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Database: PDB
Entry: 1UZD
LinkDB: 1UZD
Original site: 1UZD 
HEADER    LYASE                                   11-MAR-04   1UZD              
TITLE     CHLAMYDOMONAS,SPINACH CHIMERIC RUBISCO                                
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 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 1,           
COMPND   9  RIBULOSE BISPHOSPHATE CARBOXYLASE SMALL CHAIN 2;                    
COMPND  10 CHAIN: I, C, F, J, P, T, M, W;                                       
COMPND  11 SYNONYM: RUBISCO SMALL SUBUNIT 1,CHLOROPLAST, RUBISCO                
COMPND  12  SMALL SUBUNIT 2,OXYGENASE, RIBULOSE-1,5 BISPHOSPHATE                
COMPND  13  CARBOXYLASE/OXYGENASE;                                              
COMPND  14 EC: 4.1.1.39;                                                        
COMPND  15 OTHER_DETAILS: ONE LOOP OF CHLAMYDOMONAS RUBISCO, RESIDUES           
COMPND  16  GLU46-ASN70 HAS BEEN REPLACED WITH THE CORRESPONDING LOOP           
COMPND  17  FROM SPINACH RUBISCO, RESIDUES THR46 - GLY64                        
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, SPINACIA             
SOURCE   6  OLERACEA                                                            
KEYWDS    LYASE, RUBISCO, PHOTOSYNTHESIS, CARBON DIOXIDE FIXATION,              
KEYWDS   2 PHOTORESPIRATION, OXIDOREDUCTASE, MONOOXYGENASE,                     
KEYWDS   3 CHLOROPLAST, TRANSIT PEPTIDE, MULTIGENE FAMILY                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.KARKEHABADI,R.J.SPREITZER,I.ANDERSSON                               
REVDAT   3   24-FEB-09 1UZD    1       VERSN                                    
REVDAT   2   27-JUL-05 1UZD    1       JRNL                                     
REVDAT   1   31-MAY-05 1UZD    0                                                
JRNL        AUTH   S.KARKEHABADI,S.R.PEDDI,M.ANWARUZZAMAN,T.C.TAYLOR,           
JRNL        AUTH 2 A.CEDERLUND,T.GENKOV,I.ANDERSSON,R.J.SPREITZER               
JRNL        TITL   CHIMERIC SMALL SUBUNITS INFLUENCE CATALYSIS                  
JRNL        TITL 2 WITHOUT CAUSING GLOBAL CONFORMATIONAL CHANGES IN             
JRNL        TITL 3 THE CRYSTAL STRUCTURE OF RIBULOSE-1,5-BISPHOSPHATE           
JRNL        TITL 4 CARBOXYLASE/OXYGENASE                                        
JRNL        REF    BIOCHEMISTRY                  V.  44  9851 2005              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   16026157                                                     
JRNL        DOI    10.1021/BI050537V                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.4  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) : 2.4                            
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 190692                         
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.1884                          
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.0                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 10097                           
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 37436                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 728                                     
REMARK   3   SOLVENT ATOMS            : 1891                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 20.921                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.93                                                 
REMARK   3    B22 (A**2) : 0.29                                                 
REMARK   3    B33 (A**2) : -1.22                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.540         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.264         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.197         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 8.838         
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 1UZD COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-MAR-04.                  
REMARK 100 THE PDBE ID CODE IS EBI-14773.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-AUG-03                          
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                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9762                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 215895                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 29.800                             
REMARK 200  R MERGE                    (I) : 0.18500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.90000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
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:                                          
REMARK 280  50 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 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      110.00700            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000      112.03900            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      110.00700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000      112.03900            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY.  THE REMARK MAY ALSO PROVIDE INFORMATION ON              
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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  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     THR C   122                                                      
REMARK 465     ALA C   123                                                      
REMARK 465     ARG C   124                                                      
REMARK 465     ASP C   125                                                      
REMARK 465     PHE C   126                                                      
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     THR F   122                                                      
REMARK 465     ALA F   123                                                      
REMARK 465     ARG F   124                                                      
REMARK 465     ASP F   125                                                      
REMARK 465     PHE F   126                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     GLN H     4                                                      
REMARK 465     THR H     5                                                      
REMARK 465     GLU H     6                                                      
REMARK 465     THR I   122                                                      
REMARK 465     ALA I   123                                                      
REMARK 465     ARG I   124                                                      
REMARK 465     ASP I   125                                                      
REMARK 465     PHE I   126                                                      
REMARK 465     THR J   122                                                      
REMARK 465     ALA J   123                                                      
REMARK 465     ARG J   124                                                      
REMARK 465     ASP J   125                                                      
REMARK 465     PHE J   126                                                      
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     THR M   122                                                      
REMARK 465     ALA M   123                                                      
REMARK 465     ARG M   124                                                      
REMARK 465     ASP M   125                                                      
REMARK 465     PHE M   126                                                      
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     THR P   122                                                      
REMARK 465     ALA P   123                                                      
REMARK 465     ARG P   124                                                      
REMARK 465     ASP P   125                                                      
REMARK 465     PHE P   126                                                      
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     THR T   122                                                      
REMARK 465     ALA T   123                                                      
REMARK 465     ARG T   124                                                      
REMARK 465     ASP T   125                                                      
REMARK 465     PHE T   126                                                      
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 465     THR W   122                                                      
REMARK 465     ALA W   123                                                      
REMARK 465     ARG W   124                                                      
REMARK 465     ASP W   125                                                      
REMARK 465     PHE W   126                                                      
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   O2P  CAP H  1477  -  O    HOH H  2162              2.13            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A 324   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP A 351   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASN C   8   N   -  CA  -  C   ANGL. DEV. = -16.4 DEGREES          
REMARK 500    ASP C  63   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP E  33   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP E 160   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP E 351   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP H 286   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASN M   8   N   -  CA  -  C   ANGL. DEV. = -16.7 DEGREES          
REMARK 500    ASP M  47   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP O 160   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP R  86   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP R 160   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP R 202   CB  -  CG  -  OD2 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP R 286   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASN T   8   N   -  CA  -  C   ANGL. DEV. = -16.9 DEGREES          
REMARK 500    ASP V  86   CB  -  CG  -  OD2 ANGL. DEV. =   6.3 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      -78.15   -137.51                                   
REMARK 500    THR A  65     -166.28   -129.29                                   
REMARK 500    CYS A 172      130.18   -171.09                                   
REMARK 500    ASN A 207      -87.70   -121.04                                   
REMARK 500    MET A 212      113.86   -161.06                                   
REMARK 500    MET A 297      -10.86     88.54                                   
REMARK 500    VAL A 331      -52.27     73.29                                   
REMARK 500    ASP A 357       88.90   -161.53                                   
REMARK 500    SER B  62      -78.88   -138.48                                   
REMARK 500    THR B  65     -166.85   -123.39                                   
REMARK 500    CYS B 172      128.56   -171.79                                   
REMARK 500    ASN B 207      -88.83   -119.81                                   
REMARK 500    MET B 212      107.91   -163.44                                   
REMARK 500    ALA B 296      133.71    -39.93                                   
REMARK 500    MET B 297      -11.14     90.41                                   
REMARK 500    VAL B 331      -51.88     71.52                                   
REMARK 500    ASP B 357       91.85   -161.15                                   
REMARK 500    PHE C  12       44.81   -140.50                                   
REMARK 500    GLU C  13     -142.13     59.87                                   
REMARK 500    PHE C  15       -3.48     84.03                                   
REMARK 500    ASP C  47     -122.91   -121.76                                   
REMARK 500    LYS C  71     -122.34     56.54                                   
REMARK 500    GLN C 109       71.74     44.32                                   
REMARK 500    PRO C 128      144.87    -39.51                                   
REMARK 500    SER E  62      -82.56   -141.86                                   
REMARK 500    CYS E 172      127.45   -173.03                                   
REMARK 500    ASN E 207      -85.34   -121.63                                   
REMARK 500    MET E 212      110.85   -162.62                                   
REMARK 500    ALA E 296      135.84    -39.49                                   
REMARK 500    MET E 297      -10.73     85.97                                   
REMARK 500    VAL E 331      -52.51     71.67                                   
REMARK 500    ASP E 357       92.19   -162.57                                   
REMARK 500    ASN F   8       84.57    -13.63                                   
REMARK 500    GLU F  13     -139.36     61.92                                   
REMARK 500    PHE F  15       -6.60     88.79                                   
REMARK 500    ASP F  47     -125.16   -121.25                                   
REMARK 500    LYS F  71     -118.06     57.45                                   
REMARK 500    SER H  62      -76.43   -138.27                                   
REMARK 500    THR H  65     -169.70   -126.69                                   
REMARK 500    THR H  75     -167.87   -129.77                                   
REMARK 500    CYS H 172      127.89   -173.12                                   
REMARK 500    ASN H 207      -88.53   -120.99                                   
REMARK 500    MET H 297       -8.88     93.21                                   
REMARK 500    VAL H 331      -48.88     68.93                                   
REMARK 500    ASP H 357       94.59   -161.81                                   
REMARK 500    ASN I   8       90.56    -36.25                                   
REMARK 500    GLU I  13     -140.17     62.47                                   
REMARK 500    PHE I  15       -0.77     80.92                                   
