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Database: PDB
Entry: 1UW9
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HEADER    LYASE                                   03-FEB-04   1UW9              
TITLE     L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE LARGE CHAIN;             
COMPND   3 CHAIN: A, B, E, H, K, O, R, V;                                       
COMPND   4 SYNONYM: RUBISCO LARGE SUBUNIT, RIBULOSE-1,5 BISPHOSPHATE            
COMPND   5  CARBOXYLASE LARGE CHAIN;                                            
COMPND   6 EC: 4.1.1.39;                                                        
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1;           
COMPND  10 CHAIN: I, C, F, J, P, T, M, W;                                       
COMPND  11 SYNONYM: RUBISCO SMALL SUBUNIT 1;                                    
COMPND  12 EC: 4.1.1.39                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   3 ORGANISM_TAXID: 3055;                                                
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: CHLAMYDOMONAS REINHARDTII;                      
SOURCE   6 ORGANISM_TAXID: 3055                                                 
KEYWDS    LYASE, RUBISCO, PHOTOSYNTHESIS, PHOTORESPIRATION,                     
KEYWDS   2 OXIDOREDUCTASE, MONOOXYGENASE, CARBON DIOXIDE FIXATION               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KARKEHABADI,T.C.TAYLOR,R.J.SPREITZER,I.ANDERSSON                    
REVDAT   3   24-FEB-09 1UW9    1       VERSN                                    
REVDAT   2   24-JAN-05 1UW9    1       SSBOND                                   
REVDAT   1   12-JAN-05 1UW9    0                                                
JRNL        AUTH   S.KARKEHABADI,T.C.TAYLOR,R.J.SPREITZER,I.ANDERSSON           
JRNL        TITL   ALTERED INTERSUBUNIT INTERACTIONS IN CRYSTAL                 
JRNL        TITL 2 STRUCTURES OF CATALYTICALLY COMPROMISED                      
JRNL        TITL 3 RIBULOSE-1,5-BISPHOSPHATE CARBOXYLASE/OXYGENASE              
JRNL        REF    BIOCHEMISTRY                  V.  44   113 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   15628851                                                     
JRNL        DOI    10.1021/BI047928E                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 89                             
REMARK   3   NUMBER OF REFLECTIONS             : 226650                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.15690                         
REMARK   3   R VALUE            (WORKING SET) : 0.15690                         
REMARK   3   FREE R VALUE                     : 0.19421                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 11867                           
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 38123                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 732                                     
REMARK   3   SOLVENT ATOMS            : 2819                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 18.147                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.53                                                
REMARK   3    B22 (A**2) : -0.17                                                
REMARK   3    B33 (A**2) : 0.82                                                 
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.12                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.290         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.184         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.118         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.513         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : NULL  ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; 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  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1UW9 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON  03-FEB-04.                 
REMARK 100 THE PDBE ID CODE IS EBI-14467.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-FEB-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.934                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 295370                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.9                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.15000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 83.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.800                              
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 ENTRY 1GK8                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS  (%): NULL                                       
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0 MM HEPES PH 7.5, 8-12% PEG 4           
REMARK 280  50 MM NAHCO3, 5 MM MGCL2, 50 UM 2-CABP, 18 DEG C, 10-15 MG          
REMARK 280  PROTEIN                                                             
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       89.09800            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300                                                                      
REMARK 300 DETAILS:FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK                  
REMARK 300  350                                                                 
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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: PQS                                                   
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A,  B, E, H, K, O, R, V, I,           
REMARK 350                    AND CHAINS: C, F, J, P, T, M, W                   
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400  ENGINEERED MUTATION ALA 222 THR AND LEU 290 PHE IN                  
REMARK 400  CHAINS A, B, E, H, K, O, R AND V.                                   
REMARK 400                                                                      
REMARK 400  RUBISCO CATALYZES TWO REACTIONS: THE CARBOXYLATION OF D-            
REMARK 400  RIBULOSE 1,5-BISPHOSPHATE, THE PRIMARY EVENT IN                     
REMARK 400  PHOTOSYNTHETIC CARBON DIOXIDE FIXATION, AS WELL AS THE              
REMARK 400  OXIDATIVE FRAGMENTATION OF THE PENTOSE SUBSTRATE IN THE             
REMARK 400  PHOTORESPIRATION PROCESS. BOTH REACTIONS OCCUR SIMULTANEOUSLY       
REMARK 400  AND IN COMPETITION AT THE SAME ACTIVE SITE.                         
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     LYS A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLY A    10                                                      
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 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 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     MET K     1                                                      
REMARK 465     VAL K     2                                                      
REMARK 465     PRO K     3                                                      
REMARK 465     GLN K     4                                                      
REMARK 465     THR K     5                                                      
REMARK 465     GLU K     6                                                      
REMARK 465     MET O     1                                                      
REMARK 465     VAL O     2                                                      
REMARK 465     PRO O     3                                                      
REMARK 465     GLN O     4                                                      
REMARK 465     THR O     5                                                      
REMARK 465     GLU O     6                                                      
REMARK 465     MET R     1                                                      
REMARK 465     VAL R     2                                                      
REMARK 465     PRO R     3                                                      
REMARK 465     GLN R     4                                                      
REMARK 465     THR R     5                                                      
REMARK 465     GLU R     6                                                      
REMARK 465     THR R     7                                                      
REMARK 465     LYS R     8                                                      
REMARK 465     ALA R     9                                                      
REMARK 465     GLY R    10                                                      
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     THR V     7                                                      
REMARK 465     LYS V     8                                                      
REMARK 465     ALA V     9                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH1  ARG B    21  -  O    HOH B  2016              2.10            
REMARK 500   NH1  ARG C   130  -  O    HOH C  2073              1.79            
REMARK 500   OG1  THR E   471  -  O    HOH E  2272              1.92            
REMARK 500   CG   ASN F     8  -  O    HOH F  2005              2.11            
REMARK 500   NH1  ARG T   130  -  O    HOH T  2071              2.07            
REMARK 500   OG1  THR V   471  -  O    HOH V  2273              1.95            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500                                                                      
REMARK 500   CE   LYS K    14     OE2  GLU R   460     1646      1.53           
REMARK 500   NZ   LYS K    14     OE2  GLU R   460     1646      2.09           
REMARK 500   NH1  ARG K   439     CG   GLU O    88     1556      2.08           
REMARK 500   CG   GLU O    88     NH1  ARG K   439     1554      2.08           
REMARK 500   OE2  GLU R   460     CE   LYS K    14     1656      1.53           
REMARK 500   OE2  GLU R   460     NZ   LYS K    14     1656      2.09           
REMARK 500   CB   ALA V    11     NH2  ARG W   130     1655      2.20           
REMARK 500   NH2  ARG W   130     CB   ALA V    11     1645      2.20           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASN C   8   N   -  CA  -  C   ANGL. DEV. = -18.0 DEGREES          
REMARK 500    ASN F   8   N   -  CA  -  C   ANGL. DEV. = -18.9 DEGREES          
REMARK 500    ASP H 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASN I   8   N   -  CA  -  C   ANGL. DEV. = -17.9 DEGREES          
REMARK 500    ASN J   8   N   -  CA  -  C   ANGL. DEV. = -17.7 DEGREES          
REMARK 500    ASP K 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASN M   8   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    ASP O 160   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP O 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASN P   8   N   -  CA  -  C   ANGL. DEV. = -17.1 DEGREES          
REMARK 500    ASP R 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASN T   8   N   -  CA  -  C   ANGL. DEV. = -16.8 DEGREES          
REMARK 500    ASP T 131   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP V 203   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASN W   8   N   -  CA  -  C   ANGL. DEV. = -18.1 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 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  62      -80.99   -140.27                                   
REMARK 500    THR A  75     -169.33   -127.51                                   
REMARK 500    CYS A 172      119.97   -178.08                                   
REMARK 500    ASN A 207      -97.45   -123.33                                   
REMARK 500    MET A 212      110.49   -164.14                                   
REMARK 500    MET A 297       -5.42     84.39                                   
REMARK 500    VAL A 331      -50.83     71.02                                   
REMARK 500    ASP A 357       89.77   -163.52                                   
REMARK 500    SER B  62      -80.58   -140.17                                   
REMARK 500    THR B  65     -166.42   -128.70                                   
REMARK 500    THR B  75     -169.84   -128.82                                   
REMARK 500    CYS B 172      120.55   -177.65                                   
REMARK 500    ASN B 207      -95.11   -124.55                                   
REMARK 500    MET B 212      110.05   -165.13                                   
REMARK 500    MET B 297       -4.48     82.38                                   
REMARK 500    VAL B 331      -51.19     73.40                                   
REMARK 500    ASP B 357       90.88   -163.83                                   
REMARK 500    PHE C  12       44.75   -147.79                                   
REMARK 500    GLU C  13     -141.84     58.60                                   
REMARK 500    PHE C  15       -2.68     85.10                                   
REMARK 500    LYS C  77     -122.22     51.49                                   
REMARK 500    SER E  62      -81.88   -139.70                                   
REMARK 500    THR E  65     -167.87   -129.69                                   
REMARK 500    CYS E 172      121.03   -176.14                                   
REMARK 500    ASN E 207      -94.80   -123.79                                   
REMARK 500    MET E 212      110.67   -164.53                                   
REMARK 500    ALA E 296      131.29    -37.77                                   
REMARK 500    MET E 297       -6.09     81.83                                   
REMARK 500    VAL E 331      -48.55     70.75                                   
REMARK 500    ASP E 357       91.02   -163.81                                   
REMARK 500    PHE F  12       46.07   -145.97                                   
REMARK 500    GLU F  13     -142.25     56.92                                   
