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Database: PDB
Entry: 1CS0
LinkDB: 1CS0
Original site: 1CS0 
HEADER    LIGASE                                  16-AUG-99   1CS0              
TITLE     CRYSTAL STRUCTURE OF CARBAMOYL PHOSPHATE SYNTHETASE COMPLEXED AT      
TITLE    2 CYS269 IN THE SMALL SUBUNIT WITH THE TETRAHEDRAL MIMIC L-GLUTAMATE   
TITLE    3 GAMMA-SEMIALDEHYDE                                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CARBAMOYL PHOSPHATE SYNTHETASE: LARGE SUBUNIT;             
COMPND   3 CHAIN: A, C, E, G;                                                   
COMPND   4 EC: 6.3.5.5;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: CARBAMOYL PHOSPHATE SYNTHETASE: SMALL SUBUNIT;             
COMPND   8 CHAIN: B, D, F, H;                                                   
COMPND   9 EC: 6.3.5.5;                                                         
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_PLASMID: PDP412;                                   
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   9 ORGANISM_TAXID: 562;                                                 
SOURCE  10 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  11 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  12 EXPRESSION_SYSTEM_PLASMID: PDP412                                    
KEYWDS    TETRAHEDRAL ANALOG, AMIDOTRANSFERASE, SUBSTRATE CHANNELING, LIGASE    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.B.THODEN,X.HUANG,F.M.RAUSHEL,H.M.HOLDEN                             
REVDAT   3   13-JUL-11 1CS0    1       VERSN                                    
REVDAT   2   24-FEB-09 1CS0    1       VERSN                                    
REVDAT   1   10-DEC-99 1CS0    0                                                
JRNL        AUTH   J.B.THODEN,X.HUANG,F.M.RAUSHEL,H.M.HOLDEN                    
JRNL        TITL   THE SMALL SUBUNIT OF CARBAMOYL PHOSPHATE SYNTHETASE:         
JRNL        TITL 2 SNAPSHOTS ALONG THE REACTION PATHWAY.                        
JRNL        REF    BIOCHEMISTRY                  V.  38 16158 1999              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   10587438                                                     
JRNL        DOI    10.1021/BI991741J                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 550964                         
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.186                           
REMARK   3   R VALUE            (WORKING SET) : 0.186                           
REMARK   3   FREE R VALUE                     : 0.242                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 56524                           
REMARK   3                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : 0.1860                 
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : 550694                 
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 44256                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 387                                     
REMARK   3   SOLVENT ATOMS            : 4176                                    
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.012 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 2.140 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : ENGH & HUBER                                     
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1CS0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-AUG-99.                  
REMARK 100 THE RCSB ID CODE IS RCSB009517.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-FEB-99                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.7005                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : OTHER                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 550694                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.29300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: AMORE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.98                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.24                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 8000, TETRAETHYLAMMONIUM CHLORIDE,   
REMARK 280  POTASSIUM CHLORIDE, MANGANESE(II) CHLORIDE, ADENOSINE 5'-           
REMARK 280  DIPHOSPHATE, L-ORNITHINE, L-GLUTAMATE GAMMA-SEMIALDEHYDE, PH 7.4,   
REMARK 280  BATCH, TEMPERATURE 277K                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       75.85000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000      166.30000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       81.90000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      166.30000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       75.85000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       81.90000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8110 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46850 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -64.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46730 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -63.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 8530 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 46480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER A   717                                                      
REMARK 465     TYR A   718                                                      
REMARK 465     VAL A   719                                                      
REMARK 465     LEU A   720                                                      
REMARK 465     GLY A   721                                                      
REMARK 465     GLY A   722                                                      
REMARK 465     ARG A   723                                                      
REMARK 465     VAL A   742                                                      
REMARK 465     SER A   743                                                      
REMARK 465     VAL A   744                                                      
REMARK 465     SER A   745                                                      
REMARK 465     ASN A   746                                                      
REMARK 465     ASP A   747                                                      
REMARK 465     ALA A   748                                                      
REMARK 465     PRO A   749                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   381                                                      
REMARK 465     LYS B   382                                                      
REMARK 465     SER C   717                                                      
REMARK 465     TYR C   718                                                      
REMARK 465     VAL C   719                                                      
REMARK 465     LEU C   720                                                      
REMARK 465     GLY C   721                                                      
REMARK 465     GLY C   722                                                      
REMARK 465     ARG C   723                                                      
REMARK 465     VAL C   742                                                      
REMARK 465     SER C   743                                                      
REMARK 465     VAL C   744                                                      
REMARK 465     SER C   745                                                      
REMARK 465     ASN C   746                                                      
REMARK 465     ASP C   747                                                      
REMARK 465     ALA C   748                                                      
REMARK 465     PRO C   749                                                      
REMARK 465     MET D     1                                                      
REMARK 465     ALA D   381                                                      
REMARK 465     LYS D   382                                                      
REMARK 465     SER E   717                                                      
REMARK 465     TYR E   718                                                      
REMARK 465     VAL E   719                                                      
REMARK 465     LEU E   720                                                      
REMARK 465     GLY E   721                                                      
REMARK 465     GLY E   722                                                      
REMARK 465     ARG E   723                                                      
REMARK 465     VAL E   742                                                      
REMARK 465     SER E   743                                                      
REMARK 465     VAL E   744                                                      
REMARK 465     SER E   745                                                      
REMARK 465     ASN E   746                                                      
REMARK 465     ASP E   747                                                      
REMARK 465     ALA E   748                                                      
REMARK 465     PRO E   749                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F   381                                                      
REMARK 465     LYS F   382                                                      
REMARK 465     SER G   717                                                      
REMARK 465     TYR G   718                                                      
REMARK 465     VAL G   719                                                      
REMARK 465     LEU G   720                                                      
REMARK 465     GLY G   721                                                      
REMARK 465     GLY G   722                                                      
REMARK 465     ARG G   723                                                      
REMARK 465     VAL G   742                                                      
REMARK 465     SER G   743                                                      
REMARK 465     VAL G   744                                                      
REMARK 465     SER G   745                                                      
REMARK 465     ASN G   746                                                      
REMARK 465     ASP G   747                                                      
REMARK 465     ALA G   748                                                      
REMARK 465     PRO G   749                                                      
REMARK 465     MET H     1                                                      
REMARK 465     ALA H   381                                                      
REMARK 465     LYS H   382                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     PRO A 716    CG   CD                                             
REMARK 470     PRO C 716    CG   CD                                             
REMARK 470     PRO E 716    CG   CD                                             
REMARK 470     PRO G 716    CG   CD                                             
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   O    HOH A  5430     O    HOH A  5431              2.05            
REMARK 500   OE1  GLU C   154     O    HOH C  2077              2.06            
REMARK 500   O    HOH G  5154     O    HOH G  5227              2.06            
REMARK 500   O    HOH C  1140     O    HOH C  1867              2.06            
REMARK 500   O    HOH C  1616     O    HOH C  1987              2.07            
REMARK 500   O    GLY G   878     O    HOH G  5645              2.09            
REMARK 500   O    HOH C  1973     O    HOH C  1974              2.09            
REMARK 500   N    ILE C   884     O    HOH C  1743              2.11            
REMARK 500   O    HOH D  1837     O    HOH D  1838              2.13            
REMARK 500   O    HOH B  5162     O    HOH B  5207              2.16            
REMARK 500   N1   CYG B   269     O    HOH B  5022              2.17            
REMARK 500   OE2  GLU D   189     O    HOH D  2123              2.17            
REMARK 500   O    HOH G  5296     O    HOH G  5307              2.18            
REMARK 500   O    HOH E  5687     O    HOH E  5800              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 109   CD    GLU A 109   OE2     0.068                       
REMARK 500    GLU A 110   CD    GLU A 110   OE2     0.070                       
REMARK 500    GLU A 153   CD    GLU A 153   OE2     0.067                       
REMARK 500    GLU A 186   CD    GLU A 186   OE2     0.073                       
REMARK 500    GLU A 217   CD    GLU A 217   OE2     0.076                       
REMARK 500    GLU A 219   CD    GLU A 219   OE2     0.067                       
REMARK 500    GLU A 334   CD    GLU A 334   OE2     0.067                       
REMARK 500    GLU A 365   CD    GLU A 365   OE2     0.071                       
REMARK 500    GLU A 478   CD    GLU A 478   OE2     0.072                       
REMARK 500    GLU A 512   CD    GLU A 512   OE2     0.070                       
REMARK 500    GLU A 560   CD    GLU A 560   OE2     0.071                       
REMARK 500    GLU A 595   CD    GLU A 595   OE2     0.066                       
REMARK 500    GLU A 604   CD    GLU A 604   OE2     0.069                       
REMARK 500    GLU A 624   CD    GLU A 624   OE2     0.080                       
REMARK 500    GLU A 628   CD    GLU A 628   OE2     0.071                       
REMARK 500    GLU A 633   CD    GLU A 633   OE2     0.078                       
REMARK 500    GLU A 655   CD    GLU A 655   OE2     0.083                       
REMARK 500    GLU A 676   CD    GLU A 676   OE2     0.070                       
REMARK 500    GLU A 699   CD    GLU A 699   OE2     0.069                       
REMARK 500    GLU A 703   CD    GLU A 703   OE2     0.070                       
REMARK 500    GLU A 707   CD    GLU A 707   OE2     0.072                       
REMARK 500    GLU A 783   CD    GLU A 783   OE2     0.067                       
REMARK 500    GLU A 951   CD    GLU A 951   OE2     0.068                       
REMARK 500    GLU A 955   CD    GLU A 955   OE2     0.067                       
REMARK 500    GLU A 996   CD    GLU A 996   OE2     0.068                       
REMARK 500    GLU A1009   CD    GLU A1009   OE2     0.075                       
REMARK 500    GLU A1024   CD    GLU A1024   OE2     0.071                       
REMARK 500    GLU A1067   CD    GLU A1067   OE2     0.073                       
REMARK 500    GLU B  29   CD    GLU B  29   OE2     0.071                       
REMARK 500    GLU B 145   CD    GLU B 145   OE2     0.072                       
REMARK 500    GLU B 166   CD    GLU B 166   OE2     0.071                       
REMARK 500    GLU B 189   CD    GLU B 189   OE2     0.068                       
REMARK 500    GLU B 226   CD    GLU B 226   OE2     0.073                       
REMARK 500    GLU B 301   CD    GLU B 301   OE2     0.068                       
REMARK 500    GLU B 372   CD    GLU B 372   OE2     0.073                       
REMARK 500    GLU C  59   CD    GLU C  59   OE2     0.068                       
REMARK 500    GLU C  67   CD    GLU C  67   OE2     0.070                       
REMARK 500    GLU C  79   CD    GLU C  79   OE2     0.066                       
REMARK 500    GLU C 109   CD    GLU C 109   OE2     0.076                       
REMARK 500    GLU C 110   CD    GLU C 110   OE2     0.070                       
REMARK 500    GLU C 142   CD    GLU C 142   OE2     0.068                       
REMARK 500    GLU C 153   CD    GLU C 153   OE2     0.071                       
REMARK 500    GLU C 187   CD    GLU C 187   OE2     0.076                       
REMARK 500    GLU C 203   CD    GLU C 203   OE2     0.068                       
REMARK 500    GLU C 349   CD    GLU C 349   OE2     0.069                       
REMARK 500    GLU C 467   CD    GLU C 467   OE2     0.067                       
REMARK 500    GLU C 468   CD    GLU C 468   OE2     0.070                       
REMARK 500    GLU C 473   CD    GLU C 473   OE2     0.070                       
REMARK 500    GLU C 535   CD    GLU C 535   OE2     0.069                       
REMARK 500    GLU C 549   CD    GLU C 549   OE2     0.072                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     150 BOND DEVIATIONS.                              
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   6   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    GLU A  39   CB  -  CA  -  C   ANGL. DEV. = -12.1 DEGREES          
REMARK 500    ARG A  43   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ASP A 124   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 124   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD1 ANGL. DEV. =   8.2 DEGREES          
REMARK 500    ASP A 128   CB  -  CG  -  OD2 ANGL. DEV. =  -7.9 DEGREES          
REMARK 500    ARG A 129   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ARG A 131   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP A 161   CB  -  CG  -  OD2 ANGL. DEV. =  -6.7 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP A 223   CB  -  CG  -  OD2 ANGL. DEV. =  -7.8 DEGREES          
REMARK 500    ASP A 226   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 226   CB  -  CG  -  OD2 ANGL. DEV. =  -5.6 DEGREES          
REMARK 500    ASP A 246   CB  -  CG  -  OD2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ASP A 258   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 333   CB  -  CG  -  OD1 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP A 333   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 338   CB  -  CG  -  OD2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    ASP A 372   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG A 389   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ASP A 410   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ASP A 416   CB  -  CG  -  OD1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A 430   CB  -  CG  -  OD2 ANGL. DEV. =  -5.5 DEGREES          
REMARK 500    GLU A 468   CG  -  CD  -  OE1 ANGL. DEV. =  15.3 DEGREES          
REMARK 500    GLU A 468   CG  -  CD  -  OE2 ANGL. DEV. = -18.4 DEGREES          
REMARK 500    ARG A 471   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    ASP A 487   CB  -  CG  -  OD2 ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    ARG A 514   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG A 517   NE  -  CZ  -  NH1 ANGL. DEV. =   4.2 DEGREES          
REMARK 500    ASP A 530   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 530   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    ASP A 539   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 558   CB  -  CG  -  OD2 ANGL. DEV. =  -6.5 DEGREES          
REMARK 500    ASP A 579   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 592   CB  -  CG  -  OD1 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP A 592   CB  -  CG  -  OD2 ANGL. DEV. =  -6.3 DEGREES          
REMARK 500    ASP A 609   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 609   CB  -  CG  -  OD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    ASP A 611   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ASP A 614   CB  -  CG  -  OD1 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 614   CB  -  CG  -  OD2 ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    ASP A 625   CB  -  CG  -  OD1 ANGL. DEV. =   7.1 DEGREES          
REMARK 500    ASP A 625   CB  -  CG  -  OD2 ANGL. DEV. =  -7.6 DEGREES          
REMARK 500    TYR A 642   CB  -  CG  -  CD2 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TYR A 642   CB  -  CG  -  CD1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ASP A 667   CB  -  CG  -  OD1 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP A 667   CB  -  CG  -  OD2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    ASP A 670   CB  -  CG  -  OD1 ANGL. DEV. =   6.9 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     321 ANGLE DEVIATIONS.                             
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  23     -145.31   -116.61                                   
REMARK 500    ASN A  48      116.49   -161.59                                   
REMARK 500    ALA A  52       36.26    -83.96                                   
REMARK 500    ASP A 226        8.75     87.87                                   
REMARK 500    ASN A 292       11.55   -152.60                                   
REMARK 500    PRO A 302       46.35    -71.67                                   
REMARK 500    VAL A 328       40.37   -101.63                                   
REMARK 500    THR A 340       31.41    -92.16                                   
REMARK 500    ASP A 353       48.02   -107.03                                   
REMARK 500    ASN A 363       33.11   -147.61                                   
REMARK 500    THR A 375     -156.64   -145.39                                   
REMARK 500    PHE A 409       48.53    -82.99                                   
REMARK 500    ASP A 416       32.30    -88.81                                   
REMARK 500    ASP A 530       -3.04   -144.28                                   
REMARK 500    THR A 531      -10.81     72.37                                   
REMARK 500    ALA A 541       69.82   -111.56                                   
REMARK 500    GLU A 548     -157.35   -128.70                                   
REMARK 500    ASP A 558      -82.43    -52.29                                   
REMARK 500    ASP A 758       50.88     36.05                                   
REMARK 500    HIS A 788      129.38    -39.76                                   
REMARK 500    THR A 800      -22.56   -140.71                                   
REMARK 500    PRO A 844       48.76    -68.32                                   
REMARK 500    PRO A 905       47.46    -78.35                                   
REMARK 500    SER A 948       88.68   -158.55                                   
REMARK 500    HIS A 975      -73.71    -26.47                                   
REMARK 500    SER B 239      172.88    -57.78                                   
REMARK 500    PRO B 247        6.01    -69.65                                   
REMARK 500    CYS B 248       54.32    -91.70                                   
REMARK 500    CYG B 269     -101.06     58.94                                   
REMARK 500    ASN B 311       80.19   -164.47                                   
REMARK 500    ALA B 319        0.50    -68.79                                   
REMARK 500    ALA B 356     -130.13     47.90                                   
REMARK 500    SER B 357       72.77     62.04                                   
REMARK 500    PRO C   2     -144.43    -76.57                                   
REMARK 500    ALA C  23     -154.49   -113.54                                   
REMARK 500    ASN C  48      113.24   -167.19                                   
REMARK 500    ALA C  52       40.27    -75.78                                   
REMARK 500    ASN C 292        9.94   -150.60                                   
REMARK 500    PRO C 302       42.76    -77.28                                   
REMARK 500    VAL C 328       40.46   -106.06                                   
REMARK 500    THR C 340       41.13    -99.07                                   
REMARK 500    ASN C 363       36.71   -146.51                                   
REMARK 500    THR C 375     -157.78   -140.98                                   
REMARK 500    THR C 531       -8.98     72.09                                   
REMARK 500    ALA C 541       71.24   -118.04                                   
REMARK 500    GLU C 548     -165.03   -122.55                                   
REMARK 500    ILE C 698      -71.99    -56.60                                   
REMARK 500    GLN C 739      -85.93    -60.86                                   
REMARK 500    ASP C 758       42.55     38.57                                   
REMARK 500    GLN C 821       45.31     71.45                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     119 RAMACHANDRAN OUTLIERS.                        
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 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
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    LEU A  46        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ILE A 339        19.7      L          L   OUTSIDE RANGE           
REMARK 500    ALA A 420        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ARG A 435        20.8      L          L   OUTSIDE RANGE           
REMARK 500    ASN A 457        24.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 548        22.9      L          L   OUTSIDE RANGE           
REMARK 500    GLU A 726        22.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU A 801        24.7      L          L   OUTSIDE RANGE           
REMARK 500    HIS A 975        24.2      L          L   OUTSIDE RANGE           
REMARK 500    ASN A1007        24.5      L          L   OUTSIDE RANGE           
REMARK 500    TYR B  48        24.9      L          L   OUTSIDE RANGE           
REMARK 500    HIS B  76        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ASP B 112        25.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU B 187        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ASN B 204        23.6      L          L   OUTSIDE RANGE           
REMARK 500    ALA B 364        24.6      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 111        22.8      L          L   OUTSIDE RANGE           
REMARK 500    PHE C 172        23.2      L          L   OUTSIDE RANGE           
REMARK 500    ILE C 339         8.0      L          L   EXPECTING SP3           
REMARK 500    ARG C 435        18.7      L          L   OUTSIDE RANGE           
REMARK 500    TYR C 610        24.6      L          L   OUTSIDE RANGE           
REMARK 500    TYR C 729        24.5      L          L   OUTSIDE RANGE           
REMARK 500    LEU C 906        21.0      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 991        12.8      L          L   OUTSIDE RANGE           
REMARK 500    VAL C 994        24.4      L          L   OUTSIDE RANGE           
REMARK 500    ASP C1003        24.1      L          L   OUTSIDE RANGE           
REMARK 500    TYR D  39        25.0      L          L   OUTSIDE RANGE           
REMARK 500    ASP D 136        24.1      L          L   OUTSIDE RANGE           
REMARK 500    ALA D 246        24.6      L          L   OUTSIDE RANGE           
REMARK 500    ALA D 319        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE E  69        24.7      L          L   OUTSIDE RANGE           
REMARK 500    ILE E 139        24.5      L          L   OUTSIDE RANGE           
REMARK 500    ILE E 339        19.0      L          L   OUTSIDE RANGE           
REMARK 500    GLU E 548        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LYS E 954        24.4      L          L   OUTSIDE RANGE           
REMARK 500    LEU E 971        24.6      L          L   OUTSIDE RANGE           
REMARK 500    GLU E1024        24.1      L          L   OUTSIDE RANGE           
REMARK 500    PHE F 192        21.7      L          L   OUTSIDE RANGE           
REMARK 500    SER F 239        22.0      L          L   OUTSIDE RANGE           
REMARK 500    ALA F 246        24.5      L          L   OUTSIDE RANGE           
REMARK 500    LYS F 345        24.2      L          L   OUTSIDE RANGE           
REMARK 500    LYS G   3        24.9      L          L   OUTSIDE RANGE           
REMARK 500    LEU G  46        21.4      L          L   OUTSIDE RANGE           
REMARK 500    ASP G  62        24.4      L          L   OUTSIDE RANGE           
REMARK 500    LEU G 100        24.2      L          L   OUTSIDE RANGE           
REMARK 500    VAL G 328        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ILE G 339        17.2      L          L   OUTSIDE RANGE           
REMARK 500    ARG G 435        25.0      L          L   OUTSIDE RANGE           
REMARK 500    TYR G 729        24.8      L          L   OUTSIDE RANGE           
REMARK 500    ASP G 758        24.3      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 CHIRALITY DEVIATIONS.                         
