HOH Z1087        DISTANCE =  5.11 ANGSTROMS                       
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                              MG A 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX A 201   OQ1                                                    
REMARK 620 2 ASP A 203   OD1  89.3                                              
REMARK 620 3 GLU A 204   OE1  91.9  92.7                                        
REMARK 620 4 CAP A 501   O6  169.0  95.6  97.7                                  
REMARK 620 5 CAP A 501   O2   91.2 104.9 162.2  78.0                            
REMARK 620 6 CAP A 501   O3   87.6 176.7  86.3  87.6  76.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX B 201   OQ1                                                    
REMARK 620 2 ASP B 203   OD1  86.7                                              
REMARK 620 3 GLU B 204   OE1  92.8  95.7                                        
REMARK 620 4 CAP B 501   O3   87.9 174.0  87.2                                  
REMARK 620 5 CAP B 501   O2   88.0  99.8 164.6  77.4                            
REMARK 620 6 CAP B 501   O6  163.6  94.7 103.4  89.7  75.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG C 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX C 201   OQ1                                                    
REMARK 620 2 ASP C 203   OD1  89.6                                              
REMARK 620 3 GLU C 204   OE1  92.4  90.9                                        
REMARK 620 4 CAP C 501   O6  163.0  96.5 103.3                                  
REMARK 620 5 CAP C 501   O2   87.5 104.6 164.5  75.6                            
REMARK 620 6 CAP C 501   O3   83.8 173.2  88.2  90.3  76.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX D 201   OQ1                                                    
REMARK 620 2 ASP D 203   OD1  88.7                                              
REMARK 620 3 GLU D 204   OE1  96.2  92.4                                        
REMARK 620 4 CAP D 501   O6  163.0  94.6 100.2                                  
REMARK 620 5 CAP D 501   O2   86.3 104.8 162.7  76.8                            
REMARK 620 6 CAP D 501   O3   87.2 175.0  85.2  90.1  77.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX E 201   OQ1                                                    
REMARK 620 2 ASP E 203   OD1  88.6                                              
REMARK 620 3 GLU E 204   OE1  91.4  89.0                                        
REMARK 620 4 CAP E 501   O6  171.7  92.8  96.7                                  
REMARK 620 5 CAP E 501   O3   90.3 173.9  85.0  89.0                            
REMARK 620 6 CAP E 501   O2   94.3 108.0 162.1  77.5  78.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG F 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX F 201   OQ1                                                    
REMARK 620 2 ASP F 203   OD1  89.0                                              
REMARK 620 3 GLU F 204   OE1  91.7  90.1                                        
REMARK 620 4 CAP F 501   O3   89.5 175.7  85.9                                  
REMARK 620 5 CAP F 501   O6  169.0  94.8  98.5  87.4                            
REMARK 620 6 CAP F 501   O2   93.4 106.7 162.5  77.5  75.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG G 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX G 201   OQ1                                                    
REMARK 620 2 ASP G 203   OD1  91.7                                              
REMARK 620 3 GLU G 204   OE1  94.0  88.9                                        
REMARK 620 4 CAP G 501   O2   89.8 107.5 163.0                                  
REMARK 620 5 CAP G 501   O3   85.8 175.3  87.3  76.5                            
REMARK 620 6 CAP G 501   O6  164.7  95.5  99.5  75.2  87.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX H 201   OQ1                                                    
REMARK 620 2 ASP H 203   OD1  87.1                                              
REMARK 620 3 GLU H 204   OE1  92.0  90.5                                        
REMARK 620 4 CAP H 501   O3   87.1 174.1  88.6                                  
REMARK 620 5 CAP H 501   O6  166.7  94.2 101.2  91.7                            
REMARK 620 6 CAP H 501   O2   88.8 102.4 167.1  78.6  78.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG S 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX S 201   OQ1                                                    
REMARK 620 2 ASP S 203   OD1  86.9                                              
REMARK 620 3 GLU S 204   OE1  92.6  95.7                                        
REMARK 620 4 CAP S 501   O3   89.1 175.8  83.5                                  
REMARK 620 5 CAP S 501   O2   90.8 103.0 161.2  78.1                            
REMARK 620 6 CAP S 501   O6  166.4  94.3 100.8  89.9  75.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG T 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX T 201   OQ1                                                    
REMARK 620 2 ASP T 203   OD1  89.1                                              
REMARK 620 3 GLU T 204   OE1  91.1  88.1                                        
REMARK 620 4 CAP T 501   O6  170.1  95.1  98.0                                  
REMARK 620 5 CAP T 501   O3   88.5 175.0  87.5  88.0                            
REMARK 620 6 CAP T 501   O2   92.1 106.5 165.1  78.1  78.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG U 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX U 201   OQ1                                                    
REMARK 620 2 ASP U 203   OD1  89.9                                              
REMARK 620 3 GLU U 204   OE1  90.9  93.4                                        
REMARK 620 4 CAP U 501   O3   86.4 176.0  85.1                                  
REMARK 620 5 CAP U 501   O6  164.7  97.0 102.2  87.0                            
REMARK 620 6 CAP U 501   O2   89.3 104.6 162.0  77.0  75.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG V 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX V 201   OQ1                                                    
REMARK 620 2 ASP V 203   OD1  86.2                                              
REMARK 620 3 GLU V 204   OE1  88.2  91.2                                        
REMARK 620 4 CAP V 501   O6  170.0  98.9 100.2                                  
REMARK 620 5 CAP V 501   O2   92.3 107.5 161.3  78.0                            
REMARK 620 6 CAP V 501   O3   86.5 171.8  84.8  88.8  76.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG W 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX W 201   OQ1                                                    
REMARK 620 2 ASP W 203   OD1  88.9                                              
REMARK 620 3 GLU W 204   OE1  96.9  90.6                                        
REMARK 620 4 CAP W 501   O3   91.2 177.6  87.0                                  
REMARK 620 5 CAP W 501   O6  166.2  94.0  96.6  86.5                            
REMARK 620 6 CAP W 501   O2   90.9 104.9 162.9  77.5  75.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG X 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX X 201   OQ1                                                    
REMARK 620 2 ASP X 203   OD1  87.5                                              
REMARK 620 3 GLU X 204   OE1  93.6  96.0                                        
REMARK 620 4 CAP X 501   O6  165.8  96.4  99.5                                  
REMARK 620 5 CAP X 501   O3   87.4 174.7  85.8  88.2                            
REMARK 620 6 CAP X 501   O2   89.0 102.9 161.1  76.8  75.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Y 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX Y 201   OQ1                                                    
REMARK 620 2 ASP Y 203   OD1  90.5                                              
REMARK 620 3 GLU Y 204   OE1  93.2  94.6                                        
REMARK 620 4 CAP Y 501   O6  166.3  95.9  98.4                                  
REMARK 620 5 CAP Y 501   O3   87.8 178.2  84.9  85.9                            
REMARK 620 6 CAP Y 501   O2   90.7 104.4 160.5  76.0  76.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG Z 476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX Z 201   OQ1                                                    
REMARK 620 2 ASP Z 203   OD1  89.5                                              
REMARK 620 3 GLU Z 204   OE1  97.2  93.8                                        
REMARK 620 4 CAP Z 501   O3   89.5 178.5  87.5                                  
REMARK 620 5 CAP Z 501   O6  163.9  94.7  98.1  85.9                            
REMARK 620 6 CAP Z 501   O2   89.1 103.1 162.1  75.8  74.8                      
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 MG A 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG C 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG E 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG F 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG G 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG H 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG S 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG T 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG U 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG V 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG W 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG X 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Y 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG Z 476                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP C 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP D 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP F 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP G 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP S 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP T 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP U 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP V 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP W 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP X 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP Y 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP Z 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL B 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL D 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL F 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL G 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL H 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL E 620                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL W 601                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL X 602                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Y 603                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Z 604                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 605                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL T 606                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL U 607                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL V 608                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 609                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL X 610                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Y 611                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Z 612                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL S 613                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL T 614                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL U 615                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL V 616                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL X 617                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Y 618                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL Z 619                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL W 620                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1IR1   RELATED DB: PDB                                   
REMARK 900 1IR1 CONTAINS SPINACH RUBISCO COMPLEXED WITH CO2, MG2+ AND           
REMARK 900 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE                                 
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 There is a DIFFERENCE between seqres(PRO46) and                      
REMARK 999 sequence database(LEU46) in LARGE SUBUNIT.                           
REMARK 999 THERE IS NO QUESTION FROM THE ELECTRON                               
REMARK 999 DENSITY THAT the 46th residue is PRO.                                
DBREF  1IR2 A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 B    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 C    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 D    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 F    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 G    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 H    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 S    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 T    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 U    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 V    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 W    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 X    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 Y    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 Z    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1IR2 I    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 J    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 K    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 L    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 M    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 N    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 O    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 P    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 1    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 2    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 3    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 4    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 5    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 6    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 7    1   140  UNP    P08475   RBS2_CHLRE      46    185             
DBREF  1IR2 8    1   140  UNP    P08475   RBS2_CHLRE      46    185             
SEQADV 1IR2 PRO A   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP A  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP A  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX A  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC A  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC A  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO B   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP B  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP B  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX B  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC B  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC B  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO C   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP C  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP C  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX C  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC C  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC C  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO D   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP D  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP D  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX D  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC D  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC D  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO E   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP E  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP E  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX E  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC E  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC E  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO F   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP F  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP F  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX F  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC F  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC F  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO G   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP G  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP G  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX G  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC G  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC G  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO H   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP H  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP H  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX H  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC H  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC H  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO S   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP S  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP S  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX S  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC S  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC S  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO T   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP T  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP T  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX T  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC T  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC T  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO U   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP U  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP U  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX U  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC U  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC U  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO V   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP V  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP V  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX V  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC V  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC V  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO W   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP W  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP W  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX W  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC W  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC W  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO X   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP X  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP X  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX X  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC X  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC X  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO Y   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP Y  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP Y  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX Y  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC Y  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC Y  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 PRO Z   46  UNP  P00877    LEU    46 SEE REMARK 999                 
SEQADV 1IR2 HYP Z  104  UNP  P00877    PRO   104 MODIFIED RESIDUE               
SEQADV 1IR2 HYP Z  151  UNP  P00877    PRO   151 MODIFIED RESIDUE               
SEQADV 1IR2 KCX Z  201  UNP  P00877    LYS   201 MODIFIED RESIDUE               
SEQADV 1IR2 SMC Z  256  UNP  P00877    CYS   256 MODIFIED RESIDUE               
SEQADV 1IR2 SMC Z  369  UNP  P00877    CYS   369 MODIFIED RESIDUE               
SEQADV 1IR2 MME I    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME J    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME K    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME L    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME M    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME N    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME O    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME P    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME 1    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME 2    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME 3    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME 4    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME 5    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME 6    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME 7    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQADV 1IR2 MME 8    1  UNP  P08475    MET    46 MODIFIED RESIDUE               