REMARK 500    PHE F  15       -3.63     84.91                                   
REMARK 500    LYS F  77     -121.13     53.14                                   
REMARK 500    SER H  62      -81.50   -140.59                                   
REMARK 500    THR H  65     -167.00   -129.62                                   
REMARK 500    THR H  75     -168.09   -125.81                                   
REMARK 500    CYS H 172      122.21   -177.54                                   
REMARK 500    ASN H 207      -96.48   -123.72                                   
REMARK 500    MET H 212      112.27   -164.74                                   
REMARK 500    ALA H 296      129.69    -37.54                                   
REMARK 500    MET H 297       -5.62     82.51                                   
REMARK 500    VAL H 331      -50.35     69.84                                   
REMARK 500    ASP H 357       89.56   -164.87                                   
REMARK 500    PHE I  12       45.06   -148.75                                   
REMARK 500    GLU I  13     -143.39     58.55                                   
REMARK 500    PHE I  15       -2.28     84.42                                   
REMARK 500    LYS I  77     -123.05     52.09                                   
REMARK 500    PHE J  12       44.57   -148.43                                   
REMARK 500    GLU J  13     -141.70     57.79                                   
REMARK 500    PHE J  15       -4.11     83.66                                   
REMARK 500    LYS J  77     -121.94     52.67                                   
REMARK 500    SER K  62      -81.03   -139.86                                   
REMARK 500    THR K  65     -167.44   -129.39                                   
REMARK 500    THR K  75     -168.00   -127.18                                   
REMARK 500    CYS K 172      119.49   -179.38                                   
REMARK 500    ASN K 207      -96.05   -120.34                                   
REMARK 500    MET K 212      110.72   -164.56                                   
REMARK 500    ALA K 296      130.24    -39.81                                   
REMARK 500    MET K 297       -5.44     83.48                                   
REMARK 500    VAL K 331      -50.41     70.61                                   
REMARK 500    ASP K 357       90.03   -162.98                                   
REMARK 500    THR K 406      -55.04   -121.70                                   
REMARK 500    PHE M  12       44.13   -147.96                                   
REMARK 500    GLU M  13     -142.75     57.98                                   
REMARK 500    PHE M  15        0.34     81.74                                   
REMARK 500    LYS M  77     -122.88     51.70                                   
REMARK 500    SER O  62      -80.94   -140.96                                   
REMARK 500    THR O  65     -168.11   -128.93                                   
REMARK 500    THR O  75     -169.43   -126.85                                   
REMARK 500    CYS O 172      119.57   -178.76                                   
REMARK 500    ASN O 207      -94.15   -120.15                                   
REMARK 500    MET O 212      109.53   -164.76                                   
REMARK 500    MET O 297       -6.37     84.27                                   
REMARK 500    VAL O 331      -50.67     71.09                                   
REMARK 500    ASP O 357       91.15   -163.69                                   
REMARK 500    PHE P  12       45.55   -147.50                                   
REMARK 500    GLU P  13     -141.83     57.86                                   
REMARK 500    PHE P  15        0.71     83.71                                   
REMARK 500    LYS P  77     -122.65     53.69                                   
REMARK 500    SER R  62      -81.00   -139.79                                   
REMARK 500    CYS R 172      121.67   -177.09                                   
REMARK 500    ASN R 207      -95.25   -122.76                                   
REMARK 500    MET R 212      111.20   -166.84                                   
REMARK 500    ALA R 296      130.20    -39.99                                   
REMARK 500    MET R 297       -4.26     83.22                                   
REMARK 500    VAL R 331      -49.52     69.47                                   
REMARK 500    ASP R 357       90.81   -164.97                                   
REMARK 500    PHE T  12       43.84   -148.65                                   
REMARK 500    GLU T  13     -144.55     60.04                                   
REMARK 500    PHE T  15       -0.80     83.02                                   
REMARK 500    LYS T  77     -125.21     51.99                                   
REMARK 500    SER V  62      -82.20   -141.51                                   
REMARK 500    THR V  65     -169.63   -128.68                                   
REMARK 500    THR V  75     -169.37   -129.29                                   
REMARK 500    CYS V 172      121.06   -179.71                                   
REMARK 500    ASN V 207      -94.93   -122.64                                   
REMARK 500    MET V 212      111.99   -165.24                                   
REMARK 500    ALA V 296      128.80    -38.47                                   
REMARK 500    MET V 297       -5.05     84.91                                   
REMARK 500    VAL V 331      -49.66     69.34                                   
REMARK 500    ASP V 357       91.66   -162.50                                   
REMARK 500    PHE W  12       47.28   -146.39                                   
REMARK 500    GLU W  13     -142.10     57.78                                   
REMARK 500    PHE W  15       -0.95     83.05                                   
REMARK 500    LYS W  77     -121.40     53.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 VAL C    7     ASN C    8                  -56.04                    
REMARK 500 VAL F    7     ASN F    8                  -53.62                    
REMARK 500 VAL I    7     ASN I    8                  -58.53                    
REMARK 500 VAL J    7     ASN J    8                  -56.60                    
REMARK 500 VAL M    7     ASN M    8                  -56.14                    
REMARK 500 VAL P    7     ASN P    8                  -58.09                    
REMARK 500 VAL T    7     ASN T    8                  -58.76                    
REMARK 500 VAL W    7     ASN W    8                  -57.93                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    ASN C   8        45.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN F   8        46.3      L          L   OUTSIDE RANGE           
REMARK 500    ASN I   8        45.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN J   8        45.0      L          L   OUTSIDE RANGE           
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 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 A1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP A1477   O2                                                     
REMARK 620 2 CAP A1477   O3   71.9                                              
REMARK 620 3 CAP A1477   O6   73.2  86.5                                        
REMARK 620 4 KCX A 201   OQ2  91.0  83.8 163.4                                  
REMARK 620 5 ASP A 203   OD1 102.7 174.1  94.3  94.0                            
REMARK 620 6 GLU A 204   OE1 159.3  88.4  99.6  93.5  97.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CAP B1477   O2                                                     
REMARK 620 2 CAP B1477   O6   75.3                                              
REMARK 620 3 ASP B 203   OD1 106.6  96.8                                        
REMARK 620 4 KCX B 201   OQ2  92.3 166.3  92.2                                  
REMARK 620 5 GLU B 204   OE1 158.2  97.6  94.6  91.8                            
REMARK 620 6 CAP B1477   O3   74.0  87.6 175.5  83.4  85.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG E1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX E 201   OQ2                                                    
REMARK 620 2 CAP E1477   O2   96.2                                              
REMARK 620 3 CAP E1477   O3   86.8  73.4                                        
REMARK 620 4 CAP E1477   O6  170.7  75.0  87.8                                  
REMARK 620 5 ASP E 203   OD1  93.4 104.6 178.0  91.7                            
REMARK 620 6 GLU E 204   OE1  93.4 159.5  89.2  94.1  92.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG H1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX H 201   OQ2                                                    
REMARK 620 2 ASP H 203   OD1  94.2                                              
REMARK 620 3 CAP O1478   O3   84.0 176.5                                        
REMARK 620 4 GLU H 204   OE1  91.6  98.0  85.1                                  
REMARK 620 5 CAP O1478   O2   93.1 103.6  73.5 157.4                            
REMARK 620 6 CAP O1478   O6  164.2  96.3  84.8  98.5  73.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG K1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP K 203   OD1                                                    
REMARK 620 2 CAP R1478   O2  104.4                                              
REMARK 620 3 CAP R1478   O6   94.6  75.4                                        
REMARK 620 4 KCX K 201   OQ2  92.3  94.4 168.9                                  
REMARK 620 5 GLU K 204   OE1  96.1 157.9  95.1  92.8                            
REMARK 620 6 CAP R1478   O3  177.2  74.3  87.5  85.4  85.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG O1477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU O 204   OE1                                                    
REMARK 620 2 KCX O 201   OQ2  91.0                                              
REMARK 620 3 CAP O1476   O2  158.5  94.1                                        
REMARK 620 4 CAP O1476   O3   86.2  86.2  73.3                                  
REMARK 620 5 CAP O1476   O6   97.2 168.1  75.1  85.8                            
REMARK 620 6 ASP O 203   OD1  92.3  92.3 108.4 177.8  95.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG R1477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX R 201   OQ2                                                    
REMARK 620 2 ASP R 203   OD1  94.1                                              
REMARK 620 3 GLU R 204   OE1  93.4  93.9                                        
REMARK 620 4 CAP R1476   O2   94.7 106.2 157.6                                  
REMARK 620 5 CAP R1476   O3   87.3 178.5  85.9  73.7                            
REMARK 620 6 CAP R1476   O6  168.5  94.3  93.8  75.5  84.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG V1477  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX V 201   OQ2                                                    
REMARK 620 2 ASP V 203   OD1  92.2                                              
REMARK 620 3 GLU V 204   OE1  92.6  96.7                                        
REMARK 620 4 CAP V1476   O6  165.6  97.9  96.4                                  
REMARK 620 5 CAP V1476   O2   91.8 103.0 159.6  75.9                            
REMARK 620 6 CAP V1476   O3   82.9 174.9  85.0  86.7  75.8                      
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 A1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG B1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG E1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG H1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG K1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG O1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG R1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG V1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP A1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP B1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP E1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO E1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP O1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP O1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP R1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP R1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO T1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO T1142                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP V1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO W1141                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO W1142                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1GK8   RELATED DB: PDB                                   
REMARK 900  RUBISCO FROM CHLAMYDOMONAS REINHARDTII                              
REMARK 900 RELATED ID: 1IR2   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF ACTIVATED RIBULOSE-1,5                         
REMARK 900  -BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO) FROM                   
REMARK 900   GREEN ALGA,CHLAMYDOMONAS REINHARDTII COMPLEXED                     
REMARK 900   WITH 2-CARBOXYARABINITOL-1,5-BISPHOSPHATE (                        
REMARK 900  2-CABP)                                                             
REMARK 900 RELATED ID: 1UWA   RELATED DB: PDB                                   
REMARK 900  L290F MUTANT RUBISCO FROM CHLAMYDOMONAS                             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUE 46 IN THE LARGE SUBUNITS (CHAIN A B E H K O R V) HAS         
REMARK 999 BEEN IDENTIFIED AS A PROLINE.                                        