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A5275        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH A5282        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH A5291        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A5305        DISTANCE =  5.62 ANGSTROMS                       
REMARK 525    HOH A5462        DISTANCE =  5.54 ANGSTROMS                       
REMARK 525    HOH A5480        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH A5498        DISTANCE =  5.03 ANGSTROMS                       
REMARK 525    HOH A5506        DISTANCE =  5.46 ANGSTROMS                       
REMARK 525    HOH A5511        DISTANCE =  5.05 ANGSTROMS                       
REMARK 525    HOH A5514        DISTANCE =  6.01 ANGSTROMS                       
REMARK 525    HOH A5521        DISTANCE =  5.83 ANGSTROMS                       
REMARK 525    HOH A5523        DISTANCE =  5.51 ANGSTROMS                       
REMARK 525    HOH A5678        DISTANCE =  6.05 ANGSTROMS                       
REMARK 525    HOH A5683        DISTANCE =  5.72 ANGSTROMS                       
REMARK 525    HOH A5695        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH A5708        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH A5776        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH A5821        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH A5829        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH A5855        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH A5954        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH B5154        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH B5212        DISTANCE =  5.08 ANGSTROMS                       
REMARK 525    HOH C1263        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH C1273        DISTANCE =  7.63 ANGSTROMS                       
REMARK 525    HOH C1274        DISTANCE =  6.27 ANGSTROMS                       
REMARK 525    HOH C1280        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH C1308        DISTANCE =  5.15 ANGSTROMS                       
REMARK 525    HOH C1486        DISTANCE =  5.37 ANGSTROMS                       
REMARK 525    HOH C1504        DISTANCE =  5.32 ANGSTROMS                       
REMARK 525    HOH C1547        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH C1559        DISTANCE =  5.27 ANGSTROMS                       
REMARK 525    HOH C1716        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH C1721        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH C1898        DISTANCE =  7.24 ANGSTROMS                       
REMARK 525    HOH C1901        DISTANCE =  6.23 ANGSTROMS                       
REMARK 525    HOH C1902        DISTANCE =  6.64 ANGSTROMS                       
REMARK 525    HOH C1936        DISTANCE =  5.22 ANGSTROMS                       
REMARK 525    HOH C1972        DISTANCE =  5.09 ANGSTROMS                       
REMARK 525    HOH C1990        DISTANCE =  5.19 ANGSTROMS                       
REMARK 525    HOH D1531        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH D1939        DISTANCE =  5.56 ANGSTROMS                       
REMARK 525    HOH D2024        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH D2061        DISTANCE =  5.71 ANGSTROMS                       
REMARK 525    HOH E5257        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH E5261        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH E5263        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH E5272        DISTANCE =  5.38 ANGSTROMS                       
REMARK 525    HOH E5440        DISTANCE =  5.79 ANGSTROMS                       
REMARK 525    HOH E5455        DISTANCE =  6.13 ANGSTROMS                       
REMARK 525    HOH E5458        DISTANCE =  5.11 ANGSTROMS                       
REMARK 525    HOH E5476        DISTANCE =  5.12 ANGSTROMS                       
REMARK 525    HOH E5498        DISTANCE =  7.49 ANGSTROMS                       
REMARK 525    HOH E5499        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH E5523        DISTANCE =  6.03 ANGSTROMS                       
REMARK 525    HOH E5572        DISTANCE =  5.60 ANGSTROMS                       
REMARK 525    HOH E5659        DISTANCE =  6.41 ANGSTROMS                       
REMARK 525    HOH E5672        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH E5721        DISTANCE =  5.16 ANGSTROMS                       
REMARK 525    HOH E5793        DISTANCE =  5.84 ANGSTROMS                       
REMARK 525    HOH E5886        DISTANCE =  5.36 ANGSTROMS                       
REMARK 525    HOH E5894        DISTANCE =  5.48 ANGSTROMS                       
REMARK 525    HOH E5925        DISTANCE =  5.18 ANGSTROMS                       
REMARK 525    HOH E5934        DISTANCE =  5.55 ANGSTROMS                       
REMARK 525    HOH G5274        DISTANCE =  5.50 ANGSTROMS                       
REMARK 525    HOH G5286        DISTANCE =  6.55 ANGSTROMS                       
REMARK 525    HOH G5462        DISTANCE =  6.26 ANGSTROMS                       
REMARK 525    HOH G5477        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH G5498        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH G5654        DISTANCE =  5.02 ANGSTROMS                       
REMARK 525    HOH G5690        DISTANCE =  5.20 ANGSTROMS                       
REMARK 525    HOH G5743        DISTANCE =  5.65 ANGSTROMS                       
REMARK 525    HOH G5754        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH G5788        DISTANCE =  5.74 ANGSTROMS                       
REMARK 525    HOH G5805        DISTANCE =  5.66 ANGSTROMS                       
REMARK 525    HOH G5807        DISTANCE =  6.68 ANGSTROMS                       
REMARK 525    HOH H3446        DISTANCE =  5.11 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A5019   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  84   O                                                      
REMARK 620 2 GLY A 112   O    76.0                                              
REMARK 620 3 THR A 114   OG1  81.5 102.7                                        
REMARK 620 4 HOH A5730   O   101.6  82.8 174.2                                  
REMARK 620 5 HOH A5172   O   127.5 156.5  83.3  90.9                            
REMARK 620 6 HOH A5173   O   139.4  80.4  72.0 107.6  80.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A5003   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 215   OE2                                                    
REMARK 620 2 ASN A 236   OD1  83.4                                              
REMARK 620 3 ASP A 238   O   127.0  92.7                                        
REMARK 620 4 ALA A 239   O    93.6 155.0  69.3                                  
REMARK 620 5 ILE A 242   O    83.1 118.2 140.6  85.9                            
REMARK 620 6 SER A 247   OG  135.8  80.9  94.9 116.6  68.8                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A5002  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 285   OE1                                                    
REMARK 620 2 GLU A 299   OE2  79.7                                              
REMARK 620 3 ADP A5000   O1B 175.6 101.2                                        
REMARK 620 4 ADP A5000   O1A  89.3  87.7  86.4                                  
REMARK 620 5 HOH A5157   O    83.8 162.8  94.9  87.4                            
REMARK 620 6 PO4 A5005   O3   91.4  88.1  93.0 175.7  96.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A5021   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 285   OE1                                                    
REMARK 620 2 PO4 A5005   O3   61.9                                              
REMARK 620 3  MN A5002  MN    30.8  33.6                                        
REMARK 620 4 HOH A5162   O   133.2  93.8 109.8                                  
REMARK 620 5 ASN A 283   OD1  85.2 101.2 102.2 141.0                            
REMARK 620 6 ASN A 283   ND2 117.8 131.1 139.5 108.4  37.3                      
REMARK 620 7 HOH A5161   O   144.5  85.2 118.8  56.8  88.7  72.9                
REMARK 620 8 THR A 244   OG1  88.6  89.6  79.6  49.4 163.1 137.8 105.3          
REMARK 620 9 GLU A 217   OE1 123.0 170.3 147.9  76.8  87.8  55.8  91.5  82.4    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A5001  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 299   CD                                                     
REMARK 620 2 GLU A 299   OE1  27.8                                              
REMARK 620 3 GLU A 299   OE2  29.8  57.7                                        
REMARK 620 4 ASN A 301   OD1  85.6  85.0  87.3                                  
REMARK 620 5 ADP A5000   O3B  87.6  85.5  90.6 169.8                            
REMARK 620 6 PO4 A5005   O1  121.5 148.8  91.9  86.8 103.2                      
REMARK 620 7 HOH A5158   O   118.9  91.3 148.4  84.2  92.5 117.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A5004   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 299   OE1                                                    
REMARK 620 2 MET A 300   O    95.2                                              
REMARK 620 3 HOH A5912   O   105.1 129.6                                        
REMARK 620 4 HOH A5158   O    69.5 126.1 104.3                                  
REMARK 620 5 ALA A 126   O   139.4  81.3  53.5 142.9                            
REMARK 620 6 GLU A 127   OE1 132.9  89.7 107.3  70.0  87.7                      
REMARK 620 7 HOH A5252   O    88.3  65.4  69.6 154.9  53.3 135.0                
REMARK 620 8 HOH A5715   O   105.0 158.5  52.2  57.2  88.0  71.1 121.8          
REMARK 620 9 ASN A 301   OD1  55.0  77.1 150.9  51.3 155.5  81.0 124.4 108.3    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A5009   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 761   OE2                                                    
REMARK 620 2 HIS A 781   ND1  77.4                                              
REMARK 620 3 GLU A 783   O   133.2  93.2                                        
REMARK 620 4 GLN A 784   O    95.2 148.9  69.7                                  
REMARK 620 5 VAL A 787   O    78.2 121.4 140.0  85.5                            
REMARK 620 6 SER A 792   OG  123.0  80.9  99.8 126.4  69.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN A5007  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 829   OE1                                                    
REMARK 620 2 GLU A 841   OE2  95.0                                              
REMARK 620 3 HOH A5165   O    86.0 178.7                                        
REMARK 620 4 ADP A5006   O2A  94.1  93.9  86.8                                  
REMARK 620 5 ADP A5006   O3B 174.4  90.6  88.3  86.1                            
REMARK 620 6 HOH A5948   O   104.1  94.5  84.5 159.2  74.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A5008   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 841   OE2                                                    
REMARK 620 2 ADP A5006   O2B 100.9                                              
REMARK 620 3 ADP A5006   O3B  65.8  51.7                                        
REMARK 620 4 HOH A5613   O    77.4  53.4  82.3                                  
REMARK 620 5 GLU A 841   OE1  42.7  91.6  90.0  43.8                            
REMARK 620 6 ASN A 843   OD1  60.6 157.0 121.6 106.2  65.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K B5020   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  16   O                                                      
REMARK 620 2 ASP B 112   O   100.1                                              
REMARK 620 3 HOH B5057   O    77.7 157.2                                        
REMARK 620 4 HOH A5535   O   138.8 117.9  72.9                                  
REMARK 620 5 HOH B5058   O   116.5  79.4  81.4  87.0                            
REMARK 620 6 HOH B5173   O    86.6  90.1 112.2  78.7 155.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C5042   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY C 112   O                                                      
REMARK 620 2 THR C 114   OG1 111.1                                              
REMARK 620 3 ASP C  84   O    76.7  81.5                                        
REMARK 620 4 HOH C1171   O   143.2  91.5  78.6                                  
REMARK 620 5 THR C 114   N    67.4  51.2  46.4 112.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C5027   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 127   OE1                                                    
REMARK 620 2 GLU C 299   OE1 134.3                                              
REMARK 620 3 MET C 300   O    97.3  93.7                                        
REMARK 620 4 HOH C1849   O    94.4 105.0 139.9                                  
REMARK 620 5 ALA C 126   O    85.8 139.5  83.7  59.0                            
REMARK 620 6 HOH C1157   O    71.1  67.1 127.6  92.5 142.2                      
REMARK 620 7 HOH C1250   O   134.3  90.9  68.6  75.8  50.5 151.9                
REMARK 620 8 HOH C1850   O    63.3 102.6 160.2  45.8  90.9  52.2 121.6          
REMARK 620 9 ASN C 301   OD1  86.7  53.2  76.4 142.7 157.7  52.6 127.6 104.4    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C5045   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 143   O                                                      
REMARK 620 2 THR C 143   OG1  70.9                                              
REMARK 620 3 HOH C1259   O   117.1  67.5                                        
REMARK 620 4 ALA C 144   O    64.8  75.5  60.6                                  
REMARK 620 5 HOH C1260   O    69.2  79.2 139.7 132.5                            
REMARK 620 6 HOH C1892   O   145.0  83.7  71.6 132.0  83.1                      
REMARK 620 7 HOH C2070   O   141.9 125.8  58.9  85.2 141.4  72.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C5026   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 215   OE2                                                    
REMARK 620 2 ASN C 236   OD1  86.4                                              
REMARK 620 3 ASP C 238   O   127.9  91.8                                        
REMARK 620 4 ALA C 239   O    90.5 157.0  72.2                                  
REMARK 620 5 ILE C 242   O    77.5 117.0 144.3  84.3                            
REMARK 620 6 SER C 247   OG  133.4  77.8  96.5 119.4  71.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C5044   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 217   OE1                                                    
REMARK 620 2 GLN C 285   OE1 125.6                                              
REMARK 620 3 PO4 C5028   O3  165.0  60.8                                        
REMARK 620 4 HOH C1161   O    73.6 134.2  92.5                                  
REMARK 620 5 HOH C1160   O    93.8 140.1  82.6  56.6                            
REMARK 620 6 ASN C 283   OD1  91.7  82.6 102.8 142.3  91.1                      
REMARK 620 7 THR C 244   OG1  83.3  92.2  82.9  45.1  99.0 169.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C5025  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 285   OE1                                                    
REMARK 620 2 GLU C 299   OE2  72.7                                              
REMARK 620 3 HOH C1156   O    89.7 161.5                                        
REMARK 620 4 ADP C5023   O1A  94.9  89.4  86.6                                  
REMARK 620 5 ADP C5023   O1B 178.7 106.2  91.5  85.8                            
REMARK 620 6 PO4 C5028   O3   89.8  86.3  99.4 172.4  89.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C5024  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 299   CD                                                     
REMARK 620 2 GLU C 299   OE1  28.1                                              
REMARK 620 3 GLU C 299   OE2  30.1  58.1                                        
REMARK 620 4 ASN C 301   OD1  83.9  81.4  84.6                                  
REMARK 620 5 ADP C5023   O3B  92.9  92.5  96.0 172.4                            
REMARK 620 6 PO4 C5028   O1  123.1 149.9  93.2  87.4 100.1                      
REMARK 620 7 HOH C1157   O   125.3  97.2 154.8  87.0  89.3 110.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C5032   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 761   OE2                                                    
REMARK 620 2 HIS C 781   ND1  76.1                                              
REMARK 620 3 GLU C 783   O   129.3  94.7                                        
REMARK 620 4 VAL C 787   O    80.2 127.7 135.4                                  
REMARK 620 5 SER C 792   OG  129.7  88.2  99.0  72.4                            
REMARK 620 6 GLN C 784   O    92.1 144.1  66.6  81.9 123.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN C5030  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN C 829   OE1                                                    
REMARK 620 2 GLU C 841   OE2  93.0                                              
REMARK 620 3 ADP C5029   O3B 165.7  89.4                                        
REMARK 620 4 HOH C1851   O   100.2  87.7  93.9                                  
REMARK 620 5 ADP C5029   O2A  81.8  96.8  83.9 175.0                            
REMARK 620 6 HOH C1164   O    82.2 175.0  95.5  91.8  83.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K C5031   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU C 841   OE1                                                    
REMARK 620 2 GLU C 841   OE2  46.0                                              
REMARK 620 3 HOH C1651   O    56.1  98.6                                        
REMARK 620 4 ADP C5029   O2B  87.0  97.7  55.9                                  
REMARK 620 5 HOH C1620   O   162.0 116.0 139.1  96.3                            
REMARK 620 6 ASN C 843   OD1  69.2  64.7 108.6 156.1 105.8                      
REMARK 620 7 ADP C5029   O3B  85.3  60.8  96.3  50.5  83.3 122.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K D5043   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS D  16   O                                                      
REMARK 620 2 ASP D 112   O    87.9                                              
REMARK 620 3 HOH D1561   O    79.6 155.5                                        
REMARK 620 4 HOH C1562   O   110.3  83.3  81.4                                  
REMARK 620 5 HOH C1563   O   149.7 121.2  76.0  83.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E5065   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP E  84   O                                                      
REMARK 620 2 GLY E 112   O    76.5                                              
REMARK 620 3 HOH E5153   O   108.4 175.0                                        
REMARK 620 4 HOH E5704   O    91.8  89.4  91.7                                  
REMARK 620 5 THR E 114   OG1  88.6  96.7  82.2 173.7                            
REMARK 620 6 THR E 114   N    45.4  63.2 119.1 131.6  51.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E5050   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 127   OE1                                                    
REMARK 620 2 GLU E 299   OE1 133.8                                              
REMARK 620 3 MET E 300   O    97.3  92.4                                        
REMARK 620 4 HOH E5697   O   105.5 101.9 130.2                                  
REMARK 620 5 HOH E5233   O   141.1  84.9  73.6  60.8                            
REMARK 620 6 ALA E 126   O    88.2 137.8  85.2  52.7  53.9                      
REMARK 620 7 HOH E5140   O    70.8  65.7 121.6 107.7 146.3 147.0                
REMARK 620 8 HOH E5696   O    70.1  99.6 166.6  52.8 113.1  89.7  59.7          
REMARK 620 9 ASN E 301   OD1  80.5  59.7  72.6 153.8 128.9 153.4  49.3 108.6    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E5069   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ALA E 144   O                                                      
REMARK 620 2 HOH E5749   O   136.2                                              
REMARK 620 3 HOH E5243   O   122.1  78.8                                        
REMARK 620 4 THR E 143   OG1  72.5  82.0  70.0                                  
REMARK 620 5 THR E 143   O    63.3 133.7  61.1  63.9                            
REMARK 620 6 HOH E5863   O    76.0  81.3 159.6 111.5 138.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E5049   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 215   OE2                                                    
REMARK 620 2 ASN E 236   OD1  77.3                                              
REMARK 620 3 ASP E 238   O   125.7  94.6                                        
REMARK 620 4 ALA E 239   O    92.6 152.6  70.5                                  
REMARK 620 5 ILE E 242   O    86.0 117.4 140.3  86.6                            
REMARK 620 6 SER E 247   OG  134.2  81.8  96.0 121.6  68.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E5067   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 217   OE1                                                    
REMARK 620 2 GLN E 285   OE1 123.8                                              
REMARK 620 3 PO4 E5051   O3  166.1  66.3                                        
REMARK 620 4  MN E5048  MN   150.0  34.2  34.9                                  
REMARK 620 5 ASN E 283   ND2  58.8 115.9 128.2 139.0                            
REMARK 620 6 ASN E 283   OD1  93.2  85.4  97.4 101.7  37.4                      
REMARK 620 7 THR E 244   OG1  85.9  89.0  84.7  76.0 143.9 172.6                
REMARK 620 8 HOH E5143   O    90.2 145.0  81.9 116.8  72.4  84.6 102.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E5048  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 285   OE1                                                    
REMARK 620 2 GLU E 299   OE2  82.4                                              
REMARK 620 3 ADP E5046   O1B 177.4  96.9                                        
REMARK 620 4 HOH E5139   O    81.4 162.0  99.7                                  
REMARK 620 5 ADP E5046   O1A  92.1  82.9  90.3  90.0                            
REMARK 620 6 PO4 E5051   O3   91.8  89.5  85.7  98.8 170.9                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E5047  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 299   CD                                                     
REMARK 620 2 GLU E 299   OE1  27.0                                              
REMARK 620 3 GLU E 299   OE2  29.8  56.7                                        
REMARK 620 4 ASN E 301   OD1  89.2  87.7  92.1                                  
REMARK 620 5 ADP E5046   O3B  89.3  86.2  91.9 169.3                            
REMARK 620 6 HOH E5140   O   117.2  90.3 147.0  85.5  85.7                      
REMARK 620 7 PO4 E5051   O1  128.0 152.5  99.8  78.4 110.6 111.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E5055   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 761   OE2                                                    
REMARK 620 2 HIS E 781   ND1  84.2                                              
REMARK 620 3 GLU E 783   O   124.1  98.4                                        
REMARK 620 4 VAL E 787   O    73.7 118.0 141.9                                  
REMARK 620 5 SER E 792   OG  131.5  77.7 103.0  76.0                            
REMARK 620 6 GLN E 784   O    85.5 150.1  65.1  85.5 128.7                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN E5053  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E 829   OE1                                                    
REMARK 620 2 GLU E 841   OE2  87.1                                              
REMARK 620 3 ADP E5052   O2A  89.0  95.5                                        
REMARK 620 4 HOH E5147   O    86.2 173.3  84.1                                  