SEQRES   1 A  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 A  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 A  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 A  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 A  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 A  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 A  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 A  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 A  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 A  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 A  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 A  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 A  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 A  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 A  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 I  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 I  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 I  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 I  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 I  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 I  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 I  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 I  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 I  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 I  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 B  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 B  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 B  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 B  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 B  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 B  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 B  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 B  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 B  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 B  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 B  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 B  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 B  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 J  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 J  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 J  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 J  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 J  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 J  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 J  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 J  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 J  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 J  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 J  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 C  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 C  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 C  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 C  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 C  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 C  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 C  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 C  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 C  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 C  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 C  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 C  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 C  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 C  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 C  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 C  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 C  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 C  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 C  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 C  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 C  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 C  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 C  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 C  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 C  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 C  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 C  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 C  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 C  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 C  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 C  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 C  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 C  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 C  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 C  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 C  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 C  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 K  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 K  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 K  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 K  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 K  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 K  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 K  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 K  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 K  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 K  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 K  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 D  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 D  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 D  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 D  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 D  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 D  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 D  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 D  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 D  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 D  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 D  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 D  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 D  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 D  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 D  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 D  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 D  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 D  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 D  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 D  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 D  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 D  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 D  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 D  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 D  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 D  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 D  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 D  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 D  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 D  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 D  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 D  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 D  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 D  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 D  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 D  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 D  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 L  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 L  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 L  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 L  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 L  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 L  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 L  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 L  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 L  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 L  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 L  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 E  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 E  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 E  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 M  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 M  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 M  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 M  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 M  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 M  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 M  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 M  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 M  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 M  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 F  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 F  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 F  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 F  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 F  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 F  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 F  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 F  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 F  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 F  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 F  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 F  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 F  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 F  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 F  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 F  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 F  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 F  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 F  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 F  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 F  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 F  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 F  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 F  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 F  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 F  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 F  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 F  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 F  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 F  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 F  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 F  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 F  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 F  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 F  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 F  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 F  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 N  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 N  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 N  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 N  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 N  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 N  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 N  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 N  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 N  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 N  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 N  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 G  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 G  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 G  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 G  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 G  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 G  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 G  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 G  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 G  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 G  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 G  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 G  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 G  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 G  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 G  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 G  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 G  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 G  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 G  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 G  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 G  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 G  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 G  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 G  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 G  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 G  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 G  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 G  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 G  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 G  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 G  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 G  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 G  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 G  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 G  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 G  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 G  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 O  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 O  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 O  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 O  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 O  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 O  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 O  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 O  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 O  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 O  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 O  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 H  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 H  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 H  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 H  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 H  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 H  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 H  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 H  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 H  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 H  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 H  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 H  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 H  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 H  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 H  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 H  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 H  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 H  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 H  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 H  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 H  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 P  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 P  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 P  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 P  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 P  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 P  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 P  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 P  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 P  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 P  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 P  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 S  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 S  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 S  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 S  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 S  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 S  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 S  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 S  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 S  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 S  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 S  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 S  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 S  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 S  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 S  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 S  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 S  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 S  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 S  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 S  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 S  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 S  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 S  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 S  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 S  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 S  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 S  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 S  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 S  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 S  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 S  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 S  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 S  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 S  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 S  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 S  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 S  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 1  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 1  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 1  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 1  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 1  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 1  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 1  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 1  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 1  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 1  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 1  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 T  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 T  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 T  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 T  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 T  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 T  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 T  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 T  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 T  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 T  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 T  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 T  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 T  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 T  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 T  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 T  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 T  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 T  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 T  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 T  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 T  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 T  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 T  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 T  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 T  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 T  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 T  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 T  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 T  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 T  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 T  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 T  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 T  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 T  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 T  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 T  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 T  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 2  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 2  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 2  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 2  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 2  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 2  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 2  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 2  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 2  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 2  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 2  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 U  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 U  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 U  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 U  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 U  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 U  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 U  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 U  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 U  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 U  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 U  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 U  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 U  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 U  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 U  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 U  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 U  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 U  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 U  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 U  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 U  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 U  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 U  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 U  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 U  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 U  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 U  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 U  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 U  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 U  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 U  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 U  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 U  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 U  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 U  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 U  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 U  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 3  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 3  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 3  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 3  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 3  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 3  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 3  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 3  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 3  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 3  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 3  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 V  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 V  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 V  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 V  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 V  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 V  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 V  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 V  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 V  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 V  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 V  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 V  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 V  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 V  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 V  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 V  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 