DBREF  1UW9 A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UW9 B    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UW9 E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UW9 H    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UW9 K    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UW9 O    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UW9 R    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UW9 V    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UW9 I    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1UW9 C    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1UW9 F    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1UW9 J    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1UW9 P    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1UW9 T    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1UW9 M    1   140  UNP    P00873   RBS1_CHLRE      46    185             
DBREF  1UW9 W    1   140  UNP    P00873   RBS1_CHLRE      46    185             
SEQADV 1UW9 PRO A   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UW9 PRO B   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UW9 PRO E   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UW9 PRO H   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UW9 PRO K   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UW9 PRO O   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UW9 PRO R   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UW9 PRO V   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UW9 SER I  128  UNP  P00873    THR   173 CONFLICT                       
SEQADV 1UW9 TRP I  132  UNP  P00873    PHE   177 CONFLICT                       
SEQADV 1UW9 SER C  128  UNP  P00873    THR   173 CONFLICT                       
SEQADV 1UW9 TRP C  132  UNP  P00873    PHE   177 CONFLICT                       
SEQADV 1UW9 SER F  128  UNP  P00873    THR   173 CONFLICT                       
SEQADV 1UW9 TRP F  132  UNP  P00873    PHE   177 CONFLICT                       
SEQADV 1UW9 SER J  128  UNP  P00873    THR   173 CONFLICT                       
SEQADV 1UW9 TRP J  132  UNP  P00873    PHE   177 CONFLICT                       
SEQADV 1UW9 SER P  128  UNP  P00873    THR   173 CONFLICT                       
SEQADV 1UW9 TRP P  132  UNP  P00873    PHE   177 CONFLICT                       
SEQADV 1UW9 SER T  128  UNP  P00873    THR   173 CONFLICT                       
SEQADV 1UW9 TRP T  132  UNP  P00873    PHE   177 CONFLICT                       
SEQADV 1UW9 SER M  128  UNP  P00873    THR   173 CONFLICT                       
SEQADV 1UW9 TRP M  132  UNP  P00873    PHE   177 CONFLICT                       
SEQADV 1UW9 SER W  128  UNP  P00873    THR   173 CONFLICT                       
SEQADV 1UW9 TRP W  132  UNP  P00873    PHE   177 CONFLICT                       
SEQADV 1UW9 THR A  222  UNP  P00877    ALA   222 ENGINEERED MUTATION            
SEQADV 1UW9 PHE A  290  UNP  P00877    LEU   290 ENGINEERED MUTATION            
SEQADV 1UW9 THR B  222  UNP  P00877    ALA   222 ENGINEERED MUTATION            
SEQADV 1UW9 PHE B  290  UNP  P00877    LEU   290 ENGINEERED MUTATION            
SEQADV 1UW9 THR E  222  UNP  P00877    ALA   222 ENGINEERED MUTATION            
SEQADV 1UW9 PHE E  290  UNP  P00877    LEU   290 ENGINEERED MUTATION            
SEQADV 1UW9 THR H  222  UNP  P00877    ALA   222 ENGINEERED MUTATION            
SEQADV 1UW9 PHE H  290  UNP  P00877    LEU   290 ENGINEERED MUTATION            
SEQADV 1UW9 THR K  222  UNP  P00877    ALA   222 ENGINEERED MUTATION            
SEQADV 1UW9 PHE K  290  UNP  P00877    LEU   290 ENGINEERED MUTATION            
SEQADV 1UW9 THR O  222  UNP  P00877    ALA   222 ENGINEERED MUTATION            
SEQADV 1UW9 PHE O  290  UNP  P00877    LEU   290 ENGINEERED MUTATION            
SEQADV 1UW9 THR R  222  UNP  P00877    ALA   222 ENGINEERED MUTATION            
SEQADV 1UW9 PHE R  290  UNP  P00877    LEU   290 ENGINEERED MUTATION            
SEQADV 1UW9 THR V  222  UNP  P00877    ALA   222 ENGINEERED MUTATION            
SEQADV 1UW9 PHE V  290  UNP  P00877    LEU   290 ENGINEERED MUTATION            
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  THR 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 PHE 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 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  THR 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 PHE 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 C  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 C  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 C  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 C  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 C  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 C  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 C  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 C  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 C  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 C  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 C  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  THR 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 PHE 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 F  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 F  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 F  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 F  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 F  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 F  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 F  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 F  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 F  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 F  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 F  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  THR 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 PHE 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 I  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 I  140  THR PHE SER TYR LEU PRO PRO LEU THR 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 ALA 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 J  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 J  140  THR PHE SER TYR LEU PRO PRO LEU THR 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 ALA 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 K  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 K  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 K  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 K  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 K  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 K  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 K  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 K  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 K  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 K  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 K  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 K  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 K  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 K  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 K  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 K  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 K  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 K  475  THR GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 K  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 K  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 K  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 K  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 K  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 K  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 K  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 K  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 K  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 K  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 K  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 K  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 K  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 K  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 K  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 K  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 K  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 K  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 K  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 M  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 M  140  THR PHE SER TYR LEU PRO PRO LEU THR 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 ALA 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 O  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 O  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 O  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 O  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 O  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 O  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 O  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 O  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 O  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 O  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 O  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 O  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 O  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 O  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 O  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 O  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 O  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 O  475  THR GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 O  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 O  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 O  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 O  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 O  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 O  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 O  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 O  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 O  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 O  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 O  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 O  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 O  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 O  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 O  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 O  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 O  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 O  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 O  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 P  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 P  140  THR PHE SER TYR LEU PRO PRO LEU THR 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 ALA 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 R  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 R  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 R  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 R  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 R  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 R  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 R  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 R  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 R  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 R  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 R  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 R  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 R  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 R  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 R  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 R  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 R  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 R  475  THR GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 R  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 R  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 R  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 R  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 R  475  ASN GLY LEU PHE LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 R  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 R  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 R  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 R  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 R  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 R  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 R  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 R  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 R  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 R  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 R  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 R  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 R  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 R  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 T  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 T  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 T  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 T  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 T  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 T  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 T  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 T  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 T  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 T  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 T  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  THR 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 PHE 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 W  140  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 W  140  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 W  140  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 W  140  PRO CYS LEU GLU PHE ALA GLU ALA ASP LYS ALA TYR VAL          