REMARK 500    ASP I  47     -123.23   -119.47                                   
REMARK 500    LYS I  71     -118.84     60.91                                   
REMARK 500    PRO I 128      143.57    -39.93                                   
REMARK 500    GLU J  13     -143.90     59.44                                   
REMARK 500    PHE J  15       -3.98     85.60                                   
REMARK 500    ASP J  47     -124.94   -119.37                                   
REMARK 500    LYS J  71     -123.92     60.60                                   
REMARK 500    GLN J 109       70.82     43.77                                   
REMARK 500    SER K  62      -77.64   -140.14                                   
REMARK 500    THR K  65     -169.81   -125.52                                   
REMARK 500    CYS K 172      127.54   -174.43                                   
REMARK 500    ASN K 207      -88.28   -120.71                                   
REMARK 500    MET K 212      111.44   -164.33                                   
REMARK 500    MET K 297      -10.23     90.35                                   
REMARK 500    VAL K 331      -52.73     72.94                                   
REMARK 500    LYS K 356      130.43    -39.57                                   
REMARK 500    ASP K 357       93.44   -161.44                                   
REMARK 500    GLU M  13     -142.05     60.67                                   
REMARK 500    PHE M  15       -1.67     81.39                                   
REMARK 500    ASP M  47     -124.66   -118.24                                   
REMARK 500    LYS M  71     -122.08     62.23                                   
REMARK 500    SER O  62      -78.53   -142.60                                   
REMARK 500    THR O  65     -167.91   -122.54                                   
REMARK 500    CYS O 172      126.51   -173.18                                   
REMARK 500    ASN O 207      -90.12   -124.22                                   
REMARK 500    MET O 212      109.19   -162.74                                   
REMARK 500    ALA O 296      128.76    -34.95                                   
REMARK 500    MET O 297       -6.96     90.55                                   
REMARK 500    VAL O 331      -50.49     76.06                                   
REMARK 500    ASP O 357       92.34   -161.21                                   
REMARK 500    PHE P  12       43.19   -140.61                                   
REMARK 500    GLU P  13     -140.90     62.33                                   
REMARK 500    PHE P  15       -2.97     87.06                                   
REMARK 500    ASP P  47     -121.99   -120.80                                   
REMARK 500    LYS P  71     -118.24     59.79                                   
REMARK 500    SER R  62      -77.61   -136.01                                   
REMARK 500    THR R  65     -167.36   -125.60                                   
REMARK 500    THR R  75     -168.75   -125.74                                   
REMARK 500    CYS R 172      128.38   -174.00                                   
REMARK 500    ASN R 207      -88.49   -122.38                                   
REMARK 500    MET R 212      109.02   -161.42                                   
REMARK 500    ALA R 296      131.27    -39.53                                   
REMARK 500    MET R 297      -11.23     90.31                                   
REMARK 500    VAL R 331      -50.69     70.41                                   
REMARK 500    ASP R 357       88.99   -158.76                                   
REMARK 500    GLU T  13     -140.96     64.13                                   
REMARK 500    PHE T  15       -1.13     86.39                                   
REMARK 500    ASP T  47     -122.43   -122.31                                   
REMARK 500    LYS T  71     -120.09     60.23                                   
REMARK 500    SER V  62      -79.44   -138.09                                   
REMARK 500    CYS V 172      127.21   -175.34                                   
REMARK 500    ASN V 207      -87.02   -124.38                                   
REMARK 500    MET V 212      110.64   -165.11                                   
REMARK 500    ALA V 296      129.82    -34.29                                   
REMARK 500    MET V 297       -3.29     88.95                                   
REMARK 500    VAL V 331      -52.66     71.90                                   
REMARK 500    ASP V 357       90.16   -160.17                                   
REMARK 500    GLU W  13     -144.94     60.61                                   
REMARK 500    PHE W  15       -4.39     82.35                                   
REMARK 500    ASP W  47     -122.34   -118.37                                   
REMARK 500    LYS W  71     -120.89     59.48                                   
REMARK 500    GLN W 109       73.06     42.65                                   
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                  -66.97                    
REMARK 500 VAL F    7     ASN F    8                 -143.94                    
REMARK 500 VAL I    7     ASN I    8                 -127.14                    
REMARK 500 VAL J    7     ASN J    8                  -67.88                    
REMARK 500 VAL M    7     ASN M    8                  -65.35                    
REMARK 500 VAL P    7     ASN P    8                  -70.37                    
REMARK 500 VAL T    7     ASN T    8                  -67.22                    
REMARK 500 VAL W    7     ASN W    8                  -68.66                    
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    PHE O 345        25.0      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 ASP A 203   OD1                                                    
REMARK 620 2 GLU A 204   OE1  94.5                                              
REMARK 620 3 CAP A1477   O3  170.4  81.0                                        
REMARK 620 4 CAP A1477   O6  104.7  90.4  83.9                                  
REMARK 620 5 CAP A1477   O2  115.6 149.7  69.6  79.5                            
REMARK 620 6 KCX A 201   OQ2  91.7  90.4  80.0 163.5  91.6                      
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 KCX B 201   OQ2  98.0                                              
REMARK 620 3 ASP B 203   OD1 116.1  88.2                                        
REMARK 620 4 GLU B 204   OE1 151.8  90.8  90.8                                  
REMARK 620 5 CAP B1477   O3   76.1  84.6 166.7  78.2                            
REMARK 620 6 CAP B1477   O6   81.1 172.0  99.3  86.4  87.5                      
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 CAP E1477   O2                                                     
REMARK 620 2 CAP E1477   O3   74.4                                              
REMARK 620 3 CAP E1477   O6   76.0  95.7                                        
REMARK 620 4 KCX E 201   OQ2  88.5  77.5 164.3                                  
REMARK 620 5 ASP E 203   OD1 105.4 164.4  99.3  86.9                            
REMARK 620 6 GLU E 204   OE1 158.3  84.3 102.6  90.9  96.2                      
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  88.1                                              
REMARK 620 3 CAP H1477   O2   90.0 107.3                                        
REMARK 620 4 CAP H1477   O3   87.0 175.2  72.3                                  
REMARK 620 5 CAP H1477   O6  166.3  96.3  76.3  88.3                            
REMARK 620 6 GLU H 204   OE1  95.8  92.3 159.7  88.5  97.0                      
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 GLU K 204   OE1                                                    
REMARK 620 2 CAP K1477   O2  170.7                                              
REMARK 620 3 CAP K1477   O3   94.2  78.5                                        
REMARK 620 4 CAP K1477   O6  100.6  75.1  98.4                                  
REMARK 620 5 KCX K 201   OQ1 108.1  72.9  57.2 142.9                            
REMARK 620 6 KCX K 201   OQ2  93.8  92.7  96.3 158.5  41.4                      
REMARK 620 7 ASP K 203   OD1  86.3 101.1 179.2  82.1 122.0  83.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG O1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU O 204   OE1                                                    
REMARK 620 2 CAP O1477   O3   82.5                                              
REMARK 620 3 KCX O 201   OQ2  87.0  73.8                                        
REMARK 620 4 ASP O 203   OD1  92.4 161.1  87.8                                  
REMARK 620 5 CAP O1477   O2  152.1  69.9  89.0 115.1                            
REMARK 620 6 CAP O1477   O6   98.8  92.1 164.0 106.7  78.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG R1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 KCX R 201   OQ2                                                    
REMARK 620 2 ASP R 203   OD1  93.3                                              
REMARK 620 3 GLU R 204   OE1  94.6  94.5                                        
REMARK 620 4 CAP R1477   O2   88.8 104.1 160.8                                  
REMARK 620 5 CAP R1477   O6  163.8  99.9  93.6  79.0                            
REMARK 620 6 CAP R1477   O3   74.2 167.5  87.3  75.4  92.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG V1476  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP V 203   OD1                                                    
REMARK 620 2 CAP V1477   O2  110.6                                              
REMARK 620 3 GLU V 204   OE1  97.6 149.1                                        
REMARK 620 4 CAP V1477   O6  112.0  80.4 101.2                                  
REMARK 620 5 KCX V 201   OQ2  87.0  84.7  84.2 159.0                            
REMARK 620 6 CAP V1477   O3  159.0  70.6  78.6  88.9  72.1                      
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 O1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG R1476                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE  MG V1476                 
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 C1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO C1136                 
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 F1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP H1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO H1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO I1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO J1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP K1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO K1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO M1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP O1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO O1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO P1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP R1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO R1484                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO T1135                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO T1136                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CAP V1477                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1478                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1479                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1480                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1481                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1482                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO V1483                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO W1135                 
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: 1UW9   RELATED DB: PDB                                   
REMARK 900  L290F-A222T CHLAMYDOMONAS RUBISCO MUTANT                            
REMARK 900 RELATED ID: 1UWA   RELATED DB: PDB                                   
REMARK 900  L290F MUTANT RUBISCO FROM CHLAMYDOMONAS                             
REMARK 900 RELATED ID: 1UZH   RELATED DB: PDB                                   
REMARK 900  A CHIMERIC CHLAMYDOMONAS, SPINACH RUBISCO                           
REMARK 900  ENZYME                                                              
REMARK 900 RELATED ID: 1AA1   RELATED DB: PDB                                   
REMARK 900  ACTIVATED SPINACH RUBISCO IN COMPLEX WITH                           
REMARK 900  THE PRODUCT 3-PHOSPHOGLYCERATE                                      
REMARK 900 RELATED ID: 1AUS   RELATED DB: PDB                                   
REMARK 900  ACTIVATED UNLIGANDED SPINACH RUBISCO                                
REMARK 900 RELATED ID: 1IR1   RELATED DB: PDB                                   
REMARK 900  CRYSTAL STRUCTURE OF SPINACH RIBULOSE-1,5-                          
REMARK 900  BISPHOSPHATECARBOXYLASE/OXYGENASE (RUBISCO)                         
REMARK 900  COMPLEXED WITH CO2, MG2+AND 2-                                      
REMARK 900  CARBOXYARABINITOL-1,5-BISPHOSPHATE                                  
REMARK 900 RELATED ID: 1UPM   RELATED DB: PDB                                   
REMARK 900  ACTIVATED SPINACH RUBISCO COMPLEXED WITH 2-                         
REMARK 900  CARBOXYARABINITOL 2 BISPHOSPHAT AND CA2+.                           
REMARK 900 RELATED ID: 1UPP   RELATED DB: PDB                                   
REMARK 900  SPINACH RUBISCO IN COMPLEX WITH 2-                                  
REMARK 900  CARBOXYARABINITOL 2 BISPHOSPHATE AND CALCIUM.                       
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE SMALL SUBUNIT LOOP BA-BB OF CHLAMYDOMONAS RUBISCO,               
REMARK 999 (RESIDUES 46 - 70 ;EADKAYVSNESAIRFGSVSCLYYDN) IS 6 RESIDUES          
REMARK 999 LONGER THAN THE CORRESPONDING LOOP OF SPINACH RUBISCO                
REMARK 999 ( RESIDUES 46 - 64; TDHGFVYREHHNSPGYYDG. THE REPLACEMENT OF          
REMARK 999 CHLMYDOMONAS RUBISCO LOOP WITH SPINACH                               
REMARK 999 RUBISCO LOOP AFFECTS THE NUMBERING OF THE SMALL SUBUNIT.             