V  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 V  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 V  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 V  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 V  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 V  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 V  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 V  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 V  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 V  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 V  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 V  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 V  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 V  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 V  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 V  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 V  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 V  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 V  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 V  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 V  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 4  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 4  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 4  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 4  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 4  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 4  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 4  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 4  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 4  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 4  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 4  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 W  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 W  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 W  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 W  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 W  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 W  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 W  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 W  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 W  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 W  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 W  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 W  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 W  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 W  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 W  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 W  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 W  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 W  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 W  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 W  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 W  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 W  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 W  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 W  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 W  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 W  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 W  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 W  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 W  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 W  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 W  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 W  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 W  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 W  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 W  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 W  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 W  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 5  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 5  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 5  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 5  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 5  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 5  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 5  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 5  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 5  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 5  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 5  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 X  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 X  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 X  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 X  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 X  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 X  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 X  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 X  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 X  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 X  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 X  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 X  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 X  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 X  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 X  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 X  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 X  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 X  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 X  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 X  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 X  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 X  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 X  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 X  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 X  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 X  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 X  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 X  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 X  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 X  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 X  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 X  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 X  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 X  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 X  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 X  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 X  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 6  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 6  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 6  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 6  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 6  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 6  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 6  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 6  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 6  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 6  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 6  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 Y  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 Y  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 Y  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 Y  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 Y  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 Y  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 Y  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 Y  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 Y  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 Y  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 Y  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 Y  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 Y  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 Y  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 Y  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 Y  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 Y  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 Y  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 Y  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 Y  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 Y  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 Y  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 Y  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 Y  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 Y  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 Y  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 Y  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 Y  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 Y  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 Y  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 Y  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 Y  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 Y  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 Y  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 Y  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 Y  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 Y  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 7  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 7  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 7  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 7  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 7  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 7  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 7  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 7  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 7  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 7  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 7  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
SEQRES   1 Z  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 Z  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 Z  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 Z  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 Z  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 Z  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 Z  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 Z  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 Z  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 Z  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 Z  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 Z  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 Z  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 Z  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 Z  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 Z  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 Z  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 Z  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 Z  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 Z  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 Z  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 Z  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 Z  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 Z  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 Z  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 Z  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 Z  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 Z  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 Z  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 Z  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 Z  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 Z  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 Z  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 Z  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 Z  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 Z  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 Z  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 8  140  MME MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 8  140  THR PHE SER TYR LEU PRO PRO LEU SER ASP GLU GLN ILE          
SEQRES   3 8  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 8  140  PRO CYS LEU GLU PHE ALA GLU SER ASP LYS ALA TYR VAL          
SEQRES   5 8  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 8  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 8  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 8  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 8  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 8  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 8  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
MODRES 1IR2 HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX A  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC A  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC A  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME I    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP B  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP B  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX B  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC B  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC B  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME J    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP C  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP C  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX C  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC C  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC C  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME K    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP D  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP D  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX D  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC D  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC D  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME L    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX E  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC E  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC E  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME M    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP F  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP F  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX F  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC F  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC F  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME N    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP G  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP G  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX G  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC G  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC G  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME O    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP H  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP H  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX H  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC H  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC H  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME P    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP S  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP S  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX S  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC S  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC S  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME 1    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP T  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP T  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX T  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC T  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC T  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME 2    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP U  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP U  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX U  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC U  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC U  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME 3    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP V  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP V  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX V  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC V  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC V  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME 4    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP W  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP W  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX W  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC W  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC W  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME 5    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP X  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP X  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX X  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC X  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC X  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME 6    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP Y  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP Y  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX Y  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC Y  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC Y  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME 7    1  MET  N-METHYL METHIONINE                                
MODRES 1IR2 HYP Z  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 HYP Z  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1IR2 KCX Z  201  LYS  LYSINE NZ-CARBOXYLIC ACID                          
MODRES 1IR2 SMC Z  256  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 SMC Z  369  CYS  S-METHYLCYSTEINE                                   
MODRES 1IR2 MME 8    1  MET  N-METHYL METHIONINE                                
HET    HYP  A 104       8                                                       
HET    HYP  A 151       8                                                       
HET    KCX  A 201      12                                                       
HET    SMC  A 256       7                                                       
HET    SMC  A 369       7                                                       
HET    MME  I   1       9                                                       
HET    HYP  B 104       8                                                       
HET    HYP  B 151       8                                                       
HET    KCX  B 201      12                                                       
HET    SMC  B 256       7                                                       
HET    SMC  B 369       7                                                       
HET    MME  J   1       9                                                       
HET    HYP  C 104       8                                                       
HET    HYP  C 151       8                                                       
HET    KCX  C 201      12                                                       
HET    SMC  C 256       7                                                       
HET    SMC  C 369       7                                                       
HET    MME  K   1       9                                                       
HET    HYP  D 104       8                                                       
HET    HYP  D 151       8                                                       
HET    KCX  D 201      12                                                       
HET    SMC  D 256       7                                                       
HET    SMC  D 369       7                                                       
HET    MME  L   1       9                                                       
HET    HYP  E 104       8                                                       
HET    HYP  E 151       8                                                       
HET    KCX  E 201      12                                                       
HET    SMC  E 256       7                                                       
HET    SMC  E 369       7                                                       
HET    MME  M   1       9                                                       
HET    HYP  F 104       8                                                       
HET    HYP  F 151       8                                                       
HET    KCX  F 201      12                                                       
HET    SMC  F 256       7                                                       
HET    SMC  F 369       7                                                       
HET    MME  N   1       9                                                       
HET    HYP  G 104       8                                                       
HET    HYP  G 151       8                                                       
HET    KCX  G 201      12                                                       
HET    SMC  G 256       7                                                       
HET    SMC  G 369       7                                                       
HET    MME  O   1       9                                                       
HET    HYP  H 104       8                                                       
HET    HYP  H 151       8                                                       
HET    KCX  H 201      12                                                       
HET    SMC  H 256       7                                                       
HET    SMC  H 369       7                                                       
HET    MME  P   1       9                                                       
HET    HYP  S 104       8                                                       
HET    HYP  S 151       8                                                       
HET    KCX  S 201      12                                                       
HET    SMC  S 256       7                                                       
HET    SMC  S 369       7                                                       
HET    MME  1   1       9                                                       
HET    HYP  T 104       8                                                       
HET    HYP  T 151       8                                                       
HET    KCX  T 201      12                                                       
HET    SMC  T 256       7                                                       
HET    SMC  T 369       7                                                       
HET    MME  2   1       9                                                       
HET    HYP  U 104       8                                                       
HET    HYP  U 151       8                                                       