SEQRES   5 W  140  SER ASN GLU SER ALA ILE ARG PHE GLY SER VAL SER CYS          
SEQRES   6 W  140  LEU TYR TYR ASP ASN ARG TYR TRP THR MET TRP LYS LEU          
SEQRES   7 W  140  PRO MET PHE GLY CYS ARG ASP PRO MET GLN VAL LEU ARG          
SEQRES   8 W  140  GLU ILE VAL ALA CYS THR LYS ALA PHE PRO ASP ALA TYR          
SEQRES   9 W  140  VAL ARG LEU VAL ALA PHE ASP ASN GLN LYS GLN VAL GLN          
SEQRES  10 W  140  ILE MET GLY PHE LEU VAL GLN ARG PRO LYS SER ALA ARG          
SEQRES  11 W  140  ASP TRP GLN PRO ALA ASN LYS ARG SER VAL                      
MODRES 1UW9 HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP B  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP B  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP H  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP H  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP K  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP K  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP O  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP O  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP R  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP R  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP V  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 HYP V  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UW9 KCX A  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UW9 KCX B  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UW9 KCX E  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UW9 KCX H  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UW9 KCX K  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UW9 KCX O  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UW9 KCX R  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UW9 KCX V  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UW9 SMC A  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC A  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC B  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC B  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC E  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC E  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC H  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC H  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC K  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC K  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC O  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC O  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC R  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC R  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC V  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UW9 SMC V  369  CYS  S- METHYLCYSTEINE                                  
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    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    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    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    HYP  K 104       8                                                       
HET    HYP  K 151       8                                                       
HET    KCX  K 201      12                                                       
HET    SMC  K 256       7                                                       
HET    SMC  K 369       7                                                       
HET    HYP  O 104       8                                                       
HET    HYP  O 151       8                                                       
HET    KCX  O 201      12                                                       
HET    SMC  O 256       7                                                       
HET    SMC  O 369       7                                                       
HET    HYP  R 104       8                                                       
HET    HYP  R 151       8                                                       
HET    KCX  R 201      12                                                       
HET    SMC  R 256       7                                                       
HET    SMC  R 369       7                                                       
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     MG  A1476       1                                                       
HET     MG  B1476       1                                                       
HET     MG  E1476       1                                                       
HET     MG  H1476       1                                                       
HET     MG  K1476       1                                                       
HET     MG  O1477       1                                                       
HET     MG  R1477       1                                                       
HET     MG  V1477       1                                                       
HET    CAP  A1477      21                                                       
HET    EDO  A1478       4                                                       
HET    EDO  A1479       4                                                       
HET    EDO  A1480       4                                                       
HET    EDO  A1481       4                                                       
HET    EDO  A1482       4                                                       
HET    EDO  A1483       4                                                       
HET    CAP  B1477      21                                                       
HET    EDO  B1478       4                                                       
HET    EDO  B1479       4                                                       
HET    EDO  B1480       4                                                       
HET    EDO  B1481       4                                                       
HET    EDO  B1482       4                                                       
HET    EDO  C1141       4                                                       
HET    EDO  C1142       4                                                       
HET    CAP  E1477      21                                                       
HET    EDO  E1478       4                                                       
HET    EDO  E1479       4                                                       
HET    EDO  E1480       4                                                       
HET    EDO  E1481       4                                                       
HET    EDO  E1482       4                                                       
HET    EDO  H1477       4                                                       
HET    EDO  H1478       4                                                       
HET    EDO  H1479       4                                                       
HET    EDO  H1480       4                                                       
HET    EDO  H1481       4                                                       
HET    EDO  H1482       4                                                       
HET    EDO  I1141       4                                                       
HET    EDO  J1141       4                                                       
HET    EDO  J1142       4                                                       
HET    EDO  K1477       4                                                       
HET    EDO  K1478       4                                                       
HET    EDO  K1479       4                                                       
HET    EDO  K1480       4                                                       
HET    EDO  K1481       4                                                       
HET    EDO  M1141       4                                                       
HET    EDO  M1142       4                                                       
HET    CAP  O1476      21                                                       
HET    CAP  O1478      21                                                       
HET    EDO  O1479       4                                                       
HET    EDO  O1480       4                                                       
HET    EDO  O1481       4                                                       
HET    EDO  O1482       4                                                       
HET    EDO  O1483       4                                                       
HET    EDO  O1484       4                                                       
HET    EDO  P1141       4                                                       
HET    EDO  P1142       4                                                       
HET    CAP  R1476      21                                                       
HET    CAP  R1478      21                                                       
HET    EDO  R1479       4                                                       
HET    EDO  R1480       4                                                       
HET    EDO  R1481       4                                                       
HET    EDO  R1482       4                                                       
HET    EDO  T1141       4                                                       
HET    EDO  T1142       4                                                       
HET    CAP  V1476      21                                                       
HET    EDO  V1478       4                                                       
HET    EDO  V1479       4                                                       
HET    EDO  V1480       4                                                       
HET    EDO  V1481       4                                                       
HET    EDO  V1482       4                                                       
HET    EDO  W1141       4                                                       
HET    EDO  W1142       4                                                       
HETNAM     HYP 4-HYDROXYPROLINE                                                 
HETNAM     KCX LYSINE NZ-CARBOXYLIC ACID                                        
HETNAM     SMC S-METHYLCYSTEINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     CAP 2-CARBOXYARABINITOL-1,5-DIPHOSPHATE                              
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  HYP    16(C5 H9 N O3)                                               
FORMUL   1  KCX    8(C7 H14 N2 O4)                                              
FORMUL   1  SMC    16(C4 H9 N O2 S)                                             
FORMUL  17   MG    8(MG 2+)                                                     
FORMUL  25  CAP    8(C6 H14 O13 P2)                                             
FORMUL  26  EDO    55(C2 H6 O2)                                                 
FORMUL  88  HOH   *2819(H2 O1)                                                  
HELIX    1   1 TYR A   20  TYR A   25  1                                   6    
HELIX    2   2 PRO A   49  SER A   61  1                                  13    
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  GLY A  126  5                                   4    
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  288  1                                  20    
HELIX   14  14 MET A  297  ARG A  303  1                                   7    
HELIX   15  15 HIS A  310  GLY A  322  1                                  13    
HELIX   16  16 GLU A  338  ASP A  351  1                                  14    
HELIX   17  17 ARG A  358  GLY A  361  5                                   4    
HELIX   18  18 HIS A  383  TRP A  385  5                                   3    
HELIX   19  19 HIS A  386  GLY A  395  1                                  10    
HELIX   20  20 GLY A  403  GLY A  408  1                                   6    
HELIX   21  21 GLY A  412  GLU A  433  1                                  22    
HELIX   22  22 ASP A  436  LYS A  450  1                                  15    
HELIX   23  23 SER A  452  LYS A  463  1                                  12    
HELIX   24  24 TYR B   20  TYR B   25  1                                   6    
HELIX   25  25 PRO B   49  SER B   61  1                                  13    
HELIX   26  26 VAL B   69  THR B   75  5                                   7    
HELIX   27  27 SER B   76  LYS B   81  1                                   6    
HELIX   28  28 HYP B  104  PHE B  108  5                                   5    
HELIX   29  29 SER B  112  GLY B  122  1                                  11    
HELIX   30  30 ASN B  123  GLY B  126  5                                   4    
HELIX   31  31 PRO B  141  LYS B  146  1                                   6    
HELIX   32  32 GLY B  154  ASN B  163  1                                  10    
HELIX   33  33 SER B  181  GLY B  195  1                                  15    
HELIX   34  34 ARG B  213  GLY B  233  1                                  21    
HELIX   35  35 THR B  246  GLY B  261  1                                  16    
HELIX   36  36 TYR B  269  GLY B  288  1                                  20    
HELIX   37  37 MET B  297  ARG B  303  1                                   7    
HELIX   38  38 HIS B  310  GLY B  322  1                                  13    
HELIX   39  39 GLU B  338  ASP B  351  1                                  14    
HELIX   40  40 ARG B  358  GLY B  361  5                                   4    
HELIX   41  41 HIS B  383  TRP B  385  5                                   3    
HELIX   42  42 HIS B  386  GLY B  395  1                                  10    