REMARK 620 5 ADP E5052   O3B 175.2  90.7  86.9  95.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K E5054   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 841   OE1                                                    
REMARK 620 2 ADP E5052   O2B  92.2                                              
REMARK 620 3 ADP E5052   O3B  81.3  47.4                                        
REMARK 620 4 ASN E 843   OD1  69.1 155.0 111.1                                  
REMARK 620 5 GLU E 841   OE2  42.0  89.7  52.2  65.3                            
REMARK 620 6 HOH E5589   O    57.4  51.1  81.9 122.3  86.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K F5066   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS F  16   O                                                      
REMARK 620 2 ASP F 112   O    88.6                                              
REMARK 620 3 HOH F2618   O    75.0 152.2                                        
REMARK 620 4 HOH E5511   O   113.7  82.6  83.7                                  
REMARK 620 5 HOH E5512   O   146.0 124.3  77.2  82.0                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G5090   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLY G 112   O                                                      
REMARK 620 2 THR G 114   OG1 105.5                                              
REMARK 620 3 HOH G5177   O    73.4  84.6                                        
REMARK 620 4 HOH G5714   O   150.1  74.5  76.9                                  
REMARK 620 5 HOH G5715   O    82.6 168.5 105.7 102.6                            
REMARK 620 6 ASP G  84   O    79.9  86.9 148.5 129.5  86.6                      
REMARK 620 7 HOH G5176   O   169.9  80.0 116.0  39.1  90.8  92.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G5075   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 127   OE1                                                    
REMARK 620 2 GLU G 299   OE1 129.9                                              
REMARK 620 3 MET G 300   O    97.4  95.3                                        
REMARK 620 4 HOH G5162   O    70.1  64.4 129.2                                  
REMARK 620 5 HOH G5256   O   145.8  84.0  71.0 142.2                            
REMARK 620 6 ALA G 126   O    92.1 137.4  84.0 143.0  55.4                      
REMARK 620 7 ASN G 301   OD1  82.0  55.2  75.1  54.8 123.1 157.2                
REMARK 620 8 HOH G5704   O    71.6  96.5 167.4  53.8 114.6  90.2 108.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G5093   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR G 143   O                                                      
REMARK 620 2 THR G 143   OG1  68.8                                              
REMARK 620 3 HOH G5266   O    65.2  80.7                                        
REMARK 620 4 HOH G5265   O   130.9  74.8 138.9                                  
REMARK 620 5 HOH G5800   O   136.4 128.0 146.2  54.6                            
REMARK 620 6 ALA G 144   O    68.9  70.8 132.2  68.7  79.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G5074   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 215   OE2                                                    
REMARK 620 2 ASP G 238   O   120.4                                              
REMARK 620 3 ALA G 239   O    90.0  70.8                                        
REMARK 620 4 ILE G 242   O    87.4 141.7  84.6                                  
REMARK 620 5 SER G 247   OG  137.9  98.5 119.8  68.5                            
REMARK 620 6 ASN G 236   OD1  81.5  94.8 156.6 116.5  79.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G5092   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 285   OE1                                                    
REMARK 620 2 HOH G5165   O   150.2                                              
REMARK 620 3 PO4 G5076   O3   65.8  85.3                                        
REMARK 620 4 HOH G5161   O    46.5 121.9  55.2                                  
REMARK 620 5  MN G5073  MN    32.2 119.9  34.8  34.7                            
REMARK 620 6 ASN G 283   OD1  90.3  90.9 105.8 136.1 105.5                      
REMARK 620 7 HOH G5166   O   125.1  56.3  87.0  78.7 103.6 144.2                
REMARK 620 8 THR G 244   OG1  85.9  98.3  83.6  43.5  77.3 167.4  42.5          
REMARK 620 9 GLU G 217   OE1 118.9  90.9 162.6 114.3 143.9  91.2  76.8  80.2    
REMARK 620 N                    1     2     3     4     5     6     7     8     
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G5073  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 285   OE1                                                    
REMARK 620 2 GLU G 299   OE2  85.9                                              
REMARK 620 3 PO4 G5076   O3   94.2  87.8                                        
REMARK 620 4 HOH G5161   O    79.9 165.8  93.0                                  
REMARK 620 5 ADP G5071   O1A  95.1  88.0 169.5  93.4                            
REMARK 620 6 ADP G5071   O1B 178.4  95.5  86.6  98.7  84.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G5072  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 299   CD                                                     
REMARK 620 2 GLU G 299   OE1  27.4                                              
REMARK 620 3 GLU G 299   OE2  29.5  56.9                                        
REMARK 620 4 ASN G 301   OD1  83.8  86.7  84.3                                  
REMARK 620 5 HOH G5162   O   116.3  89.1 145.6  88.8                            
REMARK 620 6 PO4 G5076   O1  118.8 146.1  89.7  84.5 123.2                      
REMARK 620 7 ADP G5071   O3B  88.3  81.8  93.6 167.5  86.0 107.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G5080   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 761   OE2                                                    
REMARK 620 2 HIS G 781   ND1  78.9                                              
REMARK 620 3 GLU G 783   O   130.5  92.7                                        
REMARK 620 4 GLN G 784   O    90.8 147.6  70.8                                  
REMARK 620 5 VAL G 787   O    86.3 123.0 135.1  86.4                            
REMARK 620 6 SER G 792   OG  124.5  76.3  99.6 132.7  68.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MN G5078  MN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN G 829   OE1                                                    
REMARK 620 2 GLU G 841   OE2  85.7                                              
REMARK 620 3 ADP G5077   O3B 177.5  93.6                                        
REMARK 620 4 HOH G5169   O    85.2 167.1  95.1                                  
REMARK 620 5 ADP G5077   O2A  94.1  83.2  88.2 106.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K G5079   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU G 841   OE2                                                    
REMARK 620 2 HOH G5607   O    96.0                                              
REMARK 620 3 ADP G5077   O2B  91.4  61.2                                        
REMARK 620 4 ASN G 843   OD1  70.9 114.7 161.7                                  
REMARK 620 5 HOH G5705   O   166.2  97.7  96.7 101.5                            
REMARK 620 6 GLU G 841   OE1  44.2  55.7  87.1  77.1 147.0                      
REMARK 620 7 ADP G5077   O3B  66.3 103.9  47.4 124.1 111.8  94.9                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K H5091   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP H 112   O                                                      
REMARK 620 2 HIS H  16   O    86.1                                              
REMARK 620 3 HOH G5531   O   130.5 139.6                                        
REMARK 620 4 HOH G5530   O    93.1 119.8  79.9                                  
REMARK 620 5 HOH H3715   O   144.8  68.5  82.6  79.9                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                               K A5022   K                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A5261   O                                                      
REMARK 620 2 THR A 143   OG1  64.6                                              
REMARK 620 3 ALA A 144   O    57.4  76.2                                        
REMARK 620 4 THR A 143   O   105.0  63.6  60.5                                  
REMARK 620 5 HOH A5262   O   127.5  66.8 126.6  68.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 5001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 5002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5003                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5004                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 5007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5008                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5009                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5011                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5012                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5013                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5014                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5015                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 5016                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 5017                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 5018                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5019                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K B 5020                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5021                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K A 5022                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5058                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5090                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 5024                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5059                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K H 5091                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 5025                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5060                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5092                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5026                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5061                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5093                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5027                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL E 5062                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN C 5030                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 5063                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5031                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL F 5064                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5032                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5065                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5035                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K F 5066                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5036                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5067                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5037                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5068                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5038                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5069                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 5039                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 5072                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 5040                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 5073                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 5041                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5074                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5042                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: FC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5075                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K D 5043                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN G 5078                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5044                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5079                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K C 5045                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K G 5080                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5047                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5083                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: GC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5048                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5084                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5049                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5085                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5050                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5086                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN E 5053                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL G 5087                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5054                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: HC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 5088                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE K E 5055                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL H 5089                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 5005                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 C 5028                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 5051                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 E 5070                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 G 5076                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 5000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: IC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP A 5006                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN A 5010                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET A 5094                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 5023                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP C 5029                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN C 5033                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET C 5034                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 5046                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP E 5052                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: JC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN E 5056                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET E 5057                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 5071                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADP G 5077                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ORN G 5081                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: KC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NET G 5082                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1C3O   RELATED DB: PDB                                   
DBREF  1CS0 A    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1CS0 C    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1CS0 E    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1CS0 G    1  1073  UNP    P00968   CARB_ECOLI       1   1073             
DBREF  1CS0 B    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1CS0 D    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1CS0 F    1   382  UNP    P00907   CARA_ECOLI       1    382             
DBREF  1CS0 H    1   382  UNP    P00907   CARA_ECOLI       1    382             
SEQRES   1 A 1073  MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU          
SEQRES   2 A 1073  GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE          
SEQRES   3 A 1073  ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU          
SEQRES   4 A 1073  GLU GLY TYR ARG VAL ILE LEU VAL ASN SER ASN PRO ALA          
SEQRES   5 A 1073  THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR          
SEQRES   6 A 1073  ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE          
SEQRES   7 A 1073  GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY          
SEQRES   8 A 1073  GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG          
SEQRES   9 A 1073  GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY          
SEQRES  10 A 1073  ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG          
SEQRES  11 A 1073  ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR          
SEQRES  12 A 1073  ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU          
SEQRES  13 A 1073  ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG          
SEQRES  14 A 1073  PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA          
SEQRES  15 A 1073  TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY          
SEQRES  16 A 1073  LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU          
SEQRES  17 A 1073  SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL          
SEQRES  18 A 1073  ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE          
SEQRES  19 A 1073  GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER          
SEQRES  20 A 1073  ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU          
SEQRES  21 A 1073  TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG          
SEQRES  22 A 1073  GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE          
SEQRES  23 A 1073  ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU          
SEQRES  24 A 1073  MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER          
SEQRES  25 A 1073  LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS          
SEQRES  26 A 1073  LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP          
SEQRES  27 A 1073  ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER          
SEQRES  28 A 1073  ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE          
SEQRES  29 A 1073  GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN          
SEQRES  30 A 1073  MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR          
SEQRES  31 A 1073  GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU          
SEQRES  32 A 1073  VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP          
SEQRES  33 A 1073  ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS          
SEQRES  34 A 1073  ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA          
SEQRES  35 A 1073  PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU          
SEQRES  36 A 1073  THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU          
SEQRES  37 A 1073  LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE          
SEQRES  38 A 1073  THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG          
SEQRES  39 A 1073  LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY          
SEQRES  40 A 1073  VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR          
SEQRES  41 A 1073  ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA          
SEQRES  42 A 1073  ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR          
SEQRES  43 A 1073  TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG          
SEQRES  44 A 1073  GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE          
SEQRES  45 A 1073  GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA          
SEQRES  46 A 1073  SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET          
SEQRES  47 A 1073  VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP          
SEQRES  48 A 1073  THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU          
SEQRES  49 A 1073  ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY          
SEQRES  50 A 1073  VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU          
SEQRES  51 A 1073  ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY          
SEQRES  52 A 1073  THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU          
SEQRES  53 A 1073  ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN          
SEQRES  54 A 1073  PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL          
SEQRES  55 A 1073  GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG          
SEQRES  56 A 1073  PRO SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL          
SEQRES  57 A 1073  TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA          
SEQRES  58 A 1073  VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS          
SEQRES  59 A 1073  PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE          
SEQRES  60 A 1073  CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU          
SEQRES  61 A 1073  HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA          
SEQRES  62 A 1073  CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN          
SEQRES  63 A 1073  ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU          
SEQRES  64 A 1073  LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL          
SEQRES  65 A 1073  LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG          
SEQRES  66 A 1073  ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY          
SEQRES  67 A 1073  VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY          
SEQRES  68 A 1073  LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE          
SEQRES  69 A 1073  PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE          
SEQRES  70 A 1073  ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU          
SEQRES  71 A 1073  MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR          
SEQRES  72 A 1073  PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN          
SEQRES  73 A 1073  SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL          
SEQRES  74 A 1073  ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA          
SEQRES  75 A 1073  LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS          
SEQRES  76 A 1073  GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO          
SEQRES  77 A 1073  ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE          
SEQRES  78 A 1073  GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE          
SEQRES  79 A 1073  ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG          
SEQRES  80 A 1073  VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR          
SEQRES  81 A 1073  ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA          
SEQRES  82 A 1073  LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN          
SEQRES  83 A 1073  GLU MET HIS ALA GLN ILE LYS                                  
SEQRES   1 B  382  MET ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR          
SEQRES   2 B  382  GLN PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA          
SEQRES   3 B  382  VAL GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR          
SEQRES   4 B  382  GLN GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE          
SEQRES   5 B  382  VAL THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR          
SEQRES   6 B  382  ASN ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN          
SEQRES   7 B  382  GLY LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN          