DBREF  1UZD A    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UZD B    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UZD E    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UZD H    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UZD K    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UZD O    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UZD R    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UZD V    1   475  UNP    P00877   RBL_CHLRE        1    475             
DBREF  1UZD I    1    45  UNP    P00873   RBS1_CHLRE      46     90             
DBREF  1UZD I   46    64  UNP    Q43832   RBS2_SPIOL     103    121             
DBREF  1UZD I   65   134  UNP    P00873   RBS1_CHLRE     116    185             
DBREF  1UZD C    1    45  UNP    P00873   RBS1_CHLRE      46     90             
DBREF  1UZD C   46    64  UNP    Q43832   RBS2_SPIOL     103    121             
DBREF  1UZD C   65   134  UNP    P00873   RBS1_CHLRE     116    185             
DBREF  1UZD F    1    45  UNP    P00873   RBS1_CHLRE      46     90             
DBREF  1UZD F   46    64  UNP    Q43832   RBS2_SPIOL     103    121             
DBREF  1UZD F   65   134  UNP    P00873   RBS1_CHLRE     116    185             
DBREF  1UZD J    1    45  UNP    P00873   RBS1_CHLRE      46     90             
DBREF  1UZD J   46    64  UNP    Q43832   RBS2_SPIOL     103    121             
DBREF  1UZD J   65   134  UNP    P00873   RBS1_CHLRE     116    185             
DBREF  1UZD P    1    45  UNP    P00873   RBS1_CHLRE      46     90             
DBREF  1UZD P   46    64  UNP    Q43832   RBS2_SPIOL     103    121             
DBREF  1UZD P   65   134  UNP    P00873   RBS1_CHLRE     116    185             
DBREF  1UZD T    1    45  UNP    P00873   RBS1_CHLRE      46     90             
DBREF  1UZD T   46    64  UNP    Q43832   RBS2_SPIOL     103    121             
DBREF  1UZD T   65   134  UNP    P00873   RBS1_CHLRE     116    185             
DBREF  1UZD M    1    45  UNP    P00873   RBS1_CHLRE      46     90             
DBREF  1UZD M   46    64  UNP    Q43832   RBS2_SPIOL     103    121             
DBREF  1UZD M   65   134  UNP    P00873   RBS1_CHLRE     116    185             
DBREF  1UZD W    1    45  UNP    P00873   RBS1_CHLRE      46     90             
DBREF  1UZD W   46    64  UNP    Q43832   RBS2_SPIOL     103    121             
DBREF  1UZD W   65   134  UNP    P00873   RBS1_CHLRE     116    185             
SEQADV 1UZD PRO A   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UZD PRO B   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UZD PRO E   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UZD PRO H   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UZD PRO K   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UZD PRO O   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UZD PRO R   46  UNP  P00877    LEU    46 CONFLICT                       
SEQADV 1UZD PRO V   46  UNP  P00877    LEU    46 CONFLICT                       
SEQRES   1 A  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 A  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 A  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 A  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 A  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 A  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 A  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 A  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 A  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 A  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 A  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 A  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 A  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 A  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 A  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 A  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 A  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 A  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 A  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 A  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 A  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 A  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 A  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 A  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 A  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 A  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 A  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 A  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 A  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 A  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 A  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 A  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 A  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 A  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 A  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 A  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 A  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 B  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 B  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 B  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 B  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 B  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 B  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 B  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 B  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 B  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 B  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 B  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 B  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 B  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 B  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 B  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 B  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 B  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 B  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 B  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 B  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 B  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 B  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 B  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 B  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 B  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 B  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 B  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 B  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 B  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 B  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 B  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 B  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 B  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 B  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 B  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 B  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 B  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 C  134  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 C  134  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 C  134  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 C  134  PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR          
SEQRES   5 C  134  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 C  134  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG          
SEQRES   7 C  134  ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR          
SEQRES   8 C  134  LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE          
SEQRES   9 C  134  ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL          
SEQRES  10 C  134  GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN          
SEQRES  11 C  134  LYS ARG SER VAL                                              
SEQRES   1 E  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 E  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 E  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 E  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 E  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 E  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 E  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 E  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 E  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 E  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 E  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 E  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 E  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 E  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 E  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 E  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 E  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 E  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 E  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 E  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 E  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 E  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 E  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 E  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 E  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 E  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 E  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 E  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 E  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 E  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 E  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 E  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 E  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 E  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 E  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 E  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 E  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 F  134  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 F  134  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 F  134  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 F  134  PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR          
SEQRES   5 F  134  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 F  134  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG          
SEQRES   7 F  134  ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR          
SEQRES   8 F  134  LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE          
SEQRES   9 F  134  ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL          
SEQRES  10 F  134  GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN          
SEQRES  11 F  134  LYS ARG SER VAL                                              