HELIX   43  43 GLY B  403  GLY B  408  1                                   6    
HELIX   44  44 GLY B  412  GLU B  433  1                                  22    
HELIX   45  45 ASP B  436  LYS B  450  1                                  15    
HELIX   46  46 SER B  452  LYS B  463  1                                  12    
HELIX   47  47 THR C   22  ASN C   36  1                                  15    
HELIX   48  48 GLU C   46  ALA C   50  5                                   5    
HELIX   49  49 ASN C   54  PHE C   60  5                                   7    
HELIX   50  50 ASP C   85  PHE C  100  1                                  16    
HELIX   51  51 PRO C  134  ARG C  138  5                                   5    
HELIX   52  52 TYR E   20  TYR E   25  1                                   6    
HELIX   53  53 PRO E   49  SER E   61  1                                  13    
HELIX   54  54 VAL E   69  THR E   75  5                                   7    
HELIX   55  55 SER E   76  LYS E   81  1                                   6    
HELIX   56  56 HYP E  104  PHE E  108  5                                   5    
HELIX   57  57 SER E  112  GLY E  122  1                                  11    
HELIX   58  58 ASN E  123  GLY E  126  5                                   4    
HELIX   59  59 PRO E  141  LYS E  146  1                                   6    
HELIX   60  60 GLY E  154  ASN E  163  1                                  10    
HELIX   61  61 SER E  181  GLY E  195  1                                  15    
HELIX   62  62 ARG E  213  GLY E  233  1                                  21    
HELIX   63  63 THR E  246  GLY E  261  1                                  16    
HELIX   64  64 TYR E  269  GLY E  288  1                                  20    
HELIX   65  65 MET E  297  ARG E  303  1                                   7    
HELIX   66  66 HIS E  310  GLY E  322  1                                  13    
HELIX   67  67 GLU E  338  ASP E  351  1                                  14    
HELIX   68  68 ARG E  358  GLY E  361  5                                   4    
HELIX   69  69 HIS E  383  TRP E  385  5                                   3    
HELIX   70  70 HIS E  386  GLY E  395  1                                  10    
HELIX   71  71 GLY E  403  GLY E  408  1                                   6    
HELIX   72  72 GLY E  412  GLU E  433  1                                  22    
HELIX   73  73 ASP E  436  LYS E  450  1                                  15    
HELIX   74  74 SER E  452  LYS E  463  1                                  12    
HELIX   75  75 THR F   22  ASN F   36  1                                  15    
HELIX   76  76 GLU F   46  ALA F   50  5                                   5    
HELIX   77  77 ASN F   54  PHE F   60  5                                   7    
HELIX   78  78 ASP F   85  PHE F  100  1                                  16    
HELIX   79  79 PRO F  134  ARG F  138  5                                   5    
HELIX   80  80 TYR H   20  TYR H   25  1                                   6    
HELIX   81  81 PRO H   49  SER H   61  1                                  13    
HELIX   82  82 VAL H   69  THR H   75  5                                   7    
HELIX   83  83 SER H   76  LYS H   81  1                                   6    
HELIX   84  84 HYP H  104  PHE H  108  5                                   5    
HELIX   85  85 SER H  112  GLY H  122  1                                  11    
HELIX   86  86 ASN H  123  GLY H  126  5                                   4    
HELIX   87  87 PRO H  141  LYS H  146  1                                   6    
HELIX   88  88 GLY H  154  ASN H  163  1                                  10    
HELIX   89  89 SER H  181  GLY H  195  1                                  15    
HELIX   90  90 ARG H  213  GLY H  233  1                                  21    
HELIX   91  91 THR H  246  GLY H  261  1                                  16    
HELIX   92  92 TYR H  269  GLY H  288  1                                  20    
HELIX   93  93 MET H  297  ARG H  303  1                                   7    
HELIX   94  94 HIS H  310  GLY H  322  1                                  13    
HELIX   95  95 GLU H  338  ASP H  351  1                                  14    
HELIX   96  96 ARG H  358  GLY H  361  5                                   4    
HELIX   97  97 HIS H  383  TRP H  385  5                                   3    
HELIX   98  98 HIS H  386  GLY H  395  1                                  10    
HELIX   99  99 GLY H  403  GLY H  408  1                                   6    
HELIX  100 100 GLY H  412  GLU H  433  1                                  22    
HELIX  101 101 ASP H  436  LYS H  450  1                                  15    
HELIX  102 102 SER H  452  LYS H  463  1                                  12    
HELIX  103 103 THR I   22  ASN I   36  1                                  15    
HELIX  104 104 GLU I   46  ALA I   50  5                                   5    
HELIX  105 105 ASN I   54  PHE I   60  5                                   7    
HELIX  106 106 ASP I   85  PHE I  100  1                                  16    
HELIX  107 107 PRO I  134  ARG I  138  5                                   5    
HELIX  108 108 THR J   22  ASN J   36  1                                  15    
HELIX  109 109 GLU J   46  ALA J   50  5                                   5    
HELIX  110 110 ASN J   54  PHE J   60  5                                   7    
HELIX  111 111 ASP J   85  PHE J  100  1                                  16    
HELIX  112 112 PRO J  134  ARG J  138  5                                   5    
HELIX  113 113 TYR K   20  TYR K   25  1                                   6    
HELIX  114 114 PRO K   49  SER K   61  1                                  13    
HELIX  115 115 VAL K   69  THR K   75  5                                   7    
HELIX  116 116 SER K   76  LYS K   81  1                                   6    
HELIX  117 117 HYP K  104  PHE K  108  5                                   5    
HELIX  118 118 SER K  112  GLY K  122  1                                  11    
HELIX  119 119 ASN K  123  GLY K  126  5                                   4    
HELIX  120 120 PRO K  141  LYS K  146  1                                   6    
HELIX  121 121 GLY K  154  ASN K  163  1                                  10    
HELIX  122 122 SER K  181  GLY K  195  1                                  15    
HELIX  123 123 ARG K  213  GLY K  233  1                                  21    
HELIX  124 124 THR K  246  GLY K  261  1                                  16    
HELIX  125 125 TYR K  269  GLY K  288  1                                  20    
HELIX  126 126 MET K  297  ARG K  303  1                                   7    
HELIX  127 127 HIS K  310  GLY K  322  1                                  13    
HELIX  128 128 GLU K  338  ASP K  351  1                                  14    
HELIX  129 129 ARG K  358  GLY K  361  5                                   4    
HELIX  130 130 HIS K  383  TRP K  385  5                                   3    
HELIX  131 131 HIS K  386  GLY K  395  1                                  10    
HELIX  132 132 GLY K  403  GLY K  408  1                                   6    
HELIX  133 133 GLY K  412  GLU K  433  1                                  22    
HELIX  134 134 ASP K  436  LYS K  450  1                                  15    
HELIX  135 135 SER K  452  LYS K  463  1                                  12    
HELIX  136 136 THR M   22  ASN M   36  1                                  15    
HELIX  137 137 GLU M   46  ALA M   50  5                                   5    
HELIX  138 138 ASN M   54  PHE M   60  5                                   7    
HELIX  139 139 ASP M   85  PHE M  100  1                                  16    
HELIX  140 140 PRO M  134  ARG M  138  5                                   5    
HELIX  141 141 TYR O   20  TYR O   25  1                                   6    
HELIX  142 142 PRO O   49  SER O   61  1                                  13    
HELIX  143 143 VAL O   69  THR O   75  5                                   7    
HELIX  144 144 SER O   76  LYS O   81  1                                   6    
HELIX  145 145 HYP O  104  PHE O  108  5                                   5    
HELIX  146 146 SER O  112  GLY O  122  1                                  11    
HELIX  147 147 ASN O  123  GLY O  126  5                                   4    
HELIX  148 148 PRO O  141  LYS O  146  1                                   6    
HELIX  149 149 GLY O  154  ASN O  163  1                                  10    
HELIX  150 150 SER O  181  GLY O  195  1                                  15    
HELIX  151 151 ARG O  213  GLY O  233  1                                  21    
HELIX  152 152 THR O  246  GLY O  261  1                                  16    
HELIX  153 153 TYR O  269  GLY O  288  1                                  20    
HELIX  154 154 MET O  297  ARG O  303  1                                   7    
HELIX  155 155 HIS O  310  GLY O  322  1                                  13    
HELIX  156 156 GLU O  338  ASP O  351  1                                  14    
HELIX  157 157 ARG O  358  GLY O  361  5                                   4    
HELIX  158 158 HIS O  383  TRP O  385  5                                   3    
HELIX  159 159 HIS O  386  GLY O  395  1                                  10    
HELIX  160 160 GLY O  403  GLY O  408  1                                   6    
HELIX  161 161 GLY O  412  GLU O  433  1                                  22    
HELIX  162 162 ASP O  436  LYS O  450  1                                  15    
HELIX  163 163 SER O  452  LYS O  463  1                                  12    
HELIX  164 164 THR P   22  ASN P   36  1                                  15    
HELIX  165 165 GLU P   46  ALA P   50  5                                   5    
HELIX  166 166 ASN P   54  PHE P   60  5                                   7    
HELIX  167 167 ASP P   85  PHE P  100  1                                  16    
HELIX  168 168 PRO P  134  ARG P  138  5                                   5    
HELIX  169 169 TYR R   20  TYR R   25  1                                   6    
HELIX  170 170 PRO R   49  SER R   61  1                                  13    
HELIX  171 171 VAL R   69  THR R   75  5                                   7    
HELIX  172 172 SER R   76  LYS R   81  1                                   6    
HELIX  173 173 HYP R  104  PHE R  108  5                                   5    
HELIX  174 174 SER R  112  GLY R  122  1                                  11    
HELIX  175 175 ASN R  123  GLY R  126  5                                   4    
HELIX  176 176 PRO R  141  LYS R  146  1                                   6    
HELIX  177 177 GLY R  154  ASN R  163  1                                  10    
HELIX  178 178 SER R  181  GLY R  195  1                                  15    
HELIX  179 179 ARG R  213  GLY R  233  1                                  21    
HELIX  180 180 THR R  246  GLY R  261  1                                  16    
HELIX  181 181 TYR R  269  GLY R  288  1                                  20    
HELIX  182 182 MET R  297  ARG R  303  1                                   7    
HELIX  183 183 HIS R  310  GLY R  322  1                                  13    
HELIX  184 184 GLU R  338  ASP R  351  1                                  14    
HELIX  185 185 ARG R  358  GLY R  361  5                                   4    
HELIX  186 186 HIS R  383  TRP R  385  5                                   3    
HELIX  187 187 HIS R  386  GLY R  395  1                                  10    
HELIX  188 188 GLY R  403  GLY R  408  1                                   6    
HELIX  189 189 GLY R  412  GLU R  433  1                                  22    
HELIX  190 190 ASP R  436  LYS R  450  1                                  15    
HELIX  191 191 SER R  452  LYS R  463  1                                  12    
HELIX  192 192 THR T   22  ASN T   36  1                                  15    
HELIX  193 193 GLU T   46  ALA T   50  5                                   5    
HELIX  194 194 ASN T   54  PHE T   60  5                                   7    
HELIX  195 195 ASP T   85  PHE T  100  1                                  16    
HELIX  196 196 PRO T  134  ARG T  138  5                                   5    
HELIX  197 197 TYR V   20  TYR V   25  1                                   6    
HELIX  198 198 PRO V   49  SER V   61  1                                  13    
HELIX  199 199 VAL V   69  THR V   75  5                                   7    
HELIX  200 200 SER V   76  LYS V   81  1                                   6    
HELIX  201 201 HYP V  104  PHE V  108  5                                   5    
HELIX  202 202 SER V  112  GLY V  122  1                                  11    
HELIX  203 203 ASN V  123  GLY V  126  5                                   4    
HELIX  204 204 PRO V  141  LYS V  146  1                                   6    
HELIX  205 205 GLY V  154  ASN V  163  1                                  10    
HELIX  206 206 SER V  181  GLY V  195  1                                  15    
HELIX  207 207 ARG V  213  GLY V  233  1                                  21    
HELIX  208 208 THR V  246  GLY V  261  1                                  16    
HELIX  209 209 TYR V  269  GLY V  288  1                                  20    
HELIX  210 210 MET V  297  ARG V  303  1                                   7    
HELIX  211 211 HIS V  310  GLY V  322  1                                  13    
HELIX  212 212 GLU V  338  ASP V  351  1                                  14    
HELIX  213 213 ARG V  358  GLY V  361  5                                   4    