SEQRES   8 B  382  PHE ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG          
SEQRES   9 B  382  HIS ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS          
SEQRES  10 B  382  LEU THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY          
SEQRES  11 B  382  CYS ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA          
SEQRES  12 B  382  LEU GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET          
SEQRES  13 B  382  ASP LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER          
SEQRES  14 B  382  TRP THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO          
SEQRES  15 B  382  GLU ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL          
SEQRES  16 B  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET          
SEQRES  17 B  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA          
SEQRES  18 B  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP          
SEQRES  19 B  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO          
SEQRES  20 B  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 B  382  THR ASP ILE PRO VAL PHE GLY ILE CYG LEU GLY HIS GLN          
SEQRES  22 B  382  LEU LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET          
SEQRES  23 B  382  LYS PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP          
SEQRES  24 B  382  VAL GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS          
SEQRES  25 B  382  GLY PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU          
SEQRES  26 B  382  ARG VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN          
SEQRES  27 B  382  GLY ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN          
SEQRES  28 B  382  GLY HIS PRO GLU ALA SER PRO GLY PRO HIS ASP ALA ALA          
SEQRES  29 B  382  PRO LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR          
SEQRES  30 B  382  ARG LYS THR ALA LYS                                          
SEQRES   1 C 1073  MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU          
SEQRES   2 C 1073  GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE          
SEQRES   3 C 1073  ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU          
SEQRES   4 C 1073  GLU GLY TYR ARG VAL ILE LEU VAL ASN SER ASN PRO ALA          
SEQRES   5 C 1073  THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR          
SEQRES   6 C 1073  ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE          
SEQRES   7 C 1073  GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY          
SEQRES   8 C 1073  GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG          
SEQRES   9 C 1073  GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY          
SEQRES  10 C 1073  ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG          
SEQRES  11 C 1073  ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR          
SEQRES  12 C 1073  ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU          
SEQRES  13 C 1073  ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG          
SEQRES  14 C 1073  PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA          
SEQRES  15 C 1073  TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY          
SEQRES  16 C 1073  LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU          
SEQRES  17 C 1073  SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL          
SEQRES  18 C 1073  ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE          
SEQRES  19 C 1073  GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER          
SEQRES  20 C 1073  ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU          
SEQRES  21 C 1073  TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG          
SEQRES  22 C 1073  GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE          
SEQRES  23 C 1073  ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU          
SEQRES  24 C 1073  MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER          
SEQRES  25 C 1073  LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS          
SEQRES  26 C 1073  LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP          
SEQRES  27 C 1073  ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER          
SEQRES  28 C 1073  ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE          
SEQRES  29 C 1073  GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN          
SEQRES  30 C 1073  MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR          
SEQRES  31 C 1073  GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU          
SEQRES  32 C 1073  VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP          
SEQRES  33 C 1073  ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS          
SEQRES  34 C 1073  ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA          
SEQRES  35 C 1073  PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU          
SEQRES  36 C 1073  THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU          
SEQRES  37 C 1073  LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE          
SEQRES  38 C 1073  THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG          
SEQRES  39 C 1073  LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY          
SEQRES  40 C 1073  VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR          
SEQRES  41 C 1073  ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA          
SEQRES  42 C 1073  ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR          
SEQRES  43 C 1073  TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG          
SEQRES  44 C 1073  GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE          
SEQRES  45 C 1073  GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA          
SEQRES  46 C 1073  SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET          
SEQRES  47 C 1073  VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP          
SEQRES  48 C 1073  THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU          
SEQRES  49 C 1073  ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY          
SEQRES  50 C 1073  VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU          
SEQRES  51 C 1073  ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY          
SEQRES  52 C 1073  THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU          
SEQRES  53 C 1073  ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN          
SEQRES  54 C 1073  PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL          
SEQRES  55 C 1073  GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG          
SEQRES  56 C 1073  PRO SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL          
SEQRES  57 C 1073  TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA          
SEQRES  58 C 1073  VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS          
SEQRES  59 C 1073  PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE          
SEQRES  60 C 1073  CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU          
SEQRES  61 C 1073  HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA          
SEQRES  62 C 1073  CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN          
SEQRES  63 C 1073  ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU          
SEQRES  64 C 1073  LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL          
SEQRES  65 C 1073  LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG          
SEQRES  66 C 1073  ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY          
SEQRES  67 C 1073  VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY          
SEQRES  68 C 1073  LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE          
SEQRES  69 C 1073  PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE          
SEQRES  70 C 1073  ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU          
SEQRES  71 C 1073  MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR          
SEQRES  72 C 1073  PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN          
SEQRES  73 C 1073  SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL          
SEQRES  74 C 1073  ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA          
SEQRES  75 C 1073  LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS          
SEQRES  76 C 1073  GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO          
SEQRES  77 C 1073  ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE          
SEQRES  78 C 1073  GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE          
SEQRES  79 C 1073  ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG          
SEQRES  80 C 1073  VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR          
SEQRES  81 C 1073  ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA          
SEQRES  82 C 1073  LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN          
SEQRES  83 C 1073  GLU MET HIS ALA GLN ILE LYS                                  
SEQRES   1 D  382  MET ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR          
SEQRES   2 D  382  GLN PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA          
SEQRES   3 D  382  VAL GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR          
SEQRES   4 D  382  GLN GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE          
SEQRES   5 D  382  VAL THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR          
SEQRES   6 D  382  ASN ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN          
SEQRES   7 D  382  GLY LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN          
SEQRES   8 D  382  PHE ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG          
SEQRES   9 D  382  HIS ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS          
SEQRES  10 D  382  LEU THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY          
SEQRES  11 D  382  CYS ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA          
SEQRES  12 D  382  LEU GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET          
SEQRES  13 D  382  ASP LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER          
SEQRES  14 D  382  TRP THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO          
SEQRES  15 D  382  GLU ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL          
SEQRES  16 D  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET          
SEQRES  17 D  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA          
SEQRES  18 D  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP          
SEQRES  19 D  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO          
SEQRES  20 D  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 D  382  THR ASP ILE PRO VAL PHE GLY ILE CYG LEU GLY HIS GLN          
SEQRES  22 D  382  LEU LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET          
SEQRES  23 D  382  LYS PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP          
SEQRES  24 D  382  VAL GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS          
SEQRES  25 D  382  GLY PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU          
SEQRES  26 D  382  ARG VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN          
SEQRES  27 D  382  GLY ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN          
SEQRES  28 D  382  GLY HIS PRO GLU ALA SER PRO GLY PRO HIS ASP ALA ALA          
SEQRES  29 D  382  PRO LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR          
SEQRES  30 D  382  ARG LYS THR ALA LYS                                          
SEQRES   1 E 1073  MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU          
SEQRES   2 E 1073  GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE          
SEQRES   3 E 1073  ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU          
SEQRES   4 E 1073  GLU GLY TYR ARG VAL ILE LEU VAL ASN SER ASN PRO ALA          
SEQRES   5 E 1073  THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR          
SEQRES   6 E 1073  ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE          
SEQRES   7 E 1073  GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY          
SEQRES   8 E 1073  GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG          
SEQRES   9 E 1073  GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY          
SEQRES  10 E 1073  ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG          
SEQRES  11 E 1073  ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR          
SEQRES  12 E 1073  ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU          
SEQRES  13 E 1073  ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG          
SEQRES  14 E 1073  PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA          
SEQRES  15 E 1073  TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY          
SEQRES  16 E 1073  LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU          
SEQRES  17 E 1073  SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL          
SEQRES  18 E 1073  ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE          
SEQRES  19 E 1073  GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER          
SEQRES  20 E 1073  ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU          
SEQRES  21 E 1073  TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG          
SEQRES  22 E 1073  GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE          
SEQRES  23 E 1073  ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU          
SEQRES  24 E 1073  MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER          
SEQRES  25 E 1073  LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS          
SEQRES  26 E 1073  LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP          
SEQRES  27 E 1073  ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER          
SEQRES  28 E 1073  ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE          
SEQRES  29 E 1073  GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN          
SEQRES  30 E 1073  MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR          
SEQRES  31 E 1073  GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU          
SEQRES  32 E 1073  VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP          
SEQRES  33 E 1073  ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS          
SEQRES  34 E 1073  ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA          
SEQRES  35 E 1073  PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU          
SEQRES  36 E 1073  THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU          
SEQRES  37 E 1073  LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE          
SEQRES  38 E 1073  THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG          
SEQRES  39 E 1073  LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY          
SEQRES  40 E 1073  VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR          
SEQRES  41 E 1073  ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA          
SEQRES  42 E 1073  ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR          
SEQRES  43 E 1073  TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG          
SEQRES  44 E 1073  GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE          
SEQRES  45 E 1073  GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA          
SEQRES  46 E 1073  SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET          
SEQRES  47 E 1073  VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP          
SEQRES  48 E 1073  THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU          
SEQRES  49 E 1073  ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY          
SEQRES  50 E 1073  VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU          
SEQRES  51 E 1073  ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY          
SEQRES  52 E 1073  THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU          
SEQRES  53 E 1073  ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN          
SEQRES  54 E 1073  PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL          
SEQRES  55 E 1073  GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG          
SEQRES  56 E 1073  PRO SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL          
SEQRES  57 E 1073  TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA          
SEQRES  58 E 1073  VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS          
SEQRES  59 E 1073  PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE          
SEQRES  60 E 1073  CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU          
SEQRES  61 E 1073  HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA          
SEQRES  62 E 1073  CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN          
SEQRES  63 E 1073  ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU          
SEQRES  64 E 1073  LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL          
SEQRES  65 E 1073  LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG          
SEQRES  66 E 1073  ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY          
SEQRES  67 E 1073  VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY          
SEQRES  68 E 1073  LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE          
SEQRES  69 E 1073  PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE          
SEQRES  70 E 1073  ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU          
SEQRES  71 E 1073  MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR          
SEQRES  72 E 1073  PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN          
SEQRES  73 E 1073  SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL          
SEQRES  74 E 1073  ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA          
SEQRES  75 E 1073  LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS          
SEQRES  76 E 1073  GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO          
SEQRES  77 E 1073  ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE          
SEQRES  78 E 1073  GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE          
SEQRES  79 E 1073  ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG          
SEQRES  80 E 1073  VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR          
SEQRES  81 E 1073  ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA          
SEQRES  82 E 1073  LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN          
SEQRES  83 E 1073  GLU MET HIS ALA GLN ILE LYS                                  
SEQRES   1 F  382  MET ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR          
SEQRES   2 F  382  GLN PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA          
SEQRES   3 F  382  VAL GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR          
SEQRES   4 F  382  GLN GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE          
SEQRES   5 F  382  VAL THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR          
SEQRES   6 F  382  ASN ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN          
SEQRES   7 F  382  GLY LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN          
SEQRES   8 F  382  PHE ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG          
SEQRES   9 F  382  HIS ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS          
SEQRES  10 F  382  LEU THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY          
SEQRES  11 F  382  CYS ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA          
SEQRES  12 F  382  LEU GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET          
SEQRES  13 F  382  ASP LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER          
SEQRES  14 F  382  TRP THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO          
SEQRES  15 F  382  GLU ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL          
SEQRES  16 F  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET          
SEQRES  17 F  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA          
SEQRES  18 F  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP          
SEQRES  19 F  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO          
SEQRES  20 F  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 F  382  THR ASP ILE PRO VAL PHE GLY ILE CYG LEU GLY HIS GLN          
SEQRES  22 F  382  LEU LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET          
SEQRES  23 F  382  LYS PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP          
SEQRES  24 F  382  VAL GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS          
SEQRES  25 F  382  GLY PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU          
SEQRES  26 F  382  ARG VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN          
SEQRES  27 F  382  GLY ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN          
SEQRES  28 F  382  GLY HIS PRO GLU ALA SER PRO GLY PRO HIS ASP ALA ALA          
SEQRES  29 F  382  PRO LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR          
SEQRES  30 F  382  ARG LYS THR ALA LYS                                          
SEQRES   1 G 1073  MET PRO LYS ARG THR ASP ILE LYS SER ILE LEU ILE LEU          
SEQRES   2 G 1073  GLY ALA GLY PRO ILE VAL ILE GLY GLN ALA CYS GLU PHE          
SEQRES   3 G 1073  ASP TYR SER GLY ALA GLN ALA CYS LYS ALA LEU ARG GLU          
SEQRES   4 G 1073  GLU GLY TYR ARG VAL ILE LEU VAL ASN SER ASN PRO ALA          
SEQRES   5 G 1073  THR ILE MET THR ASP PRO GLU MET ALA ASP ALA THR TYR          
SEQRES   6 G 1073  ILE GLU PRO ILE HIS TRP GLU VAL VAL ARG LYS ILE ILE          
SEQRES   7 G 1073  GLU LYS GLU ARG PRO ASP ALA VAL LEU PRO THR MET GLY          
SEQRES   8 G 1073  GLY GLN THR ALA LEU ASN CYS ALA LEU GLU LEU GLU ARG          
SEQRES   9 G 1073  GLN GLY VAL LEU GLU GLU PHE GLY VAL THR MET ILE GLY          
SEQRES  10 G 1073  ALA THR ALA ASP ALA ILE ASP LYS ALA GLU ASP ARG ARG          
SEQRES  11 G 1073  ARG PHE ASP VAL ALA MET LYS LYS ILE GLY LEU GLU THR          
SEQRES  12 G 1073  ALA ARG SER GLY ILE ALA HIS THR MET GLU GLU ALA LEU          
SEQRES  13 G 1073  ALA VAL ALA ALA ASP VAL GLY PHE PRO CYS ILE ILE ARG          
SEQRES  14 G 1073  PRO SER PHE THR MET GLY GLY SER GLY GLY GLY ILE ALA          
SEQRES  15 G 1073  TYR ASN ARG GLU GLU PHE GLU GLU ILE CYS ALA ARG GLY          
SEQRES  16 G 1073  LEU ASP LEU SER PRO THR LYS GLU LEU LEU ILE ASP GLU          
SEQRES  17 G 1073  SER LEU ILE GLY TRP LYS GLU TYR GLU MET GLU VAL VAL          
SEQRES  18 G 1073  ARG ASP LYS ASN ASP ASN CYS ILE ILE VAL CYS SER ILE          
SEQRES  19 G 1073  GLU ASN PHE ASP ALA MET GLY ILE HIS THR GLY ASP SER          
SEQRES  20 G 1073  ILE THR VAL ALA PRO ALA GLN THR LEU THR ASP LYS GLU          
SEQRES  21 G 1073  TYR GLN ILE MET ARG ASN ALA SER MET ALA VAL LEU ARG          
SEQRES  22 G 1073  GLU ILE GLY VAL GLU THR GLY GLY SER ASN VAL GLN PHE          
SEQRES  23 G 1073  ALA VAL ASN PRO LYS ASN GLY ARG LEU ILE VAL ILE GLU          
SEQRES  24 G 1073  MET ASN PRO ARG VAL SER ARG SER SER ALA LEU ALA SER          
SEQRES  25 G 1073  LYS ALA THR GLY PHE PRO ILE ALA LYS VAL ALA ALA LYS          
SEQRES  26 G 1073  LEU ALA VAL GLY TYR THR LEU ASP GLU LEU MET ASN ASP          
SEQRES  27 G 1073  ILE THR GLY GLY ARG THR PRO ALA SER PHE GLU PRO SER          
SEQRES  28 G 1073  ILE ASP TYR VAL VAL THR LYS ILE PRO ARG PHE ASN PHE          
SEQRES  29 G 1073  GLU LYS PHE ALA GLY ALA ASN ASP ARG LEU THR THR GLN          
SEQRES  30 G 1073  MET LYS SER VAL GLY GLU VAL MET ALA ILE GLY ARG THR          
SEQRES  31 G 1073  GLN GLN GLU SER LEU GLN LYS ALA LEU ARG GLY LEU GLU          
SEQRES  32 G 1073  VAL GLY ALA THR GLY PHE ASP PRO LYS VAL SER LEU ASP          
SEQRES  33 G 1073  ASP PRO GLU ALA LEU THR LYS ILE ARG ARG GLU LEU LYS          
SEQRES  34 G 1073  ASP ALA GLY ALA ASP ARG ILE TRP TYR ILE ALA ASP ALA          
SEQRES  35 G 1073  PHE ARG ALA GLY LEU SER VAL ASP GLY VAL PHE ASN LEU          
SEQRES  36 G 1073  THR ASN ILE ASP ARG TRP PHE LEU VAL GLN ILE GLU GLU          