SEQRES   1 H  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 H  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 H  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 H  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 H  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 H  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 H  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 H  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 H  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 H  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 H  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 H  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 H  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 H  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 H  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 H  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 H  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 H  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 H  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 H  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 H  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 H  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 H  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 H  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 H  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 H  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 H  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 H  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 H  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 H  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 H  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 H  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 H  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 H  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 H  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 H  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 H  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 I  134  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 I  134  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 I  134  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 I  134  PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR          
SEQRES   5 I  134  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 I  134  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG          
SEQRES   7 I  134  ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR          
SEQRES   8 I  134  LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE          
SEQRES   9 I  134  ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL          
SEQRES  10 I  134  GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN          
SEQRES  11 I  134  LYS ARG SER VAL                                              
SEQRES   1 J  134  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 J  134  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 J  134  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 J  134  PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR          
SEQRES   5 J  134  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 J  134  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG          
SEQRES   7 J  134  ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR          
SEQRES   8 J  134  LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE          
SEQRES   9 J  134  ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL          
SEQRES  10 J  134  GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN          
SEQRES  11 J  134  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  ALA 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 LEU 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  134  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 M  134  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 M  134  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 M  134  PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR          
SEQRES   5 M  134  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 M  134  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG          
SEQRES   7 M  134  ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR          
SEQRES   8 M  134  LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE          
SEQRES   9 M  134  ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL          
SEQRES  10 M  134  GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN          
SEQRES  11 M  134  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  ALA 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 LEU 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  134  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 P  134  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 P  134  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 P  134  PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR          
SEQRES   5 P  134  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 P  134  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG          
SEQRES   7 P  134  ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR          
SEQRES   8 P  134  LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE          
SEQRES   9 P  134  ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL          
SEQRES  10 P  134  GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN          
SEQRES  11 P  134  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  ALA 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 LEU 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  134  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 T  134  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 T  134  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 T  134  PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR          
SEQRES   5 T  134  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 T  134  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG          
SEQRES   7 T  134  ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR          
SEQRES   8 T  134  LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE          
SEQRES   9 T  134  ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL          
SEQRES  10 T  134  GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN          
SEQRES  11 T  134  LYS ARG SER VAL                                              
SEQRES   1 V  475  MET VAL PRO GLN THR GLU THR LYS ALA GLY ALA GLY PHE          
SEQRES   2 V  475  LYS ALA GLY VAL LYS ASP TYR ARG LEU THR TYR TYR THR          
SEQRES   3 V  475  PRO ASP TYR VAL VAL ARG ASP THR ASP ILE LEU ALA ALA          
SEQRES   4 V  475  PHE ARG MET THR PRO GLN PRO GLY VAL PRO PRO GLU GLU          
SEQRES   5 V  475  CYS GLY ALA ALA VAL ALA ALA GLU SER SER THR GLY THR          
SEQRES   6 V  475  TRP THR THR VAL TRP THR ASP GLY LEU THR SER LEU ASP          
SEQRES   7 V  475  ARG TYR LYS GLY ARG CYS TYR ASP ILE GLU PRO VAL PRO          
SEQRES   8 V  475  GLY GLU ASP ASN GLN TYR ILE ALA TYR VAL ALA TYR HYP          
SEQRES   9 V  475  ILE ASP LEU PHE GLU GLU GLY SER VAL THR ASN MET PHE          
SEQRES  10 V  475  THR SER ILE VAL GLY ASN VAL PHE GLY PHE LYS ALA LEU          
SEQRES  11 V  475  ARG ALA LEU ARG LEU GLU ASP LEU ARG ILE PRO PRO ALA          
SEQRES  12 V  475  TYR VAL LYS THR PHE VAL GLY HYP PRO HIS GLY ILE GLN          
SEQRES  13 V  475  VAL GLU ARG ASP LYS LEU ASN LYS TYR GLY ARG GLY LEU          
SEQRES  14 V  475  LEU GLY CYS THR ILE LYS PRO LYS LEU GLY LEU SER ALA          
SEQRES  15 V  475  LYS ASN TYR GLY ARG ALA VAL TYR GLU CYS LEU ARG GLY          
SEQRES  16 V  475  GLY LEU ASP PHE THR KCX ASP ASP GLU ASN VAL ASN SER          
SEQRES  17 V  475  GLN PRO PHE MET ARG TRP ARG ASP ARG PHE LEU PHE VAL          
SEQRES  18 V  475  ALA GLU ALA ILE TYR LYS ALA GLN ALA GLU THR GLY GLU          
SEQRES  19 V  475  VAL LYS GLY HIS TYR LEU ASN ALA THR ALA GLY THR CYS          
SEQRES  20 V  475  GLU GLU MET MET LYS ARG ALA VAL SMC ALA LYS GLU LEU          
SEQRES  21 V  475  GLY VAL PRO ILE ILE MET HIS ASP TYR LEU THR GLY GLY          
SEQRES  22 V  475  PHE THR ALA ASN THR SER LEU ALA ILE TYR CYS ARG ASP          
SEQRES  23 V  475  ASN GLY LEU LEU LEU HIS ILE HIS ARG ALA MET HIS ALA          
SEQRES  24 V  475  VAL ILE ASP ARG GLN ARG ASN HIS GLY ILE HIS PHE ARG          
SEQRES  25 V  475  VAL LEU ALA LYS ALA LEU ARG MET SER GLY GLY ASP HIS          
SEQRES  26 V  475  LEU HIS SER GLY THR VAL VAL GLY LYS LEU GLU GLY GLU          
SEQRES  27 V  475  ARG GLU VAL THR LEU GLY PHE VAL ASP LEU MET ARG ASP          
SEQRES  28 V  475  ASP TYR VAL GLU LYS ASP ARG SER ARG GLY ILE TYR PHE          
SEQRES  29 V  475  THR GLN ASP TRP SMC SER MET PRO GLY VAL MET PRO VAL          
SEQRES  30 V  475  ALA SER GLY GLY ILE HIS VAL TRP HIS MET PRO ALA LEU          
SEQRES  31 V  475  VAL GLU ILE PHE GLY ASP ASP ALA CYS LEU GLN PHE GLY          
SEQRES  32 V  475  GLY GLY THR LEU GLY HIS PRO TRP GLY ASN ALA PRO GLY          
SEQRES  33 V  475  ALA ALA ALA ASN ARG VAL ALA LEU GLU ALA CYS THR GLN          
SEQRES  34 V  475  ALA ARG ASN GLU GLY ARG ASP LEU ALA ARG GLU GLY GLY          
SEQRES  35 V  475  ASP VAL ILE ARG SER ALA CYS LYS TRP SER PRO GLU LEU          
SEQRES  36 V  475  ALA ALA ALA CYS GLU VAL TRP LYS GLU ILE LYS PHE GLU          
SEQRES  37 V  475  PHE ASP THR ILE ASP LYS LEU                                  
SEQRES   1 W  134  MET MET VAL TRP THR PRO VAL ASN ASN LYS MET PHE GLU          
SEQRES   2 W  134  THR PHE SER TYR LEU PRO PRO LEU THR ASP GLU GLN ILE          
SEQRES   3 W  134  ALA ALA GLN VAL ASP TYR ILE VAL ALA ASN GLY TRP ILE          
SEQRES   4 W  134  PRO CYS LEU GLU PHE ALA THR ASP HIS GLY PHE VAL TYR          
SEQRES   5 W  134  ARG GLU HIS HIS ASN SER PRO GLY TYR TYR ASP GLY ARG          
SEQRES   6 W  134  TYR TRP THR MET TRP LYS LEU PRO MET PHE GLY CYS ARG          
SEQRES   7 W  134  ASP PRO MET GLN VAL LEU ARG GLU ILE VAL ALA CYS THR          
SEQRES   8 W  134  LYS ALA PHE PRO ASP ALA TYR VAL ARG LEU VAL ALA PHE          
SEQRES   9 W  134  ASP ASN GLN LYS GLN VAL GLN ILE MET GLY PHE LEU VAL          
SEQRES  10 W  134  GLN ARG PRO LYS THR ALA ARG ASP PHE GLN PRO ALA ASN          
SEQRES  11 W  134  LYS ARG SER VAL                                              
MODRES 1UZD HYP A  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP A  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP B  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP B  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP E  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP E  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP H  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP H  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP K  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP K  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP O  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP O  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP R  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP R  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP V  104  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD HYP V  151  PRO  4-HYDROXYPROLINE                                   
MODRES 1UZD KCX A  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UZD KCX B  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UZD KCX E  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UZD KCX H  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UZD KCX K  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UZD KCX O  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UZD KCX R  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UZD KCX V  201  LYS  LYSINE NZ- CARBOXYLIC ACID                         
MODRES 1UZD SMC A  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC A  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC B  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC B  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC E  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC E  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC H  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC H  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC K  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC K  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC O  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC O  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC R  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC R  369  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD SMC V  256  CYS  S- METHYLCYSTEINE                                  
MODRES 1UZD 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  O1476       1                                                       