HET    KCX  U 201      12                                                       
HET    SMC  U 256       7                                                       
HET    SMC  U 369       7                                                       
HET    MME  3   1       9                                                       
HET    HYP  V 104       8                                                       
HET    HYP  V 151       8                                                       
HET    KCX  V 201      12                                                       
HET    SMC  V 256       7                                                       
HET    SMC  V 369       7                                                       
HET    MME  4   1       9                                                       
HET    HYP  W 104       8                                                       
HET    HYP  W 151       8                                                       
HET    KCX  W 201      12                                                       
HET    SMC  W 256       7                                                       
HET    SMC  W 369       7                                                       
HET    MME  5   1       9                                                       
HET    HYP  X 104       8                                                       
HET    HYP  X 151       8                                                       
HET    KCX  X 201      12                                                       
HET    SMC  X 256       7                                                       
HET    SMC  X 369       7                                                       
HET    MME  6   1       9                                                       
HET    HYP  Y 104       8                                                       
HET    HYP  Y 151       8                                                       
HET    KCX  Y 201      12                                                       
HET    SMC  Y 256       7                                                       
HET    SMC  Y 369       7                                                       
HET    MME  7   1       9                                                       
HET    HYP  Z 104       8                                                       
HET    HYP  Z 151       8                                                       
HET    KCX  Z 201      12                                                       
HET    SMC  Z 256       7                                                       
HET    SMC  Z 369       7                                                       
HET    MME  8   1       9                                                       
HET     MG  A 476       1                                                       
HET     MG  B 476       1                                                       
HET     MG  C 476       1                                                       
HET     MG  D 476       1                                                       
HET     MG  E 476       1                                                       
HET     MG  F 476       1                                                       
HET     MG  G 476       1                                                       
HET     MG  H 476       1                                                       
HET     MG  S 476       1                                                       
HET     MG  T 476       1                                                       
HET     MG  U 476       1                                                       
HET     MG  V 476       1                                                       
HET     MG  W 476       1                                                       
HET     MG  X 476       1                                                       
HET     MG  Y 476       1                                                       
HET     MG  Z 476       1                                                       
HET    CAP  A 501      21                                                       
HET    CAP  B 501      21                                                       
HET    CAP  C 501      21                                                       
HET    CAP  D 501      21                                                       
HET    CAP  E 501      21                                                       
HET    CAP  F 501      21                                                       
HET    CAP  G 501      21                                                       
HET    CAP  H 501      21                                                       
HET    CAP  S 501      21                                                       
HET    CAP  T 501      21                                                       
HET    CAP  U 501      21                                                       
HET    CAP  V 501      21                                                       
HET    CAP  W 501      21                                                       
HET    CAP  X 501      21                                                       
HET    CAP  Y 501      21                                                       
HET    CAP  Z 501      21                                                       
HET    GOL  E 601       6                                                       
HET    GOL  F 602       6                                                       
HET    GOL  G 603       6                                                       
HET    GOL  H 604       6                                                       
HET    GOL  A 605       6                                                       
HET    GOL  B 606       6                                                       
HET    GOL  C 607       6                                                       
HET    GOL  D 608       6                                                       
HET    GOL  E 609       6                                                       
HET    GOL  B 610       6                                                       
HET    GOL  G 611       6                                                       
HET    GOL  H 612       6                                                       
HET    GOL  A 613       6                                                       
HET    GOL  B 614       6                                                       
HET    GOL  C 615       6                                                       
HET    GOL  D 616       6                                                       
HET    GOL  F 617       6                                                       
HET    GOL  G 618       6                                                       
HET    GOL  H 619       6                                                       
HET    GOL  E 620       6                                                       
HET    GOL  W 601       6                                                       
HET    GOL  X 602       6                                                       
HET    GOL  Y 603       6                                                       
HET    GOL  Z 604       6                                                       
HET    GOL  S 605       6                                                       
HET    GOL  T 606       6                                                       
HET    GOL  U 607       6                                                       
HET    GOL  V 608       6                                                       
HET    GOL  S 609       6                                                       
HET    GOL  X 610       6                                                       
HET    GOL  Y 611       6                                                       
HET    GOL  Z 612       6                                                       
HET    GOL  S 613       6                                                       
HET    GOL  T 614       6                                                       
HET    GOL  U 615       6                                                       
HET    GOL  V 616       6                                                       
HET    GOL  X 617       6                                                       
HET    GOL  Y 618       6                                                       
HET    GOL  Z 619       6                                                       
HET    GOL  W 620       6                                                       
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     SMC S-METHYLCYSTEINE                                                 
HETNAM     MME N-METHYL METHIONINE                                              
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM     GOL GLYCEROL                                                         
HETSYN     HYP HYDROXYPROLINE                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  HYP    32(C5 H9 N O3)                                               
FORMUL   1  KCX    16(C7 H14 N2 O4)                                             
FORMUL   1  SMC    32(C4 H9 N O2 S)                                             
FORMUL   2  MME    16(C6 H13 N O2 S)                                            
FORMUL  33   MG    16(MG 2+)                                                    
FORMUL  49  CAP    16(C6 H14 O13 P2)                                            
FORMUL  65  GOL    40(C3 H8 O3)                                                 
FORMUL  10  HOH   *9999(H2 O)                                                   
HELIX    1   1 TYR A   20  TYR A   25  1                                   6    
HELIX    2   2 PRO A   49  GLU A   60  1                                  12    
HELIX    3   3 VAL A   69  THR A   75  5                                   7    
HELIX    4   4 SER A   76  LYS A   81  1                                   6    
HELIX    5   5 HYP A  104  PHE A  108  5                                   5    
HELIX    6   6 SER A  112  GLY A  122  1                                  11    
HELIX    7   7 ASN A  123  PHE A  127  5                                   5    
HELIX    8   8 PRO A  141  LYS A  146  1                                   6    
HELIX    9   9 GLY A  154  ASN A  163  1                                  10    
HELIX   10  10 SER A  181  GLY A  195  1                                  15    
HELIX   11  11 ARG A  213  GLY A  233  1                                  21    
HELIX   12  12 THR A  246  GLY A  261  1                                  16    
HELIX   13  13 TYR A  269  GLY A  273  1                                   5    
HELIX   14  14 GLY A  273  GLY A  288  1                                  16    
HELIX   15  15 MET A  297  ARG A  303  1                                   7    
HELIX   16  16 HIS A  310  GLY A  322  1                                  13    
HELIX   17  17 GLU A  338  ASP A  351  1                                  14    
HELIX   18  18 ASP A  357  GLY A  361  5                                   5    
HELIX   19  19 HIS A  383  TRP A  385  5                                   3    
HELIX   20  20 HIS A  386  GLY A  395  1                                  10    
HELIX   21  21 GLY A  403  GLY A  408  1                                   6    
HELIX   22  22 GLY A  412  GLU A  433  1                                  22    
HELIX   23  23 ASP A  436  LYS A  450  1                                  15    
HELIX   24  24 SER A  452  LYS A  463  1                                  12    
HELIX   25  25 SER I   22  ASN I   36  1                                  15    
HELIX   26  26 GLU I   46  ALA I   50  5                                   5    
HELIX   27  27 ASN I   54  PHE I   60  5                                   7    
HELIX   28  28 ASP I   85  PHE I  100  1                                  16    
HELIX   29  29 PRO I  134  ARG I  138  5                                   5    
HELIX   30  30 TYR B   20  TYR B   25  1                                   6    
HELIX   31  31 PRO B   49  GLU B   60  1                                  12    
HELIX   32  32 VAL B   69  THR B   75  5                                   7    
HELIX   33  33 SER B   76  LYS B   81  1                                   6    
HELIX   34  34 HYP B  104  PHE B  108  5                                   5    
HELIX   35  35 SER B  112  VAL B  121  1                                  10    
HELIX   36  36 ASN B  123  PHE B  127  5                                   5    
HELIX   37  37 PRO B  141  LYS B  146  1                                   6    
HELIX   38  38 GLY B  154  ASN B  163  1                                  10    
HELIX   39  39 SER B  181  GLY B  195  1                                  15    
HELIX   40  40 ARG B  213  GLY B  233  1                                  21    
HELIX   41  41 THR B  246  GLY B  261  1                                  16    
HELIX   42  42 TYR B  269  GLY B  273  1                                   5    
HELIX   43  43 GLY B  273  GLY B  288  1                                  16    
HELIX   44  44 MET B  297  ARG B  303  1                                   7    
HELIX   45  45 HIS B  310  GLY B  322  1                                  13    
HELIX   46  46 GLU B  338  ASP B  351  1                                  14    
HELIX   47  47 ASP B  357  GLY B  361  5                                   5    
HELIX   48  48 HIS B  383  TRP B  385  5                                   3    
HELIX   49  49 HIS B  386  GLY B  395  1                                  10    
HELIX   50  50 GLY B  403  GLY B  408  1                                   6    
HELIX   51  51 GLY B  412  GLU B  433  1                                  22    
HELIX   52  52 ASP B  436  LYS B  450  1                                  15    
HELIX   53  53 SER B  452  LYS B  463  1                                  12    
HELIX   54  54 SER J   22  ASN J   36  1                                  15    
HELIX   55  55 GLU J   46  ALA J   50  5                                   5    
HELIX   56  56 ASN J   54  PHE J   60  5                                   7    
HELIX   57  57 ASP J   85  PHE J  100  1                                  16    
HELIX   58  58 PRO J  134  LYS J  137  5                                   4    
HELIX   59  59 TYR C   20  TYR C   25  1                                   6    
HELIX   60  60 PRO C   49  SER C   61  1                                  13    
HELIX   61  61 VAL C   69  THR C   75  5                                   7    
HELIX   62  62 SER C   76  LYS C   81  1                                   6    
HELIX   63  63 HYP C  104  PHE C  108  5                                   5    
HELIX   64  64 SER C  112  GLY C  122  1                                  11    
HELIX   65  65 ASN C  123  PHE C  127  5                                   5    
HELIX   66  66 PRO C  141  LYS C  146  1                                   6    
HELIX   67  67 GLY C  154  ASN C  163  1                                  10    
HELIX   68  68 SER C  181  GLY C  195  1                                  15    
HELIX   69  69 ARG C  213  GLY C  233  1                                  21    
HELIX   70  70 THR C  246  GLY C  261  1                                  16    
HELIX   71  71 TYR C  269  GLY C  273  1                                   5    
HELIX   72  72 GLY C  273  GLY C  288  1                                  16    
HELIX   73  73 MET C  297  ARG C  303  1                                   7    
HELIX   74  74 HIS C  310  GLY C  322  1                                  13    
HELIX   75  75 GLU C  338  ASP C  351  1                                  14    
HELIX   76  76 ASP C  357  GLY C  361  5                                   5    
HELIX   77  77 HIS C  383  TRP C  385  5                                   3    
HELIX   78  78 HIS C  386  GLY C  395  1                                  10    
HELIX   79  79 GLY C  403  GLY C  408  1                                   6    
HELIX   80  80 GLY C  412  GLU C  433  1                                  22    
HELIX   81  81 ASP C  436  LYS C  450  1                                  15    
HELIX   82  82 SER C  452  LYS C  463  1                                  12    
HELIX   83  83 SER K   22  ASN K   36  1                                  15    
HELIX   84  84 GLU K   46  ALA K   50  5                                   5    
HELIX   85  85 ASN K   54  PHE K   60  5                                   7    
HELIX   86  86 ASP K   85  PHE K  100  1                                  16    
HELIX   87  87 PRO K  134  LYS K  137  5                                   4    
HELIX   88  88 TYR D   20  TYR D   25  1                                   6    
HELIX   89  89 PRO D   49  SER D   61  1                                  13    
HELIX   90  90 VAL D   69  THR D   75  5                                   7    
HELIX   91  91 SER D   76  LYS D   81  1                                   6    
HELIX   92  92 HYP D  104  PHE D  108  5                                   5    
HELIX   93  93 SER D  112  VAL D  121  1                                  10    
HELIX   94  94 ASN D  123  PHE D  127  5                                   5    
HELIX   95  95 PRO D  141  LYS D  146  1                                   6    
HELIX   96  96 GLY D  154  ASN D  163  1                                  10    
HELIX   97  97 SER D  181  GLY D  195  1                                  15    
HELIX   98  98 ARG D  213  GLY D  233  1                                  21    
HELIX   99  99 THR D  246  GLY D  261  1                                  16    
HELIX  100 100 TYR D  269  GLY D  273  1                                   5    
HELIX  101 101 GLY D  273  GLY D  288  1                                  16    
HELIX  102 102 MET D  297  ARG D  303  1                                   7    
HELIX  103 103 HIS D  310  GLY D  322  1                                  13    
HELIX  104 104 GLU D  338  ASP D  351  1                                  14    
HELIX  105 105 ASP D  357  GLY D  361  5                                   5    
HELIX  106 106 HIS D  383  TRP D  385  5                                   3    
HELIX  107 107 HIS D  386  GLY D  395  1                                  10    
HELIX  108 108 GLY D  403  GLY D  408  1                                   6    
HELIX  109 109 GLY D  412  GLU D  433  1                                  22    
HELIX  110 110 ASP D  436  LYS D  450  1                                  15    
HELIX  111 111 SER D  452  LYS D  463  1                                  12    
HELIX  112 112 SER L   22  ASN L   36  1                                  15    
HELIX  113 113 GLU L   46  ALA L   50  5                                   5    
HELIX  114 114 ASN L   54  PHE L   60  5                                   7    
HELIX  115 115 ASP L   85  PHE L  100  1                                  16    
HELIX  116 116 PRO L  134  LYS L  137  5                                   4    
HELIX  117 117 TYR E   20  TYR E   25  1                                   6    
HELIX  118 118 PRO E   49  SER E   61  1                                  13    
HELIX  119 119 VAL E   69  THR E   75  5                                   7    
HELIX  120 120 SER E   76  LYS E   81  1                                   6    
HELIX  121 121 HYP E  104  PHE E  108  5                                   5    
HELIX  122 122 SER E  112  VAL E  121  1                                  10    
HELIX  123 123 ASN E  123  PHE E  127  5                                   5    
HELIX  124 124 PRO E  141  LYS E  146  1                                   6    
HELIX  125 125 GLY E  154  ASN E  163  1                                  10    
HELIX  126 126 SER E  181  GLY E  195  1                                  15    
HELIX  127 127 ARG E  213  GLY E  233  1                                  21    
HELIX  128 128 THR E  246  GLY E  261  1                                  16    
HELIX  129 129 TYR E  269  GLY E  273  1                                   5    
HELIX  130 130 GLY E  273  GLY E  288  1                                  16    
HELIX  131 131 MET E  297  ARG E  303  1                                   7    
HELIX  132 132 HIS E  310  GLY E  322  1                                  13    
HELIX  133 133 GLU E  338  ASP E  351  1                                  14    
HELIX  134 134 ASP E  357  GLY E  361  5                                   5    
HELIX  135 135 HIS E  383  TRP E  385  5                                   3    
HELIX  136 136 HIS E  386  GLY E  395  1                                  10    
HELIX  137 137 GLY E  403  GLY E  408  1                                   6    
HELIX  138 138 GLY E  412  GLU E  433  1                                  22    
HELIX  139 139 ASP E  436  SER E  452  1                                  17    
HELIX  140 140 SER E  452  LYS E  463  1                                  12    
HELIX  141 141 SER M   22  ASN M   36  1                                  15    
HELIX  142 142 GLU M   46  ALA M   50  5                                   5    
HELIX  143 143 ASN M   54  PHE M   60  5                                   7    
HELIX  144 144 ASP M   85  PHE M  100  1                                  16    
HELIX  145 145 PRO M  134  LYS M  137  5                                   4    
HELIX  146 146 TYR F   20  TYR F   25  1                                   6    
HELIX  147 147 PRO F   49  GLU F   60  1                                  12    
HELIX  148 148 VAL F   69  THR F   75  5                                   7    
HELIX  149 149 SER F   76  LYS F   81  1                                   6    
HELIX  150 150 HYP F  104  PHE F  108  5                                   5    
HELIX  151 151 SER F  112  VAL F  121  1                                  10    
HELIX  152 152 ASN F  123  PHE F  127  5                                   5    
HELIX  153 153 PRO F  141  LYS F  146  1                                   6    
HELIX  154 154 GLY F  154  ASN F  163  1                                  10    
HELIX  155 155 SER F  181  GLY F  195  1                                  15    
HELIX  156 156 ARG F  213  GLY F  233  1                                  21    
HELIX  157 157 THR F  246  GLY F  261  1                                  16    
HELIX  158 158 TYR F  269  GLY F  273  1                                   5    
HELIX  159 159 GLY F  273  GLY F  288  1                                  16    
HELIX  160 160 MET F  297  ARG F  303  1                                   7    
HELIX  161 161 HIS F  310  GLY F  322  1                                  13    
HELIX  162 162 GLU F  338  ASP F  351  1                                  14    
HELIX  163 163 ASP F  357  GLY F  361  5                                   5    
HELIX  164 164 HIS F  383  TRP F  385  5                                   3    
HELIX  165 165 HIS F  386  GLY F  395  1                                  10    
HELIX  166 166 GLY F  403  GLY F  408  1                                   6    
HELIX  167 167 GLY F  412  GLU F  433  1                                  22    
HELIX  168 168 ASP F  436  LYS F  450  1                                  15    
HELIX  169 169 SER F  452  LYS F  463  1                                  12    
HELIX  170 170 SER N   22  ASN N   36  1                                  15    