SEQRES  37 G 1073  LEU VAL ARG LEU GLU GLU LYS VAL ALA GLU VAL GLY ILE          
SEQRES  38 G 1073  THR GLY LEU ASN ALA ASP PHE LEU ARG GLN LEU LYS ARG          
SEQRES  39 G 1073  LYS GLY PHE ALA ASP ALA ARG LEU ALA LYS LEU ALA GLY          
SEQRES  40 G 1073  VAL ARG GLU ALA GLU ILE ARG LYS LEU ARG ASP GLN TYR          
SEQRES  41 G 1073  ASP LEU HIS PRO VAL TYR LYS ARG VAL ASP THR CYS ALA          
SEQRES  42 G 1073  ALA GLU PHE ALA THR ASP THR ALA TYR MET TYR SER THR          
SEQRES  43 G 1073  TYR GLU GLU GLU CYS GLU ALA ASN PRO SER THR ASP ARG          
SEQRES  44 G 1073  GLU LYS ILE MET VAL LEU GLY GLY GLY PRO ASN ARG ILE          
SEQRES  45 G 1073  GLY GLN GLY ILE GLU PHE ASP TYR CYS CYS VAL HIS ALA          
SEQRES  46 G 1073  SER LEU ALA LEU ARG GLU ASP GLY TYR GLU THR ILE MET          
SEQRES  47 G 1073  VAL ASN CYS ASN PRO GLU THR VAL SER THR ASP TYR ASP          
SEQRES  48 G 1073  THR SER ASP ARG LEU TYR PHE GLU PRO VAL THR LEU GLU          
SEQRES  49 G 1073  ASP VAL LEU GLU ILE VAL ARG ILE GLU LYS PRO LYS GLY          
SEQRES  50 G 1073  VAL ILE VAL GLN TYR GLY GLY GLN THR PRO LEU LYS LEU          
SEQRES  51 G 1073  ALA ARG ALA LEU GLU ALA ALA GLY VAL PRO VAL ILE GLY          
SEQRES  52 G 1073  THR SER PRO ASP ALA ILE ASP ARG ALA GLU ASP ARG GLU          
SEQRES  53 G 1073  ARG PHE GLN HIS ALA VAL GLU ARG LEU LYS LEU LYS GLN          
SEQRES  54 G 1073  PRO ALA ASN ALA THR VAL THR ALA ILE GLU MET ALA VAL          
SEQRES  55 G 1073  GLU LYS ALA LYS GLU ILE GLY TYR PRO LEU VAL VAL ARG          
SEQRES  56 G 1073  PRO SER TYR VAL LEU GLY GLY ARG ALA MET GLU ILE VAL          
SEQRES  57 G 1073  TYR ASP GLU ALA ASP LEU ARG ARG TYR PHE GLN THR ALA          
SEQRES  58 G 1073  VAL SER VAL SER ASN ASP ALA PRO VAL LEU LEU ASP HIS          
SEQRES  59 G 1073  PHE LEU ASP ASP ALA VAL GLU VAL ASP VAL ASP ALA ILE          
SEQRES  60 G 1073  CYS ASP GLY GLU MET VAL LEU ILE GLY GLY ILE MET GLU          
SEQRES  61 G 1073  HIS ILE GLU GLN ALA GLY VAL HIS SER GLY ASP SER ALA          
SEQRES  62 G 1073  CYS SER LEU PRO ALA TYR THR LEU SER GLN GLU ILE GLN          
SEQRES  63 G 1073  ASP VAL MET ARG GLN GLN VAL GLN LYS LEU ALA PHE GLU          
SEQRES  64 G 1073  LEU GLN VAL ARG GLY LEU MET ASN VAL GLN PHE ALA VAL          
SEQRES  65 G 1073  LYS ASN ASN GLU VAL TYR LEU ILE GLU VAL ASN PRO ARG          
SEQRES  66 G 1073  ALA ALA ARG THR VAL PRO PHE VAL SER LYS ALA THR GLY          
SEQRES  67 G 1073  VAL PRO LEU ALA LYS VAL ALA ALA ARG VAL MET ALA GLY          
SEQRES  68 G 1073  LYS SER LEU ALA GLU GLN GLY VAL THR LYS GLU VAL ILE          
SEQRES  69 G 1073  PRO PRO TYR TYR SER VAL LYS GLU VAL VAL LEU PRO PHE          
SEQRES  70 G 1073  ASN LYS PHE PRO GLY VAL ASP PRO LEU LEU GLY PRO GLU          
SEQRES  71 G 1073  MET ARG SER THR GLY GLU VAL MET GLY VAL GLY ARG THR          
SEQRES  72 G 1073  PHE ALA GLU ALA PHE ALA LYS ALA GLN LEU GLY SER ASN          
SEQRES  73 G 1073  SER THR MET LYS LYS HIS GLY ARG ALA LEU LEU SER VAL          
SEQRES  74 G 1073  ARG GLU GLY ASP LYS GLU ARG VAL VAL ASP LEU ALA ALA          
SEQRES  75 G 1073  LYS LEU LEU LYS GLN GLY PHE GLU LEU ASP ALA THR HIS          
SEQRES  76 G 1073  GLY THR ALA ILE VAL LEU GLY GLU ALA GLY ILE ASN PRO          
SEQRES  77 G 1073  ARG LEU VAL ASN LYS VAL HIS GLU GLY ARG PRO HIS ILE          
SEQRES  78 G 1073  GLN ASP ARG ILE LYS ASN GLY GLU TYR THR TYR ILE ILE          
SEQRES  79 G 1073  ASN THR THR SER GLY ARG ARG ALA ILE GLU ASP SER ARG          
SEQRES  80 G 1073  VAL ILE ARG ARG SER ALA LEU GLN TYR LYS VAL HIS TYR          
SEQRES  81 G 1073  ASP THR THR LEU ASN GLY GLY PHE ALA THR ALA MET ALA          
SEQRES  82 G 1073  LEU ASN ALA ASP ALA THR GLU LYS VAL ILE SER VAL GLN          
SEQRES  83 G 1073  GLU MET HIS ALA GLN ILE LYS                                  
SEQRES   1 H  382  MET ILE LYS SER ALA LEU LEU VAL LEU GLU ASP GLY THR          
SEQRES   2 H  382  GLN PHE HIS GLY ARG ALA ILE GLY ALA THR GLY SER ALA          
SEQRES   3 H  382  VAL GLY GLU VAL VAL PHE ASN THR SER MET THR GLY TYR          
SEQRES   4 H  382  GLN GLU ILE LEU THR ASP PRO SER TYR SER ARG GLN ILE          
SEQRES   5 H  382  VAL THR LEU THR TYR PRO HIS ILE GLY ASN VAL GLY THR          
SEQRES   6 H  382  ASN ASP ALA ASP GLU GLU SER SER GLN VAL HIS ALA GLN          
SEQRES   7 H  382  GLY LEU VAL ILE ARG ASP LEU PRO LEU ILE ALA SER ASN          
SEQRES   8 H  382  PHE ARG ASN THR GLU ASP LEU SER SER TYR LEU LYS ARG          
SEQRES   9 H  382  HIS ASN ILE VAL ALA ILE ALA ASP ILE ASP THR ARG LYS          
SEQRES  10 H  382  LEU THR ARG LEU LEU ARG GLU LYS GLY ALA GLN ASN GLY          
SEQRES  11 H  382  CYS ILE ILE ALA GLY ASP ASN PRO ASP ALA ALA LEU ALA          
SEQRES  12 H  382  LEU GLU LYS ALA ARG ALA PHE PRO GLY LEU ASN GLY MET          
SEQRES  13 H  382  ASP LEU ALA LYS GLU VAL THR THR ALA GLU ALA TYR SER          
SEQRES  14 H  382  TRP THR GLN GLY SER TRP THR LEU THR GLY GLY LEU PRO          
SEQRES  15 H  382  GLU ALA LYS LYS GLU ASP GLU LEU PRO PHE HIS VAL VAL          
SEQRES  16 H  382  ALA TYR ASP PHE GLY ALA LYS ARG ASN ILE LEU ARG MET          
SEQRES  17 H  382  LEU VAL ASP ARG GLY CYS ARG LEU THR ILE VAL PRO ALA          
SEQRES  18 H  382  GLN THR SER ALA GLU ASP VAL LEU LYS MET ASN PRO ASP          
SEQRES  19 H  382  GLY ILE PHE LEU SER ASN GLY PRO GLY ASP PRO ALA PRO          
SEQRES  20 H  382  CYS ASP TYR ALA ILE THR ALA ILE GLN LYS PHE LEU GLU          
SEQRES  21 H  382  THR ASP ILE PRO VAL PHE GLY ILE CYG LEU GLY HIS GLN          
SEQRES  22 H  382  LEU LEU ALA LEU ALA SER GLY ALA LYS THR VAL LYS MET          
SEQRES  23 H  382  LYS PHE GLY HIS HIS GLY GLY ASN HIS PRO VAL LYS ASP          
SEQRES  24 H  382  VAL GLU LYS ASN VAL VAL MET ILE THR ALA GLN ASN HIS          
SEQRES  25 H  382  GLY PHE ALA VAL ASP GLU ALA THR LEU PRO ALA ASN LEU          
SEQRES  26 H  382  ARG VAL THR HIS LYS SER LEU PHE ASP GLY THR LEU GLN          
SEQRES  27 H  382  GLY ILE HIS ARG THR ASP LYS PRO ALA PHE SER PHE GLN          
SEQRES  28 H  382  GLY HIS PRO GLU ALA SER PRO GLY PRO HIS ASP ALA ALA          
SEQRES  29 H  382  PRO LEU PHE ASP HIS PHE ILE GLU LEU ILE GLU GLN TYR          
SEQRES  30 H  382  ARG LYS THR ALA LYS                                          
MODRES 1CS0 CYG B  269  CYS                                                     
MODRES 1CS0 CYG D  269  CYS                                                     
MODRES 1CS0 CYG F  269  CYS                                                     
MODRES 1CS0 CYG H  269  CYS                                                     
HET    CYG  B 269      15                                                       
HET    CYG  D 269      15                                                       
HET    CYG  F 269      15                                                       
HET    CYG  H 269      15                                                       
HET     MN  A5001       1                                                       
HET     MN  A5002       1                                                       
HET      K  A5003       1                                                       
HET      K  A5004       1                                                       
HET     MN  A5007       1                                                       
HET      K  A5008       1                                                       
HET      K  A5009       1                                                       
HET     CL  A5011       1                                                       
HET     CL  A5012       1                                                       
HET     CL  A5013       1                                                       
HET     CL  A5014       1                                                       
HET     CL  A5015       1                                                       
HET     CL  B5016       1                                                       
HET     CL  B5017       1                                                       
HET     CL  A5018       1                                                       
HET      K  A5019       1                                                       
HET      K  B5020       1                                                       
HET      K  A5021       1                                                       
HET      K  A5022       1                                                       
HET     CL  E5058       1                                                       
HET      K  G5090       1                                                       
HET     MN  C5024       1                                                       
HET     CL  E5059       1                                                       
HET      K  H5091       1                                                       
HET     MN  C5025       1                                                       
HET     CL  E5060       1                                                       
HET      K  G5092       1                                                       
HET      K  C5026       1                                                       
HET     CL  E5061       1                                                       
HET      K  G5093       1                                                       
HET      K  C5027       1                                                       
HET     CL  E5062       1                                                       
HET     MN  C5030       1                                                       
HET     CL  F5063       1                                                       
HET      K  C5031       1                                                       
HET     CL  F5064       1                                                       
HET      K  C5032       1                                                       
HET      K  E5065       1                                                       
HET     CL  C5035       1                                                       
HET      K  F5066       1                                                       
HET     CL  C5036       1                                                       
HET      K  E5067       1                                                       
HET     CL  C5037       1                                                       
HET      K  E5068       1                                                       
HET     CL  C5038       1                                                       
HET      K  E5069       1                                                       
HET     CL  C5039       1                                                       
HET     MN  G5072       1                                                       
HET     CL  D5040       1                                                       
HET     MN  G5073       1                                                       
HET     CL  D5041       1                                                       
HET      K  G5074       1                                                       
HET      K  C5042       1                                                       
HET      K  G5075       1                                                       
HET      K  D5043       1                                                       
HET     MN  G5078       1                                                       
HET      K  C5044       1                                                       
HET      K  G5079       1                                                       
HET      K  C5045       1                                                       
HET      K  G5080       1                                                       
HET     MN  E5047       1                                                       
HET     CL  G5083       1                                                       
HET     MN  E5048       1                                                       
HET     CL  G5084       1                                                       
HET      K  E5049       1                                                       
HET     CL  G5085       1                                                       
HET      K  E5050       1                                                       
HET     CL  G5086       1                                                       
HET     MN  E5053       1                                                       
HET     CL  G5087       1                                                       
HET      K  E5054       1                                                       
HET     CL  H5088       1                                                       
HET      K  E5055       1                                                       
HET     CL  H5089       1                                                       
HET    PO4  A5005       5                                                       
HET    PO4  C5028       5                                                       
HET    PO4  E5051       5                                                       
HET    PO4  E5070       5                                                       
HET    PO4  G5076       5                                                       
HET    ADP  A5000      27                                                       
HET    ADP  A5006      27                                                       
HET    ORN  A5010       9                                                       
HET    NET  A5094       9                                                       
HET    ADP  C5023      27                                                       
HET    ADP  C5029      27                                                       
HET    ORN  C5033       9                                                       
HET    NET  C5034       9                                                       
HET    ADP  E5046      27                                                       
HET    ADP  E5052      27                                                       
HET    ORN  E5056       9                                                       
HET    NET  E5057       9                                                       
HET    ADP  G5071      27                                                       
HET    ADP  G5077      27                                                       
HET    ORN  G5081       9                                                       
HET    NET  G5082       9                                                       
HETNAM     CYG 2-AMINO-4-(AMINO-3-OXO-PROPYLSULFANYLCARBONYL)-BUTYRIC           
HETNAM   2 CYG  ACID                                                            
HETNAM      MN MANGANESE (II) ION                                               
HETNAM       K POTASSIUM ION                                                    
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PO4 PHOSPHATE ION                                                    
HETNAM     ADP ADENOSINE-5'-DIPHOSPHATE                                         
HETNAM     ORN L-ORNITHINE                                                      
HETNAM     NET TETRAETHYLAMMONIUM ION                                           
FORMUL   2  CYG    4(C8 H14 N2 O5 S)                                            
FORMUL   9   MN    12(MN 2+)                                                    
FORMUL  11    K    33(K 1+)                                                     
FORMUL  16   CL    29(CL 1-)                                                    
FORMUL  83  PO4    5(O4 P 3-)                                                   
FORMUL  88  ADP    8(C10 H15 N5 O10 P2)                                         
FORMUL  90  ORN    4(C5 H12 N2 O2)                                              
FORMUL  91  NET    4(C8 H20 N 1+)                                               
FORMUL  10  HOH   *4176(H2 O)                                                   
HELIX    1   1 CYS A   24  GLU A   40  1                                  17    
HELIX    2   2 THR A   53  ASP A   57  5                                   5    
HELIX    3   3 ASP A   57  ALA A   61  5                                   5    
HELIX    4   4 HIS A   70  ARG A   82  1                                  13    
HELIX    5   5 GLY A   91  GLN A  105  1                                  15    
HELIX    6   6 GLY A  106  GLY A  112  1                                   7    
HELIX    7   7 THR A  119  ASP A  128  1                                  10    
HELIX    8   8 ASP A  128  ILE A  139  1                                  12    
HELIX    9   9 THR A  151  GLY A  163  1                                  13    
HELIX   10  10 ASN A  184  SER A  199  1                                  16    
HELIX   11  11 HIS A  243  SER A  247  5                                   5    
HELIX   12  12 THR A  257  GLY A  276  1                                  20    
HELIX   13  13 SER A  305  GLY A  316  1                                  12    
HELIX   14  14 PRO A  318  VAL A  328  1                                  11    
HELIX   15  15 THR A  331  LEU A  335  5                                   5    
HELIX   16  16 ASN A  337  GLY A  341  5                                   5    
HELIX   17  17 ASN A  363  PHE A  367  5                                   5    
HELIX   18  18 THR A  390  LEU A  402  1                                  13    
HELIX   19  19 GLU A  419  ASP A  430  1                                  12    
HELIX   20  20 ASP A  434  ALA A  445  1                                  12    
HELIX   21  21 SER A  448  ASN A  457  1                                  10    
HELIX   22  22 ASP A  459  GLY A  480  1                                  22    
HELIX   23  23 ILE A  481  LEU A  484  5                                   4    
HELIX   24  24 ASN A  485  LYS A  495  1                                  11    
HELIX   25  25 ALA A  498  GLY A  507  1                                  10    
HELIX   26  26 ARG A  509  ASP A  521  1                                  13    
HELIX   27  27 GLY A  575  ASP A  592  1                                  18    
HELIX   28  28 THR A  605  ASP A  609  5                                   5    
HELIX   29  29 THR A  622  LYS A  634  1                                  13    
HELIX   30  30 GLY A  644  LYS A  649  1                                   6    
HELIX   31  31 LEU A  650  ALA A  657  1                                   8    
HELIX   32  32 SER A  665  ASP A  674  1                                  10    
HELIX   33  33 ASP A  674  LEU A  685  1                                  12    
HELIX   34  34 ALA A  697  GLY A  709  1                                  13    
HELIX   35  35 ASP A  730  ALA A  741  1                                  12    
HELIX   36  36 HIS A  788  SER A  792  5                                   5    
HELIX   37  37 SER A  802  LEU A  820  1                                  19    
HELIX   38  38 THR A  849  GLY A  858  1                                  10    
HELIX   39  39 PRO A  860  ALA A  870  1                                  11    
HELIX   40  40 SER A  873  GLY A  878  1                                   6    
HELIX   41  41 LEU A  895  PHE A  900  5                                   6    
HELIX   42  42 THR A  923  SER A  935  1                                  13    
HELIX   43  43 ARG A  950  GLU A  955  1                                   6    
HELIX   44  44 ARG A  956  GLY A  968  1                                  13    
HELIX   45  45 HIS A  975  ALA A  984  1                                  10    
HELIX   46  46 HIS A 1000  ASN A 1007  1                                   8    
HELIX   47  47 GLY A 1019  TYR A 1036  1                                  18    
HELIX   48  48 THR A 1043  ASN A 1055  1                                  13    
HELIX   49  49 SER A 1064  GLN A 1071  1                                   8    
HELIX   50  50 GLY B   38  THR B   44  1                                   7    
HELIX   51  51 ASP B   45  TYR B   48  5                                   4    
HELIX   52  52 ASN B   66  GLU B   70  5                                   5    
HELIX   53  53 ASP B   97  HIS B  105  1                                   9    
HELIX   54  54 ASP B  114  GLY B  126  1                                  13    
HELIX   55  55 ASP B  139  PHE B  150  1                                  12    
HELIX   56  56 LEU B  158  THR B  163  1                                   6    
HELIX   57  57 LYS B  186  LEU B  190  5                                   5    
HELIX   58  58 LYS B  202  ARG B  212  1                                  11    
HELIX   59  59 SER B  224  LYS B  230  1                                   7    
HELIX   60  60 CYS B  248  LEU B  259  1                                  12    
HELIX   61  61 LEU B  270  SER B  279  1                                  10    
HELIX   62  62 GLU B  318  LEU B  321  5                                   4    
HELIX   63  63 ALA B  364  LYS B  379  1                                  16    
HELIX   64  64 CYS C   24  GLU C   40  1                                  17    
HELIX   65  65 THR C   53  ASP C   57  5                                   5    
HELIX   66  66 ASP C   57  ALA C   61  5                                   5    
HELIX   67  67 HIS C   70  ARG C   82  1                                  13    
HELIX   68  68 GLY C   91  GLN C  105  1                                  15    
HELIX   69  69 GLY C  106  PHE C  111  1                                   6    
HELIX   70  70 THR C  119  ASP C  128  1                                  10    
HELIX   71  71 ASP C  128  ILE C  139  1                                  12    
HELIX   72  72 THR C  151  GLY C  163  1                                  13    
HELIX   73  73 ASN C  184  SER C  199  1                                  16    
HELIX   74  74 HIS C  243  SER C  247  5                                   5    
HELIX   75  75 THR C  257  GLY C  276  1                                  20    
HELIX   76  76 SER C  305  GLY C  316  1                                  12    
HELIX   77  77 PRO C  318  VAL C  328  1                                  11    
HELIX   78  78 THR C  331  LEU C  335  5                                   5    
HELIX   79  79 ASN C  337  GLY C  341  5                                   5    
HELIX   80  80 ASN C  363  PHE C  367  5                                   5    
HELIX   81  81 THR C  390  LEU C  402  1                                  13    
HELIX   82  82 GLU C  419  ASP C  430  1                                  12    
HELIX   83  83 ASP C  434  ALA C  445  1                                  12    
HELIX   84  84 SER C  448  ASN C  457  1                                  10    
HELIX   85  85 ASP C  459  GLY C  480  1                                  22    
HELIX   86  86 ILE C  481  LEU C  484  5                                   4    
HELIX   87  87 ASN C  485  LYS C  495  1                                  11    
HELIX   88  88 ALA C  498  GLY C  507  1                                  10    
HELIX   89  89 ARG C  509  ASP C  521  1                                  13    
HELIX   90  90 GLY C  575  ASP C  592  1                                  18    
HELIX   91  91 THR C  605  ASP C  609  5                                   5    
HELIX   92  92 ASP C  609  SER C  613  5                                   5    
HELIX   93  93 THR C  622  LYS C  634  1                                  13    
HELIX   94  94 GLY C  644  ALA C  657  1                                  14    
HELIX   95  95 SER C  665  ASP C  674  1                                  10    
HELIX   96  96 ASP C  674  LEU C  685  1                                  12    
HELIX   97  97 ALA C  697  GLY C  709  1                                  13    
HELIX   98  98 ASP C  730  ALA C  741  1                                  12    
HELIX   99  99 HIS C  788  SER C  792  5                                   5    
HELIX  100 100 SER C  802  GLN C  821  1                                  20    