HET     MG  R1476       1                                                       
HET     MG  V1476       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  C1135       4                                                       
HET    EDO  C1136       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  F1135       4                                                       
HET    CAP  H1477      21                                                       
HET    EDO  H1478       4                                                       
HET    EDO  H1479       4                                                       
HET    EDO  H1480       4                                                       
HET    EDO  H1481       4                                                       
HET    EDO  I1135       4                                                       
HET    EDO  J1135       4                                                       
HET    CAP  K1477      21                                                       
HET    EDO  K1478       4                                                       
HET    EDO  K1479       4                                                       
HET    EDO  K1480       4                                                       
HET    EDO  K1481       4                                                       
HET    EDO  K1482       4                                                       
HET    EDO  M1135       4                                                       
HET    CAP  O1477      21                                                       
HET    EDO  O1478       4                                                       
HET    EDO  O1479       4                                                       
HET    EDO  O1480       4                                                       
HET    EDO  O1481       4                                                       
HET    EDO  O1482       4                                                       
HET    EDO  O1483       4                                                       
HET    EDO  P1135       4                                                       
HET    CAP  R1477      21                                                       
HET    EDO  R1478       4                                                       
HET    EDO  R1479       4                                                       
HET    EDO  R1480       4                                                       
HET    EDO  R1481       4                                                       
HET    EDO  R1482       4                                                       
HET    EDO  R1483       4                                                       
HET    EDO  R1484       4                                                       
HET    EDO  T1135       4                                                       
HET    EDO  T1136       4                                                       
HET    CAP  V1477      21                                                       
HET    EDO  V1478       4                                                       
HET    EDO  V1479       4                                                       
HET    EDO  V1480       4                                                       
HET    EDO  V1481       4                                                       
HET    EDO  V1482       4                                                       
HET    EDO  V1483       4                                                       
HET    EDO  W1135       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    54(C2 H6 O2)                                                 
FORMUL  87  HOH   *1891(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 SER A  112  GLY A  122  1                                  11    
HELIX    6   6 ASN A  123  GLY A  126  5                                   4    
HELIX    7   7 PRO A  141  LYS A  146  1                                   6    
HELIX    8   8 GLY A  154  ASN A  163  1                                  10    
HELIX    9   9 SER A  181  GLY A  195  1                                  15    
HELIX   10  10 ARG A  213  GLY A  233  1                                  21    
HELIX   11  11 THR A  246  VAL A  255  1                                  10    
HELIX   12  12 TYR A  269  GLY A  288  1                                  20    
HELIX   13  13 MET A  297  ARG A  303  1                                   7    
HELIX   14  14 HIS A  310  GLY A  322  1                                  13    
HELIX   15  15 GLU A  338  ASP A  351  1                                  14    
HELIX   16  16 ARG A  358  GLY A  361  5                                   4    
HELIX   17  17 HIS A  383  TRP A  385  5                                   3    
HELIX   18  18 HIS A  386  GLY A  395  1                                  10    
HELIX   19  19 GLY A  403  GLY A  408  1                                   6    
HELIX   20  20 GLY A  412  GLU A  433  1                                  22    
HELIX   21  21 ASP A  436  LYS A  463  1                                  28    
HELIX   22  22 TYR B   20  TYR B   25  1                                   6    
HELIX   23  23 PRO B   49  SER B   61  1                                  13    
HELIX   24  24 VAL B   69  THR B   75  5                                   7    
HELIX   25  25 SER B   76  LYS B   81  1                                   6    
HELIX   26  26 SER B  112  GLY B  122  1                                  11    
HELIX   27  27 ASN B  123  GLY B  126  5                                   4    
HELIX   28  28 PRO B  141  LYS B  146  1                                   6    
HELIX   29  29 GLY B  154  ASN B  163  1                                  10    
HELIX   30  30 SER B  181  GLY B  195  1                                  15    
HELIX   31  31 ARG B  213  GLY B  233  1                                  21    
HELIX   32  32 THR B  246  VAL B  255  1                                  10    
HELIX   33  33 TYR B  269  GLY B  288  1                                  20    
HELIX   34  34 MET B  297  ARG B  303  1                                   7    
HELIX   35  35 HIS B  310  GLY B  322  1                                  13    
HELIX   36  36 GLU B  338  ASP B  351  1                                  14    
HELIX   37  37 ARG B  358  GLY B  361  5                                   4    
HELIX   38  38 HIS B  383  TRP B  385  5                                   3    
HELIX   39  39 HIS B  386  GLY B  395  1                                  10    
HELIX   40  40 GLY B  403  GLY B  408  1                                   6    
HELIX   41  41 GLY B  412  GLU B  433  1                                  22    
HELIX   42  42 ASP B  436  LYS B  463  1                                  28    
HELIX   43  43 THR C   22  GLY C   37  1                                  16    
HELIX   44  44 ASP C   79  PHE C   94  1                                  16    
HELIX   45  45 TYR E   20  TYR E   25  1                                   6    
HELIX   46  46 PRO E   49  SER E   61  1                                  13    
HELIX   47  47 VAL E   69  THR E   75  5                                   7    
HELIX   48  48 SER E   76  LYS E   81  1                                   6    
HELIX   49  49 SER E  112  GLY E  122  1                                  11    
HELIX   50  50 ASN E  123  GLY E  126  5                                   4    
HELIX   51  51 PRO E  141  LYS E  146  1                                   6    
HELIX   52  52 GLY E  154  ASN E  163  1                                  10    
HELIX   53  53 SER E  181  GLY E  195  1                                  15    
HELIX   54  54 ARG E  213  GLY E  233  1                                  21    
HELIX   55  55 THR E  246  VAL E  255  1                                  10    
HELIX   56  56 TYR E  269  GLY E  288  1                                  20    
HELIX   57  57 MET E  297  ARG E  303  1                                   7    
HELIX   58  58 HIS E  310  GLY E  322  1                                  13    
HELIX   59  59 GLU E  338  ASP E  351  1                                  14    
HELIX   60  60 ARG E  358  GLY E  361  5                                   4    
HELIX   61  61 HIS E  383  TRP E  385  5                                   3    
HELIX   62  62 HIS E  386  GLY E  395  1                                  10    
HELIX   63  63 GLY E  403  GLY E  408  1                                   6    
HELIX   64  64 GLY E  412  GLU E  433  1                                  22    
HELIX   65  65 ASP E  436  LYS E  463  1                                  28    
HELIX   66  66 THR F   22  GLY F   37  1                                  16    
HELIX   67  67 ASP F   79  PHE F   94  1                                  16    
HELIX   68  68 TYR H   20  TYR H   25  1                                   6    
HELIX   69  69 PRO H   49  SER H   61  1                                  13    
HELIX   70  70 VAL H   69  THR H   75  5                                   7    
HELIX   71  71 SER H   76  LYS H   81  1                                   6    
HELIX   72  72 SER H  112  VAL H  121  1                                  10    
HELIX   73  73 ASN H  123  GLY H  126  5                                   4    
HELIX   74  74 PRO H  141  LYS H  146  1                                   6    
HELIX   75  75 GLY H  154  ASN H  163  1                                  10    
HELIX   76  76 SER H  181  GLY H  195  1                                  15    
HELIX   77  77 ARG H  213  GLY H  233  1                                  21    
HELIX   78  78 THR H  246  VAL H  255  1                                  10    
HELIX   79  79 TYR H  269  GLY H  288  1                                  20    
HELIX   80  80 MET H  297  ARG H  303  1                                   7    
HELIX   81  81 HIS H  310  GLY H  322  1                                  13    
HELIX   82  82 GLU H  338  ASP H  351  1                                  14    
HELIX   83  83 ARG H  358  GLY H  361  5                                   4    
HELIX   84  84 HIS H  383  TRP H  385  5                                   3    
HELIX   85  85 HIS H  386  GLY H  395  1                                  10    
HELIX   86  86 GLY H  403  GLY H  408  1                                   6    
HELIX   87  87 GLY H  412  GLU H  433  1                                  22    
HELIX   88  88 ASP H  436  LYS H  463  1                                  28    
HELIX   89  89 THR I   22  GLY I   37  1                                  16    
HELIX   90  90 ASP I   79  PHE I   94  1                                  16    
HELIX   91  91 THR J   22  GLY J   37  1                                  16    
HELIX   92  92 ASP J   79  PHE J   94  1                                  16    
HELIX   93  93 TYR K   20  TYR K   25  1                                   6    
HELIX   94  94 PRO K   49  SER K   61  1                                  13    
HELIX   95  95 VAL K   69  THR K   75  5                                   7    
HELIX   96  96 SER K   76  LYS K   81  1                                   6    
HELIX   97  97 SER K  112  GLY K  122  1                                  11    
HELIX   98  98 ASN K  123  GLY K  126  5                                   4    
HELIX   99  99 PRO K  141  LYS K  146  1                                   6    
HELIX  100 100 GLY K  154  ASN K  163  1                                  10    
HELIX  101 101 SER K  181  GLY K  195  1                                  15    
HELIX  102 102 ARG K  213  GLY K  233  1                                  21    
HELIX  103 103 THR K  246  VAL K  255  1                                  10    
HELIX  104 104 TYR K  269  GLY K  288  1                                  20    
HELIX  105 105 MET K  297  ARG K  303  1                                   7    