HELIX  214 214 HIS V  383  TRP V  385  5                                   3    
HELIX  215 215 HIS V  386  GLY V  395  1                                  10    
HELIX  216 216 GLY V  403  GLY V  408  1                                   6    
HELIX  217 217 GLY V  412  GLU V  433  1                                  22    
HELIX  218 218 ASP V  436  LYS V  450  1                                  15    
HELIX  219 219 SER V  452  LYS V  463  1                                  12    
HELIX  220 220 THR W   22  ASN W   36  1                                  15    
HELIX  221 221 GLU W   46  ALA W   50  5                                   5    
HELIX  222 222 ASN W   54  PHE W   60  5                                   7    
HELIX  223 223 ASP W   85  PHE W  100  1                                  16    
HELIX  224 224 PRO W  134  ARG W  138  5                                   5    
SHEET    1  AA 5 ARG A  83  PRO A  89  0                                        
SHEET    2  AA 5 TYR A  97  TYR A 103 -1  O  ILE A  98   N  GLU A  88           
SHEET    3  AA 5 ILE A  36  PRO A  44 -1  O  ILE A  36   N  TYR A 103           
SHEET    4  AA 5 LEU A 130  ARG A 139 -1  N  ARG A 131   O  THR A  43           
SHEET    5  AA 5 GLY A 308  ILE A 309  1  O  GLY A 308   N  LEU A 135           
SHEET    1  AB 7 LEU A 169  GLY A 171  0                                        
SHEET    2  AB 7 CYS A 399  GLN A 401  1  O  LEU A 400   N  GLY A 171           
SHEET    3  AB 7 MET A 375  SER A 379  1  O  PRO A 376   N  CYS A 399           
SHEET    4  AB 7 HIS A 325  HIS A 327  1  O  LEU A 326   N  VAL A 377           
SHEET    5  AB 7 PHE A 290  HIS A 294  1  O  ILE A 293   N  HIS A 327           
SHEET    6  AB 7 ILE A 264  ASP A 268  1  O  ILE A 265   N  HIS A 292           
SHEET    7  AB 7 LEU A 240  ASN A 241  1  O  LEU A 240   N  MET A 266           
SHEET    1  AC 2 PHE A 199  THR A 200  0                                        
SHEET    2  AC 2 GLY A 237  HIS A 238  1  O  GLY A 237   N  THR A 200           
SHEET    1  AD 2 TYR A 353  VAL A 354  0                                        
SHEET    2  AD 2 GLN A 366  ASP A 367 -1  O  GLN A 366   N  VAL A 354           
SHEET    1  BA 5 ARG B  83  PRO B  89  0                                        
SHEET    2  BA 5 TYR B  97  TYR B 103 -1  O  ILE B  98   N  GLU B  88           
SHEET    3  BA 5 ILE B  36  PRO B  44 -1  O  ILE B  36   N  TYR B 103           
SHEET    4  BA 5 LEU B 130  ARG B 139 -1  N  ARG B 131   O  THR B  43           
SHEET    5  BA 5 GLY B 308  ILE B 309  1  O  GLY B 308   N  LEU B 135           
SHEET    1  BB 7 LEU B 169  GLY B 171  0                                        
SHEET    2  BB 7 CYS B 399  GLN B 401  1  O  LEU B 400   N  GLY B 171           
SHEET    3  BB 7 MET B 375  SER B 379  1  O  PRO B 376   N  CYS B 399           
SHEET    4  BB 7 HIS B 325  HIS B 327  1  O  LEU B 326   N  VAL B 377           
SHEET    5  BB 7 PHE B 290  HIS B 294  1  O  ILE B 293   N  HIS B 327           
SHEET    6  BB 7 ILE B 264  ASP B 268  1  O  ILE B 265   N  HIS B 292           
SHEET    7  BB 7 LEU B 240  ASN B 241  1  O  LEU B 240   N  MET B 266           
SHEET    1  BC 2 PHE B 199  THR B 200  0                                        
SHEET    2  BC 2 GLY B 237  HIS B 238  1  O  GLY B 237   N  THR B 200           
SHEET    1  BD 2 TYR B 353  VAL B 354  0                                        
SHEET    2  BD 2 GLN B 366  ASP B 367 -1  O  GLN B 366   N  VAL B 354           
SHEET    1  CA 4 THR C  74  TRP C  76  0                                        
SHEET    2  CA 4 ILE C  39  ALA C  45 -1  O  LEU C  42   N  TRP C  76           
SHEET    3  CA 4 TYR C 104  ASP C 111 -1  O  TYR C 104   N  ALA C  45           
SHEET    4  CA 4 VAL C 116  GLN C 124 -1  O  VAL C 116   N  ASP C 111           
SHEET    1  EA 5 ARG E  83  PRO E  89  0                                        
SHEET    2  EA 5 TYR E  97  TYR E 103 -1  O  ILE E  98   N  GLU E  88           
SHEET    3  EA 5 ILE E  36  PRO E  44 -1  O  ILE E  36   N  TYR E 103           
SHEET    4  EA 5 LEU E 130  ARG E 139 -1  N  ARG E 131   O  THR E  43           
SHEET    5  EA 5 GLY E 308  ILE E 309  1  O  GLY E 308   N  LEU E 135           
SHEET    1  EB 7 LEU E 169  GLY E 171  0                                        
SHEET    2  EB 7 CYS E 399  GLN E 401  1  O  LEU E 400   N  GLY E 171           
SHEET    3  EB 7 MET E 375  SER E 379  1  O  PRO E 376   N  CYS E 399           
SHEET    4  EB 7 HIS E 325  HIS E 327  1  O  LEU E 326   N  VAL E 377           
SHEET    5  EB 7 PHE E 290  HIS E 294  1  O  ILE E 293   N  HIS E 327           
SHEET    6  EB 7 ILE E 264  ASP E 268  1  O  ILE E 265   N  HIS E 292           
SHEET    7  EB 7 LEU E 240  ASN E 241  1  O  LEU E 240   N  MET E 266           
SHEET    1  EC 2 PHE E 199  THR E 200  0                                        
SHEET    2  EC 2 GLY E 237  HIS E 238  1  O  GLY E 237   N  THR E 200           
SHEET    1  ED 2 TYR E 353  VAL E 354  0                                        
SHEET    2  ED 2 GLN E 366  ASP E 367 -1  O  GLN E 366   N  VAL E 354           
SHEET    1  FA 4 THR F  74  TRP F  76  0                                        
SHEET    2  FA 4 ILE F  39  ALA F  45 -1  O  LEU F  42   N  TRP F  76           
SHEET    3  FA 4 TYR F 104  ASP F 111 -1  O  TYR F 104   N  ALA F  45           
SHEET    4  FA 4 VAL F 116  GLN F 124 -1  O  VAL F 116   N  ASP F 111           
SHEET    1  HA 5 ARG H  83  PRO H  89  0                                        
SHEET    2  HA 5 TYR H  97  TYR H 103 -1  O  ILE H  98   N  GLU H  88           
SHEET    3  HA 5 ILE H  36  PRO H  44 -1  O  ILE H  36   N  TYR H 103           
SHEET    4  HA 5 LEU H 130  ARG H 139 -1  N  ARG H 131   O  THR H  43           
SHEET    5  HA 5 GLY H 308  ILE H 309  1  O  GLY H 308   N  LEU H 135           
SHEET    1  HB 7 LEU H 169  GLY H 171  0                                        
SHEET    2  HB 7 CYS H 399  GLN H 401  1  O  LEU H 400   N  GLY H 171           
SHEET    3  HB 7 MET H 375  SER H 379  1  O  PRO H 376   N  CYS H 399           
SHEET    4  HB 7 HIS H 325  HIS H 327  1  O  LEU H 326   N  VAL H 377           
SHEET    5  HB 7 PHE H 290  HIS H 294  1  O  ILE H 293   N  HIS H 327           
SHEET    6  HB 7 ILE H 264  ASP H 268  1  O  ILE H 265   N  HIS H 292           
SHEET    7  HB 7 LEU H 240  ASN H 241  1  O  LEU H 240   N  MET H 266           
SHEET    1  HC 2 PHE H 199  THR H 200  0                                        
SHEET    2  HC 2 GLY H 237  HIS H 238  1  O  GLY H 237   N  THR H 200           
SHEET    1  HD 2 TYR H 353  VAL H 354  0                                        
SHEET    2  HD 2 GLN H 366  ASP H 367 -1  O  GLN H 366   N  VAL H 354           
SHEET    1  IA 4 THR I  74  TRP I  76  0                                        
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  76           
SHEET    3  IA 4 TYR I 104  ASP I 111 -1  O  TYR I 104   N  ALA I  45           
SHEET    4  IA 4 VAL I 116  GLN I 124 -1  O  VAL I 116   N  ASP I 111           
SHEET    1  JA 4 THR J  74  TRP J  76  0                                        
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  76           
SHEET    3  JA 4 TYR J 104  ASP J 111 -1  O  TYR J 104   N  ALA J  45           
SHEET    4  JA 4 VAL J 116  GLN J 124 -1  O  VAL J 116   N  ASP J 111           
SHEET    1  KA 5 ARG K  83  PRO K  89  0                                        
SHEET    2  KA 5 TYR K  97  TYR K 103 -1  O  ILE K  98   N  GLU K  88           
SHEET    3  KA 5 ILE K  36  PRO K  44 -1  O  ILE K  36   N  TYR K 103           
SHEET    4  KA 5 LEU K 130  ARG K 139 -1  N  ARG K 131   O  THR K  43           
SHEET    5  KA 5 GLY K 308  ILE K 309  1  O  GLY K 308   N  LEU K 135           
SHEET    1  KB 7 LEU K 169  GLY K 171  0                                        
SHEET    2  KB 7 CYS K 399  GLN K 401  1  O  LEU K 400   N  GLY K 171           
SHEET    3  KB 7 MET K 375  SER K 379  1  O  PRO K 376   N  CYS K 399           
SHEET    4  KB 7 HIS K 325  HIS K 327  1  O  LEU K 326   N  VAL K 377           
SHEET    5  KB 7 PHE K 290  HIS K 294  1  O  ILE K 293   N  HIS K 327           
SHEET    6  KB 7 ILE K 264  ASP K 268  1  O  ILE K 265   N  HIS K 292           
SHEET    7  KB 7 LEU K 240  ASN K 241  1  O  LEU K 240   N  MET K 266           
SHEET    1  KC 2 PHE K 199  THR K 200  0                                        
SHEET    2  KC 2 GLY K 237  HIS K 238  1  O  GLY K 237   N  THR K 200           
SHEET    1  KD 2 TYR K 353  VAL K 354  0                                        
SHEET    2  KD 2 GLN K 366  ASP K 367 -1  O  GLN K 366   N  VAL K 354           
SHEET    1  MA 4 THR M  74  TRP M  76  0                                        
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  76           
SHEET    3  MA 4 TYR M 104  ASP M 111 -1  O  TYR M 104   N  ALA M  45           
SHEET    4  MA 4 VAL M 116  GLN M 124 -1  O  VAL M 116   N  ASP M 111           
SHEET    1  OA 5 ARG O  83  PRO O  89  0                                        
SHEET    2  OA 5 TYR O  97  TYR O 103 -1  O  ILE O  98   N  GLU O  88           
SHEET    3  OA 5 ILE O  36  PRO O  44 -1  O  ILE O  36   N  TYR O 103           
SHEET    4  OA 5 LEU O 130  ARG O 139 -1  N  ARG O 131   O  THR O  43           
SHEET    5  OA 5 GLY O 308  ILE O 309  1  O  GLY O 308   N  LEU O 135           
SHEET    1  OB 7 LEU O 169  GLY O 171  0                                        
SHEET    2  OB 7 CYS O 399  GLN O 401  1  O  LEU O 400   N  GLY O 171           
SHEET    3  OB 7 MET O 375  SER O 379  1  O  PRO O 376   N  CYS O 399           
SHEET    4  OB 7 HIS O 325  HIS O 327  1  O  LEU O 326   N  VAL O 377           
SHEET    5  OB 7 PHE O 290  HIS O 294  1  O  ILE O 293   N  HIS O 327           
SHEET    6  OB 7 ILE O 264  ASP O 268  1  O  ILE O 265   N  HIS O 292           
SHEET    7  OB 7 LEU O 240  ASN O 241  1  O  LEU O 240   N  MET O 266           
SHEET    1  OC 2 PHE O 199  THR O 200  0                                        
SHEET    2  OC 2 GLY O 237  HIS O 238  1  O  GLY O 237   N  THR O 200           
SHEET    1  OD 2 TYR O 353  VAL O 354  0                                        
SHEET    2  OD 2 GLN O 366  ASP O 367 -1  O  GLN O 366   N  VAL O 354           
SHEET    1  PA 4 THR P  74  TRP P  76  0                                        
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  76           
SHEET    3  PA 4 TYR P 104  ASP P 111 -1  O  TYR P 104   N  ALA P  45           
SHEET    4  PA 4 VAL P 116  GLN P 124 -1  O  VAL P 116   N  ASP P 111           
SHEET    1  RA 5 ARG R  83  PRO R  89  0                                        
SHEET    2  RA 5 TYR R  97  TYR R 103 -1  O  ILE R  98   N  GLU R  88           
SHEET    3  RA 5 ILE R  36  PRO R  44 -1  O  ILE R  36   N  TYR R 103           
SHEET    4  RA 5 LEU R 130  ARG R 139 -1  N  ARG R 131   O  THR R  43           
SHEET    5  RA 5 GLY R 308  ILE R 309  1  O  GLY R 308   N  LEU R 135           
SHEET    1  RB 7 LEU R 169  GLY R 171  0                                        
SHEET    2  RB 7 CYS R 399  GLN R 401  1  O  LEU R 400   N  GLY R 171           
SHEET    3  RB 7 MET R 375  SER R 379  1  O  PRO R 376   N  CYS R 399           
SHEET    4  RB 7 HIS R 325  HIS R 327  1  O  LEU R 326   N  VAL R 377           
SHEET    5  RB 7 PHE R 290  HIS R 294  1  O  ILE R 293   N  HIS R 327           
SHEET    6  RB 7 ILE R 264  ASP R 268  1  O  ILE R 265   N  HIS R 292           
SHEET    7  RB 7 LEU R 240  ASN R 241  1  O  LEU R 240   N  MET R 266           
SHEET    1  RC 2 PHE R 199  THR R 200  0                                        
SHEET    2  RC 2 GLY R 237  HIS R 238  1  O  GLY R 237   N  THR R 200           
SHEET    1  RD 2 TYR R 353  VAL R 354  0                                        
SHEET    2  RD 2 GLN R 366  ASP R 367 -1  O  GLN R 366   N  VAL R 354           
SHEET    1  TA 4 THR T  74  TRP T  76  0                                        
SHEET    2  TA 4 ILE T  39  ALA T  45 -1  O  LEU T  42   N  TRP T  76           
SHEET    3  TA 4 TYR T 104  ASP T 111 -1  O  TYR T 104   N  ALA T  45           
SHEET    4  TA 4 VAL T 116  GLN T 124 -1  O  VAL T 116   N  ASP T 111           
SHEET    1  VA 5 ARG V  83  PRO V  89  0                                        
SHEET    2  VA 5 TYR V  97  TYR V 103 -1  O  ILE V  98   N  GLU V  88           
SHEET    3  VA 5 ILE V  36  PRO V  44 -1  O  ILE V  36   N  TYR V 103           
SHEET    4  VA 5 LEU V 130  ARG V 139 -1  N  ARG V 131   O  THR V  43           
SHEET    5  VA 5 GLY V 308  ILE V 309  1  O  GLY V 308   N  LEU V 135           
SHEET    1  VB 7 LEU V 169  GLY V 171  0                                        
SHEET    2  VB 7 CYS V 399  GLN V 401  1  O  LEU V 400   N  GLY V 171           
SHEET    3  VB 7 MET V 375  SER V 379  1  O  PRO V 376   N  CYS V 399           
SHEET    4  VB 7 HIS V 325  HIS V 327  1  O  LEU V 326   N  VAL V 377           
SHEET    5  VB 7 PHE V 290  HIS V 294  1  O  ILE V 293   N  HIS V 327           
SHEET    6  VB 7 ILE V 264  ASP V 268  1  O  ILE V 265   N  HIS V 292           
SHEET    7  VB 7 LEU V 240  ASN V 241  1  O  LEU V 240   N  MET V 266           
SHEET    1  VC 2 PHE V 199  THR V 200  0                                        
SHEET    2  VC 2 GLY V 237  HIS V 238  1  O  GLY V 237   N  THR V 200           
SHEET    1  VD 2 TYR V 353  VAL V 354  0                                        
SHEET    2  VD 2 GLN V 366  ASP V 367 -1  O  GLN V 366   N  VAL V 354           
SHEET    1  WA 4 THR W  74  TRP W  76  0                                        
SHEET    2  WA 4 ILE W  39  ALA W  45 -1  O  LEU W  42   N  TRP W  76           
SHEET    3  WA 4 TYR W 104  ASP W 111 -1  O  TYR W 104   N  ALA W  45           
SHEET    4  WA 4 VAL W 116  GLN W 124 -1  O  VAL W 116   N  ASP W 111           
SSBOND   1 CYS E  247    CYS K  247                          1555   1555  2.08  