HELIX  101 101 THR C  849  GLY C  858  1                                  10    
HELIX  102 102 PRO C  860  ALA C  870  1                                  11    
HELIX  103 103 SER C  873  GLY C  878  1                                   6    
HELIX  104 104 LEU C  895  PHE C  900  5                                   6    
HELIX  105 105 THR C  923  SER C  935  1                                  13    
HELIX  106 106 ARG C  950  GLN C  967  1                                  18    
HELIX  107 107 THR C  974  ALA C  984  1                                  11    
HELIX  108 108 HIS C 1000  GLY C 1008  1                                   9    
HELIX  109 109 GLY C 1019  LYS C 1037  1                                  19    
HELIX  110 110 THR C 1043  LEU C 1054  1                                  12    
HELIX  111 111 SER C 1064  GLN C 1071  1                                   8    
HELIX  112 112 GLY D   38  THR D   44  1                                   7    
HELIX  113 113 ASP D   45  TYR D   48  5                                   4    
HELIX  114 114 ASN D   66  GLU D   70  5                                   5    
HELIX  115 115 ASP D   97  HIS D  105  1                                   9    
HELIX  116 116 ASP D  114  GLY D  126  1                                  13    
HELIX  117 117 ASP D  139  PHE D  150  1                                  12    
HELIX  118 118 LEU D  158  THR D  163  1                                   6    
HELIX  119 119 LYS D  186  LEU D  190  5                                   5    
HELIX  120 120 LYS D  202  ARG D  212  1                                  11    
HELIX  121 121 SER D  224  LYS D  230  1                                   7    
HELIX  122 122 CYS D  248  LEU D  259  1                                  12    
HELIX  123 123 LEU D  270  SER D  279  1                                  10    
HELIX  124 124 GLU D  318  LEU D  321  5                                   4    
HELIX  125 125 PRO D  360  ALA D  363  5                                   4    
HELIX  126 126 ALA D  364  THR D  380  1                                  17    
HELIX  127 127 CYS E   24  GLU E   40  1                                  17    
HELIX  128 128 THR E   53  ASP E   57  5                                   5    
HELIX  129 129 ASP E   57  ALA E   61  5                                   5    
HELIX  130 130 HIS E   70  ARG E   82  1                                  13    
HELIX  131 131 GLY E   91  GLN E  105  1                                  15    
HELIX  132 132 GLY E  106  PHE E  111  1                                   6    
HELIX  133 133 THR E  119  ASP E  128  1                                  10    
HELIX  134 134 ASP E  128  ILE E  139  1                                  12    
HELIX  135 135 THR E  151  GLY E  163  1                                  13    
HELIX  136 136 ASN E  184  SER E  199  1                                  16    
HELIX  137 137 HIS E  243  SER E  247  5                                   5    
HELIX  138 138 THR E  257  GLY E  276  1                                  20    
HELIX  139 139 SER E  305  GLY E  316  1                                  12    
HELIX  140 140 PRO E  318  ALA E  327  1                                  10    
HELIX  141 141 ASN E  337  GLY E  341  5                                   5    
HELIX  142 142 ASN E  363  PHE E  367  5                                   5    
HELIX  143 143 THR E  390  LEU E  402  1                                  13    
HELIX  144 144 GLU E  419  ASP E  430  1                                  12    
HELIX  145 145 ASP E  434  ALA E  445  1                                  12    
HELIX  146 146 SER E  448  ASN E  457  1                                  10    
HELIX  147 147 ASP E  459  GLY E  480  1                                  22    
HELIX  148 148 ILE E  481  LEU E  484  5                                   4    
HELIX  149 149 ASN E  485  LYS E  495  1                                  11    
HELIX  150 150 ALA E  498  GLY E  507  1                                  10    
HELIX  151 151 ARG E  509  ASP E  521  1                                  13    
HELIX  152 152 GLY E  575  GLY E  593  1                                  19    
HELIX  153 153 THR E  605  ASP E  609  5                                   5    
HELIX  154 154 ASP E  609  SER E  613  5                                   5    
HELIX  155 155 THR E  622  LYS E  634  1                                  13    
HELIX  156 156 GLY E  644  LYS E  649  1                                   6    
HELIX  157 157 LEU E  650  ALA E  657  1                                   8    
HELIX  158 158 SER E  665  ASP E  674  1                                  10    
HELIX  159 159 ASP E  674  LEU E  685  1                                  12    
HELIX  160 160 ALA E  697  GLY E  709  1                                  13    
HELIX  161 161 ASP E  730  ALA E  741  1                                  12    
HELIX  162 162 HIS E  788  SER E  792  5                                   5    
HELIX  163 163 SER E  802  GLN E  821  1                                  20    
HELIX  164 164 THR E  849  GLY E  858  1                                  10    
HELIX  165 165 PRO E  860  ALA E  870  1                                  11    
HELIX  166 166 SER E  873  GLY E  878  1                                   6    
HELIX  167 167 LEU E  895  PHE E  900  5                                   6    
HELIX  168 168 THR E  923  SER E  935  1                                  13    
HELIX  169 169 ARG E  956  GLN E  967  1                                  12    
HELIX  170 170 THR E  974  ALA E  984  1                                  11    
HELIX  171 171 LYS E  993  GLY E  997  5                                   5    
HELIX  172 172 HIS E 1000  ASN E 1007  1                                   8    
HELIX  173 173 GLY E 1019  TYR E 1036  1                                  18    
HELIX  174 174 THR E 1043  LEU E 1054  1                                  12    
HELIX  175 175 SER E 1064  GLN E 1071  1                                   8    
HELIX  176 176 GLY F   38  THR F   44  1                                   7    
HELIX  177 177 ASP F   45  TYR F   48  5                                   4    
HELIX  178 178 ASN F   66  GLU F   70  5                                   5    
HELIX  179 179 ASP F   97  HIS F  105  1                                   9    
HELIX  180 180 ASP F  114  GLY F  126  1                                  13    
HELIX  181 181 ASP F  139  PHE F  150  1                                  12    
HELIX  182 182 LEU F  158  THR F  163  1                                   6    
HELIX  183 183 LYS F  186  LEU F  190  5                                   5    
HELIX  184 184 LYS F  202  ARG F  212  1                                  11    
HELIX  185 185 SER F  224  LYS F  230  1                                   7    
HELIX  186 186 CYS F  248  LEU F  259  1                                  12    
HELIX  187 187 LEU F  270  SER F  279  1                                  10    
HELIX  188 188 GLU F  318  LEU F  321  5                                   4    
HELIX  189 189 PRO F  365  THR F  380  1                                  16    
HELIX  190 190 CYS G   24  GLU G   40  1                                  17    
HELIX  191 191 THR G   53  ASP G   57  5                                   5    
HELIX  192 192 ASP G   57  ALA G   61  5                                   5    
HELIX  193 193 HIS G   70  ARG G   82  1                                  13    
HELIX  194 194 GLY G   91  GLN G  105  1                                  15    
HELIX  195 195 GLY G  106  PHE G  111  1                                   6    
HELIX  196 196 THR G  119  ASP G  128  1                                  10    
HELIX  197 197 ASP G  128  ILE G  139  1                                  12    
HELIX  198 198 THR G  151  GLY G  163  1                                  13    
HELIX  199 199 ASN G  184  SER G  199  1                                  16    
HELIX  200 200 HIS G  243  SER G  247  5                                   5    
HELIX  201 201 THR G  257  GLY G  276  1                                  20    
HELIX  202 202 SER G  305  GLY G  316  1                                  12    
HELIX  203 203 PRO G  318  VAL G  328  1                                  11    
HELIX  204 204 THR G  331  LEU G  335  5                                   5    
HELIX  205 205 ASN G  337  GLY G  341  5                                   5    
HELIX  206 206 ASN G  363  PHE G  367  5                                   5    
HELIX  207 207 THR G  390  LEU G  402  1                                  13    
HELIX  208 208 GLU G  419  ASP G  430  1                                  12    
HELIX  209 209 ASP G  434  ALA G  445  1                                  12    
HELIX  210 210 SER G  448  ASN G  457  1                                  10    
HELIX  211 211 ASP G  459  GLY G  480  1                                  22    
HELIX  212 212 ILE G  481  LEU G  484  5                                   4    
HELIX  213 213 ASN G  485  LYS G  495  1                                  11    
HELIX  214 214 ALA G  498  GLY G  507  1                                  10    
HELIX  215 215 ARG G  509  TYR G  520  1                                  12    
HELIX  216 216 GLY G  575  ASP G  592  1                                  18    
HELIX  217 217 THR G  605  ASP G  609  5                                   5    
HELIX  218 218 ASP G  609  SER G  613  5                                   5    
HELIX  219 219 THR G  622  LYS G  634  1                                  13    
HELIX  220 220 GLY G  644  LYS G  649  1                                   6    
HELIX  221 221 LEU G  650  ALA G  657  1                                   8    
HELIX  222 222 SER G  665  ASP G  674  1                                  10    
HELIX  223 223 ASP G  674  LEU G  685  1                                  12    
HELIX  224 224 ALA G  697  GLY G  709  1                                  13    
HELIX  225 225 ASP G  730  ALA G  741  1                                  12    
HELIX  226 226 HIS G  788  SER G  792  5                                   5    
HELIX  227 227 SER G  802  LEU G  820  1                                  19    
HELIX  228 228 THR G  849  GLY G  858  1                                  10    
HELIX  229 229 PRO G  860  ALA G  870  1                                  11    
HELIX  230 230 SER G  873  GLY G  878  1                                   6    
HELIX  231 231 LEU G  895  PHE G  900  5                                   6    
HELIX  232 232 THR G  923  SER G  935  1                                  13    
HELIX  233 233 ARG G  950  GLU G  955  1                                   6    
HELIX  234 234 ARG G  956  GLN G  967  1                                  12    
HELIX  235 235 HIS G  975  ALA G  984  1                                  10    
HELIX  236 236 LYS G  993  GLY G  997  5                                   5    
HELIX  237 237 HIS G 1000  ASN G 1007  1                                   8    
HELIX  238 238 GLY G 1019  TYR G 1036  1                                  18    
HELIX  239 239 THR G 1043  ALA G 1053  1                                  11    
HELIX  240 240 LEU G 1054  ALA G 1056  5                                   3    
HELIX  241 241 SER G 1064  GLN G 1071  1                                   8    
HELIX  242 242 GLY H   38  THR H   44  1                                   7    
HELIX  243 243 ASP H   45  TYR H   48  5                                   4    
HELIX  244 244 ASN H   66  GLU H   70  5                                   5    
HELIX  245 245 ASP H   97  HIS H  105  1                                   9    
HELIX  246 246 ASP H  114  GLY H  126  1                                  13    
HELIX  247 247 ASP H  139  PHE H  150  1                                  12    
HELIX  248 248 LEU H  158  THR H  163  1                                   6    
HELIX  249 249 LYS H  186  LEU H  190  5                                   5    
HELIX  250 250 LYS H  202  ARG H  212  1                                  11    
HELIX  251 251 SER H  224  LYS H  230  1                                   7    
HELIX  252 252 CYS H  248  LEU H  259  1                                  12    
HELIX  253 253 LEU H  270  GLY H  280  1                                  11    
HELIX  254 254 GLU H  318  LEU H  321  5                                   4    
HELIX  255 255 PRO H  360  ALA H  363  5                                   4    
HELIX  256 256 ALA H  364  ARG H  378  1                                  15    
SHEET    1   A 5 ALA A  63  TYR A  65  0                                        
SHEET    2   A 5 ARG A  43  VAL A  47  1  O  VAL A  44   N  ALA A  63           
SHEET    3   A 5 SER A   9  LEU A  13  1  O  ILE A  10   N  ILE A  45           
SHEET    4   A 5 ALA A  85  LEU A  87  1  O  ALA A  85   N  LEU A  11           
SHEET    5   A 5 THR A 114  MET A 115  1  O  THR A 114   N  VAL A  86           
SHEET    1   B 4 SER A 146  ALA A 149  0                                        
SHEET    2   B 4 LEU A 204  GLU A 208 -1  O  LEU A 204   N  ALA A 149           
SHEET    3   B 4 CYS A 166  PRO A 170 -1  N  ILE A 167   O  ASP A 207           
SHEET    4   B 4 GLY A 180  ALA A 182 -1  O  GLY A 180   N  ILE A 168           
SHEET    1   C 7 LEU A 295  ASN A 301  0                                        
SHEET    2   C 7 GLY A 280  VAL A 288 -1  O  ASN A 283   N  ASN A 301           
SHEET    3   C 7 LYS A 214  ARG A 222 -1  N  LYS A 214   O  VAL A 288           
SHEET    4   C 7 CYS A 228  ASN A 236 -1  N  ILE A 229   O  VAL A 221           
SHEET    5   C 7 THR A 249  ALA A 251 -1  N  VAL A 250   O  GLU A 235           
SHEET    6   C 7 VAL A 355  ARG A 361 -1  N  VAL A 356   O  ALA A 251           
SHEET    7   C 7 GLY A 382  GLY A 388 -1  O  GLY A 382   N  ARG A 361           
SHEET    1   D 7 VAL A 525  ARG A 528  0                                        
SHEET    2   D 7 TYR A 542  THR A 546 -1  O  TYR A 544   N  LYS A 527           
SHEET    3   D 7 ARG A 615  PHE A 618  1  O  LEU A 616   N  MET A 543           
SHEET    4   D 7 GLU A 595  ASN A 600  1  O  THR A 596   N  ARG A 615           
SHEET    5   D 7 LYS A 561  LEU A 565  1  O  ILE A 562   N  ILE A 597           
SHEET    6   D 7 GLY A 637  ILE A 639  1  O  GLY A 637   N  MET A 563           
SHEET    7   D 7 VAL A 661  ILE A 662  1  N  ILE A 662   O  VAL A 638           
SHEET    1   E 4 ASN A 692  THR A 694  0                                        
SHEET    2   E 4 LEU A 751  HIS A 754 -1  N  LEU A 752   O  ALA A 693           
SHEET    3   E 4 LEU A 712  ARG A 715 -1  N  VAL A 713   O  ASP A 753           
SHEET    4   E 4 GLU A 726  VAL A 728 -1  O  GLU A 726   N  VAL A 714           
SHEET    1   F 7 GLU A 836  ASN A 843  0                                        
SHEET    2   F 7 GLY A 824  LYS A 833 -1  O  ASN A 827   N  ASN A 843           
SHEET    3   F 7 VAL A 760  CYS A 768 -1  O  VAL A 760   N  VAL A 832           
SHEET    4   F 7 VAL A 773  GLN A 784 -1  N  LEU A 774   O  ILE A 767           
SHEET    5   F 7 CYS A 794  LEU A 796 -1  N  SER A 795   O  GLU A 780           
SHEET    6   F 7 TYR A 888  VAL A 894 -1  N  SER A 889   O  LEU A 796           
SHEET    7   F 7 GLY A 915  GLY A 921 -1  O  GLY A 915   N  VAL A 894           
SHEET    1   G 5 ARG A 989  VAL A 991  0                                        
SHEET    2   G 5 PHE A 969  THR A 974  1  O  LEU A 971   N  ARG A 989           
SHEET    3   G 5 GLY A 943  SER A 948  1  O  GLY A 943   N  GLU A 970           
SHEET    4   G 5 TYR A1012  ASN A1015  1  O  TYR A1012   N  LEU A 946           
SHEET    5   G 5 HIS A1039  ASP A1041  1  O  HIS A1039   N  ILE A1013           
SHEET    1   H 8 SER B   4  LEU B   9  0                                        
SHEET    2   H 8 GLN B  14  ALA B  19 -1  N  PHE B  15   O  LEU B   7           
SHEET    3   H 8 VAL B 108  ALA B 111 -1  O  ALA B 111   N  ARG B  18           
SHEET    4   H 8 GLY B  79  VAL B  81  1  O  LEU B  80   N  ILE B 110           
SHEET    5   H 8 GLN B  51  LEU B  55  1  O  GLN B  51   N  GLY B  79           
SHEET    6   H 8 GLY B  24  ASN B  33  1  O  GLU B  29   N  ILE B  52           
SHEET    7   H 8 GLN B 128  ALA B 134 -1  O  GLN B 128   N  VAL B  30           
SHEET    8   H 8 SER B   4  LEU B   9 -1  N  LEU B   6   O  ILE B 133           
SHEET    1   I10 TYR B 168  TRP B 170  0                                        
SHEET    2   I10 CYS B 214  PRO B 220 -1  N  LEU B 216   O  TRP B 170           
SHEET    3   I10 PHE B 192  ASP B 198  1  O  PHE B 192   N  ARG B 215           
SHEET    4   I10 GLY B 235  LEU B 238  1  O  GLY B 235   N  VAL B 195           
SHEET    5   I10 VAL B 265  GLY B 267  1  O  PHE B 266   N  LEU B 238           
SHEET    6   I10 ALA B 347  PHE B 350  1  N  PHE B 348   O  VAL B 265           
SHEET    7   I10 LEU B 337  ARG B 342 -1  O  ILE B 340   N  SER B 349           
SHEET    8   I10 LEU B 325  SER B 331 -1  N  ARG B 326   O  HIS B 341           
SHEET    9   I10 THR B 283  ASP B 299 -1  N  LYS B 298   O  LYS B 330           
SHEET   10   I10 VAL B 304  VAL B 316 -1  O  VAL B 304   N  ASP B 299           
SHEET    1   J 5 ALA C  63  TYR C  65  0                                        
SHEET    2   J 5 ARG C  43  VAL C  47  1  O  VAL C  44   N  ALA C  63           
SHEET    3   J 5 SER C   9  LEU C  13  1  N  ILE C  10   O  ARG C  43           
SHEET    4   J 5 ALA C  85  LEU C  87  1  O  ALA C  85   N  LEU C  11           
SHEET    5   J 5 THR C 114  MET C 115  1  O  THR C 114   N  VAL C  86           
SHEET    1   K 4 SER C 146  ALA C 149  0                                        
SHEET    2   K 4 LEU C 204  GLU C 208 -1  N  LEU C 204   O  ALA C 149           
SHEET    3   K 4 CYS C 166  PRO C 170 -1  O  ILE C 167   N  ASP C 207           
SHEET    4   K 4 GLY C 180  ALA C 182 -1  O  GLY C 180   N  ILE C 168           
SHEET    1   L 7 LEU C 295  ASN C 301  0                                        
SHEET    2   L 7 GLY C 280  VAL C 288 -1  O  ASN C 283   N  ASN C 301           
SHEET    3   L 7 LYS C 214  ARG C 222 -1  N  LYS C 214   O  VAL C 288           
SHEET    4   L 7 CYS C 228  ASN C 236 -1  N  ILE C 229   O  VAL C 221           
SHEET    5   L 7 THR C 249  ALA C 251 -1  O  VAL C 250   N  GLU C 235           
SHEET    6   L 7 VAL C 355  ARG C 361 -1  N  VAL C 356   O  ALA C 251           
SHEET    7   L 7 GLY C 382  GLY C 388 -1  O  GLY C 382   N  ARG C 361           
SHEET    1   M 7 VAL C 525  ARG C 528  0                                        
SHEET    2   M 7 TYR C 542  THR C 546 -1  O  TYR C 544   N  LYS C 527           
SHEET    3   M 7 ARG C 615  PHE C 618  1  O  LEU C 616   N  MET C 543           
SHEET    4   M 7 GLU C 595  ASN C 600  1  O  THR C 596   N  ARG C 615           
SHEET    5   M 7 LYS C 561  LEU C 565  1  O  ILE C 562   N  ILE C 597           
SHEET    6   M 7 GLY C 637  ILE C 639  1  O  GLY C 637   N  MET C 563           
SHEET    7   M 7 VAL C 661  ILE C 662  1  N  ILE C 662   O  VAL C 638           
SHEET    1   N 4 ASN C 692  THR C 694  0                                        
SHEET    2   N 4 LEU C 751  HIS C 754 -1  N  LEU C 752   O  ALA C 693           
SHEET    3   N 4 LEU C 712  ARG C 715 -1  N  VAL C 713   O  ASP C 753           
SHEET    4   N 4 GLU C 726  VAL C 728 -1  O  GLU C 726   N  VAL C 714           
SHEET    1   O 7 GLU C 836  ASN C 843  0                                        
SHEET    2   O 7 GLY C 824  LYS C 833 -1  O  ASN C 827   N  ASN C 843           
SHEET    3   O 7 VAL C 760  CYS C 768 -1  O  VAL C 760   N  VAL C 832           
SHEET    4   O 7 VAL C 773  HIS C 781 -1  N  LEU C 774   O  ILE C 767           
SHEET    5   O 7 CYS C 794  LEU C 796 -1  O  SER C 795   N  GLU C 780           
SHEET    6   O 7 TYR C 888  VAL C 894 -1  N  SER C 889   O  LEU C 796           
SHEET    7   O 7 GLY C 915  GLY C 921 -1  O  GLY C 915   N  VAL C 894           
SHEET    1   P 5 ARG C 989  LEU C 990  0                                        
SHEET    2   P 5 PHE C 969  ALA C 973  1  O  LEU C 971   N  ARG C 989           
SHEET    3   P 5 GLY C 943  SER C 948  1  O  GLY C 943   N  GLU C 970           
SHEET    4   P 5 TYR C1012  ASN C1015  1  O  TYR C1012   N  LEU C 946           
SHEET    5   P 5 HIS C1039  ASP C1041  1  O  HIS C1039   N  ILE C1013           
SHEET    1   Q 8 SER D   4  LEU D   9  0                                        
SHEET    2   Q 8 GLN D  14  ALA D  19 -1  N  PHE D  15   O  LEU D   7           
SHEET    3   Q 8 VAL D 108  ALA D 111 -1  N  ALA D 111   O  ARG D  18           
SHEET    4   Q 8 GLY D  79  VAL D  81  1  O  LEU D  80   N  ILE D 110           
SHEET    5   Q 8 GLN D  51  LEU D  55  1  O  GLN D  51   N  GLY D  79           
SHEET    6   Q 8 GLY D  24  ASN D  33  1  O  GLU D  29   N  ILE D  52           
SHEET    7   Q 8 GLN D 128  ALA D 134 -1  O  GLN D 128   N  VAL D  30           
SHEET    8   Q 8 SER D   4  LEU D   9 -1  O  LEU D   6   N  ILE D 133           
SHEET    1   R10 TYR D 168  TRP D 170  0                                        
SHEET    2   R10 CYS D 214  VAL D 219 -1  N  LEU D 216   O  TRP D 170           
SHEET    3   R10 PHE D 192  TYR D 197  1  O  PHE D 192   N  ARG D 215           
SHEET    4   R10 GLY D 235  LEU D 238  1  O  GLY D 235   N  VAL D 195           
SHEET    5   R10 VAL D 265  GLY D 267  1  O  PHE D 266   N  LEU D 238           
SHEET    6   R10 ALA D 347  PHE D 350  1  N  PHE D 348   O  VAL D 265           
SHEET    7   R10 LEU D 337  ARG D 342 -1  O  ILE D 340   N  SER D 349           
SHEET    8   R10 LEU D 325  SER D 331 -1  N  ARG D 326   O  HIS D 341           
SHEET    9   R10 THR D 283  ASP D 299 -1  N  LYS D 298   O  LYS D 330           
SHEET   10   R10 VAL D 304  VAL D 316 -1  O  VAL D 304   N  ASP D 299           
SHEET    1   S 5 ALA E  63  TYR E  65  0                                        
SHEET    2   S 5 ARG E  43  VAL E  47  1  O  VAL E  44   N  ALA E  63           
SHEET    3   S 5 SER E   9  LEU E  13  1  N  ILE E  10   O  ARG E  43           
SHEET    4   S 5 ALA E  85  LEU E  87  1  O  ALA E  85   N  LEU E  11           
SHEET    5   S 5 THR E 114  MET E 115  1  O  THR E 114   N  VAL E  86           
SHEET    1   T 4 SER E 146  ALA E 149  0                                        
SHEET    2   T 4 LEU E 204  GLU E 208 -1  N  LEU E 204   O  ALA E 149           
SHEET    3   T 4 CYS E 166  PRO E 170 -1  O  ILE E 167   N  ASP E 207           
SHEET    4   T 4 GLY E 180  ALA E 182 -1  O  GLY E 180   N  ILE E 168           
SHEET    1   U 7 LEU E 295  ASN E 301  0                                        
SHEET    2   U 7 GLY E 280  VAL E 288 -1  O  ASN E 283   N  ASN E 301           
SHEET    3   U 7 LYS E 214  ARG E 222 -1  O  LYS E 214   N  VAL E 288           
SHEET    4   U 7 CYS E 228  ASN E 236 -1  N  ILE E 229   O  VAL E 221           
SHEET    5   U 7 THR E 249  ALA E 251 -1  O  VAL E 250   N  GLU E 235           
SHEET    6   U 7 VAL E 355  ARG E 361 -1  N  VAL E 356   O  ALA E 251           
SHEET    7   U 7 GLY E 382  GLY E 388 -1  O  GLY E 382   N  ARG E 361           
SHEET    1   V 6 VAL E 525  ARG E 528  0                                        
SHEET    2   V 6 TYR E 542  THR E 546 -1  O  TYR E 544   N  LYS E 527           
SHEET    3   V 6 ARG E 615  PHE E 618  1  O  LEU E 616   N  MET E 543           
SHEET    4   V 6 GLU E 595  ASN E 600  1  O  THR E 596   N  ARG E 615           
SHEET    5   V 6 LYS E 561  LEU E 565  1  O  ILE E 562   N  ILE E 597           
SHEET    6   V 6 GLY E 637  ILE E 639  1  O  GLY E 637   N  MET E 563           
SHEET    1   W 4 ASN E 692  THR E 694  0                                        
SHEET    2   W 4 LEU E 751  HIS E 754 -1  N  LEU E 752   O  ALA E 693           
SHEET    3   W 4 LEU E 712  ARG E 715 -1  N  VAL E 713   O  ASP E 753           
SHEET    4   W 4 GLU E 726  VAL E 728 -1  O  GLU E 726   N  VAL E 714           
SHEET    1   X 7 GLU E 836  ASN E 843  0                                        
SHEET    2   X 7 GLY E 824  LYS E 833 -1  O  ASN E 827   N  ASN E 843           