HELIX  106 106 HIS K  310  GLY K  322  1                                  13    
HELIX  107 107 GLU K  338  ASP K  351  1                                  14    
HELIX  108 108 ARG K  358  GLY K  361  5                                   4    
HELIX  109 109 HIS K  383  TRP K  385  5                                   3    
HELIX  110 110 HIS K  386  GLY K  395  1                                  10    
HELIX  111 111 GLY K  403  GLY K  408  1                                   6    
HELIX  112 112 GLY K  412  GLU K  433  1                                  22    
HELIX  113 113 ASP K  436  LYS K  463  1                                  28    
HELIX  114 114 THR M   22  ASN M   36  1                                  15    
HELIX  115 115 ASP M   79  PHE M   94  1                                  16    
HELIX  116 116 TYR O   20  TYR O   25  1                                   6    
HELIX  117 117 PRO O   49  SER O   61  1                                  13    
HELIX  118 118 VAL O   69  THR O   75  5                                   7    
HELIX  119 119 SER O   76  LYS O   81  1                                   6    
HELIX  120 120 SER O  112  GLY O  122  1                                  11    
HELIX  121 121 ASN O  123  GLY O  126  5                                   4    
HELIX  122 122 PRO O  141  LYS O  146  1                                   6    
HELIX  123 123 GLY O  154  ASN O  163  1                                  10    
HELIX  124 124 SER O  181  GLY O  195  1                                  15    
HELIX  125 125 ARG O  213  GLY O  233  1                                  21    
HELIX  126 126 THR O  246  VAL O  255  1                                  10    
HELIX  127 127 TYR O  269  GLY O  288  1                                  20    
HELIX  128 128 MET O  297  ARG O  303  1                                   7    
HELIX  129 129 HIS O  310  GLY O  322  1                                  13    
HELIX  130 130 GLU O  338  ASP O  351  1                                  14    
HELIX  131 131 ARG O  358  GLY O  361  5                                   4    
HELIX  132 132 HIS O  383  TRP O  385  5                                   3    
HELIX  133 133 HIS O  386  GLY O  395  1                                  10    
HELIX  134 134 GLY O  403  GLY O  408  1                                   6    
HELIX  135 135 GLY O  412  GLU O  433  1                                  22    
HELIX  136 136 ASP O  436  LYS O  463  1                                  28    
HELIX  137 137 THR P   22  GLY P   37  1                                  16    
HELIX  138 138 ASP P   79  PHE P   94  1                                  16    
HELIX  139 139 TYR R   20  TYR R   25  1                                   6    
HELIX  140 140 PRO R   49  SER R   61  1                                  13    
HELIX  141 141 VAL R   69  THR R   75  5                                   7    
HELIX  142 142 SER R   76  LYS R   81  1                                   6    
HELIX  143 143 SER R  112  VAL R  121  1                                  10    
HELIX  144 144 ASN R  123  GLY R  126  5                                   4    
HELIX  145 145 PRO R  141  LYS R  146  1                                   6    
HELIX  146 146 GLY R  154  ASN R  163  1                                  10    
HELIX  147 147 SER R  181  GLY R  195  1                                  15    
HELIX  148 148 ARG R  213  GLY R  233  1                                  21    
HELIX  149 149 THR R  246  VAL R  255  1                                  10    
HELIX  150 150 TYR R  269  GLY R  288  1                                  20    
HELIX  151 151 MET R  297  ARG R  303  1                                   7    
HELIX  152 152 HIS R  310  GLY R  322  1                                  13    
HELIX  153 153 GLU R  338  ASP R  351  1                                  14    
HELIX  154 154 ARG R  358  GLY R  361  5                                   4    
HELIX  155 155 HIS R  383  TRP R  385  5                                   3    
HELIX  156 156 HIS R  386  GLY R  395  1                                  10    
HELIX  157 157 GLY R  403  GLY R  408  1                                   6    
HELIX  158 158 GLY R  412  GLU R  433  1                                  22    
HELIX  159 159 ASP R  436  LYS R  463  1                                  28    
HELIX  160 160 THR T   22  GLY T   37  1                                  16    
HELIX  161 161 ASP T   79  PHE T   94  1                                  16    
HELIX  162 162 TYR V   20  TYR V   25  1                                   6    
HELIX  163 163 PRO V   49  SER V   61  1                                  13    
HELIX  164 164 VAL V   69  THR V   75  5                                   7    
HELIX  165 165 SER V   76  LYS V   81  1                                   6    
HELIX  166 166 SER V  112  GLY V  122  1                                  11    
HELIX  167 167 ASN V  123  GLY V  126  5                                   4    
HELIX  168 168 PRO V  141  LYS V  146  1                                   6    
HELIX  169 169 GLY V  154  ASN V  163  1                                  10    
HELIX  170 170 SER V  181  GLY V  195  1                                  15    
HELIX  171 171 ARG V  213  GLY V  233  1                                  21    
HELIX  172 172 THR V  246  VAL V  255  1                                  10    
HELIX  173 173 TYR V  269  GLY V  288  1                                  20    
HELIX  174 174 MET V  297  ARG V  303  1                                   7    
HELIX  175 175 HIS V  310  GLY V  322  1                                  13    
HELIX  176 176 GLU V  338  ASP V  351  1                                  14    
HELIX  177 177 ARG V  358  GLY V  361  5                                   4    
HELIX  178 178 HIS V  383  TRP V  385  5                                   3    
HELIX  179 179 HIS V  386  GLY V  395  1                                  10    
HELIX  180 180 GLY V  403  GLY V  408  1                                   6    
HELIX  181 181 GLY V  412  GLU V  433  1                                  22    
HELIX  182 182 ASP V  436  LYS V  463  1                                  28    
HELIX  183 183 THR W   22  GLY W   37  1                                  16    
HELIX  184 184 ASP W   79  PHE W   94  1                                  16    
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 LEU 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 LEU 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  68  TRP C  70  0                                        
SHEET    2  CA 4 ILE C  39  ALA C  45 -1  O  LEU C  42   N  TRP C  70           
SHEET    3  CA 4 TYR C  98  ASP C 105 -1  O  TYR C  98   N  ALA C  45           
SHEET    4  CA 4 VAL C 110  GLN C 118 -1  O  VAL C 110   N  ASP C 105           
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 LEU 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  68  TRP F  70  0                                        
SHEET    2  FA 4 ILE F  39  ALA F  45 -1  O  LEU F  42   N  TRP F  70           
SHEET    3  FA 4 TYR F  98  ASP F 105 -1  O  TYR F  98   N  ALA F  45           
SHEET    4  FA 4 VAL F 110  GLN F 118 -1  O  VAL F 110   N  ASP F 105           
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 LEU 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  68  TRP I  70  0                                        
SHEET    2  IA 4 ILE I  39  ALA I  45 -1  O  LEU I  42   N  TRP I  70           
SHEET    3  IA 4 TYR I  98  ASP I 105 -1  O  TYR I  98   N  ALA I  45           
SHEET    4  IA 4 VAL I 110  GLN I 118 -1  O  VAL I 110   N  ASP I 105           
SHEET    1  JA 4 THR J  68  TRP J  70  0                                        
SHEET    2  JA 4 ILE J  39  ALA J  45 -1  O  LEU J  42   N  TRP J  70           
SHEET    3  JA 4 TYR J  98  ASP J 105 -1  O  TYR J  98   N  ALA J  45           
SHEET    4  JA 4 VAL J 110  GLN J 118 -1  O  VAL J 110   N  ASP J 105           
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 LEU 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  68  TRP M  70  0                                        
SHEET    2  MA 4 ILE M  39  ALA M  45 -1  O  LEU M  42   N  TRP M  70           
SHEET    3  MA 4 TYR M  98  ASP M 105 -1  O  TYR M  98   N  ALA M  45           
SHEET    4  MA 4 VAL M 110  GLN M 118 -1  O  VAL M 110   N  ASP M 105           
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 LEU 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  68  TRP P  70  0                                        
SHEET    2  PA 4 ILE P  39  ALA P  45 -1  O  LEU P  42   N  TRP P  70           
SHEET    3  PA 4 TYR P  98  ASP P 105 -1  O  TYR P  98   N  ALA P  45           
SHEET    4  PA 4 VAL P 110  GLN P 118 -1  O  VAL P 110   N  ASP P 105           
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 LEU 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  68  TRP T  70  0                                        
SHEET    2  TA 4 ILE T  39  ALA T  45 -1  O  LEU T  42   N  TRP T  70           
SHEET    3  TA 4 TYR T  98  ASP T 105 -1  O  TYR T  98   N  ALA T  45           
SHEET    4  TA 4 VAL T 110  GLN T 118 -1  O  VAL T 110   N  ASP T 105           
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 LEU 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  68  TRP W  70  0                                        
SHEET    2  WA 4 ILE W  39  ALA W  45 -1  O  LEU W  42   N  TRP W  70           
SHEET    3  WA 4 TYR W  98  ASP W 105 -1  O  TYR W  98   N  ALA W  45           
SHEET    4  WA 4 VAL W 110  GLN W 118 -1  O  VAL W 110   N  ASP W 105           
SSBOND   1 CYS A  247    CYS B  247                          1555   1555  2.09  
SSBOND   2 CYS E  247    CYS K  247                          1555   1555  2.10  
SSBOND   3 CYS H  247    CYS R  247                          1555   1555  2.09  
SSBOND   4 CYS O  247    CYS V  247                          1555   1555  2.10  
LINK         C   TYR A 103                 N   HYP A 104     1555   1555  1.32  
LINK         C   HYP A 104                 N   ILE A 105     1555   1555  1.32  
LINK         C   GLY A 150                 N   HYP A 151     1555   1555  1.34  
LINK         C   HYP A 151                 N   PRO A 152     1555   1555  1.34  
LINK         C   THR A 200                 N   KCX A 201     1555   1555  1.32  
LINK         C   KCX A 201                 N   ASP A 202     1555   1555  1.33  
LINK         OQ2 KCX A 201                MG    MG A1476     1555   1555  2.05  
LINK         C   VAL A 255                 N   SMC A 256     1555   1555  1.33  
LINK         C   SMC A 256                 N   ALA A 257     1555   1555  1.34  
LINK         C   TRP A 368                 N   SMC A 369     1555   1555  1.33  
LINK         C   SMC A 369                 N   SER A 370     1555   1555  1.33  
LINK        MG    MG A1476                 OD1 ASP A 203     1555   1555  1.77  
LINK        MG    MG A1476                 OE1 GLU A 204     1555   1555  2.18  
LINK        MG    MG A1476                 O3  CAP A1477     1555   1555  2.16  
LINK        MG    MG A1476                 O6  CAP A1477     1555   1555  2.19  
LINK        MG    MG A1476                 O2  CAP A1477     1555   1555  2.28  
LINK         C   TYR B 103                 N   HYP B 104     1555   1555  1.33  
LINK         C   HYP B 104                 N   ILE B 105     1555   1555  1.33  
LINK         C   GLY B 150                 N   HYP B 151     1555   1555  1.32  
LINK         C   HYP B 151                 N   PRO B 152     1555   1555  1.33  
LINK         C   THR B 200                 N   KCX B 201     1555   1555  1.32  
LINK         C   KCX B 201                 N   ASP B 202     1555   1555  1.33  
LINK         OQ2 KCX B 201                MG    MG B1476     1555   1555  1.91  
LINK         C   VAL B 255                 N   SMC B 256     1555   1555  1.32  
LINK         C   SMC B 256                 N   ALA B 257     1555   1555  1.34  