HELIX  171 171 GLU N   46  ALA N   50  5                                   5    
HELIX  172 172 ASN N   54  PHE N   60  5                                   7    
HELIX  173 173 ASP N   85  PHE N  100  1                                  16    
HELIX  174 174 PRO N  134  LYS N  137  5                                   4    
HELIX  175 175 TYR G   20  TYR G   25  1                                   6    
HELIX  176 176 PRO G   49  GLU G   60  1                                  12    
HELIX  177 177 VAL G   69  THR G   75  5                                   7    
HELIX  178 178 SER G   76  LYS G   81  1                                   6    
HELIX  179 179 HYP G  104  PHE G  108  5                                   5    
HELIX  180 180 SER G  112  GLY G  122  1                                  11    
HELIX  181 181 ASN G  123  PHE G  127  5                                   5    
HELIX  182 182 PRO G  141  LYS G  146  1                                   6    
HELIX  183 183 GLY G  154  ASN G  163  1                                  10    
HELIX  184 184 SER G  181  ARG G  194  1                                  14    
HELIX  185 185 ARG G  213  GLY G  233  1                                  21    
HELIX  186 186 THR G  246  GLY G  261  1                                  16    
HELIX  187 187 TYR G  269  GLY G  273  1                                   5    
HELIX  188 188 GLY G  273  GLY G  288  1                                  16    
HELIX  189 189 MET G  297  ARG G  303  1                                   7    
HELIX  190 190 HIS G  310  GLY G  322  1                                  13    
HELIX  191 191 GLU G  338  ASP G  351  1                                  14    
HELIX  192 192 ASP G  357  GLY G  361  5                                   5    
HELIX  193 193 HIS G  383  TRP G  385  5                                   3    
HELIX  194 194 HIS G  386  GLY G  395  1                                  10    
HELIX  195 195 GLY G  403  GLY G  408  1                                   6    
HELIX  196 196 GLY G  412  GLU G  433  1                                  22    
HELIX  197 197 ASP G  436  LYS G  450  1                                  15    
HELIX  198 198 SER G  452  LYS G  463  1                                  12    
HELIX  199 199 SER O   22  ASN O   36  1                                  15    
HELIX  200 200 GLU O   46  ALA O   50  5                                   5    
HELIX  201 201 ASN O   54  PHE O   60  5                                   7    
HELIX  202 202 ASP O   85  PHE O  100  1                                  16    
HELIX  203 203 PRO O  134  LYS O  137  5                                   4    
HELIX  204 204 TYR H   20  TYR H   25  1                                   6    
HELIX  205 205 PRO H   49  GLU H   60  1                                  12    
HELIX  206 206 VAL H   69  THR H   75  5                                   7    
HELIX  207 207 SER H   76  LYS H   81  1                                   6    
HELIX  208 208 HYP H  104  PHE H  108  5                                   5    
HELIX  209 209 SER H  112  VAL H  121  1                                  10    
HELIX  210 210 ASN H  123  PHE H  127  5                                   5    
HELIX  211 211 PRO H  141  LYS H  146  1                                   6    
HELIX  212 212 GLY H  154  ASN H  163  1                                  10    
HELIX  213 213 SER H  181  GLY H  195  1                                  15    
HELIX  214 214 ARG H  213  GLY H  233  1                                  21    
HELIX  215 215 THR H  246  GLY H  261  1                                  16    
HELIX  216 216 TYR H  269  GLY H  273  1                                   5    
HELIX  217 217 GLY H  273  GLY H  288  1                                  16    
HELIX  218 218 MET H  297  ARG H  303  1                                   7    
HELIX  219 219 HIS H  310  GLY H  322  1                                  13    
HELIX  220 220 GLU H  338  ASP H  351  1                                  14    
HELIX  221 221 ASP H  357  GLY H  361  5                                   5    
HELIX  222 222 HIS H  383  TRP H  385  5                                   3    
HELIX  223 223 HIS H  386  GLY H  395  1                                  10    
HELIX  224 224 GLY H  403  GLY H  408  1                                   6    
HELIX  225 225 GLY H  412  GLU H  433  1                                  22    
HELIX  226 226 ASP H  436  LYS H  450  1                                  15    
HELIX  227 227 SER H  452  LYS H  463  1                                  12    
HELIX  228 228 SER P   22  ASN P   36  1                                  15    
HELIX  229 229 GLU P   46  ALA P   50  5                                   5    
HELIX  230 230 ASN P   54  PHE P   60  5                                   7    
HELIX  231 231 ASP P   85  PHE P  100  1                                  16    
HELIX  232 232 PRO P  134  ARG P  138  5                                   5    
HELIX  233 233 TYR S   20  TYR S   25  1                                   6    
HELIX  234 234 PRO S   49  GLU S   60  1                                  12    
HELIX  235 235 VAL S   69  THR S   75  5                                   7    
HELIX  236 236 SER S   76  LYS S   81  1                                   6    
HELIX  237 237 HYP S  104  PHE S  108  5                                   5    
HELIX  238 238 SER S  112  GLY S  122  1                                  11    
HELIX  239 239 ASN S  123  PHE S  127  5                                   5    
HELIX  240 240 PRO S  141  LYS S  146  1                                   6    
HELIX  241 241 GLY S  154  ASN S  163  1                                  10    
HELIX  242 242 SER S  181  ARG S  194  1                                  14    
HELIX  243 243 ARG S  213  GLY S  233  1                                  21    
HELIX  244 244 THR S  246  GLY S  261  1                                  16    
HELIX  245 245 TYR S  269  GLY S  273  1                                   5    
HELIX  246 246 GLY S  273  GLY S  288  1                                  16    
HELIX  247 247 MET S  297  ARG S  303  1                                   7    
HELIX  248 248 HIS S  310  GLY S  322  1                                  13    
HELIX  249 249 GLU S  338  ASP S  351  1                                  14    
HELIX  250 250 ASP S  357  GLY S  361  5                                   5    
HELIX  251 251 HIS S  383  TRP S  385  5                                   3    
HELIX  252 252 HIS S  386  GLY S  395  1                                  10    
HELIX  253 253 GLY S  403  GLY S  408  1                                   6    
HELIX  254 254 GLY S  412  GLU S  433  1                                  22    
HELIX  255 255 ASP S  436  LYS S  450  1                                  15    
HELIX  256 256 SER S  452  LYS S  463  1                                  12    
HELIX  257 257 SER 1   22  ASN 1   36  1                                  15    
HELIX  258 258 GLU 1   46  ALA 1   50  5                                   5    
HELIX  259 259 ASN 1   54  PHE 1   60  5                                   7    
HELIX  260 260 ASP 1   85  PHE 1  100  1                                  16    
HELIX  261 261 PRO 1  134  LYS 1  137  5                                   4    
HELIX  262 262 TYR T   20  TYR T   25  1                                   6    
HELIX  263 263 PRO T   49  SER T   61  1                                  13    
HELIX  264 264 VAL T   69  THR T   75  5                                   7    
HELIX  265 265 SER T   76  LYS T   81  1                                   6    
HELIX  266 266 HYP T  104  PHE T  108  5                                   5    
HELIX  267 267 SER T  112  VAL T  121  1                                  10    
HELIX  268 268 ASN T  123  PHE T  127  5                                   5    
HELIX  269 269 PRO T  141  LYS T  146  1                                   6    
HELIX  270 270 GLY T  154  ASN T  163  1                                  10    
HELIX  271 271 SER T  181  GLY T  195  1                                  15    
HELIX  272 272 ARG T  213  GLY T  233  1                                  21    
HELIX  273 273 THR T  246  GLY T  261  1                                  16    
HELIX  274 274 TYR T  269  GLY T  273  1                                   5    
HELIX  275 275 GLY T  273  GLY T  288  1                                  16    
HELIX  276 276 MET T  297  ARG T  303  1                                   7    
HELIX  277 277 HIS T  310  GLY T  322  1                                  13    
HELIX  278 278 GLU T  338  ASP T  351  1                                  14    
HELIX  279 279 ASP T  357  GLY T  361  5                                   5    
HELIX  280 280 HIS T  383  TRP T  385  5                                   3    
HELIX  281 281 HIS T  386  GLY T  395  1                                  10    
HELIX  282 282 GLY T  403  GLY T  408  1                                   6    
HELIX  283 283 GLY T  412  GLU T  433  1                                  22    
HELIX  284 284 ASP T  436  LYS T  450  1                                  15    
HELIX  285 285 SER T  452  LYS T  463  1                                  12    
HELIX  286 286 SER 2   22  ASN 2   36  1                                  15    
HELIX  287 287 GLU 2   46  ALA 2   50  5                                   5    
HELIX  288 288 ASN 2   54  PHE 2   60  5                                   7    
HELIX  289 289 ASP 2   85  PHE 2  100  1                                  16    
HELIX  290 290 PRO 2  134  LYS 2  137  5                                   4    
HELIX  291 291 TYR U   20  TYR U   25  1                                   6    
HELIX  292 292 PRO U   49  GLU U   60  1                                  12    
HELIX  293 293 VAL U   69  THR U   75  5                                   7    
HELIX  294 294 SER U   76  LYS U   81  1                                   6    
HELIX  295 295 HYP U  104  PHE U  108  5                                   5    
HELIX  296 296 SER U  112  VAL U  121  1                                  10    
HELIX  297 297 ASN U  123  PHE U  127  5                                   5    
HELIX  298 298 PRO U  141  LYS U  146  1                                   6    
HELIX  299 299 GLY U  154  ASN U  163  1                                  10    
HELIX  300 300 SER U  181  GLY U  195  1                                  15    
HELIX  301 301 ARG U  213  GLY U  233  1                                  21    
HELIX  302 302 THR U  246  GLY U  261  1                                  16    
HELIX  303 303 TYR U  269  GLY U  273  1                                   5    
HELIX  304 304 GLY U  273  GLY U  288  1                                  16    
HELIX  305 305 MET U  297  ARG U  303  1                                   7    
HELIX  306 306 HIS U  310  GLY U  322  1                                  13    
HELIX  307 307 GLU U  338  ASP U  351  1                                  14    
HELIX  308 308 ASP U  357  GLY U  361  5                                   5    
HELIX  309 309 HIS U  383  TRP U  385  5                                   3    
HELIX  310 310 HIS U  386  GLY U  395  1                                  10    
HELIX  311 311 GLY U  403  GLY U  408  1                                   6    
HELIX  312 312 GLY U  412  GLU U  433  1                                  22    
HELIX  313 313 ASP U  436  LYS U  450  1                                  15    
HELIX  314 314 SER U  452  LYS U  463  1                                  12    
HELIX  315 315 SER 3   22  ASN 3   36  1                                  15    
HELIX  316 316 GLU 3   46  ALA 3   50  5                                   5    
HELIX  317 317 ASN 3   54  PHE 3   60  5                                   7    
HELIX  318 318 ASP 3   85  PHE 3  100  1                                  16    
HELIX  319 319 PRO 3  134  LYS 3  137  5                                   4    
HELIX  320 320 TYR V   20  TYR V   25  1                                   6    
HELIX  321 321 PRO V   49  GLU V   60  1                                  12    
HELIX  322 322 VAL V   69  THR V   75  5                                   7    
HELIX  323 323 SER V   76  LYS V   81  1                                   6    
HELIX  324 324 HYP V  104  PHE V  108  5                                   5    
HELIX  325 325 SER V  112  VAL V  121  1                                  10    
HELIX  326 326 ASN V  123  PHE V  127  5                                   5    
HELIX  327 327 PRO V  141  LYS V  146  1                                   6    
HELIX  328 328 GLY V  154  ASN V  163  1                                  10    
HELIX  329 329 SER V  181  GLY V  195  1                                  15    
HELIX  330 330 ARG V  213  GLY V  233  1                                  21    
HELIX  331 331 THR V  246  GLY V  261  1                                  16    
HELIX  332 332 TYR V  269  GLY V  273  1                                   5    
HELIX  333 333 GLY V  273  GLY V  288  1                                  16    
HELIX  334 334 MET V  297  ARG V  303  1                                   7    
HELIX  335 335 HIS V  310  GLY V  322  1                                  13    
HELIX  336 336 GLU V  338  ASP V  351  1                                  14    
HELIX  337 337 ASP V  357  GLY V  361  5                                   5    
HELIX  338 338 HIS V  383  TRP V  385  5                                   3    
HELIX  339 339 HIS V  386  GLY V  395  1                                  10    
HELIX  340 340 GLY V  403  GLY V  408  1                                   6    
HELIX  341 341 GLY V  412  GLU V  433  1                                  22    
HELIX  342 342 ASP V  436  SER V  452  1                                  17    
HELIX  343 343 SER V  452  LYS V  463  1                                  12    
HELIX  344 344 SER 4   22  ASN 4   36  1                                  15    
HELIX  345 345 GLU 4   46  ALA 4   50  5                                   5    
HELIX  346 346 ASN 4   54  PHE 4   60  5                                   7    
HELIX  347 347 ASP 4   85  PHE 4  100  1                                  16    
HELIX  348 348 PRO 4  134  ARG 4  138  5                                   5    
HELIX  349 349 TYR W   20  TYR W   25  1                                   6    
HELIX  350 350 PRO W   49  GLU W   60  1                                  12    
HELIX  351 351 VAL W   69  THR W   75  5                                   7    
HELIX  352 352 SER W   76  LYS W   81  1                                   6    
HELIX  353 353 HYP W  104  PHE W  108  5                                   5    
HELIX  354 354 SER W  112  VAL W  121  1                                  10    
HELIX  355 355 ASN W  123  PHE W  127  5                                   5    
HELIX  356 356 PRO W  141  LYS W  146  1                                   6    
HELIX  357 357 GLY W  154  ASN W  163  1                                  10    
HELIX  358 358 SER W  181  GLY W  195  1                                  15    
HELIX  359 359 ARG W  213  GLY W  233  1                                  21    
HELIX  360 360 THR W  246  GLY W  261  1                                  16    
HELIX  361 361 TYR W  269  GLY W  273  1                                   5    
HELIX  362 362 GLY W  273  GLY W  288  1                                  16    
HELIX  363 363 MET W  297  ARG W  303  1                                   7    
HELIX  364 364 HIS W  310  GLY W  322  1                                  13    
HELIX  365 365 GLU W  338  ASP W  351  1                                  14    
HELIX  366 366 ASP W  357  GLY W  361  5                                   5    
HELIX  367 367 HIS W  383  TRP W  385  5                                   3    
HELIX  368 368 HIS W  386  GLY W  395  1                                  10    
HELIX  369 369 GLY W  403  GLY W  408  1                                   6    
HELIX  370 370 GLY W  412  GLU W  433  1                                  22    
HELIX  371 371 ASP W  436  LYS W  450  1                                  15    
HELIX  372 372 SER W  452  LYS W  463  1                                  12    
HELIX  373 373 SER 5   22  ASN 5   36  1                                  15    
HELIX  374 374 GLU 5   46  ALA 5   50  5                                   5    
HELIX  375 375 ASN 5   54  PHE 5   60  5                                   7    
HELIX  376 376 ASP 5   85  PHE 5  100  1                                  16    
HELIX  377 377 PRO 5  134  ARG 5  138  5                                   5    
HELIX  378 378 TYR X   20  TYR X   25  1                                   6    
HELIX  379 379 PRO X   49  GLU X   60  1                                  12    
HELIX  380 380 VAL X   69  THR X   75  5                                   7    
HELIX  381 381 SER X   76  LYS X   81  1                                   6    
HELIX  382 382 HYP X  104  PHE X  108  5                                   5    
HELIX  383 383 SER X  112  GLY X  122  1                                  11    
HELIX  384 384 ASN X  123  PHE X  127  5                                   5    
HELIX  385 385 PRO X  141  LYS X  146  1                                   6    
HELIX  386 386 GLY X  154  ASN X  163  1                                  10    
HELIX  387 387 SER X  181  GLY X  195  1                                  15    
HELIX  388 388 ARG X  213  GLY X  233  1                                  21    
HELIX  389 389 THR X  246  LEU X  260  1                                  15    
HELIX  390 390 TYR X  269  GLY X  273  1                                   5    
HELIX  391 391 GLY X  273  GLY X  288  1                                  16    
HELIX  392 392 MET X  297  ARG X  303  1                                   7    
HELIX  393 393 HIS X  310  GLY X  322  1                                  13    
HELIX  394 394 GLU X  338  ASP X  351  1                                  14    
HELIX  395 395 ASP X  357  GLY X  361  5                                   5    
HELIX  396 396 HIS X  383  TRP X  385  5                                   3    
HELIX  397 397 HIS X  386  GLY X  395  1                                  10    
HELIX  398 398 GLY X  403  GLY X  408  1                                   6    
HELIX  399 399 GLY X  412  GLU X  433  1                                  22    
HELIX  400 400 ASP X  436  LYS X  450  1                                  15    
HELIX  401 401 SER X  452  LYS X  463  1                                  12    
HELIX  402 402 SER 6   22  ASN 6   36  1                                  15    
HELIX  403 403 GLU 6   46  ALA 6   50  5                                   5    
HELIX  404 404 ASN 6   54  PHE 6   60  5                                   7    
HELIX  405 405 ASP 6   85  PHE 6  100  1                                  16    
HELIX  406 406 PRO 6  134  LYS 6  137  5                                   4    
HELIX  407 407 TYR Y   20  TYR Y   25  1                                   6    
HELIX  408 408 PRO Y   49  SER Y   61  1                                  13    
HELIX  409 409 VAL Y   69  THR Y   75  5                                   7    
HELIX  410 410 SER Y   76  LYS Y   81  1                                   6    
HELIX  411 411 HYP Y  104  PHE Y  108  5                                   5    
HELIX  412 412 SER Y  112  VAL Y  121  1                                  10    
HELIX  413 413 ASN Y  123  PHE Y  127  5                                   5    
HELIX  414 414 PRO Y  141  LYS Y  146  1                                   6    
HELIX  415 415 GLY Y  154  ASN Y  163  1                                  10    
HELIX  416 416 SER Y  181  GLY Y  195  1                                  15    
HELIX  417 417 ARG Y  213  GLY Y  233  1                                  21    
HELIX  418 418 THR Y  246  GLY Y  261  1                                  16    
HELIX  419 419 TYR Y  269  GLY Y  273  1                                   5    
HELIX  420 420 GLY Y  273  GLY Y  288  1                                  16    
HELIX  421 421 MET Y  297  ARG Y  303  1                                   7    
HELIX  422 422 HIS Y  310  GLY Y  322  1                                  13    
HELIX  423 423 GLU Y  338  ASP Y  351  1                                  14    
HELIX  424 424 ASP Y  357  GLY Y  361  5                                   5    
HELIX  425 425 HIS Y  383  TRP Y  385  5                                   3    
HELIX  426 426 HIS Y  386  GLY Y  395  1                                  10    
HELIX  427 427 GLY Y  403  GLY Y  408  1                                   6    
HELIX  428 428 GLY Y  412  GLU Y  433  1                                  22    
HELIX  429 429 ASP Y  436  LYS Y  450  1                                  15    
HELIX  430 430 SER Y  452  LYS Y  463  1                                  12    
HELIX  431 431 SER 7   22  ASN 7   36  1                                  15    
HELIX  432 432 GLU 7   46  ALA 7   50  5                                   5    
HELIX  433 433 ASN 7   54  PHE 7   60  5                                   7    
HELIX  434 434 ASP 7   85  PHE 7  100  1                                  16    
HELIX  435 435 PRO 7  134  LYS 7  137  5                                   4    
HELIX  436 436 TYR Z   20  TYR Z   25  1                                   6    
HELIX  437 437 PRO Z   49  SER Z   61  1                                  13    
HELIX  438 438 VAL Z   69  THR Z   75  5                                   7    
HELIX  439 439 SER Z   76  LYS Z   81  1                                   6    
HELIX  440 440 HYP Z  104  PHE Z  108  5                                   5    
HELIX  441 441 SER Z  112  VAL Z  121  1                                  10    
HELIX  442 442 ASN Z  123  PHE Z  127  5                                   5    
HELIX  443 443 PRO Z  141  LYS Z  146  1                                   6    
HELIX  444 444 GLY Z  154  ASN Z  163  1                                  10    
HELIX  445 445 SER Z  181  GLY Z  195  1                                  15    
HELIX  446 446 ARG Z  213  GLY Z  233  1                                  21    
HELIX  447 447 THR Z  246  GLY Z  261  1                                  16    
HELIX  448 448 TYR Z  269  GLY Z  273  1                                   5    
HELIX  449 449 GLY Z  273  GLY Z  288  1                                  16    
HELIX  450 450 MET Z  297  ARG Z  303  1                                   7    
HELIX  451 451 HIS Z  310  GLY Z  322  1                                  13    
HELIX  452 452 GLU Z  338  ASP Z  351  1                                  14    
HELIX  453 453 ASP Z  357  GLY Z  361  5                                   5    
HELIX  454 454 HIS Z  383  TRP Z  385  5                                   3    
HELIX  455 455 HIS Z  386  GLY Z  395  1                                  10    
HELIX  456 456 GLY Z  403  GLY Z  408  1                                   6    
HELIX  457 457 GLY Z  412  GLU Z  433  1                                  22    
HELIX  458 458 ASP Z  436  SER Z  452  1                                  17    
HELIX  459 459 SER Z  452  LYS Z  463  1                                  12    