SHEET    3   X 7 VAL E 760  CYS E 768 -1  O  VAL E 760   N  VAL E 832           
SHEET    4   X 7 VAL E 773  HIS E 781 -1  N  LEU E 774   O  ILE E 767           
SHEET    5   X 7 CYS E 794  LEU E 796 -1  O  SER E 795   N  GLU E 780           
SHEET    6   X 7 TYR E 888  VAL E 894 -1  O  SER E 889   N  LEU E 796           
SHEET    7   X 7 GLY E 915  GLY E 921 -1  O  GLY E 915   N  VAL E 894           
SHEET    1   Y 5 ARG E 989  LEU E 990  0                                        
SHEET    2   Y 5 GLU E 970  ALA E 973  1  O  LEU E 971   N  ARG E 989           
SHEET    3   Y 5 ARG E 944  SER E 948  1  N  ALA E 945   O  GLU E 970           
SHEET    4   Y 5 TYR E1012  ASN E1015  1  O  TYR E1012   N  LEU E 946           
SHEET    5   Y 5 HIS E1039  ASP E1041  1  O  HIS E1039   N  ILE E1013           
SHEET    1   Z 8 SER F   4  LEU F   9  0                                        
SHEET    2   Z 8 GLN F  14  ALA F  19 -1  N  PHE F  15   O  LEU F   7           
SHEET    3   Z 8 VAL F 108  ALA F 111 -1  N  ALA F 111   O  ARG F  18           
SHEET    4   Z 8 GLY F  79  VAL F  81  1  O  LEU F  80   N  ILE F 110           
SHEET    5   Z 8 GLN F  51  LEU F  55  1  O  GLN F  51   N  GLY F  79           
SHEET    6   Z 8 GLY F  24  ASN F  33  1  O  GLU F  29   N  ILE F  52           
SHEET    7   Z 8 GLN F 128  ALA F 134 -1  O  GLN F 128   N  VAL F  30           
SHEET    8   Z 8 SER F   4  LEU F   9 -1  O  LEU F   6   N  ILE F 133           
SHEET    1  AA10 TYR F 168  TRP F 170  0                                        
SHEET    2  AA10 CYS F 214  PRO F 220 -1  N  LEU F 216   O  TRP F 170           
SHEET    3  AA10 PHE F 192  ASP F 198  1  O  PHE F 192   N  ARG F 215           
SHEET    4  AA10 GLY F 235  LEU F 238  1  O  GLY F 235   N  VAL F 195           
SHEET    5  AA10 VAL F 265  GLY F 267  1  N  PHE F 266   O  ILE F 236           
SHEET    6  AA10 ALA F 347  PHE F 350  1  N  PHE F 348   O  VAL F 265           
SHEET    7  AA10 LEU F 337  ARG F 342 -1  O  ILE F 340   N  SER F 349           
SHEET    8  AA10 LEU F 325  SER F 331 -1  N  ARG F 326   O  HIS F 341           
SHEET    9  AA10 THR F 283  ASP F 299 -1  N  LYS F 298   O  LYS F 330           
SHEET   10  AA10 VAL F 304  VAL F 316 -1  O  VAL F 304   N  ASP F 299           
SHEET    1  AB 5 ALA G  63  TYR G  65  0                                        
SHEET    2  AB 5 ARG G  43  VAL G  47  1  O  VAL G  44   N  ALA G  63           
SHEET    3  AB 5 SER G   9  LEU G  13  1  N  ILE G  10   O  ARG G  43           
SHEET    4  AB 5 ALA G  85  LEU G  87  1  O  ALA G  85   N  LEU G  11           
SHEET    5  AB 5 THR G 114  MET G 115  1  O  THR G 114   N  VAL G  86           
SHEET    1  AC 4 SER G 146  ALA G 149  0                                        
SHEET    2  AC 4 LEU G 204  GLU G 208 -1  N  LEU G 204   O  ALA G 149           
SHEET    3  AC 4 CYS G 166  PRO G 170 -1  O  ILE G 167   N  ASP G 207           
SHEET    4  AC 4 GLY G 180  ALA G 182 -1  O  GLY G 180   N  ILE G 168           
SHEET    1  AD 7 LEU G 295  ASN G 301  0                                        
SHEET    2  AD 7 GLY G 280  VAL G 288 -1  O  ASN G 283   N  ASN G 301           
SHEET    3  AD 7 LYS G 214  ARG G 222 -1  N  LYS G 214   O  VAL G 288           
SHEET    4  AD 7 CYS G 228  ASN G 236 -1  N  ILE G 229   O  VAL G 221           
SHEET    5  AD 7 THR G 249  ALA G 251 -1  O  VAL G 250   N  GLU G 235           
SHEET    6  AD 7 VAL G 355  ARG G 361 -1  N  VAL G 356   O  ALA G 251           
SHEET    7  AD 7 GLY G 382  GLY G 388 -1  O  GLY G 382   N  ARG G 361           
SHEET    1  AE 7 VAL G 525  ARG G 528  0                                        
SHEET    2  AE 7 ALA G 541  THR G 546 -1  O  TYR G 544   N  LYS G 527           
SHEET    3  AE 7 ARG G 615  TYR G 617  1  N  LEU G 616   O  ALA G 541           
SHEET    4  AE 7 GLU G 595  VAL G 599  1  O  THR G 596   N  ARG G 615           
SHEET    5  AE 7 LYS G 561  LEU G 565  1  N  ILE G 562   O  GLU G 595           
SHEET    6  AE 7 GLY G 637  ILE G 639  1  O  GLY G 637   N  MET G 563           
SHEET    7  AE 7 VAL G 661  ILE G 662  1  N  ILE G 662   O  VAL G 638           
SHEET    1  AF 4 ASN G 692  THR G 694  0                                        
SHEET    2  AF 4 LEU G 751  HIS G 754 -1  N  LEU G 752   O  ALA G 693           
SHEET    3  AF 4 LEU G 712  ARG G 715 -1  N  VAL G 713   O  ASP G 753           
SHEET    4  AF 4 GLU G 726  VAL G 728 -1  O  GLU G 726   N  VAL G 714           
SHEET    1  AG 7 VAL G 837  ASN G 843  0                                        
SHEET    2  AG 7 GLY G 824  VAL G 832 -1  O  ASN G 827   N  ASN G 843           
SHEET    3  AG 7 VAL G 760  CYS G 768 -1  O  VAL G 760   N  VAL G 832           
SHEET    4  AG 7 VAL G 773  HIS G 781 -1  N  LEU G 774   O  ILE G 767           
SHEET    5  AG 7 CYS G 794  LEU G 796 -1  O  SER G 795   N  GLU G 780           
SHEET    6  AG 7 TYR G 888  VAL G 894 -1  N  SER G 889   O  LEU G 796           
SHEET    7  AG 7 GLY G 915  GLY G 921 -1  O  GLY G 915   N  VAL G 894           
SHEET    1  AH 5 ARG G 989  VAL G 991  0                                        
SHEET    2  AH 5 PHE G 969  THR G 974  1  O  LEU G 971   N  ARG G 989           
SHEET    3  AH 5 GLY G 943  SER G 948  1  O  GLY G 943   N  GLU G 970           
SHEET    4  AH 5 TYR G1012  ASN G1015  1  O  TYR G1012   N  LEU G 946           
SHEET    5  AH 5 HIS G1039  ASP G1041  1  O  HIS G1039   N  ILE G1013           
SHEET    1  AI 8 SER H   4  LEU H   9  0                                        
SHEET    2  AI 8 GLN H  14  ALA H  19 -1  O  PHE H  15   N  LEU H   7           
SHEET    3  AI 8 ALA H 109  ALA H 111 -1  N  ALA H 111   O  ARG H  18           
SHEET    4  AI 8 GLY H  79  VAL H  81  1  O  LEU H  80   N  ILE H 110           
SHEET    5  AI 8 GLN H  51  LEU H  55  1  O  GLN H  51   N  GLY H  79           
SHEET    6  AI 8 GLY H  24  ASN H  33  1  O  GLU H  29   N  ILE H  52           
SHEET    7  AI 8 GLN H 128  ALA H 134 -1  O  GLN H 128   N  VAL H  30           
SHEET    8  AI 8 SER H   4  LEU H   9 -1  O  LEU H   6   N  ILE H 133           
SHEET    1  AJ10 TYR H 168  TRP H 170  0                                        
SHEET    2  AJ10 CYS H 214  PRO H 220 -1  O  LEU H 216   N  TRP H 170           
SHEET    3  AJ10 PHE H 192  ASP H 198  1  O  PHE H 192   N  ARG H 215           
SHEET    4  AJ10 GLY H 235  LEU H 238  1  O  GLY H 235   N  VAL H 195           
SHEET    5  AJ10 VAL H 265  GLY H 267  1  O  PHE H 266   N  LEU H 238           
SHEET    6  AJ10 ALA H 347  PHE H 350  1  N  PHE H 348   O  VAL H 265           
SHEET    7  AJ10 LEU H 337  ARG H 342 -1  O  ILE H 340   N  SER H 349           
SHEET    8  AJ10 LEU H 325  SER H 331 -1  N  ARG H 326   O  HIS H 341           
SHEET    9  AJ10 THR H 283  ASP H 299 -1  N  LYS H 298   O  LYS H 330           
SHEET   10  AJ10 VAL H 304  VAL H 316 -1  O  VAL H 304   N  ASP H 299           
LINK         O   ASP A  84                 K     K A5019     1555   1555  2.81  
LINK         O   GLY A 112                 K     K A5019     1555   1555  2.79  
LINK         OG1 THR A 114                 K     K A5019     1555   1555  2.77  
LINK         OE2 GLU A 215                 K     K A5003     1555   1555  2.67  
LINK         OD1 ASN A 236                 K     K A5003     1555   1555  2.83  
LINK         O   ASP A 238                 K     K A5003     1555   1555  2.73  
LINK         O   ALA A 239                 K     K A5003     1555   1555  2.83  
LINK         O   ILE A 242                 K     K A5003     1555   1555  2.64  
LINK         OG  SER A 247                 K     K A5003     1555   1555  2.73  
LINK         OE1 GLN A 285                MN    MN A5002     1555   1555  1.91  
LINK         OE1 GLN A 285                 K     K A5021     1555   1555  2.84  
LINK         CD  GLU A 299                MN    MN A5001     1555   1555  2.58  
LINK         OE1 GLU A 299                 K     K A5004     1555   1555  2.66  
LINK         OE1 GLU A 299                MN    MN A5001     1555   1555  2.28  
LINK         OE2 GLU A 299                MN    MN A5002     1555   1555  2.28  
LINK         OE2 GLU A 299                MN    MN A5001     1555   1555  2.28  
LINK         O   MET A 300                 K     K A5004     1555   1555  2.70  
LINK         OD1 ASN A 301                MN    MN A5001     1555   1555  1.98  
LINK         OE2 GLU A 761                 K     K A5009     1555   1555  2.71  
LINK         ND1 HIS A 781                 K     K A5009     1555   1555  2.75  
LINK         O   GLU A 783                 K     K A5009     1555   1555  2.80  
LINK         O   GLN A 784                 K     K A5009     1555   1555  2.70  
LINK         O   VAL A 787                 K     K A5009     1555   1555  2.59  
LINK         OG  SER A 792                 K     K A5009     1555   1555  2.90  
LINK         OE1 GLN A 829                MN    MN A5007     1555   1555  2.18  
LINK         OE2 GLU A 841                MN    MN A5007     1555   1555  2.38  
LINK         OE2 GLU A 841                 K     K A5008     1555   1555  2.73  
LINK         O   HIS B  16                 K     K B5020     1555   1555  2.80  
LINK         O   ASP B 112                 K     K B5020     1555   1555  2.66  
LINK         O   GLY C 112                 K     K C5042     1555   1555  2.67  
LINK         OG1 THR C 114                 K     K C5042     1555   1555  2.67  
LINK         OE1 GLU C 127                 K     K C5027     1555   1555  2.80  
LINK         O   THR C 143                 K     K C5045     1555   1555  2.86  
LINK         OG1 THR C 143                 K     K C5045     1555   1555  2.91  
LINK         OE2 GLU C 215                 K     K C5026     1555   1555  2.78  
LINK         OE1 GLU C 217                 K     K C5044     1555   1555  2.93  
LINK         OD1 ASN C 236                 K     K C5026     1555   1555  2.90  
LINK         O   ASP C 238                 K     K C5026     1555   1555  2.65  
LINK         O   ALA C 239                 K     K C5026     1555   1555  2.87  
LINK         O   ILE C 242                 K     K C5026     1555   1555  2.80  
LINK         OG  SER C 247                 K     K C5026     1555   1555  2.78  
LINK         OE1 GLN C 285                 K     K C5044     1555   1555  2.73  
LINK         OE1 GLN C 285                MN    MN C5025     1555   1555  2.03  
LINK         CD  GLU C 299                MN    MN C5024     1555   1555  2.57  
LINK         OE1 GLU C 299                MN    MN C5024     1555   1555  2.18  
LINK         OE1 GLU C 299                 K     K C5027     1555   1555  2.64  
LINK         OE2 GLU C 299                MN    MN C5025     1555   1555  2.28  
LINK         OE2 GLU C 299                MN    MN C5024     1555   1555  2.33  
LINK         O   MET C 300                 K     K C5027     1555   1555  2.70  
LINK         OD1 ASN C 301                MN    MN C5024     1555   1555  2.05  
LINK         OE2 GLU C 761                 K     K C5032     1555   1555  2.64  
LINK         ND1 HIS C 781                 K     K C5032     1555   1555  2.83  
LINK         O   GLU C 783                 K     K C5032     1555   1555  2.75  
LINK         O   VAL C 787                 K     K C5032     1555   1555  2.68  
LINK         OG  SER C 792                 K     K C5032     1555   1555  2.68  
LINK         OE1 GLN C 829                MN    MN C5030     1555   1555  2.24  
LINK         OE1 GLU C 841                 K     K C5031     1555   1555  2.88  
LINK         OE2 GLU C 841                 K     K C5031     1555   1555  2.80  
LINK         OE2 GLU C 841                MN    MN C5030     1555   1555  2.20  
LINK         O   HIS D  16                 K     K D5043     1555   1555  2.81  
LINK         O   ASP D 112                 K     K D5043     1555   1555  2.79  
LINK         O   ASP E  84                 K     K E5065     1555   1555  2.83  
LINK         O   GLY E 112                 K     K E5065     1555   1555  2.70  
LINK         OE1 GLU E 127                 K     K E5050     1555   1555  2.88  
LINK         O   ALA E 144                 K     K E5069     1555   1555  2.75  
LINK         OE2 GLU E 215                 K     K E5049     1555   1555  2.48  
LINK         OE1 GLU E 217                 K     K E5067     1555   1555  2.77  
LINK         OD1 ASN E 236                 K     K E5049     1555   1555  2.74  
LINK         O   ASP E 238                 K     K E5049     1555   1555  2.65  
LINK         O   ALA E 239                 K     K E5049     1555   1555  2.86  
LINK         O   ILE E 242                 K     K E5049     1555   1555  2.56  
LINK         OG  SER E 247                 K     K E5049     1555   1555  2.71  
LINK         OE1 GLN E 285                MN    MN E5048     1555   1555  2.14  
LINK         OE1 GLN E 285                 K     K E5067     1555   1555  2.60  
LINK         CD  GLU E 299                MN    MN E5047     1555   1555  2.62  
LINK         OE1 GLU E 299                 K     K E5050     1555   1555  2.59  
LINK         OE1 GLU E 299                MN    MN E5047     1555   1555  2.42  
LINK         OE2 GLU E 299                MN    MN E5048     1555   1555  2.31  
LINK         OE2 GLU E 299                MN    MN E5047     1555   1555  2.18  
LINK         O   MET E 300                 K     K E5050     1555   1555  2.62  
LINK         OD1 ASN E 301                MN    MN E5047     1555   1555  2.19  
LINK         OE2 GLU E 761                 K     K E5055     1555   1555  2.68  
LINK         ND1 HIS E 781                 K     K E5055     1555   1555  2.87  
LINK         O   GLU E 783                 K     K E5055     1555   1555  2.72  
LINK         O   VAL E 787                 K     K E5055     1555   1555  2.51  
LINK         OG  SER E 792                 K     K E5055     1555   1555  2.69  
LINK         OE1 GLN E 829                MN    MN E5053     1555   1555  2.06  
LINK         OE1 GLU E 841                 K     K E5054     1555   1555  2.80  
LINK         OE2 GLU E 841                MN    MN E5053     1555   1555  1.93  
LINK         O   HIS F  16                 K     K F5066     1555   1555  2.85  
LINK         O   ASP F 112                 K     K F5066     1555   1555  2.90  
LINK         O   GLY G 112                 K     K G5090     1555   1555  2.70  
LINK         OG1 THR G 114                 K     K G5090     1555   1555  2.90  
LINK         OE1 GLU G 127                 K     K G5075     1555   1555  2.85  
LINK         O   THR G 143                 K     K G5093     1555   1555  2.91  
LINK         OG1 THR G 143                 K     K G5093     1555   1555  2.83  
LINK         OE2 GLU G 215                 K     K G5074     1555   1555  2.33  
LINK         O   ASP G 238                 K     K G5074     1555   1555  2.77  
LINK         O   ALA G 239                 K     K G5074     1555   1555  2.72  
LINK         O   ILE G 242                 K     K G5074     1555   1555  2.77  
LINK         OG  SER G 247                 K     K G5074     1555   1555  2.83  
LINK         OE1 GLN G 285                 K     K G5092     1555   1555  2.71  
LINK         OE1 GLN G 285                MN    MN G5073     1555   1555  1.98  
LINK         CD  GLU G 299                MN    MN G5072     1555   1555  2.62  
LINK         OE1 GLU G 299                 K     K G5075     1555   1555  2.89  
LINK         OE1 GLU G 299                MN    MN G5072     1555   1555  2.25  
LINK         OE2 GLU G 299                MN    MN G5073     1555   1555  2.22  
LINK         OE2 GLU G 299                MN    MN G5072     1555   1555  2.31  
LINK         O   MET G 300                 K     K G5075     1555   1555  2.69  
LINK         OD1 ASN G 301                MN    MN G5072     1555   1555  2.15  
LINK         OE2 GLU G 761                 K     K G5080     1555   1555  2.50  
LINK         ND1 HIS G 781                 K     K G5080     1555   1555  2.87  
LINK         O   GLU G 783                 K     K G5080     1555   1555  2.81  
LINK         O   GLN G 784                 K     K G5080     1555   1555  2.82  
LINK         O   VAL G 787                 K     K G5080     1555   1555  2.62  
LINK         OG  SER G 792                 K     K G5080     1555   1555  2.70  
LINK         OE1 GLN G 829                MN    MN G5078     1555   1555  2.15  
LINK         OE2 GLU G 841                 K     K G5079     1555   1555  2.78  
LINK         OE2 GLU G 841                MN    MN G5078     1555   1555  2.31  
LINK         O   ASP H 112                 K     K H5091     1555   1555  2.59  
LINK        MN    MN A5001                 O3B ADP A5000     1555   1555  1.92  
LINK        MN    MN A5001                 O1  PO4 A5005     1555   1555  2.04  
LINK        MN    MN A5001                 O   HOH A5158     1555   1555  2.16  
LINK        MN    MN A5002                 O1B ADP A5000     1555   1555  2.11  
LINK        MN    MN A5002                 O1A ADP A5000     1555   1555  2.09  
LINK        MN    MN A5002                 O   HOH A5157     1555   1555  2.06  
LINK        MN    MN A5002                 O3  PO4 A5005     1555   1555  2.07  
LINK         K     K A5004                 O   HOH A5912     1555   1555  2.20  
LINK         K     K A5004                 O   HOH A5158     1555   1555  2.90  
LINK        MN    MN A5007                 O   HOH A5165     1555   1555  2.36  
LINK        MN    MN A5007                 O2A ADP A5006     1555   1555  2.05  
LINK        MN    MN A5007                 O3B ADP A5006     1555   1555  2.03  
LINK        MN    MN A5007                 O   HOH A5948     1555   1555  2.74  
LINK         K     K A5008                 O2B ADP A5006     1555   1555  2.46  
LINK         K     K A5019                 O   HOH A5730     1555   1555  2.62  
LINK         K     K A5019                 O   HOH A5172     1555   1555  2.83  
LINK         K     K B5020                 O   HOH B5057     1555   1555  2.76  
LINK         K     K A5021                 O3  PO4 A5005     1555   1555  2.70  
LINK         K     K A5022                 O   HOH A5261     1555   1555  2.51  
LINK         K     K G5090                 O   HOH G5177     1555   1555  2.72  
LINK        MN    MN C5024                 O3B ADP C5023     1555   1555  1.93  
LINK        MN    MN C5024                 O1  PO4 C5028     1555   1555  2.00  
LINK        MN    MN C5024                 O   HOH C1157     1555   1555  2.17  
LINK        MN    MN C5025                 O   HOH C1156     1555   1555  2.23  
LINK        MN    MN C5025                 O1A ADP C5023     1555   1555  2.04  
LINK        MN    MN C5025                 O1B ADP C5023     1555   1555  2.23  
LINK        MN    MN C5025                 O3  PO4 C5028     1555   1555  2.00  
LINK         K     K G5092                 O   HOH G5165     1555   1555  2.80  
LINK         K     K G5092                 O3  PO4 G5076     1555   1555  2.79  
LINK         K     K G5093                 O   HOH G5266     1555   1555  2.74  
LINK         K     K G5093                 O   HOH G5265     1555   1555  2.79  
LINK         K     K C5027                 O   HOH C1849     1555   1555  2.75  
LINK        MN    MN C5030                 O3B ADP C5029     1555   1555  2.01  
LINK        MN    MN C5030                 O   HOH C1851     1555   1555  2.39  
LINK        MN    MN C5030                 O2A ADP C5029     1555   1555  2.23  
LINK        MN    MN C5030                 O   HOH C1164     1555   1555  2.49  
LINK         K     K C5031                 O   HOH C1651     1555   1555  2.71  
LINK         K     K C5031                 O2B ADP C5029     1555   1555  2.69  
LINK         K     K F5066                 O   HOH F2618     1555   1555  2.85  
LINK         K     K F5066                 O   HOH E5511     1555   1555  2.89  
LINK        MN    MN G5072                 O   HOH G5162     1555   1555  2.14  
LINK        MN    MN G5072                 O1  PO4 G5076     1555   1555  1.88  
LINK        MN    MN G5072                 O3B ADP G5071     1555   1555  2.15  
LINK        MN    MN G5073                 O3  PO4 G5076     1555   1555  2.10  
LINK        MN    MN G5073                 O   HOH G5161     1555   1555  2.20  
LINK        MN    MN G5073                 O1A ADP G5071     1555   1555  2.12  
LINK        MN    MN G5073                 O1B ADP G5071     1555   1555  2.20  
LINK         K     K G5075                 O   HOH G5162     1555   1555  2.89  
LINK         K     K D5043                 O   HOH D1561     1555   1555  2.92  
LINK         K     K D5043                 O   HOH C1562     1555   1555  2.77  
LINK        MN    MN G5078                 O3B ADP G5077     1555   1555  2.31  
LINK        MN    MN G5078                 O   HOH G5169     1555   1555  1.80  
LINK        MN    MN G5078                 O2A ADP G5077     1555   1555  2.14  
LINK         K     K C5044                 O3  PO4 C5028     1555   1555  2.88  
LINK         K     K G5079                 O   HOH G5607     1555   1555  2.53  
LINK         K     K G5079                 O2B ADP G5077     1555   1555  2.45  
LINK         K     K C5045                 O   HOH C1259     1555   1555  2.71  
LINK        MN    MN E5047                 O3B ADP E5046     1555   1555  1.96  
LINK        MN    MN E5047                 O   HOH E5140     1555   1555  1.98  
LINK        MN    MN E5047                 O1  PO4 E5051     1555   1555  2.02  
LINK        MN    MN E5048                 O1B ADP E5046     1555   1555  2.13  
LINK        MN    MN E5048                 O   HOH E5139     1555   1555  2.44  
LINK        MN    MN E5048                 O1A ADP E5046     1555   1555  2.13  
LINK        MN    MN E5048                 O3  PO4 E5051     1555   1555  2.13  
LINK         K     K E5050                 O   HOH E5697     1555   1555  2.70  
LINK         K     K E5050                 O   HOH E5233     1555   1555  2.82  
LINK        MN    MN E5053                 O2A ADP E5052     1555   1555  2.13  
LINK        MN    MN E5053                 O   HOH E5147     1555   1555  2.21  
LINK        MN    MN E5053                 O3B ADP E5052     1555   1555  2.13  
LINK         K     K E5054                 O2B ADP E5052     1555   1555  2.65  
LINK         K     K A5004                 O   ALA A 126     1555   1555  3.19  
LINK         K     K A5004                 OE1 GLU A 127     1555   1555  2.96  
LINK         K     K A5004                 O   HOH A5252     1555   1555  3.02  
LINK         K     K A5004                 O   HOH A5715     1555   1555  3.56  
LINK         K     K A5004                 OD1 ASN A 301     1555   1555  3.42  
LINK         K     K A5008                 O3B ADP A5006     1555   1555  3.04  
LINK         K     K A5008                 O   HOH A5613     1555   1555  3.52  
LINK         K     K A5008                 OE1 GLU A 841     1555   1555  3.22  
LINK         K     K A5008                 OD1 ASN A 843     1555   1555  3.25  
LINK         K     K A5019                 O   HOH A5173     1555   1555  2.98  
LINK         K     K A5021                MN    MN A5002     1555   1555  3.68  
LINK         K     K A5021                 O   HOH A5162     1555   1555  3.44  
LINK         K     K A5021                 OD1 ASN A 283     1555   1555  3.11  
LINK         K     K A5021                 ND2 ASN A 283     1555   1555  3.69  
LINK         K     K A5021                 O   HOH A5161     1555   1555  2.95  
LINK         K     K A5021                 OG1 THR A 244     1555   1555  3.18  
LINK         K     K A5021                 OE1 GLU A 217     1555   1555  3.04  
LINK         K     K A5022                 OG1 THR A 143     1555   1555  3.13  
LINK         K     K A5022                 O   ALA A 144     1555   1555  3.02  
LINK         K     K A5022                 O   THR A 143     1555   1555  3.09  
LINK         K     K A5022                 O   HOH A5262     1555   1555  3.42  
LINK         C   ILE B 268                 N   CYG B 269     1555   1555  1.29  