LINK         C   TRP B 368                 N   SMC B 369     1555   1555  1.33  
LINK         C   SMC B 369                 N   SER B 370     1555   1555  1.35  
LINK        MG    MG B1476                 O6  CAP B1477     1555   1555  1.76  
LINK        MG    MG B1476                 O2  CAP B1477     1555   1555  2.35  
LINK        MG    MG B1476                 OD1 ASP B 203     1555   1555  1.84  
LINK        MG    MG B1476                 OE1 GLU B 204     1555   1555  2.31  
LINK        MG    MG B1476                 O3  CAP B1477     1555   1555  2.23  
LINK         C   TYR E 103                 N   HYP E 104     1555   1555  1.33  
LINK         C   HYP E 104                 N   ILE E 105     1555   1555  1.32  
LINK         C   GLY E 150                 N   HYP E 151     1555   1555  1.33  
LINK         C   HYP E 151                 N   PRO E 152     1555   1555  1.33  
LINK         C   THR E 200                 N   KCX E 201     1555   1555  1.33  
LINK         C   KCX E 201                 N   ASP E 202     1555   1555  1.33  
LINK         C   VAL E 255                 N   SMC E 256     1555   1555  1.33  
LINK         C   SMC E 256                 N   ALA E 257     1555   1555  1.33  
LINK         C   TRP E 368                 N   SMC E 369     1555   1555  1.35  
LINK         C   SMC E 369                 N   SER E 370     1555   1555  1.33  
LINK        MG    MG E1476                 O2  CAP E1477     1555   1555  2.31  
LINK        MG    MG E1476                 O3  CAP E1477     1555   1555  2.03  
LINK        MG    MG E1476                 O6  CAP E1477     1555   1555  1.98  
LINK        MG    MG E1476                 OQ2 KCX E 201     1555   1555  2.12  
LINK        MG    MG E1476                 OD1 ASP E 203     1555   1555  1.88  
LINK        MG    MG E1476                 OE1 GLU E 204     1555   1555  2.09  
LINK         C   TYR H 103                 N   HYP H 104     1555   1555  1.33  
LINK         C   HYP H 104                 N   ILE H 105     1555   1555  1.32  
LINK         C   GLY H 150                 N   HYP H 151     1555   1555  1.33  
LINK         C   HYP H 151                 N   PRO H 152     1555   1555  1.33  
LINK         C   THR H 200                 N   KCX H 201     1555   1555  1.32  
LINK         C   KCX H 201                 N   ASP H 202     1555   1555  1.34  
LINK         OQ2 KCX H 201                MG    MG H1476     1555   1555  1.99  
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                 OD1 ASP H 203     1555   1555  1.99  
LINK        MG    MG H1476                 OE1 GLU H 204     1555   1555  2.09  
LINK        MG    MG H1476                 O6  CAP H1477     1555   1555  1.91  
LINK        MG    MG H1476                 O3  CAP H1477     1555   1555  2.19  
LINK        MG    MG H1476                 O2  CAP H1477     1555   1555  2.54  
LINK         C   TYR K 103                 N   HYP K 104     1555   1555  1.32  
LINK         C   HYP K 104                 N   ILE K 105     1555   1555  1.33  
LINK         C   GLY K 150                 N   HYP K 151     1555   1555  1.33  
LINK         C   HYP K 151                 N   PRO K 152     1555   1555  1.33  
LINK         C   THR K 200                 N   KCX K 201     1555   1555  1.32  
LINK         OQ2 KCX K 201                MG    MG K1476     1555   1555  1.98  
LINK         C   KCX K 201                 N   ASP K 202     1555   1555  1.33  
LINK         C   VAL K 255                 N   SMC K 256     1555   1555  1.32  
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  1.33  
LINK        MG    MG K1476                 OD1 ASP K 203     1555   1555  2.21  
LINK        MG    MG K1476                 O6  CAP K1477     1555   1555  1.84  
LINK        MG    MG K1476                 O3  CAP K1477     1555   1555  1.85  
LINK        MG    MG K1476                 O2  CAP K1477     1555   1555  2.23  
LINK        MG    MG K1476                 OE1 GLU K 204     1555   1555  2.06  
LINK        MG    MG K1476                 OQ1 KCX K 201     1555   1555  3.15  
LINK         C   TYR O 103                 N   HYP O 104     1555   1555  1.32  
LINK         C   HYP O 104                 N   ILE O 105     1555   1555  1.34  
LINK         C   GLY O 150                 N   HYP O 151     1555   1555  1.32  
LINK         C   HYP O 151                 N   PRO O 152     1555   1555  1.32  
LINK         C   THR O 200                 N   KCX O 201     1555   1555  1.32  
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  1.33  
LINK         C   TRP O 368                 N   SMC O 369     1555   1555  1.32  
LINK         C   SMC O 369                 N   SER O 370     1555   1555  1.34  
LINK        MG    MG O1476                 O6  CAP O1477     1555   1555  1.95  
LINK        MG    MG O1476                 OD1 ASP O 203     1555   1555  1.76  
LINK        MG    MG O1476                 O2  CAP O1477     1555   1555  2.10  
LINK        MG    MG O1476                 OQ2 KCX O 201     1555   1555  2.14  
LINK        MG    MG O1476                 O3  CAP O1477     1555   1555  2.23  
LINK        MG    MG O1476                 OE1 GLU O 204     1555   1555  2.15  
LINK         C   TYR R 103                 N   HYP R 104     1555   1555  1.32  
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 R1476     1555   1555  2.01  
LINK         C   KCX R 201                 N   ASP R 202     1555   1555  1.33  
LINK         C   VAL R 255                 N   SMC R 256     1555   1555  1.32  
LINK         C   SMC R 256                 N   ALA R 257     1555   1555  1.33  
LINK         C   TRP R 368                 N   SMC R 369     1555   1555  1.33  
LINK         C   SMC R 369                 N   SER R 370     1555   1555  1.34  
LINK        MG    MG R1476                 O3  CAP R1477     1555   1555  2.18  
LINK        MG    MG R1476                 O6  CAP R1477     1555   1555  2.28  
LINK        MG    MG R1476                 OD1 ASP R 203     1555   1555  1.86  
LINK        MG    MG R1476                 OE1 GLU R 204     1555   1555  1.99  
LINK        MG    MG R1476                 O2  CAP R1477     1555   1555  2.15  
LINK         C   TYR V 103                 N   HYP V 104     1555   1555  1.34  
LINK         C   HYP V 104                 N   ILE V 105     1555   1555  1.32  
LINK         C   GLY V 150                 N   HYP V 151     1555   1555  1.34  
LINK         C   HYP V 151                 N   PRO V 152     1555   1555  1.33  
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  1.34  
LINK        MG    MG V1476                 O3  CAP V1477     1555   1555  2.38  
LINK        MG    MG V1476                 OQ2 KCX V 201     1555   1555  2.18  
LINK        MG    MG V1476                 O6  CAP V1477     1555   1555  1.80  
LINK        MG    MG V1476                 OE1 GLU V 204     1555   1555  2.10  
LINK        MG    MG V1476                 O2  CAP V1477     1555   1555  2.32  
LINK        MG    MG V1476                 OD1 ASP V 203     1555   1555  1.70  
CISPEP   1 LYS A  175    PRO A  176          0        -2.39                     
CISPEP   2 LYS B  175    PRO B  176          0         2.45                     
CISPEP   3 LYS E  175    PRO E  176          0        -0.67                     
CISPEP   4 LYS H  175    PRO H  176          0        -2.13                     
CISPEP   5 LYS K  175    PRO K  176          0        -1.13                     
CISPEP   6 LYS O  175    PRO O  176          0        -0.80                     
CISPEP   7 LYS R  175    PRO R  176          0         0.99                     
CISPEP   8 LYS V  175    PRO V  176          0        -4.23                     
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  4 KCX B 201  ASP B 203  GLU B 204  CAP B1477                    
SITE     1 AC3  5 LYS E 177  KCX E 201  ASP E 203  GLU E 204                    
SITE     2 AC3  5 CAP E1477                                                     
SITE     1 AC4  5 LYS H 177  KCX H 201  ASP H 203  GLU H 204                    
SITE     2 AC4  5 CAP H1477                                                     
SITE     1 AC5  4 KCX K 201  ASP K 203  GLU K 204  CAP K1477                    
SITE     1 AC6  5 LYS O 177  KCX O 201  ASP O 203  GLU O 204                    
SITE     2 AC6  5 CAP O1477                                                     
SITE     1 AC7  5 LYS R 177  KCX R 201  ASP R 203  GLU R 204                    
SITE     2 AC7  5 CAP R1477                                                     
SITE     1 AC8  5 LYS V 177  KCX V 201  ASP V 203  GLU V 204                    
SITE     2 AC8  5 CAP V1477                                                     
SITE     1 AC9 29 THR A 173  LYS A 175  LYS A 177  KCX A 201                    
SITE     2 AC9 29 ASP A 203  GLU A 204  HIS A 294  ARG A 295                    
SITE     3 AC9 29 HIS A 327  LYS A 334  LEU A 335  SER A 379                    
SITE     4 AC9 29 GLY A 380  GLY A 381  GLY A 403  GLY A 404                    
SITE     5 AC9 29  MG A1476  HOH A2103  HOH A2134  HOH A2135                    
SITE     6 AC9 29 HOH A2143  HOH A2172  HOH A2173  HOH A2174                    
SITE     7 AC9 29 GLU B  60  THR B  65  TRP B  66  ASN B 123                    
SITE     8 AC9 29 HOH B2028                                                     
SITE     1 BC1  7 TYR A  24  THR A  68  VAL A  69  ASP A  72                    
SITE     2 BC1  7 EDO A1479  HOH A2024  HOH A2175                               
SITE     1 BC2  9 VAL A  17  LYS A  18  THR A  65  TRP A  66                    
SITE     2 BC2  9 THR A  67  THR A  68  EDO A1478  HOH A2004                    
SITE     3 BC2  9 HOH A2175                                                     
SITE     1 BC3  2 TYR A  20  GLU A  52                                          
SITE     1 BC4  4 LYS A 466  GLU A 468  PHE A 469  HOH B2200                    
SITE     1 BC5  4 ASP A 302  GLU A 336  ASP A 473  HOH A2177                    
SITE     1 BC6  4 LEU A 270  HOH A2178  LEU B 270  HOH B2111                    
SITE     1 BC7 29 GLU A  60  THR A  65  TRP A  66  ASN A 123                    
SITE     2 BC7 29 HOH A2021  HOH A2022  HOH A2047  THR B 173                    
SITE     3 BC7 29 LYS B 175  LYS B 177  KCX B 201  ASP B 203                    
SITE     4 BC7 29 GLU B 204  HIS B 294  ARG B 295  HIS B 327                    
SITE     5 BC7 29 LYS B 334  LEU B 335  SER B 379  GLY B 380                    
SITE     6 BC7 29 GLY B 381  GLY B 403  GLY B 404   MG B1476                    
SITE     7 BC7 29 HOH B2159  HOH B2194  HOH B2195  HOH B2196                    
SITE     8 BC7 29 HOH B2197                                                     
SITE     1 BC8  6 TYR B  24  THR B  68  VAL B  69  ASP B  72                    
SITE     2 BC8  6 HOH B2031  HOH B2198                                          
SITE     1 BC9  7 VAL B  17  LYS B  18  TRP B  66  THR B  67                    
SITE     2 BC9  7 THR B  68  HOH B2198  HOH B2199                               
SITE     1 CC1  3 TYR B  20  GLU B  52  HOH B2200                               
SITE     1 CC2  3 LYS B 466  PHE B 467  GLU B 468                               
SITE     1 CC3  7 ARG B 295  SER B 328  GLY B 329  GLU B 336                    
SITE     2 CC3  7 GLY B 337  ASP B 473  HOH B2140                               
SITE     1 CC4  3 TYR C  52  GLU C  54  HOH C2055                               
SITE     1 CC5  4 GLY C  37  ILE C  39  PHE C  75  GLY C  76                    
SITE     1 CC6 28 THR E 173  LYS E 175  LYS E 177  KCX E 201                    
SITE     2 CC6 28 ASP E 203  GLU E 204  HIS E 294  ARG E 295                    
SITE     3 CC6 28 HIS E 327  LYS E 334  LEU E 335  SER E 379                    
SITE     4 CC6 28 GLY E 380  GLY E 381  GLY E 403  GLY E 404                    
SITE     5 CC6 28  MG E1476  HOH E2079  HOH E2149  HOH E2150                    
SITE     6 CC6 28 HOH E2183  HOH E2184  HOH E2185  GLU K  60                    