HELIX  460 460 SER 8   22  ASN 8   36  1                                  15    
HELIX  461 461 GLU 8   46  ALA 8   50  5                                   5    
HELIX  462 462 ASN 8   54  PHE 8   60  5                                   7    
HELIX  463 463 ASP 8   85  PHE 8  100  1                                  16    
HELIX  464 464 PRO 8  134  LYS 8  137  5                                   4    
SHEET    1   A 5 ARG A  83  PRO A  89  0                                        
SHEET    2   A 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88           
SHEET    3   A 5 ILE A  36  PRO A  44 -1  N  PHE A  40   O  ALA A  99           
SHEET    4   A 5 LEU A 130  ARG A 139 -1  O  ARG A 134   N  ARG A  41           
SHEET    5   A 5 GLY A 308  ILE A 309  1  O  GLY A 308   N  LEU A 135           
SHEET    1   B 8 LEU A 169  GLY A 171  0                                        
SHEET    2   B 8 CYS A 399  GLN A 401  1  O  LEU A 400   N  LEU A 169           
SHEET    3   B 8 MET A 375  SER A 379  1  N  ALA A 378   O  GLN A 401           
SHEET    4   B 8 HIS A 325  HIS A 327  1  N  LEU A 326   O  MET A 375           
SHEET    5   B 8 LEU A 290  HIS A 294  1  N  ILE A 293   O  HIS A 327           
SHEET    6   B 8 ILE A 264  ASP A 268  1  N  ILE A 265   O  HIS A 292           
SHEET    7   B 8 GLY A 237  ASN A 241  1  N  LEU A 240   O  MET A 266           
SHEET    8   B 8 PHE A 199  KCX A 201  1  N  THR A 200   O  TYR A 239           
SHEET    1   C 2 TYR A 353  VAL A 354  0                                        
SHEET    2   C 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  VAL A 354           
SHEET    1   D 4 THR I  74  MET I  75  0                                        
SHEET    2   D 4 ILE I  39  ALA I  45 -1  N  PHE I  44   O  THR I  74           
SHEET    3   D 4 TYR I 104  ASP I 111 -1  O  VAL I 108   N  CYS I  41           
SHEET    4   D 4 VAL I 116  GLN I 124 -1  O  VAL I 123   N  VAL I 105           
SHEET    1   E 5 ARG B  83  PRO B  89  0                                        
SHEET    2   E 5 TYR B  97  TYR B 103 -1  O  TYR B 100   N  ASP B  86           
SHEET    3   E 5 ILE B  36  PRO B  44 -1  N  MET B  42   O  TYR B  97           
SHEET    4   E 5 LEU B 130  ARG B 139 -1  O  ARG B 134   N  ARG B  41           
SHEET    5   E 5 GLY B 308  ILE B 309  1  O  GLY B 308   N  LEU B 135           
SHEET    1   F 8 LEU B 169  GLY B 171  0                                        
SHEET    2   F 8 CYS B 399  GLN B 401  1  O  LEU B 400   N  LEU B 169           
SHEET    3   F 8 MET B 375  SER B 379  1  N  ALA B 378   O  GLN B 401           
SHEET    4   F 8 HIS B 325  HIS B 327  1  N  LEU B 326   O  MET B 375           
SHEET    5   F 8 LEU B 290  HIS B 294  1  N  ILE B 293   O  HIS B 327           
SHEET    6   F 8 ILE B 264  ASP B 268  1  N  ILE B 265   O  HIS B 292           
SHEET    7   F 8 GLY B 237  ASN B 241  1  N  LEU B 240   O  MET B 266           
SHEET    8   F 8 PHE B 199  KCX B 201  1  N  THR B 200   O  TYR B 239           
SHEET    1   G 2 TYR B 353  VAL B 354  0                                        
SHEET    2   G 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  VAL B 354           
SHEET    1   H 2 VAL J   3  TRP J   4  0                                        
SHEET    2   H 2 SER J 139  VAL J 140 -1  O  VAL J 140   N  VAL J   3           
SHEET    1   I 4 THR J  74  TRP J  76  0                                        
SHEET    2   I 4 ILE J  39  ALA J  45 -1  N  PHE J  44   O  THR J  74           
SHEET    3   I 4 TYR J 104  ASP J 111 -1  O  TYR J 104   N  ALA J  45           
SHEET    4   I 4 VAL J 116  GLN J 124 -1  O  VAL J 123   N  VAL J 105           
SHEET    1   J 5 ARG C  83  PRO C  89  0                                        
SHEET    2   J 5 TYR C  97  TYR C 103 -1  O  ILE C  98   N  GLU C  88           
SHEET    3   J 5 ILE C  36  PRO C  44 -1  N  MET C  42   O  TYR C  97           
SHEET    4   J 5 LEU C 130  ARG C 139 -1  O  ARG C 131   N  THR C  43           
SHEET    5   J 5 GLY C 308  ILE C 309  1  O  GLY C 308   N  LEU C 135           
SHEET    1   K 8 LEU C 169  GLY C 171  0                                        
SHEET    2   K 8 CYS C 399  GLN C 401  1  O  LEU C 400   N  LEU C 169           
SHEET    3   K 8 MET C 375  SER C 379  1  N  ALA C 378   O  GLN C 401           
SHEET    4   K 8 HIS C 325  HIS C 327  1  N  LEU C 326   O  MET C 375           
SHEET    5   K 8 LEU C 290  HIS C 294  1  N  ILE C 293   O  HIS C 327           
SHEET    6   K 8 ILE C 264  ASP C 268  1  N  ILE C 265   O  HIS C 292           
SHEET    7   K 8 GLY C 237  ASN C 241  1  N  LEU C 240   O  MET C 266           
SHEET    8   K 8 PHE C 199  KCX C 201  1  N  THR C 200   O  TYR C 239           
SHEET    1   L 2 TYR C 353  VAL C 354  0                                        
SHEET    2   L 2 GLN C 366  ASP C 367 -1  O  GLN C 366   N  VAL C 354           
SHEET    1   M 2 VAL K   3  TRP K   4  0                                        
SHEET    2   M 2 SER K 139  VAL K 140 -1  O  VAL K 140   N  VAL K   3           
SHEET    1   N 4 THR K  74  TRP K  76  0                                        
SHEET    2   N 4 ILE K  39  ALA K  45 -1  N  PHE K  44   O  THR K  74           
SHEET    3   N 4 TYR K 104  ASP K 111 -1  O  VAL K 108   N  CYS K  41           
SHEET    4   N 4 VAL K 116  GLN K 124 -1  O  VAL K 123   N  VAL K 105           
SHEET    1   O 5 ARG D  83  PRO D  89  0                                        
SHEET    2   O 5 TYR D  97  TYR D 103 -1  O  TYR D 100   N  ASP D  86           
SHEET    3   O 5 ILE D  36  PRO D  44 -1  N  MET D  42   O  TYR D  97           
SHEET    4   O 5 LEU D 130  ARG D 139 -1  O  ARG D 134   N  ARG D  41           
SHEET    5   O 5 GLY D 308  ILE D 309  1  O  GLY D 308   N  LEU D 135           
SHEET    1   P 8 LEU D 169  GLY D 171  0                                        
SHEET    2   P 8 CYS D 399  GLN D 401  1  O  LEU D 400   N  LEU D 169           
SHEET    3   P 8 MET D 375  SER D 379  1  N  ALA D 378   O  GLN D 401           
SHEET    4   P 8 HIS D 325  HIS D 327  1  N  LEU D 326   O  MET D 375           
SHEET    5   P 8 LEU D 290  HIS D 294  1  N  ILE D 293   O  HIS D 327           
SHEET    6   P 8 ILE D 264  ASP D 268  1  N  ILE D 265   O  HIS D 292           
SHEET    7   P 8 GLY D 237  ASN D 241  1  N  LEU D 240   O  MET D 266           
SHEET    8   P 8 PHE D 199  KCX D 201  1  N  THR D 200   O  TYR D 239           
SHEET    1   Q 2 TYR D 353  VAL D 354  0                                        
SHEET    2   Q 2 GLN D 366  ASP D 367 -1  O  GLN D 366   N  VAL D 354           
SHEET    1   R 2 VAL L   3  TRP L   4  0                                        
SHEET    2   R 2 SER L 139  VAL L 140 -1  O  VAL L 140   N  VAL L   3           
SHEET    1   S 4 THR L  74  TRP L  76  0                                        
SHEET    2   S 4 ILE L  39  ALA L  45 -1  N  PHE L  44   O  THR L  74           
SHEET    3   S 4 TYR L 104  ASP L 111 -1  O  TYR L 104   N  ALA L  45           
SHEET    4   S 4 VAL L 116  GLN L 124 -1  O  VAL L 123   N  VAL L 105           
SHEET    1   T 5 ARG E  83  PRO E  89  0                                        
SHEET    2   T 5 TYR E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88           
SHEET    3   T 5 ILE E  36  PRO E  44 -1  N  MET E  42   O  TYR E  97           
SHEET    4   T 5 LEU E 130  ARG E 139 -1  O  ARG E 134   N  ARG E  41           
SHEET    5   T 5 GLY E 308  ILE E 309  1  O  GLY E 308   N  LEU E 135           
SHEET    1   U 8 LEU E 169  GLY E 171  0                                        
SHEET    2   U 8 CYS E 399  GLN E 401  1  O  LEU E 400   N  LEU E 169           
SHEET    3   U 8 MET E 375  SER E 379  1  N  ALA E 378   O  GLN E 401           
SHEET    4   U 8 HIS E 325  HIS E 327  1  N  LEU E 326   O  MET E 375           
SHEET    5   U 8 LEU E 290  HIS E 294  1  N  ILE E 293   O  HIS E 325           
SHEET    6   U 8 ILE E 264  ASP E 268  1  N  ILE E 265   O  HIS E 292           
SHEET    7   U 8 GLY E 237  ASN E 241  1  N  LEU E 240   O  MET E 266           
SHEET    8   U 8 PHE E 199  KCX E 201  1  N  THR E 200   O  TYR E 239           
SHEET    1   V 2 TYR E 353  VAL E 354  0                                        
SHEET    2   V 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  VAL E 354           
SHEET    1   W 2 VAL M   3  TRP M   4  0                                        
SHEET    2   W 2 SER M 139  VAL M 140 -1  O  VAL M 140   N  VAL M   3           
SHEET    1   X 4 THR M  74  TRP M  76  0                                        
SHEET    2   X 4 ILE M  39  ALA M  45 -1  N  PHE M  44   O  THR M  74           
SHEET    3   X 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45           
SHEET    4   X 4 VAL M 116  GLN M 124 -1  O  ILE M 118   N  ALA M 109           
SHEET    1   Y 5 ARG F  83  PRO F  89  0                                        
SHEET    2   Y 5 TYR F  97  TYR F 103 -1  O  ILE F  98   N  GLU F  88           
SHEET    3   Y 5 ILE F  36  PRO F  44 -1  N  PHE F  40   O  ALA F  99           
SHEET    4   Y 5 LEU F 130  ARG F 139 -1  O  ARG F 134   N  ARG F  41           
SHEET    5   Y 5 GLY F 308  ILE F 309  1  O  GLY F 308   N  LEU F 135           
SHEET    1   Z 8 LEU F 169  GLY F 171  0                                        
SHEET    2   Z 8 CYS F 399  GLN F 401  1  O  LEU F 400   N  LEU F 169           
SHEET    3   Z 8 MET F 375  SER F 379  1  N  ALA F 378   O  GLN F 401           
SHEET    4   Z 8 HIS F 325  HIS F 327  1  N  LEU F 326   O  VAL F 377           
SHEET    5   Z 8 LEU F 290  HIS F 294  1  N  ILE F 293   O  HIS F 327           
SHEET    6   Z 8 ILE F 264  ASP F 268  1  N  ILE F 265   O  HIS F 292           
SHEET    7   Z 8 GLY F 237  ASN F 241  1  N  LEU F 240   O  MET F 266           
SHEET    8   Z 8 PHE F 199  KCX F 201  1  N  THR F 200   O  TYR F 239           
SHEET    1  AA 2 TYR F 353  VAL F 354  0                                        
SHEET    2  AA 2 GLN F 366  ASP F 367 -1  O  GLN F 366   N  VAL F 354           
SHEET    1  AB 2 VAL N   3  TRP N   4  0                                        
SHEET    2  AB 2 SER N 139  VAL N 140 -1  O  VAL N 140   N  VAL N   3           
SHEET    1  AC 4 THR N  74  TRP N  76  0                                        
SHEET    2  AC 4 ILE N  39  ALA N  45 -1  N  LEU N  42   O  TRP N  76           
SHEET    3  AC 4 TYR N 104  ASP N 111 -1  O  TYR N 104   N  ALA N  45           
SHEET    4  AC 4 VAL N 116  GLN N 124 -1  O  VAL N 123   N  VAL N 105           
SHEET    1  AD 5 ARG G  83  PRO G  89  0                                        
SHEET    2  AD 5 TYR G  97  TYR G 103 -1  O  ILE G  98   N  GLU G  88           
SHEET    3  AD 5 ILE G  36  PRO G  44 -1  N  MET G  42   O  TYR G  97           
SHEET    4  AD 5 LEU G 130  ARG G 139 -1  O  ARG G 134   N  ARG G  41           
SHEET    5  AD 5 GLY G 308  ILE G 309  1  O  GLY G 308   N  LEU G 135           
SHEET    1  AE 8 LEU G 169  GLY G 171  0                                        
SHEET    2  AE 8 CYS G 399  GLN G 401  1  O  LEU G 400   N  LEU G 169           
SHEET    3  AE 8 MET G 375  SER G 379  1  N  ALA G 378   O  GLN G 401           
SHEET    4  AE 8 HIS G 325  HIS G 327  1  N  LEU G 326   O  MET G 375           
SHEET    5  AE 8 LEU G 290  HIS G 294  1  N  ILE G 293   O  HIS G 327           
SHEET    6  AE 8 ILE G 264  ASP G 268  1  N  ILE G 265   O  HIS G 292           
SHEET    7  AE 8 GLY G 237  ASN G 241  1  N  LEU G 240   O  MET G 266           
SHEET    8  AE 8 PHE G 199  KCX G 201  1  N  THR G 200   O  TYR G 239           
SHEET    1  AF 2 TYR G 353  VAL G 354  0                                        
SHEET    2  AF 2 GLN G 366  ASP G 367 -1  O  GLN G 366   N  VAL G 354           
SHEET    1  AG 2 VAL O   3  TRP O   4  0                                        
SHEET    2  AG 2 SER O 139  VAL O 140 -1  O  VAL O 140   N  VAL O   3           
SHEET    1  AH 4 THR O  74  TRP O  76  0                                        
SHEET    2  AH 4 ILE O  39  ALA O  45 -1  N  PHE O  44   O  THR O  74           
SHEET    3  AH 4 TYR O 104  ASP O 111 -1  O  VAL O 108   N  CYS O  41           
SHEET    4  AH 4 VAL O 116  GLN O 124 -1  O  VAL O 123   N  VAL O 105           
SHEET    1  AI 5 ARG H  83  PRO H  89  0                                        
SHEET    2  AI 5 TYR H  97  TYR H 103 -1  O  TYR H 100   N  ASP H  86           
SHEET    3  AI 5 ILE H  36  PRO H  44 -1  N  MET H  42   O  TYR H  97           
SHEET    4  AI 5 LEU H 130  ARG H 139 -1  O  ARG H 134   N  ARG H  41           
SHEET    5  AI 5 GLY H 308  ILE H 309  1  O  GLY H 308   N  LEU H 135           
SHEET    1  AJ 8 LEU H 169  GLY H 171  0                                        
SHEET    2  AJ 8 CYS H 399  GLN H 401  1  O  LEU H 400   N  LEU H 169           
SHEET    3  AJ 8 MET H 375  SER H 379  1  N  ALA H 378   O  GLN H 401           
SHEET    4  AJ 8 HIS H 325  HIS H 327  1  N  LEU H 326   O  MET H 375           
SHEET    5  AJ 8 LEU H 290  HIS H 294  1  N  ILE H 293   O  HIS H 325           
SHEET    6  AJ 8 ILE H 264  ASP H 268  1  N  ILE H 265   O  HIS H 292           
SHEET    7  AJ 8 GLY H 237  ASN H 241  1  N  LEU H 240   O  MET H 266           
SHEET    8  AJ 8 PHE H 199  KCX H 201  1  N  THR H 200   O  TYR H 239           
SHEET    1  AK 2 TYR H 353  VAL H 354  0                                        
SHEET    2  AK 2 GLN H 366  ASP H 367 -1  O  GLN H 366   N  VAL H 354           
SHEET    1  AL 4 THR P  74  TRP P  76  0                                        
SHEET    2  AL 4 ILE P  39  ALA P  45 -1  N  PHE P  44   O  THR P  74           
SHEET    3  AL 4 TYR P 104  ASP P 111 -1  O  TYR P 104   N  ALA P  45           
SHEET    4  AL 4 VAL P 116  GLN P 124 -1  O  VAL P 123   N  VAL P 105           
SHEET    1  BA 5 ARG S  83  PRO S  89  0                                        
SHEET    2  BA 5 TYR S  97  TYR S 103 -1  O  TYR S 100   N  ASP S  86           
SHEET    3  BA 5 ILE S  36  PRO S  44 -1  N  MET S  42   O  TYR S  97           
SHEET    4  BA 5 LEU S 130  ARG S 139 -1  O  ARG S 134   N  ARG S  41           
SHEET    5  BA 5 GLY S 308  ILE S 309  1  O  GLY S 308   N  LEU S 135           
SHEET    1  BB 8 LEU S 169  GLY S 171  0                                        
SHEET    2  BB 8 CYS S 399  GLN S 401  1  O  LEU S 400   N  LEU S 169           
SHEET    3  BB 8 MET S 375  SER S 379  1  N  ALA S 378   O  GLN S 401           
SHEET    4  BB 8 HIS S 325  HIS S 327  1  N  LEU S 326   O  VAL S 377           
SHEET    5  BB 8 LEU S 290  HIS S 294  1  N  ILE S 293   O  HIS S 325           
SHEET    6  BB 8 ILE S 264  ASP S 268  1  N  ILE S 265   O  HIS S 292           
SHEET    7  BB 8 GLY S 237  ASN S 241  1  N  LEU S 240   O  MET S 266           
SHEET    8  BB 8 PHE S 199  KCX S 201  1  N  THR S 200   O  TYR S 239           
SHEET    1  BC 2 TYR S 353  VAL S 354  0                                        
SHEET    2  BC 2 GLN S 366  ASP S 367 -1  O  GLN S 366   N  VAL S 354           
SHEET    1  BD 2 VAL 1   3  TRP 1   4  0                                        
SHEET    2  BD 2 SER 1 139  VAL 1 140 -1  O  VAL 1 140   N  VAL 1   3           
SHEET    1  BE 4 THR 1  74  TRP 1  76  0                                        
SHEET    2  BE 4 ILE 1  39  ALA 1  45 -1  N  PHE 1  44   O  THR 1  74           
SHEET    3  BE 4 TYR 1 104  ASP 1 111 -1  O  TYR 1 104   N  ALA 1  45           
SHEET    4  BE 4 VAL 1 116  GLN 1 124 -1  O  VAL 1 123   N  VAL 1 105           
SHEET    1  BF 5 ARG T  83  PRO T  89  0                                        
SHEET    2  BF 5 TYR T  97  TYR T 103 -1  O  ILE T  98   N  GLU T  88           
SHEET    3  BF 5 ILE T  36  PRO T  44 -1  N  MET T  42   O  TYR T  97           
SHEET    4  BF 5 LEU T 130  ARG T 139 -1  O  ARG T 134   N  ARG T  41           
SHEET    5  BF 5 GLY T 308  ILE T 309  1  O  GLY T 308   N  LEU T 135           
SHEET    1  BG 8 LEU T 169  GLY T 171  0                                        
SHEET    2  BG 8 CYS T 399  GLN T 401  1  O  LEU T 400   N  LEU T 169           
SHEET    3  BG 8 MET T 375  SER T 379  1  N  ALA T 378   O  GLN T 401           
SHEET    4  BG 8 HIS T 325  HIS T 327  1  N  LEU T 326   O  MET T 375           
SHEET    5  BG 8 LEU T 290  HIS T 294  1  N  ILE T 293   O  HIS T 325           
SHEET    6  BG 8 ILE T 264  ASP T 268  1  N  ILE T 265   O  HIS T 292           
SHEET    7  BG 8 GLY T 237  ASN T 241  1  N  LEU T 240   O  MET T 266           
SHEET    8  BG 8 PHE T 199  KCX T 201  1  N  THR T 200   O  TYR T 239           
SHEET    1  BH 2 TYR T 353  VAL T 354  0                                        
SHEET    2  BH 2 GLN T 366  ASP T 367 -1  O  GLN T 366   N  VAL T 354           
SHEET    1  BI 2 VAL 2   3  TRP 2   4  0                                        
SHEET    2  BI 2 SER 2 139  VAL 2 140 -1  O  VAL 2 140   N  VAL 2   3           
SHEET    1  BJ 4 THR 2  74  MET 2  75  0                                        
SHEET    2  BJ 4 ILE 2  39  ALA 2  45 -1  N  PHE 2  44   O  THR 2  74           
SHEET    3  BJ 4 TYR 2 104  ASP 2 111 -1  O  TYR 2 104   N  ALA 2  45           
SHEET    4  BJ 4 VAL 2 116  GLN 2 124 -1  O  VAL 2 123   N  VAL 2 105           
SHEET    1  BK 5 ARG U  83  PRO U  89  0                                        
SHEET    2  BK 5 TYR U  97  TYR U 103 -1  O  TYR U 100   N  ASP U  86           
SHEET    3  BK 5 ILE U  36  PRO U  44 -1  N  PHE U  40   O  ALA U  99           
SHEET    4  BK 5 LEU U 130  ARG U 139 -1  O  ARG U 134   N  ARG U  41           
SHEET    5  BK 5 GLY U 308  ILE U 309  1  O  GLY U 308   N  LEU U 135           
SHEET    1  BL 8 LEU U 169  GLY U 171  0                                        
SHEET    2  BL 8 CYS U 399  GLN U 401  1  O  LEU U 400   N  LEU U 169           
SHEET    3  BL 8 MET U 375  SER U 379  1  N  ALA U 378   O  GLN U 401           
SHEET    4  BL 8 HIS U 325  HIS U 327  1  N  LEU U 326   O  MET U 375           
SHEET    5  BL 8 LEU U 290  HIS U 294  1  N  ILE U 293   O  HIS U 327           
SHEET    6  BL 8 ILE U 264  ASP U 268  1  N  ILE U 265   O  HIS U 292           
SHEET    7  BL 8 GLY U 237  ASN U 241  1  N  LEU U 240   O  MET U 266           
SHEET    8  BL 8 PHE U 199  KCX U 201  1  N  THR U 200   O  TYR U 239           
SHEET    1  BM 2 TYR U 353  VAL U 354  0                                        
SHEET    2  BM 2 GLN U 366  ASP U 367 -1  O  GLN U 366   N  VAL U 354           
SHEET    1  BN 2 VAL 3   3  TRP 3   4  0                                        
SHEET    2  BN 2 SER 3 139  VAL 3 140 -1  O  VAL 3 140   N  VAL 3   3           
SHEET    1  BO 4 THR 3  74  TRP 3  76  0                                        
SHEET    2  BO 4 ILE 3  39  ALA 3  45 -1  N  PHE 3  44   O  THR 3  74           
SHEET    3  BO 4 TYR 3 104  ASP 3 111 -1  O  TYR 3 104   N  ALA 3  45           
SHEET    4  BO 4 VAL 3 116  GLN 3 124 -1  O  VAL 3 123   N  VAL 3 105           
SHEET    1  BP 5 ARG V  83  PRO V  89  0                                        
SHEET    2  BP 5 TYR V  97  TYR V 103 -1  O  TYR V 100   N  ASP V  86           
SHEET    3  BP 5 ILE V  36  PRO V  44 -1  N  MET V  42   O  TYR V  97           
SHEET    4  BP 5 LEU V 130  ARG V 139 -1  O  ARG V 134   N  ARG V  41           
SHEET    5  BP 5 GLY V 308  ILE V 309  1  O  GLY V 308   N  LEU V 135           
SHEET    1  BQ 8 LEU V 169  GLY V 171  0                                        
SHEET    2  BQ 8 CYS V 399  GLN V 401  1  O  LEU V 400   N  LEU V 169           
SHEET    3  BQ 8 MET V 375  SER V 379  1  N  ALA V 378   O  GLN V 401           
SHEET    4  BQ 8 HIS V 325  HIS V 327  1  N  LEU V 326   O  MET V 375           
SHEET    5  BQ 8 LEU V 290  HIS V 294  1  N  ILE V 293   O  HIS V 327           
SHEET    6  BQ 8 ILE V 264  ASP V 268  1  N  ILE V 265   O  HIS V 292           
SHEET    7  BQ 8 GLY V 237  ASN V 241  1  N  LEU V 240   O  MET V 266           
SHEET    8  BQ 8 PHE V 199  KCX V 201  1  N  THR V 200   O  TYR V 239           
SHEET    1  BR 2 TYR V 353  VAL V 354  0                                        
SHEET    2  BR 2 GLN V 366  ASP V 367 -1  O  GLN V 366   N  VAL V 354           
SHEET    1  BS 4 THR 4  74  TRP 4  76  0                                        
SHEET    2  BS 4 ILE 4  39  ALA 4  45 -1  N  LEU 4  42   O  TRP 4  76           
SHEET    3  BS 4 TYR 4 104  ASP 4 111 -1  O  TYR 4 104   N  ALA 4  45           
SHEET    4  BS 4 VAL 4 116  GLN 4 124 -1  O  VAL 4 123   N  VAL 4 105           
SHEET    1  BT 5 ARG W  83  PRO W  89  0                                        
SHEET    2  BT 5 TYR W  97  TYR W 103 -1  O  TYR W 100   N  ASP W  86           
SHEET    3  BT 5 ILE W  36  PRO W  44 -1  N  MET W  42   O  TYR W  97           
SHEET    4  BT 5 LEU W 130  ARG W 139 -1  O  ARG W 134   N  ARG W  41           
SHEET    5  BT 5 GLY W 308  ILE W 309  1  O  GLY W 308   N  LEU W 135           
SHEET    1  BU 8 LEU W 169  GLY W 171  0                                        
SHEET    2  BU 8 CYS W 399  GLN W 401  1  O  LEU W 400   N  LEU W 169           
SHEET    3  BU 8 MET W 375  SER W 379  1  N  ALA W 378   O  GLN W 401           
SHEET    4  BU 8 HIS W 325  HIS W 327  1  N  LEU W 326   O  MET W 375           
SHEET    5  BU 8 LEU W 290  HIS W 294  1  N  ILE W 293   O  HIS W 327           
SHEET    6  BU 8 ILE W 264  ASP W 268  1  N  ILE W 265   O  HIS W 292           
SHEET    7  BU 8 GLY W 237  ASN W 241  1  N  LEU W 240   O  MET W 266           
SHEET    8  BU 8 PHE W 199  KCX W 201  1  N  THR W 200   O  TYR W 239           
SHEET    1  BV 2 TYR W 353  VAL W 354  0                                        
SHEET    2  BV 2 GLN W 366  ASP W 367 -1  O  GLN W 366   N  VAL W 354           
SHEET    1  BW 4 THR 5  74  TRP 5  76  0                                        
SHEET    2  BW 4 ILE 5  39  ALA 5  45 -1  N  PHE 5  44   O  THR 5  74           
SHEET    3  BW 4 TYR 5 104  ASP 5 111 -1  O  TYR 5 104   N  ALA 5  45           
SHEET    4  BW 4 VAL 5 116  GLN 5 124 -1  O  VAL 5 123   N  VAL 5 105           
SHEET    1  BX 5 ARG X  83  PRO X  89  0                                        
SHEET    2  BX 5 TYR X  97  TYR X 103 -1  O  TYR X 100   N  ASP X  86           
SHEET    3  BX 5 ILE X  36  PRO X  44 -1  N  MET X  42   O  TYR X  97           
SHEET    4  BX 5 LEU X 130  ARG X 139 -1  O  ARG X 134   N  ARG X  41           
SHEET    5  BX 5 GLY X 308  ILE X 309  1  O  GLY X 308   N  LEU X 135           
SHEET    1  BY 8 LEU X 169  GLY X 171  0                                        
SHEET    2  BY 8 CYS X 399  GLN X 401  1  O  LEU X 400   N  LEU X 169           
SHEET    3  BY 8 MET X 375  SER X 379  1  N  ALA X 378   O  GLN X 401           
SHEET    4  BY 8 HIS X 325  HIS X 327  1  N  LEU X 326   O  MET X 375           
SHEET    5  BY 8 LEU X 290  HIS X 294  1  N  ILE X 293   O  HIS X 325           
SHEET    6  BY 8 ILE X 264  ASP X 268  1  N  ILE X 265   O  HIS X 292           
SHEET    7  BY 8 GLY X 237  ASN X 241  1  N  LEU X 240   O  MET X 266           
SHEET    8  BY 8 PHE X 199  KCX X 201  1  N  THR X 200   O  TYR X 239           
SHEET    1  BZ 2 TYR X 353  VAL X 354  0                                        
SHEET    2  BZ 2 GLN X 366  ASP X 367 -1  O  GLN X 366   N  VAL X 354           
SHEET    1  CA 2 VAL 6   3  TRP 6   4  0                                        
SHEET    2  CA 2 SER 6 139  VAL 6 140 -1  O  VAL 6 140   N  VAL 6   3           
SHEET    1  CB 4 THR 6  74  TRP 6  76  0                                        
SHEET    2  CB 4 ILE 6  39  ALA 6  45 -1  N  PHE 6  44   O  THR 6  74           