LINK         C   CYG B 269                 N   LEU B 270     1555   1555  1.34  
LINK         K     K B5020                 O   HOH A5535     1555   1555  3.12  
LINK         K     K B5020                 O   HOH B5058     1555   1555  3.06  
LINK         K     K B5020                 O   HOH B5173     1555   1555  3.12  
LINK         K     K C5027                 O   ALA C 126     1555   1555  3.28  
LINK         K     K C5027                 O   HOH C1157     1555   1555  3.19  
LINK         K     K C5027                 O   HOH C1250     1555   1555  2.94  
LINK         K     K C5027                 O   HOH C1850     1555   1555  3.47  
LINK         K     K C5027                 OD1 ASN C 301     1555   1555  3.36  
LINK         K     K C5031                 O   HOH C1620     1555   1555  3.26  
LINK         K     K C5031                 OD1 ASN C 843     1555   1555  3.09  
LINK         K     K C5031                 O3B ADP C5029     1555   1555  3.04  
LINK         K     K C5032                 O   GLN C 784     1555   1555  3.03  
LINK         K     K C5042                 O   ASP C  84     1555   1555  2.94  
LINK         K     K C5042                 O   HOH C1171     1555   1555  3.02  
LINK         K     K C5042                 N   THR C 114     1555   1555  3.63  
LINK         K     K C5044                 O   HOH C1161     1555   1555  3.46  
LINK         K     K C5044                 O   HOH C1160     1555   1555  2.98  
LINK         K     K C5044                 OD1 ASN C 283     1555   1555  2.98  
LINK         K     K C5044                 OG1 THR C 244     1555   1555  3.41  
LINK         K     K C5045                 O   ALA C 144     1555   1555  3.10  
LINK         K     K C5045                 O   HOH C1260     1555   1555  2.98  
LINK         K     K C5045                 O   HOH C1892     1555   1555  3.28  
LINK         K     K C5045                 O   HOH C2070     1555   1555  3.60  
LINK         C   ILE D 268                 N   CYG D 269     1555   1555  1.23  
LINK         C   CYG D 269                 N   LEU D 270     1555   1555  1.32  
LINK         K     K D5043                 O   HOH C1563     1555   1555  3.51  
LINK         K     K E5050                 O   ALA E 126     1555   1555  3.35  
LINK         K     K E5050                 O   HOH E5140     1555   1555  3.12  
LINK         K     K E5050                 O   HOH E5696     1555   1555  3.58  
LINK         K     K E5050                 OD1 ASN E 301     1555   1555  3.59  
LINK         K     K E5054                 O3B ADP E5052     1555   1555  3.31  
LINK         K     K E5054                 OD1 ASN E 843     1555   1555  3.19  
LINK         K     K E5054                 OE2 GLU E 841     1555   1555  3.27  
LINK         K     K E5054                 O   HOH E5589     1555   1555  3.59  
LINK         K     K E5055                 O   GLN E 784     1555   1555  2.94  
LINK         K     K E5065                 O   HOH E5153     1555   1555  3.14  
LINK         K     K E5065                 O   HOH E5704     1555   1555  2.98  
LINK         K     K E5065                 OG1 THR E 114     1555   1555  2.95  
LINK         K     K E5065                 N   THR E 114     1555   1555  3.67  
LINK         K     K E5067                 O3  PO4 E5051     1555   1555  2.98  
LINK         K     K E5067                MN    MN E5048     1555   1555  3.71  
LINK         K     K E5067                 ND2 ASN E 283     1555   1555  3.70  
LINK         K     K E5067                 OD1 ASN E 283     1555   1555  3.08  
LINK         K     K E5067                 OG1 THR E 244     1555   1555  3.29  
LINK         K     K E5067                 O   HOH E5143     1555   1555  3.06  
LINK         K     K E5068                 O   HOH E5152     1555   1555  3.22  
LINK         K     K E5069                 O   HOH E5749     1555   1555  3.45  
LINK         K     K E5069                 O   HOH E5243     1555   1555  3.03  
LINK         K     K E5069                 OG1 THR E 143     1555   1555  2.99  
LINK         K     K E5069                 O   THR E 143     1555   1555  3.03  
LINK         K     K E5069                 O   HOH E5863     1555   1555  3.33  
LINK         C   ILE F 268                 N   CYG F 269     1555   1555  1.35  
LINK         C   CYG F 269                 N   LEU F 270     1555   1555  1.32  
LINK         K     K F5066                 O   HOH E5512     1555   1555  3.55  
LINK         K     K G5074                 OD1 ASN G 236     1555   1555  3.08  
LINK         K     K G5075                 O   HOH G5256     1555   1555  2.97  
LINK         K     K G5075                 O   ALA G 126     1555   1555  3.22  
LINK         K     K G5075                 OD1 ASN G 301     1555   1555  3.51  
LINK         K     K G5075                 O   HOH G5704     1555   1555  3.34  
LINK         K     K G5079                 OD1 ASN G 843     1555   1555  3.32  
LINK         K     K G5079                 O   HOH G5705     1555   1555  3.01  
LINK         K     K G5079                 OE1 GLU G 841     1555   1555  3.08  
LINK         K     K G5079                 O3B ADP G5077     1555   1555  3.32  
LINK         K     K G5090                 O   HOH G5714     1555   1555  3.40  
LINK         K     K G5090                 O   HOH G5715     1555   1555  2.94  
LINK         K     K G5090                 O   ASP G  84     1555   1555  2.95  
LINK         K     K G5090                 O   HOH G5176     1555   1555  3.39  
LINK         K     K G5092                 O   HOH G5161     1555   1555  3.70  
LINK         K     K G5092                MN    MN G5073     1555   1555  3.66  
LINK         K     K G5092                 OD1 ASN G 283     1555   1555  2.95  
LINK         K     K G5092                 O   HOH G5166     1555   1555  3.51  
LINK         K     K G5092                 OG1 THR G 244     1555   1555  3.48  
LINK         K     K G5092                 OE1 GLU G 217     1555   1555  3.09  
LINK         K     K G5093                 O   HOH G5800     1555   1555  3.47  
LINK         K     K G5093                 O   ALA G 144     1555   1555  3.18  
LINK         C   ILE H 268                 N   CYG H 269     1555   1555  1.26  
LINK         C   CYG H 269                 N   LEU H 270     1555   1555  1.27  
LINK         K     K H5091                 O   HIS H  16     1555   1555  2.96  
LINK         K     K H5091                 O   HOH G5531     1555   1555  3.36  
LINK         K     K H5091                 O   HOH G5530     1555   1555  3.08  
LINK         K     K H5091                 O   HOH H3715     1555   1555  3.35  
CISPEP   1 PHE A  164    PRO A  165          0        -2.70                     
CISPEP   2 ALA A  251    PRO A  252          0        -1.09                     
CISPEP   3 TYR A  710    PRO A  711          0         0.80                     
CISPEP   4 LEU A  796    PRO A  797          0         1.93                     
CISPEP   5 ARG A  998    PRO A  999          0        -4.24                     
CISPEP   6 SER B  357    PRO B  358          0         3.14                     
CISPEP   7 PHE C  164    PRO C  165          0        -0.84                     
CISPEP   8 ALA C  251    PRO C  252          0         1.03                     
CISPEP   9 TYR C  710    PRO C  711          0         0.71                     
CISPEP  10 LEU C  796    PRO C  797          0         1.35                     
CISPEP  11 ARG C  998    PRO C  999          0        -6.41                     
CISPEP  12 SER D  357    PRO D  358          0         6.17                     
CISPEP  13 PHE E  164    PRO E  165          0        -0.89                     
CISPEP  14 ALA E  251    PRO E  252          0        -2.70                     
CISPEP  15 TYR E  710    PRO E  711          0         4.05                     
CISPEP  16 LEU E  796    PRO E  797          0         2.35                     
CISPEP  17 ARG E  998    PRO E  999          0        -2.43                     
CISPEP  18 SER F  357    PRO F  358          0         4.77                     
CISPEP  19 PHE G  164    PRO G  165          0         1.08                     
CISPEP  20 ALA G  251    PRO G  252          0         0.89                     
CISPEP  21 TYR G  710    PRO G  711          0         2.00                     
CISPEP  22 LEU G  796    PRO G  797          0         2.60                     
CISPEP  23 ARG G  998    PRO G  999          0        -1.65                     
CISPEP  24 SER H  357    PRO H  358          0         2.17                     
SITE     1 AC1  6 GLU A 299  ASN A 301  ADP A5000   MN A5002                    
SITE     2 AC1  6 PO4 A5005  HOH A5158                                          
SITE     1 AC2  7 GLN A 285  GLU A 299  ADP A5000   MN A5001                    
SITE     2 AC2  7 PO4 A5005    K A5021  HOH A5157                               
SITE     1 AC3  6 GLU A 215  ASN A 236  ASP A 238  ALA A 239                    
SITE     2 AC3  6 ILE A 242  SER A 247                                          
SITE     1 AC4  8 ALA A 126  GLU A 127  GLU A 299  MET A 300                    
SITE     2 AC4  8 ASN A 301  HOH A5158  HOH A5252  HOH A5912                    
SITE     1 AC5  5 GLN A 829  GLU A 841  ADP A5006  HOH A5165                    
SITE     2 AC5  5 HOH A5948                                                     
SITE     1 AC6  3 GLU A 841  ASN A 843  ADP A5006                               
SITE     1 AC7  6 GLU A 761  HIS A 781  GLU A 783  GLN A 784                    
SITE     2 AC7  6 VAL A 787  SER A 792                                          
SITE     1 AC8  5 GLN A  93  THR A 173  MET A 174  HOH A5133                    
SITE     2 AC8  5 HOH A5134                                                     
SITE     1 AC9  3 ASN A 289  ASN A 292  ARG A 294                               
SITE     1 BC1  4 ASN A 371  PHE A 900  PRO A 901  GLY A 902                    
SITE     1 BC2  3 LYS A 940  LYS A 941  HIS A 942                               
SITE     1 BC3  3 ARG A 950  GLY A 952  SER A1018                               
SITE     1 BC4  1 LYS B 285                                                     
SITE     1 BC5  2 ASP B 114  HOH B5058                                          
SITE     1 BC6  2 ARG A 294  HOH A5711                                          
SITE     1 BC7  6 ASP A  84  GLY A 112  THR A 114  HOH A5172                    
SITE     2 BC7  6 HOH A5173  HOH A5730                                          
SITE     1 BC8  4 HIS B  16  ASP B 112  HOH B5057  HOH B5058                    
SITE     1 BC9  7 GLU A 217  THR A 244  ASN A 283  GLN A 285                    
SITE     2 BC9  7  MN A5002  PO4 A5005  HOH A5161                               
SITE     1 CC1  3 THR A 143  ALA A 144  HOH A5261                               
SITE     1 CC2  4 GLN E  93  THR E 173  MET E 174  HOH E5116                    
SITE     1 CC3  5 ASP G  84  GLY G 112  THR G 114  HOH G5177                    
SITE     2 CC3  5 HOH G5715                                                     
SITE     1 CC4  6 GLU C 299  ASN C 301  HOH C1157  ADP C5023                    
SITE     2 CC4  6  MN C5025  PO4 C5028                                          
SITE     1 CC5  3 ASN E 289  ASN E 292  ARG E 294                               
SITE     1 CC6  3 HOH G5530  HIS H  16  ASP H 112                               
SITE     1 CC7  6 GLN C 285  GLU C 299  HOH C1156  ADP C5023                    
SITE     2 CC7  6  MN C5024  PO4 C5028                                          
SITE     1 CC8  4 ASN E 371  PHE E 900  PRO E 901  GLY E 902                    
SITE     1 CC9  7 GLU G 217  THR G 244  ASN G 283  GLN G 285                    
SITE     2 CC9  7  MN G5073  PO4 G5076  HOH G5165                               
SITE     1 DC1  6 GLU C 215  ASN C 236  ASP C 238  ALA C 239                    
SITE     2 DC1  6 ILE C 242  SER C 247                                          
SITE     1 DC2  1 LYS E 941                                                     
SITE     1 DC3  4 THR G 143  ALA G 144  HOH G5265  HOH G5266                    
SITE     1 DC4  7 ALA C 126  GLU C 127  GLU C 299  MET C 300                    
SITE     2 DC4  7 ASN C 301  HOH C1250  HOH C1849                               
SITE     1 DC5  3 ARG E 950  GLU E 951  GLY E 952                               
SITE     1 DC6  5 GLN C 829  GLU C 841  HOH C1164  HOH C1851                    
SITE     2 DC6  5 ADP C5029                                                     
SITE     1 DC7  1 LYS F 285                                                     
SITE     1 DC8  4 GLU C 841  ASN C 843  HOH C1651  ADP C5029                    
SITE     1 DC9  3 PHE F  15  ASP F 114  HOH F2657                               
SITE     1 EC1  6 GLU C 761  HIS C 781  GLU C 783  GLN C 784                    
SITE     2 EC1  6 VAL C 787  SER C 792                                          
SITE     1 EC2  4 ASP E  84  GLY E 112  THR E 114  HOH E5704                    
SITE     1 EC3  4 GLN C  93  THR C 173  MET C 174  HOH C1132                    
SITE     1 EC4  4 HOH E5511  HIS F  16  ASP F 112  HOH F2618                    
SITE     1 EC5  3 ASN C 289  ASN C 292  ARG C 294                               
SITE     1 EC6  6 GLU E 217  THR E 244  ASN E 283  GLN E 285                    
SITE     2 EC6  6 PO4 E5051  HOH E5143                                          
SITE     1 EC7  5 ALA C 370  ASN C 371  PHE C 900  PRO C 901                    
SITE     2 EC7  5 GLY C 902                                                     
SITE     1 EC8  1 THR E 279                                                     
SITE     1 EC9  2 LYS C 940  LYS C 941                                          
SITE     1 FC1  3 THR E 143  ALA E 144  HOH E5243                               
SITE     1 FC2  2 ARG C 950  SER C1018                                          
SITE     1 FC3  6 GLU G 299  ASN G 301  ADP G5071   MN G5073                    
SITE     2 FC3  6 PO4 G5076  HOH G5162                                          
SITE     1 FC4  1 LYS D 285                                                     
SITE     1 FC5  7 GLN G 285  GLU G 299  ADP G5071   MN G5072                    
SITE     2 FC5  7 PO4 G5076    K G5092  HOH G5161                               
SITE     1 FC6  5 GLU C 549  HOH C1562  PHE D  15  ASP D 114                    
SITE     2 FC6  5 HOH D1600                                                     
SITE     1 FC7  6 GLU G 215  ASN G 236  ASP G 238  ALA G 239                    
SITE     2 FC7  6 ILE G 242  SER G 247                                          
SITE     1 FC8  4 ASP C  84  GLY C 112  THR C 114  HOH C1171                    
SITE     1 FC9  7 ALA G 126  GLU G 127  GLU G 299  MET G 300                    
SITE     2 FC9  7 ASN G 301  HOH G5162  HOH G5256                               
SITE     1 GC1  4 HOH C1562  HIS D  16  ASP D 112  HOH D1561                    
SITE     1 GC2  4 GLN G 829  GLU G 841  ADP G5077  HOH G5169                    
SITE     1 GC3  6 GLU C 217  THR C 244  ASN C 283  GLN C 285                    
SITE     2 GC3  6 HOH C1160  PO4 C5028                                          
SITE     1 GC4  5 GLU G 841  ASN G 843  ADP G5077  HOH G5607                    
SITE     2 GC4  5 HOH G5705                                                     
SITE     1 GC5  4 THR C 143  ALA C 144  HOH C1259  HOH C1260                    
SITE     1 GC6  6 GLU G 761  HIS G 781  GLU G 783  GLN G 784                    
SITE     2 GC6  6 VAL G 787  SER G 792                                          
SITE     1 GC7  6 GLU E 299  ASN E 301  ADP E5046   MN E5048                    
SITE     2 GC7  6 PO4 E5051  HOH E5140                                          
SITE     1 GC8  3 GLN G  93  THR G 173  MET G 174                               
SITE     1 GC9  6 GLN E 285  GLU E 299  ADP E5046   MN E5047                    
SITE     2 GC9  6 PO4 E5051  HOH E5139                                          
SITE     1 HC1  3 ASN G 289  ASN G 292  ARG G 294                               
SITE     1 HC2  6 GLU E 215  ASN E 236  ASP E 238  ALA E 239                    
SITE     2 HC2  6 ILE E 242  SER E 247                                          
SITE     1 HC3  5 ASN G 371  PHE G 900  PRO G 901  GLY G 902                    
SITE     2 HC3  5 HOH G5313                                                     
SITE     1 HC4  7 ALA E 126  GLU E 127  GLU E 299  MET E 300                    
SITE     2 HC4  7 ASN E 301  HOH E5233  HOH E5697                               
SITE     1 HC5  2 LYS G 940  LYS G 941                                          
SITE     1 HC6  4 GLN E 829  GLU E 841  ADP E5052  HOH E5147                    
SITE     1 HC7  3 ARG G 950  GLY G 952  SER G1018                               
SITE     1 HC8  3 GLU E 841  ASN E 843  ADP E5052                               
SITE     1 HC9  1 LYS H 285                                                     
SITE     1 IC1  6 GLU E 761  HIS E 781  GLU E 783  GLN E 784                    
SITE     2 IC1  6 VAL E 787  SER E 792                                          
SITE     1 IC2  3 GLU G 549  PHE H  15  ASP H 114                               
SITE     1 IC3 15 MET A 174  GLY A 175  HIS A 243  GLN A 285                    
SITE     2 IC3 15 GLU A 299  ASN A 301  ARG A 303  ARG A 306                    
SITE     3 IC3 15 ADP A5000   MN A5001   MN A5002    K A5021                    
SITE     4 IC3 15 HOH A5157  HOH A5159  HOH A5161                               
SITE     1 IC4 14 MET C 174  GLY C 175  HIS C 243  GLN C 285                    
SITE     2 IC4 14 GLU C 299  ASN C 301  ARG C 303  ARG C 306                    
SITE     3 IC4 14 HOH C1158  HOH C1160  ADP C5023   MN C5024                    
SITE     4 IC4 14  MN C5025    K C5044                                          
SITE     1 IC5 14 MET E 174  GLY E 175  HIS E 243  GLN E 285                    
SITE     2 IC5 14 GLU E 299  ASN E 301  ARG E 303  ARG E 306                    
SITE     3 IC5 14 ADP E5046   MN E5047   MN E5048    K E5067                    
SITE     4 IC5 14 HOH E5141  HOH E5143                                          
SITE     1 IC6  4 PRO E 797  PRO E 885  PRO E 886  TYR E 888                    
SITE     1 IC7 13 MET G 174  GLY G 175  HIS G 243  GLN G 285                    
SITE     2 IC7 13 GLU G 299  ASN G 301  ARG G 303  ARG G 306                    
SITE     3 IC7 13 ADP G5071   MN G5072   MN G5073    K G5092                    
SITE     4 IC7 13 HOH G5163                                                     
SITE     1 IC8 26 ARG A 129  ILE A 167  ARG A 169  MET A 174                    
SITE     2 IC8 26 GLY A 175  GLY A 176  GLU A 208  LEU A 210                    
SITE     3 IC8 26 ILE A 211  GLU A 215  MET A 240  GLY A 241                    
SITE     4 IC8 26 ILE A 242  HIS A 243  THR A 244  GLN A 285                    
SITE     5 IC8 26 ILE A 298  GLU A 299  THR A 376   MN A5001                    
SITE     6 IC8 26  MN A5002  PO4 A5005  HOH A5151  HOH A5157                    
SITE     7 IC8 26 HOH A5158  HOH A5714                                          
SITE     1 IC9 18 ARG A 715  MET A 725  HIS A 754  PHE A 755                    
SITE     2 IC9 18 LEU A 756  GLU A 761  ALA A 785  GLY A 786                    
SITE     3 IC9 18 VAL A 787  HIS A 788  SER A 789  GLN A 829                    
SITE     4 IC9 18 GLU A 841   MN A5007    K A5008  HOH A5165                    
SITE     5 IC9 18 HOH A5613  HOH A5948                                          
SITE     1 JC1 10 GLU A 783  ASP A 791  ALA A 793  GLU A 892                    
SITE     2 JC1 10 LEU A 907  TYR A1040  ASP A1041  THR A1042                    
SITE     3 JC1 10 HOH A5095  HOH A5100                                          
SITE     1 JC2  4 GLN A  22  THR A  94  ASN A  97  ASN A 936                    
SITE     1 JC3 28 ARG C 129  ILE C 167  ARG C 169  THR C 173                    
SITE     2 JC3 28 MET C 174  GLY C 175  GLY C 176  GLU C 208                    
SITE     3 JC3 28 SER C 209  LEU C 210  ILE C 211  GLU C 215                    
SITE     4 JC3 28 MET C 240  GLY C 241  ILE C 242  HIS C 243                    
SITE     5 JC3 28 THR C 244  GLN C 285  ILE C 298  GLU C 299                    
SITE     6 JC3 28 THR C 376  HOH C1150  HOH C1156  HOH C1157                    
SITE     7 JC3 28 HOH C1848   MN C5024   MN C5025  PO4 C5028                    
SITE     1 JC4 18 ARG C 715  MET C 725  HIS C 754  PHE C 755                    
SITE     2 JC4 18 LEU C 756  GLU C 761  ALA C 785  GLY C 786                    
SITE     3 JC4 18 VAL C 787  HIS C 788  SER C 789  GLN C 829                    
SITE     4 JC4 18 GLU C 841  HOH C1164  HOH C1651  HOH C1852                    
SITE     5 JC4 18  MN C5030    K C5031                                          
SITE     1 JC5 10 GLU C 783  ASP C 791  GLU C 892  VAL C 893                    
SITE     2 JC5 10 LEU C 907  TYR C1040  ASP C1041  THR C1042                    
SITE     3 JC5 10 HOH C1094  HOH C1099                                          
SITE     1 JC6  3 THR C  94  ASN C  97  ASN C 936                               
SITE     1 JC7 27 ARG E 129  ILE E 167  ARG E 169  THR E 173                    
SITE     2 JC7 27 MET E 174  GLY E 175  GLY E 176  GLU E 208                    
SITE     3 JC7 27 LEU E 210  ILE E 211  GLU E 215  MET E 240                    
SITE     4 JC7 27 GLY E 241  ILE E 242  HIS E 243  THR E 244                    
SITE     5 JC7 27 GLN E 285  ILE E 298  GLU E 299  THR E 376                    
SITE     6 JC7 27  MN E5047   MN E5048  PO4 E5051  HOH E5133                    
SITE     7 JC7 27 HOH E5139  HOH E5140  HOH E5698                               
SITE     1 JC8 18 ARG E 715  MET E 725  HIS E 754  PHE E 755                    
SITE     2 JC8 18 LEU E 756  GLU E 761  ALA E 785  GLY E 786                    
SITE     3 JC8 18 VAL E 787  HIS E 788  SER E 789  GLN E 829                    
SITE     4 JC8 18 GLU E 841   MN E5053    K E5054  HOH E5146                    
SITE     5 JC8 18 HOH E5147  HOH E5589                                          
SITE     1 JC9 11 GLU E 783  ASP E 791  ALA E 793  GLU E 892                    
SITE     2 JC9 11 LEU E 907  TYR E1040  ASP E1041  THR E1042                    
SITE     3 JC9 11 HOH E5077  HOH E5079  HOH E5082                               
SITE     1 KC1  2 GLN E  22  THR E  94                                          
SITE     1 KC2 27 ARG G 129  ILE G 167  ARG G 169  THR G 173                    
SITE     2 KC2 27 MET G 174  GLY G 175  GLY G 176  GLU G 208                    
SITE     3 KC2 27 LEU G 210  ILE G 211  GLU G 215  MET G 240                    
SITE     4 KC2 27 GLY G 241  ILE G 242  HIS G 243  THR G 244                    
SITE     5 KC2 27 GLN G 285  ILE G 298  GLU G 299  THR G 376                    
SITE     6 KC2 27  MN G5072   MN G5073  PO4 G5076  HOH G5155                    
SITE     7 KC2 27 HOH G5161  HOH G5162  HOH G5703                               
SITE     1 KC3 19 ARG G 715  MET G 725  HIS G 754  PHE G 755                    
SITE     2 KC3 19 LEU G 756  GLU G 761  ALA G 785  GLY G 786                    
SITE     3 KC3 19 VAL G 787  HIS G 788  SER G 789  GLN G 829                    
SITE     4 KC3 19 GLU G 841   MN G5078    K G5079  HOH G5169                    
SITE     5 KC3 19 HOH G5170  HOH G5573  HOH G5607                               
SITE     1 KC4 12 GLU G 783  ASP G 791  ALA G 793  GLU G 892                    
SITE     2 KC4 12 VAL G 893  LEU G 907  TYR G1040  ASP G1041                    
SITE     3 KC4 12 THR G1042  HOH G5099  HOH G5101  HOH G5104                    
SITE     1 KC5  3 GLN G  22  THR G  94  ASN G  97                               
CRYST1  151.700  163.800  332.600  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.006592  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006105  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003007        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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