SSBOND   2 CYS E  247    CYS K  247                          1555   1555  2.06  
SSBOND   3 CYS H  247    CYS R  247                          1555   1555  2.06  
SSBOND   4 CYS H  247    CYS R  247                          1555   1555  2.06  
SSBOND   5 CYS O  247    CYS V  247                          1555   1555  2.06  
SSBOND   6 CYS O  247    CYS V  247                          1555   1555  2.08  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.33  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.33  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.33  
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         OQ2 KCX A 201                MG    MG A1476     1555   1555  2.04  
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  1.34  
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.34  
LINK        MG    MG A1476                 O2  CAP A1477     1555   1555  2.28  
LINK        MG    MG A1476                 O3  CAP A1477     1555   1555  2.18  
LINK        MG    MG A1476                 O6  CAP A1477     1555   1555  2.12  
LINK        MG    MG A1476                 OD1 ASP A 203     1555   1555  1.95  
LINK        MG    MG A1476                 OE1 GLU A 204     1555   1555  1.96  
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.34  
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.33  
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.33  
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.33  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.33  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.34  
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.34  
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.33  
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.34  
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.34  
LINK        MG    MG B1476                 O6  CAP B1477     1555   1555  2.01  
LINK        MG    MG B1476                 O2  CAP B1477     1555   1555  2.25  
LINK        MG    MG B1476                 OD1 ASP B 203     1555   1555  1.95  
LINK        MG    MG B1476                 OQ2 KCX B 201     1555   1555  2.12  
LINK        MG    MG B1476                 OE1 GLU B 204     1555   1555  2.04  
LINK        MG    MG B1476                 O3  CAP B1477     1555   1555  2.18  
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.33  
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.33  
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.33  
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         OQ2 KCX E 201                MG    MG E1476     1555   1555  2.03  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.34  
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33  
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.34  
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.33  
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.34  
LINK        MG    MG E1476                 O6  CAP E1477     1555   1555  2.16  
LINK        MG    MG E1476                 OD1 ASP E 203     1555   1555  2.00  
LINK        MG    MG E1476                 OE1 GLU E 204     1555   1555  2.03  
LINK        MG    MG E1476                 O2  CAP E1477     1555   1555  2.30  
LINK        MG    MG E1476                 O3  CAP E1477     1555   1555  2.13  
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.33  
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.33  
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.33  
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.34  
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         OQ2 KCX H 201                MG    MG H1476     1555   1555  2.04  
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  1.34  
LINK         C   SMC H 369                 N   SER H 370     1555   1555  1.34  
LINK        MG    MG H1476                 OE1 GLU H 204     1555   1555  2.02  
LINK        MG    MG H1476                 OD1 ASP H 203     1555   1555  1.93  
LINK        MG    MG H1476                 O6  CAP O1478     1555   1555  2.09  
LINK        MG    MG H1476                 O2  CAP O1478     1555   1555  2.38  
LINK        MG    MG H1476                 O3  CAP O1478     1555   1555  2.15  
LINK         C   TYR K 103                 N   HYP K 104     1555   1555  1.33  
LINK         C   HYP K 104                 N   ILE K 105     1555   1555  1.33  
LINK         C   GLY K 150                 N   HYP K 151     1555   1555  1.32  
LINK         C   HYP K 151                 N   PRO K 152     1555   1555  1.33  
LINK         C   THR K 200                 N   KCX K 201     1555   1555  1.33  
LINK         OQ2 KCX K 201                MG    MG K1476     1555   1555  2.04  
LINK         C   KCX K 201                 N   ASP K 202     1555   1555  1.33  
LINK         C   VAL K 255                 N   SMC K 256     1555   1555  1.33  
LINK         C   SMC K 256                 N   ALA K 257     1555   1555  1.33  
LINK         C   TRP K 368                 N   SMC K 369     1555   1555  1.34  
LINK         C   SMC K 369                 N   SER K 370     1555   1555  1.34  
LINK        MG    MG K1476                 O2  CAP R1478     1555   1555  2.34  
LINK        MG    MG K1476                 O6  CAP R1478     1555   1555  1.97  
LINK        MG    MG K1476                 OE1 GLU K 204     1555   1555  2.05  
LINK        MG    MG K1476                 OD1 ASP K 203     1555   1555  1.95  
LINK        MG    MG K1476                 O3  CAP R1478     1555   1555  2.24  
LINK         C   TYR O 103                 N   HYP O 104     1555   1555  1.34  
LINK         C   HYP O 104                 N   ILE O 105     1555   1555  1.33  
LINK         C   GLY O 150                 N   HYP O 151     1555   1555  1.33  
LINK         C   HYP O 151                 N   PRO O 152     1555   1555  1.33  
LINK         C   THR O 200                 N   KCX O 201     1555   1555  1.34  
LINK         OQ2 KCX O 201                MG    MG O1477     1555   1555  2.04  
LINK         C   KCX O 201                 N   ASP O 202     1555   1555  1.34  
LINK         C   VAL O 255                 N   SMC O 256     1555   1555  1.34  
LINK         C   SMC O 256                 N   ALA O 257     1555   1555  1.34  
LINK         C   TRP O 368                 N   SMC O 369     1555   1555  1.33  
LINK         C   SMC O 369                 N   SER O 370     1555   1555  1.34  
LINK        MG    MG O1477                 O2  CAP O1476     1555   1555  2.20  
LINK        MG    MG O1477                 OD1 ASP O 203     1555   1555  2.01  
LINK        MG    MG O1477                 O6  CAP O1476     1555   1555  2.12  
LINK        MG    MG O1477                 O3  CAP O1476     1555   1555  2.22  
LINK        MG    MG O1477                 OE1 GLU O 204     1555   1555  2.04  
LINK         C   TYR R 103                 N   HYP R 104     1555   1555  1.33  
LINK         C   HYP R 104                 N   ILE R 105     1555   1555  1.33  
LINK         C   GLY R 150                 N   HYP R 151     1555   1555  1.33  
LINK         C   HYP R 151                 N   PRO R 152     1555   1555  1.33  
LINK         C   THR R 200                 N   KCX R 201     1555   1555  1.33  
LINK         OQ2 KCX R 201                MG    MG R1477     1555   1555  2.00  
LINK         C   KCX R 201                 N   ASP R 202     1555   1555  1.34  
LINK         C   VAL R 255                 N   SMC R 256     1555   1555  1.33  
LINK         C   SMC R 256                 N   ALA R 257     1555   1555  1.33  
LINK         C   TRP R 368                 N   SMC R 369     1555   1555  1.34  
LINK         C   SMC R 369                 N   SER R 370     1555   1555  1.34  
LINK        MG    MG R1477                 O6  CAP R1476     1555   1555  2.22  
LINK        MG    MG R1477                 O3  CAP R1476     1555   1555  2.11  
LINK        MG    MG R1477                 O2  CAP R1476     1555   1555  2.25  
LINK        MG    MG R1477                 OE1 GLU R 204     1555   1555  2.05  
LINK        MG    MG R1477                 OD1 ASP R 203     1555   1555  1.94  
LINK         C   TYR V 103                 N   HYP V 104     1555   1555  1.33  
LINK         C   HYP V 104                 N   ILE V 105     1555   1555  1.33  
LINK         C   GLY V 150                 N   HYP V 151     1555   1555  1.33  
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  1.34  
LINK         C   SMC V 256                 N   ALA V 257     1555   1555  1.33  
LINK         C   TRP V 368                 N   SMC V 369     1555   1555  1.34  
LINK         C   SMC V 369                 N   SER V 370     1555   1555  1.33  
LINK        MG    MG V1477                 O6  CAP V1476     1555   1555  2.09  
LINK        MG    MG V1477                 O2  CAP V1476     1555   1555  2.26  
LINK        MG    MG V1477                 O3  CAP V1476     1555   1555  2.20  
LINK        MG    MG V1477                 OE1 GLU V 204     1555   1555  1.97  
LINK        MG    MG V1477                 OD1 ASP V 203     1555   1555  1.94  
LINK        MG    MG V1477                 OQ2 KCX V 201     1555   1555  2.07  
CISPEP   1 LYS A  175    PRO A  176          0         2.32                     
CISPEP   2 LYS B  175    PRO B  176          0         0.62                     
CISPEP   3 LYS E  175    PRO E  176          0         0.38                     
CISPEP   4 LYS H  175    PRO H  176          0        -0.22                     
CISPEP   5 LYS K  175    PRO K  176          0         1.55                     
CISPEP   6 LYS O  175    PRO O  176          0        -1.18                     
CISPEP   7 LYS R  175    PRO R  176          0        -0.96                     
CISPEP   8 LYS V  175    PRO V  176          0         2.41                     
SITE     1 AC1  5 LYS A 177  KCX A 201  ASP A 203  GLU A 204                    
SITE     2 AC1  5 CAP A1477                                                     
SITE     1 AC2  5 LYS B 177  KCX B 201  ASP B 203  GLU B 204                    
SITE     2 AC2  5 CAP B1477                                                     
SITE     1 AC3  4 KCX E 201  ASP E 203  GLU E 204  CAP E1477                    
SITE     1 AC4  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     2 AC4  5 CAP O1478                                                     
SITE     1 AC5  5 LYS K 177  KCX K 201  ASP K 203  GLU K 204                    
SITE     2 AC5  5 CAP R1478                                                     
SITE     1 AC6  4 KCX O 201  ASP O 203  GLU O 204  CAP O1476                    
SITE     1 AC7  4 KCX R 201  ASP R 203  GLU R 204  CAP R1476                    
SITE     1 AC8  5 LYS V 177  KCX V 201  ASP V 203  GLU V 204                    
SITE     2 AC8  5 CAP V1476                                                     
SITE     1 AC9 28 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 AC9 28 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 AC9 28 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 AC9 28 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 AC9 28  MG A1476  HOH A2162  HOH A2216  HOH A2217                    
SITE     6 AC9 28 HOH A2271  HOH A2272  HOH A2273  HOH A2274                    
SITE     7 AC9 28 GLU B  60  THR B  65  TRP B  66  ASN B 123                    
SITE     1 BC1  8 TYR A  24  THR A  68  VAL A  69  ASP A  72                    
SITE     2 BC1  8 EDO A1479  HOH A2042  HOH A2275  HOH A2277                    
SITE     1 BC2  8 LYS A  18  THR A  65  TRP A  66  THR A  67                    
SITE     2 BC2  8 THR A  68  EDO A1478  HOH A2276  HOH A2277                    
SITE     1 BC3  3 GLU A  52  ALA A 129  HOH B2273                               
SITE     1 BC4  4 LYS A 466  GLU A 468  PHE A 469  HOH A2278                    
SITE     1 BC5  7 PHE A 311  GLU A 336  ASP A 473  HOH A2164                    
SITE     2 BC5  7 HOH A2268  HOH A2279  HOH A2280                               
SITE     1 BC6  6 LEU A 270  HOH A2152  HOH A2281  HOH A2282                    
SITE     2 BC6  6 HOH A2283  LEU B 270                                          
SITE     1 BC7 29 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 BC7 29 HOH A2081  THR B 173  LYS B 175  LYS B 177                    
SITE     3 BC7 29 KCX B 201  ASP B 203  GLU B 204  HIS B 294                    
SITE     4 BC7 29 ARG B 295  HIS B 327  LYS B 334  LEU B 335                    
SITE     5 BC7 29 SER B 379  GLY B 380  GLY B 381  GLY B 403                    
SITE     6 BC7 29 GLY B 404   MG B1476  HOH B2105  HOH B2263                    
SITE     7 BC7 29 HOH B2264  HOH B2265  HOH B2266  HOH B2267                    
SITE     8 BC7 29 HOH B2268                                                     
SITE     1 BC8  8 TYR B  24  THR B  68  VAL B  69  ASP B  72                    
SITE     2 BC8  8 LEU B  77  HOH B2269  HOH B2270  HOH B2271                    
SITE     1 BC9  8 VAL B  17  LYS B  18  THR B  65  TRP B  66                    
SITE     2 BC9  8 THR B  67  THR B  68  HOH B2018  HOH B2271                    
SITE     1 CC1  2 HOH A2278  GLU B  52                                          
SITE     1 CC2  4 LYS B 466  GLU B 468  PHE B 469  HOH B2273                    
SITE     1 CC3  8 HIS B 298  PHE B 311  GLU B 336  ASP B 473                    
SITE     2 CC3  8 HOH B2195  HOH B2274  HOH B2275  HOH B2276                    
SITE     1 CC4  4 LYS C  49  GLU C  55  TYR V 226  LYS V 227                    
SITE     1 CC5  7 GLY C  37  TRP C  38  ILE C  39  PHE C  81                    
SITE     2 CC5  7 GLY C  82  CYS C  83  HOH C2080                               
SITE     1 CC6 29 THR E 173  LYS E 175  LYS E 177  KCX E 201                    
SITE     2 CC6 29 ASP E 203  GLU E 204  HIS E 294  ARG E 295                    
SITE     3 CC6 29 HIS E 327  LYS E 334  LEU E 335  SER E 379                    