SHEET    3  CB 4 TYR 6 104  ASP 6 111 -1  O  VAL 6 108   N  CYS 6  41           
SHEET    4  CB 4 VAL 6 116  GLN 6 124 -1  O  VAL 6 123   N  VAL 6 105           
SHEET    1  CC 5 ARG Y  83  PRO Y  89  0                                        
SHEET    2  CC 5 TYR Y  97  TYR Y 103 -1  O  ILE Y  98   N  GLU Y  88           
SHEET    3  CC 5 ILE Y  36  PRO Y  44 -1  N  MET Y  42   O  TYR Y  97           
SHEET    4  CC 5 LEU Y 130  ARG Y 139 -1  O  ARG Y 134   N  ARG Y  41           
SHEET    5  CC 5 GLY Y 308  ILE Y 309  1  O  GLY Y 308   N  LEU Y 135           
SHEET    1  CD 8 LEU Y 169  GLY Y 171  0                                        
SHEET    2  CD 8 CYS Y 399  GLN Y 401  1  O  LEU Y 400   N  LEU Y 169           
SHEET    3  CD 8 MET Y 375  SER Y 379  1  N  ALA Y 378   O  GLN Y 401           
SHEET    4  CD 8 HIS Y 325  HIS Y 327  1  N  LEU Y 326   O  VAL Y 377           
SHEET    5  CD 8 LEU Y 290  HIS Y 294  1  N  ILE Y 293   O  HIS Y 327           
SHEET    6  CD 8 ILE Y 264  ASP Y 268  1  N  ILE Y 265   O  HIS Y 292           
SHEET    7  CD 8 GLY Y 237  ASN Y 241  1  N  LEU Y 240   O  MET Y 266           
SHEET    8  CD 8 PHE Y 199  KCX Y 201  1  N  THR Y 200   O  TYR Y 239           
SHEET    1  CE 2 TYR Y 353  VAL Y 354  0                                        
SHEET    2  CE 2 GLN Y 366  ASP Y 367 -1  O  GLN Y 366   N  VAL Y 354           
SHEET    1  CF 2 VAL 7   3  TRP 7   4  0                                        
SHEET    2  CF 2 SER 7 139  VAL 7 140 -1  O  VAL 7 140   N  VAL 7   3           
SHEET    1  CG 4 THR 7  74  TRP 7  76  0                                        
SHEET    2  CG 4 ILE 7  39  ALA 7  45 -1  N  PHE 7  44   O  THR 7  74           
SHEET    3  CG 4 TYR 7 104  ASP 7 111 -1  O  TYR 7 104   N  ALA 7  45           
SHEET    4  CG 4 VAL 7 116  GLN 7 124 -1  O  VAL 7 123   N  VAL 7 105           
SHEET    1  CH 5 ARG Z  83  PRO Z  89  0                                        
SHEET    2  CH 5 TYR Z  97  TYR Z 103 -1  O  TYR Z 100   N  ASP Z  86           
SHEET    3  CH 5 ILE Z  36  PRO Z  44 -1  N  PHE Z  40   O  ALA Z  99           
SHEET    4  CH 5 LEU Z 130  ARG Z 139 -1  O  ARG Z 134   N  ARG Z  41           
SHEET    5  CH 5 GLY Z 308  ILE Z 309  1  O  GLY Z 308   N  LEU Z 135           
SHEET    1  CI 8 LEU Z 169  GLY Z 171  0                                        
SHEET    2  CI 8 CYS Z 399  GLN Z 401  1  O  LEU Z 400   N  LEU Z 169           
SHEET    3  CI 8 MET Z 375  SER Z 379  1  N  ALA Z 378   O  GLN Z 401           
SHEET    4  CI 8 HIS Z 325  HIS Z 327  1  N  LEU Z 326   O  VAL Z 377           
SHEET    5  CI 8 LEU Z 290  HIS Z 294  1  N  ILE Z 293   O  HIS Z 327           
SHEET    6  CI 8 ILE Z 264  ASP Z 268  1  N  ILE Z 265   O  HIS Z 292           
SHEET    7  CI 8 GLY Z 237  ASN Z 241  1  N  LEU Z 240   O  MET Z 266           
SHEET    8  CI 8 PHE Z 199  KCX Z 201  1  N  THR Z 200   O  TYR Z 239           
SHEET    1  CJ 2 TYR Z 353  VAL Z 354  0                                        
SHEET    2  CJ 2 GLN Z 366  ASP Z 367 -1  O  GLN Z 366   N  VAL Z 354           
SHEET    1  CK 2 VAL 8   3  TRP 8   4  0                                        
SHEET    2  CK 2 SER 8 139  VAL 8 140 -1  O  VAL 8 140   N  VAL 8   3           
SHEET    1  CL 4 THR 8  74  TRP 8  76  0                                        
SHEET    2  CL 4 ILE 8  39  ALA 8  45 -1  N  LEU 8  42   O  TRP 8  76           
SHEET    3  CL 4 TYR 8 104  ASP 8 111 -1  O  TYR 8 104   N  ALA 8  45           
SHEET    4  CL 4 VAL 8 116  GLN 8 124 -1  O  VAL 8 123   N  VAL 8 105           
SSBOND   1 CYS A  247    CYS E  247                          1555   1555  2.76  
SSBOND   2 CYS B  247    CYS F  247                          1555   1555  2.79  
SSBOND   3 CYS C  247    CYS G  247                          1555   1555  2.72  
SSBOND   4 CYS D  247    CYS H  247                          1555   1555  2.80  
SSBOND   5 CYS S  247    CYS W  247                          1555   1555  2.77  
SSBOND   6 CYS T  247    CYS X  247                          1555   1555  2.79  
SSBOND   7 CYS U  247    CYS Y  247                          1555   1555  2.77  
SSBOND   8 CYS V  247    CYS Z  247                          1555   1555  2.76  
LINK        MG    MG A 476                 OQ1 KCX A 201     1555   1555  2.14  
LINK        MG    MG A 476                 OD1 ASP A 203     1555   1555  2.02  
LINK        MG    MG A 476                 OE1 GLU A 204     1555   1555  2.03  
LINK        MG    MG A 476                 O6  CAP A 501     1555   1555  2.15  
LINK        MG    MG B 476                 OQ1 KCX B 201     1555   1555  2.15  
LINK        MG    MG B 476                 OD1 ASP B 203     1555   1555  2.06  
LINK        MG    MG B 476                 OE1 GLU B 204     1555   1555  1.97  
LINK        MG    MG B 476                 O3  CAP B 501     1555   1555  2.17  
LINK        MG    MG C 476                 OQ1 KCX C 201     1555   1555  2.16  
LINK        MG    MG C 476                 OD1 ASP C 203     1555   1555  2.03  
LINK        MG    MG C 476                 OE1 GLU C 204     1555   1555  1.97  
LINK        MG    MG C 476                 O6  CAP C 501     1555   1555  2.18  
LINK        MG    MG D 476                 OQ1 KCX D 201     1555   1555  2.08  
LINK        MG    MG D 476                 OD1 ASP D 203     1555   1555  2.00  
LINK        MG    MG D 476                 OE1 GLU D 204     1555   1555  2.03  
LINK        MG    MG D 476                 O6  CAP D 501     1555   1555  2.19  
LINK        MG    MG E 476                 OQ1 KCX E 201     1555   1555  2.12  
LINK        MG    MG E 476                 OD1 ASP E 203     1555   1555  2.03  
LINK        MG    MG E 476                 OE1 GLU E 204     1555   1555  2.11  
LINK        MG    MG E 476                 O6  CAP E 501     1555   1555  2.19  
LINK        MG    MG F 476                 OQ1 KCX F 201     1555   1555  2.08  
LINK        MG    MG F 476                 OD1 ASP F 203     1555   1555  2.07  
LINK        MG    MG F 476                 OE1 GLU F 204     1555   1555  2.05  
LINK        MG    MG F 476                 O3  CAP F 501     1555   1555  2.20  
LINK        MG    MG G 476                 OQ1 KCX G 201     1555   1555  2.10  
LINK        MG    MG G 476                 OD1 ASP G 203     1555   1555  2.05  
LINK        MG    MG G 476                 OE1 GLU G 204     1555   1555  1.98  
LINK        MG    MG H 476                 OQ1 KCX H 201     1555   1555  2.15  
LINK        MG    MG H 476                 OD1 ASP H 203     1555   1555  2.10  
LINK        MG    MG H 476                 OE1 GLU H 204     1555   1555  2.02  
LINK        MG    MG H 476                 O3  CAP H 501     1555   1555  2.15  
LINK        MG    MG H 476                 O6  CAP H 501     1555   1555  2.15  
LINK        MG    MG S 476                 OQ1 KCX S 201     1555   1555  2.13  
LINK        MG    MG S 476                 OD1 ASP S 203     1555   1555  2.00  
LINK        MG    MG S 476                 OE1 GLU S 204     1555   1555  2.03  
LINK        MG    MG T 476                 OQ1 KCX T 201     1555   1555  2.13  
LINK        MG    MG T 476                 OD1 ASP T 203     1555   1555  2.06  
LINK        MG    MG T 476                 OE1 GLU T 204     1555   1555  2.05  
LINK        MG    MG T 476                 O6  CAP T 501     1555   1555  2.17  
LINK        MG    MG U 476                 OQ1 KCX U 201     1555   1555  2.11  
LINK        MG    MG U 476                 OD1 ASP U 203     1555   1555  2.00  
LINK        MG    MG U 476                 OE1 GLU U 204     1555   1555  1.96  
LINK        MG    MG V 476                 OQ1 KCX V 201     1555   1555  2.18  
LINK        MG    MG V 476                 OD1 ASP V 203     1555   1555  1.97  
LINK        MG    MG V 476                 OE1 GLU V 204     1555   1555  2.13  
LINK        MG    MG V 476                 O6  CAP V 501     1555   1555  2.14  
LINK        MG    MG W 476                 OQ1 KCX W 201     1555   1555  2.06  
LINK        MG    MG W 476                 OD1 ASP W 203     1555   1555  1.99  
LINK        MG    MG W 476                 OE1 GLU W 204     1555   1555  2.01  
LINK        MG    MG W 476                 O3  CAP W 501     1555   1555  2.19  
LINK        MG    MG X 476                 OQ1 KCX X 201     1555   1555  2.19  
LINK        MG    MG X 476                 OD1 ASP X 203     1555   1555  2.00  
LINK        MG    MG X 476                 OE1 GLU X 204     1555   1555  2.03  
LINK        MG    MG X 476                 O6  CAP X 501     1555   1555  2.19  
LINK        MG    MG Y 476                 OQ1 KCX Y 201     1555   1555  2.07  
LINK        MG    MG Y 476                 OD1 ASP Y 203     1555   1555  1.99  
LINK        MG    MG Y 476                 OE1 GLU Y 204     1555   1555  2.07  
LINK        MG    MG Z 476                 OQ1 KCX Z 201     1555   1555  2.10  
LINK        MG    MG Z 476                 OD1 ASP Z 203     1555   1555  2.01  
LINK        MG    MG Z 476                 OE1 GLU Z 204     1555   1555  2.04  
LINK         C   MME 1   1                 N   MET 1   2     1555   1555  1.33  
LINK         C   MME 2   1                 N   MET 2   2     1555   1555  1.33  
LINK         C   MME 3   1                 N   MET 3   2     1555   1555  1.33  
LINK         C   MME 4   1                 N   MET 4   2     1555   1555  1.33  
LINK         C   MME 5   1                 N   MET 5   2     1555   1555  1.33  
LINK         C   MME 6   1                 N   MET 6   2     1555   1555  1.33  
LINK         C   MME 7   1                 N   MET 7   2     1555   1555  1.33  
LINK         C   MME 8   1                 N   MET 8   2     1555   1555  1.33  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.35  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.34  
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.34  
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.33  
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33  
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.33  
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.33  
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.33  
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33  
LINK        MG    MG A 476                 O2  CAP A 501     1555   1555  2.30  
LINK        MG    MG A 476                 O3  CAP A 501     1555   1555  2.26  
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.35  
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.33  
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.35  
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.34  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33  
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.33  
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.33  
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.33  
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.33  
LINK        MG    MG B 476                 O2  CAP B 501     1555   1555  2.33  
LINK        MG    MG B 476                 O6  CAP B 501     1555   1555  2.21  
LINK         C   TYR C 103                 N   HYP C 104     1555   1555  1.35  
LINK         C   HYP C 104                 N   ILE C 105     1555   1555  1.33  
LINK         C   GLY C 150                 N   HYP C 151     1555   1555  1.35  
LINK         C   HYP C 151                 N   PRO C 152     1555   1555  1.35  
LINK         C   THR C 200                 N   KCX C 201     1555   1555  1.33  
LINK         C   KCX C 201                 N   ASP C 202     1555   1555  1.33  
LINK         C   VAL C 255                 N   SMC C 256     1555   1555  1.33  
LINK         C   SMC C 256                 N   ALA C 257     1555   1555  1.33  
LINK         C   TRP C 368                 N   SMC C 369     1555   1555  1.33  
LINK         C   SMC C 369                 N   SER C 370     1555   1555  1.33  
LINK        MG    MG C 476                 O2  CAP C 501     1555   1555  2.33  
LINK        MG    MG C 476                 O3  CAP C 501     1555   1555  2.22  
LINK         C   TYR D 103                 N   HYP D 104     1555   1555  1.35  
LINK         C   HYP D 104                 N   ILE D 105     1555   1555  1.33  
LINK         C   GLY D 150                 N   HYP D 151     1555   1555  1.34  
LINK         C   HYP D 151                 N   PRO D 152     1555   1555  1.34  
LINK         C   THR D 200                 N   KCX D 201     1555   1555  1.33  
LINK         C   KCX D 201                 N   ASP D 202     1555   1555  1.33  
LINK         C   VAL D 255                 N   SMC D 256     1555   1555  1.33  
LINK         C   SMC D 256                 N   ALA D 257     1555   1555  1.33  
LINK         C   TRP D 368                 N   SMC D 369     1555   1555  1.33  
LINK         C   SMC D 369                 N   SER D 370     1555   1555  1.33  
LINK        MG    MG D 476                 O2  CAP D 501     1555   1555  2.30  
LINK        MG    MG D 476                 O3  CAP D 501     1555   1555  2.21  
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.35  
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.33  
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.35  
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.34  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33  
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33  
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.33  
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.33  
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33  
LINK        MG    MG E 476                 O3  CAP E 501     1555   1555  2.23  
LINK        MG    MG E 476                 O2  CAP E 501     1555   1555  2.25  
LINK         C   TYR F 103                 N   HYP F 104     1555   1555  1.35  
LINK         C   HYP F 104                 N   ILE F 105     1555   1555  1.33  
LINK         C   GLY F 150                 N   HYP F 151     1555   1555  1.35  
LINK         C   HYP F 151                 N   PRO F 152     1555   1555  1.34  
LINK         C   THR F 200                 N   KCX F 201     1555   1555  1.33  
LINK         C   KCX F 201                 N   ASP F 202     1555   1555  1.33  
LINK         C   VAL F 255                 N   SMC F 256     1555   1555  1.33  
LINK         C   SMC F 256                 N   ALA F 257     1555   1555  1.33  
LINK         C   TRP F 368                 N   SMC F 369     1555   1555  1.33  
LINK         C   SMC F 369                 N   SER F 370     1555   1555  1.33  
LINK        MG    MG F 476                 O6  CAP F 501     1555   1555  2.27  
LINK        MG    MG F 476                 O2  CAP F 501     1555   1555  2.28  
LINK         C   TYR G 103                 N   HYP G 104     1555   1555  1.35  
LINK         C   HYP G 104                 N   ILE G 105     1555   1555  1.33  
LINK         C   GLY G 150                 N   HYP G 151     1555   1555  1.35  
LINK         C   HYP G 151                 N   PRO G 152     1555   1555  1.34  
LINK         C   THR G 200                 N   KCX G 201     1555   1555  1.33  
LINK         C   KCX G 201                 N   ASP G 202     1555   1555  1.33  
LINK         C   VAL G 255                 N   SMC G 256     1555   1555  1.33  
LINK         C   SMC G 256                 N   ALA G 257     1555   1555  1.33  
LINK         C   TRP G 368                 N   SMC G 369     1555   1555  1.33  
LINK         C   SMC G 369                 N   SER G 370     1555   1555  1.33  
LINK        MG    MG G 476                 O2  CAP G 501     1555   1555  2.32  
LINK        MG    MG G 476                 O3  CAP G 501     1555   1555  2.23  
LINK        MG    MG G 476                 O6  CAP G 501     1555   1555  2.21  
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.35  
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.33  
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.35  
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.35  
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.33  
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.34  
LINK         C   VAL H 255                 N   SMC H 256     1555   1555  1.33  
LINK         C   SMC H 256                 N   ALA H 257     1555   1555  1.33  
LINK         C   TRP H 368                 N   SMC H 369     1555   1555  1.33  
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.33  
LINK        MG    MG H 476                 O2  CAP H 501     1555   1555  2.29  
LINK         C   MME I   1                 N   MET I   2     1555   1555  1.33  
LINK         C   MME J   1                 N   MET J   2     1555   1555  1.33  
LINK         C   MME K   1                 N   MET K   2     1555   1555  1.33  
LINK         C   MME L   1                 N   MET L   2     1555   1555  1.32  
LINK         C   MME M   1                 N   MET M   2     1555   1555  1.33  
LINK         C   MME N   1                 N   MET N   2     1555   1555  1.33  
LINK         C   MME O   1                 N   MET O   2     1555   1555  1.33  
LINK         C   MME P   1                 N   MET P   2     1555   1555  1.33  
LINK         C   TYR S 103                 N   HYP S 104     1555   1555  1.35  
LINK         C   HYP S 104                 N   ILE S 105     1555   1555  1.33  
LINK         C   GLY S 150                 N   HYP S 151     1555   1555  1.35  
LINK         C   HYP S 151                 N   PRO S 152     1555   1555  1.35  
LINK         C   THR S 200                 N   KCX S 201     1555   1555  1.33  
LINK         C   KCX S 201                 N   ASP S 202     1555   1555  1.33  
LINK         C   VAL S 255                 N   SMC S 256     1555   1555  1.33  
LINK         C   SMC S 256                 N   ALA S 257     1555   1555  1.33  
LINK         C   TRP S 368                 N   SMC S 369     1555   1555  1.33  
LINK         C   SMC S 369                 N   SER S 370     1555   1555  1.33  
LINK        MG    MG S 476                 O3  CAP S 501     1555   1555  2.22  
LINK        MG    MG S 476                 O2  CAP S 501     1555   1555  2.28  
LINK        MG    MG S 476                 O6  CAP S 501     1555   1555  2.23  
LINK         C   TYR T 103                 N   HYP T 104     1555   1555  1.35  
LINK         C   HYP T 104                 N   ILE T 105     1555   1555  1.33  
LINK         C   GLY T 150                 N   HYP T 151     1555   1555  1.35  
LINK         C   HYP T 151                 N   PRO T 152     1555   1555  1.35  
LINK         C   THR T 200                 N   KCX T 201     1555   1555  1.33  
LINK         C   KCX T 201                 N   ASP T 202     1555   1555  1.33  
LINK         C   VAL T 255                 N   SMC T 256     1555   1555  1.33  
LINK         C   SMC T 256                 N   ALA T 257     1555   1555  1.33  
LINK         C   TRP T 368                 N   SMC T 369     1555   1555  1.33  
LINK         C   SMC T 369                 N   SER T 370     1555   1555  1.33  
LINK        MG    MG T 476                 O3  CAP T 501     1555   1555  2.22  
LINK        MG    MG T 476                 O2  CAP T 501     1555   1555  2.26  
LINK         C   TYR U 103                 N   HYP U 104     1555   1555  1.35  
LINK         C   HYP U 104                 N   ILE U 105     1555   1555  1.33  
LINK         C   GLY U 150                 N   HYP U 151     1555   1555  1.35  
LINK         C   HYP U 151                 N   PRO U 152     1555   1555  1.35  
LINK         C   THR U 200                 N   KCX U 201     1555   1555  1.33  
LINK         C   KCX U 201                 N   ASP U 202     1555   1555  1.33  
LINK         C   VAL U 255                 N   SMC U 256     1555   1555  1.33  
LINK         C   SMC U 256                 N   ALA U 257     1555   1555  1.33  
LINK         C   TRP U 368                 N   SMC U 369     1555   1555  1.33  
LINK         C   SMC U 369                 N   SER U 370     1555   1555  1.33  
LINK        MG    MG U 476                 O3  CAP U 501     1555   1555  2.22  
LINK        MG    MG U 476                 O6  CAP U 501     1555   1555  2.24  
LINK        MG    MG U 476                 O2  CAP U 501     1555   1555  2.31  
LINK         C   TYR V 103                 N   HYP V 104     1555   1555  1.35  
LINK         C   HYP V 104                 N   ILE V 105     1555   1555  1.33  
LINK         C   GLY V 150                 N   HYP V 151     1555   1555  1.35  
LINK         C   HYP V 151                 N   PRO V 152     1555   1555  1.34  
LINK         C   THR V 200                 N   KCX V 201     1555   1555  1.33  
LINK         C   KCX V 201                 N   ASP V 202     1555   1555  1.33  
LINK         C   VAL V 255                 N   SMC V 256     1555   1555  1.33  
LINK         C   SMC V 256                 N   ALA V 257     1555   1555  1.33  
LINK         C   TRP V 368                 N   SMC V 369     1555   1555  1.33  
LINK         C   SMC V 369                 N   SER V 370     1555   1555  1.33  
LINK        MG    MG V 476                 O2  CAP V 501     1555   1555  2.28  
LINK        MG    MG V 476                 O3  CAP V 501     1555   1555  2.26  
LINK         C   TYR W 103                 N   HYP W 104     1555   1555  1.35  
LINK         C   HYP W 104                 N   ILE W 105     1555   1555  1.33  
LINK         C   GLY W 150                 N   HYP W 151     1555   1555  1.34  
LINK         C   HYP W 151                 N   PRO W 152     1555   1555  1.34  
LINK         C   THR W 200                 N   KCX W 201     1555   1555  1.33  
LINK         C   KCX W 201                 N   ASP W 202     1555   1555  1.33  
LINK         C   VAL W 255                 N   SMC W 256     1555   1555  1.33  
LINK         C   SMC W 256                 N   ALA W 257     1555   1555  1.33  
LINK         C   TRP W 368                 N   SMC W 369     1555   1555  1.33  
LINK         C   SMC W 369                 N   SER W 370     1555   1555  1.33  
LINK        MG    MG W 476                 O6  CAP W 501     1555   1555  2.25  
LINK        MG    MG W 476                 O2  CAP W 501     1555   1555  2.33  
LINK         C   TYR X 103                 N   HYP X 104     1555   1555  1.35  
LINK         C   HYP X 104                 N   ILE X 105     1555   1555  1.33  
LINK         C   GLY X 150                 N   HYP X 151     1555   1555  1.35  
LINK         C   HYP X 151                 N   PRO X 152     1555   1555  1.34  
LINK         C   THR X 200                 N   KCX X 201     1555   1555  1.33  
LINK         C   KCX X 201                 N   ASP X 202     1555   1555  1.33  
LINK         C   VAL X 255                 N   SMC X 256     1555   1555  1.33  
LINK         C   SMC X 256                 N   ALA X 257     1555   1555  1.33  
LINK         C   TRP X 368                 N   SMC X 369     1555   1555  1.33  
LINK         C   SMC X 369                 N   SER X 370     1555   1555  1.33  
LINK        MG    MG X 476                 O3  CAP X 501     1555   1555  2.27  
LINK        MG    MG X 476                 O2  CAP X 501     1555   1555  2.32  
LINK         C   TYR Y 103                 N   HYP Y 104     1555   1555  1.35  
LINK         C   HYP Y 104                 N   ILE Y 105     1555   1555  1.33  
LINK         C   GLY Y 150                 N   HYP Y 151     1555   1555  1.35  
LINK         C   HYP Y 151                 N   PRO Y 152     1555   1555  1.34  