SITE     7 CC6 28 THR K  65  TRP K  66  ASN K 123  HOH K2057                    
SITE     1 CC7  7 TYR E  24  GLY E  64  THR E  68  VAL E  69                    
SITE     2 CC7  7 ASP E  72  EDO E1479  HOH E2037                               
SITE     1 CC8  8 LYS E  18  TYR E  20  THR E  65  TRP E  66                    
SITE     2 CC8  8 THR E  67  THR E  68  EDO E1478  HOH E2014                    
SITE     1 CC9  5 TYR E  20  GLU E  52  ALA E 129  HOH E2015                    
SITE     2 CC9  5 HOH E2186                                                     
SITE     1 DC1  4 LYS E 466  PHE E 467  GLU E 468  EDO K1480                    
SITE     1 DC2  4 LEU E 270  GLY E 273  PHE E 274  LEU K 270                    
SITE     1 DC3  4 GLY F  37  TRP F  38  ILE F  39  GLY F  76                    
SITE     1 DC4 27 THR H 173  LYS H 175  LYS H 177  KCX H 201                    
SITE     2 DC4 27 ASP H 203  GLU H 204  HIS H 294  ARG H 295                    
SITE     3 DC4 27 HIS H 327  LYS H 334  LEU H 335  SER H 379                    
SITE     4 DC4 27 GLY H 380  GLY H 381  GLY H 403  GLY H 404                    
SITE     5 DC4 27  MG H1476  HOH H2144  HOH H2162  HOH H2163                    
SITE     6 DC4 27 HOH H2164  HOH H2165  GLU R  60  THR R  65                    
SITE     7 DC4 27 TRP R  66  ASN R 123  HOH R2022                               
SITE     1 DC5  8 TYR H  24  THR H  68  VAL H  69  ASP H  72                    
SITE     2 DC5  8 LEU H  77  EDO H1479  HOH H2030  HOH H2166                    
SITE     1 DC6  9 LYS H  18  TYR H  20  THR H  65  TRP H  66                    
SITE     2 DC6  9 THR H  67  THR H  68  EDO H1478  HOH H2010                    
SITE     3 DC6  9 HOH H2166                                                     
SITE     1 DC7  4 TYR H  20  GLU H  52  ALA H 129  HOH H2024                    
SITE     1 DC8  4 ARG H 295  GLU H 336  ASP H 473  HOH H2125                    
SITE     1 DC9  3 GLY I  37  ILE I  39  GLY I  76                               
SITE     1 EC1  4 GLY J  37  ILE J  39  PHE J  75  GLY J  76                    
SITE     1 EC2 28 GLU E  60  THR E  65  TRP E  66  ASN E 123                    
SITE     2 EC2 28 HOH E2033  THR K 173  LYS K 175  LYS K 177                    
SITE     3 EC2 28 KCX K 201  ASP K 203  GLU K 204  HIS K 294                    
SITE     4 EC2 28 ARG K 295  HIS K 327  LYS K 334  LEU K 335                    
SITE     5 EC2 28 SER K 379  GLY K 380  GLY K 381  GLY K 403                    
SITE     6 EC2 28 GLY K 404   MG K1476  HOH K2125  HOH K2183                    
SITE     7 EC2 28 HOH K2184  HOH K2185  HOH K2186  HOH K2187                    
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 K2027  HOH K2188                    
SITE     3 EC3  9 HOH K2189                                                     
SITE     1 EC4  6 LYS K  18  TRP K  66  THR K  67  THR K  68                    
SITE     2 EC4  6 HOH K2027  HOH K2190                                          
SITE     1 EC5  2 EDO E1481  GLU K  52                                          
SITE     1 EC6  4 LYS K 466  PHE K 467  GLU K 468  HOH K2191                    
SITE     1 EC7  2 GLU K 336  ASP K 473                                          
SITE     1 EC8  4 GLY M  37  ILE M  39  GLY M  76  CYS M  77                    
SITE     1 EC9 29 THR O 173  LYS O 175  LYS O 177  KCX O 201                    
SITE     2 EC9 29 ASP O 203  GLU O 204  HIS O 294  ARG O 295                    
SITE     3 EC9 29 HIS O 327  LYS O 334  LEU O 335  SER O 379                    
SITE     4 EC9 29 GLY O 380  GLY O 381  GLY O 403  GLY O 404                    
SITE     5 EC9 29  MG O1476  HOH O2108  HOH O2144  HOH O2184                    
SITE     6 EC9 29 HOH O2185  HOH O2186  GLU V  60  THR V  65                    
SITE     7 EC9 29 TRP V  66  ASN V 123  HOH V2026  HOH V2028                    
SITE     8 EC9 29 HOH V2059                                                     
SITE     1 FC1  8 TYR O  24  THR O  68  VAL O  69  ASP O  72                    
SITE     2 FC1  8 LEU O  77  EDO O1479  HOH O2024  HOH O2188                    
SITE     1 FC2  7 LYS O  18  THR O  65  TRP O  66  THR O  67                    
SITE     2 FC2  7 EDO O1478  HOH O2187  HOH O2188                               
SITE     1 FC3  2 GLU O  52  EDO V1482                                          
SITE     1 FC4  4 LYS O 466  PHE O 467  GLU O 468  PHE O 469                    
SITE     1 FC5  4 ARG O 295  GLU O 336  ASP O 473  HOH O2111                    
SITE     1 FC6  6 TYR M  52  HIS M  55  ASP M  63  HOH M2018                    
SITE     2 FC6  6 GLU O 223  LYS O 227                                          
SITE     1 FC7  7 GLY P  37  TRP P  38  ILE P  39  PHE P  75                    
SITE     2 FC7  7 GLY P  76  CYS P  77  HOH P2051                               
SITE     1 FC8 28 GLU H  60  THR H  65  TRP H  66  ASN H 123                    
SITE     2 FC8 28 THR R 173  LYS R 175  LYS R 177  KCX R 201                    
SITE     3 FC8 28 ASP R 203  GLU R 204  HIS R 294  ARG R 295                    
SITE     4 FC8 28 HIS R 327  LYS R 334  LEU R 335  SER R 379                    
SITE     5 FC8 28 GLY R 380  GLY R 381  GLY R 403  GLY R 404                    
SITE     6 FC8 28  MG R1476  HOH R2066  HOH R2110  HOH R2138                    
SITE     7 FC8 28 HOH R2179  HOH R2180  HOH R2181  HOH R2182                    
SITE     1 FC9  8 TYR R  24  GLY R  64  THR R  68  VAL R  69                    
SITE     2 FC9  8 ASP R  72  HOH R2023  HOH R2027  HOH R2183                    
SITE     1 GC1  7 LYS R  18  THR R  65  TRP R  66  THR R  67                    
SITE     2 GC1  7 THR R  68  HOH R2013  HOH R2183                               
SITE     1 GC2  4 TYR R  20  GLU R  52  EDO R1484  HOH R2010                    
SITE     1 GC3  4 LYS R 466  PHE R 467  GLU R 468  PHE R 469                    
SITE     1 GC4  7 TYR P  52  HIS P  55  ASP P  63  HOH P2023                    
SITE     2 GC4  7 GLU R 223  TYR R 226  LYS R 227                               
SITE     1 GC5  5 LEU H 270  GLY H 273  PHE H 274  LEU R 270                    
SITE     2 GC5  5 THR R 271                                                     
SITE     1 GC6  3 ARG B 439  LYS H 466  EDO R1480                               
SITE     1 GC7  6 TYR A 226  ALA A 230  HIS T  48  TYR T  52                    
SITE     2 GC7  6 GLU T  54  HIS T  55                                          
SITE     1 GC8  5 GLY T  37  TRP T  38  ILE T  39  GLY T  76                    
SITE     2 GC8  5 HOH T2048                                                     
SITE     1 GC9 29 GLU O  60  THR O  65  TRP O  66  ASN O 123                    
SITE     2 GC9 29 HOH O2021  HOH O2049  THR V 173  LYS V 175                    
SITE     3 GC9 29 LYS V 177  KCX V 201  ASP V 203  GLU V 204                    
SITE     4 GC9 29 HIS V 294  ARG V 295  HIS V 327  LYS V 334                    
SITE     5 GC9 29 LEU V 335  SER V 379  GLY V 380  GLY V 381                    
SITE     6 GC9 29 GLY V 403  GLY V 404   MG V1476  HOH V2078                    
SITE     7 GC9 29 HOH V2122  HOH V2123  HOH V2190  HOH V2191                    
SITE     8 GC9 29 HOH V2192                                                     
SITE     1 HC1  3 LEU O 270  LEU V 270  PHE V 274                               
SITE     1 HC2  7 TYR V  24  THR V  68  VAL V  69  ASP V  72                    
SITE     2 HC2  7 LEU V  77  EDO V1480  HOH V2193                               
SITE     1 HC3  7 LYS V  18  TYR V  20  THR V  65  TRP V  66                    
SITE     2 HC3  7 THR V  67  EDO V1479  HOH V2194                               
SITE     1 HC4  2 PHE O 469  GLU V  52                                          
SITE     1 HC5  6 ARG E 439  EDO O1480  LYS V 466  PHE V 467                    
SITE     2 HC5  6 GLU V 468  PHE V 469                                          
SITE     1 HC6  3 ARG V 295  GLU V 336  ASP V 473                               
SITE     1 HC7  5 GLY W  37  TRP W  38  GLY W  76  CYS W  77                    
SITE     2 HC7  5 HOH W2034                                                     
CRYST1  220.014  224.078  111.725  90.00  90.00  90.00 P 21 21 2    32          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.004545  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004463  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008950        0.00000                         
MTRIX1   1  0.944700  0.319800  0.072140      -13.04000    1                    
MTRIX2   1  0.319800 -0.947400  0.011780       67.49000    1                    
MTRIX3   1  0.072110  0.011940 -0.997300       51.69000    1                    
MTRIX1   2 -0.320800  0.947100  0.003269       43.13000    1                    
MTRIX2   2  0.947100  0.320800  0.003249      -31.23000    1                    
MTRIX3   2  0.002028  0.004139 -1.000000       56.75000    1                    
MTRIX1   3 -0.947200 -0.320300  0.010540      141.89999    1                    
MTRIX2   3 -0.320300  0.944900 -0.067150       25.25000    1                    
MTRIX3   3  0.011550 -0.066980 -0.997700       59.24000    1                    
MTRIX1   4 -0.001938  0.997600 -0.068640       22.02000    1                    
MTRIX2   4 -0.999900 -0.002908 -0.014030      111.60000    1                    
MTRIX3   4 -0.014200  0.068600  0.997500       -2.15400    1                    
MTRIX1   5  0.008612 -0.999900 -0.014900      111.10000    1                    
MTRIX2   5  0.997600  0.007575  0.068280      -22.13000    1                    
MTRIX3   5 -0.068160 -0.015460  0.997600        5.26800    1                    
MTRIX1   6 -0.996500 -0.006193 -0.083820      133.39999    1                    
MTRIX2   6  0.001507 -0.998400  0.055850       89.54000    1                    
MTRIX3   6 -0.084040  0.055530  0.994900        3.15800    1                    
MTRIX1   7  0.321900 -0.943500  0.079110       85.28000    1                    
MTRIX2   7 -0.943300 -0.326700 -0.057750      124.00000    1                    
MTRIX3   7  0.080330 -0.056040 -0.995200       54.15000    1                    
MTRIX1   8  0.942400  0.326500  0.072810      -13.24000    1                    
MTRIX2   8  0.326800 -0.945100  0.008759       67.14000    1                    
MTRIX3   8  0.071670  0.015540 -0.997300       51.56000    1                    
MTRIX1   9 -0.322700  0.946500  0.002013       43.32000    1                    
MTRIX2   9  0.946500  0.322700  0.000834      -31.17000    1                    
MTRIX3   9  0.000140  0.002175 -1.000000       56.90000    1                    
MTRIX1  10 -0.946400 -0.322700  0.015480      141.89999    1                    
MTRIX2  10 -0.322900  0.943900 -0.069000       25.55000    1                    
MTRIX3  10  0.007651 -0.070300 -0.997500       59.76000    1                    
MTRIX1  11 -0.000736  0.997500 -0.070390       22.04000    1                    
MTRIX2  11 -0.999900 -0.001476 -0.010460      111.40000    1                    
MTRIX3  11 -0.010540  0.070380  0.997500       -2.44600    1                    
MTRIX1  12  0.002121 -0.999900 -0.015480      111.50000    1                    
MTRIX2  12  0.997400  0.000993  0.072470      -21.92000    1                    
MTRIX3  12 -0.072450 -0.015590  0.997300        5.54500    1                    
MTRIX1  13 -0.996700 -0.001846 -0.081380      133.10001    1                    
MTRIX2  13 -0.002854 -0.998300  0.057590       89.83000    1                    
MTRIX3  13 -0.081350  0.057630  0.995000        2.80300    1                    
MTRIX1  14  0.322500 -0.943300  0.078780       85.22000    1                    
MTRIX2  14 -0.943200 -0.327200 -0.057430      124.10000    1                    
MTRIX3  14  0.079950 -0.055790 -0.995200       54.20000    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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