SITE     4 CC6 29 GLY E 380  GLY E 381  GLY E 403  GLY E 404                    
SITE     5 CC6 29  MG E1476  HOH E2165  HOH E2219  HOH E2275                    
SITE     6 CC6 29 HOH E2276  HOH E2277  HOH E2278  GLU K  60                    
SITE     7 CC6 29 THR K  65  TRP K  66  ASN K 123  HOH K2028                    
SITE     8 CC6 29 HOH K2063                                                     
SITE     1 CC7  8 TYR E  24  GLY E  64  THR E  68  VAL E  69                    
SITE     2 CC7  8 ASP E  72  HOH E2039  HOH E2045  HOH E2279                    
SITE     1 CC8  9 VAL E  17  LYS E  18  TYR E  20  THR E  65                    
SITE     2 CC8  9 TRP E  66  THR E  67  THR E  68  HOH E2279                    
SITE     3 CC8  9 HOH E2280                                                     
SITE     1 CC9  2 GLU E  52  HOH K2250                                          
SITE     1 DC1  5 LYS E 466  PHE E 467  GLU E 468  PHE E 469                    
SITE     2 DC1  5 HOH E2281                                                     
SITE     1 DC2  6 LEU E 270  HOH E2282  HOH E2283  HOH E2284                    
SITE     2 DC2  6 HOH E2285  LEU K 270                                          
SITE     1 DC3  4 LEU H 270  HOH H2263  HOH H2264  LEU R 270                    
SITE     1 DC4  8 TYR H  24  THR H  68  VAL H  69  ASP H  72                    
SITE     2 DC4  8 EDO H1479  HOH H2265  HOH H2266  HOH H2267                    
SITE     1 DC5  8 LYS H  18  THR H  65  TRP H  66  THR H  67                    
SITE     2 DC5  8 THR H  68  EDO H1478  HOH H2019  HOH H2267                    
SITE     1 DC6  2 GLU H  52  HOH R2260                                          
SITE     1 DC7  5 LYS H 466  GLU H 468  PHE H 469  HOH H2268                    
SITE     2 DC7  5 HOH H2269                                                     
SITE     1 DC8  8 HIS H 298  PHE H 311  GLU H 336  ASP H 473                    
SITE     2 DC8  8 HOH H2173  HOH H2190  HOH H2270  HOH H2271                    
SITE     1 DC9  6 LYS I  49  GLU I  55  ASP I  69  HOH I2034                    
SITE     2 DC9  6 TYR K 226  LYS K 227                                          
SITE     1 EC1  7 TYR E 226  LYS E 227  HOH E2134  LYS J  49                    
SITE     2 EC1  7 GLU J  55  HOH J2038  HOH J2040                               
SITE     1 EC2  7 GLY J  37  TRP J  38  ILE J  39  PHE J  81                    
SITE     2 EC2  7 GLY J  82  CYS J  83  HOH J2074                               
SITE     1 EC3  9 TYR K  24  GLY K  64  THR K  68  VAL K  69                    
SITE     2 EC3  9 ASP K  72  LEU K  77  HOH K2036  HOH K2248                    
SITE     3 EC3  9 HOH K2249                                                     
SITE     1 EC4  7 VAL K  17  LYS K  18  TRP K  66  THR K  67                    
SITE     2 EC4  7 THR K  68  HOH K2007  HOH K2249                               
SITE     1 EC5  2 HOH E2281  GLU K  52                                          
SITE     1 EC6  5 LYS K 466  GLU K 468  PHE K 469  HOH K2250                    
SITE     2 EC6  5 HOH K2251                                                     
SITE     1 EC7  8 HIS K 298  PHE K 311  GLU K 336  ASP K 473                    
SITE     2 EC7  8 HOH K2161  HOH K2180  HOH K2252  HOH K2253                    
SITE     1 EC8  6 LYS M  49  GLU M  55  HOH M2045  HOH M2047                    
SITE     2 EC8  6 TYR O 226  HOH O2132                                          
SITE     1 EC9  3 GLY M  37  ILE M  39  GLY M  82                               
SITE     1 FC1 28 THR O 173  LYS O 175  LYS O 177  KCX O 201                    
SITE     2 FC1 28 ASP O 203  GLU O 204  HIS O 294  ARG O 295                    
SITE     3 FC1 28 HIS O 327  LYS O 334  LEU O 335  SER O 379                    
SITE     4 FC1 28 GLY O 380  GLY O 381  GLY O 403  GLY O 404                    
SITE     5 FC1 28  MG O1477  HOH O2261  HOH O2262  HOH O2263                    
SITE     6 FC1 28 HOH O2264  HOH O2265  HOH O2266  GLU V  60                    
SITE     7 FC1 28 THR V  65  TRP V  66  ASN V 123  HOH V2080                    
SITE     1 FC2 29 THR H 173  LYS H 175  LYS H 177  KCX H 201                    
SITE     2 FC2 29 ASP H 203  GLU H 204  HIS H 294  ARG H 295                    
SITE     3 FC2 29 HIS H 327  LYS H 334  LEU H 335  SER H 379                    
SITE     4 FC2 29 GLY H 380  GLY H 381  GLY H 403  GLY H 404                    
SITE     5 FC2 29  MG H1476  HOH H2215  HOH H2216  HOH O2267                    
SITE     6 FC2 29 HOH O2268  HOH O2269  HOH O2270  GLU R  60                    
SITE     7 FC2 29 THR R  65  TRP R  66  ASN R 123  HOH R2037                    
SITE     8 FC2 29 HOH R2075                                                     
SITE     1 FC3  9 TYR O  24  GLY O  64  THR O  68  VAL O  69                    
SITE     2 FC3  9 ASP O  72  LEU O  77  HOH O2039  HOH O2271                    
SITE     3 FC3  9 HOH O2272                                                     
SITE     1 FC4  7 LYS O  18  THR O  65  TRP O  66  THR O  67                    
SITE     2 FC4  7 THR O  68  HOH O2272  HOH O2273                               
SITE     1 FC5  3 GLU O  52  HOH O2007  HOH V2286                               
SITE     1 FC6  5 LYS O 466  GLU O 468  PHE O 469  HOH O2274                    
SITE     2 FC6  5 HOH O2275                                                     
SITE     1 FC7  8 ARG O 295  HIS O 298  PHE O 311  GLU O 336                    
SITE     2 FC7  8 ASP O 473  HOH O2276  HOH O2277  HOH O2278                    
SITE     1 FC8  5 LEU O 270  HOH O2279  HOH O2280  HOH O2281                    
SITE     2 FC8  5 LEU V 270                                                     
SITE     1 FC9  5 LYS P  49  GLU P  55  HOH P2024  HOH P2029                    
SITE     2 FC9  5 TYR R 226                                                     
SITE     1 GC1  6 TRP P  38  ILE P  39  GLY P  82  CYS P  83                    
SITE     2 GC1  6 HOH P2059  HOH P2060                                          
SITE     1 GC2 29 GLU H  60  THR H  65  TRP H  66  ASN H 123                    
SITE     2 GC2 29 THR R 173  LYS R 175  LYS R 177  KCX R 201                    
SITE     3 GC2 29 ASP R 203  GLU R 204  HIS R 294  ARG R 295                    
SITE     4 GC2 29 HIS R 327  LYS R 334  LEU R 335  SER R 379                    
SITE     5 GC2 29 GLY R 380  GLY R 381  GLY R 403  GLY R 404                    
SITE     6 GC2 29  MG R1477  HOH R2106  HOH R2246  HOH R2247                    
SITE     7 GC2 29 HOH R2248  HOH R2249  HOH R2250  HOH R2251                    
SITE     8 GC2 29 HOH R2252                                                     
SITE     1 GC3 29 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     2 GC3 29 HOH E2080  THR K 173  LYS K 175  LYS K 177                    
SITE     3 GC3 29 KCX K 201  ASP K 203  GLU K 204  HIS K 294                    
SITE     4 GC3 29 ARG K 295  HIS K 327  LYS K 334  LEU K 335                    
SITE     5 GC3 29 SER K 379  GLY K 380  GLY K 381  GLY K 403                    
SITE     6 GC3 29 GLY K 404   MG K1476  HOH K2094  HOH K2203                    
SITE     7 GC3 29 HOH R2253  HOH R2254  HOH R2255  HOH R2256                    
SITE     8 GC3 29 HOH R2257                                                     
SITE     1 GC4  9 TYR R  24  GLY R  64  THR R  68  VAL R  69                    
SITE     2 GC4  9 ASP R  72  LEU R  77  HOH R2040  HOH R2258                    
SITE     3 GC4  9 HOH R2259                                                     
SITE     1 GC5  9 GLY R  16  VAL R  17  LYS R  18  THR R  65                    
SITE     2 GC5  9 TRP R  66  THR R  67  THR R  68  HOH R2011                    
SITE     3 GC5  9 HOH R2259                                                     
SITE     1 GC6  2 HOH H2268  GLU R  52                                          
SITE     1 GC7  5 LYS R 466  GLU R 468  PHE R 469  HOH R2260                    
SITE     2 GC7  5 HOH R2261                                                     
SITE     1 GC8  6 TYR A 226  LYS A 227  HOH A2126  LYS T  49                    
SITE     2 GC8  6 GLU T  55  HOH T2045                                          
SITE     1 GC9  5 GLY T  37  ILE T  39  PHE T  81  GLY T  82                    
SITE     2 GC9  5 CYS T  83                                                     
SITE     1 HC1 29 GLU O  60  THR O  65  TRP O  66  ASN O 123                    
SITE     2 HC1 29 HOH O2033  HOH O2080  THR V 173  LYS V 175                    
SITE     3 HC1 29 LYS V 177  KCX V 201  ASP V 203  GLU V 204                    
SITE     4 HC1 29 HIS V 294  ARG V 295  HIS V 327  LYS V 334                    
SITE     5 HC1 29 LEU V 335  SER V 379  GLY V 380  GLY V 381                    
SITE     6 HC1 29 GLY V 403  GLY V 404   MG V1477  HOH V2277                    
SITE     7 HC1 29 HOH V2278  HOH V2279  HOH V2280  HOH V2281                    
SITE     8 HC1 29 HOH V2282                                                     
SITE     1 HC2  9 TYR V  24  GLY V  64  THR V  68  VAL V  69                    
SITE     2 HC2  9 ASP V  72  EDO V1479  HOH V2283  HOH V2284                    
SITE     3 HC2  9 HOH V2285                                                     
SITE     1 HC3  8 VAL V  17  LYS V  18  THR V  65  THR V  67                    
SITE     2 HC3  8 THR V  68  EDO V1478  HOH V2011  HOH V2285                    
SITE     1 HC4  3 HOH O2275  GLU V  52  ALA V 129                               
SITE     1 HC5  5 LYS V 466  GLU V 468  PHE V 469  HOH V2286                    
SITE     2 HC5  5 HOH V2287                                                     
SITE     1 HC6  7 HIS V 298  PHE V 311  GLU V 336  ASP V 473                    
SITE     2 HC6  7 HOH V2193  HOH V2288  HOH V2289                               
SITE     1 HC7  7 TYR H 226  LYS H 227  ALA H 230  HOH H2134                    
SITE     2 HC7  7 LYS W  49  GLU W  55  HOH W2049                               
SITE     1 HC8  4 GLY W  37  ILE W  39  GLY W  82  CYS W  83                    
CRYST1  126.073  178.196  120.463  90.00 120.35  90.00 P 1 21 1     16          
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      0.007932  0.000000  0.004644        0.00000                         
SCALE2      0.000000  0.005612  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009620        0.00000                         
MTRIX1   1 -0.379100  0.487500  0.786500        8.92600    1                    
MTRIX2   1  0.487800 -0.617100  0.617500      131.60001    1                    
MTRIX3   1  0.786400  0.617800 -0.003834      -74.52000    1                    
MTRIX1   2  0.251100  0.968000 -0.001311      -67.39000    1                    
MTRIX2   2  0.968000 -0.251100 -0.000909       87.20000    1                    
MTRIX3   2 -0.001209 -0.001041 -1.000000       17.05000    1                    
MTRIX1   3  0.376800 -0.490300 -0.785900       72.51000    1                    
MTRIX2   3 -0.474500  0.626500 -0.618400       55.41000    1                    
MTRIX3   3  0.795500  0.605900  0.003402      -73.73000    1                    
MTRIX1   4  0.372100 -0.477300  0.796100       58.03000    1                    
MTRIX2   4 -0.494100  0.624200  0.605200       45.86000    1                    
MTRIX3   4 -0.785700 -0.618600 -0.003552       91.36000    1                    
MTRIX1   5 -0.380300  0.487300  0.786100       -8.87300    1                    
MTRIX2   5  0.491000 -0.613900  0.618100      131.20000    1                    
MTRIX3   5  0.783800  0.621000 -0.005782      -74.62000    1                    
MTRIX1   6 -0.370000  0.481400 -0.794600        4.76200    1                    
MTRIX2   6  0.480600 -0.632800 -0.607200      143.60001    1                    
MTRIX3   6 -0.795100 -0.606500  0.002824       90.51000    1                    
MTRIX1   7 -0.250300 -0.968100  0.007761      130.39999    1                    
MTRIX2   7 -0.968100  0.250200 -0.012310      101.20000    1                    
MTRIX3   7  0.009977 -0.010600 -0.999900       17.61000    1                    
MTRIX1   8 -1.000000 -0.000740 -0.008347       63.23000    1                    
MTRIX2   8  0.000636 -0.999900  0.012380      188.00000    1                    
MTRIX3   8 -0.008356  0.012380  0.999900       -0.92570    1                    
MTRIX1   9  0.245100  0.969500  0.001500      -67.35000    1                    
MTRIX2   9  0.969500 -0.245100 -0.002284       86.71000    1                    
MTRIX3   9  0.000147  0.000151 -1.000000       16.84000    1                    
MTRIX1  10 -0.369400  0.485400 -0.792400        4.32600    1                    
MTRIX2  10  0.476600 -0.633100 -0.610000      143.89999    1                    
MTRIX3  10 -0.797800 -0.603000  0.002554       90.40000    1                    
MTRIX1  11  0.374100 -0.490900 -0.786800       72.63000    1                    
MTRIX2  11 -0.471600  0.629800 -0.617200       54.96000    1                    
MTRIX3  11  0.798500  0.601900  0.004126      -73.31000    1                    
MTRIX1  12  0.372800 -0.476500  0.796200       57.94000    1                    
MTRIX2  12 -0.496300  0.622600  0.605000       46.05000    1                    
MTRIX3  12 -0.784000 -0.620700 -0.004390       91.61000    1                    
MTRIX1  13 -0.241500 -0.970300  0.011580      130.39999    1                    
MTRIX2  13 -0.970400  0.241400 -0.007339      102.30000    1                    
MTRIX3  13  0.004325 -0.013010 -0.999900       18.07000    1                    
MTRIX1  14 -1.000000 -0.001236 -0.007342       63.28000    1                    
MTRIX2  14  0.001153 -0.999900  0.011290      188.00000    1                    
MTRIX3  14 -0.007356  0.011280  0.999900       -0.90520    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system