LINK         C   THR Y 200                 N   KCX Y 201     1555   1555  1.33  
LINK         C   KCX Y 201                 N   ASP Y 202     1555   1555  1.33  
LINK         C   VAL Y 255                 N   SMC Y 256     1555   1555  1.33  
LINK         C   SMC Y 256                 N   ALA Y 257     1555   1555  1.33  
LINK         C   TRP Y 368                 N   SMC Y 369     1555   1555  1.33  
LINK         C   SMC Y 369                 N   SER Y 370     1555   1555  1.33  
LINK        MG    MG Y 476                 O6  CAP Y 501     1555   1555  2.23  
LINK        MG    MG Y 476                 O3  CAP Y 501     1555   1555  2.25  
LINK        MG    MG Y 476                 O2  CAP Y 501     1555   1555  2.33  
LINK         C   TYR Z 103                 N   HYP Z 104     1555   1555  1.35  
LINK         C   HYP Z 104                 N   ILE Z 105     1555   1555  1.33  
LINK         C   GLY Z 150                 N   HYP Z 151     1555   1555  1.35  
LINK         C   HYP Z 151                 N   PRO Z 152     1555   1555  1.34  
LINK         C   THR Z 200                 N   KCX Z 201     1555   1555  1.33  
LINK         C   KCX Z 201                 N   ASP Z 202     1555   1555  1.33  
LINK         C   VAL Z 255                 N   SMC Z 256     1555   1555  1.33  
LINK         C   SMC Z 256                 N   ALA Z 257     1555   1555  1.33  
LINK         C   TRP Z 368                 N   SMC Z 369     1555   1555  1.33  
LINK         C   SMC Z 369                 N   SER Z 370     1555   1555  1.33  
LINK        MG    MG Z 476                 O3  CAP Z 501     1555   1555  2.24  
LINK        MG    MG Z 476                 O6  CAP Z 501     1555   1555  2.23  
LINK        MG    MG Z 476                 O2  CAP Z 501     1555   1555  2.34  
CISPEP   1 LYS A  175    PRO A  176          0        -0.07                     
CISPEP   2 LYS B  175    PRO B  176          0        -0.05                     
CISPEP   3 LYS C  175    PRO C  176          0        -0.14                     
CISPEP   4 LYS D  175    PRO D  176          0         0.01                     
CISPEP   5 LYS E  175    PRO E  176          0        -0.14                     
CISPEP   6 LYS F  175    PRO F  176          0        -0.09                     
CISPEP   7 LYS G  175    PRO G  176          0        -0.06                     
CISPEP   8 LYS H  175    PRO H  176          0        -0.27                     
CISPEP   9 LYS S  175    PRO S  176          0        -0.05                     
CISPEP  10 LYS T  175    PRO T  176          0        -0.09                     
CISPEP  11 LYS U  175    PRO U  176          0        -0.30                     
CISPEP  12 LYS V  175    PRO V  176          0        -0.12                     
CISPEP  13 LYS W  175    PRO W  176          0        -0.16                     
CISPEP  14 LYS X  175    PRO X  176          0        -0.11                     
CISPEP  15 LYS Y  175    PRO Y  176          0        -0.19                     
CISPEP  16 LYS Z  175    PRO Z  176          0        -0.07                     
SITE     1 AC1  4 KCX A 201  ASP A 203  GLU A 204  CAP A 501                    
SITE     1 AC2  5 LYS B 177  KCX B 201  ASP B 203  GLU B 204                    
SITE     2 AC2  5 CAP B 501                                                     
SITE     1 AC3  5 LYS C 177  KCX C 201  ASP C 203  GLU C 204                    
SITE     2 AC3  5 CAP C 501                                                     
SITE     1 AC4  4 KCX D 201  ASP D 203  GLU D 204  CAP D 501                    
SITE     1 AC5  4 KCX E 201  ASP E 203  GLU E 204  CAP E 501                    
SITE     1 AC6  5 LYS F 177  KCX F 201  ASP F 203  GLU F 204                    
SITE     2 AC6  5 CAP F 501                                                     
SITE     1 AC7  5 LYS G 177  KCX G 201  ASP G 203  GLU G 204                    
SITE     2 AC7  5 CAP G 501                                                     
SITE     1 AC8  4 KCX H 201  ASP H 203  GLU H 204  CAP H 501                    
SITE     1 AC9  4 KCX S 201  ASP S 203  GLU S 204  CAP S 501                    
SITE     1 BC1  4 KCX T 201  ASP T 203  GLU T 204  CAP T 501                    
SITE     1 BC2  5 LYS U 177  KCX U 201  ASP U 203  GLU U 204                    
SITE     2 BC2  5 CAP U 501                                                     
SITE     1 BC3  4 KCX V 201  ASP V 203  GLU V 204  CAP V 501                    
SITE     1 BC4  5 LYS W 177  KCX W 201  ASP W 203  GLU W 204                    
SITE     2 BC4  5 CAP W 501                                                     
SITE     1 BC5  5 LYS X 177  KCX X 201  ASP X 203  GLU X 204                    
SITE     2 BC5  5 CAP X 501                                                     
SITE     1 BC6  5 LYS Y 177  KCX Y 201  ASP Y 203  GLU Y 204                    
SITE     2 BC6  5 CAP Y 501                                                     
SITE     1 BC7  5 LYS Z 177  KCX Z 201  ASP Z 203  GLU Z 204                    
SITE     2 BC7  5 CAP Z 501                                                     
SITE     1 BC8 29 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 BC8 29 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 BC8 29 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 BC8 29 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 BC8 29  MG A 476  HOH A 616  HOH A 617  HOH A 621                    
SITE     6 BC8 29 HOH A 630  HOH A 660  HOH A 679  GLU E  60                    
SITE     7 BC8 29 THR E  65  TRP E  66  ASN E 123  HOH E 678                    
SITE     8 BC8 29 HOH E 731                                                     
SITE     1 BC9 29 THR B 173  LYS B 175  LYS B 177  KCX B 201                    
SITE     2 BC9 29 ASP B 203  GLU B 204  HIS B 294  ARG B 295                    
SITE     3 BC9 29 HIS B 327  LYS B 334  LEU B 335  SER B 379                    
SITE     4 BC9 29 GLY B 380  GLY B 381  GLY B 403  GLY B 404                    
SITE     5 BC9 29  MG B 476  HOH B 615  HOH B 622  HOH B 653                    
SITE     6 BC9 29 HOH B 657  HOH B 678  HOH B 700  GLU F  60                    
SITE     7 BC9 29 THR F  65  TRP F  66  ASN F 123  HOH F 646                    
SITE     8 BC9 29 HOH F 648                                                     
SITE     1 CC1 29 THR C 173  LYS C 175  LYS C 177  KCX C 201                    
SITE     2 CC1 29 ASP C 203  GLU C 204  HIS C 294  ARG C 295                    
SITE     3 CC1 29 HIS C 327  LYS C 334  LEU C 335  SER C 379                    
SITE     4 CC1 29 GLY C 380  GLY C 381  GLY C 403  GLY C 404                    
SITE     5 CC1 29  MG C 476  HOH C 618  HOH C 625  HOH C 637                    
SITE     6 CC1 29 HOH C 646  HOH C 657  HOH C 909  GLU G  60                    
SITE     7 CC1 29 THR G  65  TRP G  66  ASN G 123  HOH G 639                    
SITE     8 CC1 29 HOH G 675                                                     
SITE     1 CC2 29 THR D 173  LYS D 175  LYS D 177  KCX D 201                    
SITE     2 CC2 29 ASP D 203  GLU D 204  HIS D 294  ARG D 295                    
SITE     3 CC2 29 HIS D 327  LYS D 334  LEU D 335  SER D 379                    
SITE     4 CC2 29 GLY D 380  GLY D 381  GLY D 403  GLY D 404                    
SITE     5 CC2 29  MG D 476  HOH D 617  HOH D 618  HOH D 621                    
SITE     6 CC2 29 HOH D 658  HOH D 661  HOH D 805  GLU H  60                    
SITE     7 CC2 29 THR H  65  TRP H  66  ASN H 123  HOH H 621                    
SITE     8 CC2 29 HOH H 644                                                     
SITE     1 CC3 30 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 CC3 30 HOH A 657  HOH A 779  THR E 173  LYS E 175                    
SITE     3 CC3 30 LYS E 177  KCX E 201  ASP E 203  GLU E 204                    
SITE     4 CC3 30 HIS E 294  ARG E 295  HIS E 327  LYS E 334                    
SITE     5 CC3 30 LEU E 335  SER E 379  GLY E 380  GLY E 381                    
SITE     6 CC3 30 GLY E 403  GLY E 404   MG E 476  HOH E 623                    
SITE     7 CC3 30 HOH E 630  HOH E 632  HOH E 635  HOH E 659                    
SITE     8 CC3 30 HOH E 698  HOH E 778                                          
SITE     1 CC4 29 GLU B  60  THR B  65  TRP B  66  ASN B 123                    
SITE     2 CC4 29 HOH B 620  HOH B 666  THR F 173  LYS F 175                    
SITE     3 CC4 29 LYS F 177  KCX F 201  ASP F 203  GLU F 204                    
SITE     4 CC4 29 HIS F 294  ARG F 295  HIS F 327  LYS F 334                    
SITE     5 CC4 29 LEU F 335  SER F 379  GLY F 380  GLY F 381                    
SITE     6 CC4 29 GLY F 403  GLY F 404   MG F 476  HOH F 619                    
SITE     7 CC4 29 HOH F 625  HOH F 641  HOH F 652  HOH F 704                    
SITE     8 CC4 29 HOH F 786                                                     
SITE     1 CC5 29 GLU C  60  THR C  65  TRP C  66  ASN C 123                    
SITE     2 CC5 29 HOH C 621  HOH C 645  THR G 173  LYS G 175                    
SITE     3 CC5 29 LYS G 177  KCX G 201  ASP G 203  GLU G 204                    
SITE     4 CC5 29 HIS G 294  ARG G 295  HIS G 327  LYS G 334                    
SITE     5 CC5 29 LEU G 335  SER G 379  GLY G 380  GLY G 381                    
SITE     6 CC5 29 GLY G 403  GLY G 404   MG G 476  HOH G 620                    
SITE     7 CC5 29 HOH G 631  HOH G 642  HOH G 648  HOH G 656                    
SITE     8 CC5 29 HOH G 721                                                     
SITE     1 CC6 29 GLU D  60  THR D  65  TRP D  66  ASN D 123                    
SITE     2 CC6 29 HOH D 652  HOH D 659  THR H 173  LYS H 175                    
SITE     3 CC6 29 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     4 CC6 29 HIS H 294  ARG H 295  HIS H 327  LYS H 334                    
SITE     5 CC6 29 LEU H 335  SER H 379  GLY H 380  GLY H 381                    
SITE     6 CC6 29 GLY H 403  GLY H 404   MG H 476  HOH H 624                    
SITE     7 CC6 29 HOH H 628  HOH H 630  HOH H 637  HOH H 682                    
SITE     8 CC6 29 HOH H 726                                                     
SITE     1 CC7 29 THR S 173  LYS S 175  LYS S 177  KCX S 201                    
SITE     2 CC7 29 ASP S 203  GLU S 204  HIS S 294  ARG S 295                    
SITE     3 CC7 29 HIS S 327  LYS S 334  LEU S 335  SER S 379                    
SITE     4 CC7 29 GLY S 380  GLY S 381  GLY S 403  GLY S 404                    
SITE     5 CC7 29  MG S 476  HOH S 614  HOH S 615  HOH S 623                    
SITE     6 CC7 29 HOH S 653  HOH S 676  HOH S 694  HOH S 758                    
SITE     7 CC7 29 GLU W  60  THR W  65  TRP W  66  ASN W 123                    
SITE     8 CC7 29 HOH W 629                                                     
SITE     1 CC8 28 THR T 173  LYS T 175  LYS T 177  KCX T 201                    
SITE     2 CC8 28 ASP T 203  GLU T 204  HIS T 294  ARG T 295                    
SITE     3 CC8 28 HIS T 327  LYS T 334  LEU T 335  SER T 379                    
SITE     4 CC8 28 GLY T 380  GLY T 381  GLY T 403  GLY T 404                    
SITE     5 CC8 28  MG T 476  HOH T 615  HOH T 662  HOH T 717                    
SITE     6 CC8 28 HOH T 721  HOH T 802  HOH T 886  GLU X  60                    
SITE     7 CC8 28 THR X  65  TRP X  66  ASN X 123  HOH X 633                    
SITE     1 CC9 29 THR U 173  LYS U 175  LYS U 177  KCX U 201                    
SITE     2 CC9 29 ASP U 203  GLU U 204  HIS U 294  ARG U 295                    
SITE     3 CC9 29 HIS U 327  LYS U 334  LEU U 335  SER U 379                    
SITE     4 CC9 29 GLY U 380  GLY U 381  GLY U 403  GLY U 404                    
SITE     5 CC9 29  MG U 476  HOH U 620  HOH U 625  HOH U 667                    
SITE     6 CC9 29 HOH U 705  HOH U 706  HOH U 779  GLU Y  60                    
SITE     7 CC9 29 THR Y  65  TRP Y  66  ASN Y 123  HOH Y 619                    
SITE     8 CC9 29 HOH Y 715                                                     
SITE     1 DC1 28 THR V 173  LYS V 175  LYS V 177  KCX V 201                    
SITE     2 DC1 28 ASP V 203  GLU V 204  HIS V 294  ARG V 295                    
SITE     3 DC1 28 HIS V 327  LYS V 334  LEU V 335  SER V 379                    
SITE     4 DC1 28 GLY V 380  GLY V 381  GLY V 403  GLY V 404                    
SITE     5 DC1 28  MG V 476  HOH V 617  HOH V 620  HOH V 623                    
SITE     6 DC1 28 HOH V 673  HOH V 701  HOH V 703  GLU Z  60                    
SITE     7 DC1 28 THR Z  65  TRP Z  66  ASN Z 123  HOH Z 657                    
SITE     1 DC2 30 GLU S  60  THR S  65  TRP S  66  ASN S 123                    
SITE     2 DC2 30 HOH S 624  THR W 173  LYS W 175  LYS W 177                    
SITE     3 DC2 30 KCX W 201  ASP W 203  GLU W 204  HIS W 294                    
SITE     4 DC2 30 ARG W 295  HIS W 327  LYS W 334  LEU W 335                    
SITE     5 DC2 30 SER W 379  GLY W 380  GLY W 381  GLY W 403                    
SITE     6 DC2 30 GLY W 404   MG W 476  HOH W 626  HOH W 632                    
SITE     7 DC2 30 HOH W 655  HOH W 661  HOH W 662  HOH W 665                    
SITE     8 DC2 30 HOH W 704  HOH W 874                                          
SITE     1 DC3 29 GLU T  60  THR T  65  TRP T  66  ASN T 123                    
SITE     2 DC3 29 HOH T 664  HOH T 680  THR X 173  LYS X 175                    
SITE     3 DC3 29 LYS X 177  KCX X 201  ASP X 203  GLU X 204                    
SITE     4 DC3 29 HIS X 294  ARG X 295  HIS X 327  LYS X 334                    
SITE     5 DC3 29 LEU X 335  SER X 379  GLY X 380  GLY X 381                    
SITE     6 DC3 29 GLY X 403  GLY X 404   MG X 476  HOH X 618                    
SITE     7 DC3 29 HOH X 635  HOH X 637  HOH X 650  HOH X 652                    
SITE     8 DC3 29 HOH X 764                                                     
SITE     1 DC4 30 GLU U  60  THR U  65  TRP U  66  ASN U 123                    
SITE     2 DC4 30 HOH U 622  HOH U 629  THR Y 173  LYS Y 175                    
SITE     3 DC4 30 LYS Y 177  KCX Y 201  ASP Y 203  GLU Y 204                    
SITE     4 DC4 30 HIS Y 294  ARG Y 295  HIS Y 327  LYS Y 334                    
SITE     5 DC4 30 LEU Y 335  SER Y 379  GLY Y 380  GLY Y 381                    
SITE     6 DC4 30 GLY Y 403  GLY Y 404   MG Y 476  HOH Y 620                    
SITE     7 DC4 30 HOH Y 627  HOH Y 629  HOH Y 645  HOH Y 659                    
SITE     8 DC4 30 HOH Y 749  HOH Y 750                                          
SITE     1 DC5 28 GLU V  60  THR V  65  TRP V  66  ASN V 123                    
SITE     2 DC5 28 HOH V 671  THR Z 173  LYS Z 175  LYS Z 177                    
SITE     3 DC5 28 KCX Z 201  ASP Z 203  GLU Z 204  HIS Z 294                    
SITE     4 DC5 28 ARG Z 295  HIS Z 327  LYS Z 334  LEU Z 335                    
SITE     5 DC5 28 SER Z 379  GLY Z 380  GLY Z 381  GLY Z 403                    
SITE     6 DC5 28 GLY Z 404   MG Z 476  HOH Z 624  HOH Z 625                    
SITE     7 DC5 28 HOH Z 627  HOH Z 628  HOH Z 629  HOH Z 787                    
SITE     1 DC6  9 VAL E  17  LYS E  18  THR E  65  TRP E  66                    
SITE     2 DC6  9 THR E  67  THR E  68  HOH E 656  HOH E 670                    
SITE     3 DC6  9 HOH E 792                                                     
SITE     1 DC7  9 VAL F  17  LYS F  18  THR F  65  TRP F  66                    
SITE     2 DC7  9 THR F  67  THR F  68  HOH F 659  HOH F 701                    
SITE     3 DC7  9 HOH F 795                                                     
SITE     1 DC8  9 VAL G  17  LYS G  18  THR G  65  TRP G  66                    
SITE     2 DC8  9 THR G  67  THR G  68  HOH G 676  HOH G 776                    
SITE     3 DC8  9 HOH G 780                                                     
SITE     1 DC9  8 LYS H  18  TYR H  24  THR H  65  TRP H  66                    
SITE     2 DC9  8 THR H  67  THR H  68  HOH H 732  HOH H 784                    
SITE     1 EC1  9 LYS A  18  THR A  65  TRP A  66  THR A  67                    
SITE     2 EC1  9 THR A  68  HOH A 688  HOH A 751  HOH A 795                    
SITE     3 EC1  9 HOH A 821                                                     
SITE     1 EC2 10 VAL B  17  LYS B  18  THR B  65  TRP B  66                    
SITE     2 EC2 10 THR B  67  THR B  68  HOH B 638  HOH B 652                    
SITE     3 EC2 10 HOH B 726  HOH B 728                                          
SITE     1 EC3 10 VAL C  17  LYS C  18  THR C  65  TRP C  66                    
SITE     2 EC3 10 THR C  67  THR C  68  HOH C 627  HOH C 761                    
SITE     3 EC3 10 HOH C 763  HOH C 954                                          
SITE     1 EC4  9 VAL D  17  LYS D  18  THR D  65  TRP D  66                    
SITE     2 EC4  9 THR D  67  THR D  68  HOH D 665  HOH D 741                    
SITE     3 EC4  9 HOH D 815                                                     
SITE     1 EC5  6 LEU A 270  LEU E 270  MET E 297  HOH E 717                    
SITE     2 EC5  6 HOH E 729  HOH E 813                                          
SITE     1 EC6  6 LEU B 270  HOH B 769  HOH B 789  LEU F 270                    
SITE     2 EC6  6 MET F 297  HOH F 663                                          
SITE     1 EC7  6 LEU C 270  HOH C 648  LEU G 270  MET G 297                    
SITE     2 EC7  6 HOH G 636  HOH G 816                                          
SITE     1 EC8  6 LEU D 270  LEU H 270  MET H 297  HOH H 675                    
SITE     2 EC8  6 HOH H 742  HOH H 922                                          
SITE     1 EC9  8 VAL A 149  ARG A 285  ASP A 286  HOH A 710                    
SITE     2 EC9  8 HOH A 769  HOH A 974  LYS B 252  HOH B 634                    
SITE     1 FC1  6 ILE B 282  ARG B 285  ASP B 286  HOH B 661                    
SITE     2 FC1  6 HOH B 747  LYS C 252                                          
SITE     1 FC2  7 ILE C 282  ARG C 285  ASP C 286  HOH C 719                    
SITE     2 FC2  7 HOH C1060  LYS D 252  HOH D 642                               
SITE     1 FC3  8 LYS A 252  HOH A 642  ILE D 282  ARG D 285                    
SITE     2 FC3  8 ASP D 286  HOH D 720  HOH D 875  HOH D1059                    
SITE     1 FC4  6 LYS E 252  HOH E 683  ILE F 282  ARG F 285                    
SITE     2 FC4  6 ASP F 286  HOH F 757                                          
SITE     1 FC5  6 LYS F 252  HOH F 722  ARG G 285  ASP G 286                    
SITE     2 FC5  6 HOH G 732  HOH G1026                                          
SITE     1 FC6  7 LYS G 252  HOH G 740  ILE H 282  ASP H 286                    
SITE     2 FC6  7 HOH H 739  HOH H 906  HOH H1023                               
SITE     1 FC7  9 VAL E 149  ILE E 282  ARG E 285  ASP E 286                    
SITE     2 FC7  9 HOH E 701  HOH E1004  HOH E1057  LYS H 252                    
SITE     3 FC7  9 HOH H 671                                                     
SITE     1 FC8  9 VAL W  17  LYS W  18  THR W  65  TRP W  66                    
SITE     2 FC8  9 THR W  67  THR W  68  HOH W 731  HOH W 794                    
SITE     3 FC8  9 HOH W 910                                                     
SITE     1 FC9 10 VAL X  17  LYS X  18  THR X  65  TRP X  66                    
SITE     2 FC9 10 THR X  67  THR X  68  HOH X 636  HOH X 648                    
SITE     3 FC9 10 HOH X 738  HOH X 869                                          
SITE     1 GC1  9 VAL Y  17  LYS Y  18  THR Y  65  TRP Y  66                    
SITE     2 GC1  9 THR Y  67  THR Y  68  HOH Y 634  HOH Y 842                    
SITE     3 GC1  9 HOH Y 957                                                     
SITE     1 GC2 10 VAL Z  17  LYS Z  18  THR Z  65  TRP Z  66                    
SITE     2 GC2 10 THR Z  67  THR Z  68  HOH Z 769  HOH Z 772                    
SITE     3 GC2 10 HOH Z 800  HOH Z 867                                          
SITE     1 GC3  9 VAL S  17  LYS S  18  THR S  65  TRP S  66                    
SITE     2 GC3  9 THR S  67  THR S  68  HOH S 773  HOH S 888                    
SITE     3 GC3  9 HOH S 901                                                     
SITE     1 GC4  9 VAL T  17  LYS T  18  THR T  65  TRP T  66                    
SITE     2 GC4  9 THR T  67  THR T  68  HOH T 655  HOH T 770                    
SITE     3 GC4  9 HOH T 894                                                     
SITE     1 GC5 10 VAL U  17  LYS U  18  THR U  65  TRP U  66                    
SITE     2 GC5 10 THR U  67  THR U  68  HOH U 659  HOH U 717                    
SITE     3 GC5 10 HOH U 888  HOH U 945                                          
SITE     1 GC6  9 VAL V  17  LYS V  18  THR V  65  TRP V  66                    
SITE     2 GC6  9 THR V  67  THR V  68  HOH V 624  HOH V 751                    
SITE     3 GC6  9 HOH V 806                                                     
SITE     1 GC7  8 LEU S 270  MET S 297  HOH S 638  HOH S 677                    
SITE     2 GC7  8 HOH S 992  HOH S1002  LEU W 270  ILE W 301                    
SITE     1 GC8  6 LEU T 270  HOH T 749  LEU X 270  MET X 297                    
SITE     2 GC8  6 HOH X 726  HOH X 812                                          
SITE     1 GC9  6 LEU U 270  LEU Y 270  MET Y 297  HOH Y 670                    
SITE     2 GC9  6 HOH Y 724  HOH Y 869                                          
SITE     1 HC1  6 LEU V 270  MET V 297  LEU Z 270  HOH Z 673                    
SITE     2 HC1  6 HOH Z 728  HOH Z 959                                          
SITE     1 HC2  8 ILE S 282  ARG S 285  ASP S 286  HOH S 680                    
SITE     2 HC2  8 HOH S 892  HOH S1034  LYS T 252  HOH T 631                    
SITE     1 HC3  7 ARG T 285  ASP T 286  HOH T 726  HOH T 981                    
SITE     2 HC3  7 GLU U 249  LYS U 252  HOH U 639                               
SITE     1 HC4  8 VAL U 149  ILE U 282  ARG U 285  ASP U 286                    
SITE     2 HC4  8 HOH U 686  HOH U 985  LYS V 252  HOH V 714                    
SITE     1 HC5  9 LYS S 252  HOH S 656  VAL V 149  ILE V 282                    
SITE     2 HC5  9 ARG V 285  ASP V 286  HOH V 719  HOH V 808                    
SITE     3 HC5  9 HOH V1019                                                     
SITE     1 HC6  6 LYS W 252  ARG X 285  ASP X 286  HOH X 673                    
SITE     2 HC6  6 HOH X 753  HOH X 921                                          
SITE     1 HC7  8 LYS X 252  HOH X 710  VAL Y 149  ILE Y 282                    
SITE     2 HC7  8 ASP Y 286  HOH Y 887  HOH Y 923  HOH Y 951                    
SITE     1 HC8  7 LYS Y 252  HOH Y 692  ARG Z 285  ASP Z 286                    
SITE     2 HC8  7 HOH Z 726  HOH Z 752  HOH Z 921                               
SITE     1 HC9  8 VAL W 149  ILE W 282  ARG W 285  ASP W 286                    
SITE     2 HC9  8 HOH W 675  HOH W 841  LYS Z 252  HOH Z 623                    
CRYST1  129.170  174.750  222.270  90.00  97.75  90.00 P 1 21 1     32          
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      0.007742  0.000000  0.001054        0.00000                         
SCALE2      0.000000  0.005722  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004541        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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